Publications

Below you will find the full list of peer-reviewed scientific publications that have acknowledged Instruct-ERIC funding and resources to carry out the research.

 

Simply select the dropdown and find all publications from that year.

 

 

2023

  1. Arias-Alpizar, G., et al. (2023). Phase-Separated Liposomes Hijack Endogenous Lipoprotein Transport and Metabolism Pathways to Target Subsets of Endothelial Cells In Vivo. Adv. Healthc. Mater. doi: 10.1002/adhm.202202709
  2. Azad, K., et al. (2023). Structural basis of CHMP2A-CHMP3 ESCRT-III polymer assembly and membrane cleavage. Nat. Struct. Mol. Biol. doi: 10.1038/s41594-022-00867-8
  3. Banneville, A. S. (2023). Structural and functional characterization of DdrC, a novel DNA damage-induced nucleoid associated protein involved in DNA compaction (vol 50, pg 7680, 2022). Nucleic Acids Res. doi: 10.1093/nar/gkad041
  4. Becker, L. M., et al. (2023). The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic-Angle-Spinning NMR Spectroscopy of Aromatic Residues. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202219314
  5. Bellomo, G., et al. (2023). Cerebrospinal fluid lipoproteins inhibit alpha-synuclein aggregation by interacting with oligomeric species in seed amplification assays. Mol. Neurodegener. doi: 10.1186/s13024-023-00613-8
  6. Brandmeier, J. C., et al. (2023). Digital and Analog Detection of SARS-CoV-2 Nucleocapsid Protein via an Upconversion-Linked Immunosorbent Assay. Anal. Chem. doi: 10.1021/acs.analchem.2c05670
  7. Brunetti, A., et al. (2023). Graphene-Oxide Mediated Chemodivergent Ring-Opening of Cyclobutanols. Chin. J. Chem. doi: 10.1002/cjoc.202200757
  8. Cawez, F., et al. (2023). Development of Nanobodies as Theranostic Agents against CMY-2-Like Class C beta-Lactamases. Antimicrob. Agents Chemother. doi: 10.1128/aac.01499-22
  9. Chyba, J., et al. (2023). Nature of NMR Shifts in Paramagnetic Octahedral Ru(III) Complexes with Axial Pyridine-Based Ligands. Inorg. Chem. doi: 10.1021/acs.inorgchem.2c03282
  10. Czubinsk, J., et al. (2023). Characteristics of N-Glycosylation and Its Impact on the Molecular Behavior of Lupinus angustifolius ?-Conglutin. J. Agric. Food Chem. doi: 10.1021/acs.jafc.3c00727
  11. d'Acapito, A., et al. (2023). Structural Study of the Cobetia marina Bacteriophage 1 (Carin-1) by Cryo-EM. J. Virol. doi: 10.1128/jvi.00248-23
  12. De, S., et al. (2023). Potato virus A particles-A versatile material for self-assembled nanopatterned surfaces. Virology. doi: 10.1016/j.virol.2022.11.010
  13. De Vallee, A., et al. (2023). Extracellular Vesicles of the Plant Pathogen Botrytis cinerea. J. Fungi. doi: 10.3390/jof9040495
  14. Degroux, S., et al. (2023). Deciphering Bacteriophage T5 Host Recognition Mechanism and Infection Trigger. J. Virol. doi: 10.1128/jvi.01584-22
  15. Di Lorenzo, F., et al. (2023). Expanding Knowledge of Methylotrophic Capacity: Structure and Properties of the Rough-Type Lipopolysaccharide from Methylobacterium extorquens and Its Role on Membrane Resistance to Methanol. JACS Au. doi: 10.1021/jacsau.3c00025
  16. Dijokaite-Guraliuc, A., et al. (2023). Rapid escape of new SARS-CoV-2 Omicron variants from BA.2-directed antibody responses. Cell Reports. doi: 10.1016/j.celrep.2023.112271
  17. Dufour, S., et al. (2023). Nanoscale imaging of CD47 informs how plasma membrane modifications shape apoptotic cell recognition. Commun. Biol. doi: 10.1038/s42003-023-04558-y
  18. Dvorak, J., et al. (2023). The rapid detection of procalcitonin in septic serum using immunoaffinity MALDI chips. Clin. Proteom. doi: 10.1186/s12014-023-09410-3
  19. Fernandes, A. D., et al. (2023). Conservation and divergence of the G-interfaces of Drosophila melanogaster septins. Cytoskeleton. doi: 10.1002/cm.21740
  20. Frechin, L., et al. (2023). High-resolution cryo-EM performance comparison of two latest-generation cryo electron microscopes on the human ribosome. J. Struct. Biol. doi: 10.1016/j.jsb.2022.107905
  21. Gauto, D. F., et al. (2023). Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. J. Struct. Biol.- X. doi: 10.1016/j.yjsbx.2022.100079
  22. Giorgi, M., et al. (2023). Structural Characterization of Murine Phosphodiesterase 5 Isoforms and Involvement of Cysteine Residues in Supramolecular Assembly. Int. J. Mol. Sci. doi: 10.3390/ijms24021108
  23. Gomez-Bouzo, U., et al. (2023). Structural analysis and biological activities of C25-amino and C25-nitro vitamin D analogs. Bioorganic Chem. doi: 10.1016/j.bioorg.2023.106528
  24. Grifagni, D., et al. (2023). Relaxation-based NMR assignment: Spotlights on ligand binding sites in human CISD3. J. Inorg. Biochem. doi: 10.1016/j.jinorgbio.2022.112089
  25. Guseva, S., et al. (2023). Liquid-Liquid Phase Separation Modifies the Dynamic Properties of Intrinsically Disordered Proteins. J. Am. Chem. Soc. doi: 10.1021/jacs.2c13647
  26. Hasanova, Z., et al. (2023). Human senataxin is a bona fide R-loop resolving enzyme and transcription termination factor. Nucleic Acids Res. doi: 10.1093/nar/gkad092
  27. Hoffmann, G., et al. (2023). Adenosine-Dependent Activation Mechanism of Prodrugs Targeting an Aminoacyl-tRNA Synthetase. J. Am. Chem. Soc. doi: 10.1021/jacs.2c04808
  28. Hosseinpoor, S., et al. (2023). Competing and directing interactions in new phosphoramide/thiophosphoramide structures: energy considerations and evidence for CHMIDLINE HORIZONTAL ELLIPSISHC contacts and aliphatic-aromatic stacking. CrystEngComm. doi: 10.1039/d3ce00204g
  29. Hradsky, D., et al. (2023). Catalytic performance of micro-mesoporous zirconosilicates prepared by non-hydrolytic sol-gel in ethanol-acetaldehyde conversion to butadiene and related reactions. Appl. Catal. A-Gen. doi: 10.1016/j.apcata.2023.119037
  30. Huliciak, M., et al. (2023). Combined in vitro and cell-based selection display method producing specific binders against IL-9 receptor in high yields. FEBS J. doi: 10.1111/febs.16726
  31. Huo, J. D., et al. (2023). A delicate balance between antibody evasion and ACE2 affinity for Omicron BA.2.75. Cell Reports. doi: 10.1016/j.celrep.2022.111903
  32. Janacova, L., et al. (2023). Catechol-O-methyl transferase suppresses cell invasion and interplays with MET signaling in estrogen dependent breast cancer. Sci Rep. doi: 10.1038/s41598-023-28078-1
  33. Janet-Maitre, M., et al. (2023). Genome-wide screen in human plasma identifies multifaceted complement evasion of Pseudomonas aeruginosa. PLoS Pathog. doi: 10.1371/journal.ppat.1011023
  34. Jones , R., et al. (2023). Structural basis and dynamics of Chikungunya alphavirus RNA capping by nsP1 capping pores. PNAS. doi: 10.1073/pnas.221393412
  35. Kemna, J., et al. (2023). IFN gamma binding to extracellular matrix prevents fatal systemic toxicity. Nat. Immunol. doi: 10.1038/s41590-023-01420-5
  36. Kouba, T., et al. (2023). Direct observation of backtracking by influenza A and B polymerases upon consecutive incorporation of the nucleoside analog T1106. Cell Reports. doi: 10.1016/j.celrep.2022.111901
  37. Kuntova, L., et al. (2023). Staphylococcus aureus Prophage-Encoded Protein Causes Abortive Infection and Provides Population Immunity against Kayviruses. mBio. doi: 10.1128/mbio.02490-22
  38. Lapcik, P., et al. (2023). DiaPASEF proteotype analysis indicates changes in cell growth and metabolic switch induced by caspase-9 inhibition in chondrogenic cells. Proteomics. doi: 10.1002/pmic.202200408
  39. Lauer, A. R., et al. (2023). Deciphering strontium sulfate precipitation via Ostwald's rule of stages: From prenucleation clusters to solution-mediated phase tranformation. J. Chem. Phys. doi: 10.1063/5.0136870
  40. Leesch, F., et al. (2023). A molecular network of conserved factors keeps ribosomes dormant in the egg. Nature. doi: 10.1038/s41586-022-05623-y
  41. Leesch, F., et al. (2023). A molecular network of conserved factors keeps ribosomes dormant in the egg. Nature. doi: 10.1038/s41586-022-05623-y
  42. Legartova, S., et al. (2023). Irradiation potentiates p53 phosphorylation and p53 binding to the promoter and coding region of the TP53 gene. Biochimie. doi: 10.1016/j.biochi.2022.09.013
  43. Linares, R., et al. (2023). Structural basis of bacteriophage T5 infection trigger and E. coli cell wall perforation. Sci Adv. doi: 10.1126/sciadv.ade9674
  44. Llauger, G., et al. (2023). A Fijivirus Major Viroplasm Protein Shows RNA-Stimulated ATPase Activity by Adopting Pentameric and Hexameric Assemblies of Dimers. mBio. doi: 10.1128/mbio.00023-23
  45. Lorvellec, M., et al. (2023). HMGB1 cleavage by complement C1s and its potent anti-inflammatory product. Front. Immunol. doi: 10.3389/fimmu.2023.1151731
  46. Maekelae, A. R., et al. (2023). Intranasal trimeric sherpabody inhibits SARS-CoV-2 including recent immunoevasive Omicron subvariants. Nat. Commun. doi: 10.1038/s41467-023-37290-6
  47. Makarov, A., et al. (2023). The role of invariant surface glycoprotein 75 in xenobiotic acquisition by African trypanosomes. Microb. Cell. doi: 10.15698/mic2023.02.790
  48. Makarov, M., et al. (2023). Early Selection of the Amino Acid Alphabet Was Adaptively Shaped by Biophysical Constraints of Foldability. J. Am. Chem. Soc. doi: 10.1021/jacs.2c12987
  49. Morichaud, Z., et al. (2023). Structural basis of the mycobacterial stress-response RNA polymerase auto-inhibition via oligomerization. Nat. Commun. doi: 10.1038/s41467-023-36113-y
  50. Moskalevska, I., et al. (2023). Intracellular accumulation and immunological response of NIR-II polymeric nanoparticles. Int. J. Pharm. doi: 10.1016/j.ijpharm.2022.122439
  51. Mrazova, K., et al. (2023). Urany-Less Low Voltage Transmission Electron Microscopy: A Powerful Tool for Ultrastructural Studying of Cyanobacterial Cells. Microorganisms. doi: 10.3390/microorganisms11040888
  52. Mukherjee, A., et al. (2023). An investigation on the multiple roles of CeO2 nanoparticle in electrochemical sensing: Biomimetic activity and electron acceptor. J. Electroanal. Chem. doi: 10.1016/j.jelechem.2023.117301
  53. Okhrimenko, I. S., et al. (2023). Mirror proteorhodopsins. Comm. Chem. doi: 10.1038/s42004-023-00884-8
  54. Pampararo, G., et al. (2023). Ethanol dehydrogenation to acetaldehyde with mesoporous Cu-SiO2 catalysts prepared by aerosol-assisted sol-gel. Chem. Eng. J. doi: 10.1016/j.cej.2023.142715
  55. Parigi, G., et al. (2023). Paramagnetic NMR restraints for the characterization of protein structural rearrangements. Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2023.102595
  56. Pham, L. B. T., et al. (2023). Direct Expression of Fluorinated Proteins in Human Cells for F-19 In-Cell NMR Spectroscopy. J. Am. Chem. Soc. doi: 10.1021/jacs.2c12086
  57. Popov, A. M., et al. (2023). Peltier-Based Experimental Device for Studying the Effect of Temperature on Protein Crystallization Kinetics. Cryst. Growth Des. doi: 10.1021/acs.cgd.2c01151
  58. Porkolab, V., et al. (2023). Powerful Avidity with a Limited Valency for Virus-Attachment Blockers on DC-SIGN: Combining Chelation and Statistical Rebinding with Structural Plasticity of the Receptor. ACS Central Sci. doi: 10.1021/acscentsci.2c01136
  59. Postel, S., et al. (2023). Quaternary glucocorticoid receptor structure highlights allosteric interdomain communication. Nat. Struct. Mol. Biol. doi: 10.1038/s41594-022-00914-4
  60. Prouteau, M., et al. (2023). EGOC inhibits TOROID polymerization by structurally activating TORC1. Nat. Struct. Mol. Biol. doi: 10.1038/s41594-022-00912-6
  61. Prysiazhnyi, V., et al. (2023). Fate of Gold Nanoparticles in Laser Desorption/Ionization Mass Spectrometry: Toward the Imaging of Individual Nanoparticles. J. Am. Soc. Mass Spectrom. doi: 10.1021/jasms.2c00300
  62. Querci, L., et al. (2023). NMR of Paramagnetic Proteins: C-13 Derived Paramagnetic Relaxation Enhancements Are an Additional Source of Structural Information in Solution. Magnetochemistry. doi: 10.3390/magnetochemistry9030066
  63. Ramic, D., et al. (2023). The Role of luxS in Campylobacter jejuni Beyond Intercellular Signaling. Microbiol. Spectr. doi: 10.1128/spectrum.02572-22
  64. Rehan, S., et al. (2023). Signal peptide mimicry primes Sec61 for client-selective inhibition. Nat. Chem. Biol. doi: 10.1038/s41589-023-01326-1
  65. Reiss, P., et al. (2023). Narrow Near-Infrared Emission from InP QDs Synthesized with Indium(I) Halides and Aminophosphine. J. Am. Chem. Soc. doi: 10.1021/jacs.2c13834
  66. Riccardi, C., et al. (2023). Metabolic Robustness to Growth Temperature of a Cold- Adapted Marine Bacterium. mSystems. doi: 10.1128/msystems.01124-22
  67. Rieu, P., et al. (2023). The F-box protein UFO controls flower development by redirecting the master transcription factor LEAFY to new cis-elements. Nat. Plants. doi: 10.1038/s41477-022-01336-2
  68. Saleun, S., et al. (2023). Analytical ultracentrifugation sedimentation velocity for the characterization of recombinant adeno-associated virus vectors sub-populations. Eur. Biophys. J. Biophys. Lett. doi: 10.1007/s00249-023-01650-3
  69. Schwarzer, S., et al. (2023). Archaeal Host Cell Recognition and Viral Binding of HFTV1 to Its Haloferax Host. mBio. doi: 10.1128/mbio.01833-22
  70. Selvaraj, M., et al. (2023). Structural basis underlying specific biochemical activities of non-muscle tropomyosin isoforms. Cell Reports. doi: 10.1016/j.celrep.2022.111900
  71. Simmonds, P., et al. (2023). Four principles to establish a universal virus taxonomy. PLoS. Biol. doi: 10.1371/journal.pbio.3001922
  72. Soulie, M., et al. (2023). Zwitterionic fluorinated detergents: From design to membrane protein applications. Biochimie. doi: 10.1016/j.biochi.2022.11.003
  73. Szczepanik, P. M., et al. (2023). Convergent Assembly of the Tricyclic Labdane Core Enables Synthesis of Diverse Forskolin-like Molecules. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202213183
  74. Tang, J. H., et al. (2023). Molecular Engineering of Self-Immolative Bioresponsive MR Probes. J. Am. Chem. Soc. doi: 10.1021/jacs.2c13672
  75. Torres, A., et al. (2023). About the Transient Effects of Synthetic Amorphous Silica: An In Vitro Study on Macrophages. Int. J. Mol. Sci. doi: 10.3390/ijms24010220
  76. Toubhans, B., et al. (2023). Selenium nanoparticles modulate histone methylation via lysine methyltransferase activity and S-adenosylhomocysteine depletion. Redox Biol. doi: 10.1016/j.redox.2023.102641
  77. Trapani, S., et al. (2023). Structure-guided mutagenesis of the capsid protein indicates that a nanovirus requires assembled viral particles for systemic infection. PLoS Pathog. doi: 10.1371/journal.ppat.1011086
  78. Trivellato, D., et al. (2023). Site-directed double monoubiquitination of the repeat domain of the amyloid-forming protein tau impairs self-assembly and coacervation. Bioorganic Chem. doi: 10.1016/j.bioorg.2023.106347
  79. Tsirigotaki, A., et al. (2023). Mechanism of receptor assembly via the pleiotropic adipokine Leptin. Nat. Struct. Mol. Biol. doi: 10.1038/s41594-023-00941-9
  80. Tully, M. D., et al. (2023). BioSAXS at European Synchrotron Radiation Facility - Extremely Brilliant Source: BM29 with an upgraded source, detector, robot, sample environment, data collection and analysis software. J. Synchrot. Radiat. doi: 10.1107/s1600577522011286
  81. Turner, D., et al. (2023). Abolishment of morphology-based taxa and change to binomial species names: 2022 taxonomy update of the ICTV bacterial viruses subcommittee. Arch. Virol. doi: 10.1007/s00705-022-05694-2
  82. Urzhumtseva, L., et al. (2023). Algorithms and programs for the shell decomposition of oscillating functions in space. J. Appl. Crystallogr. doi: 10.1107/s160057672201144x
  83. Vallet, A., et al. (2023). The plasma membrane-associated cation-binding protein PCaP1 of Arabidopsis thaliana is a uranyl-binding protein. J. Hazard. Mater. doi: 10.1016/j.jhazmat.2022.130668
  84. Vavra, J., et al. (2023). Characterization of the interaction between the tumour suppressor p53 and heme and its role in the protein conformational dynamics studied by various spectroscopic techniques and hydrogen/deuterium exchange coupled with mass spectrometry. J. Inorg. Biochem. doi: 10.1016/j.jinorgbio.2023.112180
  85. Verrucchi, M., et al. (2023). Characterization of a Ruthenium(II) Complex in Singlet Oxygen-Mediated Photoelectrochemical Sensing. Langmuir. doi: 10.1021/acs.langmuir.2c03042
  86. Veverka, P., et al. (2023). Electron microscopy reveals toroidal shape of master neuronal cell differentiator REST - RE1-silencing transcription factor. Comp. Struct. Biotechnol. J.. doi: 10.1016/j.csbj.2022.12.026
  87. Vrchovecka, K., et al. (2023). Effect of titanium nanostructured surface on fibroblast behavior. J. Biomed. Mater. Res. Part A. doi: 10.1002/jbm.a.37531

2022

  1. Abouelezz, A., et al. (2022). The mammalian endocytic cytoskeleton. Eur. J. Cell Biol. doi: 10.1016/j.ejcb.2022.151222
  2. Adam, V., et al. (2022). Rational Control of Off-State Heterogeneity in a Photoswitchable Fluorescent Protein Provides Switching Contrast Enhancement. ChemPhysChem. doi: 10.1002/cphc.202200192
  3. Adamkova, K., et al. (2022). Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects. Acta Crystallogr. Sect. D-Struct. Biol. doi: 10.1107/s2059798322008397
  4. Albert, L., et al. (2022). Bistable Photoswitch Allows in Vivo Control of Hematopoiesis. ACS Central Sci. doi: 10.1021/acscentsci.1c00434
  5. Almeida-Souza, L., et al. (2022). A kinder approach to science. doi: 10.1016/j.tcb.2021.11.003
  6. Al-Otaibi, N., et al. (2022). Sample preparation in single particle cryo-EM: general discussion. Faraday Discuss. doi: 10.1039/d2fd90059a
  7. Altmannova, V., et al. (2022). The role of bivalent ions in the regulation of D-loop extension mediated by DMC1 during meiotic recombination. iScience. doi: 10.1016/j.isci.2022.105439
  8. Amara, P., et al. (2022). L-tyrosine-bound ThiH structure reveals C-C bond break differences within radical SAM aromatic amino acid lyases. Nat. Commun. doi: 10.1038/s41467-022-29980-4
  9. Andreeva, E. A., et al. (2022). Oligomerization processes limit photoactivation and recovery of the orange carotenoid protein. Biophys. J. doi: 10.1016/j.bpj.2022.07.004
  10. Andronov, L., et al. (2022). splitSMLM, a spectral demixing method for high-precision multi-color localization microscopy applied to nuclear pore complexes. Commun. Biol. doi: 10.1038/s42003-022-04040-1
  11. Araujo, L. D. S., et al. (2022). Hierarchical assembly of pH-responsive surfactant-cyclodextrin complexes. Soft Matter. doi: 10.1039/d2sm00807f
  12. Arias-Alpizar, G., et al. (2022). Phase-Separated Liposomes Hijack Endogenous Lipoprotein Transport and Metabolism Pathways to Target Subsets of Endothelial Cells In Vivo. Adv. Healthc. Mater. doi: 10.1002/adhm.202202709
  13. Arragain, B., et al. (2022). Structural snapshots of La Crosse virus polymerase reveal the mechanisms underlying Peribunyaviridae replication and transcription. Nat. Commun. doi: 10.1038/s41467-022-28428-z
  14. Asai, S., et al. (2022). Characterization of insulin crystalline form in isolated beta-cell secretory granules. Open Biol. doi: 10.1098/rsob.220322
  15. Ashok, Y., et al. (2022). Reconstitution of the DTX3L PARP9 complex reveals determinants for high-affinity heterodimerization and multimeric assembly. Biochem. J. doi: 10.1042/bcj20210722
  16. Astashkin, R., et al. (2022). Structural insights into light-driven anion pumping in cyanobacteria. Nat. Commun. doi: 10.1038/s41467-022-34019-9
  17. Aumonier, S., et al. (2022). Slow protein dynamics probed by time-resolved oscillation crystallography at room temperature. IUCrJ. doi: 10.1107/s2052252522009150
  18. Bahar, M. W., et al. (2022). A conserved glutathione binding site in poliovirus is a target for antivirals and vaccine stabilisation. Commun. Biol. doi: 10.1038/s42003-022-04252-5
  19. Barbone, G. E., et al. (2022). X-ray multiscale 3D neuroimaging to quantify cellular aging and neurodegeneration postmortem in a model of Alzheimer's disease. Eur. J. Nucl. Med. Mol. Imaging. doi: 10.1007/s00259-022-05896-5
  20. Beinsteiner, B., et al. (2022). A novel nuclear receptor subfamily enlightens the origin of heterodimerization. BMC Biol. doi: 10.1186/s12915-022-01413-0
  21. Beniamino, Y., et al. (2022). The Ni(II)-Binding Activity of the Intrinsically Disordered Region of Human NDRG1, a Protein Involved in Cancer Development. Biomolecules. doi: 10.3390/biom12091272
  22. Berg, H., et al. (2022). Comprehensive Fragment Screening of the SARS-CoV-2 Proteome Explores Novel Chemical Space for Drug Development. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202205858
  23. Bernaudat, F., et al. (2022). Structural basis of DNA methylation-dependent site selectivity of the Epstein-Barr virus lytic switch protein ZEBRA/Zta/BZLF1. Nucleic Acids Res. doi: 10.1093/nar/gkab1183
  24. Bertuzzi, S., et al. (2022). Immobilization of Biantennary N-Glycans Leads to Branch Specific Epitope Recognition by LSECtin. ACS Central Sci. doi: 10.1021/acscentsci.2c00719
  25. Bessa, L. M., et al. (2022). The intrinsically disordered SARS-CoV-2 nucleoprotein in dynamic complex with its viral partner nsp3a. Sci. Adv. doi: 10.1126/sciadv.abm4034
  26. Besson, S., et al. (2022). Adenovirus-Inspired Virus-Like-Particles Displaying Melanoma Tumor Antigen Specifically Target Human DC Subsets and Trigger Antigen-Specific Immune Responses. Biomedicines. doi: 10.3390/biomedicines10112881
  27. Blaha, J., et al. (2022). Structure of the human NK cell NKR-P1:LLT1 receptor:ligand complex reveals clustering in the immune synapse. Nat. Commun. doi: 10.1038/s41467-022-32577-6
  28. Blahut, J., et al. (2022). Sensitivity-Enhanced Multidimensional Solid-State NMR Spectroscopy by Optimal-Control-Based Transverse Mixing Sequences. J. Am. Chem. Soc. doi: 10.1021/jacs.2c06568
  29. Borshchevskiy, V., et al. (2022). True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins. Nat. Struct. Mol. Biol. doi: 10.1038/s41594-022-00762-2
  30. Bouchalova, P., et al. (2022). Characterization of the AGR2 Interactome Uncovers New Players of Protein Disulfide Isomerase Network in Cancer Cells. Mol. Cell. Proteomics. doi: 10.1016/j.mcpro.2021.100188
  31. Bourhis, J. M., et al. (2022). Structural Dynamics of the C-terminal X Domain of Nipah and Hendra Viruses Controls the Attachment to the C-terminal Tail of the Nucleocapsid Protein. J. Mol. Biol. doi: 10.1016/j.jmb.2022.167551
  32. Bruno, F., et al. (2022). Lysozyme is Sterically Trapped Within the Silica Cage in Bioinspired Silica-Lysozyme Composites: A Multi-Technique Understanding of Elusive Protein-Material Interactions. Langmuir. doi: 10.1021/acs.langmuir.2c00836
  33. Bulteau, F., et al. (2022). Targeting Tn-Antigen-Positive Human Tumors with a Recombinant Human Macrophage Galactose C-Type Lectin. Mol. Pharm. doi: 10.1021/acs.molpharmaceut.1c00744
  34. Camacho-Zarco, A. R., et al. (2022). NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins. Chem. Rev. doi: 10.1021/acs.chemrev.1c01023
  35. Camponeschi, F., et al. (2022). Metal trafficking in the cell: Combining atomic resolution with cellular dimension. FEBS Lett. doi: 10.1002/1873-3468.14524
  36. Camponeschi, F., et al. (2022). Molecular Basis of Rare Diseases Associated to the Maturation of Mitochondrial 4Fe-4S -Containing Proteins. Biomolecules. doi: 10.3390/biom12071009
  37. Camponeschi, F., et al. (2022). The Intriguing mitoNEET: Functional and Spectroscopic Properties of a Unique 2Fe-2S Cluster Coordination Geometry. Molecules. doi: 10.3390/molecules27238218
  38. Cantini, F., et al. (2022). 2D NMR Analysis as a Sensitive Tool for Evaluating the Higher-Order Structural Integrity of Monoclonal Antibody against COVID-19. Pharmaceutics. doi: 10.3390/pharmaceutics14101981
  39. Caputo, S., et al. (2022). Study and application of graphene oxide in the synthesis of 2,3-disubstituted quinolines via a Povarov multicomponent reaction and subsequent oxidation. RSC Adv. doi: 10.1039/d2ra01752k
  40. Casasnovas, J. M., et al. (2022). Nanobodies Protecting From Lethal SARS-CoV-2 Infection Target Receptor Binding Epitopes Preserved in Virus Variants Other Than Omicron. Front. Immunol. doi: 10.3389/fimmu.2022.863831
  41. Cawood, E. E., et al. (2022). Microsecond Backbone Motions Modulate the Oligomerization of the DNAJB6 Chaperone. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202116403
  42. Cerofolini, L., et al. (2022). Solid-state NMR methods for the characterization of bioconjugations and protein-material interactions. Solid State Nucl. Magn. Reson. doi: 10.1016/j.ssnmr.2022.101828
  43. Cerofolini, L., et al. (2023). Solid-state NMR - a complementary technique for protein framework characterization. Chem. Commun. doi: 10.1039/d2cc05725e
  44. Chambon, L., et al. (2022). PAP8/pTAC6 Is Part of a Nuclear Protein Complex and Displays RNA Recognition Motifs of Viral Origin. Int. J. Mol. Sci. doi: 10.3390/ijms23063059
  45. Chaptal, V., et al. (2022). Substrate-bound and substrate-free outward-facing structures of a multidrug ABC exporter. Sci. Adv. doi: 10.1126/sciadv.abg9215
  46. Chen, H. Y., et al. (2022). Assembly of Fluorescent Polymer Nanoparticles Using Different Microfluidic Mixers. Langmuir. doi: 10.1021/acs.langmuir.2c00534
  47. Cherrier, M. V., et al. (2022). Oxygen-Sensitive Metalloprotein Structure Determination by Cryo-Electron Microscopy. Biomolecules. doi: 10.3390/biom12030441
  48. Chevillard, C., et al. (2022). Elicitation of potent SARS-CoV-2 neutralizing antibody responses through immunization with a versatile adenovirus-inspired multimerization platform. Mol. Ther. doi: 10.1016/j.ymthe.2022.02.011
  49. Chouquet, A., et al. (2022). Biophysical Characterization of the Oligomeric States of Recombinant Immunoglobulins Type-M and Their C1q-Binding Kinetics by Biolayer Interferometry. Front. Bioeng. Biotechnol. doi: 10.3389/fbioe.2022.816275
  50. Christie, M. S., et al. (2022). Characterisation of a common hotspot variant in acute intermittent porphyria sheds light on the mechanism of hydroxymethylbilane synthase function. FEBS Open Bio. doi: 10.1002/2211-5463.13490
  51. Chuzeville, L., et al. (2022). Eco-friendly processes for the synthesis of amorphous calcium carbonate nanoparticles in ethanol and their stabilisation in aqueous media. Green Chem. doi: 10.1039/d1gc03396d
  52. Ciani, C., et al. (2022). Identification and Characterization of an RRM-Containing, RNA Binding Protein in Acinetobacter baumannii. Biomolecules. doi: 10.3390/biom12070922
  53. Clark, J. M., et al. (2022). Structure-Based Design of a Novel Class of Autotaxin Inhibitors Based on Endogenous Allosteric Modulators. J. Med. Chem. doi: 10.1021/acs.jmedchem.2c00368
  54. Cojocaru, R., et al. (2022). A biological nanofoam: The wall of coniferous bisaccate pollen. Sci. Adv. doi: 10.1126/sciadv.abd0892
  55. Combes, A., et al. (2022). Protein-like particles through nanoprecipitation of mixtures of polymers of opposite charge. J. Colloid Interface Sci. doi: 10.1016/j.jcis.2021.09.080
  56. Condado, J. G., et al. (2022). Automatic determination of the handedness of single-particle maps of macromolecules solved by CryoEM. J. Struct. Biol. doi: 10.1016/j.jsb.2022.107915
  57. Conti, L., et al. (2022). Ferritin nanocomposites for the selective delivery of photosensitizing ruthenium-polypyridyl compounds to cancer cells. Inorg. Chem. Front. doi: 10.1039/d1qi01268a
  58. Corbeski, I., et al. (2022). Chaperoning of the histone octamer by the acidic domain of DNA repair factor APLF. Sci. Adv. doi: 10.1126/sciadv.abo0517
  59. Cousido-Siah, A., et al. (2022). A scalable strategy to solve structures of PDZ domains and their complexes. doi: 10.1107/s2059798322001784
  60. Darouich, O., et al. (2022). 3D multiscale analysis of the hierarchical porosity in Coscinodiscus sp. diatoms using a combination of tomographic techniques. Nanoscale Adv. doi: 10.1039/d1na00691f
  61. Dave, Z., et al. (2022). Lyn Phosphorylates and Controls ROR1 Surface Dynamics During Chemotaxis of CLL Cells. Front. Cell. Dev. Biol. doi: 10.3389/fcell.2022.838871
  62. de la Morena, J. J., et al. (2022). ScipionTomo: Towards cryo-electron tomography software integration, reproducibility, and validation. J. Struct. Biol. doi: 10.1016/j.jsb.2022.107872
  63. De Simone, N. A., et al. (2022). Monofunctionalized Fluorinated Bambusurils and Their Conjugates for Anion Transport and Extraction. J. Org. Chem. doi: 10.1021/acs.joc.2c00870
  64. Decelle, J., et al. (2022). Intracellular development and impact of a marine eukaryotic parasite on its zombified microalgal host. Isme J. doi: 10.1038/s41396-022-01274-z
  65. Dejnirattisai, W., et al. (2022). SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses. Cell. doi: 10.1016/j.cell.2021.12.046
  66. Dejnirattisai, W., et al. (2022). Reduced neutralisation of SARS-CoV-2 omicron B.1.1.529 variant by post-immunisation serum. Lancet. doi: 10.1016/s0140-6736(21)02844-0
  67. Demina, T. A., et al. (2022). Virus-Host Interactions and Genetic Diversity of Antarctic Sea Ice Bacteriophages. mBio. doi: 10.1128/mbio.00651-22
  68. Depelteau, J. S., et al. (2022). UVC inactivation of pathogenic samples suitable for cryo-EM analysis. Commun. Biol. doi: 10.1038/s42003-021-02962-w
  69. Devcic, J., et al. (2022). Immediate and Sustained Effects of Cobalt and Zinc-Containing Pigments on Macrophages. Front. Immunol. doi: 10.3389/fimmu.2022.865239
  70. Dey, S., et al. (2022). Structural insights into RNA-mediated transcription regulation in bacteria. Mol. Cell. doi: 10.1016/j.molcel.2022.09.020
  71. Dhawan, V., et al. (2022). Polysaccharide and monosaccharide guided liver delivery of Sorafenib Tosylate - A nano-strategic approach and comparative assessment of hepatospecificity. Int. J. Pharm. doi: 10.1016/j.ijpharm.2022.122039
  72. Di Cesare, F., et al. (2022). Age- and Sex-Dependent Changes of Free Circulating Blood Metabolite and Lipid Abundances, Correlations, and Ratios. J. Gerontol. Ser. A-Biol. Sci. Med. Sci. doi: 10.1093/gerona/glab335
  73. Di Cesare, F., et al. (2022). Association of Plasma Metabolites and Lipoproteins with Rh and ABO Blood Systems in Healthy Subjects. J. Proteome Res. doi: 10.1021/acs.jproteome.2c00375
  74. Di Cesare, F., et al. (2022). Lipid and metabolite correlation networks specific to clinical and biochemical covariate show differences associated with sexual dimorphism in a cohort of nonagenarians. GeroScience. doi: 10.1007/s11357-021-00404-3
  75. Di Micco, S., et al. (2022). Rational design of the zonulin inhibitor AT1001 derivatives as potential anti SARS-CoV-2. Eur. J. Med. Chem. doi: 10.1016/j.ejmech.2022.114857
  76. Dijokaite-Guraliuc, A., et al. (2022). Antigenic characterization of SARS-CoV-2 Omicron subvariant BA.4.6. Cell Discov. doi: 10.1038/s41421-022-00493-0
  77. Dimitri, G. M., et al. (2022). NMR Spectroscopy Combined with Machine Learning Approaches for Age Prediction in Healthy and Parkinson's Disease Cohorts through Metabolomic Fingerprints. Appl. Sci.-Basel. doi: 10.3390/app12188954
  78. Dolce, L. G., et al. (2022). Structural basis for sequence-independent substrate selection by eukaryotic wobble base tRNA deaminase ADAT2/3. Nat. Commun. doi: 10.1038/s41467-022-34441-z
  79. Domanska, A., et al. (2022). Structural Studies Reveal that Endosomal Cations Promote Formation of Infectious Coxsackievirus A9 A-Particles, Facilitating RNA and VP4 Release. J. Virol. doi: 10.1128/jvi.01367-22
  80. Dou, Y. N., et al. (2022). Chemical fingerprinting of phenolic compounds in Finnish berry wines using Fourier transform ion cyclotron resonance mass spectrometry. Food Chem. doi: 10.1016/j.foodchem.2022.132303
  81. Drillien, R., et al. (2022). Efficient production of protein complexes in mammalian cells using a poxvirus vector. PLoS One. doi: 10.1371/journal.pone.0279038
  82. Duong, T. M., et al. (2022). Room-Temperature Doping of CsPbBr3 Nanocrystals with Aluminum. J. Phys. Chem. Lett. doi: 10.1021/acs.jpclett.2c01021
  83. Duong, T. M., et al. (2022). Practice of electron microscopy on nanoparticles sensitive to radiation damage: CsPbBr3 nanocrystals as a case study. Front. Chem. doi: 10.3389/fchem.2022.1058620
  84. Durnik, R., et al. (2022). Bile Acids Transporters of Enterohepatic Circulation for Targeted Drug Delivery. Molecules. doi: 10.3390/molecules27092961
  85. El Masri, R., et al. (2022). Extracellular endosulfatase Sulf-2 harbors a chondroitin/dermatan sulfate chain that modulates its enzyme activity. Cell Reports. doi: 10.1016/j.celrep.2022.110516
  86. Engelberg, Y., et al. (2022). Rare by Natural Selection: Disulfide-Bonded Supramolecular Antimicrobial Peptides. Biomacromolecules. doi: 10.1021/acs.biomac.1c01353
  87. Eskelin, K., et al. (2022). Archaeal Viruses: Production of Virus Particles and Vesicle-like Viruses and Purification Using Asymmetrical Flow Field-Flow Fractionation. Methods Mol Biol. doi: 10.1007/978-1-0716-2445-6_31
  88. Fagiewicz, R., et al. (2022). In vitro characterization of the full-length human dynein-1 cargo adaptor BicD2. Structure. doi: 10.1016/j.str.2022.08.009
  89. Falchi, F. A., et al. (2022). Suppressor Mutations in LptF Bypass Essentiality of LptC by Forming a Six-Protein Transenvelope Bridge That Efficiently Transports Lipopolysaccharide. mBio. doi: 10.1128/mbio.02202-22
  90. Farci, D., et al. (2022). The structured organization of Deinococcus radiodurans' cell envelope. Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.2209111119
  91. Felix, J., et al. (2022). The AAA plus ATPase RavA and its binding partner ViaA modulate E. coli aminoglycoside sensitivity through interaction with the inner membrane. Nat. Commun. doi: 10.1038/s41467-022-32992-9
  92. Felli, I. C., et al. (2022). C-13 Direct Detected NMR for Challenging Systems. Chem. Rev. doi: 10.1021/acs.chemrev.1c00871
  93. Fernandes, A. D., et al. (2022). Conservation and divergence of the G-interfaces of Drosophila melanogaster septins. Cytoskeleton. doi: 10.1002/cm.21740
  94. Fernandes, C. A. H., et al. (2022). Cryo-electron microscopy unveils unique structural features of the human Kir2.1 channel. Sci. Adv. doi: 10.1126/sciadv.abq8489
  95. Flanders, P. L., et al. (2022). Combined Structural Analysis and Molecular Dynamics Reveal Penicillin-Binding Protein Inhibition Mode with ?-Lactones. ACS Chem. Biol. doi: 10.1021/acschembio.2c00503
  96. Foucher, A. E., et al. (2022). Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex. Nat. Commun. doi: 10.1038/s41467-022-32542-3
  97. Furlan, C., et al. (2022). Structural insight on the mechanism of an electron-bifurcating [FeFe] hydrogenase. eLife. doi: 10.7554/eLife.79361
  98. Fuzik, T., et al. (2022). Structure of Human Enterovirus 70 and Its Inhibition by Capsid-Binding Compounds. J. Virol. doi: 10.1128/jvi.00604-22
  99. Gahura, O., et al. (2022). An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases. Nat. Commun. doi: 10.1038/s41467-022-33588-z
  100. Galera-Prat, A., et al. (2022). Protein engineering approach to enhance activity assays of mono-ADP-ribosyltransferases through proximity. Protein Eng. Des. Sel. doi: 10.1093/protein/gzac006
  101. Gallorini, R., et al. (2022). Subcritical Hydrothermal Liquefaction as a Pretreatment for Enzymatic Degradation of Polyurethane. ACS Omega. doi: 10.1021/acsomega.2c04734
  102. Gauto, D. F., et al. (2022). Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR. Nat. Commun. doi: 10.1038/s41467-022-29423-0
  103. Gerard, F. C. A., et al. (2022). Structure and Dynamics of the Unassembled Nucleoprotein of Rabies Virus in Complex with Its Phosphoprotein Chaperone Module. Viruses-Basel. doi: 10.3390/v14122813
  104. Ghini, V., et al. (2022). Impact of the pre-examination phase on multicenter metabolomic studies. New Biotech. doi: 10.1016/j.nbt.2022.01.006
  105. Ghini, V., et al. (2022). Serum NMR Profiling Reveals Differential Alterations in the Lipoproteome Induced by Pfizer-BioNTech Vaccine in COVID-19 Recovered Subjects and Naive Subjects. Front. Mol. Biosci. doi: 10.3389/fmolb.2022.839809
  106. Ghini, V., et al. (2022). Comparative NMR metabolomics of the responses of A2780 human ovarian cancer cells to clinically established Pt-based drugs. Dalton Trans. doi: 10.1039/d2dt02068h
  107. Ghini, V., et al. (2022). Profiling metabolites and lipoproteins in COMETA, an Italian cohort of COVID-19 patients. PLoS Pathog. doi: 10.1371/journal.ppat.1010443
  108. Giallongo, S., et al. (2022). Histone Variant macroH2A1.1 Enhances Nonhomologous End Joining-dependent DNA Double-strand-break Repair and Reprogramming Efficiency of Human iPSCs. Stem Cells. doi: 10.1093/stmcls/sxab004
  109. Gogl, G., et al. (2022). Quantitative fragmentomics allow affinity mapping of interactomes. Nat. Commun. doi: 10.1038/s41467-022-33018-0
  110. Golan, N., et al. (2022). Structure and Conservation of Amyloid Spines From the Candida albicans Als5 Adhesin. Front. Mol. Biosci. doi: 10.3389/fmolb.2022.926959
  111. Gomez-Bouzo, U., et al. (2022). Development of novel Gemini-cholesterol analogues for retinoid-related orphan receptors. Org. Chem. Front. doi: 10.1039/d2qo00040g
  112. Gomez-Oca, R., et al. (2022). Differential impact of ubiquitous and muscle dynamin 2 isoforms in muscle physiology and centronuclear myopathy. Nat. Commun. doi: 10.1038/s41467-022-34490-4
  113. Gonnin, L., et al. (2022). Importance of RNA length for in vitro encapsidation by the nucleoprotein of human respiratory syncytial virus. J. Biol. Chem. doi: 10.1016/j.jbc.2022.102337
  114. Gory-Fauré, S., et al. (2022). Cryo-EM Visualization of Neuronal Particles Inside Microtubules. Methods Mol Biol. doi: 10.1007/978-1-0716-1983-4_24
  115. Goti, G., et al. (2022). Precision Glycodendrimers for DC-SIGN Targeting. Eur. J. Org. Chem. doi: 10.1002/ejoc.202200113
  116. Goutam, K., et al. (2022). Structural basis of sodium-dependent bile salt uptake into the liver. Nature. doi: 10.1038/s41586-022-04723-z
  117. Grybchuk, D., et al. (2022). Structures of L-BC virus and its open particle provide insight into Totivirus capsid assembly. Commun. Biol. doi: 10.1038/s42003-022-03793-z
  118. Guillon, A., et al. (2022). Host succinate inhibits influenza virus infection through succinylation and nuclear retention of the viral nucleoprotein. Embo J. doi: 10.15252/embj.2021108306
  119. Hadjidemetriou, K., et al. (2022). Time-resolved serial femtosecond crystallography on fatty-acid photodecarboxylase: lessons learned. Acta Crystallogr. Sect. D-Struct. Biol. doi: 10.1107/s2059798322007525
  120. Hanbouch, L., et al. (2022). Specific Mutations in the Cholesterol-Binding Site of APP Alter Its Processing and Favor the Production of Shorter, Less Toxic A beta Peptides. Mol. Neurobiol. doi: 10.1007/s12035-022-03025-9
  121. Haye, L., et al. (2022). Enhancing Near Infrared II Emission of Gold Nanoclusters via Encapsulation in Small Polymer Nanoparticles. Adv. Opt. Mater. doi: 10.1002/adom.202201474
  122. Henot, F., et al. (2022). NMR assignment of human HSP90 N-terminal domain bound to a long residence time resorcinol ligand. Biomol. NMR Assign. doi: 10.1007/s12104-022-10089-0
  123. Henot, F., et al. (2022). Visualizing the transiently populated closed-state of human HSP90 ATP binding domain. Nat Commun. doi: 10.1038/s41467-022-35399-8
  124. Herrera-Gonzalez, I., et al. (2022). Mannobioside biomimetics that trigger DC-SIGN binding selectivity. Chem. Commun. doi: 10.1039/d2cc04478a
  125. Hluchy, M., et al. (2022). CDK11 regulates pre-mRNA splicing by phosphorylation of SF3B1. Nature. doi: 10.1038/s41586-022-05204-z
  126. Hochheiser, I. V., et al. (2022). Structure of the NLRP3 decamer bound to the cytokine release inhibitor CRID3. Nature. doi: 10.1038/s41586-022-04467-w
  127. Hogrel, G., et al. (2022). Cyclic nucleotide-induced helical structure activates a TIR immune effector. Nature. doi: 10.1038/s41586-022-05070-9
  128. Hogrel, G., et al. (2022). Characterization of a small tRNA-binding protein that interacts with the archaeal proteasome complex. Mol. Microbiol. doi: 10.1111/mmi.14948
  129. Hricovini, M., et al. (2022). Chemistry towards Biology-Instruct: Snapshot. Int. J. Mol. Sci. doi: 10.3390/ijms232314815
  130. Hruska, P., et al. (2022). Proteomic Signatures of Human Visceral and Subcutaneous Adipocytes. J. Clin. Endocrinol. Metab. doi: 10.1210/clinem/dgab756
  131. Huang, K. Y. A., et al. (2022). Structures and therapeutic potential of anti-RBD human monoclonal antibodies against SARS-CoV-2. Theranostics. doi: 10.7150/thno.65563
  132. Hurdiss, D. L., et al. (2022). Fluoxetine targets an allosteric site in the enterovirus 2C AAA+ ATPase and stabilizes a ring-shaped hexameric complex. Sci. Adv. doi: 10.1126/sciadv.abj7615
  133. Hutin, S., et al. (2022). The Vaccinia Virus DNA Helicase Structure from Combined Single-Particle Cryo-Electron Microscopy and AlphaFold2 Prediction. Viruses-Basel. doi: 10.3390/v14102206
  134. Iannelli, G., et al. (2022). Turning Nonselective Inhibitors of Type I Protein Arginine Methyltransferases into Potent and Selective Inhibitors of Protein Arginine Methyltransferase 4 through a Deconstruction- Reconstruction and Fragment-Growing Approach. J. Med. Chem. doi: 10.1021/acs.jmedchem.2c00252
  135. Ibrahim, Z., et al. (2022). Structural insights into p300 regulation and acetylation-dependent genome organisation. Nat Commun. doi: 10.1038/s41467-022-35375-2
  136. Indorato, R. L., et al. (2022). Drug resistance dependent on allostery: A P-loop rigor Eg5 mutant exhibits resistance to allosteric inhibition by STLC. Front. Oncol. doi: 10.3389/fonc.2022.965455
  137. Jaklin, M., et al. (2022). A new fibrillization mechanism of fl-lactoglobulin in glycine solutions. Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2022.06.182
  138. Janata, M., et al. (2022). Tailoring Butyl Methacrylate/Methacrylic Acid Copolymers for the Solubilization of Membrane Proteins: The Influence of Composition and Molecular Weight. Macromol. Biosci. doi: 10.1002/mabi.202200284
  139. Javed, W., et al. (2022). Structural Insights into the Catalytic Cycle of a Bacterial Multidrug ABC Efflux Pump. J. Mol. Biol. doi: 10.1016/j.jmb.2022.167541
  140. Jessop, M., et al. (2022). Structural and biochemical characterisation of the Providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation. Commun. Biol. doi: 10.1038/s42003-022-03276-1
  141. Jezkova, P., et al. (2022). Differentiation of Sialyl Linkages Using a Combination of Alkyl Esterification and Phenylhydrazine Derivatization: Application for N-Glycan Profiling in the Sera of Patients with Lung Cancer. Anal. Chem. doi: 10.1021/acs.analchem.2c00105
  142. Jover, A. B., et al. (2022). The archaeal division protein CdvB1 assembles into polymers that are depolymerized by CdvC. FEBS Lett. doi: 10.1002/1873-3468.14324
  143. K., K., et al. (2022). Swarms of chemically modified antiviral siRNA targeting herpes simplex virus infection in human corneal epithelial cells. PLoS Path. doi: 10.1371/journal.ppat.1010688
  144. Kabanov, D., et al. (2022). Atomic force spectroscopy is a promising tool to study contractile properties of cardiac cells. Micron. doi: 10.1016/j.micron.2021.103199
  145. Kabelka, I., et al. (2022). Magainin 2 and PGLa in bacterial membrane mimics III: Membrane fusion and disruption. Biophys. J. doi: 10.1016/j.bpj.2021.12.035
  146. Kalina, M., et al. (2022). Biochar Texture-A Parameter Influencing Physicochemical Properties, Morphology, and Agronomical Potential. Agronomy-Basel. doi: 10.3390/agronomy12081768
  147. Kao, W. C., et al. (2022). Structural basis for safe and efficient energy conversion in a respiratory supercomplex. Nat. Commun. doi: 10.1038/s41467-022-28179-x
  148. Kasiliauskaite, A., et al. (2022). Cooperation between intrinsically disordered and ordered regions of Spt6 regulates nucleosome and Pol II CTD binding, and nucleosome assembly. Nucleic Acids Res. doi: 10.1093/nar/gkac451
  149. Katri, E., et al. (2022). Analysis and purification of ssRNA and dsRNA molecules using asymmetrical flow field flow fractionation. J. Chromatogr. A. doi: 10.1016/j.chroma.2022.463525
  150. Kaurov, I., et al. (2022).

    The essential cysteines in the CIPC motif of the thioredoxin-like Trypanosoma brucei MICOS subunit TbMic20 do not form an intramolecular disulfide bridge in vivo

    . Mol. Biochem. Parasitol. doi: 10.1016/j.molbiopara.2022.111463
  151. Kaushik, M., et al. (2022). Trehalose matrices for high temperature dynamic nuclear polarization enhanced solid state NMR. Phys. Chem. Chem. Phys. doi: 10.1039/d2cp00970f
  152. Kehlenbeck, D. M., et al. (2022). Cryo-EM structure of MsbA in saposin-lipid nanoparticles (Salipro) provides insights into nucleotide coordination. Febs J. doi: 10.1111/febs.16327
  153. Kejzar, N., et al. (2022). Cryo-EM structure of ssDNA bacteriophage ΦCjT23 provides insight into early virus evolution. Nat Commun. doi: 10.1038/s41467-022-35123-6
  154. Kelly, J. J., et al. (2022). Snapshots of actin and tubulin folding inside the TRiC chaperonin. Nat. Struct. Mol. Biol. doi: 10.1038/s41594-022-00755-1
  155. Keown, J. R., et al. (2022). Mapping inhibitory sites on the RNA polymerase of the 1918 pandemic influenza virus using nanobodies. Nat. Commun. doi: 10.1038/s41467-021-27950-w
  156. Khorramaki, M., et al. (2022). Competitor hydrogen-bond acceptors in the SP(NH)3-based structures: Comparison of structural features - Computational/database and experimental. Polyhedron. doi: 10.1016/j.poly.2022.116157
  157. Killer, M., et al. (2022). Cryo-EM Structure of an Atypical Proton-Coupled Peptide Transporter: Di- and Tripeptide Permease C. Front. Mol. Biosci. doi: 10.3389/fmolb.2022.917725
  158. Klimovic, S., et al. (2022). Aminophylline Induces Two Types of Arrhythmic Events in Human Pluripotent Stem Cell–Derived Cardiomyocytes. Front. Pharmacol. doi: 10.3389/fphar.2021.789730
  159. Klodova, B., et al. (2022). Regulatory dynamics of gene expression in the developing male gametophyte of Arabidopsis. Plant Reprod. doi: 10.1007/s00497-022-00452-5
  160. Koktava, M., et al. (2022). Metal Oxide Laser Ionization Mass Spectrometry Imaging of Fatty Acids and Their Double Bond Positional Isomers. Anal. Chem. doi: 10.1021/acs.analchem.2c00551
  161. Koning, R. I., et al. (2022). Automated vitrification of cryo-EM samples with controllable sample thickness using suction and real-time optical inspection. Nat. Commun. doi: 10.1038/s41467-022-30562-7
  162. Kopf, A. H., et al. (2022). Synthesis and Evaluation of a Library of Alternating Amphipathic Copolymers to Solubilize and Study Membrane Proteins. doi: 10.1021/acs.biomac.1c01166
  163. Kotila, T., et al. (2022). Structural basis of rapid actin dynamics in the evolutionarily divergent Leishmania parasite. Nat. Commun. doi: 10.1038/s41467-022-31068-y
  164. Koval'ova, T., et al. (2022). The first structure-function study of GH151 alpha-l-fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity. Febs J. doi: 10.1111/febs.16387
  165. Kracikova, L., et al. (2022). Phosphorus-Containing Polymeric Zwitterion: A Pioneering Bioresponsive Probe for P-31-Magnetic Resonance Imaging. Macromol. Biosci. doi: 10.1002/mabi.202100523
  166. Kuchaříková, H., et al. (2022). Quantitative Analysis of Posttranslational Modifications of Plant Histones. Methods Mol Biol. doi: 10.1007/978-1-0716-2469-2_18
  167. Kundrat, V., et al. (2022). Nanofibers of solid-solution thorium(IV)-uranium(IV) oxides by electrospinning. J. Nucl. Mater. doi: 10.1016/j.jnucmat.2022.153731
  168. Kundrat, V., et al. (2022). Preparation of polycrystalline tungsten nanofibers by needleless electrospinning. J. Alloy. Compd. doi: 10.1016/j.jallcom.2021.163542
  169. Kurttila, M., et al. (2022). The structural effect between the output module and chromophore-binding domain is a two-way street via the hairpin extension. Photochem. Photobiol. Sci. doi: 10.1007/s43630-022-00265-5
  170. Lafaye, C., et al. (2022). Riboflavin-binding proteins for singlet oxygen production. Photochem. Photobiol. Sci. doi: 10.1007/s43630-021-00156-1
  171. Landskron, L., et al. (2022). Posttranslational modification of microtubules by the MATCAP detyrosinase. Science. doi: 10.1126/science.abn6020
  172. Lapcik, P., et al. (2022). A large-scale assay library for targeted protein quantification in renal cell carcinoma tissues. Proteomics. doi: 10.1002/pmic.202100228
  173. Latrova, K., et al. (2023). R-Type Fonticins Produced by Pragia fontium Form Large Pores with High Conductance. J. Bacteriol. doi: 10.1128/jb.00315-22
  174. Legartova, S., et al. (2022). The Highest Density of Phosphorylated Histone H1 Appeared in Prophase and Prometaphase in Parallel with Reduced H3K9me3, and HDAC1 Depletion Increased H1.2/H1.3 and H1.4 Serine 38 Phosphorylation. Life-Basel. doi: 10.3390/life12060798
  175. Leisico, F., et al. (2022). Structure of the human heparan sulfate polymerase complex EXT1-EXT2. Nat. Commun. doi: 10.1038/s41467-022-34882-6
  176. Levanova, A. A., et al. (2022). Native RNA Purification Method for Small RNA Molecules Based on Asymmetrical Flow Field-Flow Fractionation. Pharmaceuticals. doi: 10.3390/ph15020261
  177. Licari, C., et al. (2022). Nuclear Magnetic Resonance-Based Metabolomics to Predict Early and Late Adverse Outcomes in Ischemic Stroke Treated with Intravenous Thrombolysis. J. Proteome Res. doi: 10.1021/acs.jproteome.2c00333
  178. Licciardi, G., et al. (2022). Not only manganese, but fruit component effects dictate the efficiency of fruit juice as an oral magnetic resonance imaging contrast agent. NMR Biomed. doi: 10.1002/nbm.4623
  179. Licciardi, G., et al. (2022). Large Protein Assemblies for High-Relaxivity Contrast Agents: The Case of Gadolinium-Labeled Asparaginase. Bioconjugate Chem. doi: 10.1021/acs.bioconjchem.2c00506
  180. Lionello, V. M., et al. (2022). BIN1 modulation in vivo rescues dynamin-related myopathy. Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.2109576119
  181. Liu, B. W., et al. (2022). Structural insights into ring-building motif domains involved in bacterial sporulation. J. Struct. Biol. doi: 10.1016/j.jsb.2021.107813
  182. Liu, C., et al. (2022). The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants. Cell Host Microbe. doi: 10.1016/j.chom.2021.11.013
  183. Liu, Y., et al. (2022). ICTV Virus Taxonomy Profile: Pleolipoviridae 2022. doi: https://doi.org/10.1099/jgv.0.001793
  184. Liu, Y. X., et al. (2022). Unexpected structures formed by the kinase RET C634R mutant extracellular domain suggest potential oncogenic mechanisms in MEN2A. J. Biol. Chem. doi: 10.1016/j.jbc.2022.102380
  185. Lopes, J., et al. (2022). Socialization of Providencia stuartii Enables Resistance to Environmental Insults. Microorganisms. doi: 10.3390/microorganisms10050901
  186. Luchinat, E., et al. (2022). In-cell NMR: From target structure and dynamics to drug screening. Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2022.102374
  187. Luchinat, E., et al. (2022). Radio Signals from Live Cells: The Coming of Age of In-Cell Solution NMR. Chem. Rev. doi: 10.1021/acs.chemrev.1c00790
  188. Maestre-Reyna, M., et al. (2022). Serial crystallography captures dynamic control of sequential electron and proton transfer events in a flavoenzyme. Nat. Chem. doi: 10.1038/s41557-022-00922-3
  189. Maloney, F. P., et al. (2022). Structure, substrate recognition and initiation of hyaluronan synthase. Nature. doi: 10.1038/s41586-022-04534-2
  190. Manigrasso, J., et al. (2022). Visualizing group II intron dynamics between the first and second steps of splicing (vol 11, 2837, 2020). Nat. Commun. doi: 10.1038/s41467-021-27699-2
  191. Marcia, M. (2022). The multiple molecular dimensions of long noncoding RNAs that regulate gene expression and tumorigenesis. Curr. Opin. Oncol. doi: 10.1097/cco.0000000000000813
  192. Marotta, R., et al. (2022). Unravelling the regulation pathway of photosynthetic AB-GAPDH. Acta Crystallogr. Sect. D-Struct. Biol. doi: 10.1107/s2059798322010014
  193. Marques, C., et al. (2022). Glycosyltransferases EXTL2 and EXTL3 cellular balance dictates heparan sulfate biosynthesis and shapes gastric cancer cell motility and invasion. J. Biol. Chem. doi: 10.1016/j.jbc.2022.102546
  194. Martin-Malpartida, P., et al. (2022). HTSDSF Explorer, A Novel Tool to Analyze High-throughput DSF Screenings. J. Mol. Biol. doi: 10.1016/j.jmb.2021.167372
  195. Maso, L., et al. (2022). Nanobodies targeting LexA autocleavage disclose a novel suppression strategy of SOS-response pathway. Structure. doi: 10.1016/j.str.2022.09.004
  196. Massai, L., et al. (2022). Gold-Based Metal Drugs as Inhibitors of Coronavirus Proteins: The Inhibition of SARS-CoV-2 Main Protease by Auranofin and Its Analogs. Biomolecules. doi: 10.3390/biom12111675
  197. Mattila, A. L. K., et al. (2022). Condition dependence in biosynthesized chemical defenses of an aposematic and mimetic Heliconius butterfly. Ecol. Evol. doi: 10.1002/ece3.9041
  198. Mavria, A., et al. (2022). Sustainable Production of Novel Oleogels Valorizing Microbial Oil Rich in Carotenoids Derived from Spent Coffee Grounds. J. Agric. Food Chem. doi: 10.1021/acs.jafc.2c03478
  199. Mejsnar, J. A., et al. (2022). Amino acid dipeptide formation induced by experimental irradiance of a solar flare power. Int. J. Astrobiol. doi: 10.1017/s1473550422000118
  200. Meoni, G., et al. (2022). Metabolite and lipoprotein profiles reveal sex-related oxidative stress imbalance in de novo drug-naive Parkinson's disease patients. npj Parkinsons Dis. doi: 10.1038/s41531-021-00274-8
  201. Michálek, O., et al. (2022). Composition and toxicity of venom produced by araneophagous white-tailed spiders (Lamponidae: Lampona sp.). Sci Rep. doi: 10.1038/s41598-022-24694-5
  202. Michalopoulou, V. A., et al. (2022). The host exocyst complex is targeted by a conserved bacterial type-III effector that promotes virulence. Plant Cell. doi: 10.1093/plcell/koac162
  203. Milder, F. J., et al. (2022). Universal stabilization of the influenza hemagglutinin by structure-based redesign of the pH switch regions. Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.2115379119
  204. Minadakis, M. P., et al. (2022). A glucose-based molecular rotor inhibitor of glycogen phosphorylase as a probe of cellular enzymatic function. Org. Biomol. Chem. doi: 10.1039/d1ob02211c
  205. Montaser, A. B., et al. (2022). Enhanced drug delivery by a prodrug approach effectively relieves neuroinflammation in mice. Life Sci. doi: 10.1016/j.lfs.2022.121088
  206. Mukherjee, S., et al. (2022). Silver Nanoparticle-Decorated Reduced Graphene Oxide Nanomaterials Exert Membrane Stress and Induce Immune Response to Inhibit the Early Phase of HIV-1 Infection. Adv. Mater. Interfaces. doi: 10.1002/admi.202201996
  207. Munari, F., et al. (2022). Structural Basis for Chaperone-Independent Ubiquitination of Tau Protein by Its E3 Ligase CHIP. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202112374
  208. Neofytos, D. D., et al. (2022). Formation and physicochemical properties of glycogen phosphorylase in complex with a cationic polyelectrolyte. Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2022.02.136
  209. Nguyen, H., et al. (2022). Characterization of a Radical SAM Oxygenase for the Ether Crosslinking in Darobactin Biosynthesis. J. Am. Chem. Soc. doi: 10.1021/jacs.2c05565
  210. Nguyen, T. Q., et al. (2022). Structure and Catalytic Mechanism of Radical SAM Methylases. Life-Basel. doi: 10.3390/life12111732
  211. Nicastro, G., et al. (2022). CP-MAS and Solution NMR Studies of Allosteric Communication in CA-assem- blies of HIV-1. J. Mol. Biol. doi: 10.1016/j.jmb.2022.167691
  212. Nikolopoulos, N., et al. (2022). DltC acts as an interaction hub for AcpS, DltA and DltB in the teichoic acid d-alanylation pathway of Lactiplantibacillus plantarum. Sci Rep. doi: 10.1038/s41598-022-17434-2
  213. Nizi, M. G., et al. (2022). Potent 2,3-dihydrophthalazine-1,4-dione derivatives as dual inhibitors for mono-ADP-ribosyltransferases PARP10 and PARP15. Eur. J. Med. Chem. doi: 10.1016/j.ejmech.2022.114362
  214. Njume, F. N., et al. (2022). A lipid transfer protein ensures nematode cuticular impermeability. iScience. doi: 10.1016/j.isci.2022.105357
  215. Noone, D. P., et al. (2022). PTX3 structure determination using a hybrid cryoelectron microscopy and AlphaFold approach offers insights into ligand binding and complement activation. Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.2208144119
  216. Nore, A., et al. (2022). TOPOVIBL-REC114 interaction regulates meiotic DNA double-strand breaks. Nat. Commun. doi: 10.1038/s41467-022-34799-0
  217. Nutalai, R., et al. (2022). Potent cross-reactive antibodies following Omicron breakthrough in vaccinees. Cell. doi: 10.1016/j.cell.2022.05.014
  218. Nys, M., et al. (2022). The molecular mechanism of snake short-chain alpha-neurotoxin binding to muscle-type nicotinic acetylcholine receptors. Nat. Commun. doi: 10.1038/s41467-022-32174-7
  219. Ojha, S., et al. (2022). Measurement of Liver Stiffness using Atomic Force Microscopy Coupled with Polarization Microscopy. J. Vis. Exp. doi: 10.3791/63974
  220. Oksanen, L., et al. (2022). Combining Phi6 as a surrogate virus and computational large-eddy simulations to study airborne transmission of SARS-CoV-2 in a restaurant. Indoor Air. doi: 10.1111/ina.13165
  221. Olga, K., et al. (2022). HR-Bac, a toolbox based on homologous recombination for expression, screening and production of multiprotein complexes using the baculovirus expression system. Sci Rep. doi: 10.1038/s41598-021-04715-5
  222. Osipov, E. M., et al. (2022). Discovery of novel druggable pockets on polyomavirus VP1 through crystallographic fragment-based screening to develop capsid assembly inhibitors. RSC Chem. Biol. doi: 10.1039/d2cb00052k
  223. Parigi, G., et al. (2022). Paramagnetic effects in NMR for protein structures and ensembles: Studies of metalloproteins. Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2022.102386
  224. Pavlovic, A., et al. (2022). Diethyl ether anesthesia induces transient cytosolic Ca2+ increase, heat shock proteins, and heat stress tolerance of photosystem II in Arabidopsis. Front. Plant Sci. doi: 10.3389/fpls.2022.995001
  225. Peng, X., et al. (2022). Self-Propelled Magnetic Dendrite-Shaped Microrobots for Photodynamic Prostate Cancer Therapy. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202213505
  226. Peng, X., et al. (2022). Shape-Controlled Self-Assembly of Light-Powered Microrobots into Ordered Microchains for Cells Transport and Water Remediation. ACS Nano. doi: 10.1021/acsnano.1c11136
  227. Perez, L. M., et al. (2022). Visualizing protein breathing motions associated with aromatic ring flipping. Nature. doi: 10.1038/s41586-022-04417-6
  228. Peter, M. F., et al. (2022). Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter. Nat. Commun. doi: 10.1038/s41467-022-31907-y
  229. Pichard, S., et al. (2022). Insect Cells-Baculovirus System for the Production of Difficult to Express Proteins: From Expression Screening for Soluble Constructs to Protein Quality Control. doi: 10.1007/978-1-0716-1859-2_17
  230. Pivato, R., et al. (2022). hESC derived cardiomyocyte biosensor to detect the different types of arrhythmogenic properties of drugs. Anal. Chim. Acta. doi: 10.1016/j.aca.2022.339959
  231. Plavec, Z., et al. (2022). SARS-CoV-2 Production, Purification Methods and UV Inactivation for Proteomics and Structural Studies. Viruses-Basel. doi: 10.3390/v14091989
  232. Pohl, C., et al. (2022). pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils. Nat. Commun. doi: 10.1038/s41467-022-30462-w
  233. Poirson, J., et al. (2022). High-Risk Mucosal Human Papillomavirus 16 (HPV16) E6 Protein and Cutaneous HPV5 and HPV8 E6 Proteins Employ Distinct Strategies To Interfere with Interferon Regulatory Factor 3-Mediated Beta Interferon Expression. J. Virol. doi: 10.1128/jvi.01875-21
  234. Pollastri, S., et al. (2022). Glycomimetic ligands block the interaction of SARS-CoV-2 spike protein with C-type lectin co-receptors. Chem. Commun. doi: 10.1039/d2cc00121g
  235. Polsinelli, I., et al. (2022). Erwinia tasmaniensis levansucrase shows enantiomer selection for (S)-1,2,4-butanetriol. Acta Crystallogr. F-Struct. Biol. Commun. doi: 10.1107/s2053230x2200680x
  236. Ponomareva, S., et al. (2022). Magnetic particles for triggering insulin release in INS-1E cells subjected to a rotating magnetic field. Nanoscale. doi: 10.1039/d2nr02009b
  237. Pontoriero, L., et al. (2022). NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering. Biomolecules. doi: 10.3390/biom12070929
  238. Pourali, P., et al. (2022). Investigation of Protein Corona Formed around Biologically Produced Gold Nanoparticles. Materials. doi: 10.3390/ma15134615
  239. Pulkkinen, L. I. A., et al. (2022). Molecular Organisation of Tick-Borne Encephalitis Virus. Viruses-Basel. doi: 10.3390/v14040792
  240. Rada, P., et al. (2022). Double-Stranded RNA Viruses Are Released From Trichomonas vaginalis Inside Small Extracellular Vesicles and Modulate the Exosomal Cargo. Front. Microbiol. doi: 10.3389/fmicb.2022.893692
  241. Ragonis-Bachar, P., et al. (2022). Natural Antimicrobial Peptides Self-assemble as alpha/beta Chameleon Amyloids. Biomacromolecules. doi: 10.1021/acs.biomac.2c00582
  242. Rando, C., et al. (2022). Highly Efficient and Selective Recognition of Dicyanoaurate(I) by a Bambusuril Macrocycle in Water. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202210184
  243. Ravera, E., et al. (2022). The evolution of paramagnetic NMR as a tool in structural biology. Phys. Chem. Chem. Phys. doi: 10.1039/d2cp01838a
  244. Renard, P., et al. (2022). Puy de Dome Station (France): A Stoichiometric Approach to Compound Classification in Clouds. J. Geophys. Res.-Atmos. doi: 10.1029/2022jd036635
  245. Rivaux, C., et al. (2022). Continuous Flow Aqueous Synthesis of Highly Luminescent AgInS2 and AgInS2/ZnS Quantum Dots. J. Phys. Chem. C. doi: 10.1021/acs.jpcc.2c06849
  246. Rizzo, D., et al. (2022). Epitope Mapping and Binding Assessment by Solid-State NMR Provide a Way for the Development of Biologics under the Quality by Design Paradigm. J. Am. Chem. Soc. doi: 10.1021/jacs.2c03232
  247. Rodrigues, M. J., et al. (2022). Trapping and structural characterisation of a covalent intermediate in vitamin B-6 biosynthesis catalysed by the Pdx1 PLP synthase. RSC Chem. Biol. doi: 10.1039/d1cb00160d
  248. Roy, A., et al. (2022). Discovery of compounds that inhibit SARS-CoV-2 Mac1-ADP-ribose binding by high-throughput screening. Antiviral Res. doi: 10.1016/j.antiviral.2022.105344
  249. Rudolfova, J., et al. (2022). Adamantane-Substituted Purine Nucleosides: Synthesis, Host-Guest Complexes with beta-Cyclodextrin and Biological Activity. Int. J. Mol. Sci. doi: 10.3390/ijms232315143
  250. Ruedas, R., et al. (2022). Three-Dimensional Envelope and Subunit Interactions of the Plastid-Encoded RNA Polymerase from Sinapis alba. Int. J. Mol. Sci. doi: 10.3390/ijms23179922
  251. Ruskamo, S., et al. (2022). Human myelin proteolipid protein structure and lipid bilayer stacking. Cell. Mol. Life Sci. doi: 10.1007/s00018-022-04428-6
  252. Sakari, M., et al. (2022). Exotoxin-Targeted Drug Modalities as Antibiotic Alternatives. ACS Infect. Dis. doi: 10.1021/acsinfecdis.1c00296
  253. Sakari, M., et al. (2022). Crystal structures of pertussis toxin with NAD(+) and analogs provide structural insights into the mechanism of its cytosolic ADP-ribosylation activity. J. Biol. Chem. doi: 10.1016/j.jbc.2022.101892
  254. Salom, D., et al. (2022). Stabilization of Meta-I Rhodopsin Conformation by a Nanobody. Faseb J. doi: 10.1096/fasebj.2022.36.S1.R2572
  255. Salvi, N., et al. (2022). Convergent views on disordered protein dynamics from NMR and computational approaches. Biophys. J. doi: 10.1016/j.bpj.2022.09.016
  256. Santana, F. S., et al. (2022). A dysprosium single molecule magnet outperforming current pseudocontact shift agents. Chem. Sci. doi: 10.1039/d2sc01619b
  257. Santos, T., et al. (2022). Stabilization of a DNA aptamer by ligand binding. Biochimie. doi: 10.1016/j.biochi.2022.05.002
  258. Santos, T., et al. (2022). Pre-miRNA-149 G-quadruplex as a molecular agent to capture nucleolin. Eur. J. Pharm. Sci. doi: 10.1016/j.ejps.2021.106093
  259. Santos, T., et al. (2022). Targeting a G-quadruplex from let-7e pre-miRNA with small molecules and nucleolin. J. Pharm. Biomed. Anal. doi: 10.1016/j.jpba.2022.114757
  260. Saudino, G., et al. (2022). Protein-Interaction Affinity Gradient Drives 4Fe-4S ClusterInsertion in Human Lipoyl Synthase. J. Am. Chem. Soc. doi: 10.1021/jacs.1c13626
  261. Schaack, B., et al. (2022). Microbiota-Derived Extracellular Vesicles Detected in Human Blood from Healthy Donors. Int. J. Mol. Sci. doi: 10.3390/ijms232213787
  262. Schiavina, M., et al. (2022). The Role of Disordered Regions in Orchestrating the Properties of Multidomain Proteins: The SARS-CoV-2 Nucleocapsid Protein and Its Interaction with Enoxaparin. Biomolecules. doi: 10.3390/biom12091302
  263. Schiffrin, B., et al. (2022). Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding. Commun. Biol. doi: 10.1038/s42003-022-03502-w
  264. Schonn, M. A., et al. (2022). Inline-tandem purification of viruses from cell lysate by agarose-based chromatography. J. Chromatogr. B. doi: 10.1016/j.jchromb.2022.123140
  265. Seck, A., et al. (2022). In vitro reconstitution of an efficient nucleotide excision repair system using mesophilic enzymes from Deinococcus radiodurans. Commun. Biol. doi: 10.1038/s42003-022-03064-x
  266. Sedlacek, I., et al. (2022). Characterisation of Waterborne Psychrophilic Massilia Isolates with Violacein Production and Description of Massilia antarctica sp. nov. Microorganisms. doi: 10.3390/microorganisms10040704
  267. Seoane, S., et al. (2022). Design, Synthesis, Biological Activity, and Structural Analysis of Novel Des-C-Ring and Aromatic-D-Ring Analogues of 1 alpha,25. J. Med. Chem. doi: 10.1021/acs.jmedchem.2c00900
  268. Sherrill, L. M., et al. (2022). Design, synthesis and evaluation of inhibitors of the SARS-CoV-2 nsp3 macrodomain. Bioorg. Med. Chem. doi: 10.1016/j.bmc.2022.116788
  269. Shukla, R., et al. (2022). Teixobactin kills bacteria by a two-pronged attack on the cell envelope. Nature. doi: 10.1038/s41586-022-05019-y
  270. Shukla, S., et al. (2022). In-solution structure and oligomerization of human histone deacetylase 6-an integrative approach. Febs J. doi: 10.1111/febs.16616
  271. Siborova, M., et al. (2022). Tail proteins of phage SU10 reorganize into the nozzle for genome delivery. Nat. Commun. doi: 10.1038/s41467-022-33305-w
  272. Sigueiro, R., et al. (2022). Advances in Vitamin D Receptor Function and Evolution Based on the 3D Structure of the Lamprey Ligand-Binding Domain br. J. Med. Chem. doi: 10.1021/acs.jmedchem.2c00171
  273. Silva, J. M., et al. (2022). H-1, C-13 and N-15 assignment of the human mitochondrial paramagnetic iron-sulfur protein CISD3. Biomol. NMR Assign. doi: 10.1007/s12104-022-10113-3
  274. Simonci, M., et al. (2022). Biomolecular Complexation on the "Wrong Side": A Case Study of the Influence of Salts and Sugars on the Interactions between Bovine Serum Albumin and Sodium Polystyrene Sulfonate. Biomacromolecules. doi: 10.1021/acs.biomac.2c00933
  275. Singh, R. K., et al. (2022). Nanobodies as allosteric modulators of Parkinson's disease-associated LRRK2. Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.2112712119
  276. Šišoláková, I., et al. (2022). Colloidal lithography as a novel approach for the development of Ni-nanocavity insulin sensor. Sci Rep. doi: 10.1038/s41598-022-15283-7
  277. Skoda, D., et al. (2022). Vanadium metal-organic frameworks derived VOx/Carbon nano-sheets and paperclip-like VOx/nitrogen-doped carbon nanocomposites for sodium-ion battery electrodes. Mater. Chem. Phys. doi: 10.1016/j.matchemphys.2021.125584
  278. Sokolov, J., et al. (2022). Synthesis of Glycoluril Dimers with the Ability to Form Polymeric Self-Associates in Water. Chemistry-Switz. doi: 10.3390/chemistry4030053
  279. Sorzano, C. O. S., et al. (2022). Cryo-Electron Microscopy: The field of 1,000(+) methods. J. Struct. Biol. doi: 10.1016/j.jsb.2022.107861
  280. Sorzano, C. O. S., et al. (2022). On bias, variance, overfitting, gold standard and consensus in single-particle analysis by cryo-electron microscopy. doi: 10.1107/s2059798322001978
  281. Sorzano, C. O. S., et al. (2022). Image processing tools for the validation of CryoEM maps. Faraday Discuss. doi: 10.1039/d2fd00059h
  282. Sourrouille, Z. A., et al. (2022). The Viral Susceptibility of the Haloferax Species. Viruses-Basel. doi: 10.3390/v14061344
  283. Sowa, S. T., et al. (2022). An Evolutionary Perspective on the Origin, Conservation and Binding Partner Acquisition of Tankyrases. Biomolecules. doi: 10.3390/biom12111688
  284. Sowa, S. T., et al. (2022). Preparation of screening assays for ADP-ribosyl readers and erasers using the GAP-tag as a binding probe. STAR Protocols. doi: 10.1016/j.xpro.2022.101147
  285. Sowa, S. T., et al. (2022). The zinc-binding motif in tankyrases is required for the structural integrity of the catalytic ADP-ribosyltransferase domain. Open Biol. doi: 10.1098/rsob.210365
  286. Stiborek, M., et al. (2022). Infrared Laser Desorption of Intact Nanoparticles for Digital Tissue Imaging. Anal. Chem. doi: 10.1021/acs.analchem.2c05216
  287. Stroch, M., et al. (2022). Spruce versus Arabidopsis: different strategies of photosynthetic acclimation to light intensity change. Photosynth. Res. doi: 10.1007/s11120-022-00949-0
  288. Sulbaran, G., et al. (2022). Immunization with synthetic SARS-CoV-2 S glycoprotein virus-like particles protects macaques from infection. Cell Rep. Med. doi: 10.1016/j.xcrm.2022.100528
  289. Suys, O., et al. (2022). ATR-FTIR Biosensors for Antibody Detection and Analysis. Int. J. Mol. Sci. doi: 10.3390/ijms231911895
  290. Svec, P., et al. (2022). Pedobacter fastidiosus sp. nov., isolated from glacial habitats of maritime Antarctica. Int. J. Syst. Evol. Microbiol. doi: 10.1099/ijsem.0.005309
  291. Svestka, D., et al. (2022). Asymmetric Organocatalyzed Friedel-Crafts Reaction of Trihaloacetaldehydes and Phenols. Adv. Synth. Catal. doi: 10.1002/adsc.202200180
  292. Tarbouriech, N., et al. (2022). Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing. Viruses-Basel. doi: 10.3390/v14112358
  293. Tetreau, G., et al. (2022). De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals. Nat. Commun. doi: 10.1038/s41467-022-31746-x
  294. Tharra, P. R., et al. (2022). Short Synthesis of (+)-Actinobolin: Simple Entry to Complex Small-Molecule Inhibitors of Protein Synthesis. Angew. Chem.-Int. Edit. doi: 10.1002/anie.202116520
  295. Torner, R., et al. (2022). Structural basis for the inhibition of IAPP fibril formation by the co-chaperonin prefoldin. Nat. Commun. doi: 10.1038/s41467-022-30042-y
  296. Torres, A., et al. (2022). Repeated Exposure of Macrophages to Synthetic Amorphous Silica Induces Adaptive Proteome Changes and a Moderate Cell Activation. Nanomaterials. doi: 10.3390/nano12091424
  297. Torricella, F., et al. (2022). Protein delivery to living cells by thermal stimulation for biophysical investigation. Sci Rep. doi: 10.1038/s41598-022-21103-9
  298. Tran, N. T., et al. (2022). Human and Insect Cell-Produced Recombinant Adeno-Associated Viruses Show Differences in Genome Heterogeneity. Hum. Gene Ther. doi: 10.1089/hum.2022.050
  299. Tricomi, J., et al. (2022). Ball milled glyco-graphene oxide conjugates markedly disrupted Pseudomonas aeruginosa biofilms. Nanoscale. doi: 10.1039/d2nr02027k
  300. Trindade, I. B., et al. (2022). NMR of paramagnetic metalloproteins in solution: Ubi venire, quo vadis? J. Inorg. Biochem. doi: 10.1016/j.jinorgbio.2022.111871
  301. Tuekprakhon, A., et al. (2022). Antibody escape of SARS-CoV-2 Omicron BA.4 and BA.5 from vaccine and BA.1 serum. Cell. doi: 10.1016/j.cell.2022.06.005
  302. Urzhumtsev, A., et al. (2022). Analytic modeling of inhomogeneous-resolution maps in cryo-electron microscopy and crystallography. IUCrJ. doi: 10.1107/s2052252522008260
  303. Urzhumtsev, A. G., et al. (2022). Toward Real Real-Space Refinement of Atomic Models. Int. J. Mol. Sci. doi: 10.3390/ijms232012101
  304. Urzhumtsev, A. G., et al. (2022). Direct calculation of cryo-EM and crystallographic model maps for real-space refinement. Acta Crystallogr. Sect. D-Struct. Biol. doi: 10.1107/s2059798322010907
  305. van der Linden, P., et al. (2022). A miniature airlock system to aid the cryo-cooling of protein crystals grown under anoxic conditions. J. Appl. Crystallogr. doi: 10.1107/s1600576722007580
  306. van der Verren, M., et al. (2022). Airborne Preparation of Small Gold Nanoparticles Dispersed on Mesoporous Silica for the Catalytic Oxidation of Glycerol to Dihydroxyacetone. ACS Appl. Nano Mater. doi: 10.1021/acsanm.2c04786
  307. Van Driessche, A. E. S., et al. (2022). Nucleation of glucose isomerase protein crystals in a nonclassical disguise: The role of crystalline precursors. Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.2108674119
  308. Vavrova, A., et al. (2022). One-step synthesis of gold nanoparticles for catalysis and SERS applications using selectively dicarboxylated cellulose and hyaluronate. Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2022.03.043
  309. Vesela, H., et al. (2022). The Pork Meat or the Environment of the Production Facility? The Effect of Individual Technological Steps on the Bacterial Contamination in Cooked Hams. Microorganisms. doi: 10.3390/microorganisms10061106
  310. Vicar, T., et al. (2022). Cancer cell viscoelasticity measurement by quantitative phase and flow stress induction. Biophys. J. doi: 10.1016/j.bpj.2022.04.002
  311. Vignoli, A., et al. (2022). Metabolomics Fingerprint Predicts Risk of Death in Dilated Cardiomyopathy and Heart Failure. Front. Cardiovasc. Med. doi: 10.3389/fcvm.2022.851905
  312. Vignoli, A., et al. (2022). Serum or Plasma (and Which Plasma), That Is the Question br. J. Proteome Res. doi: 10.1021/acs.jproteome.1c00935
  313. Viola, G., et al. (2022). New Paradigm for Nano-Bio Interactions: Multimolecular Assembly of a Prototypical Disordered Protein with Ultrasmall Nanoparticles. Nano Lett. doi: 10.1021/acs.nanolett.2c02902
  314. Vrchovecka, K., et al. (2022). A release of Ti-ions from nanostructured titanium oxide surfaces. Surf. Interfaces. doi: 10.1016/j.surfin.2021.101699
  315. Walker, P. J., et al. (2022). Recent changes to virus taxonomy ratified by the International Committee on Taxonomy of Viruses (2022). Arch. Virol. doi: 10.1007/s00705-022-05516-5
  316. Weerakkody, J. S., et al. (2022). Surfactant-like Peptide Self-Assembled into Hybrid Nanostructures for Electronic Nose Applications. ACS Nano. doi: 10.1021/acsnano.1c10734
  317. Weinhaupl, K., et al. (2022). Structure of the drug target ClpC1 unfoldase in action provides insights on antibiotic mechanism of action. J. Biol. Chem. doi: 10.1016/j.jbc.2022.102553
  318. Wilson, A., et al. (2022). Structure-function-dynamics relationships in the peculiar Planktothrix PCC7805 OCP1: Impact of his-tagging and carotenoid type. Biochim. Biophys. Acta-Bioenerg. doi: 10.1016/j.bbabio.2022.148584
  319. Wul, J., et al. (2022). mEos4b Photoconversion Efficiency Depends on Laser Illumination Conditions Used in PALM. J. Phys. Chem. Lett. doi: 10.1021/acs.jpclett.2c00933
  320. Xie, Y. F., et al. (2022). Two Types of Liposomal Formulations Improve the Therapeutic Ratio of Prednisolone Phosphate in a Zebrafish Model for Inflammation. Cells. doi: 10.3390/cells11040671
  321. Yrjanainen, A., et al. (2022). Biochemical and Biophysical Characterization of Carbonic Anhydrase VI from Human Milk and Saliva. Protein J. doi: 10.1007/s10930-022-10070-9
  322. Yu, X. L., et al. (2022). Cryo-EM structures of perforin-2 in isolation and assembled on a membrane suggest a mechanism for pore formation. Embo J. doi: 10.15252/embj.2022111857
  323. Zambo, B., et al. (2022). Native holdup (nHU) to measure binding affinities from cell extracts. Sci. Adv. doi: 10.1126/sciadv.ade3828
  324. Zarkadas, E., et al. (2022). Conformational transitions and ligand-binding to a muscle-type nicotinic acetylcholine receptor. Neuron. doi: 10.1016/j.neuron.2022.01.013
  325. Zavarise, A., et al. (2022). Structures of lactaldehyde reductase, FucO, link enzyme activity to hydrogen bond networks and conformational dynamics. Febs J. doi: 10.1111/febs.16603
  326. Zerbini, F. M., et al. (2022). Differentiating between viruses and virus species by writing their names correctly. Arch. Virol. doi: 10.1007/s00705-021-05323-4
  327. Zhang, Y. R., et al. (2022). A Direct Assay for Measuring the Activity and Inhibition of Coactivator-Associated Arginine Methyltransferase 1. Biochemistry. doi: 10.1021/acs.biochem.2c00075
  328. Zhu, C. J., et al. (2022). Transcription factors modulate RNA polymerase conformational equilibrium. Nat. Commun. doi: 10.1038/s41467-022-29148-0
  329. Zrimsek, M., et al. (2022). Quantitative Acetylomics Uncover Acetylation-Mediated Pathway Changes Following Histone Deacetylase Inhibition in Anaplastic Large Cell Lymphoma. Cells. doi: 10.3390/cells11152380

2021

  1. Abrishami, V., et al. (2021). Localized reconstruction in Scipion expedites the analysis of symmetry mismatches in cryo-EM data. Prog. Biophys. Mol. Biol. 160:43-52. doi: 10.1016/j.pbiomolbio.2020.05.004
  2. Adiram-Filiba, N., et al. (2021). Structure and Dynamics Perturbations in Ubiquitin Adsorbed or Entrapped in Silica Materials Are Related to Disparate Surface Chemistries Resolved by Solid-State NMR Spectroscopy. Biomacromolecules. 22(9):3718-3730. doi: 10.1021/acs.biomac.1c00495
  3. Ahmad, M. U. D., et al. (2021). Nano-Differential Scanning Fluorimetry for Screening in Fragment-based Lead Discovery. J. Vis. Exp. (171):18. doi: 10.3791/62469
  4. Alam, J., et al. (2021). Expression and analysis of the SAM-dependent RNA methyltransferase Rsm22 from Saccharomyces cerevisiae. Acta Crystallogr. Sect. D-Struct. Biol. 77(Pt 6):840-853. doi: 10.1107/s2059798321004149
  5. Alqabandi, M., et al. (2021). The ESCRT-III isoforms CHMP2A and CHMP2B display different effects on membranes upon polymerization. BMC Biol. 19(1):18. doi: 10.1186/s12915-021-00983-9
  6. Altincekic, N., et al. (2021). Large-Scale Recombinant Production of the SARS-CoV-2 Proteome for High-Throughput and Structural Biology Applications. Front. Mol. Biosci. 8:25. doi: 10.3389/fmolb.2021.653148
  7. Alves, I., et al. (2021). Protein Mannosylation as a Diagnostic and Prognostic Biomarker of Lupus Nephritis: An Unusual Glycan Neoepitope in Systemic Lupus Erythematosus. Arthritis Rheumatol.:9. doi: 10.1002/art.41768
  8. Andronov, L., et al. (2021). Practical Aspects of Super-Resolution Imaging and Segmentation of Macromolecular Complexes by dSTORM. In: Poterszman, A., ed. Multiprotein Complexes. New York, NY: SpringerLink 2021. doi: 10.1007/978-1-0716-1126-5_15
  9. Aryafard, M., et al. (2021). Novel room temperature ionic liquids and low melting mixtures based on imidazolium: Cheap ionic solvents for chemical and biological applications. J. Mol. Liq. 344:7. doi: 10.1016/j.molliq.2021.117877
  10. Axmann, M., et al. (2021). Plasma Membrane Lipids: An Important Binding Site for All Lipoprotein Classes. Membranes. 11(11):11. doi: 10.3390/membranes11110882
  11. Baddam, V., et al. (2021). Thermoresponsive Polycation-Stabilized Nanoparticles through PISA. Control of Particle Morphology with a Salt. Macromolecules. 54(9):4288-4299. doi: 10.1021/acs.macromol.0c02771
  12. Baeta, T., et al. (2021). The lipopolysaccharide-transporter complex LptB(2)FG also displays adenylate kinase activity in vitro dependent on the binding partners LptC/LptA. J. Biol. Chem. 297(6):8. doi: 10.1016/j.jbc.2021.101313
  13. Balder, Y., et al. (2021). Exploration of Blood Lipoprotein and Lipid Fraction Profiles in Healthy Subjects through Integrated Univariate, Multivariate, and Network Analysis Reveals Association of Lipase Activity and Cholesterol Esterification with Sex and Age. 11(5). doi: 10.3390/metabo11050326
  14. Bally, I., et al. (2021). Functional recombinant human complement C1q with different affinity tags. J. Immunol. Methods. 492:8. doi: 10.1016/j.jim.2021.113001
  15. Banchelli, M., et al. (2021). Probing the Structure of Toxic Amyloid-beta Oligomers with Electron Spin Resonance and Molecular Modeling. ACS Chem. Neurosci. 12(7):1150-1161. doi: 10.1021/acschemneuro.0c00714
  16. Barbieri, L., et al. (2021). Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor. J. Vis. Exp. (169):17. doi: 10.3791/62323
  17. Basbous, H., et al. (2021). Transient Formation of a Second Active Site Cavity during Quinolinic Acid Synthesis by NadA. ACS Chem. Biol.16(11):2423-2433. doi: 10.1021/acschembio.1c00541
  18. Bauer, V., et al. (2021). Conformational editing of intrinsically disordered protein by alpha-methylation. Chem. Sci. 12(3):1080-1089. doi: 10.1039/d0sc04482b
  19. Beinsteiner, B., et al. (2021). A structural signature motif enlightens the origin and diversification of nuclear receptors. PLoS Genet. 17(4):32. doi: 10.1371/journal.pgen.1009492
  20. Benova-Liszekova, D., et al. (2021). An apocrine mechanism delivers a fully immunocompetent exocrine secretion. Sci Rep. 11(1):12. doi: 10.1038/s41598-021-95309-8
  21. Bersch, B., et al. (2021). Solution Structure of the C-terminal Domain of A20, the Missing Brick for the Characterization of the Interface between Vaccinia Virus DNA Polymerase and its Processivity Factor. J. Mol. Biol. 433(13):14. doi: 10.1016/j.jmb.2021.167009
  22. Bertling, E., et al. (2021). Carbonic anhydrase seven bundles filamentous actin and regulates dendritic spine morphology and density. EMBO Rep. 22(4):17. doi: 10.15252/embr.202050145
  23. Blanquart, S., et al. (2021). Resurrection of Ancestral Malate Dehydrogenases Reveals the Evolutionary History of Halobacterial Proteins: Deciphering Gene Trajectories and Changes in Biochemical Properties. Mol. Biol. Evol. 38(9):3754-3774. doi: 10.1093/molbev/msab146
  24. Blum, T. B., et al. (2021). Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals. Acta Cryst.  D. 77(1):75-85. doi: 10.1107/S2059798320014540
  25. Bocharov, E. V., et al. (2021). All-D-Enantiomeric Peptide D3 Designed for Alzheimer's Disease Treatment Dynamically Interacts with Membrane-Bound Amyloid-beta Precursors. J. Med. Chem. 64(22):16464-16479. doi: 10.1021/acs.jmedchem.1c00632
  26. Bonaccorsi di Patti, M. C., et al. (2021). Production of Recombinant Human Ceruloplasmin: Improvements and Perspectives. Int. J. Mol. Sci.22(15):10. doi: 10.3390/ijms22158228
  27. Bonucci, A., et al. (2021). Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR1. Front. Mol. Biosci. 8:14. doi: 10.3389/fmolb.2021.684622
  28. Bora, P., et al. (2021). DDX21 is a p38-MAPK-sensitive nucleolar protein necessary for mouse preimplantation embryo development and cell-fate specification. Open Biol. 11(7):15. doi: 10.1098/rsob.210092
  29. Bora, P., et al. (2021). p38-MAPK-mediated translation regulation during early blastocyst development is required for primitive endoderm differentiation in mice. Commun. Biol. 4(1):19. doi: 10.1038/s42003-021-02290-z
  30. Bou-Nader, C., et al. (2021). An enzymatic activation of formaldehyde for nucleotide methylation. Nat. Commun. 12(1):8. doi: 10.1038/s41467-021-24756-8
  31. Browning, C., et al. (2021). Nonsteroidal ecdysone receptor agonists use a water channel for binding to the ecdysone receptor complex EcR/USP. J. Pestic. Sci. 46(1-2):88-100. doi: 10.1584/jpestics.D20-095
  32. Caillat, C., et al. (2021). Structure of HIV-1 gp41 with its membrane anchors targeted by neutralizing antibodies. eLife. 10:26. doi: 10.7554/eLife.65005
  33. Caliandro, R., et al. (2021). The structural and functional characterization of Malus domestica double bond reductase MdDBR provides insights towards the identification of its substrates. Int. J. Biol. Macromol. 171:89-99. doi: 10.1016/j.ijbiomac.2020.12.190
  34. Calisto, B. M., et al. (2021). Sulfotyrosine-Mediated Recognition of Human Thrombin by a Tsetse Fly Anticoagulant Mimics Physiological Substrates. Cell Chem. Biol. 28(1):26-+. doi: 10.1016/j.chembiol.2020.10.002
  35. Camponeschi, F., et al. (2021). The long-standing relationship between paramagnetic NMR and iron–sulfur proteins: the mitoNEET example. An old method for new stories or the other way around? Magn. Reson. 2(1):203-221. doi: 10.5194/mr-2-203-2021
  36. Castro, C., et al. (2021). A practical guide to teaching with Proteopedia. Biochem. Mol. Biol. Educ. 49(5):707-719. doi: 10.1002/bmb.21548
  37. Caulier, B., et al. (2021). Evaluation of the human type 3 adenoviral dodecahedron as a vector to target acute myeloid leukemia. Mol. Ther.-Methods Clin. Dev. 20:181-190. doi: 10.1016/j.omtm.2020.11.009
  38. Chaud, J., et al. (2021). Two-Photon Sensitive Coumarinyl Photoremovable Protecting Groups with Rigid Electron-Rich Cycles Obtained by Domino Reactions Initiated by a 5-exo-Dig Cyclocarbopalladation. Org. Lett. 23(19):7580-7585. doi: 10.1021/acs.orglett.1c02778
  39. Chikunova, A., et al. (2021). Conserved residues Glu37 and Trp229 play an essential role in protein folding of beta-lactamase. Febs J.:15. doi: 10.1111/febs.15854
  40. Christou, N. E., et al. (2021). Disentangling Chromophore States in a Reversibly Switchable Green Fluorescent Protein: Mechanistic Insights from NMR Spectroscopy. J. Am. Chem. Soc. 143(19):7521-7530. doi: 10.1021/jacs.1c02442
  41. Ciambellotti, S., et al. (2021). Iron Binding in the Ferroxidase Site of Human Mitochondrial Ferritin. Chem.-Eur. J. 27(59):14690-14701. doi: 10.1002/chem.202102270
  42. Conrady, M. C., et al. (2021). Structure of High-Risk Papillomavirus 31 E6 Oncogenic Protein and Characterization of E6/E6AP/p53 Complex Formation. J. Virol. 95(2):15. doi: 10.1128/jvi.00730-20
  43. Coupland, C. E., et al. (2021). Structure, mechanism, and inhibition of Hedgehog acyltransferase. Mol. Cell. 81(24):5025-+. doi: 10.1016/j.molcel.2021.11.018
  44. Covelo-Molares, H., et al. (2021). The comprehensive interactomes of human adenosine RNA methyltransferases and demethylases reveal distinct functional and regulatory features. Nucleic Acids Res. 49(19):10895-10910. doi: 10.1093/nar/gkab900
  45. Cristofalo, A. E., et al. (2021). Synthesis, self-assembly and Langerin recognition studies of a resorcinarene-based glycocluster exposing a hyaluronic acid thiodisaccharide mimetic. Org. Biomol. Chem. 19(29):13. doi: 10.1039/d1ob00895a
  46. Cura, V., et al. (2021). Structure, Activity and Function of the PRMT2 Protein Arginine Methyltransferase. Life-Basel. 11(11):13. doi: 10.3390/life11111263
  47. Cussol, L., et al. (2021). Structural Basis for alpha-Helix Mimicry and Inhibition of Protein-Protein Interactions with Oligourea Foldamers. Angew. Chem.-Int. Edit. 60(5):2296-2303. doi: 10.1002/anie.202008992
  48. Dalwani, S., et al. (2021). Substrate specificity and conformational flexibility properties of the Mycobacterium tuberculosis beta-oxidation trifunctional enzyme. J. Struct. Biol. 213(3):14. doi: 10.1016/j.jsb.2021.107776
  49. Dalzon, B., et al. (2021). A Low-Serum Culture System for Prolonged in Vitro Toxicology Experiments on a Macrophage System. Front. Toxicology. 3. doi: 10.3389/ftox.2021.780778
  50. Daniel, E., et al. (2021). IceBear: an intuitive and versatile web application for research-data tracking from crystallization experiment to PDB deposition. Acta Crystallogr. Sect. D-Struct. Biol. 77:151-163. doi: 10.1107/s2059798320015223
  51. de Carvalho, D. M., et al. (2021). Active role of lignin in anchoring wood-based stabilizers to the emulsion interface. Green Chem. 23(22):15. doi: 10.1039/d1gc02891j
  52. de la Mora, E., et al. (2021). Nanoscale architecture of a VAP-A-OSBP tethering complex at membrane contact sites. Nat. Commun. 12(1):14. doi: 10.1038/s41467-021-23799-1
  53. De Meutter, J., et al. (2021). Protein Structural Denaturation Evaluated by MCR-ALS of Protein Microarray FTIR Spectra. Anal. Chem.93(40):13441-13449. doi: 10.1021/acs.analchem.1c01416
  54. de Muizon, C. J., et al. (2021). Self-organization Properties of a GPCR-Binding Peptide with a Fluorinated Tail Studied by Fluorine NMR Spectroscopy. ChemBioChem. 22(4):657-661. doi: 10.1002/cbic.202000601
  55. de Wijn, R., et al. (2021). CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacterium Planococcus halocryophilus. Comp. Struct. Biotechnol. J.. 19:5845-5855. doi: 10.1016/j.csbj.2021.10.018
  56. Decelle, J., et al. (2021). Subcellular architecture and metabolic connection in the planktonic photosymbiosis between Collodaria (radiolarians) and their microalgae. Environ. Microbiol.:18. doi: 10.1111/1462-2920.15766
  57. Dejnirattisai, W., et al. (2021). The antigenic anatomy of SARS-CoV-2 receptor binding domain. Cell. 184(8):2183-+. doi: 10.1016/j.cell.2021.02.032
  58. Dejnirattisai, W., et al. (2021). Antibody evasion by the P.1 strain of SARS-CoV-2. Cell. 184(11):2939-+. doi: 10.1016/j.cell.2021.03.055
  59. Del Amo-Maestro, L., et al. (2021). An Integrative Structural Biology Analysis of Von Willebrand Factor Binding and Processing by ADAMTS-13 in Solution. J. Mol. Biol. 433(13):18. doi: 10.1016/j.jmb.2021.166954
  60. Del Campo, J., et al. (2021). OVX836 Heptameric Nucleoprotein Vaccine Generates Lung Tissue-Resident Memory CD8+T-Cells for Cross-Protection Against Influenza. Front. Immunol. 12:13. doi: 10.3389/fimmu.2021.678483
  61. Di Cesare, F., et al. (2021). Lipid and metabolite correlation networks specific to clinical and biochemical covariate show differences associated with sexual dimorphism in a cohort of nonagenarians. GeroScience.20. doi: 10.1007/s11357-021-00404-3
  62. Di Donato, S., et al. (2021). A Serum Metabolomics Classifier Derived from Elderly Patients with Metastatic Colorectal Cancer Predicts Relapse in the Adjuvant Setting. Cancers. 13(11):18. doi: 10.3390/cancers13112762
  63. Di Maio, A., et al. (2021). Controlled density glycodendron microarrays for studying carbohydrate-lectin interactions. Org. Biomol. Chem.:6. doi: 10.1039/d1ob00872b
  64. Dickson-Murray, E., et al. (2021). The Mia40/CHCHD4 Oxidative Folding System: Redox Regulation and Signaling in the Mitochondrial Intermembrane Space. Antioxidants. 10(4):19. doi: 10.3390/antiox10040592
  65. Dimogkioka, A. R., et al. (2021). Protein import in mitochondria biogenesis: guided by targeting signals and sustained by dedicated chaperones. RSC Adv. 11(51):32476-32493. doi: 10.1039/d1ra04497d
  66. Dohnalek, J., et al. (2021). Chitinase Chit62J4 Essential for Chitin Processing by Human Microbiome Bacterium Clostridium paraputrificum J4. Molecules. 26(19):16. doi: 10.3390/molecules26195978
  67. Domanska, A., et al. (2021). A comparative analysis of parechovirus protein structures with other picornaviruses. Open Biol. 11(7):14. doi: 10.1098/rsob.210008
  68. Duraffourg, N., et al. (2021). Hybrid Amyloid-Based Redox Hydrogel for Bioelectrocatalytic H-2 Oxidation. Angew. Chem.-Int. Edit.:11. doi: 10.1002/anie.202101700
  69. Dussert, F., et al. (2021). Evaluation of the Dermal Toxicity of InZnP Quantum Dots Before and After Accelerated Weathering: Toward a Safer-By-Design Strategy. Front. Toxicol. 3. doi: 10.3389/ftox.2021.636976
  70. Duyvesteyn, H. M. E., et al. (2021). Bacteriophage PRD1 as a nanoscaffold for drug loading. Nanoscale.9. doi: 10.1039/d1nr04153c
  71. Eaglesfield, R., et al. (2021). Targeting and Insertion of Membrane Proteins in Mitochondria. Front. Cell. Dev. Biol. 9:15. doi: 10.3389/fcell.2021.803205
  72. Ebel, C., et al. (2021). Sedimentation Velocity Methods for the Characterization of Protein Heterogeneity and Protein Affinity Interactions. In: Poterszman, A., ed. Multiprotein Complexes. New York, NY: SpringerLink 2021. doi: 10.1007/978-1-0716-1126-5_9
  73. Edwards, R., et al. (2021). The mitochondrial intermembrane space: the most constricted mitochondrial sub-compartment with the largest variety of protein import pathways. Open Biol. 11(3):13. doi: 10.1098/rsob.210002
  74. Effantin, G., et al. (2021). High Resolution Structure of the Mature Capsid of Ralstonia solanacearum Bacteriophage fRSA1 by Cryo-Electron Microscopy. Int. J. Mol. Sci. 22(20):11. doi: 10.3390/ijms222011053
  75. England, P., et al. (2021). Community-building and promotion of technological excellence in molecular biophysics: the ARBRE-MOBIEU network. Eur. Biophys. J. Biophys. Lett. 50(3-4):307-311. doi: 10.1007/s00249-021-01550-4
  76. Eskelin, K., et al. (2021). Sample carryover and cleaning procedures for asymmetrical flow field-flow fractionation instrument. J. Chromatogr. B. 1181:9. doi: 10.1016/j.jchromb.2021.122920
  77. Farhat, D. C., et al. (2021). A plant-like mechanism coupling m6A reading to polyadenylation safeguards transcriptome integrity and developmental gene partitioning in Toxoplasma. eLife. 10:37. doi: 10.7554/eLife.68312
  78. Favier, A., et al. (2021). The Plastid-Encoded RNA Polymerase-Associated Protein PAP9 Is a Superoxide Dismutase With Unusual Structural Features. Front. Plant Sci. 12:15. doi: 10.3389/fpls.2021.668897
  79. Felix, J., et al. (2021). Structural and functional analysis of the Francisella lysine decarboxylase as a key actor in oxidative stress resistance. Sci. Rep. 11(1):19. doi: 10.1038/s41598-020-79611-5
  80. Felli, I. C., et al. (2021). Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues. Magn. Reson. 2(1):511-522. doi: 10.5194/mr-2-511-2021
  81. Ferrero, D. S., et al. (2021). Snapshots of a Non-Canonical RdRP in Action. Viruses-Basel. 13(7):16. doi: 10.3390/v13071260
  82. Figueiredo, P., et al. (2021). Green Fabrication Approaches of Lignin Nanoparticles from Different Technical Lignins: A Comparison Study. ChemSusChem.14. doi: 10.1002/cssc.202101356
  83. Fisarova, L., et al. (2021). Staphylococcus epidermidis Phages Transduce Antimicrobial Resistance Plasmids and Mobilize Chromosomal Islands. mSphere. 6(3):19. doi: 10.1128/mSphere.00223-21
  84. Flatt, J. W., et al. (2021). Identification of a conserved virion-stabilizing network inside the interprotomer pocket of enteroviruses. Commun. Biol.4(1):8. doi: 10.1038/s42003-021-01779-x
  85. Fojtik, L., et al. (2021). Fast Fluoroalkylation of Proteins Uncovers the Structure and Dynamics of Biological Macromolecules. J. Am. Chem. Soc.143(49):20670-20679. doi: 10.1021/jacs.1c07771
  86. Fouet, G., et al. (2021). Molecular Basis of Complement C1q Collagen-Like Region Interaction with the Immunoglobulin-Like Receptor LAIR-1. Int. J. Mol. Sci. 22(10):18. doi: 10.3390/ijms22105125
  87. Fraga, R., et al. (2021). Design, Synthesis, Evaluation and Structure of Allenic 1 alpha,25-Dihydroxyvitamin D-3 Analogs with Locked Mobility at C-17. Chem.-Eur. J.:7. doi: 10.1002/chem.202101578
  88. Frechard, A., et al. (2021). Optimization of Sample Preparation for the Observation of Macromolecular Complexes by Electron (cryo-) Microscopy. In: Poterszman, A., ed. Multiprotein Complexes. New York, NY: SpringerLink 2021. doi: 10.1007/978-1-0716-1126-5_13
  89. Gaikwad, S., et al. (2021). Lithocholic acid-based design of noncalcemic vitamin D receptor agonists. Bioorganic Chem. 111:13. doi: 10.1016/j.bioorg.2021.104878
  90. Gallo, A., et al. (2021). H-1,C-13 and N-15 chemical shift assignments of the SUD domains of SARS-CoV-2 non-structural protein 3c: "The SUD-M and SUD-C domains". Biomol. NMR Assign.:7. doi: 10.1007/s12104-020-10000-9
  91. Gambelli, L., et al. (2021). The Polygonal Cell Shape and Surface Protein Layer of Anaerobic Methane-Oxidizing Methylomirabilislanthanidiphila Bacteria. Front. Microbiol. 12. doi: 10.3389/fmicb.2021.766527
  92. Garcia-Jimenez, M. J., et al. (2021). Midkine Interaction with Chondroitin Sulfate Model Synthetic Tetrasaccharides and Their Mimetics: The Role of Aromatic Interactions. Chem.-Eur. J.:16. doi: 10.1002/chem.202101674
  93. Garcia-Reyes, S., et al. (2021). Vfr or CyaB promote the expression of the pore-forming toxin exlBA operon in Pseudomonas aeruginosa ATCC 9027 without increasing its virulence in mice. Microbiology-(UK). 167(8):9. doi: 10.1099/mic.0.001083
  94. Garcia-Saez, I., et al. (2021). Eg5 targeting agents: From new anti-mitotic based inhibitor discovery to cancer therapy and resistance. Biochem. Pharmacol. 184:17. doi: 10.1016/j.bcp.2020.114364
  95. Gauthier, L., et al. (2021). Lectin recognition and hepatocyte endocytosis of GalNAc-decorated nanostructured lipid carriers. J. Drug Target.29(1):99-107. doi: 10.1080/1061186x.2020.1806286
  96. Geldon, S., et al. (2021). Redox-Mediated Regulation of Mitochondrial Biogenesis, Dynamics, and Respiratory Chain Assembly in Yeast and Human Cells. Front. Cell. Dev. Biol. 9:24. doi: 10.3389/fcell.2021.720656
  97. Geny, S., et al. (2021). Tagging Proteins with Fluorescent Reporters Using the CRISPR/Cas9 System and Double-Stranded DNA Donors. In: Poterszman, A., ed. Multiprotein Complexes. New York, NY: SpringerLink 2021. doi: 10.1007/978-1-0716-1126-5_3
  98. Geny, S., et al. (2021). Gene Tagging with the CRISPR-Cas9 System to Facilitate Macromolecular Complex Purification. In: Owens, R. J., ed. Structural Proteomics: High-Throughput Methods. New York, NY: Springer US 2021:153-174. doi: 10.1007/978-1-0716-1406-8_8
  99. Ghashghaei, O., et al. (2021). Extended Multicomponent Reactions with Indole Aldehydes: Access to Unprecedented Polyheterocyclic Scaffolds, Ligands of the Aryl Hydrocarbon Receptor. Angew. Chem.-Int. Edit. 60(5):2603-2608. doi: 10.1002/anie.202011253
  100. Giachin, G., et al. (2021). Assembly of the mitochondrial Complex I assembly complex suggests a regulatory role for deflavination. Angew. Chem. Int. Ed. Engl. 60(9):4689-4697. doi: 10.1002/anie.202011548
  101. Giallongo, S., et al. (2021). Phosphorylation within Intrinsic Disordered Region Discriminates Histone Variant macroH2A1 Splicing Isoforms-macroH2A1.1 and macroH2A1.2. Biology-Basel. 10(7):13. doi: 10.3390/biology10070659
  102. Gigli, L., et al. (2021). NMR for Single Ion Magnets. Magnetochemistry. 7(7):20. doi: 10.3390/magnetochemistry7070096
  103. Gigli, L., et al. (2021). On the Mechanism of Bioinspired Formation of Inorganic Oxides: Structural Evidence of the Electrostatic Nature of the Interaction between a Mononuclear Inorganic Precursor and Lysozyme. Biomolecules. 11(1):9. doi: 10.3390/biom11010043
  104. Gilbert, R. J. C. (2021). Electron microscopy as a critical tool in the determination of pore forming mechanisms in proteins. In: Heuck, A. P., ed. Pore-Forming Toxins. San Diego: Elsevier Academic Press Inc 2021:71-102. doi: 10.1016/bs.mie.2021.01.034
  105. Gimenez, E. F., et al. (2021). Cryo-EM density maps adjustment for subtraction, consensus and sharpening. J. Struct. Biol. 213(4):11. doi: 10.1016/j.jsb.2021.107780
  106. Gogl, G., et al. (2021). Hierarchized phosphotarget binding by the seven human 14-3-3 isoforms. Nat. Commun. 12(1):12. doi: 10.1038/s41467-021-21908-8
  107. Gonzalez, C. M., et al. (2021). Design, synthesis and evaluation of side-chain hydroxylated derivatives of lithocholic acid as potent agonists of the vitamin D receptor (VDR). Bioorganic Chem. 115:7. doi: 10.1016/j.bioorg.2021.105202
  108. Goodfellow, B. J., et al. (2021). The SOUL family of heme-binding proteins: Structure and function 15 years later. Coord. Chem. Rev. 448:12. doi: 10.1016/j.ccr.2021.214189
  109. Grabarczyk, D. B., et al. (2021). HUWE1 employs a giant substrate-binding ring to feed and regulate its HECT E3 domain. Nat. Chem. Biol.:20. doi: 10.1038/s41589-021-00831-5
  110. Grifagni, D., et al. (2021). SARS-CoV-2 M-pro inhibition by a zinc ion: structural features and hints for drug design. Chem. Commun.:4. doi: 10.1039/d1cc02956h
  111. Gu, R., et al. (2021). Constitutional Dynamic Selection at Low Reynolds Number in a Triple Dynamic System: Covalent Dynamic Adaptation Driven by Double Supramolecular Self-Assembly. J. Am. Chem. Soc. 143(35):14136-14146. doi: 10.1021/jacs.1c04446
  112. Guseva, S., et al. (2021). H-1, C-13 and N-15 Backbone chemical shift assignments of the n-terminal and central intrinsically disordered domains of SARS-CoV-2 nucleoprotein. Biomol. NMR Assign.:6. doi: 10.1007/s12104-021-10014-x
  113. Guyomar, C., et al. (2021). Structures of tmRNA and SmpB as they transit through the ribosome. Nat. Commun. 12(1):14. doi: 10.1038/s41467-021-24881-4
  114. Hauser, A., et al. (2021). Stepwise Conformational Stabilization of a HIV-1 Clade C Consensus Envelope Trimer Immunogen Impacts the Profile of Vaccine-Induced Antibody Responses. Vaccines. 9(7):23. doi: 10.3390/vaccines9070750
  115. Henot, F., et al. (2021). Optimized precursor to simplify assignment transfer between backbone resonances and stereospecifically labelled valine and leucine methyl groups: application to human Hsp90 N-terminal domain. J. Biomol. NMR.12. doi: 10.1007/s10858-021-00370-0
  116. Honorato, R. V., et al. (2021). Structural Biology in the Clouds: The WeNMR-EOSC Ecosystem. 8:729513. doi: 10.3389/fmolb.2021.729513
  117. Houser, J., et al. (2021). Development of 48-condition buffer screen for protein stability assessment. Eur. Biophys. J. Biophys. Lett.:11. doi: 10.1007/s00249-021-01497-6
  118. Ibrahim, A., et al. (2021). MeCP2 is a microsatellite binding protein that protects CA repeats from nucleosome invasion. Science. 372(6549):1411-+. doi: 10.1126/science.abd5581
  119. Ilíková, I., et al. (2021). Towards spruce-type photosystem II: consequences of the loss of light-harvesting proteins LHCB3 and LHCB6 in Arabidopsis. Plant Phys. 187(4):2691-2715. doi: 10.1093/plphys/kiab396
  120. Imbert, L., et al. (2021). In Vitro Production of Perdeuterated Proteins in H2O for Biomolecular NMR Studies. In: Chen, Y. W. and Yiu, C. B., eds. Structural Genomics. New York, NY: SpringerLink 2021. doi: 10.1007/978-1-0716-0892-0_8
  121. Iorio, A., et al. (2021). Biochemical, structural and dynamical studies reveal strong differences in the thermal-dependent allosteric behavior of two extremophilic lactate dehydrogenases. J. Struct. Biol. 213(3):11. doi: 10.1016/j.jsb.2021.107769
  122. Jamgotchian, L., et al. (2021). Tumor-targeted superfluorinated micellar probe for sensitive in vivo(19)F-MRI. Nanoscale. 13(4):2373-2377. doi: 10.1039/d0nr08200g
  123. Jessop, M., et al. (2021). Supramolecular assembly of the Escherichia coli LdcI upon acid stress. Proc. Natl. Acad. Sci. U. S. A. 118(2):11. doi: 10.1073/pnas.2014383118
  124. Jimenez-Moreno, A., et al. (2021). Cryo-EM and Single-Particle Analysis with Scipion. J. Vis. Exp. (171):27. doi: 10.3791/62261
  125. Jimenez-Moreno, A., et al. (2021). DeepAlign, a 3D alignment method based on regionalized deep learning for Cryo-EM. J. Struct. Biol.213(2):14. doi: 10.1016/j.jsb.2021.107712
  126. Jones, R., et al. (2021). Capping pores of alphavirus nsP1 gate membranous viral replication factories. Nature. 589(7843):615-+. doi: 10.1038/s41586-020-3036-8
  127. Jurasek, M., et al. (2021). Phosphorylation-induced changes in the PDZ domain of Dishevelled 3. Sci Rep. 11(1):14. doi: 10.1038/s41598-020-79398-5
  128. Juraszek, J., et al. (2021). Stabilizing the closed SARS-CoV-2 spike trimer. Nat. Commun. 12(1):8. doi: 10.1038/s41467-020-20321-x
  129. Jurcek, O., et al. (2021). Hexagonal Microparticles from Hierarchical Self-Organization of Chiral Trigonal Pd3L6 Macrotetracycles. Cell Rep. Phys. Sci. 2(1):19. doi: 10.1016/j.xcrp.2020.100303
  130. Kehlenbeck, D. M., et al. (2021). Cryo-EM structure of MsbA in saposin-lipid nanoparticles (Salipro) provides insights into nucleotide coordination. Febs J.:12. doi: 10.1111/febs.16327
  131. Kellner, R., et al. (2021). Protein formulation through automated screening of pH and buffer conditions, using the Robotein (R) high throughput facility. Eur. Biophys. J. Biophys. Lett. 50(3-4):473-490. doi: 10.1007/s00249-021-01510-y
  132. Kelpsas, V., et al. (2021). Neutron structures of Leishmania mexicana triosephosphate isomerase in complex with reaction-intermediate mimics shed light on the proton-shuttling steps. IUCrJ. 8(Pt 4):633-643. doi: 10.1107/s2052252521004619
  133. Khodr, V., et al. (2021). High-throughput measurements of bone morphogenetic protein/bone morphogenetic protein receptor interactions using biolayer interferometry. Biointerphases. 16(3):12. doi: 10.1116/6.0000926
  134. Klaholz, B. P. (2021). Studying the Structural Organization of Polyribosomes with Alexander S. Spirin. Biochem.-Moscow. 86(9):1053-1059. doi: 10.1134/s0006297921090030
  135. Kolarova, K., et al. (2021). Disruption of NAP1 genes in Arabidopsis thaliana suppresses the fas1 mutant phenotype, enhances genome stability and changes chromatin compaction. Plant J.:18. doi: 10.1111/tpj.15145
  136. Kolenko, P., et al. (2021). SHELIXIR: automation of experimental phasing procedures using SHELXC/D/E. J. Appl. Crystallogr. 54:996-1005. doi: 10.1107/s1600576721002454
  137. Korn, P., et al. (2021). Evaluation of 3-and 4-Phenoxybenzamides as Selective Inhibitors of the Mono-ADP-Ribosyltransferase PARP10. ChemistryOpen. 10(10):939-948. doi: 10.1002/open.202100087
  138. Krasnoselska, G. O., et al. (2021). Transient Transfection and Expression of Eukaryotic Membrane Proteins in Expi293F Cells and Their Screening on a Small Scale: Application for Structural Studies. In: Owens, R. J., ed. Structural Proteomics: High-Throughput Methods. New York, NY: Springer US 2021:105-128. doi: 10.1007/978-1-0716-1406-8_5
  139. Kraushar, M. L., et al. (2021). Protein Synthesis in the Developing Neocortex at Near-Atomic Resolution Reveals Ebp1-Mediated Neuronal Proteostasis at the 60S Tunnel Exit. Mol. Cell. 81(2):304-+. doi: 10.1016/j.molcel.2020.11.037
  140. Krupovic, M., et al. (2021). Bacterial Viruses Subcommittee and Archaeal Viruses Subcommittee of the ICTV: update of taxonomy changes in 2021. Arch. Virol. 166(11):6. doi: 10.1007/s00705-021-05205-9
  141. Kubackova, J., et al. (2021). Oligonucleotide Delivery across the Caco-2 Monolayer: The Design and Evaluation of Self-Emulsifying Drug Delivery Systems (SEDDS). Pharmaceutics. 13(4):27. doi: 10.3390/pharmaceutics13040459
  142. Kucera, O., et al. (2021). Anillin propels myosin-independent constriction of actin rings. Nat. Commun. 12(1):12. doi: 10.1038/s41467-021-24474-1
  143. Kucharikova, H., et al. (2021). Trimethylacetic Anhydride-Based Derivatization Facilitates Quantification of Histone Marks at the MS1 Level. Mol. Cell. Proteomics. 20:14. doi: 10.1016/j.mcpro.2021.100114
  144. Kundratova, K., et al. (2021). Transcriptomic and Proteomic Analysis of Drought Stress Response in Opium Poppy Plants during the First Week of Germination. Plants-Basel. 10(9):15. doi: 10.3390/plants10091878
  145. Lai, X. L., et al. (2021). The intervening domain is required for DNA-binding and functional identity of plant MADS transcription factors. Nat. Commun. 12(1):13. doi: 10.1038/s41467-021-24978-w
  146. Lapcik, P., et al. (2021). A large-scale assay library for targeted protein quantification in renal cell carcinoma tissues. Proteomics.7. doi: 10.1002/pmic.202100228
  147. Lazaro, M., et al. (2021). 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme. Commun. Biol. 4(1):8. doi: 10.1038/s42003-021-02222-x
  148. Leonardo, D. A., et al. (2021). Orientational Ambiguity in Septin Coiled Coils and its Structural Basis. J. Mol. Biol. 433(9):19. doi: 10.1016/j.jmb.2021.166889
  149. Levanova, A. A., et al. (2021). RNA-Dependent RNA Polymerase from Heterobasidion RNA Virus 6 Is an Active Replicase In Vitro. Viruses-Basel. 13(9):20. doi: 10.3390/v13091738
  150. Liaci, A. M., et al. (2021). Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage. Mol. Cell. 81(19):3934-+. doi: 10.1016/j.molcel.2021.07.031
  151. Liu, C., et al. (2021). Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum. Cell. 184(16):4220-+. doi: 10.1016/j.cell.2021.06.020
  152. Liu, J., et al. (2021). Clinical Images: Rice bodies in cinematic rendering. Arthritis Rheumatol. 73(11):2077-2077. doi: 10.1002/art.41890
  153. Liu, S. S., et al. (2021). Evaluation of dsRNA delivery methods for targeting macrophage migration inhibitory factor MIF in RNAi-based aphid control. J. Plant Dis. Prot.:12. doi: 10.1007/s41348-021-00464-9
  154. Liu, Y., et al. (2021). Diversity, taxonomy, and evolution of archaeal viruses of the class Caudoviricetes. PLoS. Biol. 19(11):26. doi: 10.1371/journal.pbio.3001442
  155. Lopez-Mendez, B., et al. (2021). Reproducibility and accuracy of microscale thermophoresis in the NanoTemper Monolith: a multi laboratory benchmark study. Eur. Biophys. J. Biophys. Lett.:17. doi: 10.1007/s00249-021-01532-6
  156. Luchinat, E., et al. (2021). Protein in-cell NMR spectroscopy at 1.2 GHz. J. Biomol. NMR. 75(2-3):97-107. doi: 10.1007/s10858-021-00358-w
  157. Luchinat, E., et al. (2021). Determination of intracellular protein-ligand binding affinity by competition binding in-cell NMR. Acta Crystallogr. Sect. D-Struct. Biol. 77:1270-1281. doi: 10.1107/s2059798321009037
  158. Macias, J. R., et al. (2021). 3DBionotes COVID-19 edition. Bioinformatics. 37(22):4258-4260. doi: 10.1093/bioinformatics/btab397
  159. Mahieu, E., et al. (2021). The power of SANS, combined with deuteration and contrast variation, for structural studies of functional and dynamic biomacromolecular systems in solution. EPJ Web Conf. 236:03002. doi: 10.1051/epjconf/202023603002
  160. Maksimainen, M. M., et al. (2021). Analogs of TIQ-A as inhibitors of human mono-ADP-ribosylating PARPs. Bioorg. Med. Chem. 52:116511. doi: 10.1016/j.bmc.2021.116511
  161. Malki, A., et al. (2021). Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress. Angew. Chem.-Int. Edit.:6. doi: 10.1002/anie.202109961
  162. Manigrasso, J., et al. (2021). Computer-aided design of RNA-targeted small molecules: A growing need in drug discovery. Chem. 7(11):2965-2988. doi: 10.1016/j.chempr.2021.05.021
  163. Mantynen, S., et al. (2021). Black box of phage-bacterium interactions: exploring alternative phage infection strategies. Open Biol. 11(9):12. doi: 10.1098/rsob.210188
  164. Marcia, M., et al. (2021). Finding the Ion in the RNA-Stack: Can Computational Models Accurately Predict Key Functional Elements in Large Macromolecular Complexes? J. Chem Inf. Model. 61(6):2511-2515. doi: 10.1021/acs.jcim.1c00572
  165. Marek, M., et al. (2021). Species-selective targeting of pathogens revealed by the atypical structure and active site of Trypanosoma cruzi histone deacetylase DAC2. Cell Reports. 37(12):27. doi: 10.1016/j.celrep.2021.110129
  166. Martin, W. J., et al. (2021). Screening strategies for identifying RNA- and ribonucleoprotein-targeted compounds. Trends Pharmacol. Sci.42(9):758-771. doi: 10.1016/j.tips.2021.06.001
  167. Martin-Malpartida, P., et al. (2021). HTSDSF Explorer, A Novel Tool to Analyze High-throughput DSF Screenings. J. Mol. Biol.:167372. doi: 10.1016/j.jmb.2021.167372
  168. Martins, A., et al. (2021). Self-association of MreC as a regulatory signal in bacterial cell wall elongation. Nat. Commun. 12(1):10. doi: 10.1038/s41467-021-22957-9
  169. Massai, L., et al. (2021). Direct detection of iron clusters in L ferritins through ESI-MS experiments. Dalton Trans. 50(45):4. doi: 10.1039/d1dt03106f
  170. Matteucci, S., et al. (2021). In Cellulo Mossbauer and EPR Studies Bring New Evidence to the Long-Standing Debate on Iron-Sulfur Cluster Binding in Human Anamorsin. Angew. Chem.-Int. Edit.:6. doi: 10.1002/anie.202102910
  171. Mattila, A. L. K., et al. (2021). Evolutionary and ecological processes influencing chemical defense variation in an aposematic and mimetic Heliconius butterfly. PeerJ. 9:29. doi: 10.7717/peerj.11523
  172. Mayer, M., et al. (2021). Structural and Functional Insights into the Biofilm-Associated BceF Tyrosine Kinase Domain from Burkholderia cepacia. Biomolecules. 11(8):15. doi: 10.3390/biom11081196
  173. Mayeux, G., et al. (2021). Cell-free expression of the outer membrane protein OprF of Pseudomonas aeruginosa for vaccine purposes. Life Sci. Alliance. 4(6):16. doi: 10.26508/lsa.202000958
  174. McGregor, L., et al. (2021). Joint neutron/X-ray crystal structure of a mechanistically relevant complex of perdeuterated urate oxidase and simulations provide insight into the hydration step of catalysis. IUCrJ. 8(1). doi: 10.1107/S2052252520013615
  175. Menzildjian, G., et al. (2021). Efficient Dynamic Nuclear Polarization up to 230 K with Hybrid BDPA-Nitroxide Radicals at a High Magnetic Field. J. Phys. Chem. B. 125(48):13329-13338. doi: 10.1021/acs.jpcb.1c07307
  176. Meoni, G., et al. (2021). Metabolomic/lipidomic profiling of COVID-19 and individual response to tocilizumab. PLoS Pathog. 17(2):14. doi: 10.1371/journal.ppat.1009243
  177. Miele, A. E., et al. (2021). Biophysical characterization of the complex between the iron-responsive transcription factor Fep1 and DNA. Eur. Biophys. J. Biophys. Lett.:12. doi: 10.1007/s00249-020-01489-y
  178. Mikulasek, K., et al. (2021). SP3 Protocol for Proteomic Plant Sample Preparation Prior LC-MS/MS. Front. Plant Sci. 12:12. doi: 10.3389/fpls.2021.635550
  179. Moeglin, E., et al. (2021). A Novel Nanobody Precisely Visualizes Phosphorylated Histone H2AX in Living Cancer Cells under Drug-Induced Replication Stress. Cancers. 13(13):25. doi: 10.3390/cancers13133317
  180. Monttinen, H. A. M., et al. (2021). Structure Unveils Relationships between RNA Virus Polymerases. Viruses. 13(2):17. doi: 10.3390/v13020313
  181. Moravcová, J., et al. (2021). Cryo-Focused Ion Beam Lamella Preparation Protocol for in Situ Structural Biology. In: Owens, R. J., ed. Structural Proteomics: High-Throughput Methods. New York, NY: Springer US 2021:301-322. doi: 10.1007/978-1-0716-1406-8_15
  182. Moravcova, J., et al. (2021). Preparation and Cryo-FIB micromachining of Saccharomyces cerevisiae for Cryo-Electron Tomography. J. Vis. Exp.(177):16. doi: 10.3791/62351
  183. Mustonen, V., et al. (2021). Crystal and solution structure of NDRG1, a membrane-binding protein linked to myelination and tumour suppression. FEBS J.:23. doi: 10.1111/febs.15660
  184. Naudi-Fabra, S., et al. (2021). Quantitative Description of Intrinsically Disordered Proteins Using Single-Molecule FRET, NMR, and SAXS. J. Am. Chem. Soc. 143(48):20109-20121. doi: 10.1021/jacs.1c06264
  185. Naudin, E. A., et al. (2021). Acyl Transfer Catalytic Activity in De Novo Designed Protein with N-Terminus of alpha-Helix As Oxyanion-Binding Site. J. Am. Chem. Soc. 143(9):3330-3339. doi: 10.1021/jacs.0c10053
  186. Nemec, A., et al. (2021). Delineation of a novel environmental phylogroup of the genus Acinetobacter encompassing Acinetobacter terrae sp. nov., Acinetobacter terrestris sp. nov. and three other tentative species. Syst. Appl. Microbiol. 44(4):9. doi: 10.1016/j.syapm.2021.126217
  187. Noone, D. P., et al. (2021). Cryo-Electron Microscopy and Biochemical Analysis Offer Insights Into the Effects of Acidic pH, Such as Occur During Acidosis, on the Complement Binding Properties of C-Reactive Protein. Front. Immunol. 12:14. doi: 10.3389/fimmu.2021.757633
  188. Novotny, J., et al. (2021). Crystal and Substituent Effects on Paramagnetic NMR Shifts in Transition-Metal Complexes. Inorg. Chem.60(13):9368-9377. doi: 10.1021/acs.inorgchem.1c00204
  189. Obaji, E., et al. (2021). Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition. Nat. Commun. 12(1):8. doi: 10.1038/s41467-021-23800-x
  190. Oborilova, R., et al. (2021). Atomic force microscopy and surface plasmon resonance for real-time single-cell monitoring of bacteriophage-mediated lysis of bacteria. Nanoscale. 13(31):12. doi: 10.1039/d1nr02921e
  191. Paclikova, P., et al. (2021). Roles of individual human Dishevelled paralogs in the Wnt signalling pathways. Cell. Signal. 85:11. doi: 10.1016/j.cellsig.2021.110058
  192. Parigi, G., et al. (2021). Unveiling protein dynamics in solution with field-cycling NMR relaxometry. Prog. Nucl. Magn. Reson. Spectrosc. 124:85-98. doi: 10.1016/j.pnmrs.2021.05.001
  193. Pastucha, M., et al. (2021). Upconversion-Linked Immunoassay for the Diagnosis of Honeybee Disease American Foulbrood. IEEE J. Sel. Top. Quantum Electron. 27(5):11. doi: 10.1109/jstqe.2021.3049689
  194. Peleg, Y., et al. (2021). Community-Wide Experimental Evaluation of the PROSS Stability-Design Method. J. Mol. Biol. 433(13):14. doi: 10.1016/j.jmb.2021.166964
  195. Perestrelo, A. R., et al. (2021). Multiscale Analysis of Extracellular Matrix Remodeling in the Failing Heart. Circ.Res. 128(1):24-38. doi: 10.1161/circresaha.120.317685
  196. Perez-Ruiz, M., et al. (2021). Assisted assembly of bacteriophage T7 core components for genome translocation across the bacterial envelope. Proc. Natl. Acad. Sci. U. S. A. 118(34):10. doi: 10.1073/pnas.2026719118
  197. Peterkova, K., et al. (2021). c-kit2 G-quadruplex stabilized via a covalent probe: exploring G-quartet asymmetry. Nucleic Acids Res. 49(15):8947-8960. doi: 10.1093/nar/gkab659
  198. Piticchio, S. G., et al. (2021). Discovery of Novel BRD4 Ligand Scaffolds by Automated Navigation of the Fragment Chemical Space. J. Med. Chem. 64(24):14. doi: 10.1021/acs.jmedchem.1c01108
  199. Plavec, Z., et al. (2021). Virus structure and structure-based antivirals. Curr. Opin. Virol. 51:16-24. doi: 10.1016/j.coviro.2021.09.005
  200. Polykretis, P. (2021). Advanced glycation end-products as potential triggering factors of self-reactivity against myelin antigens in Multiple Sclerosis. Med.   Hypotheses. 157:110702. doi: 10.1016/j.mehy.2021.110702
  201. Polykretis, P., et al. (2021). Biophysical characterization of the interaction between the full-length XIAP and Smac/DIABLO. Biochem.   Biophys.   Res.   Commun. 568:180-185. doi: 10.1016/j.bbrc.2021.06.077
  202. Popovic, M., et al. (2021). In vivo and in vitro cell-based model of lung adenocarcinoma from patients with pleural effusion. Neoplasma. 68(3):498-508. doi: 10.4149/neo_2021_200906N953
  203. Porizka, P., et al. (2021). Laser-induced breakdown spectroscopy as a readout method for immunocytochemistry with upconversion nanoparticles. Microchim. Acta. 188(5):10. doi: 10.1007/s00604-021-04816-y
  204. Pounot, K., et al. (2021). Zinc determines dynamical properties and aggregation kinetics of human insulin. Biophys. J. 120(5):886-898. doi: 10.1016/j.bpj.2020.11.2280
  205. Pradhan, S., et al. (2021). Stable lead-halide perovskite quantum dots as efficient visible light photocatalysts for organic transformations. Nanoscale Adv. 3(5):1464-1472. doi: 10.1039/d0na00992j
  206. Prasanna, M., et al. (2021). On the use of adenovirus dodecahedron as a carrier for glycoconjugate vaccines. Glycoconjugate J.:10. doi: 10.1007/s10719-021-09999-3
  207. Prechoux, A., et al. (2021). Deciphering the structural attributes of protein-heparan sulfate interactions using chemo-enzymatic approaches and NMR spectroscopy. Glycobiology. 31(7):851-858. doi: 10.1093/glycob/cwab012
  208. Prochazkova, M., et al. (2021). Capsid Structure of Leishmania RNA Virus 1. J. Virol. 95(3):12. doi: 10.1128/jvi.01957-20
  209. Prusty, N. R., et al. (2021). The human YAE1-ORAOV1 complex of the cytosolic iron-sulfur protein assembly machinery binds a 4Fe-4S cluster. Inorg. Chim. Acta. 518:10. doi: 10.1016/j.ica.2021.120252
  210. Ramirez-Aportela, E., et al. (2021). FSC-Q: a CryoEM map-to-atomic model quality validation based on the local Fourier shell correlation. Nat. Commun. 12(1):7. doi: 10.1038/s41467-020-20295-w
  211. Ramos, J., et al. (2021). Structural insights into protein folding, stability and activity using in vivo perdeuteration of hen egg-white lysozyme. IUCrJ. 8(Pt 3):372-386. doi: 10.1107/s2052252521001299
  212. Ramos-Morales, E., et al. (2021). The structure of the mouse ADAT2/ADAT3 complex reveals the molecular basis for mammalian tRNA wobble adenosine-to-inosine deamination. Nucleic Acids Res. 49(11):6529-6548. doi: 10.1093/nar/gkab436
  213. Rathinaswamy, M. K., et al. (2021). Structure of the phosphoinositide 3-kinase (PI3K) p110 gamma-p101 complex reveals molecular mechanism of GPCR activation. Sci. Adv. 7(35):19. doi: 10.1126/sciadv.abj4282
  214. Rathinaswamy, M. K., et al. (2021). HDX-MS-optimized approach to characterize nanobodies as tools for biochemical and structural studies of class IB phosphoinositide 3-kinases. Structure. 29(12):1371-+. doi: 10.1016/j.str.2021.07.002
  215. Ravera, E. (2021). Phase distortion-free paramagnetic NMR spectra. J. Magn. Reson. 8-9:100022. doi: 10.1016/j.jmro.2021.100022
  216. Ravera, E., et al. (2021). A Quantum Chemistry View on Two Archetypical Paramagnetic Pentacoordinate Nickel(II) Complexes Offers a Fresh Look on Their NMR Spectra. Inorg. Chem. 60(3):2068-2075. doi: 10.1021/acs.inorgchem.0c03635
  217. Ravera, E., et al. (2021). A High-Resolution View of the Coordination Environment in a Paramagnetic Metalloprotein from its Magnetic Properties. Angew. Chem.-Int. Edit.:8. doi: 10.1002/anie.202101149
  218. Redhead, M. A., et al. (2021). Bispecific repurposed medicines targeting the viral and immunological arms of COVID-19. Sci Rep. 11(1):14. doi: 10.1038/s41598-021-92416-4
  219. Richtar, J., et al. (2021). Adamantane Substitution Effects on Crystallization and Electrooptical Properties of Epindolidione and Quinacridone Dyes. ChemPhotoChem.13. doi: 10.1002/cptc.202100127
  220. Rivas Serna, I. M., et al. (2021). Lipidomic Profiling Identifies Signatures of Poor Cardiovascular Health. Metabolites. 11(11):15. doi: 10.3390/metabo11110747
  221. Rizzo, D., et al. (2021). Evaluation of the Higher Order Structure of Biotherapeutics Embedded in Hydrogels for Bioprinting and Drug Release. Anal. Chem. 93(32):11208-11214. doi: 10.1021/acs.analchem.1c01850
  222. Rizzo, D., et al. (2021). Origin of the MRI Contrast in Natural and Hydrogel Formulation of Pineapple Juice. Bioinorg. Chem. Appl. 2021:12. doi: 10.1155/2021/6666018
  223. Rizzuto, C. (2021). The ERIC Consortium a new type of EU research institution. Europhys.   News. 51(3):25-27. doi: 10.1051/epn/2020305
  224. Roche, B., et al. (2021). Identification of the fatty acid coenzyme-A ligase FadD1 as an interacting partner of FptX in the Pseudomonas aeruginosa pyochelin pathway. FEBS Lett.:9. doi: 10.1002/1873-3468.14012
  225. Rodrigues, J., et al. (2021). High Throughput Expression Screening of Arabinofuranosyltransferases from Mycobacteria. Processes. 9(4):18. doi: 10.3390/pr9040629
  226. Rohac, R., et al. (2021). Crystal Structure of the FeFe -Hydrogenase Maturase HydE Bound to Complex-B. J. Am. Chem. Soc. 143(22):8499-8508. doi: 10.1021/jacs.1c03367
  227. Rossolillo, P., et al. (2021). Production of Multiprotein Complexes Using the Baculovirus Expression System: Homology-Based and Restriction-Free Cloning Strategies for Construct Design. In: Poterszman, A., ed. Multiprotein Complexes. New York, NY: SpringerLink 2021. doi: 10.1007/978-1-0716-1126-5_2
  228. Rovito, D., et al. (2021). Myod1 and GR coordinate myofiber-specific transcriptional enhancers. Nucleic Acids Res. 49(8):4472-4492. doi: 10.1093/nar/gkab226
  229. Ruiz, L., et al. (2021). Unveiling the dimer/monomer propensities of Smad MH1-DNA complexes. Comp. Struct. Biotechnol. J.. 19:632-646. doi: 10.1016/j.csbj.2020.12.044
  230. Salinas, N., et al. (2021). The amphibian antimicrobial peptide uperin 3.5 is a cross-alpha/cross-beta chameleon functional amyloid. Proc. Natl. Acad. Sci. U. S. A. 118(3):8. doi: 10.1073/pnas.2014442118
  231. Salladini, E., et al. (2021). Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation. Biomolecules. 11(9):33. doi: 10.3390/biom11091324
  232. Salvi, N., et al. (2021). H-1, C-13 and N-15 backbone chemical shift assignments of SARS-CoV-2 nsp3a. Biomol. NMR Assign.:4. doi: 10.1007/s12104-020-10001-8
  233. Saudino, G., et al. (2021). Molecular Basis of Multiple Mitochondrial Dysfunctions Syndrome 2 Caused by CYS59TYR BOLA3 Mutation. Int. J. Mol. Sci. 22(9):18. doi: 10.3390/ijms22094848
  234. Schep, R., et al. (2021). Impact of chromatin context on Cas9-induced DNA double-strand break repair pathway balance. Mol. Cell. 81(10):2216-+. doi: 10.1016/j.molcel.2021.03.032
  235. Schiavina, M., et al. (2021). The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1-248 residue construct: sequence-specific resonance assignments through NMR. Biomol. NMR Assign. 15(1):219-227. doi: 10.1007/s12104-021-10009-8
  236. Schiro, G., et al. (2021). Diffusivelike Motions in a Solvent-Free Protein-Polymer Hybrid. Phys. Rev. Lett. 126(8):7. doi: 10.1103/PhysRevLett.126.088102
  237. Scholl, D., et al. (2021). A topological switch in CFTR modulates channel activity and sensitivity to unfolding. Nat. Chem. Biol. 17(9):22. doi: 10.1038/s41589-021-00844-0
  238. Schreiber, V., et al. (2021). Extensive NEUROG3 occupancy in the human pancreatic endocrine gene regulatory network. Mol. Metab. 53:15. doi: 10.1016/j.molmet.2021.101313
  239. Schwarzer, S., et al. (2021). Growth Phase Dependent Cell Shape of Haloarcula. Microorganisms. 9(2):14. doi: 10.3390/microorganisms9020231
  240. Sedlacek, I., et al. (2021). Classification of a Violacein-Producing Psychrophilic Group of Isolates Associated with Freshwater in Antarctica and Description of Rugamonas violacea sp. nov. Microbiol. Spectr. 9(1):14. doi: 10.1128/Spectrum.00452-21
  241. Signor, L., et al. (2021). Divalent cations influence the dimerization mode of murine S100A9 protein by modulating its disulfide bond pattern. J. Struct. Biol. 213(1):16. doi: 10.1016/j.jsb.2020.107689
  242. Silman, I., et al. (2021). Torpedo californica acetylcholinesterase is stabilized by binding of a divalent metal ion to a novel and versatile 4D motif. Protein Sci. 30(5):966-981. doi: 10.1002/pro.4061
  243. Sinnaeve, D., et al. (2021). Fluorine NMR study of proline-rich sequences using fluoroprolines. Magn. Reson. 2(2):795-813. doi: 10.5194/mr-2-795-2021
  244. Sobska, J., et al. (2021). Counterion-insulated near-infrared dyes in biodegradable polymer nanoparticles for in vivo imaging. Nanoscale Adv.:10. doi: 10.1039/d1na00649e
  245. Sojka, M., et al. (2021). Supramolecular Coronation of Platinum(II) Complexes by Macrocycles: Structure, Relativistic DFT Calculations, and Biological Effects. Inorg. Chem.  . 60(23):17911-17925. doi: 10.1021/acs.inorgchem.1c02467
  246. Sopousek, J., et al. (2021). Thick nanoporous matrices of polystyrene nanoparticles and their potential for electrochemical biosensing. Electrochim. Acta. 368:9. doi: 10.1016/j.electacta.2020.137607
  247. Sorigue, D., et al. (2021). Mechanism and dynamics of fatty acid photodecarboxylase. Science. 372(6538):148-+. doi: 10.1126/science.abd5687
  248. Sorzano, C. O. S., et al. (2021). Principal component analysis is limited to low-resolution analysis in cryoEM. Acta Crystallogr. Sect. D-Struct. Biol. 77:835-839. doi: 10.1107/s2059798321002291
  249. Sorzano, C. O. S., et al. (2021). Algorithmic robustness to preferred orientations in single particle analysis by CryoEM. J. Struct. Biol. 213(1):5. doi: 10.1016/j.jsb.2020.107695
  250. Sowa, S. T., et al. (2021). A molecular toolbox for ADP-ribosyl binding proteins. 1(8):100121. doi: 10.1016/j.crmeth.2021.100121
  251. Sowa, S. T., et al. (2021). High-resolution Crystal Structure of Human pERp1, A Saposin-like Protein Involved in IgA, IgM and Integrin Maturation in the Endoplasmic Reticulum. J. Mol. Biol. 433(5):15. doi: 10.1016/j.jmb.2021.166826
  252. Sponer, J. E., et al. (2021). Questions and Answers Related to the Prebiotic Production of Oligonucleotide Sequences from 3 ',5 ' Cyclic Nucleotide Precursors. Life-Basel. 11(8):13. doi: 10.3390/life11080800
  253. Sponer, J. E., et al. (2021). Non-Enzymatic, Template-Free Polymerization of 3',5' Cyclic Guanosine Monophosphate on Mineral Surfaces. ChemSystemsChem.9. doi: 10.1002/syst.202100017
  254. Strelak, D., et al. (2021). Advances in Xmipp for Cryo-Electron Microscopy: From Xmipp to Scipion. Molecules. 26(20):14. doi: 10.3390/molecules26206224
  255. Suarez, V. T., et al. (2021). Correlative transmission electron microscopy and high-resolution hard X-ray fluorescence microscopy of cell sections to measure trace element concentrations at the organelle level. J. Struct. Biol. 213(3):8. doi: 10.1016/j.jsb.2021.107766
  256. Sukenik, L., et al. (2021). Cargo Release from Nonenveloped Viruses and Virus-like Nanoparticles: Capsid Rupture or Pore Formation. ACS Nano. 15(12):11. doi: 10.1021/acsnano.1c04814
  257. Supasa, P., et al. (2021). Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera. Cell. 184(8):2201-+. doi: 10.1016/j.cell.2021.02.033
  258. Suraci, D., et al. (2021). ISCA1 Orchestrates ISCA2 and NFU1 in the Maturation of Human Mitochondrial 4Fe-4S Proteins. J. Mol. Biol.433(10):17. doi: 10.1016/j.jmb.2021.166924
  259. Swedlow, J. R., et al. (2021). A global view of standards for open image data formats and repositories. Nat. Methods. 18(12):1440-1446. doi: 10.1038/s41592-021-01113-7
  260. Taher, R., et al. (2021). A structure-function study of ZraP and ZraS provides new insights into the two-component system Zra. Biochim. Biophys. Acta-Gen. Subj. 1865(3):9. doi: 10.1016/j.bbagen.2020.129810
  261. Tarasova, E. V., et al. (2021). European Biomedical Research Infrastructures and the Fight against COVID-19 Pandemic. Sovrem. Tehnol. Med.13(1):6-13. doi: 10.17691/stm2021.13.1.01
  262. Thepaut, M., et al. (2021). DC/L-SIGN recognition of spike glycoprotein promotes SARS-CoV-2 trans-infection and can be inhibited by a glycomimetic antagonist. PLoS Pathog. 17(5):27. doi: 10.1371/journal.ppat.1009576
  263. Tittes, C., et al. (2021). Cellular and Genomic Properties of Haloferax gibbonsii LR2-5, the Host of Euryarchaeal Virus HFTV1. Front. Microbiol.12:14. doi: 10.3389/fmicb.2021.625599
  264. Tomecek, J., et al. (2021). Modes of Micromolar Host-Guest Binding of beta-Cyclodextrin Complexes Revealed by NMR Spectroscopy in Salt Water. J. Org. Chem. 86(6):4483-4496. doi: 10.1021/acs.joc.0c02917
  265. Torner, R., et al. (2021). Backbone and methyl resonances assignment of the 87 kDa prefoldin from Pyrococcus horikoshii. Biomol. NMR Assign.:10. doi: 10.1007/s12104-021-10029-4
  266. Torricella, F., et al. (2021). Rapid protein delivery to living cells for biomolecular investigation. Biochem. Biophys. Res. Commun. 570:82-88. doi: 10.1016/j.bbrc.2021.07.006
  267. Torricella, F., et al. (2021). Nitroxide spin labels and EPR spectroscopy: A powerful association for protein dynamics studies. BBA-Proteins Proteomics. 1869(7):14. doi: 10.1016/j.bbapap.2021.140653
  268. Trindade, I. B., et al. (2021). Sequence-specific assignments in NMR spectra of paramagnetic systems: A non-systematic approach. Inorg. Chim. Acta. 514:8. doi: 10.1016/j.ica.2020.119984
  269. Trouillon, J., et al. (2021). Determination of the two-component systems regulatory network reveals core and accessory regulations across Pseudomonas aeruginosa lineages. Nucleic Acids Res. 49(20):11476-11490. doi: 10.1093/nar/gkab928
  270. Trouve, J., et al. (2021). Metabolic biorthogonal labeling and dSTORM imaging of peptidoglycan synthesis in Streptococcus pneumoniae. STAR Prot. 2(4):101006. doi: 10.1016/j.xpro.2021.101006
  271. Trouve, J., et al. (2021). Nanoscale dynamics of peptidoglycan assembly during the cell cycle of Streptococcus pneumoniae. Curr. Biol.31(13):2844-+. doi: 10.1016/j.cub.2021.04.041
  272. Truebestein, L., et al. (2021). Structure of autoinhibited Akt1 reveals mechanism of PIP3-mediated activation. Proc. Natl. Acad. Sci. U. S. A.118(33):11. doi: 10.1073/pnas.2101496118
  273. Tully, M. D., et al. (2021). Analysis of SEC-SAXS data via EFA deconvolution and Scatter. J. Vis. Exp. (167):16. doi: 10.3791/61578
  274. Tumova, P., et al. (2021). Inheritance of the reduced mitochondria of Giardia intestinalis is coupled to the flagellar maturation cycle. BMC Biol.19(1):20. doi: 10.1186/s12915-021-01129-7
  275. Uchanski, T., et al. (2021). Megabodies expand the nanobody toolkit for protein structure determination by single-particle cryo-EM. Nat. Methods. 18(1):60-+. doi: 10.1038/s41592-020-01001-6
  276. Urso, M., et al. (2021). Breaking Polymer Chains with Self-Propelled Light-Controlled Navigable Hematite Microrobots. Adv. Funct. Mater.:10. doi: 10.1002/adfm.202101510
  277. Uwizeye, C., et al. (2021). Cytoklepty in the plankton: A host strategy to optimize the bioenergetic machinery of endosymbiotic algae. Proc. Natl. Acad. Sci. U. S. A. 118(27):11. doi: 10.1073/pnas.2025252118|1of11
  278. Uwizeye, C., et al. (2021). Morphological bases of phytoplankton energy management and physiological responses unveiled by 3D subcellular imaging. Nat. Commun. 12(1):12. doi: 10.1038/s41467-021-21314-0
  279. Van Driessche, A. E. S., et al. (2021). Nucleation of protein mesocrystals via oriented attachment. Nat. Commun. 12(1):8. doi: 10.1038/s41467-021-24171-z
  280. Vanden Broeck, A., et al. (2021). Structural basis for allosteric regulation of Human Topoisomerase II alpha. Nat. Commun. 12(1):13. doi: 10.1038/s41467-021-23136-6
  281. Vignoli, A., et al. (2021). Exploring Serum NMR-Based Metabolomic Fingerprint of Colorectal Cancer Patients: Effects of Surgery and Possible Associations with Cancer Relapse. Appl. Sci.-Basel. 11(23):12. doi: 10.3390/app112311120
  282. Vignoli, A., et al. (2021). Differential Network Analysis Reveals Molecular Determinants Associated with Blood Pressure and Heart Rate in Healthy Subjects. J. Proteome Res. 20(1):1040-1051. doi: 10.1021/acs.jproteome.0c00882
  283. von Loeffelholz, O., et al. (2021). Setup and Troubleshooting of Volta Phase Plate Cryo-EM Data Collection. In: Owens, R. J., ed. Structural Proteomics: High-Throughput Methods. New York, NY: Springer US 2021:291-299. doi: 10.1007/978-1-0716-1406-8_14
  284. Waldie, S., et al. (2021). ApoE and ApoE Nascent-Like HDL Particles at Model Cellular Membranes: Effect of Protein Isoform and Membrane Composition. Front. Chem. 9:15. doi: 10.3389/fchem.2021.630152
  285. Walker, P. J., et al. (2021). Changes to virus taxonomy and to the International Code of Virus Classification and Nomenclature ratified by the International Committee on Taxonomy of Viruses (2021). Arch. Virol. 166(9):16. doi: 10.1007/s00705-021-05156-1
  286. Walsh, M. A., et al. (2021). Diamond Light Source: contributions to SARS-CoV-2 biology and therapeutics. Biochem. Biophys. Res. Commun.538:40-46. doi: 10.1016/j.bbrc.2020.11.041
  287. Wang, J. M., et al. (2021). Identification of Mg2+ ions next to nucleotides in cryo-EM maps using electrostatic potential maps. Acta Crystallogr. Sect. D-Struct. Biol. 77:534-539. doi: 10.1107/s2059798321001893
  288. Webster, M. W., et al. (2021). The intricate relationship between transcription and translation. Proc. Natl. Acad. Sci. U. S. A. 118(21):3. doi: 10.1073/pnas.2106284118
  289. Webster, M. W., et al. (2021). Macromolecular assemblies supporting transcription-translation coupling. Transcr.-Austin. 12(4):103-125. doi: 10.1080/21541264.2021.1981713
  290. Wehbie, M., et al. (2021). Glucose-Based Fluorinated Surfactants as Additives for the Crystallization of Membrane Proteins: Synthesis and Preliminary Physical-Chemical and Biochemical Characterization. ACS Omega. 6(38):24397-24406. doi: 10.1021/acsomega.1c02581
  291. Wehbie, M., et al. (2021). Maltose-Based Fluorinated Surfactants for Membrane-Protein Extraction and Stabilization. Langmuir. 37(6):2111-2122. doi: 10.1021/acs.langmuir.0c03214
  292. Weinhaupl, K., et al. (2021). Architecture and assembly dynamics of the essential mitochondrial chaperone complex TIM9.10.12. Structure. 29(9):1065-+. doi: 10.1016/j.str.2021.04.009
  293. Wicker-Planquart, C., et al. (2021). Insights into the ligand binding specificity of SREC-II (scavenger receptor expressed by endothelial cells). FEBS Open Bio. 11(10):12. doi: 10.1002/2211-5463.13260
  294. Wienk, H., et al. (2021). iNEXT-Discovery and Instruct-ERIC: Integrating High-End Services for Translational Research in Structural Biology. J. Vis. Exp. (177):6. doi: 10.3791/63435
  295. Wiese, A. J., et al. (2021). Arabidopsis bZIP18 and bZIP52 Accumulate in Nuclei Following Heat Stress where They Regulate the Expression of a Similar Set of Genes. Int. J. Mol. Sci. 22(2):24. doi: 10.3390/ijms22020530
  296. Yang, Y., et al. (2021). The molecular basis of regulation of bacterial capsule assembly by Wzc. Nat. Commun. 12(1):13. doi: 10.1038/s41467-021-24652-1
  297. Yon, M., et al. (2021). Hybrid Polymeric Nanostructures Stabilized by Zirconium and Gadolinium Ions for Use as Magnetic Resonance Imaging Contrast Agents. ACS Appl. Nano Mater. 4(5):4974-4982. doi: 10.1021/acsanm.1c00495
  298. Zeronian, M. R., et al. (2021). Notch-Jagged signaling complex defined by an interaction mosaic. Proc. Natl. Acad. Sci. U. S. A. 118(30):12. doi: 10.1073/pnas.2102502118
  299. Zhang, Y. R., et al. (2021). Structural Studies Provide New Insights into the Role of Lysine Acetylation on Substrate Recognition by CARM1 and Inform the Design of Potent Peptidomimetic Inhibitors. ChemBioChem.9. doi: 10.1002/cbic.202100506
  300. Zhou, D. M., et al. (2021). Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera. Cell. 184(9):2348-+. doi: 10.1016/j.cell.2021.02.037
  301. Zouhir, S., et al. (2021). MagC is a NplC/P60-like member of the alpha-2-macroglobulin Mag complex of Pseudomonas aeruginosa that interacts with peptidoglycan. FEBS Lett.:13. doi: 10.1002/1873-3468.14148

2020

  1. Aarestrup, F. M., et al. (2020). Towards a European health research and innovation cloud (HRIC). Genome Medicine. 12(1):18. doi: 10.1186/s13073-020-0713-z
  2. Abelein, A., et al. (2020). High-yield Production of Amyloid-beta Peptide Enabled by a Customized Spider Silk Domain. Scientific Reports. 10(1):235. doi: 10.1038/s41598-019-57143-x
  3. Achilli, S., et al. (2020). TETRALEC, Artificial Tetrameric Lectins: A Tool to Screen Ligand and Pathogen Interactions. International Journal of Molecular Sciences. 21(15):19. doi: 10.3390/ijms21155290
  4. Aguilar, P. P., et al. (2020). Capture and purification of Human Immunodeficiency Virus-1 virus-like particles: Convective media vs porous beads. Journal of Chromatography A. 1627:461378. doi: 10.1016/j.chroma.2020.461378
  5. Albanese, P., et al. (2020). How paired PSII-LHCII supercomplexes mediate the stacking of plant thylakoid membranes unveiled by structural mass-spectrometry. Nature Communications. 11(1):1361. doi: 10.1038/s41467-020-15184-1
  6. Alleva, C., et al. (2020). Na+-dependent gate dynamics and electrostatic attraction ensure substrate coupling in glutamate transporters. Science Advances. 6(47):12. doi: 10.1126/sciadv.aba9854
  7. Andres, G., et al. (2020). The cryo-EM structure of African swine fever virus unravels a unique architecture comprising two icosahedral protein capsids and two lipoprotein membranes. Journal of Biological Chemistry. 295(1):1-12. doi: 10.1074/jbc.AC119.011196
  8. Antonaros, F., et al. (2020). Plasma metabolome and cognitive skills in Down syndrome. Scientific Reports. 10(1):10491. doi: 10.1038/s41598-020-67195-z
  9. Arias-Alpizar, G., et al. (2020). Light-triggered switching of liposome surface charge directs delivery of membrane impermeable payloads in vivo. Nature Communications. 11(1):3638. doi: 10.1038/s41467-020-17360-9
  10. Arragain, B., et al. (2020). Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes. Nature Communications. 11(1):3590. doi: 10.1038/s41467-020-17349-4
  11. Aumonier, S., et al. (2020). Millisecond time-resolved serial oscillation crystallography of a blue-light photoreceptor at a synchrotron. IUCrJ. 7(4):728-736. doi: 10.1107/s2052252520007411
  12. Ayala, I., et al. (2020). Asymmetric Synthesis of Methyl Specifically Labelled L-Threonine and Application to the NMR Studies of High Molecular Weight Proteins. ChemistrySelect. 5(17):5092-5098. doi: 10.1002/slct.202000827
  13. Barylski, J., et al. (2020). Analysis of Spounaviruses as a Case Study for the Overdue Reclassification of Tailed Phages. Systematic Biology. 69(1):110-123. doi: 10.1093/sysbio/syz036
  14. Basoglu, A., et al. (2020). NMR based serum metabolomics for monitoring newborn preterm calves' health. Japanese Journal of Veterinary Research. 68(2):105-115. doi: 10.14943/jjvr.68.2.105
  15. Basoglu, A., et al. (2020). Nuclear magnetic resonance (NMR)-based metabolome profile evaluation in dairy cows with and without displaced abomasum. Veterinary Quarterly. 40(1):1-15. doi: 10.1080/01652176.2019.1707907
  16. Basoglu, A., et al. (2020). NMR based serum extracts' metabolomics for evaluation of canine Ehrlichiosis. Japanese Journal of Veterinary Research. 68(4):227-236. doi: 10.14943/jjvr.68.4.227
  17. Belorusova, A. Y., et al. (2020). Molecular determinants of MED1 interaction with the DNA bound VDR-RXR heterodimer. Nucleic Acids Research. 48(19):11199-11213. doi: 10.1093/nar/gkaa775
  18. Belorusova, A. Y., et al. (2020). Structural Analysis of VDR Complex with ZK168281 Antagonist. Journal of Medicinal Chemistry. 63(17):9457-9463. doi: 10.1021/acs.jmedchem.0c00656
  19. Bertin, A., et al. (2020). Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation. Nature Communications. 11(1):2663. doi: 10.1038/s41467-020-16368-5
  20. Bertrand, Q., et al. (2020). Exolysin (ExlA) from Pseudomonas aeruginosa Punctures Holes into Target Membranes Using a Molten Globule Domain. Journal of Molecular Biology. 432(16):4466-4480. doi: 10.1016/j.jmb.2020.05.025
  21. Bhaskar, V., et al. (2020). Dynamics of uS19 C-Terminal Tail during the Translation Elongation Cycle in Human Ribosomes. Cell Reports. 31(1):107473. doi: 10.1016/j.celrep.2020.03.037
  22. Bhattarai, M., et al. (2020). Colloidal features of softwood galactoglucomannans-rich extract. Carbohydrate Polymers. 241:116368. doi: 10.1016/j.carbpol.2020.116368
  23. Bhattarai, M., et al. (2020). Time-dependent self-association of spruce galactoglucomannans depends on pH and mechanical shearing. Food Hydrocolloids. 102:12. doi: 10.1016/j.foodhyd.2019.105607
  24. Bonhoure, A., et al. (2020). Benchtop holdup assay for quantitative affinity-based analysis of sequence determinants of protein-motif interactions. Analytical Biochemistry. 603:17. doi: 10.1016/j.ab.2020.113772
  25. Boni, F., et al. (2020). Modulation of Guanylate Cyclase Activating Protein 1 (GCAP1) Dimeric Assembly by Ca2+ or Mg2+: Hints to Understand Protein Activity. Biomolecules. 10(10):17. doi: 10.3390/biom10101408
  26. Bonucci, A., et al. (2020). A combined NMR and EPR investigation on the effect of the disordered RGG regions in the structure and the activity of the RRM domain of FUS. Scientific Reports. 10(1):20956. doi: 10.1038/s41598-020-77899-x
  27. Bouillot, S., et al. (2020). Inflammasome activation byPseudomonas aeruginosa's ExlA pore-forming toxin is detrimental for the host. Cellular Microbiology. 22(11):e13251. doi: 10.1111/cmi.13251
  28. Brams, M., et al. (2020). Modulation of the Erwinia ligand-gated ion channel (ELIC) and the 5-HT3 receptor via a common vestibule site. eLife. 9:e51511. doi: 10.7554/eLife.51511
  29. Brillet, K., et al. (2020). Different views of the dynamic landscape covered by the 5 '-hairpin of the 7SK small nuclear RNA. RNA. 26(9):1184-1197. doi: 10.1261/rna.074955.120
  30. Bruno, F., et al. (2020). Multivariate Curve Resolution for 2D Solid-State NMR spectra. Analytical Chemistry. 92(6):4451-4458. doi: 10.1021/acs.analchem.9b05420
  31. Buckles, T. C., et al. (2020). The G-Protein Rab5A Activates VPS34 Complex II, a Class III PI3K, by a Dual Regulatory Mechanism. Biophysical Journal. 119(11):2205-2218. doi: 10.1016/j.bpj.2020.10.028
  32. Burt, A., et al. (2020). Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain. Nature Communications. 11(1):743. doi: 10.1038/s41467-020-14350-9
  33. Camacho-Zarco, A. R., et al. (2020). Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A. Nature Communications. 11(1):3656. doi: 10.1038/s41467-020-17407-x
  34. Camponeschi, F., et al. (2020). GLRX3 Acts as a 2Fe-2S Cluster Chaperone in the Cytosolic Iron- Sulfur Assembly Machinery Transferring 2Fe-2S Clusters to NUBP1. Journal of the American Chemical Society. 142(24):10794-10805. doi: 10.1021/jacs.0c02266
  35. Cantini, F., et al. (2020). H-1,C-13, and(15)N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b. Biomolecular NMR Assignments. 14(2):339-346. doi: 10.1007/s12104-020-09973-4
  36. Carrique, L., et al. (2020). Structure and catalytic regulation of Plasmodium falciparum IMP specific nucleotidase. Nature Communications. 11(1):3228. doi: 10.1038/s41467-020-17013-x
  37. Carter, S. D., et al. (2020). Ribosome-associated vesicles: A dynamic subcompartment of the endoplasmic reticulum in secretory cells. Science Advances. 6(14):eaay9572. doi: 10.1126/sciadv.aay9572
  38. Caveney, N. A., et al. (2020). Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa. Structure. 28(6):643-650.e5. doi: 10.1016/j.str.2020.03.012
  39. Cerofolini, L., et al. (2020). Orientation of immobilized antigens on common surfaces by a simple computational model: Exposition of SARS-CoV-2 Spike protein RBD epitopes. Biophysical Chemistry. 265:106441. doi: 10.1016/j.bpc.2020.106441
  40. Cerofolini, L., et al. (2020). Mixing A beta(1-40) and A beta(1-42) peptides generates unique amyloid fibrils. Chemical Communications. 56(62):8830-8833. doi: 10.1039/d0cc02463e
  41. Chatzikonstantinou, A. V., et al. (2020). The NMR tube bioreactor. In: Shukla, A. K., ed. Chemical and Synthetic Biology Approaches to Understand Cellular Functions - Pt C. London: Academic Press Ltd-Elsevier Science Ltd 2020:71-101. doi: 10.1016/bs.mie.2019.10.032
  42. Che, T., et al. (2020). Nanobody-enabled monitoring of kappa opioid receptor states. Nature Communications. 11(1):1145. doi: 10.1038/s41467-020-14889-7
  43. Chen, G. F., et al. (2020). Augmentation of Bri2 molecular chaperone activity against amyloid-beta reduces neurotoxicity in mouse hippocampus in vitro. Communications Biology. 3(1):32. doi: 10.1038/s42003-020-0757-z
  44. Chillon, I., et al. (2020). The molecular structure of long non-coding RNAs: emerging patterns and functional implications. Critical Reviews in Biochemistry and Molecular Biology. 55(6):662-690. doi: 10.1080/10409238.2020.1828259
  45. Ciambellotti, S., et al. (2020). Iron Biomineral Growth from the Initial Nucleation Seed in L-Ferritin. Chemistry - A European Journal. 26(26):5770-5773. doi: 10.1002/chem.202000064
  46. Cioce, A., et al. (2020). Rapid On-Chip Synthesis of Complex Glycomimetics from N-Glycan Scaffolds for Improved Lectin Targeting. Chemistry - A European Journal. 26(56):12809-12817. doi: 10.1002/chem.202000026
  47. Custers, R., et al. (2020). Discussions on the quality of antibodies are no reason to ban animal immunization. EMBO Reports. 21(12):e51761. doi: 10.15252/embr.202051761
  48. Cuveillier, C., et al. (2020). MAP6 is an intraluminal protein that induces neuronal microtubules to coil. Science Advances. 6(14):eaaz4344. doi: 10.1126/sciadv.aaz4344
  49. da Silva, V. M., et al. (2020). High-resolution structure of a modular hyperthermostable endo-beta-1,4-mannanase from Thermotoga petrophila: The ancillary immunoglobulin-like module is a thermostabilizing domain. Biochimica Et Biophysica Acta-Proteins and Proteomics. 1868(8):140437. doi: 10.1016/j.bbapap.2020.140437
  50. Dalzon, B., et al. (2020). Influences of Nanoparticles Characteristics on the Cellular Responses: The Example of Iron Oxide and Macrophages. Nanomaterials. 10(2):18. doi: 10.3390/nano10020266
  51. de la Cruz, N., et al. (2020). Influence of the reducing-end anomeric configuration of the Man(9)epitope on DC-SIGN recognition. Organic & Biomolecular Chemistry. 18(31):6086-6094. doi: 10.1039/d0ob01380c
  52. De, S., et al. (2020). Association of host protein VARICOSE with HCPro within a multiprotein complex is crucial for RNA silencing suppression, translation, encapsidation and systemic spread of potato virus A infection. PLoS Pathogens. 16(10). doi: 10.1371/journal.ppat.1008956
  53. de Wijn, R., et al. (2020). Monitoring the Production of High Diffraction-Quality Crystals of Two Enzymes in Real Time Using In Situ Dynamic Light Scattering. Crystals. 10(2). doi: 10.3390/cryst10020065
  54. De Zitter, E., et al. (2020). Mechanistic Investigations of Green mEos4b Reveal a Dynamic Long-Lived Dark State. Journal of the American Chemical Society. 142(25):10978-10988. doi: 10.1021/jacs.0c01880
  55. Decelle, J., et al. (2020). Subcellular Chemical Imaging: New Avenues in Cell Biology. Trends in Cell Biology. 30(3):173-188. doi: 10.1016/j.tcb.2019.12.007
  56. Dekoninck, K., et al. (2020). Defining the function of OmpA in the Rcs stress response. eLife. 9. doi: 10.7554/eLife.60861
  57. Delices, A., et al. (2020). Aqueous Synthesis of DNA-Functionalized Near-Infrared AgInS2/ZnS Core/Shell Quantum Dots. ACS Applied Materials & Interfaces. 12(39):44026-44038. doi: 10.1021/acsami.0c11337
  58. Demina, T. A., et al. (2020). Pleomorphic archaeal viruses: the familyPleolipoviridaeis expanding by seven new species. Archives of Virology. 165(11):2723-2731. doi: 10.1007/s00705-020-04689-1
  59. Denis, M., et al. (2020). The Photocatalyzed Thiol-ene reaction: A New Tag to Yield Fast, Selective and reversible Paramagnetic Tagging of Proteins. ChemPhysChem. 21(9):863-869. doi: 10.1002/cphc.202000071
  60. Di Mattia, T., et al. (2020). FFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts. EMBO Journal. 39(23):e104369. doi: 10.15252/embj.2019104369
  61. Domenichini, E., et al. (2020). Steric hindrances and spectral distributions affecting energy transfer rate: A comparative study on specifically designed donor-acceptor pairs. Dyes and Pigments. 174:9. doi: 10.1016/j.dyepig.2019.108010
  62. Dominguez-Rodriguez, P., et al. (2020). Second-Generation Dendrimers with Chondroitin Sulfate Type-E Disaccharides as Multivalent Ligands for Langerin. Biomacromolecules. 21(7):2726-2734. doi: 10.1021/acs.biomac.0c00476
  63. Donchet, A., et al. (2020). Differential Behaviours and Preferential Bindings of Influenza Nucleoproteins on Importins-alpha. Viruses. 12(8):16. doi: 10.3390/v12080834
  64. Dussert, F., et al. (2020). Toxicity to RAW264.7 Macrophages of Silica Nanoparticles and the E551 Food Additive, in Combination with Genotoxic Agents. Nanomaterials. 10(7):17. doi: 10.3390/nano10071418
  65. El Masri, R., et al. (2020). HS and Inflammation: A Potential Playground for the Sulfs? Frontiers in Immunology. 11:570. doi: 10.3389/fimmu.2020.00570
  66. Engelberg, Y., et al. (2020). The Human LL-37(17-29) antimicrobial peptide reveals a functional supramolecular structure. Nature Communications. 11(1):3894. doi: 10.1038/s41467-020-17736-x
  67. Erba, E. B., et al. (2020). Exploring the structure and dynamics of macromolecular complexes by native mass spectrometry. Journal of Proteomics. 222:103799. doi: 10.1016/j.jprot.2020.103799
  68. Fajardo, A. S., et al. (2020). Structural Insights into the Mechanism of the Radical SAM Carbide Synthase NifB, a Key Nitrogenase Cofactor Maturating Enzyme. Journal of the American Chemical Society. 142(25):11006-11012. doi: 10.1021/jacs.0c02243
  69. Fouet, G., et al. (2020). Headless C1q: a new molecular tool to decipher its collagen-like functions. FEBS Journal.12. doi: 10.1111/febs.15543
  70. Fouet, G., et al. (2020). Complement C1q Interacts With LRP1 Clusters II and IV Through a Site Close but Different From the Binding Site of Its C1r and C1s-Associated Proteases. Frontiers in Immunology. 11:583754. doi: 10.3389/fimmu.2020.583754
  71. Gallo, A., et al. (2020). H-1,C-13 and N-15 chemical shift assignments of the SUD domains of SARS-CoV-2 non-structural protein 3c: "the N-terminal domain-SUD-N". Biomolecular NMR Assignments.5. doi: 10.1007/s12104-020-09987-y
  72. Garcia, X., et al. (2020). Aggregates Dramatically Alter Fibrin Ultrastructure. Biophysical Journal. 118(1):172-181. doi: 10.1016/j.bpj.2019.10.034
  73. Gerard, F. C. A., et al. (2020). Vesicular Stomatitis Virus Phosphoprotein Dimerization Domain Is Dispensable for Virus Growth. Journal of Virology. 94(6):15. doi: 10.1128/jvi.01789-19
  74. Gilles, A., et al. (2020). Targeting the Human 80S Ribosome in Cancer: From Structure to Function and Drug Design for Innovative Adjuvant Therapeutic Strategies. Cells. 9(3):22. doi: 10.3390/cells9030629
  75. Glavier, M., et al. (2020). Antibiotic export by MexB multidrug efflux transporter is allosterically controlled by a MexA-OprM chaperone-like complex. Nature Communications. 11(1):4948. doi: 10.1038/s41467-020-18770-5
  76. Gogl, G., et al. (2020). Dual Specificity PDZ- and 14-3-3-Binding Motifs: A Structural and Interactomics Study. Structure. 28(7):747-759.e3. doi: 10.1016/j.str.2020.03.010
  77. Gormal, R. S., et al. (2020). Modular transient nanoclustering of activated beta 2-adrenergic receptors revealed by single-molecule tracking of conformation-specific nanobodies. Proceedings of the National Academy of Sciences of the United States of America. 117(48):30476-30487. doi: 10.1073/pnas.2007443117
  78. Guseva, S., et al. (2020). Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly. Science Advances. 6(14):11. doi: 10.1126/sciadv.aaz7095
  79. Guseva, S., et al. (2020). Structure, dynamics and phase separation of measles virus RNA replication machinery. Current Opinion in Virology. 41:59-67. doi: 10.1016/j.coviro.2020.05.006
  80. Gushchin, I., et al. (2020). Crystal Structure of a Proteolytic Fragment of the Sensor Histidine Kinase NarQ. Crystals. 10(3):9. doi: 10.3390/cryst10030149
  81. Gushchin, I., et al. (2020). Sensor Histidine Kinase NarQ Activates via Helical Rotation, Diagonal Scissoring, and Eventually Piston-Like Shifts. International Journal of Molecular Sciences. 21(9):18. doi: 10.3390/ijms21093110
  82. Hennicke, J., et al. (2020). Transient pentameric IgM fulfill biological function-Effect of expression host and transfection on IgM properties. PLoS One. 15(3):e0229992. doi: 10.1371/journal.pone.0229992
  83. Hoang, M. D., et al. (2020). Self-assembled Polydiacetylene Nanoribbons for Semi-heterogeneous and Enantioselective Organocatalysis of Aldol Reactions in Water. ChemCatChem. 12(4):1156-1160. doi: 10.1002/cctc.201901960
  84. Hograindleur, M. A., et al. (2020). Binding Mechanism Elucidation of the Acute Respiratory Disease Causing Agent Adenovirus of Serotype 7 to Desmoglein-2. Viruses. 12(10):15. doi: 10.3390/v12101075
  85. Hosek, T., et al. (2020). Structural features of the interaction of MapZ with FtsZ and membranes in Streptococcus pneumoniae. Scientific Reports. 10(1):4051. doi: 10.1038/s41598-020-61036-9
  86. Huang, K. Y. A., et al. (2020). Structural and functional analysis of protective antibodies targeting the threefold plateau of enterovirus 71. Nature Communications. 11(1):5253. doi: 10.1038/s41467-020-19013-3
  87. Humbert, N., et al. (2020). (Thia)calixarenephosphonic Acids as Potent Inhibitors of the Nucleic Acid Chaperone Activity of the HIV-1 Nucleocapsid Protein with a New Binding Mode and Multitarget Antiviral Activity. ACS Infectious Diseases. 6(4):687-702. doi: 10.1021/acsinfecdis.9b00290
  88. Huo, J., et al. (2020). Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2. Nature Structural & Molecular Biology. 27(9):846-854. doi: 10.1038/s41594-020-0469-6
  89. Huo, J. D., et al. (2020). Neutralization of SARS-CoV-2 by Destruction of the Prefusion Spike. Cell Host & Microbe. 28(3):445-454.e6. doi: 10.1016/j.chom.2020.06.010
  90. Invernici, M., et al. (2020). Measuring transverse relaxation in highly paramagnetic systems. Journal of Biomolecular NMR. 74(8-9):431-442. doi: 10.1007/s10858-020-00334-w
  91. Jensen, M. R., et al. (2020). Structural Description of the Nipah Virus Phosphoprotein and Its Interaction with STAT1. Biophysical Journal. 118(10):2470-2488. doi: 10.1016/j.bpj.2020.04.010
  92. Jessop, M., et al. (2020). Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex. Communications Biology. 3(1):46. doi: 10.1038/s42003-020-0772-0
  93. Jiang, T., et al. (2020). Tracking Crystallophore Nucleating Properties: Setting Up a Database for Statistical Analysis. Crystal Growth & Design. 20(8):5322-5329. doi: 10.1021/acs.cgd.0c00556
  94. Jung, J. H., et al. (2020). A prion-like domain in ELF3 functions as a thermosensor in Arabidopsis. Nature. 585(7824):256-260. doi: 10.1038/s41586-020-2644-7
  95. Kalke, K., et al. (2020). Herpes Simplex Virus Type 1 Clinical Isolates Respond to UL29-Targeted siRNA Swarm Treatment Independent of Their Acyclovir Sensitivity. Viruses. 12(12):1434. doi: 10.3390/v12121434
  96. Kanja, M., et al. (2020). NKNK: a New Essential Motif in the C-Terminal Domain of HIV-1 Group M Integrases. Journal of Virology. 94(20):23. doi: 10.1128/jvi.01035-20
  97. Karki, S., et al. (2020). Structural basis of SALM3 dimerization and synaptic adhesion complex formation with PTP sigma. Scientific Reports. 10(1):11557. doi: 10.1038/s41598-020-68502-4
  98. Kobera, L., et al. (2020). Gallium Species Incorporated into MOF Structure: Insight into the Formation of a 3D Polycrystalline Gallium-Imidazole Framework. Inorganic Chemistry. 59(19):13933-13941. doi: 10.1021/acs.inorgchem.0c01563
  99. Kosol, S., et al. (2020). Interaction between the scaffold proteins CBP by IQGAP1 provides an interface between gene expression and cytoskeletal activity. Scientific Reports. 10(1):5753. doi: 10.1038/s41598-020-62069-w
  100. Kovalev, K., et al. (2020). Molecular mechanism of light-driven sodium pumping. Nature Communications. 11(1):2137. doi: 10.1038/s41467-020-16032-y
  101. Kovalev, K., et al. (2020). High-resolution structural insights into the heliorhodopsin family. Proceedings of the National Academy of Sciences of the United States of America. 117(8):4131-4141. doi: 10.1073/pnas.1915888117
  102. Kumar, H., et al. (2020). Diversity in kinetics correlated with structure in nano body-stabilized LacY. PLoS One. 15(5):e0232846. doi: 10.1371/journal.pone.0232846
  103. Lalli, D., et al. (2020). Distal Unfolding of Ferricytochrome c Induced by the F82K Mutation. International Journal of Molecular Sciences. 21(6):11. doi: 10.3390/ijms21062134
  104. Lang, L., et al. (2020). Solution of a Puzzle: High-Level Quantum-Chemical Treatment of Pseudocontact Chemical Shifts Confirms Classic Semiempirical Theory. Journal of Physical Chemistry Letters. 11(20):8735-8744. doi: 10.1021/acs.jpclett.0c02462
  105. Laurinmaki, P., et al. (2020). Structure of Nora virus at 2.7 angstrom resolution and implications for receptor binding, capsid stability and taxonomy. Scientific Reports. 10(1):19675. doi: 10.1038/s41598-020-76613-1
  106. le Maire, A., et al. (2020). Two Novel Cases of Resistance to Thyroid Hormone Due to THRA Mutation. Thyroid. 30(8):1217-1221. doi: 10.1089/thy.2019.0602
  107. Leemans, M., et al. (2020). Allosteric modulation of the GTPase activity of a bacterial LRRK2 homolog by conformation-specific Nanobodies. Biochemical Journal. 477(7):1203-1218. doi: 10.1042/bcj20190843
  108. Levanova, A. A., et al. (2020). Enzymatically synthesized 2 '-fluoro-modified Dicer-substrate siRNA swarms against herpes simplex virus demonstrate enhanced antiviral efficacy and low cytotoxicity. Antiviral Research. 182:104916. doi: 10.1016/j.antiviral.2020.104916
  109. Li, R. J. E., et al. (2020). Targeting of the C-Type Lectin Receptor Langerin Using Bifunctional Mannosylated Antigens. Frontiers in Cell and Developmental Biology. 8:556. doi: 10.3389/fcell.2020.00556
  110. Liebers, M., et al. (2020). Nucleo-plastidic PAP8/pTAC6 couples chloroplast formation with photomorphogenesis. EMBO Journal. 39(33):e104941. doi: 10.15252/embj.2020104941
  111. Liebschner, D., et al. (2020). Implementation of the riding hydrogen model in CCTBX to support the next generation of X-ray and neutron joint refinement in Phenix. In: Moody, P. C. E., ed. Neutron Crystallography in Structural Biology. London: Academic Press Ltd-Elsevier Science Ltd 2020:177-199. doi: 10.1016/bs.mie.2020.01.007
  112. Linares, R., et al. (2020). Structure, function and assembly of the long, flexible tail of siphophages. Current Opinion in Virology. 45:34-42. doi: 10.1016/j.coviro.2020.06.010
  113. Liu, D. R., et al. (2020). Endocytosis of BRASSINOSTEROID INSENSITIVE1 Is Partly Driven by a Canonical Tyr-Based Motif. Plant Cell. 32(11):3598-3612. doi: 10.1105/tpc.20.00384
  114. Liu, Y., et al. (2020). Expression and purification of the extracellular domain of wild-type humanRET and the dimeric oncogenic mutant C634R. International Journal of Biological Macromolecules. 164:1621-1630. doi: 10.1016/j.ijbiomac.2020.07.290
  115. Lopez-Perrote, A., et al. (2020). Regulation of RUVBL1-RUVBL2 AAA-ATPases by the nonsense-mediated mRNA decay factor DHX34, as evidenced by Cryo-EM. eLife. 9. doi: 10.7554/eLife.63042
  116. Lotz, C., et al. (2020). The interplay between DNA topoisomerase 2α post-translational modifications and drug resistance. Cancer Drug Resistance. (3):149-160. doi: 10.20517/cdr.2019.114
  117. Luchinat, E., et al. (2020). Real-Time Quantitative In-Cell NMR: Ligand Binding and Protein Oxidation Monitored in Human Cells Using Multivariate Curve Resolution. Analytical Chemistry. 92(14):9997-10006. doi: 10.1021/acs.analchem.0c01677
  118. Luchinat, E., et al. (2020). Drug Screening in Human Cells by NMR Spectroscopy Allows the Early Assessment of Drug Potency. Angewandte Chemie-International Edition. 59(16):6535-6539. doi: 10.1002/anie.201913436
  119. Luchinat, E., et al. (2020). Intracellular Binding/Unbinding Kinetics of Approved Drugs to Carbonic Anhydrase II Observed by in-Cell NMR. ACS Chemical Biology. 15(10):2792-2800. doi: 10.1021/acschembio.0c00590
  120. Mahieu, E., et al. (2020). Observing Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering. Biophysical Journal. 119(2):375-388. doi: 10.1016/j.bpj.2020.06.015
  121. Maione, V., et al. (2020). CIAO3 protein forms a stable ternary complex with two key players of the human cytosolic iron-sulfur cluster assembly machinery. Journal of Biological Inorganic Chemistry. 25(3):501-508. doi: 10.1007/s00775-020-01778-z
  122. Manigrasso, J., et al. (2020). Visualizing group II intron dynamics between the first and second steps of splicing. Nature Communications. 11(1):2837. doi: 10.1038/s41467-020-16741-4
  123. Mantynen, S., et al. (2020). ICTV Virus Taxonomy Profile: Finnlakeviridae. Journal of General Virology. 101(9):894-895. doi: 10.1099/jgv.0.001488
  124. Marchioni, M., et al. (2020). Safer-by-design biocides made of tri-thiol bridged silver nanoparticle assemblies. Nanoscale Horizons. 5(3):507-513. doi: 10.1039/c9nh00286c
  125. Martinelli, L., et al. (2020). Structural analysis of the LDL receptor-interacting FERM domain in the E3 ubiquitin ligase IDOL reveals an obscured substrate-binding site. Journal of Biological Chemistry. 295(39):13570-13583. doi: 10.1074/jbc.RA120.014349
  126. Martínez, M., et al. (2020). Integration of Cryo-EM Model Building Software in Scipion. Journal of Chemical Information and Modeling. 60(5):2533-2540. doi: 10.1021/acs.jcim.9b01032
  127. Mateos, B., et al. (2020). The Ambivalent Role of Proline Residues in an Intrinsically Disordered Protein: From Disorder Promoters to Compaction Facilitators. Journal of Molecular Biology. 432(9):3093-3111. doi: 10.1016/j.jmb.2019.11.015
  128. Mavreas, K. F., et al. (2020). Synthesis, Kinetic and Conformational Studies of 2-Substituted-5-(beta-d-glucopyranosyl)-pyrimidin-4-ones as Potential Inhibitors of Glycogen Phosphorylase. Molecules. 25(22):17. doi: 10.3390/molecules25225463
  129. McClelland, L. J., et al. (2020). Structure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to G alpha i1. Nature Communications. 11(1):1077. doi: 10.1038/s41467-020-14943-4
  130. McLeod, S. M., et al. (2020). Maximizing Magnetic Resonance Contrast in Gd(III) Nanoconjugates: Investigation of Proton Relaxation in Zirconium Metal-Organic Frameworks. ACS Applied Materials & Interfaces. 12(37):41157-41166. doi: 10.1021/acsami.0c13571
  131. Melero, R., et al. (2020). Continuous flexibility analysis of SARS-CoV-2 spike prefusion structures. IUCrJ. 7(6):1059-1069. doi: 10.1107/s2052252520012725
  132. Meoni, G., et al. (2020). Nuclear Magnetic Resonance-Based Metabolomic Comparison of Breast Milk and Organic and Traditional Formula Milk Brands for Infants and Toddlers. OMICS-a Journal of Integrative Biology. 24(7):424-436. doi: 10.1089/omi.2019.0125
  133. Montanari, R., et al. (2020). Insights into PPAR gamma Phosphorylation and Its Inhibition Mechanism. Journal of Medicinal Chemistry. 63(9):4811-4823. doi: 10.1021/acs.jmedchem.0c00048
  134. Moura, E. C. C. M., et al. (2020). Thanatin Impairs Lipopolysaccharide Transport Complex Assembly by Targeting LptC-LptA Interaction and Decreasing LptA Stability. Frontiers in Microbiology. 11:909. doi: 10.3389/fmicb.2020.00909
  135. Murrali, M. G., et al. (2020). Adenoviral E1A Exploits Flexibility and Disorder to Target Cellular Proteins. Biomolecules. 10(11). doi: 10.3390/biom10111541
  136. Nasta, V., et al. (2020). A pathway for assembling 4Fe-4S (2+) clusters in mitochondrial iron-sulfur protein biogenesis. FEBS Journal. 287(11):2312-2327. doi: 10.1111/febs.15140
  137. Neumann, E., et al. (2020). 3D structure of three jumbo phage heads. Journal of General Virology. 101(11):1219-1226. doi: 10.1099/jgv.0.001487
  138. Orlov, I., et al. (2020). Structural basis of nanobody recognition of grapevine fanleaf virus and of virus resistance loss. Proceedings of the National Academy of Sciences of the United States of America. 117(20):10848-10855. doi: 10.1073/pnas.1913681117
  139. Osz, J., et al. (2020). Structural basis for DNA recognition and allosteric control of the retinoic acid receptors RAR-RXR. Nucleic Acids Research. 48(17):9969-9985. doi: 10.1093/nar/gkaa697
  140. Ouaguia, L., et al. (2020). Hepatitis B virus exploits C-type lectin receptors to hijack cDC1s, cDC2s and pDCs. Clinical & Translational Immunology. 9(12):e1208. doi: 10.1002/cti2.1208
  141. Papai, G., et al. (2020). Structure of SAGA and mechanism of TBP deposition on gene promoters. Nature. 577(7792):711-716. doi: 10.1038/s41586-020-1944-2
  142. Paris, C., et al. (2020). CO2 Hydrogenation to Methanol with Ga- and Zn-Doped Mesoporous Cu/SiO2 Catalysts Prepared by the Aerosol-Assisted Sol-Gel Process. ChemSusChem. 13(23):6409-6417. doi: 10.1002/cssc.202001951
  143. Pazos, M., et al. (2020). SPOR Proteins Are Required for Functionality of Class A Penicillin-Binding Proteins in Escherichia coli. mBio. 11(6):16. doi: 10.1128/mBio.02796-20
  144. Peissert, S., et al. (2020). In TFIIH the Arch domain of XPD is mechanistically essential for transcription and DNA repair. Nature Communications. 11(1):1667. doi: 10.1038/s41467-020-15241-9
  145. Peluso-Iltis, C., et al. (2020). DNA recognition by retinoic acid nuclear receptors. In: Pohl, E., ed. Retinoid Signaling Pathways. London: Academic Press Ltd-Elsevier Science Ltd 2020:235-260. doi: 10.1016/bs.mie.2020.03.001
  146. Perrin, E., et al. (2020). Diauxie and co-utilization of carbon sources can coexist during bacterial growth in nutritionally complex environments. Nature Communications. 11(1):3135. doi: 10.1038/s41467-020-16872-8
  147. Piccioli, M. (2020). Paramagnetic NMR Spectroscopy Is a Tool to Address Reactivity, Structure, and Protein-Protein Interactions of Metalloproteins: The Case of Iron-Sulfur Proteins. Magnetochemistry. 6(4):21. doi: 10.3390/magnetochemistry6040046
  148. Polykretis, P., et al. (2020). Methylglyoxal interaction with superoxide dismutase 1. Redox Biology. 30:101421. doi: 10.1016/j.redox.2019.101421
  149. Pontoriero, L., et al. (2020). Monitoring the Interaction of alpha-Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments. Angew Chem Int Ed Engl. 59(42):18537-18545. doi: 10.1002/anie.202008079
  150. Porkolab, V., et al. (2020). Development of C-type lectin-oriented surfaces for high avidity glycoconjugates: towards mimicking multivalent interactions on the cell surface. Organic & Biomolecular Chemistry. 18(25):4763-4772. doi: 10.1039/d0ob00781a
  151. Pounot, K., et al. (2020). Tracking Internal and Global Diffusive Dynamics During Protein Aggregation by High-Resolution Neutron Spectroscopy. Journal of Physical Chemistry Letters. 11(15):6299-6304. doi: 10.1021/acs.jpclett.0c01530
  152. Puglisi, R., et al. (2020). A Guide to Native Mass Spectrometry to determine complex interactomes of molecular machines. FEBS Journal. 287(12):2428-2439. doi: 10.1111/febs.15281
  153. Ramirez-Aportela, E., et al. (2020). Automatic local resolution-based sharpening of cryo-EM maps. Bioinformatics. 36(3):765-772. doi: 10.1093/bioinformatics/btz671
  154. Rampelt, H., et al. (2020). The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments. BMC Biology. 18(1):2. doi: 10.1186/s12915-019-0733-6
  155. Rasmussen, K. K., et al. (2020). Revealing the mechanism of repressor inactivation during switching of a temperate bacteriophage. Proceedings of the National Academy of Sciences of the United States of America. 117(34):20576-20585. doi: 10.1073/pnas.2005218117
  156. Rathner, P., et al. (2020). Interhelical interactions within the STIM1 CC1 domain modulate CRAC channel activation. Nature Chemical Biology. (2):196-204. doi: 10.1038/s41589-020-00672-8
  157. Ravera, E., et al. (2020). Different flavors of diffusion in paramagnetic systems: Unexpected NMR signal intensity and relaxation enhancements. Journal of Magnetic Resonance Open. 2-3. doi: 10.1016/j.jmro.2020.100003
  158. Salomon, E., et al. (2020). Aminobenzosuberone derivatives as PfA-M1 inhibitors: Molecular recognition and antiplasmodial evaluation. Bioorganic Chemistry. 98:103750. doi: 10.1016/j.bioorg.2020.103750
  159. Sanchez-Garcia, R., et al. (2020). MicrographCleaner: A python package for cryo-EM micrograph cleaning using deep learning. Journal of Structural Biology. 210(3):107498. doi: 10.1016/j.jsb.2020.107498
  160. Schiavina, M., et al. (2020). Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS. Scientific Reports. 10(1):19574. doi: 10.1038/s41598-020-76522-3
  161. Schirò, A., et al. (2020). On the complementarity of X-ray and NMR data. Journal of Structural Biology: X. 4:100019. doi: 10.1016/j.yjsbx.2020.100019
  162. Seifert, M., et al. (2020). Temperature controlled high-throughput magnetic tweezers show striking difference in activation energies of replicating viral RNA-dependent RNA polymerases. Nucleic Acids Research. 48(10):5591-5602. doi: 10.1093/nar/gkaa233
  163. Selegato, D. M., et al. (2020). Comparison of Different Reweighting Approaches for the Calculation of Conformational Variability of Macromolecules from Molecular Simulations. ChemPhysChem. 22(1):127-138. doi: 10.1002/cphc.202000714
  164. Senarisoy, M., et al. (2020). Forster Resonance Energy Transfer Based Biosensor for Targeting the hNTH1-YB1 Interface as a Potential Anticancer Drug Target. ACS Chemical Biology. 15(4):990-1003. doi: 10.1021/acschembio.9b01023
  165. Setyawati, I., et al. (2020). In vitro reconstitution of dynamically interacting integral membrane subunits of energy-coupling factor transporters. eLife. 9. doi: 10.7554/eLife.64389
  166. Sharma, V. R., et al. (2020). Canalicular domain structure and function in matrix-free hepatic spheroids. Biomaterials Science. 8(1):485-496. doi: 10.1039/c9bm01143a
  167. Shrestha, A., et al. (2020). Integrated Proteo-Transcriptomic Analyses Reveal Insights into Regulation of Pollen Development Stages and Dynamics of Cellular Response to Apple Fruit Crinkle Viroid (AFCVd)-Infection in Nicotiana tabacum. International Journal of Molecular Sciences. 21(22):24. doi: 10.3390/ijms21228700
  168. Siebert, C., et al. (2020). Physicochemical Evidence that Francisella FupA and FupB Proteins Are Porins. International Journal of Molecular Sciences. 21(15):12. doi: 10.3390/ijms21155496
  169. Silva, C. S., et al. (2020). Molecular mechanisms of Evening Complex activity in Arabidopsis. Proceedings of the National Academy of Sciences of the United States of America. 117(12):6901-6909. doi: 10.1073/pnas.1920972117
  170. Silva, Y. R. O., et al. (2020). Bacterial secretins: Mechanisms of assembly and membrane targeting. Protein Science. 29(4):893-904. doi: 10.1002/pro.3835
  171. Siren, S., et al. (2020). Candida antarctica Lipase A-Based Enantiorecognition of a Highly Strained 4-Dibenzocyclooctynol (DIBO) Used for PET Imaging. Molecules. 25(4):12. doi: 10.3390/molecules25040879
  172. Skalova, T., et al. (2020). Disruption of the dimerization interface of the sensing domain in the dimeric heme-based oxygen sensor AfGcHK abolishes bacterial signal transduction. Journal of Biological Chemistry. 295(6):1587-1597. doi: 10.1074/jbc.RA119.011574
  173. Skorepa, O., et al. (2020). Natural Killer Cell Activation Receptor NKp30 Oligomerization Depends on ItsN-Glycosylation. Cancers. 12(7):24. doi: 10.3390/cancers12071998
  174. Sorzano, C. O. S., et al. (2020). Improvements on marker-free images alignment for electron tomography,. Journal of Structural Biology: X. 4:100037. doi: 10.1016/j.yjsbx.2020.100037
  175. Sowa, S. T., et al. (2020). A FRET-based high-throughput screening platform for the discovery of chemical probes targeting the scaffolding functions of human tankyrases. Scientific Reports. 10(1):12357. doi: 10.1038/s41598-020-69229-y
  176. Spano, M., et al. (2020). Bacterial Diversity in the Asphalt Concrete Lining of the Upper Water Reservoir of a Pumped-Storage Scheme. Water. 12(11):15. doi: 10.3390/w12113045
  177. Spehner, D., et al. (2020). Cryo-FIB-SEM as a promising tool for localizing proteins in 3D. Journal of Structural Biology. 211(1):107528. doi: 10.1016/j.jsb.2020.107528
  178. Sridhar, S., et al. (2020). Crystallographic binding studies of rat peroxisomal multifunctional enzyme type 1 with 3-ketodecanoyl-CoA: capturing active and inactive states of its hydratase and dehydrogenase catalytic sites. Acta Crystallographica Section D-Structural Biology. 76(12):1256-1269. doi: 10.1107/s2059798320013819
  179. Stevanato, G., et al. (2020). Open and Closed Radicals: Local Geometry around Unpaired Electrons Governs Magic-Angle Spinning Dynamic Nuclear Polarization Performance. Journal of the American Chemical Society. 142(39):16587-16599. doi: 10.1021/jacs.0c04911
  180. Strelak, D., et al. (2020). FlexAlign: An Accurate and Fast Algorithm for Movie Alignment in Cryo-Electron Microscopy. Electronics. 9(6):25. doi: 10.3390/electronics9061040
  181. Suarez, V. T., et al. (2020). Nuclear translocation of silver ions and hepatocyte nuclear receptor impairment upon exposure to silver nanoparticles. Environmental Science-Nano. 7(5):1373-1387. doi: 10.1039/c9en01348b
  182. Sucec, I., et al. (2020). Structural basis of client specificity in mitochondrial membrane-protein chaperones. Science Advances. 6(51):15. doi: 10.1126/sciadv.abd0263
  183. Sutton, G., et al. (2020). Assembly intermediates of orthoreovirus captured in the cell. Nature Communications. 11(1):4445. doi: 10.1038/s41467-020-18243-9
  184. Swale, C., et al. (2020). X-ray Structure of the Human Karyopherin RanBP5, an Essential Factor for Influenza Polymerase Nuclear Trafficking. Journal of Molecular Biology. 432(10):3353-3359. doi: 10.1016/j.jmb.2020.03.021
  185. Talsma, D. T., et al. (2020). MASP-2 Is a Heparin-Binding Protease, Identification of Blocking Oligosaccharides. Frontiers in Immunology. 11:732. doi: 10.3389/fimmu.2020.00732
  186. Tan, Y. Z., et al. (2020). Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis. Nature Communications. 11(1):3396. doi: 10.1038/s41467-020-17202-8
  187. Tayeb-Fligelman, E., et al. (2020). Staphylococcus aureus PSM alpha 3 Cross-alpha Fibril Polymorphism and Determinants of Cytotoxicity. Structure. 28(3):301-313.e6. doi: 10.1016/j.str.2019.12.006
  188. Tetreau, G., et al. (2020). Serial femtosecond crystallography on in vivo-grown crystals drives elucidation of mosquitocidal Cyt1Aa bioactivation cascade. Nature Communications. 11(1):1153. doi: 10.1038/s41467-020-14894-w
  189. Torner, R., et al. (2020). Spectral editing of intra- and inter-chain methyl-methyl NOEs in protein complexes. Journal of Biomolecular NMR. 74(1):83-94. doi: 10.1007/s10858-019-00293-x
  190. Torres, A., et al. (2020). How Reversible Are the Effects of Fumed Silica on Macrophages? A Proteomics-Informed View. Nanomaterials. 10(10):17. doi: 10.3390/nano10101939
  191. Trindade, I. B., et al. (2020). (1)H, (13)C and (15)N assignment of the paramagnetic high potential iron-sulfur protein (HiPIP) PioC from Rhodopseudomonas palustris TIE-1. Biomolecular NMR Assignments. 14(2):211-215. doi: 10.1007/s12104-020-09947-6
  192. Trindade, I. B., et al. (2020). PRE-driven protein NMR structures: an alternative approach in highly paramagnetic systems. FEBS Journal.14. doi: 10.1111/febs.15615
  193. Uchański, T., et al. (2020). Nanobodies to study protein conformational states. Current Opinion in Structural Biology. 60:117-123. doi: 10.1016/j.sbi.2020.01.003
  194. Urbanek, A., et al. (2020). Flanking Regions Determine the Structure of the Poly-Glutamine in Huntingtin through Mechanisms Common among Glutamine-Rich Human Proteins. Structure. 28(7):733-746.e5. doi: 10.1016/j.str.2020.04.008
  195. Uroda, T., et al. (2020). Visualizing the functional 3D shape and topography of long noncoding RNAs by single-particle atomic force microscopy and in-solution hydrodynamic techniques. Nature Protocols. 15(6):2107-2139. doi: 10.1038/s41596-020-0323-7
  196. Usachev, K. S., et al. (2020). Dimerization of long hibernation promoting factor from Staphylococcus aureus: Structural analysis and biochemical characterization. Journal of Structural Biology. 209(1):107408. doi: 10.1016/j.jsb.2019.107408
  197. Vallet, A., et al. (2020). ssNMRlib: a comprehensive library and tool box for acquisition of solid-state nuclear magnetic resonance experiments on Bruker spectrometers. Magnetic Resonance. 1(2):331-345. doi: 10.5194/mr-1-331-2020
  198. van Kruijsbergen, I., et al. (2020). Strategy for Development of Site-Specific Ubiquitin Antibodies. Frontiers in Chemistry. 8:111. doi: 10.3389/fchem.2020.00111
  199. Vauclare, P., et al. (2020). Surviving salt fluctuations: stress and recovery in Halobacterium salinarum, an extreme halophilic Archaeon. Scientific Reports. 10(1):3298. doi: 10.1038/s41598-020-59681-1
  200. Vermot, A., et al. (2020). Interdomain Flexibility within NADPH Oxidase Suggested by SANS Using LMNG Stealth Carrier. Biophysical Journal. 119(3):605-618. doi: 10.1016/j.bpj.2020.06.025
  201. Vignoli, A., et al. (2020). Effect of Estrogen Receptor Status on Circulatory Immune and Metabolomics Profiles of HER2-Positive Breast Cancer Patients Enrolled for Neoadjuvant Targeted Chemotherapy. Cancers. 12(2):16. doi: 10.3390/cancers12020314
  202. Vignoli, A., et al. (2020). Fingerprinting Alzheimer's Disease by H-1 Nuclear Magnetic Resonance Spectroscopy of Cerebrospinal Fluid. Journal of Proteome Research. 19(4):1696-1705. doi: 10.1021/acs.jproteome.9b00850
  203. Vignoli, A., et al. (2020). NMR-Based Metabolomics for the Assessment of Inhaled Pharmacotherapy in Chronic Obstructive Pulmonary Disease Patients. Journal of Proteome Research. 19(1):64-74. doi: 10.1021/acs.jproteome.9b00345
  204. Vignoli, A., et al. (2020). Differential Network Analysis Reveals Metabolic Determinants Associated with Mortality in Acute Myocardial Infarction Patients and Suggests Potential Mechanisms Underlying Different Clinical Scores Used To Predict Death. Journal of Proteome Research. 19(2):949-961. doi: 10.1021/acs.jproteome.9b00779
  205. Vilas, J. L., et al. (2020). Measuring local-directional resolution and local anisotropy in cryo-EM maps. Nature Communications. 11(1):55. doi: 10.1038/s41467-019-13742-w
  206. Vilas, J. L., et al. (2020). Re-examining the spectra of macromolecules. Current practice of spectral quasi B-factor flattening. Journal of Structural Biology. 209(3):107447. doi: 10.1016/j.jsb.2020.107447
  207. Vrettos, E. I., et al. (2020). Single Peptide Backbone Surrogate Mutations to Regulate Angiotensin GPCR Subtype Selectivity. Chemistry. 26(47):10690-10694. doi: 10.1002/chem.202000924
  208. Wagemans, J., et al. (2020). Structural Analysis of Jumbo Coliphage phAPEC6. International Journal of Molecular Sciences. 21(9):13. doi: 10.3390/ijms21093119
  209. Waldie, S., et al. (2020). Lipoprotein ability to exchange and remove lipids from model membranes as a function of fatty acid saturation and presence of cholesterol. Biochimica Et Biophysica Acta-Molecular and Cell Biology of Lipids. 1865(10):158769. doi: 10.1016/j.bbalip.2020.158769
  210. Wandi, B. N., et al. (2020). Evolution-guided engineering of non-heme iron enzymes involved in nogalamycin biosynthesis. FEBS Journal. 287(14):2998-3011. doi: 10.1111/febs.15192
  211. Wandzik, J. M., et al. (2020). A Structure-Based Model for the Complete Transcription Cycle of Influenza Polymerase. Cell. 181(4):877-893.e21. doi: 10.1016/j.cell.2020.03.061
  212. Wazir, S., et al. (2020). Multiple crystal forms of human MacroD2. Acta Crystallographica Section F-Structural Biology Communications. 76(10):477-482. doi: 10.1107/s2053230x20011309
  213. Webster, M. W., et al. (2020). Structural basis of transcription-translation coupling and collision in bacteria. Science. 369(6509):1355-1359. doi: 10.1126/science.abb5036
  214. Wicker-Planquart, C., et al. (2020). Molecular and Cellular Interactions of Scavenger Receptor SR-F1 With Complement C1q Provide Insights Into Its Role in the Clearance of Apoptotic Cells. Frontiers in Immunology. 11:544. doi: 10.3389/fimmu.2020.00544
  215. Wodak, S. J., et al. (2020). Modeling protein interactions and complexes in CAPRI: Seventh CAPRI evaluation meeting, April 3-5 EMBL-EBI, Hinxton, UK. Proteins. 88(8):913-915. doi: 10.1002/prot.25883
  216. Woodhouse, J., et al. (2020). Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy. Nature Communications. 11(1):741. doi: 10.1038/s41467-020-14537-0
  217. Zabelskii, D., et al. (2020). Viral rhodopsins 1 are an unique family of light-gated cation channels. Nature Communications. 11(1):5707. doi: 10.1038/s41467-020-19457-7
  218. Zarate-Potes, A., et al. (2020). The C.elegans GATA transcription factorelt-2 mediates distinct transcriptional responses and opposite infection outcomes towards different Bacillus thuringiensis strains. PLoS Pathogens. 16(9):e1008826. doi: 10.1371/journal.ppat.1008826
  219. Zarkadas, E., et al. (2020). The Binding of Palonosetron and Other Antiemetic Drugs to the Serotonin 5-HT3 Receptor. Structure. 28(10):1131-1140.e4. doi: 10.1016/j.str.2020.07.004
  220. Zarzecka, U., et al. (2020). Functional analysis and cryo-electron microscopy of Campylobacter jejuni serine protease HtrA. Gut Microbes. 12(1):1-16. doi: 10.1080/19490976.2020.1810532
  221. Zhao, Y. G., et al. (2020). Caffeine inhibits Notum activity by binding at the catalytic pocket. Communications Biology. 3(1):235. doi: 10.1038/s42003-020-01286-5
  222. Zhao, Y. G., et al. (2020). Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10. Nature Communications. 11(1):38. doi: 10.1038/s41467-019-13936-2
  223. Zheng, M., et al. (2020). Including crystallographic symmetry in quantum-based refinement: Q|R#2. Acta Crystallographica Section D-Structural Biology. 76:41-50. doi: 10.1107/s2059798319015122
  224. Zhou, D. R. N., et al. (2020). Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient. Nature Structural & Molecular Biology. 27(10):950-958. doi: 10.1038/s41594-020-0480-y
  225. Zinn, T., et al. (2020). Phoretic dynamics of colloids in a phase separating critical liquid mixture. Physical Review Research. 2(3):13. doi: 10.1103/PhysRevResearch.2.033177

2019

  1. Abdelkareem, M., et al. (2019). Structural Basis of Transcription: RNA Polymerase Backtracking and Its Reactivation. Molecular Cell. 75(2):298-309.e4. doi: 10.1016/j.molcel.2019.04.029
  2. Abdelnabi, R., et al. (2019). A novel druggable interprotomer pocket in the capsid of rhino- and enteroviruses. PLOS Biology. 17(6):17. doi: 10.1371/journal.pbio.3000281
  3. Adamski, W., et al. (2019). A Unified Description of Intrinsically Disordered Protein Dynamics under Physiological Conditions Using NMR Spectroscopy. Journal of the American Chemical Society. 141(44):17817-17829. doi: 10.1021/jacs.9b09002
  4. Aguilar, P. P., et al. (2019). Polymer-grafted chromatography media for the purification of enveloped virus-like particles, exemplified with HIV-1 gag VLP. Vaccine. 37(47):7070-7080. doi: 10.1016/j.vaccine.2019.07.001
  5. Alfano, M., et al. (2019). A Solvent-Exposed Cysteine Forms a Peculiar Ni-II-Binding Site in the Metallochaperone CooT from Rhodospirillum rubrum. Chemistry - A European Journal. 25(67):15351-15360. doi: 10.1002/chem.201903492
  6. Andronov, L., et al. (2019). CENP-A nucleosome clusters form rosette-like structures around HJURP during G1. Nature Communications. 10:8. doi: 10.1038/s41467-019-12383-3
  7. Arragain, B., et al. (2019). High resolution cryo-EM structure of the helical RNA-bound Hantaan virus nucleocapsid reveals its assembly mechanisms. eLife. 8. doi: 10.7554/eLife.43075
  8. Bally, I., et al. (2019). Two Different Missense C1S Mutations, Associated to Periodontal Ehlers-Danlos Syndrome, Lead to Identical Molecular Outcomes. Frontiers in Immunology. 10:9. doi: 10.3389/fimmu.2019.02962
  9. Barbieri, L., et al. (2019). Backbone resonance assignment of human DJ-1 in the reduced state and in the cysteine sulfinic acid state. Biomolecular NMR Assignments. 13(2):371-376. doi: 10.1007/s12104-019-09908-8
  10. Becatti, M., et al. (2019). Different Antioxidant Efficacy of Two Mn-II-Containing Superoxide Anion Scavengers on Hypoxia/Reoxygenation-Exposed Cardiac Muscle Cells. Scientific Reports. 9:20. doi: 10.1038/s41598-019-46476-2
  11. Belime, A., et al. (2019). Recognition protein C1q of innate immunity agglutinates nanodiamonds without activating complement. Nanomedicine: Nanotechnology, Biology and Medicine. 18:292-302. doi: 10.1016/j.nano.2018.09.009
  12. Bellomo, G., et al. (2019). Dissecting the Interactions between Human Serum Albumin and alpha-Synuclein: New Insights on the Factors Influencing alpha-Synuclein Aggregation in Biological Fluids. Journal of Physical Chemistry B. 123(20):4380-4386. doi: 10.1021/acs.jpcb.9b02381
  13. Beňová-Liszeková, D., et al. (2019). Fine infrastructure of released and solidified Drosophila larval salivary secretory glue using SEM. Bioinspiration & Biomimetics. 14(5):11. doi: 10.1088/1748-3190/ab2b2b
  14. Beňová-Liszeková, D., et al. (2019). A protocol for processing the delicate larval and prepupal salivary glands of Drosophila for scanning electron microscopy. Microscopy Research and Technique. 82(7):1145-1156. doi: 10.1002/jemt.23263
  15. Bonam, S. R., et al. (2019). HSPA8/HSC70 in Immune Disorders: A Molecular Rheostat that Adjusts Chaperone-Mediated Autophagy Substrates. Cells. 8(8):26. doi: 10.3390/cells8080849
  16. Bougault, C., et al. (2019). Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency. Journal of Structural Biology. 206(1):66-72. doi: 10.1016/j.jsb.2018.07.009
  17. Bratanov, D., et al. (2019). Unique structure and function of viral rhodopsins. Nature Communications. 10:13. doi: 10.1038/s41467-019-12718-0
  18. Brennecke, P. (2019). EU-OPENSCREEN: A Novel Collaborative Approach to Facilitate Chemical Biology. SLAS Discovery: Advancing the Science of Drug Discovery. 24(3):398-413. doi: 10.1177/2472555218816276
  19. Brenzinger, S., et al. (2019). Structural and Proteomic Changes in Viable but Non-culturable Vibrio cholerae. Frontiers in Microbiology. 10:793. doi: 10.3389/fmicb.2019.00793
  20. Bresk, C. A., et al. (2019). Induction of Tier 1 HIV Neutralizing Antibodies by Envelope Trimers Incorporated into a Replication Competent Vesicular Stomatitis Virus Vector. Viruses. 11(2):20. doi: 10.3390/v11020159
  21. Breyton, C., et al. (2019). Assemblies of lauryl maltose neopentyl glycol (LMNG) and LMNG-solubilized membrane proteins. Biochimica et Biophysica Acta - Biomembranes. 1861(5):939-957. doi: 10.1016/j.bbamem.2019.02.003
  22. Busselez, J., et al. (2019). Cryo-Electron Tomography and Proteomics studies of centrosomes from differentiated quiescent thymocytes. Scientific Reports. 9:12. doi: 10.1038/s41598-019-43338-9
  23. Calvez, P., et al. (2019). Lipid Phases and Cell Geometry During the Cell Cycle of Streptococcus pneumoniae. Frontiers in Microbiology. 10(351):10. doi: 10.3389/fmicb.2019.00351
  24. Camponeschi, F., et al. (2019). Metal cofactors trafficking and assembly in the cell: a molecular view. Pure and Applied Chemistry. 91(2):231-245. doi: 10.1515/pac-2018-0720
  25. Camponeschi, F., et al. (2019). Paramagnetic H-1 NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes. Journal of Molecular Biology. 431(22):4514-4522. doi: 10.1016/j.jmb.2019.08.018
  26. Caputo, F., et al. (2019). Measuring Particle Size Distribution by Asymmetric Flow Field Flow Fractionation: A Powerful Method for the Preclinical Characterization of Lipid-Based Nanoparticles. Molecular Pharmaceutics. 16(2):756-767. doi: 10.1021/acs.molpharmaceut.8b01033
  27. Carl, N., et al. (2019). Invertible Micelles Based on Ion-Specific Interactions of Sr2+ and Ba2+ with Double Anionic Block Copolyelectrolytes. Macromolecules. 52(22):8759-8770. doi: 10.1021/acs.macromol.9b01924
  28. Carlon, A., et al. (2019). Assessing Structural Preferences of Unstructured Protein Regions by NMR. Biophysical Journal. 117(10):1948-1953. doi: 10.1016/j.bpj.2019.10.008
  29. Carlon, A., et al. (2019). Joint X-ray/NMR structure refinement of multidomain/multisubunit systems. Journal of Biomolecular NMR. 73(6-7):265-278. doi: 10.1007/s10858-018-0212-3
  30. Cerofolini, L., et al. (2019). Mechanism and Inhibition of Matrix Metalloproteinases. Current Medicinal Chemistry. 26(15):2609-2633. doi: 10.2174/0929867325666180326163523
  31. Cerofolini, L., et al. (2019). Integrative Approaches in Structural Biology: A More Complete Picture from the Combination of Individual Techniques. Biomolecules. 9(8). doi: 10.3390/biom9080370
  32. Cerofolini, L., et al. (2019). Real-Time Insights into Biological Events: In-Cell Processes and Protein-Ligand Interactions. Biophysical Journal. 116(2):239-247. doi: 10.1016/j.bpj.2018.11.3132
  33. Cerofolini, L., et al. (2019). Characterization of PEGylated Asparaginase: New Opportunities from NMR Analysis of Large PEGylated Therapeutics. Chemistry - A European Journal. 25(8):1984-1991. doi: 10.1002/chem.201804488
  34. Cerofolini, L., et al. (2019). Structural characterization of a protein adsorbed on aluminum hydroxide adjuvant in vaccine formulation. npj Vaccines. 4:5. doi: 10.1038/s41541-019-0115-7
  35. Cerofolini, L., et al. (2019). How Do Nuclei Couple to the Magnetic Moment of a Paramagnetic Center? A New Theory at the Gauntlet of the Experiments. Journal of Physical Chemistry Letters. 10(13):3610-3614. doi: 10.1021/acs.jpclett.9b01128
  36. Chicano, A., et al. (2019). Frozen-hydrated chromatin from metaphase chromosomes has an interdigitated multilayer structure. EMBO Journal. 38(7):12. doi: 10.15252/embj.201899769
  37. Christou, N. E., et al. (2019). NMR Reveals Light-Induced Changes in the Dynamics of a Photoswitchable Fluorescent Protein. Biophysical Journal. 117(11):2087-2100. doi: 10.1016/j.bpj.2019.10.035
  38. Ciambellotti, S., et al. (2019). Structural Biology of Iron-Binding Proteins by NMR Spectroscopy. European Journal of Inorganic Chemistry. 2019(5):569-576. doi: 10.1002/ejic.201801261
  39. Clemente, I., et al. (2019). Green Nanovectors for Phytodrug Delivery: In-Depth Structural and Morphological Characterization. ACS Sustainable Chemistry & Engineering. 7(15):12838-12846. doi: 10.1021/acssuschemeng.9b01748
  40. Cordeiro, T. N., et al. (2019). Interplay of Protein Disorder in Retinoic Acid Receptor Heterodimer and Its Corepressor Regulates Gene Expression. Structure. 27(8):1270-1285.e6. doi: 10.1016/j.str.2019.05.001
  41. Cuervo, A., et al. (2019). Structures of T7 bacteriophage portal and tail suggest a viral DNA retention and ejection mechanism. Nature Communications. 10(1). doi: 10.1038/s41467-019-11705-9
  42. D'Alessandro, G., et al. (2019). H-1-NMR metabolomics reveals the Glabrescione B exacerbation of glycolytic metabolism beside the cell growth inhibitory effect in glioma. Cell Communication and Signaling. 17(1):12. doi: 10.1186/s12964-019-0421-8
  43. Dalzon, B., et al. (2019). Utility of macrophages in an antitumor strategy based on the vectorization of iron oxide nanoparticles. Nanoscale. 11(19):9341-9352. doi: 10.1039/c8nr03364a
  44. Daniels, M. J., et al. (2019). Cyclized NDGA modifies dynamic α-synuclein monomers preventing aggregation and toxicity. Scientific Reports. 9(1):2937. doi: 10.1038/s41598-019-39480-z
  45. Davey, N. E., et al. (2019). An intrinsically disordered proteins community for ELIXIR. F1000Research. 8. doi: 10.12688/f1000research.20136.1
  46. De Colibus, L., et al. (2019). Assembly of complex viruses exemplified by a halophilic euryarchaeal virus. Nature Communications. 10:9. doi: 10.1038/s41467-019-09451-z
  47. De Zitter, E., et al. (2019). Mechanistic investigation of mEos4b reveals a strategy to reduce track interruptions in sptPALM. Nature Methods. 16(8):707-710. doi: 10.1038/s41592-019-0462-3
  48. Decelle, J., et al. (2019). Algal Remodeling in a Ubiquitous Planktonic Photosymbiosis. Current Biology. 29(6):968-978.e4. doi: 10.1016/j.cub.2019.01.073
  49. Desfosses, A., et al. (2019). Assembly and cryo-EM structures of RNA-specific measles virus nucleocapsids provide mechanistic insight into paramyxoviral replication. Proceedings of the National Academy of Sciences of the United States of America. 116(10):4256-4264. doi: 10.1073/pnas.1816417116
  50. Desfosses, A., et al. (2019). Atomic structures of an entire contractile injection system in both the extended and contracted states. Nature Microbiology. 4(11):1885-1894. doi: 10.1038/s41564-019-0530-6
  51. Domanska, A., et al. (2019). A 2.8-Angstrom-Resolution Cryo-Electron Microscopy Structure of Human Parechovirus 3 in Complex with Fab from a Neutralizing Antibody. Journal of Virology. 93(4):e01597-18. doi: 10.1128/JVI.01597-18
  52. Donchet, A., et al. (2019). The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NPCORE, with or without a NPTAIL for nuclear transport. Scientific Reports. 9:14. doi: 10.1038/s41598-018-37306-y
  53. Eberhardt, J., et al. (2019). A revisited version of the apo structure of the ligand-binding domain of the human nuclear receptor retinoic X receptor alpha. Acta Crystallographica Section F - Structural Biology Communications. 75:98-104. doi: 10.1107/s2053230x18018022
  54. El Omari, K., et al. (2019). The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins. Nature Communications. 10:11. doi: 10.1038/s41467-019-08728-7
  55. Engilberge, S., et al. (2019). Protein crystal structure determination with the crystallophore, a nucleating and phasing agent. Journal of Applied Crystallography. 52:722-731. doi: 10.1107/s1600576719006381
  56. Errasti-Murugarren, E., et al. (2019). L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction. Nature Communications. 10(1):12. doi: 10.1038/s41467-019-09837-z
  57. Everts-Graber, J., et al. (2019). Proteomic analysis of neutrophils in ANCA-associated vasculitis reveals a dysregulation in proteinase 3-associated proteins such as annexin-A1 involved in apoptotic cell clearance. Kidney International. 96(2):397-408. doi: 10.1016/j.kint.2019.02.017
  58. Fan, H. T., et al. (2019). Structures of influenza A virus RNA polymerase offer insight into viral genome replication. Nature. 573(7773):287-+. doi: 10.1038/s41586-019-1530-7
  59. Favier, A., et al. (2019). NMRlib: user-friendly pulse sequence tools for Bruker NMR spectrometers. Journal of Biomolecular NMR. 73(5):199-211. doi: 10.1007/s10858-019-00249-1
  60. Favier, A. L., et al. (2019). Involvement of Surfactant Protein D in Ebola Virus Infection Enhancement via Glycoprotein Interaction. Viruses. 11(1):17. doi: 10.3390/v11010015
  61. Fenwick, C., et al. (2019). Tumor suppression of novel anti-PD-1 antibodies mediated through CD28 costimulatory pathway. Journal of Experimental Medicine. 216(7):1525-1541. doi: 10.1084/jem.20182359
  62. Floc'h, K., et al. (2019). Cell morphology and nucleoid dynamics in dividing Deinococcus radiodurans. Nature Communications. 10:13. doi: 10.1038/s41467-019-11725-5
  63. Flygaard, R. K., et al. (2019). Purification and characterization of native human elongation factor 2. Protein Expression and Purification. 158:15-19. doi: 10.1016/j.pep.2019.02.005
  64. Fragai, M., et al. (2019). Relaxivity of Gd-Based MRI Contrast Agents in Crosslinked Hyaluronic Acid as a Model for Tissues. ChemPhysChem. 20(17):2204-2209. doi: 10.1002/cphc.201900587
  65. Gabel, F., et al. (2019). Medical contrast media as possible tools for SAXS contrast variation. IUCrJ. 6(Pt 4):521-525. doi: 10.1107/s2052252519005943
  66. Galves, M., et al. (2019). Ubiquitin Signaling and Degradation of Aggregate-Prone Proteins. Trends in Biochemical Sciences. 44(10):872-884. doi: 10.1016/j.tibs.2019.04.007
  67. Garcia-Rodriguez, F. M., et al. (2019). A group II intron-encoded protein interacts with the cellular replicative machinery through the beta-sliding clamp. Nucleic Acids Research. 47(14):7605-7617. doi: 10.1093/nar/gkz468
  68. Garratt, R. C. (2019). A brief history of protein crystallography in Brazil. Biophysical Reviews.509-511. doi: 10.1007/s12551-019-00562-x
  69. Gauto, D. F., et al. (2019). Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. 10:12. doi: 10.1038/s41467-019-10490-9
  70. Gauto, D. F., et al. (2019). Aromatic Ring Dynamics, Thermal Activation, and Transient Conformations of a 468 kDa Enzyme by Specific H-1-C-13 Labeling and Fast Magic-Angle Spinning NMR. Journal of the American Chemical Society. 141(28):11183-11195. doi: 10.1021/jacs.9b04219
  71. Geissner, A., et al. (2019). Microbe-focused glycan array screening platform. Proceedings of the National Academy of Sciences of the United States of America. 116(6):1958-1967. doi: 10.1073/pnas.1800853116
  72. Genna, V., et al. (2019). A Transient and Flexible Cation-pi Interaction Promotes Hydrolysis of Nucleic Acids in DNA and RNA Nucleases. Journal of the American Chemical Society. 141(27):10770-10776. doi: 10.1021/jacs.9b03663
  73. Ghini, V., et al. (2019). About the use of C-13-C-13 NOESY in bioinorganic chemistry. Journal of Inorganic Biochemistry. 192:25-32. doi: 10.1016/j.jinorgbio.2018.12.006
  74. Giustini, C., et al. (2019). Tyrosine metabolism: identification of a key residue in the acquisition of prephenate aminotransferase activity by 1 beta aspartate aminotransferase. FEBS Journal. 286(11):2118-2134. doi: 10.1111/febs.14789
  75. Gourdoupis, S. N., Veronica; Ciofi-Baffoni, Simone; Banci, Lucia; Calderone, Vito, (2019). In-house high-energy-remote SAD phasing using the magic triangle: how to tackle the P1 low symmetry using multiple orientations of the same crystal of human IBA57 to increase the multiplicity. Acta Crystallographica Section D - Structural Biology. 75(3):317-324. doi: 10.1107/S2059798319000214
  76. Gröbner, R., et al. (2019). C1R Mutations Trigger Constitutive Complement 1 Activation in Periodontal Ehlers-Danlos Syndrome. Frontiers in Immunology. 10(2537):14. doi: 10.3389/fimmu.2019.02537
  77. Guillet, P., et al. (2019). Hydrogenated Diglucose Detergents for Membrane-Protein Extraction and Stabilization. Langmuir. 35(12):4287-4295. doi: 10.1021/acs.langmuir.8b02842
  78. Gupta, R., et al. (2019). Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies. Journal of Physical Chemistry B. 123(24):5048-5058. doi: 10.1021/acs.jpcb.9b02293
  79. Gusach, A., et al. (2019). Structural basis of ligand selectivity and disease mutations in cysteinyl leukotriene receptors. Nature Communications. 10:9. doi: 10.1038/s41467-019-13348-2
  80. Hedison, T. M., et al. (2019). Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis. ACS Catalysis. 9(7):6087-6099. doi: 10.1021/acscatal.9b01266
  81. Hénault, C. M., et al. (2019). A lipid site shapes the agonist response of a pentameric ligand-gated ion channel. Nature Chemical Biology. 15(12):1156-1164. doi: 10.1038/s41589-019-0369-4
  82. Hill, C. H., et al. (2019). Activation of the Endonuclease that Defines mRNA 3 ' Ends Requires Incorporation into an 8-Subunit Core Cleavage and Polyadenylation Factor Complex. Molecular Cell. 73(6):1217-+. doi: 10.1016/j.molcel.2018.12.023
  83. Hoang, M.-D., et al. (2019). Self-assembled polydiacetylene nanoribbons for semi-heterogeneous and enantioselective organocatalysis of aldol reactions in water. ChemCatChem. n/a(n/a). doi: 10.1002/cctc.201901960
  84. Howard, S. P., et al. (2019). Structure and assembly of pilotin-dependent and -independent secretins of the type II secretion system. PLOS Pathogens. 15(5):e1007731. doi: 10.1371/journal.ppat.1007731
  85. Ilca, S. L., et al. (2019). Multiple liquid crystalline geometries of highly compacted nucleic acid in a dsRNA virus. Nature. 570(7760):252-+. doi: 10.1038/s41586-019-1229-9
  86. Indorato, R. L., et al. (2019). Is the Fate of Clinical Candidate Arry-520 Already Sealed? Predicting Resistance in Eg5-Inhibitor Complexes. Molecular Cancer Therapeutics. 18(12):2394-2406. doi: 10.1158/1535-7163.mct-19-0154
  87. Ivic, N., et al. (2019). Fuzzy Interactions Form and Shape the Histone Transport Complex. Molecular Cell. 73(6):1191-1203.e6. doi: 10.1016/j.molcel.2019.01.032
  88. Jespersen, N. E., et al. (2019). The LC8-RavP ensemble Structure Evinces A Role for LC8 in Regulating Lyssavirus Polymerase Functionality. Journal of Molecular Biology. 431(24):4959-4977. doi: 10.1016/j.jmb.2019.10.011
  89. Jimenez, A., et al. (2019). Validation of electron microscopy initial models via small angle X-ray scattering curves. Bioinformatics. 35(14):2427-2433. doi: 10.1093/bioinformatics/bty985
  90. Kandiah, E., et al. (2019). Structure, Function, and Evolution of the Pseudomonas aeruginosa Lysine Decarboxylase LdcA. Structure. 27(12):1842-+. doi: 10.1016/j.str.2019.10.003
  91. Kanzari-Mnallah, D. E., M.; Pavlíček, J.; Vellieux, F.; Boughzala, H.; Akacha, A (2019). Synthesis, Conformational Analysis and Crystal Structure of New Thioxo, Oxo, Seleno Diastereomeric Cyclophosphamides Containing 1,3,2-dioxaphosphorinane. Current Organic Chemistry. 23(2):205-213. doi: 10.2174/1385272823666190213142748
  92. Kiema, T.-R., et al. (2019). The peroxisomal zebrafish SCP2-thiolase (type-1) is a weak transient dimer as revealed by crystal structures and native mass spectrometry. Biochemical Journal. 476(2):307. doi: 10.1042/BCJ20180788
  93. Klaholz, B. P. (2019). Deriving and refining atomic models in crystallography and cryo-EM: the latest Phenix tools to facilitate structure analysis. Acta Crystallographica Section D - Structural Biology. 75(Pt 10):878-881. doi: 10.1107/s2059798319013391
  94. Kolesnikova, O., et al. (2019). TFIIH: A multi-subunit complex at the cross-roads of transcription and DNA repair. In: Donev, R., ed. DNA Repair. San Diego: Elsevier Academic Press Inc 2019:21-67. doi: 10.1016/bs.apcsb.2019.01.003
  95. Kopera, E., et al. (2019). High-Titre Neutralizing Antibodies to H1N1 Influenza Virus after Mouse Immunization with Yeast Expressed H1 Antigen: A Promising Influenza Vaccine Candidate. Journal of Immunology Research. 2019:10. doi: 10.1155/2019/2463731
  96. Kovalev, K., et al. (2019). Structure and mechanisms of sodium-pumping KR2 rhodopsin. Science Advances. 5(4):10. doi: 10.1126/sciadv.aav2671
  97. Kuban, V., et al. (2019). Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase. Journal of the American Chemical Society. 141(42):16817-16828. doi: 10.1021/jacs.9b07837
  98. Kukic, P., et al. (2019). The free energy landscape of the oncogene protein E7 of human papillomavirus type 16 reveals a complex interplay between ordered and disordered regions. Scientific Reports. 9(1):12. doi: 10.1038/s41598-019-41925-4
  99. Kuzina, E. S., et al. (2019). Structures of ligand-occupied beta-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity. Proceedings of the National Academy of Sciences of the United States of America. 116(16):7819-7824. doi: 10.1073/pnas.1822055116
  100. Laddomada, F., et al. (2019). The MurG glycosyltransferase provides an oligomeric scaffold for the cytoplasmic steps of peptidoglycan biosynthesis in the human pathogen Bordetella pertussis. Scientific Reports. 9(1):17. doi: 10.1038/s41598-019-40966-z
  101. Laverty, D., et al. (2019). Cryo-EM structure of the human alpha 1 beta 3 gamma 2 GABA(A) receptor in a lipid bilayer. Nature. 565(7740):516-+. doi: 10.1038/s41586-018-0833-4
  102. Levy, N., et al. (2019). Structural Basis for E. coli Penicillin Binding Protein (PBP) 2 Inhibition, a Platform for Drug Design. Journal of Medicinal Chemistry. 62(9):4742-4754. doi: 10.1021/acs.jmedchem.9b00338
  103. Li, R. J. E., et al. (2019). Systematic Dual Targeting of Dendritic Cell C-Type Lectin Receptor DC-SIGN and TLR7 Using a Trifunctional Mannosylated Antigen. Frontiers in Chemistry. 7:15. doi: 10.3389/fchem.2019.00650
  104. Liebschner, D., et al. (2019). Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Acta Crystallographica Section D - Structural Biology. 75:861-877. doi: 10.1107/s2059798319011471
  105. Lombardi, C., et al. (2019). Structural and Functional Characterization of the Type Three Secretion System (T3SS) Needle of Pseudomonas aeruginosa. Frontiers in Microbiology. 10:15. doi: 10.3389/fmicb.2019.00573
  106. Lombardo, C. M., et al. (2019). Design and Structure Determination of a Composite Zinc Finger Containing a Nonpeptide Foldamer Helical Domain. Journal of the American Chemical Society. 141(6):2516-2525. doi: 10.1021/jacs.8b12240
  107. Lopes de Carvalho, L., et al. (2019). Evolution and functional classification of mammalian copper amine oxidases. Molecular Phylogenetics and Evolution. 139:106571. doi: 10.1016/j.ympev.2019.106571
  108. Luginina, A., et al. (2019). Structure-based mechanism of cysteinyl leukotriene receptor inhibition by antiasthmatic drugs. Science Advances. 5(10):10. doi: 10.1126/sciadv.aax2518
  109. Lunin, V. Y. L., Natalia L.; Petrova, Tatiana E.; Baumstark, Manfred W.; Urzhumtsev, Alexandre G. (2019). Mask-based approach to phasing of single-particle diffraction data. II. Likelihood-based selection criteria. Acta Crystallographica Section D - Structural Biology. 75:79-89. doi: 10.1107/S2059798318016959
  110. Maalej, M., et al. (2019). Human Macrophage Galactose-Type Lectin (MGL) Recognizes the Outer Core of Escherichia coli Lipooligosaccharide. ChemBioChem. 20(14):1778-1782. doi: 10.1002/cbic.201900087
  111. Machon, C., et al. (2019). Atomic structure of the Epstein-Barr virus portal. Nature Communications. 10:7. doi: 10.1038/s41467-019-11706-8
  112. Maity, S., et al. (2019). VPS4 triggers constriction and cleavage of ESCRT-III helical filaments. Science Advances. 5(4):9. doi: 10.1126/sciadv.aau7198
  113. Maluenda, D., et al. (2019). Flexible workflows for on-the-fly electron-microscopy single-particle image processing using Scipion. Acta Crystallographica Section D - Structural Biology. 75:882-894. doi: 10.1107/s2059798319011860
  114. Mantynen, S., et al. (2019). Half a Century of Research on Membrane-Containing Bacteriophages: Bringing New Concepts to Modern Virology. Viruses. 11(1):17. doi: 10.3390/v11010076
  115. Marabelli, C., et al. (2019). A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex. Cell Reports. 27(2):387-399.e7. doi: 10.1016/j.celrep.2019.03.061
  116. Marin-Montesinos, I., et al. (2019). Selective high-resolution DNP-enhanced NMR of biomolecular binding sites. Chemical Science. 10(11):3366-3374. doi: 10.1039/c8sc05696j
  117. Marion, D., et al. (2019). Microsecond Protein Dynamics from Combined Bloch-McConnell and Near-Rotary-Resonance R-1p Relaxation-Dispersion MAS NMR. ChemPhysChem. 20(2):276-284. doi: 10.1002/cphc.201800935
  118. Masiulis, S., et al. (2019). GABA(A) receptor signalling mechanisms revealed by structural pharmacology. Nature. 565(7740):454-+. doi: 10.1038/s41586-018-0832-5
  119. Mateos, B., et al. (2019). NMR Characterization of Long-Range Contacts in Intrinsically Disordered Proteins from Paramagnetic Relaxation Enhancement in C-13 Direct-Detection Experiments. ChemBioChem. 20(3):335-339. doi: 10.1002/cbic.201800539
  120. Maurice, F., et al. (2019). In vitro dimerization of human RIO2 kinase. RNA Biology. 16(11):1633-1642. doi: 10.1080/15476286.2019.1653679
  121. Mauro, E., et al. (2019). Human H4 tail stimulates HIV-1 integration through binding to the carboxy-terminal domain of integrase. Nucleic Acids Research. 47(7):3607-3618. doi: 10.1093/nar/gkz091
  122. McCartney, A., et al. (2019). Metabolomic analysis of serum may refine 21-gene expression assay risk recurrence stratification. npj Breast Cancer. 5:5. doi: 10.1038/s41523-019-0123-9
  123. Medve, L., et al. (2019). Enhancing Potency and Selectivity of a DC-SIGN Glycomimetic Ligand by Fragment-Based Design: Structural Basis. Chemistry – A European Journal. 25(64):14659-14668. doi: 10.1002/chem.201903391
  124. Miyachiro, M. M., et al. (2019). Complex Formation between Mur Enzymes from Streptococcus pneumoniae. Biochemistry. 58(30):3314-3324. doi: 10.1021/acs.biochem.9b00277
  125. Mizuno, C. M., et al. (2019). Novel haloarchaeal viruses from Lake Retba infecting Haloferax and Halorubrum species. Environmental Microbiology. 21(6):2129-2147. doi: 10.1111/1462-2920.14604
  126. Mizuta, R., et al. (2019). Hierarchical Nanotube Self-Assembly of DNA Minor Groove-Binding Ligand DB921 via Alkali Halide Triggering. Macromolecular Symposia. 386(1):7. doi: 10.1002/masy.201800243
  127. Montanier, C. Y., et al. (2019). Changing surface grafting density has an effect on the activity of immobilized xylanase towards natural polysaccharides. Scientific Reports. 9:12. doi: 10.1038/s41598-019-42206-w
  128. Morris, C., et al. (2019). West-Life: A Virtual Research Environment for structural biology. Journal of Structural Biology: X. 1:100006. doi: 10.1016/j.yjsbx.2019.100006
  129. Moulin, M., et al. (2019). Towards a molecular understanding of the water purification properties of Moringa seed proteins. Journal of Colloid and Interface Science. 554:296-304. doi: 10.1016/j.jcis.2019.06.071
  130. Nasta, V., et al. (2019). Structural properties of 2Fe-2S ISCA2-IBA57: a complex of the mitochondrial iron-sulfur cluster assembly machinery. Scientific Reports. 9:12. doi: 10.1038/s41598-019-55313-5
  131. Njume, F. N., et al. (2019). Identification and characterization of the Onchocerca volvulus Excretory Secretory Product Ov28CRP, a putative GM2 activator protein. PLOS Neglected Tropical Diseases. 13(7):28. doi: 10.1371/journal.pntd.0007591
  132. Oksanen, H. M., et al. (2019). Membrane-Containing Icosahedral Bacteriophage PRD1: The Dawn of Viral Lineages. In: Greber, U. F., ed. Physical Virology: Virus Structure and Mechanics. Cham: Springer International Publishing Ag 2019:85-109. doi: 10.1007/978-3-030-14741-9_5
  133. Pagliuso, A., et al. (2019). An RNA-Binding Protein Secreted by a Bacterial Pathogen Modulates RIG-I Signaling. Cell Host & Microbe. 26(6):823-+. doi: 10.1016/j.chom.2019.10.004
  134. Parigi, G., et al. (2019). Pseudocontact shifts and paramagnetic susceptibility in semiempirical and quantum chemistry theories. Journal of Chemical Physics. 150(14):11. doi: 10.1063/1.5037428
  135. Parigi, G., et al. (2019). Understanding Overhauser Dynamic Nuclear Polarisation through NMR relaxometry. Molecular Physics. 117(7-8):888-897. doi: 10.1080/00268976.2018.1527409
  136. Parigi, G., et al. (2019). Magnetic susceptibility and paramagnetism-based NMR. Progress in Nuclear Magnetic Resonance Spectroscopy. 114:211-236. doi: 10.1016/j.pnmrs.2019.06.003
  137. Peschiera, I., et al. (2019). Structural basis for cooperativity of human monoclonal antibodies to meningococcal factor H-binding protein. Communications Biology. 2:9. doi: 10.1038/s42003-019-0493-4
  138. Picchioni, D., et al. (2019). Mitochondrial Protein Synthesis and mtDNA Levels Coordinated through an Aminoacyl-tRNA Synthetase Subunit. Cell Reports. 27(1):40-+. doi: 10.1016/j.celrep.2019.03.022
  139. Pinto, D., et al. (2019). Structural Basis for Broad HIV-1 Neutralization by the MPER-Specific Human Broadly Neutralizing Antibody LN01. Cell Host & Microbe. 26(5):623-+. doi: 10.1016/j.chom.2019.09.016
  140. Polykretis, P., et al. (2019). Cadmium effects on superoxide dismutase 1 in human cells revealed by NMR. Redox Biology. 21:7. doi: 10.1016/j.redox.2019.101102
  141. Polykretis, P., et al. (2019). Conformational characterization of full-length X-chromosome-linked inhibitor of apoptosis protein (XIAP) through an integrated approach. IUCrJ. 6:948-957. doi: 10.1107/s205225251901073x
  142. Pooch, F., et al. (2019). Poly(2-isopropyl-2-oxazoline)-b-poly(lactide) (PiPOx-b-PLA) Nanoparticles in Water: Interblock van der Waals Attraction Opposes Amphiphilic Phase Separation. Macromolecules. 52(3):1317-1326. doi: 10.1021/acs.macromol.8b02558
  143. Pozzi, C., et al. (2019). Effect of the point mutation H54N on the ferroxidase process of Rana catesbeiana H ' ferritin. Journal of Inorganic Biochemistry. 197:10. doi: 10.1016/j.jinorgbio.2019.110697
  144. Ramirez-Aportela, E., et al. (2019). DeepRes: a new deep-learning- and aspect-based local resolution method for electron-microscopy maps. IUCrJ. 6:1054-1063. doi: 10.1107/s2052252519011692
  145. Randich, A. M., et al. (2019). Origin of a Core Bacterial Gene via Co-option and Detoxification of a Phage Lysin. Current Biology. 29(10):1634-1646.e6. doi: 10.1016/j.cub.2019.04.032
  146. Rapisarda, C., et al. (2019). In situ and high-resolution cryo-EM structure of a bacterial type VI secretion system membrane complex. EMBO Journal. 38(10):18. doi: 10.15252/embj.2018100886
  147. Ravera, E., et al. (2019). What are the methodological and theoretical prospects for paramagnetic NMR in structural biology? A glimpse into the crystal ball. Journal of Magnetic Resonance. 306:173-179. doi: 10.1016/j.jmr.2019.07.027
  148. Renko, M., et al. (2019). Rotational symmetry of the structured Chip/LDB-SSDP core module of the Wnt enhanceosome. Proceedings of the National Academy of Sciences of the United States of America. 116(42):20977-20983. doi: 10.1073/pnas.1912705116
  149. Roche, J., et al. (2019). The archaeal LDH-like malate dehydrogenase from Ignicoccus islandicus displays dual substrate recognition, hidden allostery and a non-canonical tetrameric oligomeric organization. Journal of Structural Biology. 208(1):7-17. doi: 10.1016/j.jsb.2019.07.006
  150. Rochel, N., et al. (2019). Recurrent activating mutations of PPARgamma associated with luminal bladder tumors. Nature Communications. 10(1):253. doi: 10.1038/s41467-018-08157-y
  151. Rudolf, A. F., et al. (2019). The morphogen Sonic hedgehog inhibits its receptor Patched by a pincer grasp mechanism. Nature Chemical Biology. 15(10):975-+. doi: 10.1038/s41589-019-0370-y
  152. Ruprecht, J. J., et al. (2019). The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier. Cell. 176(3):435-447.e15. doi: 10.1016/j.cell.2018.11.025
  153. Salvador, D., et al. (2019). Minimal nanodisc without exogenous lipids for stabilizing membrane proteins in detergent-free buffer. Biochimica et Biophysica Acta - Biomembranes. 1861(4):852-860. doi: 10.1016/j.bbamem.2019.01.013
  154. Sanchez-Garcia, R., et al. (2019). BIPSPI: a method for the prediction of partner-specific protein-protein interfaces. Bioinformatics. 35(3):470-477. doi: 10.1093/bioinformatics/bty647
  155. Santos-Perez, I., et al. (2019). Structural basis for assembly of vertical single beta-barrel viruses. Nature Communications. 10:9. doi: 10.1038/s41467-019-08927-2
  156. Schiavina, M., et al. (2019). Taking Simultaneous Snapshots of Intrinsically Disordered Proteins in Action. Biophysical Journal. 117(1):46-55. doi: 10.1016/j.bpj.2019.05.017
  157. Seffouh, A., et al. (2019). Expression and purification of recombinant extracellular sulfatase HSulf-2 allows deciphering of enzyme sub-domain coordinated role for the binding and 6-O-desulfation of heparan sulfate. Cellular and Molecular Life Sciences. 76(9):1807-1819. doi: 10.1007/s00018-019-03027-2
  158. Shaikh, F., et al. (2019). Structure-Based in Silico Screening Identifies a Potent Ebolavirus Inhibitor from a Traditional Chinese Medicine Library. Journal of Medicinal Chemistry. 62(6):2928-2937. doi: 10.1021/acs.jmedchem.8b01328
  159. Sigoillot, M., et al. (2019). Domain-interface dynamics of CFTR revealed by stabilizing nanobodies. Nature Communications. 10:12. doi: 10.1038/s41467-019-10714-y
  160. Silva, J. M., et al. (2019). Metal centers in biomolecular solid-state NMR. Journal of Structural Biology. 206(1):99-109. doi: 10.1016/j.jsb.2018.11.013
  161. Silva, J. M., et al. (2019). Non-crystallographic symmetry in proteins: Jahn-Teller-like and Butterfly-like effects? Journal of Biological Inorganic Chemistry. 24(1):91-101. doi: 10.1007/s00775-018-1630-0
  162. Silvestre-Roig, C., et al. (2019). Externalized histone H4 orchestrates chronic inflammation by inducing lytic cell death. Nature. 569(7755):236-240. doi: 10.1038/s41586-019-1167-6
  163. Sjöstedt, N., et al. (2019). Endogenous, cholesterol-activated ATP-dependent transport in membrane vesicles from Spodoptera frugiperda cells. European Journal of Pharmaceutical Sciences. 137:9. doi: 10.1016/j.ejps.2019.104963
  164. Strokappe, N. M., et al. (2019). Super Potent Bispecific Llama VHH Antibodies Neutralize HIV via a Combination of gp41 and gp120 Epitopes. Antibodies. 8(2):19. doi: 10.3390/antib8020038
  165. Tarantini, A., et al. (2019). Physicochemical alterations and toxicity of InP alloyed quantum dots aged in environmental conditions: A safer by design evaluation. NanoImpact. 14:13. doi: 10.1016/j.impact.2019.100168
  166. Teulon, J. M., et al. (2019). On the Operational Aspects of Measuring Nanoparticle Sizes. Nanomaterials. 9(1):29. doi: 10.3390/nano9010018
  167. Thangaraj, S. K., et al. (2019). Thermokinetic Analysis of Protein Subunit Exchange by Variable-Temperature Native Mass Spectrometry. Biochemistry. 58(50):5025-5029. doi: 10.1021/acs.biochem.9b00911
  168. Torra, J., et al. (2019). Tailing miniSOG: structural bases of the complex photophysics of a flavin-binding singlet oxygen photosensitizing protein. Scientific Reports. 9:10. doi: 10.1038/s41598-019-38955-3
  169. Uchanski, T., et al. (2019). An improved yeast surface display platform for the screening of nanobody immune libraries. Scientific Reports. 9:12. doi: 10.1038/s41598-018-37212-3
  170. Ural-Blimke, Y., et al. (2019). Structure of Prototypic Peptide Transporter DtpA from E. coli in Complex with Valganciclovir Provides Insights into Drug Binding of Human PepT1. Journal of the American Chemical Society. 141(6):2404-2412. doi: 10.1021/jacs.8b11343
  171. Uroda, T., et al. (2019). Conserved Pseudoknots in lncRNA MEG3 Are Essential for Stimulation of the p53 Pathway. Molecular Cell. 75(5):982-+. doi: 10.1016/j.molcel.2019.07.025
  172. Urzhumtsev, A. G., et al. (2019). Introduction to crystallographic refinement of macromolecular atomic models. Crystallography Reviews. 25(3):164-262. doi: 10.1080/0889311x.2019.1631817
  173. Urzhumtseva, L., et al. (2019). py_convrot: rotation conventions, to understand and to apply. Journal of Applied Crystallography. 52:869-881. doi: 10.1107/s1600576719007313
  174. Vallet, A., et al. (2019). Aromatic SOFAST-HMBC for proteins at natural C-13 abundance. Journal of Magnetic Resonance. 300:95-102. doi: 10.1016/j.jmr.2019.01.009
  175. Van Zandt, M. C., et al. (2019). Discovery of N-Substituted 3-Amino-4-(3-boronopropyl)pyrrolidine-3-carboxylic Acids as Highly Potent Third-Generation Inhibitors of Human Arginase I and II. Journal of Medicinal Chemistry. 62(17):8164-8177. doi: 10.1021/acs.jmedchem.9b00931
  176. Vanden Broeck, A., et al. (2019). Cryo-EM structure of the complete E. coli DNA gyrase nucleoprotein complex. Nature Communications. 10:12. doi: 10.1038/s41467-019-12914-y
  177. Vanden Broeck, A., et al. (2019). Structural Basis for DNA Gyrase Interaction with Coumermycin A1. Journal of Medicinal Chemistry. 62(8):4225-4231. doi: 10.1021/acs.jmedchem.8b01928
  178. Vanek, O., et al. (2019). Production of recombinant soluble dimeric C-type lectin-like receptors of rat natural killer cells. Scientific Reports. 9:16. doi: 10.1038/s41598-019-52114-8
  179. Vassal-Stermann, E., et al. (2019). CryoEM structure of adenovirus type 3 fibre with desmoglein 2 shows an unusual mode of receptor engagement. Nature Communications. 10:7. doi: 10.1038/s41467-019-09220-y
  180. Vassal-Stermann, E., et al. (2019). Intermediate-resolution crystal structure of the human adenovirus B serotype 3 fibre knob in complex with the EC2-EC3 fragment of desmoglein 2. Acta Crystallographica Section F - Structural Biology Communications. 75:750-757. doi: 10.1107/s2053230x19015784
  181. Veronesi, G., et al. (2019). In Vivo Biotransformations of Indium Phosphide Quantum Dots Revealed by X-Ray Microspectroscopy. ACS Applied Materials & Interfaces. 11(39):35630-35640. doi: 10.1021/acsami.9b15433
  182. Verschueren, K. H. G., et al. (2019). Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature. 568(7753):571-575. doi: 10.1038/s41586-019-1095-5
  183. Vignoli, A., et al. (2019). Metabolic Signature of Primary Biliary Cholangitis and Its Comparison with Celiac Disease. Journal of Proteome Research. 18(3):1228-1236. doi: 10.1021/acs.jproteome.8b00849
  184. Vignoli, A., et al. (2019). NMR-based metabolomics identifies patients at high risk of death within two years after acute myocardial infarction in the AMI-Florence II cohort. BMC Medicine. 17(1):3. doi: 10.1186/s12916-018-1240-2
  185. Vilas, J. L., et al. (2019). Measurement of local resolution in electron tomography. Journal of Structural Biology: X.100016. doi: 10.1016/j.yjsbx.2019.100016
  186. Vlasov, A. V., et al. (2019). Unusual features of the c-ring of F1FO ATP synthases. Scientific Reports. 9:11. doi: 10.1038/s41598-019-55092-z
  187. Vragniau, C., et al. (2019). Synthetic self-assembling ADDomer platform for highly efficient vaccination by genetically encoded multiepitope display. Science Advances. 5(9):8. doi: 10.1126/sciadv.aaw2853
  188. Waldie, S., et al. (2019). The Production of Matchout-Deuterated Cholesterol and the Study of Bilayer-Cholesterol Interactions. Scientific Reports. 9:11. doi: 10.1038/s41598-019-41439-z
  189. Wegner, K. D., et al. (2019). Influence of the Core/Shell Structure of Indium Phosphide Based Quantum Dots on Their Photostability and Cytotoxicity. Frontiers in Chemistry. 7:12. doi: 10.3389/fchem.2019.00466
  190. Wegner, K. D., et al. (2019). Gallium - a versatile element for tuning the photoluminescence properties of InP quantum dots. ChemComm. 55(11):1663-1666. doi: 10.1039/c8cc09740b
  191. Wu, H., et al. (2019). Decapping Enzyme NUDT12 Partners with BLMH for Cytoplasmic Surveillance of NAD-Capped RNAs. Cell Reports. 29(13):4422-+. doi: 10.1016/j.celrep.2019.11.108
  192. Yee, A. W., et al. (2019). A molecular mechanism for transthyretin amyloidogenesis. Nature Communications. 10:10. doi: 10.1038/s41467-019-08609-z
  193. Zhou, D. M., et al. (2019). Unexpected mode of engagement between enterovirus 71 and its receptor SCARB2. Nature Microbiology. 4(3):414-419. doi: 10.1038/s41564-018-0319-z

2018

  1. Afonine, P. V., et al. (2018). From deep TLS validation to ensembles of atomic models built from elemental motions. II. Analysis of TLS refinement results by explicit interpretation. Acta Crystallographica Section D-Structural Biology. 74:621-631. doi: 10.1107/s2059798318005764
  2. Afonine, P. V., et al. (2018). Real-space refinement in PHENIX for cryo-EM and crystallography. Acta crystallographica. Section D, Structural biology. 74(Pt 6):531-544. doi: 10.1107/S2059798318006551
  3. Aleksandrova, N., et al. (2018). Robo1 Forms a Compact Dimer-of-Dimers Assembly. Structure. 26(2):320-328.e4. doi: https://doi.org/10.1016/j.str.2017.12.003
  4. Andronov, L., et al. (2018). 3DClusterViSu: 3D clustering analysis of super-resolution microscopy data by 3D Voronoi tessellations. Bioinformatics. doi: 10.1093/bioinformatics/bty200
  5. Barbieri, L., et al. (2018). Intracellular metal binding and redox behavior of human DJ-1. Journal of Biological Inorganic Chemistry. 23(1):61-69. doi: 10.1007/s00775-017-1509-5
  6. Basbous, H., et al. (2018). Characterization of a Glycyl-Specific TET Aminopeptidase Complex from Pyrococcus horikoshii. Journal of Bacteriology. 200(17):11. doi: 10.1128/jb.00059-18
  7. Bedez, C., et al. (2018). Post-translational modifications in DNA topoisomerase 2 alpha highlight the role of a eukaryote-specific residue in the ATPase domain. Scientific Reports. 8:12. doi: 10.1038/s41598-018-27606-8
  8. Belime, A., et al. (2018). Mode of PEG Coverage on Carbon Nanotubes Affects Binding of Innate Immune Protein C1q. J Phys Chem B. 122(2):757-763. doi: 10.1021/acs.jpcb.7b06596
  9. Belime, A., et al. (2018). Recognition protein C1q of innate immunity agglutinates nanodiamonds without activating complement. Nanomedicine: Nanotechnology, Biology and Medicine. doi: https://doi.org/10.1016/j.nano.2018.09.009
  10. Bellomo, G., et al. (2018). Aggregation kinetics of the A beta 1-40 peptide monitored by NMR. Chemical Communications. 54(55):7601-7604. doi: 10.1039/c8cc01710g
  11. Bilokapic, S., et al. (2018). Histone octamer rearranges to adapt to DNA unwrapping. Nat Struct Mol Biol. 25(1):101-108. doi: 10.1038/s41594-017-0005-5
  12. Bonnard, D., et al. (2018). Structure-function analyses unravel distinct effects of allosteric inhibitors of HIV-1 integrase on viral maturation and integration. J Biol Chem. 293(16):6172-6186. doi: 10.1074/jbc.M117.816793
  13. Bonnet, J., et al. (2018). Nascent teichoic acids insertion into the cell wall directs the localization and activity of the major pneumococcal autolysin LytA. The Cell Surface. 2:24-37. doi: https://doi.org/10.1016/j.tcsw.2018.05.001
  14. Boussambe, G. N. M., et al. (2018). Fluorinated diglucose detergents for membrane-protein extraction. Methods. 147:84-94. doi: https://doi.org/10.1016/j.ymeth.2018.05.025
  15. Campbell, R. A., et al. (2018). Adsorption of Denaturated Lysozyme at the Air-Water Interface: Structure and Morphology. Langmuir. 34(17):5020-5029. doi: 10.1021/acs.langmuir.8b00545
  16. Cantini, F., et al. (2018). Structural Knowledge for Molecular Optimization: The Cases of Metal-Mediated Protein–Protein Interactions and Structural Vaccinology. European Journal of Inorganic Chemistry. 2018(37):4108-4116. doi: 10.1002/ejic.201800699
  17. Cantini, F., et al. (2018). Interaction of Half Oxa-/Half cis-Platin Complex with Human Superoxide Dismutase and Induced Reduction of Neurotoxicity. ACS Medicinal Chemistry Letters. 9(11):1094-1098. doi: 10.1021/acsmedchemlett.8b00199
  18. Capper, M. J., et al. (2018). The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation. Nature Communications. 9(1):1693. doi: 10.1038/s41467-018-04114-x
  19. Caracausi, M., et al. (2018). Plasma and urinary metabolomic profiles of Down syndrome correlate with alteration of mitochondrial metabolism. Scientific Reports. 8(1):2977. doi: 10.1038/s41598-018-20834-y
  20. Carlon, A., et al. (2018). Joint X-ray/NMR structure refinement of multidomain/multisubunit systems. J Biomol NMR. doi: 10.1007/s10858-018-0212-3
  21. Cattiaux, L., et al. (2018). New branched amino acids for high affinity dendrimeric DC-SIGN ligands. Bioorg Med Chem. 26(5):1006-1015. doi: 10.1016/j.bmc.2017.12.036
  22. Cerofolini, L., et al. (2018). Mechanism and Inhibition of Matrix Metalloproteinases. Curr Med Chem. doi: 10.2174/0929867325666180326163523
  23. Cerofolini, L., et al. (2018). Characterization of PEGylated asparaginase: new opportunities from NMR analysis of large pegylated therapeutics. Chemistry. doi: 10.1002/chem.201804488
  24. Cerofolini, L., et al. (2018). Long-range paramagnetic NMR data can provide a closer look on metal coordination in metalloproteins. Journal of Biological Inorganic Chemistry. 23(1):71-80. doi: 10.1007/s00775-017-1511-y
  25. Chatzikonstantinou, A. V., et al. (2018). Enriching the biological space of natural products and charting drug metabolites, through real time biotransformation monitoring: The NMR tube bioreactor. Biochimica et Biophysica Acta (BBA) - General Subjects. 1862(1):1-8. doi: https://doi.org/10.1016/j.bbagen.2017.09.021
  26. Che, T., et al. (2018). Structure of the Nanobody-Stabilized Active State of the Kappa Opioid Receptor. Cell. 172(1):55-67.e15. doi: https://doi.org/10.1016/j.cell.2017.12.011
  27. Checcucci, A., et al. (2018). Creation and Characterization of a Genomically Hybrid Strain in the Nitrogen-Fixing Symbiotic Bacterium Sinorhizobium meliloti. ACS Synthetic Biology. 7(10):2365-2378. doi: 10.1021/acssynbio.8b00158
  28. Chegkazi, M. S., et al. (2018). Rational Drug Design Using Integrative Structural Biology. Methods Mol Biol. 1824:89-111. doi: 10.1007/978-1-4939-8630-9_6
  29. Ciofi-Baffoni, S., et al. (2018). Protein networks in the maturation of human iron-sulfur proteins. Metallomics. 10(1):49-72. doi: 10.1039/c7mt00269f
  30. Colin, P., et al. (2018). CCR5 structural plasticity shapes HIV-1 phenotypic properties. PLoS Pathog. 14(12):e1007432. doi: 10.1371/journal.ppat.1007432
  31. Crespo, I., et al. (2018). Design, synthesis, structure-activity relationships and X-ray structural studies of novel 1-oxopyrimido 4,5-c quinoline-2-acetic acid derivatives as selective and potent inhibitors of human aldose reductase. European Journal of Medicinal Chemistry. 152:160-174. doi: 10.1016/j.ejmech.2018.04.015
  32. da Silveira Tome, C., et al. (2018). High concentrations of GTP induce conformational changes in the essential bacterial GTPase EngA and enhance its binding to the ribosome. Febs j. 285(1):160-177. doi: 10.1111/febs.14333
  33. Delaforge, E., et al. (2018). Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy. Journal of the American Chemical Society. 140(3):1148-1158. doi: 10.1021/jacs.7b12407
  34. Delbart, F., et al. (2018). An allosteric binding site of the alpha7 nicotinic acetylcholine receptor revealed in a humanized acetylcholine-binding protein. J Biol Chem. 293(7):2534-2545. doi: 10.1074/jbc.M117.815316
  35. Duyvesteyn, H. M. E., et al. (2018). Towards in cellulo virus crystallography. Scientific Reports. 8(1):3771. doi: 10.1038/s41598-018-21693-3
  36. Egan, A. J. F., et al. (2018). Induced conformational changes activate the peptidoglycan synthase PBP1B. Molecular Microbiology. 110(3):335-356. doi: 10.1111/mmi.14082
  37. Eiler, S., et al. (2018). Unstable Protein Purification Through the Formation of Stable Complexes. Methods Mol Biol. 1764:315-328. doi: 10.1007/978-1-4939-7759-8_20
  38. Eymard-Vernain, E., et al. (2018). Impact of a Model Soil Microorganism and of Its Secretome on the Fate of Silver Nanoparticles. Environ Sci Technol. 52(1):71-78. doi: 10.1021/acs.est.7b04071
  39. Faridounnia, M., et al. (2018). Function and Interactions of ERCC1-XPF in DNA Damage Response. Molecules. 23(12). doi: 10.3390/molecules23123205
  40. Floc’h, K., et al. (2018). Bacterial cell wall nanoimaging by autoblinking microscopy. Scientific Reports. 8(1):14038. doi: 10.1038/s41598-018-32335-z
  41. Flygaard, R. K., et al. (2018). Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism. Nature Communications. 9(1):4179. doi: 10.1038/s41467-018-06724-x
  42. Galilee, M., et al. (2018). The structure of FIV reverse transcriptase and its implications for non-nucleoside inhibitor resistance. PLoS Pathog. 14(1):e1006849. doi: 10.1371/journal.ppat.1006849
  43. Garcia-Maurino, S. M., et al. (2018). A putative RNA binding protein from Plasmodium vivax apicoplast. FEBS Open Bio. 8(2):177-188. doi: 10.1002/2211-5463.12351
  44. Garcia-Saez, I., et al. (2018). Structure of an H1-Bound 6-Nucleosome Array Reveals an Untwisted Two-Start Chromatin Fiber Conformation. Molecular Cell. doi: https://doi.org/10.1016/j.molcel.2018.09.027
  45. Genna, V., et al. (2018). Second-Shell Basic Residues Expand the Two-Metal-Ion Architecture of DNA and RNA Processing Enzymes. Structure. 26(1):40-50.e2. doi: https://doi.org/10.1016/j.str.2017.11.008
  46. Gigli, L., et al. (2018). Assessing protein conformational landscapes: integration of DEER data in Maximum Occurrence analysis. Phys Chem Chem Phys. 20(43):27429-27438. doi: 10.1039/c8cp06195e
  47. Gogoi, P., et al. (2018). Aromatic-Based Design of Highly Active and Noncalcemic Vitamin D Receptor Agonists. Journal of Medicinal Chemistry. 61(11):4928-4937. doi: 10.1021/acs.jmedchem.8b00337
  48. Gourdoupis, S., et al. (2018). IBA57 Recruits ISCA2 to Form a [2Fe-2S] Cluster-Mediated Complex. Journal of the American Chemical Society. 140(43):14401-14412. doi: 10.1021/jacs.8b09061
  49. Grigoras, I., et al. (2018). Nanovirus DNA-N encodes a protein mandatory for aphid transmission. Virology. 522:281-291. doi: 10.1016/j.virol.2018.07.001
  50. Grimaldi, M., et al. (2018). Structural basis of antiviral activity of peptides from MPER of FIV gp36. PLOS ONE. 13(9):e0204042. doi: 10.1371/journal.pone.0204042
  51. Grimes, J. M., et al. (2018). Where is crystallography going? Acta Crystallographica Section D. 74(2):152-166. doi: doi:10.1107/S2059798317016709
  52. Guo, X., et al. (2018). Structural Basis for NusA Stabilized Transcriptional Pausing. Mol Cell. 69(5):816-827.e4. doi: 10.1016/j.molcel.2018.02.008
  53. Halby, L., et al. (2018). Hijacking DNA methyltransferase transition state analogues to produce chemical scaffolds for PRMT inhibitors. Philosophical Transactions of the Royal Society B-Biological Sciences. 373(1748):15. doi: 10.1098/rstb.2017.0072
  54. Heymann, J. B., et al. (2018). The first single particle analysis Map Challenge: A summary of the assessments. Journal of Structural Biology. 204(2):291-300. doi: https://doi.org/10.1016/j.jsb.2018.08.010
  55. Howard, E., et al. (2018). Structural Basis of Outstanding Multivalent Effects in Jack Bean -Mannosidase Inhibition. Angewandte Chemie-International Edition. 57(27):8002-8006. doi: 10.1002/anie.201801202
  56. Jacq, M., et al. (2018). The cell wall hydrolase Pmp23 is important for assembly and stability of the division ring in Streptococcus pneumoniae. Scientific Reports. 8(1):7591. doi: 10.1038/s41598-018-25882-y
  57. Jacquet, M., et al. (2018). C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on CCP24-25 Modules. Front Immunol. 9:453. doi: 10.3389/fimmu.2018.00453
  58. Jiménez, A., et al. (2018). Validation of electron microscopy initial models via small angle X-ray scattering curves. Bioinformatics. 35(14):2427-2433. doi: 10.1093/bioinformatics/bty985
  59. Karmakar, A., et al. (2018). Cu(II)-Doped Cs2SbAgCl6 Double Perovskite: A Lead-Free, Low-Bandgap Material. Chemistry of Materials. 30(22):8280-8290. doi: 10.1021/acs.chemmater.8b03755
  60. Khalturin, K., et al. (2018). NR3E receptors in cnidarians: A new family of steroid receptor relatives extends the possible mechanisms for ligand binding. J Steroid Biochem Mol Biol. 184:11-19. doi: 10.1016/j.jsbmb.2018.06.014
  61. Kohler, M., et al. (2018). Binding Specificities of Nanobody center dot Membrane Protein Complexes Obtained from Chemical Cross-Linking and High-Mass MALDI Mass Spectrometry. Analytical Chemistry. 90(8):5306-5313. doi: 10.1021/acs.analchem.8b00236
  62. Kolesnikova, O., et al. (2018). Molecular structure of promoter-bound yeast TFIID. Nature Communications. 9(1):4666. doi: 10.1038/s41467-018-07096-y
  63. Koning, R. I., et al. (2018). Advances in cryo-electron tomography for biology and medicine. Annals of Anatomy - Anatomischer Anzeiger. 217:82-96. doi: https://doi.org/10.1016/j.aanat.2018.02.004
  64. Kovalevskiy, O., et al. (2018). Overview of refinement procedures within REFMAC5: utilizing data from different sources. Acta Crystallogr D Struct Biol. 74(Pt 3):215-227. doi: 10.1107/s2059798318000979
  65. Kovaľová, T., et al. (2018). Active site complementation and hexameric arrangement in the GH family 29, a structure–function study of α-l-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus. Glycobiology. 29(1):59-73. doi: 10.1093/glycob/cwy078
  66. Kumar, H., et al. (2018). Crystal Structure of a ligand-bound LacY-Nanobody Complex. Proceedings of the National Academy of Sciences of the United States of America. 115(35):8769-8774. doi: 10.1073/pnas.1801774115
  67. Lee, S., et al. (2018). Structures of beta-klotho reveal a 'zip code'-like mechanism for endocrine FGF signalling. Nature. 553(7689):501-+. doi: 10.1038/nature25010
  68. Lin, Y. H., et al. (2018). RavN is a member of a previously unrecognized group of Legionella pneumophila E3 ubiquitin ligases. PLoS Pathog. 14(2):e1006897. doi: 10.1371/journal.ppat.1006897
  69. Lin, Z. T., et al. (2018). Investigation of 20S-hydroxyvitamin D-3 analogs and their 1 alpha-OH derivatives as potent vitamin D receptor agonists with anti-inflammatory activities. Scientific Reports. 8:11. doi: 10.1038/s41598-018-19183-7
  70. Liu, W.-Q., et al. (2018). 1,2-Diol Dehydration by the Radical SAM Enzyme AprD4: A Matter of Proton Circulation and Substrate Flexibility. Journal of the American Chemical Society. 140(4):1365-1371. doi: 10.1021/jacs.7b10501
  71. Louka, A., et al. (2018). Engineering l-asparaginase for spontaneous formation of calcium phosphate bioinspired microreactors. Phys Chem Chem Phys. doi: 10.1039/c8cp00419f
  72. Luchinat, E., et al. (2018). In-Cell NMR in Human Cells: Direct Protein Expression Allows Structural Studies of Protein Folding and Maturation. Accounts of Chemical Research. 51(6):1550-1557. doi: 10.1021/acs.accounts.8b00147
  73. Maione, V., et al. (2018). Investigating the role of the human CIA2A-CIAO1 complex in the maturation of aconitase. Biochimica Et Biophysica Acta-General Subjects. 1862(9):1980-1987. doi: 10.1016/j.bbagen.2018.05.019
  74. Malabirade, A., et al. (2018). The RNA Complement of Outer Membrane Vesicles From Salmonella enterica Serovar Typhimurium Under Distinct Culture Conditions. Frontiers in Microbiology. 9(2015). doi: 10.3389/fmicb.2018.02015
  75. Marchanka, A., et al. (2018). Rapid access to RNA resonances by proton-detected solid-state NMR at > 100 kHz MAS. Chemical Communications. 54(65):8972-8975. doi: 10.1039/c8cc04437f
  76. Marek, M., et al. (2018). Characterization of Histone Deacetylase 8 (HDAC8) Selective Inhibition Reveals Specific Active Site Structural and Functional Determinants. J Med Chem. 61(22):10000-10016. doi: 10.1021/acs.jmedchem.8b01087
  77. Marra, A., et al. (2018). Protein Glycosylation through Sulfur Fluoride Exchange (SuFEx) Chemistry: The Key Role of a Fluorosulfate Thiolactoside. Chemistry. doi: 10.1002/chem.201803912
  78. Martino, F., et al. (2018). RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex. Nat Commun. 9(1):1501. doi: 10.1038/s41467-018-03942-1
  79. Mas, G., et al. (2018). Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. Science Advances. 4(9). doi:
  80. Mateos, B., et al. (2018). NMR characterization of long-range contacts in intrinsically disordered proteins from paramagnetic relaxation enhancement in 13C direct-detected experiments. Chembiochem. doi: 10.1002/cbic.201800539
  81. Mazur, M., et al. (2018). Targeting Acidic Mammalian chitinase Is Effective in Animal Model of Asthma. Journal of Medicinal Chemistry. 61(3):695-710. doi: 10.1021/acs.jmedchem.7b01051
  82. Melcr, J., et al. (2018). Accurate Binding of Sodium and Calcium to a POPC Bilayer by Effective Inclusion of Electronic Polarization. Journal of Physical Chemistry B. 122(16):4546-4557. doi: 10.1021/acs.jpcb.7b12510
  83. Mikulecky, P., et al. (2018). Human viperin catalyzes the modification of GPP and FPP potentially affecting cholesterol synthesis. FEBS Lett. 592(2):199-208. doi: 10.1002/1873-3468.12941
  84. Milles, S., et al. (2018). An ultraweak interaction in the intrinsically disordered replication machinery is essential for measles virus function. Science Advances. 4(8):10. doi: 10.1126/sciadv.aat7778
  85. Mitri, E., et al. (2018). (15)N isotopic labelling for in-cell protein studies by NMR spectroscopy and single-cell IR synchrotron radiation FTIR microscopy: a correlative study. Analyst. 143(5):1171-1181. doi: 10.1039/c7an01464c
  86. Mizuta, R., et al. (2018). Dynamic self-assembly of DNA minor groove-binding ligand DB921 into nanotubes triggered by an alkali halide. Nanoscale. 10(12):5550-5558. doi: 10.1039/c7nr03875e
  87. Monte, D., et al. (2018). Crystal structure of human Mediator subunit MED23. Nature Communications. 9:7. doi: 10.1038/s41467-018-05967-y
  88. Moroni, A., et al. (2018). Structure-guided design of a cell penetrating peptide preventing cAMP modulation of HCN channels. bioRxiv. doi: 10.1101/253096
  89. Moulin, M., et al. (2018). Perdeuteration of cholesterol for neutron scattering applications using recombinant Pichia pastoris. Chem Phys Lipids. 212:80-87. doi: 10.1016/j.chemphyslip.2018.01.006
  90. Murillo, J. L., et al. (2018). Nucleoprotein from the unique human infecting Orthobunyavirus of Simbu serogroup (Oropouche virus) forms higher order oligomers in complex with nucleic acids in vitro. Amino Acids. doi: 10.1007/s00726-018-2560-4
  91. Murrali, M. G., et al. (2018). Proline Fingerprint in Intrinsically Disordered Proteins. Chembiochem. 19(15):1625-1629. doi: 10.1002/cbic.201800172
  92. Murrali, M. G., et al. (2018). 13C APSY-NMR for sequential assignment of intrinsically disordered proteins. Journal of Biomolecular NMR. 70(3):167-175. doi: 10.1007/s10858-018-0167-4
  93. Natchiar, S. K., et al. (2018). Visualizing the Role of 2'-OH rRNA Methylations in the Human Ribosome Structure. Biomolecules. 8(4). doi: 10.3390/biom8040125
  94. Orelle, C., et al. (2018). A multidrug ABC transporter with a taste for GTP. Scientific Reports. 8(1):2309. doi: 10.1038/s41598-018-20558-z
  95. Orlov, I., et al. (2018). Structural features of the salivary gland hypertrophy virus of the tsetse fly revealed by cryo-electron microscopy and tomography. Virology. 514:165-169. doi: 10.1016/j.virol.2017.11.016
  96. Osmani, N., et al. (2018). An Arf6- and caveolae-dependent pathway links hemidesmosome remodeling and mechanoresponse. Mol Biol Cell. 29(4):435-451. doi: 10.1091/mbc.E17-06-0356
  97. Parigi, G. B., Ladislav; Ravera, Enrico; Romanelli, Maurizio; Luchinat, Claudio (2018). Pseudocontact shifts and paramagnetic susceptibility in classical and quantum chemistry theories. ArXiv e-prints. doi:
  98. Pellegrini, E., et al. (2018). RIP2 filament formation is required for NOD2 dependent NF-κB signalling. Nature Communications. 9(1):4043. doi: 10.1038/s41467-018-06451-3
  99. Pfanzagl, V., et al. (2018). Roles of distal aspartate and arginine of B-class dye-decolorizing peroxidase in heterolytic hydrogen peroxide cleavage. Journal of Biological Chemistry. 293(38):14823-14838. doi: 10.1074/jbc.RA118.004773
  100. Pflug, A., et al. (2018). Capped RNA primer binding to influenza polymerase and implications for the mechanism of cap-binding inhibitors. Nucleic Acids Research. 46(2):956-971. doi: 10.1093/nar/gkx1210
  101. Polovinkin, L., et al. (2018). Conformational transitions of the serotonin 5-HT3 receptor. Nature. 563(7730):275-279. doi: 10.1038/s41586-018-0672-3
  102. Prezel, E., et al. (2018). Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles. Molecular Biology of the Cell. 29(2):154-165. doi: 10.1091/mbc.E17-06-0429
  103. Putignano, V., et al. (2018). MetalPDB in 2018: a database of metal sites in biological macromolecular structures. Nucleic Acids Res. 46(D1):D459-d464. doi: 10.1093/nar/gkx989
  104. Ravera, E., et al. (2018). Paramagnetic NMR as a new tool in structural biology. Emerging Topics in Life Sciences. doi: 10.1042/etls20170084
  105. Ravera, E., et al. (2018). NMR Spectroscopy and Metal Ions in Life Sciences. European Journal of Inorganic Chemistry. 2018(44):4752-4770. doi: 10.1002/ejic.201800875
  106. Ren, J., et al. (2018). Target Identification and Mode of Action of Four Chemically Divergent Drugs against Ebolavirus Infection. Journal of Medicinal Chemistry. 61(3):724-733. doi: 10.1021/acs.jmedchem.7b01249
  107. Richardson, J. S., et al. (2018). Model validation: local diagnosis, correction and when to quit. Acta Crystallographica Section D. 74(2):132-142. doi: doi:10.1107/S2059798317009834
  108. Roca, C., et al. (2018). Deciphering the Inhibition of the Neuronal Calcium Sensor 1 and the Guanine Exchange Factor Ric8a with a Small Phenothiazine Molecule for the Rational Generation of Therapeutic Synapse Function Regulators. Journal of Medicinal Chemistry. 61(14):5910-5921. doi: 10.1021/acs.jmedchem.8b00088
  109. Sanchez-Garcia, R., et al. (2018). BIPSPI: a method for the prediction of partner-specific protein–protein interfaces. Bioinformatics. 35(3):470-477. doi: 10.1093/bioinformatics/bty647
  110. Saponaro, A., et al. (2018). A synthetic peptide that prevents cAMP regulation in mammalian hyperpolarization-activated cyclic nucleotide-gated (HCN) channels. Elife. 7. doi: 10.7554/eLife.35753
  111. Schlauderer, F., et al. (2018). Molecular architecture and regulation of BCL10-MALT1 filaments. Nature Communications. 9(1):4041. doi: 10.1038/s41467-018-06573-8
  112. Schult, P., et al. (2018). microRNA-122 amplifies hepatitis C virus translation by shaping the structure of the internal ribosomal entry site. Nature Communications. 9(1):2613. doi: 10.1038/s41467-018-05053-3
  113. Schulze, W. M., et al. (2018). Structural analysis of human ARS2 as a platform for co-transcriptional RNA sorting. Nature Communications. 9:15. doi: 10.1038/s41467-018-04142-7
  114. Silva, J. M., et al. (2018). Non-crystallographic symmetry in proteins: Jahn-Teller-like and Butterfly-like effects? J Biol Inorg Chem. doi: 10.1007/s00775-018-1630-0
  115. Simoben, C. V., et al. (2018). A Novel Class of Schistosoma mansoni Histone Deacetylase 8 (HDAC8) Inhibitors Identified by Structure-Based Virtual Screening and In Vitro Testing. Molecules. 23(3). doi: 10.3390/molecules23030566
  116. Simonini, S., et al. (2018). Auxin sensing is a property of an unstructured domain in the Auxin Response Factor ETTIN of Arabidopsis thaliana. Scientific Reports. 8(1):13563. doi: 10.1038/s41598-018-31634-9
  117. Stolt-Bergner, P., et al. (2018). Baculovirus-driven protein expression in insect cells: A benchmarking study. Journal of Structural Biology. 203(2):71-80. doi: 10.1016/j.jsb.2018.03.004
  118. Suarez, I., et al. (2018). Structural Insights in Multifunctional Papillomavirus Oncoproteins. Viruses-Basel. 10(1):22. doi: 10.3390/v10010037
  119. Suarez, I. P., et al. (2018). Conformational sampling of the intrinsically disordered dsRBD-1 domain from Arabidopsis thaliana DCL1. Phys Chem Chem Phys. 20(16):11237-11246. doi: 10.1039/c7cp07908g
  120. Szekely, O., et al. (2018). High-Resolution 2D NMR of Disordered Proteins Enhanced by Hyperpolarized Water. Anal Chem. doi: 10.1021/acs.analchem.8b00585
  121. Tacnet-Delorme, P., et al. (2018). Proteinase 3 Interferes With C1q-Mediated Clearance of Apoptotic Cells. Frontiers in Immunology. 9:9. doi: 10.3389/fimmu.2018.00818
  122. Takis, P. G., et al. (2018). Fingerprinting Acute Digestive Diseases by Untargeted NMR Based Metabolomics. Int J Mol Sci. 19(11). doi: 10.3390/ijms19113288
  123. Thielens, N. M., et al. (2018). Impact of the surface charge of polydiacetylene micelles on their interaction with human innate immune protein C1q and the complement system. Int J Pharm. 536(1):434-439. doi: 10.1016/j.ijpharm.2017.11.072
  124. Timr, S., et al. (2018). Calcium Sensing by Recoverin: Effect of Protein Conformation on Ion Affinity. Journal of Physical Chemistry Letters. 9(7):1613-1619. doi: 10.1021/acs.jpclett.8b00495
  125. Trundova, M., et al. (2018). Highly stable single-strand-specific 3'-nuclease/nucleotidase from Legionella pneumophila. Int J Biol Macromol. 114:776-787. doi: 10.1016/j.ijbiomac.2018.03.113
  126. van Beusekom, B., et al. (2018). Characterization and structure determination of a llama-derived nanobody targeting the J-base binding protein 1. Acta Crystallogr F Struct Biol Commun. 74(Pt 11):690-695. doi: 10.1107/s2053230x18010282
  127. Vilas, J. L., et al. (2018). MonoRes: Automatic and Accurate Estimation of Local Resolution for Electron Microscopy Maps. Structure. 26(2):337-344.e4. doi: 10.1016/j.str.2017.12.018
  128. von Loeffelholz, O., et al. (2018). Volta phase plate data collection facilitates image processing and cryo-EM structure determination. Journal of Structural Biology. doi: https://doi.org/10.1016/j.jsb.2018.01.003
  129. Vosegaard, T. (2018). Fast simulations of multidimensional NMR spectra of proteins and peptides. Magn Reson Chem. 56(6):438-448. doi: 10.1002/mrc.4663
  130. Wang, Y., et al. (2018). The cellular economy of the Saccharomyces cerevisiae zinc proteome. Metallomics. doi: 10.1039/C8MT00269J
  131. Weinhäupl, K., et al. (2018). Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space. Cell. 175(5):1365-1379.e25. doi: https://doi.org/10.1016/j.cell.2018.10.039
  132. Wienen-Schmidt, B., et al. (2018). Paradoxically, Most Flexible Ligand Binds Most Entropy-Favored: Intriguing Impact of Ligand Flexibility and Solvation on Drug-Kinase Binding. J Med Chem. doi: 10.1021/acs.jmedchem.8b00105
  133. Woznicka-Misaila, A., et al. (2018). Cell-free production, purification and characterization of human mitochondrial ADP/ATP carriers. Protein Expression and Purification. 144:46-54. doi: https://doi.org/10.1016/j.pep.2017.11.008
  134. Wright, G. S. A., et al. (2018). Architecture of the complete oxygen-sensing FixL-FixJ two-component signal transduction system. Sci Signal. 11(525). doi: 10.1126/scisignal.aaq0825
  135. Xiang, S., et al. (2018). Site-Specific Studies of Nucleosome Interactions by Solid-State NMR. Angew Chem Int Ed Engl. doi: 10.1002/anie.201713158
  136. Zhang, X., et al. (2018). Macromolecular pHPMA-Based Nanoparticles with Cholesterol for Solid Tumor Targeting: Behavior in HSA Protein Environment. Biomacromolecules. 19(2):470-480. doi: 10.1021/acs.biomac.7b01579
  137. Zhao, Y., et al. (2018). Structures of Ebola Virus Glycoprotein Complexes with Tricyclic Antidepressant and Antipsychotic Drugs. J Med Chem. 61(11):4938-4945. doi: 10.1021/acs.jmedchem.8b00350
  138. Zouhir, S., et al. (2018). Assembly of an atypical α-macroglobulin complex from Pseudomonas aeruginosa. Scientific Reports. 8(1):527. doi: 10.1038/s41598-017-18083-6

2017

  1. Adriaenssens, E. M., et al. (2017). Taxonomy of prokaryotic viruses: 2016 update from the ICTV bacterial and archaeal viruses subcommittee. Archives of Virology, 162(4), 1153-1157. doi:10.1007/s00705-016-3173-4
  2. Albanese, P., et al. (2017). Pea PSII-LHCII supercomplexes form pairs by making connections across the stromal gap. Scientific Reports, 7. doi:10.1038/s41598-017-10700-8
  3. Allorent, G., et al. (2017). Photoreceptor-dependent regulation of photoprotection. Curr Opin Plant Biol, 37, 102-108. doi:10.1016/j.pbi.2017.03.016
  4. Amadori, C., et al. (2017). The HIV-1 integrase-LEDGF allosteric inhibitor MUT-A: resistance profile, impairment of virus maturation and infectivity but without influence on RNA packaging or virus immunoreactivity. Retrovirology, 14, 50. doi:10.1186/s12977-017-0373-2
  5. Anderson, L., et al. (2017). Histone deacetylase inhibition modulates histone acetylation at gene promoter regions and affects genome-wide gene transcription in Schistosoma mansoni. Plos Neglected Tropical Diseases, 11(4). doi:10.1371/journal.pntd.0005539
  6. Andrałojć, W., et al. (2017). Identification of productive and futile encounters in an electron transfer protein complex. Proceedings of the National Academy of Sciences of the United States of America, 114(10), E1840-E1847. doi:10.1073/pnas.1616813114
  7. Andralojc, W., et al. (2017). Identification of productive and futile encounters in an electron transfer protein complex. Proc Natl Acad Sci U S A, 114(10), E1840-e1847. doi:10.1073/pnas.1616813114
  8. Anumala, U. R., et al. (2017). Discovery of a Novel Series of Tankyrase Inhibitors by a Hybridization Approach. Journal of Medicinal Chemistry, 60(24), 10013-10025. doi:10.1021/acs.jmedchem.7b00883
  9. Arnaud, C.-A., et al. (2017). Bacteriophage T5 tail tube structure suggests a trigger mechanism for Siphoviridae DNA ejection. Nature Communications, 8(1), 1953. doi:10.1038/s41467-017-02049-3
  10. Atherton, J., et al. (2017). The divergent mitotic kinesin MKLP2 exhibits atypical structure and mechanochemistry. Elife, 6. doi:10.7554/eLife.27793
  11. Awad, R., et al. (2017). Structural insights into the substrate recognition and reaction specificity of the PLP-dependent fold-type I isoleucine 2-epimerase from Lactobacillus buchneri. Biochimie, 137, 165-173. doi:10.1016/j.biochi.2017.03.015
  12. Baquero, E., et al. (2017). Structural intermediates in the fusion-associated transition of vesiculovirus glycoprotein. Embo j, 36(5), 679-692. doi:10.15252/embj.201694565
  13. Baran, D., et al. (2017). Principles for computational design of binding antibodies. Proc Natl Acad Sci U S A, 114(41), 10900-10905. doi:10.1073/pnas.1707171114
  14. Barker, C. E., et al. (2017). CCL2 nitration is a negative regulator of chemokine-mediated inflammation. Sci Rep, 7, 44384. doi:10.1038/srep44384
  15. Baronti, L., et al. (2017). Fragment-Based NMR Study of the Conformational Dynamics in the bHLH Transcription Factor Ascl1. Biophys J, 112(7), 1366-1373. doi:10.1016/j.bpj.2017.02.025
  16. Barros-Álvarez, X., et al. (2017). Leishmania donovani tyrosyl-tRNA synthetase structure in complex with a tyrosyl adenylate analog and comparisons with human and protozoan counterparts. Biochimie, 138, 124-136. doi:https://doi.org/10.1016/j.biochi.2017.04.006
  17. Basso, P., et al. (2017). Pseudomonas aeruginosa Pore-Forming Exolysin and Type IV Pili Cooperate To Induce Host Cell Lysis. MBio, 8(1). doi:10.1128/mBio.02250-16
  18. Bednar, J., et al. (2017). Structure and Dynamics of a 197 bp Nucleosome in Complex with Linker Histone H1. Molecular Cell, 66(3), 384-+. doi:10.1016/j.molcel.2017.04.012
  19. Belorusova, A. Y., et al. (2017). Structure-activity relationship study of vitamin D analogs with oxolane group in their side chain. European Journal of Medicinal Chemistry, 134, 86-96. doi:10.1016/j.ejmech.2017.03.081
  20. Belorusova, A. Y., et al. (2017). Structural analysis and biological activities of BXL0124, a gemini analog of vitamin D. Journal of Steroid Biochemistry and Molecular Biology, 173, 69-74. doi:10.1016/j.jsbmb.2016.09.015
  21. Benleulmi, M. S., et al. (2017). Modulation of the functional association between the HIV-1 intasome and the nucleosome by histone amino-terminal tails. Retrovirology, 14. doi:10.1186/s12977-017-0378-x
  22. Bernacchioni, C., et al. (2017). NMR metabolomics highlights sphingosine kinase-1 as a new molecular switch in the orchestration of aberrant metabolic phenotype in cancer cells. Mol Oncol, 11(5), 517-533. doi:10.1002/1878-0261.12048
  23. Bersch, B., et al. (2017). Proton-Detected Solid-State NMR Spectroscopy of a Zinc Diffusion Facilitator Protein in Native Nanodiscs. Angew Chem Int Ed Engl, 56(9), 2508-2512. doi:10.1002/anie.201610441
  24. Bersch, B., et al. (2017). Protonendetektierte Festkörper-NMR-Spektroskopie an einem Zinktransporter-Membranprotein in nativen Nanoscheiben. Angewandte Chemie, 129(9), 2549-2553. doi:10.1002/ange.201610441
  25. Bertarello, A., et al. (2017). Paramagnetic Properties of a Crystalline Iron-Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy. Inorganic Chemistry, 56(11), 6624-6629. doi:10.1021/acs.inorgchem.7b00674
  26. Bertolotti, B., et al. (2017). Polyvalent C-glycomimetics based on l-fucose or d-mannose as potent DC-SIGN antagonists. Organic & Biomolecular Chemistry, 15(18), 3995-4004. doi:10.1039/C7OB00322F
  27. Bharat, T. A. M., et al. (2017). Structure of the hexagonal surface layer on Caulobacter crescentus cells. Nat Microbiol, 2, 17059. doi:10.1038/nmicrobiol.2017.59
  28. Bhat, J. Y., et al. (2017). Mechanism of Enzyme Repair by the AAA+ Chaperone Rubisco Activase. Molecular Cell, 67(5), 744-756.e746. doi:https://doi.org/10.1016/j.molcel.2017.07.004
  29. Bláha, J., et al. (2017). High-level expression and purification of soluble form of human natural killer cell receptor NKR-P1 in HEK293S GnTI− cells. Protein Expression and Purification, 140, 36-43. doi:https://doi.org/10.1016/j.pep.2017.07.016
  30. Bonnet, J., et al. (2017). Autocatalytic association of proteins by covalent bond formation: a Bio Molecular Welding toolbox derived from a bacterial adhesin. Sci Rep, 7, 43564. doi:10.1038/srep43564
  31. Bonnet, J., et al. (2017). Peptidoglycan O-acetylation is functionally related to cell wall biosynthesis and cell division in Streptococcus pneumoniae. Mol Microbiol, 106(5), 832-846. doi:10.1111/mmi.13849
  32. Bouillot, S., et al. (2017). Pseudomonas aeruginosa Exolysin promotes bacterial growth in lungs, alveolar damage and bacterial dissemination. Scientific Reports, 7(1), 2120. doi:10.1038/s41598-017-02349-0
  33. Bradley, A. R., et al. (2017). The SGC beyond structural genomics: redefining the role of 3D structures by coupling genomic stratification with fragment-based discovery. Essays Biochem, 61(5), 495-503. doi:10.1042/ebc20170051
  34. Brancaccio, D., et al. (2017). 4Fe-4S Cluster Assembly in Mitochondria and Its Impairment by Copper. Journal of the American Chemical Society, 139(2), 719-730. doi:10.1021/jacs.6b09567
  35. Brault, J., et al. (2017). Therapeutic effects of proteoliposomes on X-linked chronic granulomatous disease: proof of concept using macrophages differentiated from patient-specific induced pluripotent stem cells. Int J Nanomedicine, 12, 2161-2177. doi:10.2147/ijn.S128611
  36. Bruno, S., et al. (2017). Magnesium and calcium ions differentially affect human serine racemase activity and modulate its quaternary equilibrium toward a tetrameric form. Biochimica Et Biophysica Acta-Proteins and Proteomics, 1865(4), 381-387. doi:10.1016/j.bbapap.2017.01.001
  37. Calderone, V., et al. (2017). Solving the crystal structure of human calcium-free S100Z: the siege and conquer of one of the last S100 family strongholds. Journal of Biological Inorganic Chemistry, 22(4), 519-526. doi:10.1007/s00775-017-1437-4
  38. Calvez, P., et al. (2017). Substitutions in PBP2b from beta-Lactam-resistant Streptococcus pneumoniae Have Different Effects on Enzymatic Activity and Drug Reactivity. J Biol Chem, 292(7), 2854-2865. doi:10.1074/jbc.M116.764696
  39. Cao, S. Y., et al. (2017). Structural Insight into Ubiquitin-Like Protein Recognition and Oligomeric States of JAMM/MPNI+ Proteases. Structure, 25(6), 823-+. doi:10.1016/j.str.2017.04.002
  40. Cerofolini, L., et al. (2017). Synthesis and binding monitoring of a new nanomolar PAMAM-based matrix metalloproteinases inhibitor (MMPIs). Bioorganic & Medicinal Chemistry, 25(2), 523-527. doi:10.1016/j.bmc.2016.11.028
  41. Cerofolini, L., et al. (2017). High-Resolution Solid-State NMR Characterization of Ligand Binding to a Protein Immobilized in a Silica Matrix. Journal of Physical Chemistry B, 121(34), 8094-8101. doi:10.1021/acs.jpcb.7b05679
  42. Cerutti, N., et al. (2017). Antigp41 membrane proximal external region antibodies and the art of using the membrane for neutralization. Current Opinion in Hiv and Aids, 12(3), 250-256. doi:10.1097/coh.0000000000000364
  43. Chebaro, Y., et al. (2017). Allosteric Regulation in the Ligand Binding Domain of Retinoic Acid Receptor gamma. Plos One, 12(1). doi:10.1371/journal.pone.0171043
  44. Chen, G. F., et al. (2017). Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state. Nature Communications, 8. doi:10.1038/s41467-017-02056-4
  45. Collins, P. J., et al. (2017). Epithelial chemokine CXCL14 synergizes with CXCL12 via allosteric modulation of CXCR4. Faseb Journal, 31(7), 3084-3097. doi:10.1096/fj.201700013R
  46. Contreras-Martel, C., et al. (2017). Molecular architecture of the PBP2–MreC core bacterial cell wall synthesis complex. Nature Communications, 8(1), 776. doi:10.1038/s41467-017-00783-2
  47. Contreras-Martos, S., et al. (2017). Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. Scientific Reports, 7(1), 4676. doi:10.1038/s41598-017-04611-x
  48. Cuenca-Alba, J., et al. (2017). ScipionCloud: An integrative and interactive gateway for large scale cryo electron microscopy image processing on commercial and academic clouds. Journal of Structural Biology, 200(1), 20-27. doi:10.1016/j.jsb.2017.06.004
  49. Cuevas Arenas, R., et al. (2017). Fast Collisional Lipid Transfer Among Polymer-Bounded Nanodiscs. Scientific Reports, 7, 45875. doi:10.1038/srep45875 https://www.nature.com/articles/srep45875#supplementary-information
  50. Cura, V., et al. (2017). Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors. Febs Journal, 284(1), 77-96. doi:10.1111/febs.13953
  51. Dalzon, B., et al. (2017). Differential proteomics highlights macrophage-specific responses to amorphous silica nanoparticles. Nanoscale, 9(27), 9641-9658. doi:10.1039/c7nr02140b
  52. Das, D., et al. (2017). Single-stranded DNA Binding by the Helix-Hairpin-Helix Domain of XPF Protein Contributes to the Substrate Specificity of the ERCC1-XPF Protein Complex. J Biol Chem, 292(7), 2842-2853. doi:10.1074/jbc.M116.747857
  53. Demina, T., et al. (2017). HCIV-1 and Other Tailless Icosahedral Internal Membrane-Containing Viruses of the Family Sphaerolipoviridae. Viruses, 9(2), 32.
  54. Denay, G., et al. (2017). A flower is born: an update on Arabidopsis floral meristem formation. Curr Opin Plant Biol, 35, 15-22. doi:10.1016/j.pbi.2016.09.003
  55. Desravines, D. C., et al. (2017). Structural Characterization of the SMRT Corepressor Interacting with Histone Deacetylase 7. Scientific Reports, 7(1), 3678. doi:10.1038/s41598-017-03718-5
  56. Di Guilmi, A. M., et al. (2017). Specific and spatial labeling of choline-containing teichoic acids in Streptococcus pneumoniae by click chemistry. Chem Commun (Camb), 53(76), 10572-10575. doi:10.1039/c7cc05646j
  57. Dominguez Pardo, J. J., et al. (2017). Solubilization of lipids and lipid phases by the styrene–maleic acid copolymer. European Biophysics Journal, 46(1), 91-101. doi:10.1007/s00249-016-1181-7
  58. Dominguez Pardo, J. J., et al. (2017). Thermotropic properties of phosphatidylcholine nanodiscs bounded by styrene-maleic acid copolymers. Chem Phys Lipids, 208, 58-64. doi:10.1016/j.chemphyslip.2017.08.010
  59. Dunne, O., et al. (2017). Matchout deuterium labelling of proteins for small-angle neutron scattering studies using prokaryotic and eukaryotic expression systems and high cell-density cultures. Eur Biophys J, 46(5), 425-432. doi:10.1007/s00249-016-1186-2
  60. El Khatib, M., et al. (2017). Providencia stuartii form biofilms and floating communities of cells that display high resistance to environmental insults. Plos One, 12(3), e0174213. doi:10.1371/journal.pone.0174213
  61. Emily, S., et al. (2017). An effective introduction to structural crystallography using 1D Gaussian atoms. European Journal of Physics, 38(6), 065501.
  62. Engilberge, S., et al. (2017). Crystallophore: a versatile lanthanide complex for protein crystallography combining nucleating effects, phasing properties, and luminescence. Chemical Science, 8(9), 5909-5917. doi:10.1039/c7sc00758b
  63. Erez, Z., et al. (2017). Communication between viruses guides lysis-lysogeny decisions. Nature, 541(7638), 488-493. doi:10.1038/nature21049
  64. Ersayin, A., et al. (2017). Catalytically inactive Gla-domainless factor Xa binds to TFPI and restores ex vivo coagulation in hemophilia plasma. Haematologica, 102(12), e483-e485. doi:10.3324/haematol.2017.174037
  65. Eskelin, K., et al. (2017). Halophilic viruses with varying biochemical and biophysical properties are amenable to purification with asymmetrical flow field-flow fractionation. Extremophiles, 21(6), 1119-1132. doi:10.1007/s00792-017-0963-x
  66. Flori, S., et al. (2017). Plastid thylakoid architecture optimizes photosynthesis in diatoms. Nature Communications, 8, 15885. doi:10.1038/ncomms15885 https://www.nature.com/articles/ncomms15885#supplementary-information
  67. Fraga, H., et al. (2017). Solid-State NMR H-N-(C)-H and H-N-C-C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins. Chemphyschem, 18(19), 2697-2703. doi:10.1002/cphc.201700572
  68. Franco, R., et al. (2017). Optimized fast mixing device for real-time NMR applications. J Magn Reson, 281, 125-129. doi:10.1016/j.jmr.2017.05.016
  69. Franco, R., et al. (2017). Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR. J Am Chem Soc, 139(3), 1065-1068. doi:10.1021/jacs.6b12089
  70. Franco-Echevarria, E., et al. (2017). The crystal structure of mammalian inositol 1,3,4,5,6-pentakisphosphate 2-kinase reveals a new zinc-binding site and key features for protein function. Journal of Biological Chemistry, 292(25), 10534-10548. doi:10.1074/jbc.M117.780395
  71. Franco-Echevarria, E., et al. (2017). Crystallization and Preliminary X-Ray Diffraction Analysis of a Mammal Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase. Protein Journal, 36(4), 240-248. doi:10.1007/s10930-017-9717-y
  72. Gauto, D. F., et al. (2017). Protein conformational dynamics studied by (15)N and (1)H R1rho relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State Nucl Magn Reson, 87, 86-95. doi:10.1016/j.ssnmr.2017.04.002
  73. Ginn, H. M., et al. (2017). The slip-and-slide algorithm: a refinement protocol for detector geometry. Journal of Synchrotron Radiation, 24(Pt 6), 1152-1162. doi:10.1107/S1600577517013327
  74. Giuntini, S., et al. (2017). Characterization of the Conjugation Pattern in Large Polysaccharide-Protein Conjugates by NMR Spectroscopy. Angewandte Chemie-International Edition, 56(47), 14997-15001. doi:10.1002/anie.201709274
  75. Giuntini, S., et al. (2017). Atomic structural details of a protein grafted onto gold nanoparticles. Scientific Reports, 7. doi:10.1038/s41598-017-18109-z
  76. Goosens, V. J., et al. (2017). Reconstitution of a minimal machinery capable of assembling periplasmic type IV pili. Proceedings of the National Academy of Sciences of the United States of America, 114(25), E4978-E4986. doi:10.1073/pnas.1618539114
  77. Gotthard, G., et al. (2017). Chromophore Isomer Stabilization Is Critical to the Efficient Fluorescence of Cyan Fluorescent Proteins. Biochemistry, 56(49), 6418-6422. doi:10.1021/acs.biochem.7b01088
  78. Gray, E. R., et al. (2017). Unravelling the Molecular Basis of High Affinity Nanobodies against HIV p24: In Vitro Functional, Structural, and in Silico Insights. ACS Infect Dis, 3(7), 479-491. doi:10.1021/acsinfecdis.6b00189
  79. Gushchin, I., et al. (2017). Mechanism of transmembrane signaling by sensor histidine kinases. Science, 356(6342). doi:10.1126/science.aah6345
  80. Hajjar, C., et al. (2017). The NOX Family of Proteins Is Also Present in Bacteria. MBio, 8(6). doi:10.1128/mBio.01487-17
  81. Haselbach, D., et al. (2017). Long-range allosteric regulation of the human 26S proteasome by 20S proteasome-targeting cancer drugs. Nature Communications, 8. doi:10.1038/ncomms15578
  82. Henrich, E., et al. (2017). Analyzing native membrane protein assembly in nanodiscs by combined non-covalent mass spectrometry and synthetic biology. Elife, 6. doi:10.7554/eLife.20954
  83. Henriet, E., et al. (2017). A jasmonic acid derivative improves skin healing and induces changes in proteoglycan expression and glycosaminoglycan structure. Biochim Biophys Acta, 1861(9), 2250-2260. doi:10.1016/j.bbagen.2017.06.006
  84. Hoang, T. V., et al. (2017). Automatic segmentation of high pressure frozen and freeze-substituted mouse retina nuclei from FIB-SEM tomograms. Journal of Structural Biology, 197(2), 123-134. doi:10.1016/j.jsb.2016.10.005
  85. Ibrahim, Z., et al. (2017). Time-resolved neutron scattering provides new insight into protein substrate processing by a AAA+ unfoldase. Scientific Reports, 7, 40948. doi:10.1038/srep40948 https://www.nature.com/articles/srep40948#supplementary-information
  86. Ishchenko, A., et al. (2017). New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex. Scientific Reports, 7, 41811. doi:10.1038/srep41811 https://www.nature.com/articles/srep41811#supplementary-information
  87. Juillan-Binard, C., et al. (2017). A Two-component NADPH Oxidase (NOX)-like System in Bacteria Is Involved in the Electron Transfer Chain to the Methionine Sulfoxide Reductase MsrP. J Biol Chem, 292(6), 2485-2494. doi:10.1074/jbc.M116.752014
  88. Kaczmarska, Z., et al. (2017). Structure of p300 in complex with acyl-CoA variants. Nat Chem Biol, 13(1), 21-29. doi:10.1038/nchembio.2217
  89. Kalliokoski, S., et al. (2017). Transglutaminase 2-specific coeliac disease autoantibodies induce morphological changes and signs of inflammation in the small-bowel mucosa of mice. Amino Acids, 49(3), 529-540. doi:10.1007/s00726-016-2306-0
  90. Kalouskova, B., et al. (2017). Recombinant expression of natural killer cell activating immunocomplex NKp80:AICL and its structural characterisation. Febs Journal, 284, 192-192.
  91. Karuppasamy, M., et al. (2017). Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2. Nature Communications, 8(1), 1729. doi:10.1038/s41467-017-01862-0
  92. Kilin, V., et al. (2017). Dynamics of Methylated Cytosine Flipping by UHRF1. Journal of the American Chemical Society, 139(6), 2520-2528. doi:10.1021/jacs.7b00154
  93. Kurauskas, V., et al. (2017). Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. Nat Commun, 8(1), 145. doi:10.1038/s41467-017-00165-8
  94. Labaronne, A., et al. (2017). Structural analysis of the complex between influenza B nucleoprotein and human importin-α. Scientific Reports, 7(1), 17164. doi:10.1038/s41598-017-17458-z
  95. Lacroix, M., et al. (2017). Interaction of Complement Defence Collagens C1q and Mannose-Binding Lectin with BMP-1/Tolloid-like Proteinases. Scientific Reports, 7(1), 16958. doi:10.1038/s41598-017-17318-w
  96. Laguri, C., et al. (2017). Interaction of lipopolysaccharides at intermolecular sites of the periplasmic Lpt transport assembly. Sci Rep, 7(1), 9715. doi:10.1038/s41598-017-10136-0
  97. Lenton, S., et al. (2017). Effect of Phosphorylation on a Human-like Osteopontin Peptide. Biophys J, 112(8), 1586-1596. doi:10.1016/j.bpj.2017.03.005
  98. Leupold, S., et al. (2017). Structural insights into the architecture of the Shigella flexneri virulence factor IcsA/VirG and motifs involved in polar distribution and secretion. J Struct Biol, 198(1), 19-27. doi:10.1016/j.jsb.2017.03.003
  99. Li, Y. E., et al. (2017). Identification of high-confidence RNA regulatory elements by combinatorial classification of RNA-protein binding sites. Genome Biology, 18. doi:10.1186/s13059-017-1298-8
  100. Lin, Z. T., et al. (2017). 1 alpha,20S-Dihydroxyvitamin D-3 Interacts with Vitamin D Receptor: Crystal Structure and Route of Chemical Synthesis. Scientific Reports, 7. doi:10.1038/s41598-017-10917-7
  101. Liu, G. Q., et al. (2017). One-thousand-fold enhancement of high field liquid nuclear magnetic resonance signals at room temperature. Nature Chemistry, 9(7), 676-680. doi:10.1038/nchem.2723
  102. Ljubetič, A., et al. (2017). Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo. Nature Biotechnology, 35, 1094. doi:10.1038/nbt.3994 https://www.nature.com/articles/nbt.3994#supplementary-information
  103. Lopez, S., et al. (2017). Efficient conversion of alkenes to chlorohydrins by a Ru-based artificial enzyme. Chem Commun (Camb), 53(25), 3579-3582. doi:10.1039/c6cc08873b
  104. Luchinat, E., et al. (2017). A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants. Scientific Reports, 7. doi:10.1038/s41598-017-17815-y
  105. Luchinat, E., et al. (2017). Identification of a novel nucleophosmin-interaction motif in the tumor suppressor p14arf. Febs j. doi:10.1111/febs.14373
  106. Macchi, S., et al. (2017). Self-aggregation propensity of the Tat peptide revealed by UV-Vis, NMR and MD analyses. Physical Chemistry Chemical Physics, 19(35), 23910-23914. doi:10.1039/C7CP04320A
  107. Macek, P., et al. (2017). Unraveling self-assembly pathways of the 468-kDa proteolytic machine TET2. Sci Adv, 3(4). doi:10.1126/sciadv.1601601
  108. Macioła, A. K., et al. (2017). The Length of N-Glycans of Recombinant H5N1 Hemagglutinin Influences the Oligomerization and Immunogenicity of Vaccine Antigen. Front Immunol, 8. doi:10.3389/fimmu.2017.00444
  109. Mansilla, A., et al. (2017). Interference of the complex between NCS-1 and Ric8a with phenothiazines regulates synaptic function and is an approach for fragile X syndrome. Proceedings of the National Academy of Sciences of the United States of America, 114(6), E999-E1008. doi:10.1073/pnas.1611089114
  110. Martel, A., et al. (2017). Membrane Permeation versus Amyloidogenicity: A Multitechnique Study of Islet Amyloid Polypeptide Interaction with Model Membranes. J Am Chem Soc, 139(1), 137-148. doi:10.1021/jacs.6b06985
  111. Martinez-Zapien, D., et al. (2017). The crystal structure of the 5 ' functional domain of the transcription riboregulator 7SK. Nucleic Acids Research, 45(6), 3568-3579. doi:10.1093/nar/gkw1351
  112. Mas, P. J., et al. (2017). ESPRIT: A Method for Defining Soluble Expression Constructs in Poorly Understood Gene Sequences. Methods Mol Biol, 1586, 45-63. doi:10.1007/978-1-4939-6887-9_4
  113. Mas, Y. M. S., et al. (2017). Crystal Structure of the Chloroplastic Oxoene Reductase ceQORH from Arabidopsis thaliana. Front Plant Sci, 8, 329. doi:10.3389/fpls.2017.00329
  114. Melnikov, I., et al. (2017). Fast iodide-SAD phasing for high-throughput membrane protein structure determination. Science Advances, 3(5). doi:10.1126/sciadv.1602952
  115. Mietton, F., et al. (2017). Selective BET bromodomain inhibition as an antifungal therapeutic strategy. Nat Commun, 8, 15482. doi:10.1038/ncomms15482
  116. Miller, P. S., et al. (2017). Structural basis for GABAA receptor potentiation by neurosteroids. Nature Structural &Amp; Molecular Biology, 24, 986. doi:10.1038/nsmb.3484 https://www.nature.com/articles/nsmb.3484#supplementary-information
  117. Mohideen-Abdul, K., et al. (2017). Importance of the Sequence-Directed DNA Shape for Specific Binding Site Recognition by the Estrogen-Related Receptor. Front Endocrinol (Lausanne), 8, 140. doi:10.3389/fendo.2017.00140
  118. Monneau, Y. R., et al. (2017). Solution structure of CXCL13 and heparan sulfate binding show that GAG binding site and cellular signalling rely on distinct domains. Open Biol, 7(10). doi:10.1098/rsob.170133
  119. Monniaux, M., et al. (2017). Conservation vs divergence in LEAFY and APETALA1 functions between Arabidopsis thaliana and Cardamine hirsuta. New Phytol, 216(2), 549-561. doi:10.1111/nph.14419
  120. Morbioli, I., et al. (2017). Mannosylcalix[n]arenes as multivalent ligands for DC-SIGN. Carbohydr Res, 453-454, 36-43. doi:10.1016/j.carres.2017.10.017
  121. Moreau, C., et al. (2017). Deciphering Key Residues Involved in the Virulence-promoting Interactions between Streptococcus pneumoniae and Human Plasminogen. J Biol Chem, 292(6), 2217-2225. doi:10.1074/jbc.M116.764209
  122. Moreno-Beltran, B., et al. (2017). Structural basis of mitochondrial dysfunction in response to cytochrome c phosphorylation at tyrosine 48. Proc Natl Acad Sci U S A, 114(15), E3041-e3050. doi:10.1073/pnas.1618008114
  123. Moyroud, E., et al. (2017). A link between LEAFY and B-gene homologues in Welwitschia mirabilis sheds light on ancestral mechanisms prefiguring floral development. New Phytol, 216(2), 469-481. doi:10.1111/nph.14483
  124. Mylona, A., et al. (2017). A Novel Approach to Data Collection for Difficult Structures: Data Management for Large Numbers of Crystals with the BLEND Software. Crystals (Basel), 7(8), 242. doi:10.3390/cryst7080242
  125. Nasta, V., et al. (2017). Structural insights into the molecular function of human 2Fe-2S BOLA1-GRX5 and 2Fe-2S BOLA3-GRX5 complexes. Biochimica Et Biophysica Acta-General Subjects, 1861(8), 2119-2131. doi:10.1016/j.bbagen.2017.05.005
  126. Natchiar, S. K., et al. (2017). Atomic model building and refinement into high-resolution cryo-EM maps.
  127. Natchiar, S. K., et al. (2017). Visualization of chemical modifications in the human 80S ribosome structure. Nature, 551(7681), 472-+. doi:10.1038/nature24482
  128. Nikolaev, M., et al. (2017). Integral Membrane Proteins Can Be Crystallized Directly from Nanodiscs. Crystal Growth & Design, 17(3), 945-948. doi:10.1021/acs.cgd.6b01631 Nogueira, M. O., et al. (2017). Monitoring HPV-16 E7 phosphorylation events. Virology, 503, 70-75. doi:10.1016/j.virol.2016.12.030
  129. Noguera, M. E., et al. (2017). Structural variability of E. coli thioredoxin captured in the crystal structures of single-point mutants. Scientific Reports, 7. doi:10.1038/srep42343
  130. Oksanen, H. M., et al. (2017). ICTV Virus Taxonomy Profile: Corticoviridae. J Gen Virol, 98(5), 888-889. doi:10.1099/jgv.0.000795
  131. Orlov, I., et al. (2017). The integrative role of cryo electron microscopy in molecular and cellular structural biology. Biology of the Cell, 109(2), 81-93. doi:10.1111/boc.201600042
  132. Osman, R., et al. (2017). Calreticulin Release at an Early Stage of Death Modulates the Clearance by Macrophages of Apoptotic Cells. Frontiers in Immunology, 8. doi:10.3389/fimmu.2017.01034
  133. Otón, J., et al. (2017). XTEND: Extending the depth of field in cryo soft X-ray tomography. Scientific Reports, 7, 45808. doi:10.1038/srep45808 https://www.nature.com/articles/srep45808#supplementary-information
  134. Pansieri, J., et al. (2017). Multimodal imaging Gd-nanoparticles functionalized with Pittsburgh compound B or a nanobody for amyloid plaques targeting. Nanomedicine (Lond), 12(14), 1675-1687. doi:10.2217/nnm-2017-0079
  135. Pellach, M., et al. (2017). A Two-Tailed Phosphopeptide Crystallizes to Form a Lamellar Structure. Angew Chem Int Ed Engl, 56(12), 3252-3255. doi:10.1002/anie.201609877
  136. Pellegrini, E., et al. (2017). Structural Basis for the Subversion of MAP Kinase Signaling by an Intrinsically Disordered Parasite Secreted Agonist. Structure(London, England:1993), 25(1), 16-26. doi:10.1016/j.str.2016.10.011
  137. Pellegrini, E., et al. (2017). Structures of the inactive and active states of RIP2 kinase inform on the mechanism of activation. Plos One, 12(5), e0177161. doi:10.1371/journal.pone.0177161
  138. Peng, G. Y., et al. (2017). Insight into the remarkable affinity and selectivity of the aminobenzosuberone scaffold for the M1 aminopeptidases family based on structure analysis. Proteins-Structure Function and Bioinformatics, 85(8), 1413-1421. doi:10.1002/prot.25301
  139. Perez, C., et al. (2017). Structural basis of inhibition of lipid-linked oligosaccharide flippase PglK by a conformational nanobody. Scientific Reports, 7. doi:10.1038/srep46641
  140. Perras, F. A., et al. (2017). Observation of CHpi Interactions between Methyl and Carbonyl Groups in Proteins. Angew Chem Int Ed Engl, 56(26), 7564-7567. doi:10.1002/anie.201702626
  141. Pietila, M. K., et al. (2017). Polyprotein Processing as a Determinant for In Vitro Activity of Semliki Forest Virus Replicase. Viruses-Basel, 9(10). doi:10.3390/v9100292
  142. Pinker, F., et al. (2017). Biophysical analysis of Arabidopsis protein-only RNase P alone and in complex with tRNA provides a refined model of tRNA binding. J Biol Chem, 292(34), 13904-13913. doi:10.1074/jbc.M117.782078
  143. Ponna, S. K., et al. (2017). Structure of an unconventional SH3 domain from the postsynaptic density protein Shank3 at ultrahigh resolution. Biochem Biophys Res Commun, 490(3), 806-812. doi:https://doi.org/10.1016/j.bbrc.2017.06.121
  144. Portaliou, A. G., et al. (2017). Hierarchical protein targeting and secretion is controlled by an affinity switch in the type III secretion system of enteropathogenic Escherichia coli. Embo Journal, 36(23), 3517-3531. doi:10.15252/embj.201797515
  145. Pozzi, C., et al. (2017). Chemistry at the protein-mineral interface in L-ferritin assists the assembly of a functional (mu(3)-oxo)Tris (mu(2)-peroxo) triiron(III) cluster. Proceedings of the National Academy of Sciences of the United States of America, 114(10), 2580-2585. doi:10.1073/pnas.1614302114
  146. Prokhorova, I., et al. (2017). Aminoglycoside interactions and impacts on the eukaryotic ribosome. Proceedings of the National Academy of Sciences, 114(51), E10899-E10908. doi:10.1073/pnas.1715501114
  147. Quistgaard, E. M., et al. (2017). Structure determination of a major facilitator peptide transporter: Inward facing PepTSt from Streptococcus thermophilus crystallized in space group P3121. Plos One, 12(3), e0173126. doi:10.1371/journal.pone.0173126
  148. Radu, L., et al. (2017). The intricate network between the p34 and p44 subunits is central to the activity of the transcription/DNA repair factor TFIIH. Nucleic Acids Research, 45(18), 10872-10883. doi:10.1093/nar/gkx743
  149. Ravera, E., et al. (2017). Perspectives on paramagnetic NMR from a life sciences infrastructure. Journal of Magnetic Resonance, 282, 154-169. doi:10.1016/j.jmr.2017.07.013
  150. Reich, S., et al. (2017). An in vitro fluorescence based study of initiation of RNA synthesis by influenza B polymerase. Nucleic Acids Res, 45(6), 3353-3368. doi:10.1093/nar/gkx043
  151. Renauld, S., et al. (2017). Functional reconstitution of cell-free synthesized purified Kv channels. Biochim Biophys Acta, 1859(12), 2373-2380. doi:10.1016/j.bbamem.2017.09.002
  152. Rennella, E., et al. (2017). RNA binding and chaperone activity of the E. coli cold-shock protein CspA. Nucleic Acids Res, 45(7), 4255-4268. doi:10.1093/nar/gkx044
  153. Rivera-Calzada, A., et al. (2017). The Structure of the R2TP Complex Defines a Platform for Recruiting Diverse Client Proteins to the HSP90 Molecular Chaperone System. Structure, 25(7), 1145-1152.e1144. doi:https://doi.org/10.1016/j.str.2017.05.016
  154. Romano-Moreno, M., et al. (2017). Molecular mechanism for the subversion of the retromer coat by the Legionella effector RidL. Proc Natl Acad Sci U S A, 114(52), E11151-e11160. doi:10.1073/pnas.1715361115
  155. Rues, R. B., et al. (2017). Membrane Protein Production in E. coli Lysates in Presence of Preassembled Nanodiscs. Methods Mol Biol, 1586, 291-312. doi:10.1007/978-1-4939-6887-9_19
  156. Ruiz, F. X., et al. (2017). Structural basis for the inhibition of AKR1B10 by the C3 brominated TTNPB derivative UVI2008. Chemico-Biological Interactions, 276, 174-181. doi:10.1016/j.cbi.2017.01.026
  157. Saint-Cricq, M., et al. (2017). Human Immune Protein C1q Selectively Disaggregates Carbon Nanotubes. Nano Lett, 17(6), 3409-3415. doi:10.1021/acs.nanolett.7b00189
  158. Saletti, D., et al. (2017). The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model. Sci Rep, 7. doi:10.1038/srep40801
  159. Salvi, N., et al. (2017). Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation. Prog Nucl Magn Reson Spectrosc, 102-103, 43-60. doi:10.1016/j.pnmrs.2017.06.001
  160. Salvi, N., et al. (2017). Analytical Description of NMR Relaxation Highlights Correlated Dynamics in Intrinsically Disordered Proteins. Angew Chem Int Ed Engl, 56(45), 14020-14024. doi:10.1002/anie.201706740
  161. Salvi, N., et al. (2017). Dynamic Descriptions of Highly Flexible Molecules from NMR Dipolar Couplings: Physical Basis and Limitations. J Am Chem Soc. doi:10.1021/jacs.7b01566
  162. Sanchez-Garcia, R., et al. (2017). 3DCONS-DB: A Database of Position-Specific Scoring Matrices in Protein Structures. Molecules, 22(12). doi:10.3390/molecules22122230
  163. Santos-Perez, I., et al. (2017). Membrane-assisted viral DNA ejection. Biochimica Et Biophysica Acta-General Subjects, 1861(3), 664-672. doi:10.1016/j.bbagen.2016.12.013
  164. Sauer, P. V., et al. (2017). Insights into the molecular architecture and histone H3-H4 deposition mechanism of yeast Chromatin assembly factor 1. Elife, 6. doi:10.7554/eLife.23474
  165. Sayers, Z., et al. (2017). G Protein Signaling in Plants: Characterization of Alpha and Gamma Subunits. Biophysical Journal, 112(3), 189A-190A. doi:10.1016/j.bpj.2016.11.1052
  166. Schacherl, M., et al. (2017). Crystallographic and biochemical characterization of the dimeric architecture of site-2 protease. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1859(10), 1859-1871. doi:https://doi.org/10.1016/j.bbamem.2017.05.006
  167. Schenck, S., et al. (2017). Generation and Characterization of Anti-VGLUT Nanobodies Acting as Inhibitors of Transport. Biochemistry, 56(30), 3962-3971. doi:10.1021/acs.biochem.7b00436
  168. Schubert, A. F., et al. (2017). Structure of PINK1 in complex with its substrate ubiquitin. Nature, 552(7683), 51-+. doi:10.1038/nature24645
  169. Schulze, W. M., et al. (2017). Structural basis for mutually exclusive co-transcriptional nuclear cap-binding complexes with either NELF-E or ARS2. Nature Communications, 8(1), 1302. doi:10.1038/s41467-017-01402-w
  170. Segura, J., et al. (2017). 3DBIONOTES v2.0: a web server for the automatic annotation of macromolecular structures. Bioinformatics, 33(22), 3655-3657. doi:10.1093/bioinformatics/btx483
  171. Sharov, G., et al. (2017). Structure of the transcription activator target Tra1 within the chromatin modifying complex SAGA. Nature Communications, 8. doi:10.1038/s41467-017-01564-7
  172. Shevchenko, V., et al. (2017). Sodium and Engineered Potassium Light-Driven Pumps. In K. Appasani (Ed.), Optogenetics: From Neuronal Function to Mapping and Disease Biology(pp. 79-92). Cambridge: Cambridge University Press.
  173. Shevchenko, V., et al. (2017). Inward H(+) pump xenorhodopsin: Mechanism and alternative optogenetic approach. Science Advances, 3(9), e1603187. doi:10.1126/sciadv.1603187
  174. Sorrenti, A., et al. (2017). Non-equilibrium steady states in supramolecular polymerization. Nature Communications, 8, 15899. doi:10.1038/ncomms15899 https://www.nature.com/articles/ncomms15899#supplementary-information
  175. Sorzano, C. O. S., et al. (2017). A Survey of the Use of Iterative Reconstruction Algorithms in Electron Microscopy. Biomed Research International. doi:10.1155/2017/6482567
  176. Stamogiannos, A., et al. (2017). Critical Role of Interdomain Interactions in the Conformational Change and Catalytic Mechanism of Endoplasmic Reticulum Aminopeptidase 1. Biochemistry, 56(10), 1546-1558. doi:10.1021/acs.biochem.6b01170
  177. Steinbach, T., et al. (2017). Reversible Bioconjugation: Biodegradable Poly(phosphate)-Protein Conjugates. Macromol Biosci, 17(10). doi:10.1002/mabi.201600377
  178. Stranava, M., et al. (2017). Coordination and redox state-dependent structural changes of the heme-based oxygen sensor AfGcHK associated with intraprotein signal transduction. Journal of Biological Chemistry, 292(51), 20921-20935. doi:10.1074/jbc.M117.817023
  179. Sukackaite, R., et al. (2017). Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1). Scientific Reports, 7(1), 2119. doi:10.1038/s41598-017-01910-1
  180. Sun, Z., et al. (2017). Double-stranded RNA virus outer shell assembly by bona fide domain-swapping. Nat Commun, 8, 14814. doi:10.1038/ncomms14814
  181. Sun, Z. Y., et al. (2017). Double-stranded RNA virus outer shell assembly by bona fide domain-swapping. Nature Communications, 8. doi:10.1038/ncomms14814
  182. Swainsbury, D. J. K., et al. (2017). The effectiveness of styrene-maleic acid (SMA) copolymers for solubilisation of integral membrane proteins from SMA-accessible and SMA-resistant membranes. Biochim Biophys Acta, 1859(10), 2133-2143. doi:10.1016/j.bbamem.2017.07.011
  183. Takis, P. G., et al. (2017). Gelified Biofluids for High-Resolution Magic Angle Spinning H-1 NMR Analysis: The Case of Urine. Analytical Chemistry, 89(2), 1054-1058. doi:10.1021/acs.analchem.6b04318
  184. Tamburrini, A., et al. (2017). Facile access to pseudo-thio-1,2-dimannoside, a new glycomimetic DC-SIGN antagonist. Bioorg Med Chem, 25(19), 5142-5147. doi:10.1016/j.bmc.2017.03.046
  185. Tarbouriech, N., et al. (2017). The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding. Nat Commun, 8(1), 1455. doi:10.1038/s41467-017-01542-z
  186. Tesei, G., et al. (2017). Self-association of a highly charged arginine-rich cell-penetrating peptide. Proc Natl Acad Sci U S A, 114(43), 11428-11433. doi:10.1073/pnas.1712078114
  187. Thedie, D., et al. (2017). Photoswitching of Green mEos2 by Intense 561 nm Light Perturbs Efficient Green-to-Red Photoconversion in Localization Microscopy. J Phys Chem Lett, 8(18), 4424-4430. doi:10.1021/acs.jpclett.7b01701
  188. van Haren, M. J., et al. (2017). Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1. Proceedings of the National Academy of Sciences of the United States of America, 114(14), 3625-3630. doi:10.1073/pnas.1618401114
  189. van Zundert, G. C., et al. (2017). The DisVis and PowerFit Web Servers: Explorative and Integrative Modeling of Biomolecular Complexes. J Mol Biol, 429(3), 399-407. doi:10.1016/j.jmb.2016.11.032
  190. Volkov, O., et al. (2017). Structural insights into ion conduction by channelrhodopsin 2. Science, 358(6366). doi:10.1126/science.aan8862
  191. von Stetten, D., et al. (2017). Online Raman spectroscopy for structural biology on beamline ID29 of the ESRF. Journal of Structural Biology, 200(2), 124-127. doi:https://doi.org/10.1016/j.jsb.2017.10.004
  192. Waberer, L., et al. (2017). The synaptic vesicle protein SV31 assembles into a dimer and transports Zn2+. Journal of Neurochemistry, 140(2), 280-293. doi:10.1111/jnc.13886
  193. Wojtas, D. H., et al. (2017). Analysis of XFEL serial diffraction data from individual crystalline fibrils. Iucrj, 4(6), 795-811. doi:doi:10.1107/S2052252517014324 
  194. Wutz, D., et al. (2017). Photochromic histone deacetylase inhibitors based on dithienylethenes and fulgimides. Organic & Biomolecular Chemistry, 15(22), 4882-4896. doi:10.1039/c7ob00976c

2016

  1. Abyzov, A., et al. (2016). Identification of Dynamic Modes in an Intrinsically Disordered Protein Using Temperature-Dependent NMR Relaxation. Journal of the American Chemical Society, 138(19), 6240-6251. doi:10.1021/jacs.6b02424
  2. Aguilar-Gurrieri, C., et al. (2016). Structural evidence for Nap1-dependent H2A-H2B deposition and nucleosome assembly. Embo j, 35(13), 1465-1482. doi:10.15252/embj.201694105
  3. Andralojc, W., et al. (2016). Inter-helical conformational preferences of HIV-1 TAR-RNA from maximum occurrence analysis of NMR data and molecular dynamics simulations. Physical Chemistry Chemical Physics, 18(8), 5743-5752. doi:10.1039/c5cp03993b
  4. Andronov, L., et al. (2016). SharpViSu: integrated analysis and segmentation of super-resolution microscopy data. Bioinformatics, 32(14), 2239-2241. doi:10.1093/bioinformatics/btw123
  5. Andronov, L., et al. (2016). ClusterViSu, a method for clustering of protein complexes by Voronoi tessellation in super-resolution microscopy. Scientific Reports, 6. doi:10.1038/srep24084
  6. Anvarian, Z., et al. (2016). Axin cancer mutants form nanoaggregates to rewire the Wnt signaling network. Nat Struct Mol Biol, 23(4), 324-332. doi:10.1038/nsmb.3191
  7. Arien, K. K., et al. (2016). CD4-mimetic sulfopeptide conjugates display sub-nanomolar anti-HIV-1 activity and protect macaques against a SHIV162P3 vaginal challenge. Sci Rep, 6, 34829. doi:10.1038/srep34829
  8. Arzumanyan, G. M., et al. (2016). Highly Sensitive Coherent Anti-Stokes Raman Scattering Imaging of Protein Crystals. J Am Chem Soc. doi:10.1021/jacs.6b04464
  9. Asencio-Hernandez, J., et al. (2016). NMR WaterLOGSY Reveals Weak Binding of Bisphenol
  10. A with Amyloid Fibers of a Conserved 11 Residue Peptide from Androgen Receptor. Plos One, 11(9). doi:10.1371/journal.pone.0161948
  11. Aubert, V., et al. (2016). A simple acoustofluidic chip for microscale manipulation using evanescent Scholte waves. Lab Chip, 16(13), 2532-2539. doi:10.1039/c6lc00534a
  12. Baldoneschi, V., et al. (2016). Active-Site Targeting Paramagnetic Probe for Matrix Metalloproteinases. Chempluschem, 81(12), 1333-1338. doi:10.1002/cplu.201600375
  13. Barbieri, L., et al. (2016). Characterization of proteins by in-cell NMR spectroscopy in cultured mammalian cells. Nat Protoc, 11(6), 1101-1111. doi:10.1038/nprot.2016.061
  14. Baser, B., et al. (2016). A method for specifically targeting two independent genomic integration sites for co-expression of genes in CHO cells. Methods, 95, 3-12. doi:10.1016/j.ymeth.2015.11.022
  15. Belorusova, A. Y., et al. (2016). Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein. Biochemistry, 55(12), 1741-1748. doi:10.1021/acs.biochem.5b01122
  16. Benjelloun, F., et al. (2016). First Membrane Proximal External Region-Specific Anti-HIV1 Broadly Neutralizing Monoclonal IgA1 Presenting Short CDRH3 and Low Somatic Mutations. J Immunol, 197(5), 1979-1988. doi:10.4049/jimmunol.1600309
  17. Berardozzi, R., et al. (2016). Arginine 66 Controls Dark-State Formation in Green-to-Red Photoconvertible Fluorescent Proteins. J Am Chem Soc, 138(2), 558-565. doi:10.1021/jacs.5b09923
  18. Bernacchioni, C., et al. (2016). Ferroxidase Activity in Eukaryotic Ferritin is Controlled by Accessory-Iron-Binding Sites in the Catalytic Cavity. Chemistry-a European Journal, 22(45), 16213-16219. doi:10.1002/chem.201602842
  19. Bertolotti, B., et al. (2016). Nonhydrolyzable C-disaccharides, a new class of DC-SIGN ligands. Carbohydrate Research, 435, 7-18. doi:https://doi.org/10.1016/j.carres.2016.09.005
  20. Bleckmann, M., et al. (2016). Fast Plasmid Based Protein Expression Analysis in Insect Cells Using an Automated SplitGFP Screen. Biotechnology and Bioengineering, 113(9), 1975-1983. doi:10.1002/bit.25956
  21. Botte, M., et al. (2016). A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion. Scientific Reports, 6. doi:10.1038/srep38399
  22. Bourbigot, S., et al. (2016). Solution structure of the 5 '-terminal hairpin of the 7SK small
  23. nuclear RNA. Rna, 22(12), 1844-1858. doi:10.1261/rna.056523.116
  24. Brandt, K., et al. (2016). Stoichiometry and deletion analyses of subunits in the heterotrimeric F-ATP synthase c ring from the acetogenic bacterium Acetobacterium woodii. Febs Journal, 283(3), 510-520. doi:10.1111/febs.13606
  25. Burhan, I., et al. (2016). Interplay between transglutaminases and heparan sulphate in progressive renal scarring. Scientific Reports, 6, 31343. doi:10.1038/srep31343
  26. Buslaev, P., et al. (2016). Principal Component Analysis of Lipid Molecule Conformational Changes in Molecular Dynamics Simulations. J Chem Theory Comput, 12(3), 1019-1028. doi:10.1021/acs.jctc.5b01106
  27. Carlon, A., et al. (2016). How to tackle protein structural data from solution and solid state: An integrated approach. Progress in Nuclear Magnetic Resonance Spectroscopy, 92-93, 54-70. doi:10.1016/j.pnmrs.2016.01.001
  28. Carlon, A., et al. (2016). Improved Accuracy from Joint X-ray and NMR Refinement of a Protein-RNA Complex Structure. Journal of the American Chemical Society, 138(5), 1601-1610. doi:10.1021/jacs.5b11598
  29. Cerofolini, L., et al. (2016). Bilayer Membrane Modulation of Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Structure and Proteolytic Activity. Scientific Reports, 6. doi:10.1038/srep29511
  30. Chang, V. T., et al. (2016). Initiation of T cell signaling by CD45 segregation at 'close contacts'. Nature Immunology, 17(5), 574-+. doi:10.1038/ni.3392
  31.  30, Chevallet, M., et al. (2016). Metal homeostasis disruption and mitochondrial dysfunction in hepatocytes exposed to sub-toxic doses of zinc oxide nanoparticles. Nanoscale, 8(43), 18495-18506. doi:10.1039/c6nr05306h
  32. Claes, K., et al. (2016). Modular Integrated Secretory System Engineering in Pichia pastoris To Enhance G-Protein Coupled Receptor Expression. Acs Synthetic Biology, 5(10), 1070-1075. doi:10.1021/acssynbio.6b00032
  33. Colletier, J. P., et al. (2016). Serial Femtosecond Crystallography and Ultrafast Absorption Spectroscopy of the Photoswitchable Fluorescent Protein IrisFP. J Phys Chem Lett, 7(5), 882-887. doi:10.1021/acs.jpclett.5b02789
  34. Connell, B. J., et al. (2016). A Cinnamon-Derived Procyanidin Compound Displays Anti-HIV-1 Activity by Blocking Heparan Sulfate- and Co-Receptor- Binding Sites on gp120 and Reverses T Cell Exhaustion via Impeding Tim-3 and PD-1 Upregulation. Plos One, 11(10), e0165386.doi:10.1371/journal.pone.0165386
  35. Connell, B. J., et al. (2016). Heparan sulfate differentially controls CXCL12alpha- and CXCL12gamma-mediated cell migration through differential presentation to their receptor CXCR4. Sci Signal, 9(452), ra107. doi:10.1126/scisignal.aaf1839
  36. Coscia, F., et al. (2016). Fusion to a homo-oligomeric scaffold allows cryo-EM analysis of a small protein. Scientific Reports, 6, 30909. doi:10.1038/srep30909
  37. Cousido-Siah, A., et al. (2016). IDD388 Polyhalogenated Derivatives as Probes for an Improved Structure-Based Selectivity of AKR1B10 Inhibitors. Acs Chemical Biology, 11(10), 2693-2705. doi:10.1021/acschembio.6b00382
  38. Cousido-Siah, A., et al. (2016). IDD388 Polyhalogenated Derivatives as Probes for an Improved Structure-Based Selectivity of AKR1B10 Inhibitors. Acs Chemical Biology, 11(10), 2693-2705. doi:10.1021/acschembio.6b00382
  39. da Mata Madeira, P. V., et al. (2016). Structural Basis of Lipid Targeting and Destruction by the Type V Secretion System of Pseudomonas aeruginosa. J Mol Biol, 428(9 Pt A), 1790-1803. doi:10.1016/j.jmb.2016.03.012
  40. de la Rosa-Trevin, J. M., et al. (2016). Scipion: A software framework toward integration, reproducibility and validation in 3D electron microscopy. Journal of Structural Biology, 195(1), 93-99. doi:10.1016/j.jsb.2016.04.010
  41. Delaforge, E., et al. (2016). Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions. Front Mol Biosci, 3. doi:10.3389/fmolb.2016.00054
  42. Demina, T. A., et al. (2016). Vesicle-like virion of Haloarcula hispanica pleomorphic virus 3 preserves high infectivity in saturated salt. Virology, 499, 40 51. doi:https://doi.org/10.1016/j.virol.2016.09.002
  43. Ebel, C. (2016). AUC in the High Concentration of Salts/Cosolvent. In S. Uchiyama, F. Arisaka, W. F. Stafford, & T. Laue (Eds.), Analytical Ultracentrifugation: Instrumentation, Software, and Applications(pp. 355-373). Tokyo: Springer Japan.
  44. Effantin, G., et al. (2016). Cryo-electron Microscopy Structure of the Native Prototype Foamy Virus Glycoprotein and Virus Architecture. PLoS Pathog, 12(7), e1005721. doi:10.1371/journal.ppat.1005721
  45. El Khatib, M., et al. (2016). Rational design of ultrastable and reversibly photoswitchable fluorescent proteins for super-resolution imaging of the bacterial periplasm. Scientific Reports, 6, 18459. doi:10.1038/srep18459
  46. Eskelin, K., et al. (2016). Asymmetric flow field flow fractionation methods for virus purification. J Chromatogr A, 1469, 108-119. doi:10.1016/j.chroma.2016.09.055
  47. Farkaš, R., et al. (2016). Massive excretion of calcium oxalate from late prepupal salivary glands of Drosophila melanogaster demonstrates active nephridial-like anion transport. Development, Growth & Differentiation, 58(6), 562-574. doi:10.1111/dgd.12300
  48. Favier, A. L., et al. (2016). Enhancement of Ebola Virus Infection via Ficolin-1 Interaction with the Mucin Domain of GP Glycoprotein. J Virol, 90(11), 5256-5269. doi:10.1128/jvi.00232-16
  49. Feifel, S. C., et al. (2016). Insights into Interprotein Electron Transfer of Human Cytochrome c Variants Arranged in Multilayer Architectures by Means of an Artificial Silica Nanoparticle Matrix. ACS Omega, 1(6), 1058-1066. doi:10.1021/acsomega.6b00213
  50. Ginn, H. M., et al. (2016). On the release of cppxfel for processing X-ray free-electron laser images. J Appl Crystallogr, 49(Pt 3), 1065-1072. doi:10.1107/s1600576716006981
  51. Goldenzweig, A., et al. (2016). Automated Structure- and Sequence-Based Design of Proteins for High Bacterial Expression and Stability. Mol Cell, 63(2), 337-346. doi:10.1016/j.molcel.2016.06.012
  52. Gushchin, I., et al. (2016). Structure of the light-driven sodium pump KR2 and its implications for optogenetics. Febs j, 283(7), 1232-1238. doi:10.1111/febs.13585
  53. Haikarainen, T., et al. (2016). Development and structural analysis of adenosine site binding tankyrase inhibitors. Bioorganic & Medicinal Chemistry Letters, 26(2), 328-333. doi:https://doi.org/10.1016/j.bmcl.2015.12.018
  54. Heimburg, T., et al. (2016). Structure-Based Design and Synthesis of Novel Inhibitors Targeting HDAC8 from Schistosoma mansoni for the Treatment of Schistosomiasis. Journal of Medicinal Chemistry, 59(6), 2423-2435. doi:10.1021/acs.jmedchem.5b01478
  55. Heinnburg, T., et al. (2016). Structure-Based Design and Synthesis of Novel Inhibitors Targeting HDAC8 from Schistosoma mansoni for the Treatment of Schistosomiasis. Journal of Medicinal Chemistry, 59(6), 2423-2435. doi:10.1021/acs.jmedchem.5b01478
  56. Henrich, E., et al. (2016). Lipid Requirements for the Enzymatic Activity of MraY Translocases and in Vitro Reconstitution of the Lipid II Synthesis Pathway. Journal of Biological Chemistry, 291(5), 2535-2546. doi:10.1074/jbc.M115.664292
  57. Hosek, T., et al. (2016). Structural and Dynamic Characterization of the Molecular Hub Early Region 1A (E1A) from Human Adenovirus. Chemistry, 22(37), 13010-13013. doi:10.1002/chem.201602510
  58. Howard, E. I., et al. (2016). High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution. Iucrj, 3, 115-126. doi:10.1107/s2052252515024161
  59. Hutin, S., et al. (2016). Domain Organization of Vaccinia Virus Helicase-Primase D5. J Virol, 90(9), 4604-4613. doi:10.1128/jvi.00044-16
  60. Jiang, X., et al. (2016). Crystal structure of a LacY–nanobody complex in a periplasmic-open conformation. Proceedings of the National Academy of Sciences of the United States of America, 113(44), 12420-12425. doi:10.1073/pnas.1615414113
  61. Kandiah, E., et al. (2016). Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA. Sci Rep, 6, 24601. doi:10.1038/srep24601
  62. Kaplan, M., et al. (2016). EGFR Dynamics Change during Activation in Native Membranes as Revealed by NMR. Cell, 167(5), 1241-1251.e1211. doi:10.1016/j.cell.2016.10.038
  63. Kereiche, S., et al. (2016). The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease. Scientific Reports, 6. doi:10.1038/srep33631
  64. Khoshouei, M., et al. (2016). Volta phase plate cryo-EM of the small protein complex Prx3. Nature Communications, 7. doi:10.1038/ncomms10534
  65. Kim, H. S., et al. (2016). SAXS/SANS on Supercharged Proteins Reveals Residue-Specific Modifications of the Hydration Shell. Biophys J, 110(10), 2185-2194. doi:10.1016/j.bpj.2016.04.013
  66. Kobbi, L., et al. (2016). An evolutionary conserved Hexim1 peptide binds to the Cdk9 catalytic site to inhibit P-TEFb. Proceedings of the National Academy of Sciences of the United States of America, 113(45), 12721-12726. doi:10.1073/pnas.1612331113
  67. Koning, R. I., et al. (2016). Asymmetric cryo-EM reconstruction of phage MS2 reveals genome structure in situ. Nature Communications, 7. doi:10.1038/ncomms12524
  68. Koval, T., et al. (2016). Structural and Catalytic Properties of S1 Nuclease from Aspergillus oryzae Responsible for Substrate Recognition, Cleavage, Non-Specificity, and Inhibition. Plos One, 11(12), e0168832. doi:10.1371/journal.pone.0168832
  69. Kurauskas, V., et al. (2016). Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit. Chem Commun (Camb), 52(61), 9558-9561. doi:10.1039/c6cc04484k
  70. Kurauskas, V., et al. (2016). Cross-Correlated Relaxation of Dipolar Coupling and Chemical-Shift Anisotropy in Magic-Angle Spinning R1ρ NMR Measurements: Application to Protein Backbone Dynamics Measurements. The Journal of Physical Chemistry B, 120(34), 8905-8913. doi:10.1021/acs.jpcb.6b06129
  71. Labaronne, A., et al. (2016). Binding ofRNA by the Nucleoproteins of Influenza Viruses A and B. Viruses, 8(9).doi:10.3390/v8090247
  72. Lassalle, L., et al. (2016). Newinsights into the mechanism of substrates trafficking inGlyoxylate/Hydroxypyruvate reductases. SciRep, 6, 20629. doi:10.1038/srep20629
  73. Latrick, C. M., et al. (2016). Molecularbasis and specificity of H2A.Z-H2B recognition and deposition by the histonechaperone YL1. Nature Structural & Molecular Biology, 23(4),309-316. doi:10.1038/nsmb.3189
  74. Lepage, M. L., et al. (2016).Iminosugar-Cyclopeptoid Conjugates Raise Multivalent Effect in GlycosidaseInhibition at Unprecedented High Levels. Chemistry-a European Journal, 22(15),5151-5155. doi:10.1002/chem.201600338
  75. Levy, N., et al. (2016). Production ofunstable proteins through the formation of stable core complexes. NatureCommunications, 7. doi:10.1038/ncomms10932
  76. Louros, N. N., et al. (2016). Intrinsicaggregation propensity of the CsgB nucleator protein is crucial for curli fiberformation. Journal of Structural Biology, 195(2), 179-189.doi:https://doi.org/10.1016/j.jsb.2016.05.012
  77. Luchinat, E., et al. (2016). Sequentialprotein expression and selective labeling for in-cell NMR in human cells. BiochimicaEt Biophysica Acta-General Subjects, 1860(3), 527-533.doi:10.1016/j.bbagen.2015.12.023
  78. Manuse, S., et al. (2016).Structure–function analysis of the extracellular domain of the pneumococcalcell division site positioning protein MapZ. Nature Communications, 7,12071. doi:10.1038/ncomms12071
  79. Marabini, R., et al. (2016). TheElectron Microscopy eXchange (EMX) initiative. Journal of StructuralBiology, 194(2), 156-163. doi:10.1016/j.jsb.2016.02.008
  80. Marechal, M., et al. (2016).Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized atthe division site. BMC Microbiol, 16(1), 239.doi:10.1186/s12866-016-0844-y
  81. Marek, M., et al. (2016). Large-ScaleOverproduction and Purification of Recombinant Histone Deacetylase 8 (HDAC8)from the Human-Pathogenic Flatworm Schistosoma mansoni. Methods Mol Biol,1436, 109-118. doi:10.1007/978-1-4939-3667-0_8
  82. Martelli, T., et al. (2016).Atomic-Level Quality Assessment of Enzymes Encapsulated in Bioinspired Silica. Chemistry-aEuropean Journal, 22(1), 425-432. doi:10.1002/chem.201503613
  83. Martin, F., et al. (2016). Ribosomal 18SrRNA base pairs with mRNA during eukaryotic translation initiation. NatureCommunications, 7. doi:10.1038/ncomms12622
  84. Martinez-Lumbreras, S., et al. (2016). Gbp2interacts with THO/TREX through a novel type of RRM domain. Nucleic AcidsResearch, 44(1), 437-448. doi:10.1093/nar/gkv1303
  85. Martinez-Zapien, D., et al. (2016).Structure of the E6/E6AP/p53 complex required for HPV-mediated degradation ofp53. Nature, 529(7587), 541-+. doi:10.1038/nature16481
  86. Mayerhofer, H., et al. (2016).Structural Insights into the Nucleotide-Binding Domains of the P1B-type ATPasesHMA6 and HMA8 from Arabidopsis thaliana. Plos One, 11(11), e0165666.doi:10.1371/journal.pone.0165666
  87. Menezes, M. C., et al. (2016).Recombinant expression of the precursor of the hemorrhagic metalloproteinaseHF3 and its non-catalytic domains using a cell-free synthesis system. AminoAcids, 48(9), 2205-2214. doi:10.1007/s00726-016-2255-7
  88. Mercatelli, E., et al. (2016). Directstructural evidence of protein redox regulation obtained by in-cell NMR. Biochimicaet Biophysica Acta (BBA) - Molecular Cell Research, 1863(2), 198-204.doi:https://doi.org/10.1016/j.bbamcr.2015.11.009
  89. Meyer, S., et al. (2016). Backbone H-1,N-15, C-13 NMR assignment of the 518-627 fragment of the androgen receptorencompassing N-terminal and DNA binding domains. Biomolecular NmrAssignments, 10(1), 175-178. doi:10.1007/s12104-015-9661-8
  90. Milles, S., et al. (2016). Self-Assemblyof Measles Virus Nucleocapsid-like Particles: Kinetics and RNA SequenceDependence. Angew Chem Int Ed Engl, 55(32), 9356-9360.doi:10.1002/anie.201602619
  91. Moreau, C., et al. (2016). Structuraland Functional Characterization of a Single-Chain Form of the RecognitionDomain of Complement Protein C1q. Front Immunol, 7, 79.doi:10.3389/fimmu.2016.00079
  92. Moreau, C., et al. (2016). Structures ofparasite calreticulins provide insights into their flexibility and dualcarbohydrate/peptide-binding properties. Iucrj, 3(Pt 6), 408-419.doi:10.1107/s2052252516012847
  93. Myasnikov, A. G., et al. (2016).Structure-function insights reveal the human ribosome as a cancer target forantibiotics. Nature Communications, 7. doi:10.1038/ncomms12856
  94. Nguyen-Huynh, N. T., et al. (2016).Monitoring of the retinoic acid receptor-retinoid X receptor dimerization uponDNA binding by native mass spectrometry. Biophysical Chemistry, 210,2-8. doi:10.1016/j.bpc.2015.10.006
  95. Nicolaou, K. C., et al. (2016).Synthesis and Biopharmaceutical Evaluation of Imatinib Analogues FeaturingUnusual Structural Motifs. Chemmedchem, 11(1), 31-37.doi:10.1002/cmdc.201500510
  96. Nuttle, X., et al. (2016). Emergence ofa Homo sapiens-specific gene family and chromosome 16p11.2 CNV susceptibility. Nature,536(7615), 205-209. doi:10.1038/nature19075
  97. Ohayon, D., et al. (2016). Cytoplasmicproliferating cell nuclear antigen connects glycolysis and cell survival inacute myeloid leukemia. Scientific Reports, 6, 35561. doi:10.1038/srep35561
  98. Olsen, G., et al. (2016). Optimizingwater hyperpolarization and dissolution for sensitivity-enhanced 2Dbiomolecular NMR. Journal of Magnetic Resonance, 264, 49-58.doi:https://doi.org/10.1016/j.jmr.2016.01.005
  99. Ordanini, S., et al. (2016). SolutionBehavior of Amphiphilic Glycodendrimers with a Rod-Like Core. MacromolBiosci, 16(6), 896-905. doi:10.1002/mabi.201500452
  100. Otero, R., et al. (2016).Carborane-based design of a potent vitamin D receptor agonist. ChemicalScience, 7(2), 1033-1037. doi:10.1039/c5sc03084f
  101. Pasi, M., et al. (2016). DNA minicirclesclarify the specific role of DNA structure on retroviral integration. NucleicAcids Research, 44(16), 7830-7847. doi:10.1093/nar/gkw651
  102. Pebay-Peyroula, E. (2016). FromMolecules to Living Organisms: An Interplay Between Biology and Physics:Lecture Notes of the Les Houches School of Physics: Volume 102, July 2014(E. Pebay-Peyroula, H. Nury, F. Parcy, R. W. H. Ruigrok, C. Ziegler, & L.F. Cugliandolo Eds.). Oxford: Oxford University Press.
  103. Piai, A., et al. (2016). Just aFlexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed byNMR Spectroscopy. Biophys J, 110(2), 372-381.doi:10.1016/j.bpj.2015.11.3516
  104. Pietila, M. K., et al. (2016).Pleolipoviridae, a newly proposed family comprising archaeal pleomorphicviruses with single-stranded or double-stranded DNA genomes. Archives ofVirology, 161(1), 249-256. doi:10.1007/s00705-015-2613-x
  105. Pietrzak, M., et al. (2016). An avianinfluenza H5N1 virus vaccine candidate based on the extracellular domainproduced in yeast system as subviral particles protects chickens from lethalchallenge. Antiviral Res, 133, 242-249.doi:10.1016/j.antiviral.2016.08.001
  106. Pilsl, M., et al. (2016). Structure ofthe initiation-competent RNA polymerase I and its implication fortranscription. Nature Communications, 7. doi:10.1038/ncomms12126
  107. Podobnik, M., et al. (2016). Crystalstructure of an invertebrate cytolysin pore reveals unique properties andmechanism of assembly. Nature Communications, 7. doi:10.1038/ncomms11598
  108. Polidori, A., et al. (2016). Sparinglyfluorinated maltoside-based surfactants for membrane-protein stabilization. NewJournal of Chemistry, 40(6), 5364-5378. doi:10.1039/C5NJ03502C
  109. Pukancsik, M., et al. (2016). SecondaryStructure Prediction of Protein Constructs Using Random Incremental Truncationand Vacuum-Ultraviolet CD Spectroscopy. Plos One, 11(6), e0156238.doi:10.1371/journal.pone.0156238
  110. Rammohan,N., et al. (2016). Nanodiamond-Gadolinium(III) Aggregates for Tracking CancerGrowth In Vivo at High Field. Nano Letters, 16(12), 7551-7564.doi:10.1021/acs.nanolett.6b03378
  111. Rasmussen, K. K., et al. (2016).Structural and dynamics studies of a truncated variant of CI repressor frombacteriophage TP901-1. Scientific Reports, 6, 29574.doi:10.1038/srep29574
  112. Ravera, E., et al. (2016). 1H-detectedsolid-state NMR of proteins entrapped in bioinspired silica: a new tool forbiomaterials characterization. Scientific Reports, 6, 27851.doi:10.1038/srep27851
  113. Ravera, E., et al. (2016). Solid-State NMRof PEGylated Proteins. Angewandte Chemie-International Edition, 55(7),2446-2449. doi:10.1002/anie.201510148
  114. Ravera, E., et al. (2016). Basic factsand perspectives of Overhauser DNP NMR. Journal of Magnetic Resonance, 264,78-87. doi:10.1016/j.jmr.2015.12.013
  115. Ravera, E., et al. (2016). Biosilicaand bioinspired silica studied by solid-state NMR. Coordination ChemistryReviews, 327, 110-122. doi:10.1016/j.ccr.2016.06.003
  116. Ravera, E., et al. (2016). A criticalassessment of methods to recover information from averaged data. PhysicalChemistry Chemical Physics, 18(8), 5686-5701. doi:10.1039/c5cp04077a
  117. Renner, M., et al. (2016). Nucleocapsidassembly in pneumoviruses is regulated by conformational switching of the Nprotein. Elife, 5, e12627. doi:10.7554/eLife.1262
  118. Richard, J. P., et al. (2016).Structure–Function Studies of Hydrophobic Residues That Clamp a Basic GlutamateSide Chain during Catalysis by Triosephosphate Isomerase. Biochemistry, 55(21),3036-3047. doi:10.1021/acs.biochem.6b00311
  119. Rodrigues, C. D., et al. (2016). Aring-shaped conduit connects the mother cell and forespore during sporulationin Bacillus subtilis. Proc Natl Acad Sci U S A, 113(41), 11585-11590.doi:10.1073/pnas.1609604113
  120. Roulland, Y., et al. (2016). TheFlexible Ends of CENP-A Nucleosome Are Required for Mitotic Fidelity. MolecularCell, 63(4), 674-685. doi:https://doi.org/10.1016/j.molcel.2016.06.023
  121. Rues, R. B., et al. (2016).Co-translational formation and pharmacological characterization ofbeta1-adrenergic receptor/nanodisc complexes with different lipid environments.Biochimica Et Biophysica Acta-Biomembranes, 1858(6), 1306-1316.doi:10.1016/j.bbamem.2016.02.031
  122. Ruiz, J., et al. (2016). Covalent Tethering and Residues with Bulky Hydrophobic Side Chains Enable Self-Assembly of Distinct Amyloid Structures. Chembiochem, 17(23), 2274-2285. doi:10.1002/cbic.201600440
  123. Salvi, N., et al. (2016). Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation. J Phys Chem Lett, 7(13), 2483-2489. doi:10.1021/acs.jpclett.6b00885
  124. Sayou, C., et al. (2016). A SAM oligomerization domain shapes the genomic binding landscape of the LEAFY transcription factor. Nat Commun, 7, 11222. doi:10.1038/ncomms11222
  125. Schrader, J., et al. (2016). The inhibition mechanism of human 20Sproteasomes enables next-generation inhibitor design. Science, 353(6299), 594-598. doi:10.1126/science.aaf8993
  126. Schulte, T., et al. (2016). The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation. Scientific Reports, 6, 32371. doi:10.1038/srep32371
  127. Schulze, Jörg O., et al. (2016). Bidirectional Allosteric Communication between the ATP-Binding Site and the Regulatory PIF Pocket in PDK1 Protein Kinase. Cell Chemical Biology, 23(10), 1193-1205. doi:https://doi.org/10.1016/j.chembiol.2016.06.017
  128. Secci, E., et al. (2016). The Casein Kinase 2-Dependent Phosphorylation of NS5A Domain3 from HepatitisC Virus Followed by Time-Resolved NMR Spectroscopy. Chembiochem, 17(4), 328-333. doi:10.1002/cbic.201500551
  129. Senger, J., et al. (2016). Synthesis and Biological Investigation of Oxazole Hydroxamates as Highly Selective Histone Deacetylase 6 (HDAC6) Inhibitors. Journal of Medicinal Chemistry, 59(4), 1545-1555. doi:10.1021/acs.jmedchem.5b01493
  130. Sethu, R., et al. (2016). Reaction of PerR with Molecular Oxygen May Assist H2O2 Sensing in Anaerobes. ACS Chem Biol, 11(5), 1438-1444. doi:10.1021/acschembio.5b01054
  131. Sherman, S., et al. (2016). Resolving new ultrastructural features of cytokinetic abscission with soft-X-ray cryo-tomography. Scientific Reports, 6. doi:10.1038/srep27629
  132. Sicoli, G., et al. (2016). Fine-tuning of a radical-based reaction by radical S-adenosyl-L-methionine tryptophan lyase. Science, 351(6279), 1320-1323. doi:10.1126/science.aad8995
  133. Simonetti, A., et al. (2016). eIF3 Peripheral Subunits Rearrangement after mRNA Binding and Start-Codon Recognition. Molecular Cell, 63(2), 206-217. doi:10.1016/j.molcel.2016.05.033
  134. Sink, R., et al. (2016). Crystallographic Study of Peptidoglycan Biosynthesis Enzyme MurD: Domain Movement Revisited. Plos One, 11(3), e0152075. doi:10.1371/journal.pone.0152075
  135. Smock, R. G., et al. (2016). De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints. Cell, 164(3), 476-486. doi:10.1016/j.cell.2015.12.024
  136. Sonawane, P. D., et al. (2016). Plant cholesterol biosynthetic pathway overlaps with phytosterol metabolism. Nat Plants, 3, 16205. doi:10.1038/nplants.2016.205
  137. Stark, H., et al. (2016). Sample preparation of biological macromolecular assemblies for the determination of high-resolution structures by cryo-electron microscopy. Microscopy, 65(1), 23-34. doi:10.1093/jmicro/dfv367
  138. Stupfler, B., et al. (2016). BTG2 bridges PABPC1 RNA-binding domains and CAF1 deadenylase to control cell proliferation. Nature Communications, 7. doi:10.1038/ncomms10811
  139. Swale, C., et al. (2016). Structural characterization of recombinant IAV polymerase reveals a stable complex between viral PA-PB1 heterodimer and host RanBP5. Sci Rep, 6, 24727. doi:10.1038/srep24727
  140. Tabas-Madrid, D., et al. (2016). 3DBIONOTES: A unified, enriched and interactive view of macromolecular information. J Struct Biol, 194(2), 231-234. doi:10.1016/j.jsb.2016.02.007
  141. Thebault, S., et al. (2016). TCTP contains a BH3-like domain, which instead of inhibiting, activates Bcl-xL. Scientific Reports, 6. doi:10.1038/srep19725
  142. Timucin, E., et al. (2016). Probing the roles of two tryptophans surrounding the unique zinc coordination site in lipase family I.5. Proteins-Structure Function and Bioinformatics, 84(1), 129-142. doi:10.1002/prot.24961
  143. Uchikawa, E., et al. (2016). Structural Analysis of dsRNA Binding to Anti-viral Pattern Recognition Receptors LGP2 and MDA5. Molecular Cell, 62(4), 586-602. doi:https://doi.org/10.1016/j.molcel.2016.04.021
  144. Urbina, P., et al. (2016). Structural and Functional Investigation of the Ag(+)/Cu(+) Binding Domains of the Periplasmic Adaptor Protein SilB from Cupriavidus metallidurans CH34. Biochemistry, 55(20), 2883-2897. doi:10.1021/acs.biochem.6b00022
  145. Urzhumtseva, L., et al. (2016). COMPaRS: a stand-alone program for map comparison using quantile rank scaling. J Appl Crystallogr, 49(6), 2270-2275. doi:doi:10.1107/S1600576716015752
  146. Uzarska, M. A., et al. (2016). Mitochondrial Bol1 and Bol3 function as assembly factors for specific iron-sulfur proteins. Elife, 5. doi:10.7554/eLife.16673
  147. Valsecchi, W. M., et al. (2016). The role of the C-terminal region on the oligomeric state and enzymatic activity of Trypanosoma cruzi hypoxanthine phosphoribosyl transferase. Biochimica Et Biophysica Acta-Proteins and Proteomics, 1864(6), 655-666. doi:10.1016/j.bbapap.2016.03.005
  148. Vavrinska, A., et al. (2016). Impact of nucleic acid self-alignment in a strong magnetic field on the interpretation of indirect spin-spin interactions. Journal of Biomolecular Nmr, 64(1), 53-62. doi:10.1007/s10858-015-0005-x
  149. Veronesi, G., et al. (2016). Visualization, quantification and coordination of Ag+ ions released from silver nanoparticles in hepatocytes. Nanoscale, 8(38), 17012-17021. doi:10.1039/C6NR04381J
  150. Wallner-Liebmann, S., et al. (2016). Individual Human Metabolic Phenotype Analyzed by 1H NMR of Saliva Samples. Journal of Proteome Research, 15(6), 1787-1793. doi:10.1021/acs.jproteome.5b01060
  151. Wijckmans, E., et al. (2016). Functional and Biochemical Characterization of Alvinella pompejana Cys-Loop Receptor Homologues. Plos One, 11(3). doi:10.1371/journal.pone.0151183
  152. Yee, A. W., et al. (2016). Impact of Deuteration on the Assembly Kinetics of Transthyretin Monitored by Native Mass Spectrometry and Implications for Amyloidoses. Angew Chem Int Ed Engl, 55(32), 9292-9296. doi:10.1002/anie.201602747
  153. Zhao, Y., et al. (2016). Toremifene interacts with and destabilizes the Ebola virus glycoprotein. Nature, 535(7610), 169-172. doi:10.1038/nature18615
  154. Zhao, Y., et al. (2016). Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions. FEBS Lett, 590(5), 605-612. doi:10.1002/1873-3468.12089

2015

  1. Abla, M., et al. (2015). Micellar and biochemical properties of a propyl-ended fluorinated surfactant designed for membrane–protein study. Journal of Colloid and Interface Science, 445, 127-136. doi:https://doi.org/10.1016/j.jcis.2014.12.066
  2. Abrishami, V., et al. (2015). A fast iterative convolution weighting approach for gridding-based direct Fourier three-dimensional reconstruction with correction for the contrast transfer function. Ultramicroscopy, 157, 79-87. doi:10.1016/j.ultramic.2015.05.018
  3. Abrishami, V., et al. (2015). Alignment of direct detection device micrographs using a robust Optical Flow approach. Journal of Structural Biology, 189(3), 163-176. doi:10.1016/j.jsb.2015.02.001
  4. Afonina, Z. A., et al. (2015). Conformation transitions of eukaryotic polyribosomes during multi-round translation. Nucleic Acids Res, 43(1), 618-628. doi:10.1093/nar/gku1270
  5. Amara, M. S., et al. (2015). Hybrid, Tunable-Diameter, Metal Oxide Nanotubes for Trapping of Organic Molecules. Chemistry of Materials, 27(5), 1488-1494. doi:10.1021/cm503428q
  6. Andralojc, W., et al. (2015). Information content of long-range NMR data for the characterization of conformational heterogeneity. Journal of Biomolecular Nmr, 62(3), 353-371. doi:10.1007/s10858-015-9951-6
  7. Atanasova, N. S., et al. (2015). Haloarchaeal virus morphotypes. Biochimie, 118, 333-343. doi:https://doi.org/10.1016/j.biochi.2015.07.002
  8. Atanasova, N. S., et al. (2015). Haloviruses of archaea, bacteria, and eukaryotes. Curr Opin Microbiol, 25, 40-48. doi:10.1016/j.mib.2015.04.001
  9. Atanasova, N. S., et al. (2015). Comparison of lipid-containing bacterial and archaeal viruses. Adv Virus Res, 92, 1-61. doi:10.1016/bs.aivir.2014.11.005
  10. Awad, R., et al. (2015). The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif. FEBS Open Bio, 5, 99-106. doi:10.1016/j.fob.2015.01.009
  11. Banci, L., et al. (2015). Elucidating the Molecular Function of Human BOLA2 in GRX3-Dependent Anamorsin Maturation Pathway. Journal of the American Chemical Society, 137(51), 16133-16143. doi:10.1021/jacs.5b10592
  12. Banci, L., et al. (2015). N-terminal domains mediate 2Fe-2S cluster transfer from glutaredoxin-3 to anamorsin. Nature Chemical Biology, 11(10), 772-+. doi:10.1038/nchembio.1892
  13. Barbieri, L., et al. (2015). Protein interaction patterns in different cellular environments are revealed by in-cell NMR. Scientific Reports, 5. doi:10.1038/srep14456
  14. Baronti, L., et al. (2015). Dynamics of the intrinsically disordered C-terminal domain of the nipah virus nucleoprotein and interaction with the x domain of the phosphoprotein as unveiled by NMR spectroscopy. Chembiochem, 16(2), 268-276. doi:10.1002/cbic.201402534
  15. Bazin, A., et al. (2015). Structure and primase-mediated activation of a bacterial dodecameric replicative helicase. Nucleic Acids Res, 43(17), 8564-8576. doi:10.1093/nar/gkv792
  16. Bego, M. G., et al. (2015). Vpu Exploits the Cross-Talk between BST2 and the ILT7 Receptor to Suppress Anti-HIV-1 Responses by Plasmacytoid Dendritic Cells. PLoS Pathog, 11(7), e1005024. doi:10.1371/journal.ppat.1005024
  17. Beinsteiner, B., et al. (2015). IBiSS, a versatile and interactive tool for integrated sequence and 3D structure analysis of large macromolecular complexes. Bioinformatics, 31(20), 3339-3344. doi:10.1093/bioinformatics/btv347
  18. Berger, I., et al. (2015). Baculovirus expression: old dog, new tricks. Bioengineered, 6(6), 316-322. doi:10.1080/21655979.2015.1104433
  19. Bertsch, J., et al. (2015). Heterotrimeric NADH-Oxidizing Methylenetetrahydrofolate Reductase from the Acetogenic Bacterium Acetobacterium woodii. Journal of Bacteriology, 197(9), 1681-1689. doi:10.1128/jb.00048-15
  20. Bisson-Filho, A. W., et al. (2015). FtsZ filament capping by MciZ, a developmental regulator of bacterial division. Proc Natl Acad Sci U S A, 112(17), E2130-2138. doi:10.1073/pnas.1414242112
  21. Bittame, A., et al. (2015). Toxoplasma gondii: biochemical and biophysical characterization of recombinant soluble dense granule proteins GRA2 and GRA6. Biochem Biophys Res Commun, 459(1), 107-112. doi:10.1016/j.bbrc.2015.02.078
  22. Bleckmann, M., et al. (2015). Genomic Analysis and Isolation of RNA Polymerase II Dependent Promoters from Spodoptera frugiperda. Plos One, 10(8). doi:10.1371/journal.pone.0132898
  23. Boeri Erba, E., et al. (2015). Combining a NHS ester and glutaraldehyde improves crosslinking prior to MALDI MS analysis of intact protein complexes. J Mass Spectrom, 50(10), 1114-1119. doi:10.1002/jms.3626
  24. Bogorodskiy, A., et al. (2015). Nucleation and Growth of Membrane Protein Crystals In Meso—A Fluorescence Microscopy Study. Crystal Growth & Design, 15(12), 5656-5660. doi:10.1021/acs.cgd.5b01061
  25. Bonnefond, L., et al. (2015). Functional insights from high resolution structures of mouse protein arginine methyltransferase 6. Journal of Structural Biology, 191(2), 175-183. doi:https://doi.org/10.1016/j.jsb.2015.06.017
  26. Borshchevskiy, V., et al. (2015). Structural and Functional Investigation of Flavin Binding Center of the NqrC Subunit of Sodium-Translocating NADH: Quinone Oxidoreductase from Vibrio harveyi. Plos One, 10(3). doi:10.1371/journal.pone.0118548
  27. Brady, J. P., et al. (2015). A conserved amphipathic helix is required for membrane tubule formation by Yop1p. Proceedings of the National Academy of Sciences of the United States of America, 112(7), E639-E648. doi:10.1073/pnas.1415882112
  28. Bratanov, D., et al. (2015). An Approach to Heterologous Expression of Membrane Proteins. The Case of Bacteriorhodopsin. Plos One, 10(6), e0128390. doi:10.1371/journal.pone.0128390
  29. Burmeister, W. P., et al. (2015). Structure determination of feline calicivirus virus-like particles in the context of a pseudo-octahedral arrangement. Plos One, 10(3), e0119289. doi:10.1371/journal.pone.0119289
  30. Bussow, K. (2015). Stable mammalian producer cell lines for structural biology. Current Opinion in Structural Biology, 32, 81-90. doi:10.1016/j.sbi.2015.03.002
  31. Caillat, C., et al. (2015). Asymmetric ring structure of Vps4 required for ESCRT-III disassembly. Nature Communications, 6, 8781. doi:10.1038/ncomms9781 https://www.nature.com/articles/ncomms9781#supplementary-information
  32. Cerofolini, L., et al. (2015). Probing the interaction of distamycin A with S100 beta: the "unexpected" ability of S100 beta to bind to DNA-binding ligands. Journal of Molecular Recognition, 28(6), 376-384. doi:10.1002/jmr.2452
  33. Chakrabarti, A., et al. (2015). HDAC8: a multifaceted target for therapeutic interventions. Trends in Pharmacological Sciences, 36(7), 481-492. doi:10.1016/j.tips.2015.04.013
  34. Chari, A., et al. (2015). ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space. Nature Methods, 12(9), 859-+. doi:10.1038/nmeth.3493
  35. Cousido-Siah, A., et al. (2015). Structural analysis of sulindac as an inhibitor of aldose reductase and AKR1B10. Chemico-Biological Interactions, 234, 290-296. doi:10.1016/j.cbi.2014.12.018
  36. Crepin, T., et al. (2015). Polyproteins in structural biology. Curr Opin Struct Biol, 32, 139-146. doi:10.1016/j.sbi.2015.04.007
  37. DeBonis, S., et al. (2015). Self protein-protein interactions are involved in TPPP/p25 mediated microtubule bundling. Sci Rep, 5, 13242. doi:10.1038/srep13242
  38. Delaforge, E., et al. (2015). Large-Scale Conformational Dynamics Control H5N1 Influenza Polymerase PB2 Binding to Importin alpha. J Am Chem Soc, 137(48), 15122-15134. doi:10.1021/jacs.5b07765
  39. Dyachenko, A., et al. (2015). Tandem Native Mass-Spectrometry on Antibody-Drug Conjugates and Submillion Da Antibody-Antigen Protein Assemblies on an Orbitrap EMR Equipped with a High-Mass Quadrupole Mass Selector. Anal Chem, 87(12), 6095-6102. doi:10.1021/acs.analchem.5b00788
  40. Fadel, F., et al. (2015). New insights into the enzymatic mechanism of human chitotriosidase (CHIT1) catalytic domain by atomic resolution X-ray diffraction and hybrid QM/MM. Acta Crystallogr D Biol Crystallogr, 71(Pt 7), 1455-1470. doi:10.1107/s139900471500783x
  41. Fadel, F., et al. (2015). New insights into the enzymatic mechanism of human chitotriosidase (CHIT1) catalytic domain by atomic resolution X-ray diffraction and hybrid QM/MM. Acta Crystallographica Section D-Structural Biology, 71, 1455-1470. doi:10.1107/s139900471500783x
  42. Fanfrlik, J., et al. (2015). The Effect of Halogen-to-Hydrogen Bond Substitution on Human Aldose Reductase Inhibition. Acs Chemical Biology, 10(7), 1637-1642. doi:10.1021/acschembio.5b00151
  43. Faridounnia, M., et al. (2015). The Cerebro-oculo-facio-skeletal Syndrome Point Mutation F231L in the ERCC1 DNA Repair Protein Causes Dissociation of the ERCC1-XPF Complex. J Biol Chem, 290(33), 20541-20555. doi:10.1074/jbc.M114.635169
  44. Farkas, R., et al. (2015). Respiratory metabolism of salivary glands during the late larval and prepupal development of Drosophila melanogaster. J Insect Physiol, 81, 109-117. doi:10.1016/j.jinsphys.2015.06.013
  45. Felli, I. C., et al. (2015). Spin-state-selective methods in solution- and solid-state biomolecular 13C NMR. Prog Nucl Magn Reson Spectrosc, 84-85, 1-13. doi:10.1016/j.pnmrs.2014.10.001
  46. Gaubitz, C., et al. (2015). Molecular Basis of the Rapamycin Insensitivity of Target Of Rapamycin Complex 2. Mol Cell, 58(6), 977-988. doi:10.1016/j.molcel.2015.04.031
  47. Geertsma, E. R., et al. (2015). Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family. Nature Structural & Molecular Biology, 22(10), 803-808. doi:10.1038/nsmb.3091
  48. Gerlach, P., et al. (2015). Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter. Cell, 161(6), 1267-1279. doi:10.1016/j.cell.2015.05.006
  49. Gil-Carton, D., et al. (2015). Insight into the Assembly of Viruses with Vertical Single beta-barrel Major Capsid Proteins. Structure, 23(10), 1866-1877. doi:10.1016/j.str.2015.07.015
  50. Gimenez-Dejoz, J., et al. (2015). Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15: A Novel Human Retinaldehyde Reductase. Plos One, 10(7). doi:10.1371/journal.pone.0134506
  51. Gushchin, I., et al. (2015). Crystal structure of a light-driven sodium pump. Nat Struct Mol Biol, 22(5), 390-395. doi:10.1038/nsmb.3002
  52. Gutsche, I., et al. (2015). Structural virology. Near-atomic cryo-EM structure of the helical measles virus nucleocapsid. Science, 348(6235), 704-707. doi:10.1126/science.aaa5137
  53. Henrich, E., et al. (2015). Membrane protein production in Escherichia coli cell-free lysates. FEBS Lett, 589(15), 1713-1722. doi:10.1016/j.febslet.2015.04.045
  54. Hosek, T., et al. (2015). Longitudinal relaxation properties of H-1(N) and H-1(alpha) determined by direct-detected C-13 NMR experiments to study intrinsically disordered proteins (IDPs). Journal of Magnetic Resonance, 254, 19-26. doi:10.1016/j.jmr.2015.01.017
  55. Huet, T., et al. (2015). A Vitamin D Receptor Selectively Activated by Gemini Analogs Reveals Ligand Dependent and Independent Effects. Cell Reports, 10(4), 516-526. doi:10.1016/j.celrep.2014.12.045
  56. Jacomin, A. C., et al. (2015). The Deubiquitinating Enzyme UBPY Is Required for Lysosomal Biogenesis and Productive Autophagy in Drosophila. Plos One, 10(11). doi:10.1371/journal.pone.0143078
  57. Jacq, M., et al. (2015). Remodeling of the Z-Ring Nanostructure during the Streptococcus pneumoniae Cell Cycle Revealed by Photoactivated Localization Microscopy. MBio, 6(4). doi:10.1128/mBio.01108-15
  58. Kaplan, M., et al. (2015). Probing a cell-embedded megadalton protein complex by DNP-supported solid-state NMR. Nat Methods, 12(7), 649-652. doi:10.1038/nmeth.3406
  59. Karttunen, J., et al. (2015). Non-structural proteins P17 and P33 are involved in the assembly of the internal membrane-containing virus PRD1. Virology, 482, 225-233. doi:10.1016/j.virol.2015.03.049
  60. Kerfah, R., et al. (2015). CH3-specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample. J Biomol NMR, 63(4), 389-402. doi:10.1007/s10858-015-9998-4
  61. Kerfah, R., et al. (2015). Scrambling free combinatorial labeling of alanine-beta, isoleucine-delta1, leucine-proS and valine-proS methyl groups for the detection of long range NOEs. J Biomol NMR, 61(1), 73-82. doi:10.1007/s10858-014-9887-2
  62. Kerfah, R., et al. (2015). Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins. Curr Opin Struct Biol, 32, 113-122. doi:10.1016/j.sbi.2015.03.009
  63. Khatter, H., et al. (2015). Structure of the human 80S ribosome. Nature, 520(7549), 640-U338. doi:10.1038/nature14427
  64. Kragelj, J., et al. (2015). Structure and dynamics of the MKK7-JNK signaling complex. Proc Natl Acad Sci U S A, 112(11), 3409-3414. doi:10.1073/pnas.1419528112
  65. Kukumberg, P., et al. (2015). New perspectives in human tear analysis? Neuro endocrinology letters, 36(3), 185-186.
  66. LaGuerre, A., et al. (2015). Labeling of membrane proteins by cell-free expression. Methods Enzymol, 565, 367-388. doi:10.1016/bs.mie.2015.06.001
  67. Lancelot, J., et al. (2015). Schistosome sirtuins as drug targets. Future Medicinal Chemistry, 7(6), 765-782. doi:10.4155/fmc.15.24
  68. Lantez, V., et al. (2015). Rapid automated detergent screening for the solubilization and purification of membrane proteins and complexes. Engineering in Life Sciences, 15(1), 39-50. doi:10.1002/elsc.201400187
  69. Le Roy, A., et al. (2015). AUC and Small-Angle Scattering for Membrane Proteins. Methods Enzymol, 562, 257-286. doi:10.1016/bs.mie.2015.06.010
  70. Lebrette, H., et al. (2015). Novel insights into nickel import in Staphylococcus aureus: the positive role of free histidine and structural characterization of a new thiazolidine-type nickel chelator. Metallomics, 7(4), 613-621. doi:10.1039/c4mt00295d
  71. Lopez, J., et al. (2015). Intravacuolar Membranes Regulate CD8 T Cell Recognition of Membrane-Bound Toxoplasma gondii Protective Antigen. Cell Reports, 13(10), 2273-2286. doi:10.1016/j.celrep.2015.11.001
  72. Luchinat, E., et al. (2015). Combining in-cell NMR and X-ray fluorescence microscopy to reveal the intracellular maturation states of human superoxide dismutase 1. Chemical Communications, 51(3), 584-587. doi:10.1039/c4cc08129c
  73. Ma, P., et al. (2015). Observing the overall rocking motion of a protein in a crystal. Nature Communications, 6, 8361. doi:10.1038/ncomms9361 https://www.nature.com/articles/ncomms9361#supplementary-information
  74. Mance, D., et al. (2015). An Efficient Labelling Approach to Harness Backbone and Side-Chain Protons in 1H-Detected Solid-State NMR Spectroscopy. Angewandte Chemie International Edition, 54(52), 15799-15803. doi:10.1002/anie.201509170
  75. Marabini, R., et al. (2015). CTF Challenge: Result summary. Journal of Structural Biology, 190(3), 348-359. doi:10.1016/j.jsb.2015.04.003
  76. Martinelli, L., et al. (2015). A major determinant for gliding motility in Mycoplasma genitalium: the interaction between the terminal organelle proteins MG200 and MG491. J Biol Chem, 290(3), 1699-1711. doi:10.1074/jbc.M114.594762
  77. Mas y mas, S., et al. (2015). Analytical ultracentrifugation and preliminary X-ray studies of the chloroplast envelope quinone oxidoreductase homologue from Arabidopsis thaliana. Acta Crystallogr F Struct Biol Commun, 71(Pt 4), 455-458. doi:10.1107/s2053230x1500480x
  78. Mayer, F., et al. (2015). Na+ Transport by the A(1)A(O)-ATP Synthase Purified from Thermococcus onnurineus and Reconstituted into Liposomes. Journal of Biological Chemistry, 290(11), 6994-7002. doi:10.1074/jbc.M114.616862
  79. Melesina, J., et al. (2015). Homology modeling of parasite histone deacetylases to guide the structure-based design of selective inhibitors. Journal of Molecular Graphics & Modelling, 62, 342-361. doi:10.1016/j.jmgm.2015.10.006
  80. Monlezun, L., et al. (2015). PscI is a type III secretion needle anchoring protein with in vitro polymerization capacities. Mol Microbiol, 96(2), 419-436. doi:10.1111/mmi.12947
  81. Monod, A., et al. (2015). Learning from structure-based drug design and new antivirals targeting the ribonucleoprotein complex for the treatment of influenza. Expert Opin Drug Discov, 10(4), 345-371. doi:10.1517/17460441.2015.1019859
  82. Muñoz-García, J. C., et al. (2015). Langerin–Heparin Interaction: Two Binding Sites for Small and Large Ligands As Revealed by a Combination of NMR Spectroscopy and Cross-Linking Mapping Experiments. Journal of the American Chemical Society, 137(12), 4100-4110. doi:10.1021/ja511529x
  83. Newman, J. A., et al. (2015). Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes. Nucleic Acids Research, 43(10), 5221-5235. doi:10.1093/nar/gkv373
  84. Nguyen-Huynh, N. T., et al. (2015). Chemical cross-linking and mass spectrometry to determine the subunit interaction network in a recombinant human SAGA HAT subcomplex. Protein Science, 24(8), 1232-1246. doi:10.1002/pro.2676
  85. Nkizinkiko, Y., et al. (2015). Discovery of potent and selective nonplanar tankyrase inhibiting nicotinamide mimics. Bioorganic & Medicinal Chemistry, 23(15), 4139-4149. doi:https://doi.org/10.1016/j.bmc.2015.06.063
  86. Noguera, M. E., et al. (2015). Structural characterization of metal binding to a cold-adapted frataxin. Journal of Biological Inorganic Chemistry, 20(4), 653-664. doi:10.1007/s00775-015-1251-9
  87. Noirclerc-Savoye, M., et al. (2015). Tail proteins of phage T5: Investigation of the effect of the His6-tag position, from expression to crystallisation. Protein Expression and Purification, 109, 70-78. doi:https://doi.org/10.1016/j.pep.2015.02.003
  88. Nomine, Y., et al. (2015). Antibody Binding Selectivity: Alternative Sets of Antigen Residues Entail High-Affinity Recognition. Plos One, 10(12), e0143374. doi:10.1371/journal.pone.0143374
  89. Oikonomou, M., et al. (2015). Accurate DOSY measure for out-of-equilibrium systems using permutated DOSY (p-DOSY). Journal of Magnetic Resonance, 258, 12-16. doi:https://doi.org/10.1016/j.jmr.2015.06.002
  90. Orlov, I., et al. (2015). Live cell immunogold labelling of RNA polymerase II. Scientific Reports, 5. doi:10.1038/srep08324
  91. Osz, J., et al. (2015). Structural Basis of Natural Promoter Recognition by the Retinoid X Nuclear Receptor. Scientific Reports, 5, 8216. doi:10.1038/srep08216 https://www.nature.com/articles/srep08216#supplementary-information
  92. Oton, J., et al. (2015). Measurement of the modulation transfer function of an X-ray microscope based on multiple Fourier orders analysis of a Siemens star. Optics Express, 23(8), 9567-9572. doi:10.1364/oe.23.009567
  93. Pegeot, M., et al. (2015). Profiling sulfation/epimerization pattern of full-length heparan sulfate by NMR following cell culture C-13-glucose metabolic labeling. Glycobiology, 25(2), 151-156. doi:10.1093/glycob/cwu114
  94. Petit-Hartlein, I., et al. (2015). Biophysical and physiological characterization of ZraP from Escherichia coli, the periplasmic accessory protein of the atypical ZraSR two-component system. Biochem J, 472(2), 205-216. doi:10.1042/bj20150827
  95. Petrovskaya, L. E., et al. (2015). ESR - a retinal protein with unusual properties from Exiguobacterium sibiricum. Biochemistry (Mosc), 80(6), 688-700. doi:10.1134/s000629791506005x
  96. Philippe, J., et al. (2015). Mechanism of beta-Lactam Action in Streptococcus pneumoniae: the Piperacillin Paradox. Antimicrobial Agents and Chemotherapy, 59(1), 609-621. doi:10.1128/aac.04283-14
  97. Ponnusamy, R., et al. (2015). KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA. Nucleic Acids Research, 43(20), 10039-10054. doi:10.1093/nar/gkv987
  98. Postupalenko, V., et al. (2015). Protein Delivery System Containing a Nickel-Immobilized Polymer for Multimerization of Affinity-Purified His-Tagged Proteins Enhances Cytosolic Transfer. Angewandte Chemie-International Edition, 54(36), 10583-10586. doi:10.1002/anie.201505437
  99. Prechoux, A., et al. (2015). C5-epimerase and 2-O-sulfotransferase associate in vitro to generate contiguous epimerized and 2-O-sulfated heparan sulfate domains. ACS Chem Biol, 10(4), 1064-1071. doi:10.1021/cb501037a
  100. Quade, N., et al. (2015). Cryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-angstrom resolution. Nature Communications, 6. doi:10.1038/ncomms8646
  101. Ravera, E., et al. (2015). Differences in Dynamics between Crosslinked and Non-Crosslinked Hyaluronates Measured by using Fast Field-Cycling Relaxometry. Chemphyschem, 16(13), 2803-2809. doi:10.1002/cphc.201500446
  102. Ravera, E., et al. (2015). Biosilica-Entrapped Enzymes Studied by Using Dynamic Nuclear-Polarization-Enhanced High-Field NMR Spectroscopy. Chemphyschem, 16(13), 2751-2754. doi:10.1002/cphc.201500549
  103. Ravera, E., et al. (2015). NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins. Journal of Magnetic Resonance, 253, 60-70. doi:10.1016/j.jmr.2014.12.019
  104. Rippa, V., et al. (2015). Molecular Engineering of Ghfp, the Gonococcal Orthologue of Neisseria meningitidis Factor H Binding Protein. Clinical and Vaccine Immunology, 22(7), 769-777. doi:10.1128/cvi.00794-14
  105. Rostislavleva, K., et al. (2015). Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. Science, 350(6257), aac7365. doi:10.1126/science.aac7365
  106. Ruiz, F. X., et al. (2015). Structural Determinants of the Selectivity of 3-Benzyluracil-1-acetic Acids toward Human Enzymes Aldose Reductase and AKR1B10. Chemmedchem, 10(12), 1989-2003. doi:10.1002/cmdc.201500393
  107. Shaik, M. M., et al. (2015). A structural snapshot of type II pilus formation in Streptococcus pneumoniae. J Biol Chem, 290(37), 22581-22592. doi:10.1074/jbc.M115.647834
  108. Sheth, L. K., et al. (2015). Visualization and quality assessment of the contrast transfer function estimation. Journal of Structural Biology, 192(2), 222-234. doi:https://doi.org/10.1016/j.jsb.2015.06.012
  109. Skalova, T., et al. (2015). Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states. Acta Crystallographica Section D-Structural Biology, 71, 578-591. doi:10.1107/s1399004714027928
  110. Skolakova, P., et al. (2015). Unique C. elegans telomeric overhang structures reveal the evolutionarily conserved properties of telomeric DNA. Nucleic Acids Research, 43(9), 4733-4745. doi:10.1093/nar/gkv296
  111. Sólyom, Z., et al. (2015). The Disordered Region of the HCV Protein NS5A: Conformational Dynamics, SH3 Binding, and Phosphorylation. Biophysical Journal, 109(7), 1483-1496. doi:10.1016/j.bpj.2015.06.040
  112. Sorzano, C. O. S., et al. (2015). Fast and accurate conversion of atomic models into electron density maps. Aims Biophysics, 2(1), 8-20. doi:10.3934/biophy.2015.1.8
  113. Thierry, E., et al. (2015). Production and characterisation of Epstein-Barr virus helicase-primase complex and its accessory protein BBLF2/3. Virus Genes, 51(2), 171-181. doi:10.1007/s11262-015-1233-6
  114. Torchy, M. P., et al. (2015). Structure and function insights into the NuRD chromatin remodeling complex. Cellular and Molecular Life Sciences, 72(13), 2491-2507. doi:10.1007/s00018-015-1880-8
  115. Van Benschoten, A. H., et al. (2015). Predicting X-ray diffuse scattering from translation-libration-screw structural ensembles. Acta Crystallographica Section D-Structural Biology, 71, 1657-1667. doi:10.1107/s1399004715007415
  116. van Rooyen, J. M., et al. (2015). Recombinant expression, purification, and crystallization of the glutaminyl-tRNA synthetase from Toxoplasma gondii. Protein Expr Purif, 110, 115-121. doi:10.1016/j.pep.2015.02.017
  117. van Zundert, G. C., et al. (2015). DisVis: quantifying and visualizing accessible interaction space of distance-restrained biomolecular complexes. Bioinformatics, 31(19), 3222-3224. doi:10.1093/bioinformatics/btv333
  118. van Zundert, G. C. P., et al. (2015). Integrative Modeling of Biomolecular Complexes: HADDOCKing with Cryo-Electron Microscopy Data. Structure, 23(5), 949-960. doi:10.1016/j.str.2015.03.014
  119. Vangone, A., et al. (2015). Contacts-based prediction of binding affinity in protein-protein complexes. Elife, 4, e07454. doi:10.7554/eLife.07454
  120. Vernet, T., et al. (2015). Spot peptide arrays and SPR measurements: throughput and quantification in antibody selectivity studies. J Mol Recognit, 28(10), 635-644. doi:10.1002/jmr.2477
  121. Volbeda, A., et al. (2015). The crystal structure of the global anaerobic transcriptional regulator FNR explains its extremely fine-tuned monomer-dimer equilibrium. Science Advances, 1(11). doi:10.1126/sciadv.1501086
  122. Zhao, H. Y., et al. (2015). A Multilaboratory Comparison of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation. Plos One, 10(5). doi:10.1371/journal.pone.0126420

2014

  1. Afonina, Z. A., et al. (2014). Formation of circular polyribosomes on eukaryotic mRNA without cap-structure and poly(A)-tail: a cryo electron tomography study. Nucleic Acids Research, 42(14), 9461-9469. doi:10.1093/nar/gku599
  2. Amara, M. S., et al. (2014). Hexagonalization of Aluminogermanate Imogolite Nanotubes Organized into Closed-Packed Bundles. Journal of Physical Chemistry C, 118(17), 9299-9306. doi:10.1021/jp5029678
  3. Andralojc, W., et al. (2014). Exploring Regions of Conformational Space Occupied by Two-Domain Proteins. Journal of Physical Chemistry B, 118(36), 10576-10587. doi:10.1021/jp504820w
  4. Appolaire, A., et al. (2014). The TET2 and TET3 aminopeptidases from Pyrococcus horikoshii form a hetero-subunit peptidasome with enhanced peptide destruction properties. Molecular Microbiology, 94(4), 803-814. doi:10.1111/mmi.12775
  5. Asencio-Hernandez, J., et al. (2014). Reversible Amyloid Fiber Formation in the N Terminus of Androgen Receptor. Chembiochem, 15(16), 2370-2373. doi:10.1002/cbic.201402420
  6. Axford, D., et al. (2014). In cellulo structure determination of a novel cypovirus polyhedrin. Acta Crystallographica Section D-Biological Crystallography, 70, 1435-1441. doi:10.1107/s1399004714004714
  7. Banci, L., et al. (2014). Solid-state NMR studies of metal-free SOD1 fibrillar structures. Journal of Biological Inorganic Chemistry, 19(4-5), 659-666. doi:10.1007/s00775-014-1130-9
  8. Banci, L., et al. (2014). 2Fe-2S cluster transfer in iron-sulfur protein biogenesis. Proceedings of the National Academy of Sciences of the United States of America, 111(17), 6203-6208. doi:10.1073/pnas.1400102111
  9. Barbieri, L., et al. (2014). Structural insights of proteins in sub-cellular compartments: In-mitochondria NMR. Biochimica Et Biophysica Acta-Molecular Cell Research, 1843(11), 2492-2496. doi:10.1016/j.bbamcr.2014.06.009
  10. Belorusova, A. Y., et al. (2014). Structural Insights into the Molecular Mechanism of Vitamin D Receptor Activation by Lithocholic Acid Involving a New Mode of Ligand Recognition. Journal of Medicinal Chemistry, 57(11), 4710-4719. doi:10.1021/jm5002524
  11. Belorusova, A. Y., et al. (2014). Modulators of Vitamin D Nuclear Receptor: Recent Advances from Structural Studies. Current Topics in Medicinal Chemistry, 14(21), 2368-2377. doi:10.2174/1568026615666141208095937
  12. Bermejo-Das-Neves, C., et al. (2014). A comprehensive study of small non-frameshift insertions/deletions in proteins and prediction of their phenotypic effects by a machine learning method (KD4i). Bmc Bioinformatics, 15. doi:10.1186/1471-2105-15-111
  13. Bianco, M. I., et al. (2014). Biophysical characterization of the outer membrane polysaccharide export protein and the polysaccharide co-polymerase protein from Xanthomonas campestris. Protein Expression and Purification, 101, 42-53. doi:10.1016/j.pep.2014.06.002
  14. Blanc, M., et al. (2014). Intrinsic disorder within the erythrocyte binding-like proteins from Plasmodium falciparum. Biochimica Et Biophysica Acta-Proteins and Proteomics, 1844(12), 2306-2314. doi:10.1016/j.bbapap.2014.09.023
  15. Boland, C., et al. (2014). Cell-free expression and in meso crystallisation of an integral membrane kinase for structure determination. Cellular and Molecular Life Sciences, 71(24), 4895-4910. doi:10.1007/s00018-014-1655-7
  16. Brancaccio, D., et al. (2014). Formation of 4Fe-4S Clusters in the Mitochondrial Iron-Sulfur Cluster Assembly Machinery. Journal of the American Chemical Society, 136(46), 16240-16250. doi:10.1021/ja507822j
  17. Bui, S., et al. (2014). Direct Evidence for a Peroxide Intermediate and a Reactive Enzyme-Substrate-Dioxygen Configuration in a Cofactor-free Oxidase. Angewandte Chemie-International Edition, 53(50), 13710-13714. doi:10.1002/anie.201405485
  18. Cerofolini, L., et al. (2014). G-triplex structure and formation propensity. Nucleic Acids Research, 42(21), 13393-13404. doi:10.1093/nar/gku1084
  19. Chiron, L., et al. (2014). Efficient denoising algorithms for large experimental datasets and their applications in Fourier transform ion cyclotron resonance mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America, 111(4), 1385-1390. doi:10.1073/pnas.1306700111
  20. Ciofi-Baffoni, S., et al. (2014). The IR-N-15-HSQC-AP experiment: a new tool for NMR spectroscopy of paramagnetic molecules. Journal of Biomolecular Nmr, 58(2), 123-128. doi:10.1007/s10858-013-9810-2
  21. Corzilius, B., et al. (2014). Dynamic Nuclear Polarization of H-1, C-13, and Co-59 in a Tris(ethylenediamine)cobalt(III) Crystalline Lattice Doped with Cr(III). Journal of the American Chemical Society, 136(33), 11716-11727. doi:10.1021/ja5044374
  22. Cousido-Siah, A., et al. (2014). Identification of a novel polyfluorinated compound as a lead to inhibit the human enzymes aldose reductase and AKR1B10: structure determination of both ternary complexes and implications for drug design. Acta Crystallographica Section D-Biological Crystallography, 70, 889-903. doi:10.1107/s1399004713033452
  23. Crublet, E., et al. (2014). A Cost-Effective Protocol for the Parallel Production of Libraries of 13CH3-Specifically Labeled Mutants for NMR Studies of High Molecular Weight Proteins # T Structural Genomics(Vol. 1091, pp. 229-244).
  24. Cura, V., et al. (2014). Cloning, expression, purification and preliminary X-ray crystallographic analysis of mouse protein arginine methyltransferase 7. Acta Crystallographica Section F-Structural Biology Communications, 70, 80-86. doi:10.1107/s2053230x13032871
  25.  25, Cura, V., et al. (2014). Structural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active site. Acta Crystallographica Section D-Biological Crystallography, 70, 2401-2412. doi:10.1107/s1399004714014278
  26. Discola, K. F., et al. (2014). Membrane and Chaperone Recognition by the Major Translocator Protein PopB of the Type III Secretion System of Pseudomonas aeruginosa. Journal of Biological Chemistry, 289(6), 3591-3601. doi:10.1074/jbc.M113.517920
  27. Durand, A., et al. (2014). Mapping the Deubiquitination Module within the SAGA Complex. Structure, 22(11), 1553-1559. doi:10.1016/j.str.2014.07.017
  28. Egan, A. J. F., et al. (2014). Outer-membrane lipoprotein LpoB spans the periplasm to stimulate the peptidoglycan synthase PBP1B. Proceedings of the National Academy of Sciences of the United States of America, 111(22), 8197-8202. doi:10.1073/pnas.1400376111
  29. Ehrnstorfer, I. A., et al. (2014). Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport. Nat Struct Mol Biol, 21(11), 990-996. doi:10.1038/nsmb.2904
  30. Elsen, S., et al. (2014). A type III secretion negative clinical strain of Pseudomonas aeruginosa employs a two-partner secreted exolysin to induce hemorrhagic pneumonia. Cell Host Microbe, 15(2), 164-176. doi:10.1016/j.chom.2014.01.003
  31. Farkas, R., et al. (2014). Apocrine Secretion in Drosophila Salivary Glands: Subcellular Origin, Dynamics, and Identification of Secretory Proteins. Plos One, 9(4). doi:10.1371/journal.pone.0094383
  32. Felli, I. C., et al. (2014). In-cell C-13 NMR spectroscopy for the study of intrinsically disordered proteins. Nature Protocols, 9(9), 2005-2016. doi:10.1038/nprot.2014.124
  33. Flayhan, A., et al. (2014). Crystal Structure of pb9, the Distal Tail Protein of Bacteriophage T5: a Conserved Structural Motif among All Siphophages. Journal of Virology, 88(2), 820-828. doi:10.1128/jvi.02135-13
  34. Fragai, M., et al. (2014). SSNMR of biosilica-entrapped enzymes permits an easy assessment of preservation of native conformation in atomic detail. Chemical Communications, 50(4), 421-423. doi:10.1039/c3cc46896h
  35. Gabel, F., et al. (2014). Probing the Conformation of FhaC with Small-Angle Neutron Scattering and Molecular Modeling. Biophysical Journal, 107(1), 185-196. doi:10.1016/j.bpj.2014.05.025
  36. Gil-Caballero, S., et al. (2014). HNCA plus, HNCO plus, and HNCACB plus experiments: improved performance by simultaneous detection of orthogonal coherence transfer pathways. Journal of Biomolecular Nmr, 60(1), 1-9. doi:10.1007/s10858-014-9847-x
  37. Granell, M., et al. (2014). Crystallization of the carboxy-terminal region of the bacteriophage T4 proximal long tail fibre protein gp34. Acta Crystallographica Section F-Structural Biology Communications, 70, 970-975. doi:10.1107/s2053230x14010449
  38. Guilligay, D., et al. (2014). Comparative Structural and Functional Analysis of Orthomyxovirus Polymerase Cap-Snatching Domains. Plos One, 9(1). doi:10.1371/journal.pone.0084973
  39. Hamann, M. V., et al. (2014). The cooperative function of arginine residues in the Prototype Foamy Virus Gag C-terminus mediates viral and cellular RNA encapsidation. Retrovirology, 11. doi:10.1186/s12977-014-0087-7
  40. Hong, C., et al. (2014). A Structural Model of the Genome Packaging Process in a Membrane-Containing Double Stranded DNA Virus. Plos Biology, 12(12). doi:10.1371/journal.pbio.1002024
  41. Jean, N. L., et al. (2014). Elongated Structure of the Outer-Membrane Activator of Peptidoglycan Synthesis LpoA: Implications for PBP1A Stimulation. Structure, 22(7), 1047-1054. doi:10.1016/j.str.2014.04.017
  42. Jorgensen, R., et al. (2014). Structures of a human blood group glycosyltransferase in complex with a photo-activatable UDP-Gal derivative reveal two different binding conformations. Acta Crystallographica Section F-Structural Biology Communications, 70, 1015-1021. doi:10.1107/s2053230x1401259x
  43. Kannan, S., et al. (2014). Discovery of Inhibitors of Schistosoma mansoni HDAC8 by Combining Homology Modeling, Virtual Screening, and in Vitro Validation. Journal of Chemical Information and Modeling, 54(10), 3005-3019. doi:10.1021/ci5004653
  44. Khatter, H., et al. (2014). Purification, characterization and crystallization of the human 80S ribosome. Nucleic Acids Research, 42(6). doi:10.1093/nar/gkt1404
  45. Koehler, C., et al. (2014). DNA Binding by Sgf11 Protein Affects Histone H2B Deubiquitination by Spt-Ada-Gcn5-Acetyltransferase ( SAGA). Journal of Biological Chemistry, 289(13), 8989-8999. doi:10.1074/jbc.M113.500868
  46. Krupovic, M., et al. (2014). Conservation of major and minor jelly-roll capsid proteins in Polinton (Maverick) transposons suggests that they are bona fide viruses. Biology Direct, 9. doi:10.1186/1745-6150-9-6
  47. Kuznets, G., et al. (2014). A Relay Network of Extracellular Heme-Binding Proteins Drives C-albicans Iron Acquisition from Hemoglobin. Plos Pathogens, 10(10). doi:10.1371/journal.ppat.1004407
  48. Laffly, E., et al. (2014). Human ficolin-2 recognition versatility extended: An update on the binding of ficolin-2 to sulfated/phosphated carbohydrates. Febs Letters, 588(24), 4694-4700. doi:10.1016/j.febslet.2014.10.042
  49. Lai, R. P., et al. (2014). A fusion intermediate gp41 immunogen elicits neutralizing antibodies to HIV-1. J Biol Chem, 289(43), 29912-29926. doi:10.1074/jbc.M114.569566
  50. Le Roy, A., et al. (2014). Analytical Ultracentrifugation and Size-Exclusion Chromatography Coupled with Light Scattering for the Characterization of Membrane Proteins in Solution. In I. Mus-Veteau (Ed.), Membrane Proteins Production for Structural Analysis(pp. 267-287). New York, NY: Springer New York. 
  51. Lebars, I., et al. (2014). A fully enzymatic method for site-directed spin labeling of long RNA. Nucleic Acids Research, 42(15). doi:10.1093/nar/gku553     
  52. Lebreton, A., et al. (2014). Structural basis for the inhibition of the chromatin repressor BAHD1 by the bacterial nucleomodulin LntA. MBio, 5(1), e00775-00713. doi:10.1128/mBio.00775-13
  53. Lemaitre, C., et al. (2014). Nuclear position dictates DNA repair pathway choice. Genes & Development, 28(22), 2450-2463. doi:10.1101/gad.248369.114
  54. Luchinat, E., et al. (2014). In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants. Nature Communications, 5. doi:10.1038/ncomms6502
  55. Luhtanen, A. M., et al. (2014). Isolation and characterization of phage-host systems from the Baltic Sea ice. Extremophiles, 18(1), 121-130. doi:10.1007/s00792-013-0604-y
  56. Ma, P., et al. (2014). Bestimmung transienter Konformationszustände von Proteinen durch Festkörper-R1ρ-Relaxationsdispersions-NMR-Spektroskopie. Angewandte Chemie, 126(17), 4400-4405. doi:10.1002/ange.201311275
  57. Ma, P. X., et al. (2014). Probing Transient Conformational States of Proteins by Solid-State R11 Relaxation- Dispersion NMR Spectroscopy. Angewandte Chemie-International Edition, 53(17), 4312-4317. doi:10.1002/anie.201311275
  58. Maillard, A. P., et al. (2014). The Crystal Structure of the Anti-sigma Factor CnrY in Complex with the sigma Factor CnrH Shows a New Structural Class of Anti-sigma Factors Targeting Extracytoplasmic Function sigma Factors. Journal of Molecular Biology, 426(12), 2313-2327. doi:10.1016/j.jmb.2014.04.003
  59. Malet, H., et al. (2014). Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins. Elife, 3. doi:10.7554/eLife.03653
  60. Maletta, M., et al. (2014). The palindromic DNA-bound USP/EcR nuclear receptor adopts an asymmetric organization with allosteric domain positioning. Nature Communications, 5. doi:10.1038/ncomms5139
  61. Marquez, J. A., et al. (2014). CrystalDirect: a novel approach for automated crystal harvesting based on photoablation of thin films. Methods Mol Biol, 1091, 197-203. doi:10.1007/978-1-62703-691-7_14
  62. Martinez-Zapien, D., et al. (2014). Production and characterization of a retinoic acid receptor RAR gamma construction encompassing the DNA binding domain and the disordered N-terminal proline rich domain. Protein Expression and Purification, 95, 113-120. doi:10.1016/j.pep.2013.12.001
  63. Meola, A., et al. (2014). Robust and low cost uniform N-15-labeling of proteins expressed in Drosophila S2 cells and Spodoptera frugiperda Sf9 cells for NMR applications. Journal of Structural Biology, 188(1), 71-78. doi:10.1016/j.jsb.2014.08.002
  64. Michaelis, V. K., et al. (2014). Topical Developments in High-Field Dynamic Nuclear Polarization. Israel Journal of Chemistry, 54(1-2), 207-221. doi:10.1002/ijch.201300126
  65. Monttinen, H. A. M., et al. (2014). Automated Structural Comparisons Clarify the Phylogeny of the Right-Hand-Shaped Polymerases. Molecular Biology and Evolution, 31(10), 2741-2752. doi:10.1093/molbev/msu219
  66. Myasnikov, A. G., et al. (2014). The molecular structure of the left-handed supra-molecular helix of eukaryotic polyribosomes. Nature Communications, 5. doi:10.1038/ncomms6294
  67. Nguyen, H., et al. (2014). Heterogeneous biological data integration with declarative query language. Ibm Journal of Research and Development, 58(2-3). doi:10.1147/jrd.2014.2309032
  68. Nicolet, Y., et al. (2014). Crystal Structure of Tryptophan Lyase (NosL): Evidence for Radical Formation at the Amino Group of Tryptophan. Angewandte Chemie-International Edition, 53(44), 11840-11844. doi:10.1002/anie.201407320
  69. Obri, A., et al. (2014). ANP32E is a histone chaperone that removes H2A.Z from chromatin. Nature, 505(7485), 648-+. doi:10.1038/nature12922
  70. Pathare, G. R., et al. (2014). Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11. Proceedings of the National Academy of Sciences of the United States of America, 111(8), 2984-2989. doi:10.1073/pnas.1400546111
  71. Petoukhov, M. V., et al. (2014). Endophilin-A1 BAR domain interaction with arachidonyl CoA. Front Mol Biosci, 1, 20. doi:10.3389/fmolb.2014.00020
  72. Philippe, J., et al. (2014). The Elongation of Ovococci. Microbial Drug Resistance, 20(3), 215-221. doi:10.1089/mdr.2014.0032
  73. Piai, A., et al. (2014). "CON-CON'' assignment strategy for highly flexible intrinsically disordered proteins. Journal of Biomolecular Nmr, 60(4), 209-218. doi:10.1007/s10858-014-9867-6
  74. Pietila, M. K., et al. (2014). Archaeal viruses and bacteriophages: comparisons and contrasts. Trends in Microbiology, 22(6), 334-344. doi:10.1016/j.tim.2014.02.007
  75. Polovinkin, V., et al. (2014). Nanoparticle Surface-Enhanced Raman Scattering of Bacteriorhodopsin Stabilized by Amphipol A8-35. Journal of Membrane Biology, 247(9-10), 971-980. doi:10.1007/s00232-014-9701-9
  76. Preiss, L., et al. (2014). The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle. Molecular Microbiology, 92(5), 973-984. doi:10.1111/mmi.12605
  77. Puranik, S., et al. (2014). Structural Basis for the Oligomerization of the MADS Domain Transcription Factor SEPALLATA3 in Arabidopsis. Plant Cell, 26(9), 3603-3615. doi:10.1105/tpc.114.127910
  78. Radzimanowski, J., et al. (2014). Conformational plasticity of the Ebola virus matrix protein. Protein Science, 23(11), 1519-1527. doi:10.1002/pro.2541
  79. Ravera, E. (2014). The bigger they are, the harder they fall: A topical review on sedimented solutes for solid-state NMR. Concepts in Magnetic Resonance Part A, 43(6), 209-227. doi:10.1002/cmr.a.21318
  80. Ravera, E., et al. (2014). Pairwise binding competition experiments for sorting hub-protein/effector interaction hierarchy and simultaneous equilibria. Journal of Biomolecular Nmr, 60(1), 29-36. doi:10.1007/s10858-014-9846-y
  81. Ravera, E., et al. (2014). DNP-Enhanced MAS NMR of Bovine Serum Albumin Sediments and Solutions. Journal of Physical Chemistry B, 118(11), 2957-2965. doi:10.1021/jp500016f
  82. Ravera, E., et al. (2014). Insights into Domain-Domain Motions in Proteins and RNA from Solution NMR. Accounts of Chemical Research, 47(10), 3118-3126. doi:10.1021/ar5002318
  83. Reiser, J. B., et al. (2014). Analysis of Relationships between Peptide/MHC Structural Features and Naive T Cell Frequency in Humans. Journal of Immunology, 193(12), 5816-5826. doi:10.4049/jimmunol.1303084
  84. Rennella, E., et al. (2014). Measuring hydrogen exchange in proteins by selective water saturation in H-1-N-15 SOFAST/BEST-type experiments: advantages and limitations. Journal of Biomolecular Nmr, 60(2-3), 99-107. doi:10.1007/s10858-014-9857-8
  85. Rinaldelli, M., et al. (2014). Simultaneous use of solution NMR and X-ray data in REFMAC5 for joint refinement/detection of structural differences. Acta Crystallographica Section D-Biological Crystallography, 70, 958-967. doi:10.1107/s1399004713034160
  86. Robin, G., et al. (2014). Restricted Diversity of Antigen Binding Residues of Antibodies Revealed by Computational Alanine Scanning of 227 Antibody-Antigen Complexes. Journal of Molecular Biology, 426(22), 3729-3743. doi:10.1016/j.jmb.2014.08.013
  87. Sarre, A., et al. (2014). Expression, purification and crystallization of two endonuclease III enzymes from Deinococcus radiodurans. Acta Crystallographica Section F-Structural Biology Communications, 70, 1688-1692. doi:10.1107/s2053230x14024935
  88. Schanda, P., et al. (2014). Atomic Model of a Cell-Wall Cross-Linking Enzyme in Complex with an Intact Bacterial Peptidoglycan. Journal of the American Chemical Society, 136(51), 17852-17860. doi:10.1021/ja5105987
  89. Schulte, T., et al. (2014). The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold. Open Biology, 4(1). doi:10.1098/rsob.130090
  90. Shaik, M. M., et al. (2014). Structural Basis of Pilus Anchoring by the Ancillary Pilin RrgC of Streptococcus pneumoniae. Journal of Biological Chemistry, 289(24), 16988-16997. doi:10.1074/jbc.M114.555854
  91. Shevchenko, V., et al. (2014). Crystal Structure of Escherichia coli-Expressed Haloarcula marismortui Bacteriorhodopsin I in the Trimeric Form. Plos One, 9(12). doi:10.1371/journal.pone.0112873
  92. Sorzano, C. O. S., et al. (2014). Outlier detection for single particle analysis in Electron Microscopy.
  93. Stolfa, D. A., et al. (2014). Molecular Basis for the Antiparasitic Activity of a Mercaptoacetamide Derivative That Inhibits Histone Deacetylase 8 (HDAC8) from the Human Pathogen Schistosoma mansoni. Journal of Molecular Biology, 426(20), 3442-3453. doi:10.1016/j.jmb.2014.03.007
  94. Sueur, C., et al. (2014). Difference in cytokine production and cell cycle progression induced by Epstein-Barr virus Lmp1 deletion variants in Kmh2, a Hodgkin lymphoma cell line. Virology Journal, 11. doi:10.1186/1743-422x-11-94
  95. Sukackaite, R., et al. (2014). Structural and biophysical characterization of murine rif1 C terminus reveals high specificity for DNA cruciform structures. J Biol Chem, 289(20), 13903-13911. doi:10.1074/jbc.M114.557843
  96. Sumarheni, S., et al. (2014). Human Full-Length Coagulation Factor X and a GLA Domain-Derived 40-mer Polypeptide Bind to Different Regions of the Adenovirus Serotype 5 Hexon Capsomer. Human Gene Therapy, 25(4), 339-349. doi:10.1089/hum.2013.222
  97. Sun, X. Y., et al. (2014). Electrostatic Interactions Drive the Self-Assembly and the Transcription Activity of the Pseudomonas Phage phi 6 Procapsid. Journal of Virology, 88(12), 7112-7116. doi:10.1128/jvi.00467-14
  98. Tosi, T., et al. (2014). Structural Similarity of Secretins from Type II and Type Ill Secretion Systems. Structure, 22(9), 1348-1355. doi:10.1016/j.str.2014.07.005
  99. Tufar, P., et al. (2014). Crystal Structure of a PCP/Sfp Complex Reveals the Structural Basis for Carrier Protein Posttranslational Modification. Chemistry & Biology, 21(4), 552-562. doi:10.1016/j.chembiol.2014.02.014
  100. Urzhumtsev, A., et al. (2014). Metrics for comparison of crystallographic maps. Acta Crystallographica Section D-Biological Crystallography, 70, 2593-2606. doi:10.1107/s1399004714016289
  101. Vassal-Stermann, E., et al. (2014). Human L-Ficolin Recognizes Phosphocholine Moieties of Pneumococcal Teichoic Acid. Journal of Immunology, 193(11), 5699-5708. doi:10.4049/jimmunol.1400127
  102. Webert, H., et al. (2014). Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin. Nature Communications, 5. doi:10.1038/ncomms6013
  103. Wong, S. G., et al. (2014). Structure of a bacterial alpha(2)-macroglobulin reveals mimicry of eukaryotic innate immunity. Nature Communications, 5. doi:10.1038/ncomms5917
  104. Yabukarsi, F., et al. (2014). Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone. Nature Structural & Molecular Biology, 21(9), 754-759. doi:10.1038/nsmb.2868
  105. Zhao, Y. G., et al. (2014). Lysosome sorting of beta-glucocerebrosidase by LIMP-2 is targeted by the mannose 6-phosphate receptor. Nature Communications, 5. doi:10.1038/ncomms5321
  106. Zivanovic, Y., et al. (2014). Insights into Bacteriophage T5 Structure from Analysis of Its Morphogenesis Genes and Protein Components. Journal of Virology, 88(2), 1162-1174. doi:10.1128/jvi.02262-13

2013

  1. Abrishami, V., et al. (2013). A pattern matching approach to the automatic selection of particles from low-contrast electron micrographs. Bioinformatics, 29(19), 2460-2468. doi:10.1093/bioinformatics/btt429
  2. Bally, I., et al. (2013). Expression of recombinant human complement C1q allows identification of the C1r/C1s-binding sites. Proc Natl Acad Sci U S A, 110(21), 8650-8655. doi:10.1073/pnas.1304894110
  3. Banci, L., et al. (2013). Atomic-resolution monitoring of protein maturation in live human cells by NMR. Nature Chemical Biology, 9(5), 297-+. doi:10.1038/nchembio.1202
  4. Banci, L., et al. (2013). Molecular view of an electron transfer process essential for iron-sulfur protein biogenesis. Proceedings of the National Academy of Sciences of the United States of America, 110(18), 7136-7141. doi:10.1073/pnas.1302378110
  5. Banci, L., et al. (2013). Mechanistic Aspects of hSOD1 Maturation from the Solution Structure of Cu-I-Loaded hCCS Domain 1 and Analysis of Disulfide-Free hSOD1 Mutants. Chembiochem, 14(14), 1839-1844. doi:10.1002/cbic.201300042
  6. Banci, L., et al. (2013). Human anamorsin binds 2Fe-2S clusters with unique electronic properties. Journal of Biological Inorganic Chemistry, 18(8), 883-893. doi:10.1007/s00775-013-1033-1
  7. Bersch, B., et al. (2013). New insights into histidine triad proteins: solution structure of a Streptococcus pneumoniae PhtD domain and zinc transfer to AdcAII. Plos One, 8(11), e81168. doi:10.1371/journal.pone.0081168
  8. Bertini, I., et al. (2013). Solution structure and dynamics of human S100A14. Journal of Biological Inorganic Chemistry, 18(2), 183-194. doi:10.1007/s00775-012-0963-3
  9. Bertini, I., et al. (2013). Formation Kinetics and Structural Features of Beta-Amyloid Aggregates by Sedimented Solute NMR. Chembiochem, 14(14), 1891-1897. doi:10.1002/cbic.201300141
  10. Bertini, I., et al. (2013). SedNMR: On the Edge between Solution and Solid-State NMR. Accounts of Chemical Research, 46(9), 2059-2069. doi:10.1021/ar300342f
  11. Bhaumik, A., et al. (2013). NMR crystallography on paramagnetic systems: solved and open issues. Crystengcomm, 15(43), 8639-8656. doi:10.1039/c3ce41485j
  12. Bieniossek, C., et al. (2013). The architecture of human general transcription factor TFIID core complex. Nature, 493(7434), 699-702. doi:10.1038/nature11791
  13. Breyton, C., et al. (2013). Assessing the Conformational Changes of pb5, the Receptor-binding Protein of Phage T5, upon Binding to Its Escherichia coli Receptor FhuA. Journal of Biological Chemistry, 288(42), 30763-30772. doi:10.1074/jbc.M113.501536
  14. Cerofolini, L., et al. (2013). Examination of Matrix Metalloproteinase-1 in Solution A PREFERENCE FOR THE PRE-COLLAGENOLYSIS STATE. Journal of Biological Chemistry, 288(42), 30659-30671. doi:10.1074/jbc.M113.477240
  15. de la Rosa-Trevin, J. M., et al. (2013). Xmipp 3.0: An improved software suite for image processing in electron microscopy. Journal of Structural Biology, 184(2), 321-328. doi:10.1016/j.jsb.2013.09.015
  16. Delvecchio, M., et al. (2013). Structure of the p300 catalytic core and implications for chromatin targeting and HAT regulation. Nature Structural & Molecular Biology, 20(9), 1040-+. doi:10.1038/nsmb.2642
  17. Dian, C., et al. (2013). Structure of a Truncation Mutant of the Nuclear Export Factor CRM1 Provides Insights into the Auto-Inhibitory Role of Its C Terminal Helix. Structure, 21(8), 1338-1349. doi:10.1016/j.str.2013.06.003
  18. Duan, C. X., et al. (2013). Structural Evidence for a Two-Regime Photobleaching Mechanism in a Reversibly Switchable Fluorescent Protein. Journal of the American Chemical Society, 135(42), 15841-15850. doi:10.1021/ja406860e
  19. Durand, A., et al. (2013). Structure, assembly and dynamics of macromolecular complexes by single particle cryo-electron microscopy. Journal of Nanobiotechnology, 11. doi:10.1186/1477-3155-11-s1-s4
  20. Duval, M., et al. (2013). Escherichia coli Ribosomal Protein S1 Unfolds Structured mRNAs Onto the Ribosome for Active Translation Initiation. Plos Biology, 11(12). doi:10.1371/journal.pbio.1001731
  21. Fallecker, C., et al. (2013). Structural and functional characterization of the single-chain Fv fragment from a unique HCV E1E2-specific monoclonal antibody. Febs Letters, 587(20), 3335-3340. doi:10.1016/j.febslet.2013.07.057
  22. Favini-Stabile, S., et al. (2013). MreB and MurG as scaffolds for the cytoplasmic steps of peptidoglycan biosynthesis. Environmental Microbiology, 15(12), 3218-3228. doi:10.1111/1462-2920.12171
  23. Ferella, L., et al. (2013). SedNMR: a web tool for optimizing sedimentation of macromolecular solutes for SSNMR. Journal of Biomolecular Nmr, 57(4), 319-326. doi:10.1007/s10858-013-9795-x
  24. Fragai, M., et al. (2013). Practical considerations over spectral quality in solid state NMR spectroscopy of soluble proteins. Journal of Biomolecular Nmr, 57(2), 155-166. doi:10.1007/s10858-013-9776-0
  25. Hanhijarvi, K. J., et al. (2013). DNA Ejection from an Archaeal Virus-A Single-Molecule Approach. Biophysical Journal, 104(10), 2264-2272. doi:10.1016/j.bpj.2013.03.061
  26. Le Rouzic, E., et al. (2013). Dual inhibition of HIV-1 replication by integrase-LEDGF allosteric inhibitors is predominant at the post-integration stage. Retrovirology, 10. doi:10.1186/1742-4690-10-144
  27. Le Roy, A., et al. (2013). Sedimentation velocity analytical ultracentrifugation in hydrogenated and deuterated solvents for the characterization of membrane proteins. Methods Mol Biol, 1033, 219-251. doi:10.1007/978-1-62703-487-6_15
  28. Luchinat, C., et al. (2013). Water and Protein Dynamics in Sedimented Systems: A Relaxometric Investigation. Chemphyschem, 14(13), 3156-3161. doi:10.1002/cphc.201300167
  29. Maillot, B., et al. (2013). Structural and Functional Role of INI1 and LEDGF in the HIV-1 Preintegration Complex. Plos One, 8(4). doi:10.1371/journal.pone.0060734
  30. Marabini, R., et al. (2013). On the development of three new tools for organizing and sharing information in three-dimensional electron microscopy. Acta Crystallographica Section D-Biological Crystallography, 69, 695-700. doi:10.1107/s0907444913007038
  31. Mas, G., et al. (2013). Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins. Journal of Biomolecular Nmr, 57(3), 251-262. doi:10.1007/s10858-013-9785-z
  32. Meyer, S., et al. (2013). Multi-Host Expression System for Recombinant Production of Challenging Proteins. Plos One, 8(7). doi:10.1371/journal.pone.0068674
  33. Mori, M., et al. (2013). Discovery of a New Class of Potent MMP Inhibitors by Structure-Based Optimization of the Arylsulfonamide Scaffold. Acs Medicinal Chemistry Letters, 4(6), 565-569. doi:10.1021/ml300446a
  34. Neves, D., et al. (2013). Structure of Internalin InIK from the Human Pathogen Listeria monocytogenes. Journal of Molecular Biology, 425(22), 4520-4529. doi:10.1016/j.jmb.2013.08.010
  35. Noirclerc-Savoye, M., et al. (2013). Reconstitution of Membrane Protein Complexes Involved in Pneumococcal Septal Cell Wall Assembly. Plos One, 8(9). doi:10.1371/journal.pone.0075522
  36. Nozach, H., et al. (2013). High throughput screening identifies disulfide isomerase DsbC as a very efficient partner for recombinant expression of small disulfide-rich proteins in E. coli. Microbial Cell Factories, 12. doi:10.1186/1475-2859-12-37
  37. Papillon, J., et al. (2013). Structural insight into negative DNA supercoiling by DNA gyrase, a bacterial type 2A DNA topoisomerase. Nucleic Acids Research, 41(16), 7815-7827. doi:10.1093/nar/gkt560
  38. Pastor-Flores, D., et al. (2013). PIF-Pocket as a Target for C. albicans Pkh Selective Inhibitors. Acs Chemical Biology, 8(10), 2283-2292. doi:10.1021/cb400452z
  39. Peralta, B., et al. (2013). Mechanism of Membranous Tunnelling Nanotube Formation in Viral Genome Delivery. Plos Biology, 11(9). doi:10.1371/journal.pbio.1001667
  40. Petoukhov, M. V., et al. (2013). Reconstruction of Quaternary Structure from X-ray Scattering by Equilibrium Mixtures of Biological Macromolecules. Biochemistry, 52(39), 6844-6855. doi:10.1021/bi400731u
  41. Pietila, M. K., et al. (2013). Modified coat protein forms the flexible spindle-shaped virion of haloarchaeal virus His1. Environmental Microbiology, 15(6), 1674-1686. doi:10.1111/1462-2920.12030
  42. Pietila, M. K., et al. (2013). Insights into Head-Tailed Viruses Infecting Extremely Halophilic Archaea. Journal of Virology, 87(6), 3248-3260. doi:10.1128/jvi.03397-12
  43. Pietila, M. K., et al. (2013). Structure of the archaeal head-tailed virus HSTV-1 completes the HK97 fold story. Proceedings of the National Academy of Sciences of the United States of America, 110(26), 10604-10609. doi:10.1073/pnas.1303047110
  44. Ravantti, J., et al. (2013). Automatic comparison and classification of protein structures. Journal of Structural Biology, 183(1), 47-56. doi:10.1016/j.jsb.2013.05.007
  45. Ravera, E., et al. (2013). Dynamic Nuclear Polarization of Sedimented Solutes. Journal of the American Chemical Society, 135(5), 1641-1644. doi:10.1021/ja312553b
  46. Ravera, E., et al. (2013). Experimental Determination of Microsecond Reorientation Correlation Times in Protein Solutions. Journal of Physical Chemistry B, 117(13), 3548-3553. doi:10.1021/jp312561f
  47. Rennella, E., et al. (2013). Oligomeric States along the Folding Pathways of beta 2-Microglobulin: Kinetics, Thermodynamics, and Structure. Journal of Molecular Biology, 425(15), 2722-2736. doi:10.1016/j.jmb.2013.04.028
  48. Rissanen, I., et al. (2013). Bacteriophage P23-77 Capsid Protein Structures Reveal the Archetype of an Ancient Branch from a Major Virus Lineage. Structure, 21(5), 718-726. doi:10.1016/j.str.2013.02.026
  49. Rousseau, A., et al. (2013). TRAF4 Is a Novel Phosphoinositide-Binding Protein Modulating Tight Junctions and Favoring Cell Migration. Plos Biology, 11(12). doi:10.1371/journal.pbio.1001726
  50. Sencilo, A., et al. (2013). Snapshot of haloarchaeal tailed virus genomes. Rna Biology, 10(5), 803-816. doi:10.4161/rna.24045
  51. Signor, L., et al. (2013). Matrix-assisted Laser Desorption/Ionization Time of Flight (MALDI-TOF) Mass Spectrometric Analysis of Intact Proteins Larger than 100 kDa. Jove-Journal of Visualized Experiments(79). doi:10.3791/50635
  52. Simonetti, A., et al. (2013). Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor. Proceedings of the National Academy of Sciences of the United States of America, 110(39), 15656-15661. doi:10.1073/pnas.1309578110
  53. Simonetti, A., et al. (2013). Structure of the protein core of translation initiation factor 2 in apo, GTP-bound and GDP-bound forms. Acta Crystallographica Section D-Biological Crystallography, 69, 925-933. doi:10.1107/s0907444913006422
  54. Sun, X. Y., et al. (2013). Rescue of Maturation Off-Pathway Products in the Assembly of Pseudomonas Phage phi 6. Journal of Virology, 87(24), 13279-13286. doi:10.1128/jvi.02285-13
  55. Takacs, M., et al. (2013). The Asymmetric Binding of PGC-1 alpha to the ERR alpha and ERR gamma Nuclear Receptor Homodimers Involves a Similar Recognition Mechanism. Plos One, 8(7). doi:10.1371/journal.pone.0067810
  56. Urzhumtsev, A., et al. (2013). TLS from fundamentals to practice. Crystallography Reviews, 19(4), 230-270. doi:10.1080/0889311x.2013.835806
  57. Urzhumtseva, L., et al. (2013). On effective and optical resolutions of diffraction data sets. Acta Crystallographica Section D-Biological Crystallography, 69, 1921-1934. doi:10.1107/s0907444913016673
  58. Vitale, R., et al. (2013). Lipid fingerprints of intact viruses by MALDI-TOF/mass spectrometry. Biochimica Et Biophysica Acta-Molecular and Cell Biology of Lipids, 1831(4), 872-879. doi:10.1016/j.bbalip.2013.01.011
  59. Zanier, K., et al. (2013). Structural basis for hijacking of cellular LxxLL motifs by papillomavirus E6 oncoproteins. Science, 339(6120), 694-698. doi:10.1126/science.1229934
  60. Zapun, A., et al. (2013). In vitro Reconstitution of Peptidoglycan Assembly from the Gram-Positive Pathogen Streptococcus pneumoniae. Acs Chemical Biology, 8(12), 2688-2696. doi:10.1021/cb400575t

2012

  1. Aalto, A. P., et al. (2012). Snapshot of virus evolution in hypersaline environments from the characterization of a membrane-containing Salisaeta icosahedral phage 1. Proceedings of the National Academy of Sciences of the United States of America, 109(18), 7079-7084. doi:10.1073/pnas.1120174109
  2. Bertini, I., et al. (2012). On the use of ultracentrifugal devices for sedimented solute NMR. Journal of Biomolecular Nmr, 54(2), 123-127. doi:10.1007/s10858-012-9657-y
  3. Bieniossek, C., et al. (2012). MultiBac: expanding the research toolbox for multiprotein complexes. Trends in Biochemical Sciences, 37(2), 49-57. doi:10.1016/j.tibs.2011.10.005
  4. Burkhardt, J., et al. (2012). Unusual N-terminal alpha alpha beta alpha beta beta alpha Fold of PilQ from Thermus thermophilus Mediates Ring Formation and Is Essential for Piliation. Journal of Biological Chemistry, 287(11), 8484-8494. doi:10.1074/jbc.M111.334912
  5. Busschots, K., et al. (2012). Substrate-Selective Inhibition of Protein Kinase PDK1 by Small Compounds that Bind to the PIF-Pocket Allosteric Docking Site. Chemistry & Biology, 19(9), 1152-1163. doi:10.1016/j.chembiol.2012.07.017
  6. Jaakkola, S. T., et al. (2012). Closely Related Archaeal Haloarcula hispanica Icosahedral Viruses HHIV-2 and SH1 Have Nonhomologous Genes Encoding Host Recognition Functions. Journal of Virology, 86(9), 4734-4742. doi:10.1128/jvi.06666-11
  7. Kandiba, L., et al. (2012). Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid. Molecular Microbiology, 84(3), 578-593. doi:10.1111/j.1365-2958.2012.08045.x
  8. Kliefoth, M., et al. (2012). Genetic analysis of MA4079, an aldehyde dehydrogenase homolog, in Methanosarcina acetivorans. Archives of Microbiology, 194(2), 75-85. doi:10.1007/s00203-011-0727-4
  9. Oksanen, H. M., et al. (2012). Monolithic ion exchange chromatographic methods for virus purification. Virology, 434(2), 271-277. doi:10.1016/j.virol.2012.09.019
  10. Perez, A. B., et al. (2012). Extraction of Glomalin and Associated Compounds with Two Chemical Solutions in Cultivated Tepetates of Mexico. Communications in Soil Science and Plant Analysis, 43(1-2), 28-35. doi:10.1080/00103624.2012.631403
  11. Ruskamo, S., et al. (2012). The C-terminal rod 2 fragment of filamin A forms a compact structure that can be extended. Biochemical Journal, 446, 261-269. doi:10.1042/bj20120361
  12. Senčilo, A., et al. (2012). Related haloarchaeal pleomorphic viruses contain different genome types. Nucleic Acids Research, 40(12), 5523-5534. doi:10.1093/nar/gks215
  13. Sun, X. Y., et al. (2012). Probing, by Self-Assembly, the Number of Potential Binding Sites for Minor Protein Subunits in the Procapsid of Double-Stranded RNA Bacteriophage phi 6. Journal of Virology, 86(22), 12208-12216. doi:10.1128/jvi.01505-12
  14. Thielmann, Y., et al. (2012). The ESFRI Instruct Core Centre Frankfurt: automated high-throughput crystallization suited for membrane proteins and more. J Struct Funct Genomics, 13(2), 63-69. doi:10.1007/s10969-011-9118-y
  15. Trowitzsch, S., et al. (2012). MultiBac complexomics. Expert Review of Proteomics, 9(4), 363-373. doi:10.1586/epr.12.32 

2011

  1. Banci, L., et al. (2011). NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Diemutase. Journal of the American Chemical Society, 133(2), 345-349. doi:10.1021/ja1069689
  2. Bertini, I., et al. (2011). High-Resolution Characterization of Intrinsic Disorder in Proteins: Expanding the Suite of C-13-Detected NMR Spectroscopy Experiments to Determine Key Observables. Chembiochem, 12(15), 2347-2352. doi:10.1002/cbic.201100406
  3. Bertini, I., et al. (2011). C-13 Direct-Detection Biomolecular NMR Spectroscopy in Living Cells. Angewandte Chemie-International Edition, 50(10), 2339-2341. doi:10.1002/anie.201006636
  4. Bertini, I., et al. (2011). A New Structural Model of A beta(40) Fibrils. Journal of the American Chemical Society, 133(40), 16013-16022. doi:10.1021/ja2035859
  5. Daniel, E., et al. (2011). xtalPiMS: A PiMS-based web application for the management and monitoring of crystallization trials. Journal of Structural Biology, 175(2), 230-235. doi:10.1016/j.jsb.2011.05.008
  6. Hedderich, T., et al. (2011). PICKScreens, A New Database for the Comparison of Crystallization Screens for Biological Macromolecules. Crystal Growth & Design, 11(2), 488-491. doi:10.1021/cg101267n
  7. Imasaki, T., et al. (2011). Architecture of the Mediator head module. Nature, 475(7355), 240-U245. doi:10.1038/nature10162
  8. Morris, C., et al. (2011). The Protein Information Management System (PiMS): a generic tool for any structural biology research laboratory. Acta Crystallographica Section D-Biological Crystallography, 67, 249-260. doi:10.1107/s0907444911007943
  9. Perrakis, A., et al. (2011). From SPINE to SPINE-2 complexes and beyond. J Struct Biol, 175(2), 105. doi:10.1016/j.jsb.2011.05.013
  10. Popoff, V., et al. (2011). Several ADP-ribosylation Factor (Arf) Isoforms Support COPI Vesicle Formation. Journal of Biological Chemistry, 286(41), 35634-35642. doi:10.1074/jbc.M111.261800
  11. Praper, T., et al. (2011). Perforin activity at membranes leads to invaginations and vesicle formation. Proceedings of the National Academy of Sciences of the United States of America, 108(52), 21016-21021. doi:10.1073/pnas.1107473108
  12. Trowitzsch, S., et al. (2011). Light it up: Highly efficient multigene delivery in mammalian cells. Bioessays, 33(12), 946-955. doi:10.1002/bies.201100109
  13. Vijayachandran, L. S., et al. (2011). Robots, pipelines, polyproteins: Enabling multiprotein expression in prokaryotic and eukaryotic cells. Journal of Structural Biology, 175(2), 198-208. doi:10.1016/j.jsb.2011.03.007
  14. Yumerefendi, H., et al. (2011). Library-based methods for identification of soluble expression constructs. Methods, 55(1), 38-43. doi:10.1016/j.ymeth.2011.06.007
  15. Zhao, Y. G., et al. (2011). Automation of large scale transient protein expression in mammalian cells. Journal of Structural Biology, 175(2), 209-215. doi:10.1016/j.jsb.2011.04.017

2010

  1. Banci, L., et al. (2011). NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Diemutase. Journal of the American Chemical Society, 133(2), 345-349. doi:10.1021/ja1069689
  2. Bertini, I., et al. (2011). High-Resolution Characterization of Intrinsic Disorder in Proteins: Expanding the Suite of C-13-Detected NMR Spectroscopy Experiments to Determine Key Observables. Chembiochem, 12(15), 2347-2352. doi:10.1002/cbic.201100406
  3. Bertini, I., et al. (2011). C-13 Direct-Detection Biomolecular NMR Spectroscopy in Living Cells. Angewandte Chemie-International Edition, 50(10), 2339-2341. doi:10.1002/anie.201006636
  4. Bertini, I., et al. (2011). A New Structural Model of A beta(40) Fibrils. Journal of the American Chemical Society, 133(40), 16013-16022. doi:10.1021/ja2035859
  5. Daniel, E., et al. (2011). xtalPiMS: A PiMS-based web application for the management and monitoring of crystallization trials. Journal of Structural Biology, 175(2), 230-235. doi:10.1016/j.jsb.2011.05.008
  6. Hedderich, T., et al. (2011). PICKScreens, A New Database for the Comparison of Crystallization Screens for Biological Macromolecules. Crystal Growth & Design, 11(2), 488-491. doi:10.1021/cg101267n
  7. Imasaki, T., et al. (2011). Architecture of the Mediator head module. Nature, 475(7355), 240-U245. doi:10.1038/nature10162
  8. Morris, C., et al. (2011). The Protein Information Management System (PiMS): a generic tool for any structural biology research laboratory. Acta Crystallographica Section D-Biological Crystallography, 67, 249-260. doi:10.1107/s0907444911007943
  9. Perrakis, A., et al. (2011). From SPINE to SPINE-2 complexes and beyond. J Struct Biol, 175(2), 105. doi:10.1016/j.jsb.2011.05.013
  10. Popoff, V., et al. (2011). Several ADP-ribosylation Factor (Arf) Isoforms Support COPI Vesicle Formation. Journal of Biological Chemistry, 286(41), 35634-35642. doi:10.1074/jbc.M111.261800
  11. Praper, T., et al. (2011). Perforin activity at membranes leads to invaginations and vesicle formation. Proceedings of the National Academy of Sciences of the United States of America, 108(52), 21016-21021. doi:10.1073/pnas.1107473108
  12. Trowitzsch, S., et al. (2011). Light it up: Highly efficient multigene delivery in mammalian cells. Bioessays, 33(12), 946-955. doi:10.1002/bies.201100109
  13. Vijayachandran, L. S., et al. (2011). Robots, pipelines, polyproteins: Enabling multiprotein expression in prokaryotic and eukaryotic cells. Journal of Structural Biology, 175(2), 198-208. doi:10.1016/j.jsb.2011.03.007
  14. Yumerefendi, H., et al. (2011). Library-based methods for identification of soluble expression constructs. Methods, 55(1), 38-43. doi:10.1016/j.ymeth.2011.06.007
  15. Zhao, Y. G., et al. (2011). Automation of large scale transient protein expression in mammalian cells. Journal of Structural Biology, 175(2), 209-215. doi:10.1016/j.jsb.2011.04.017

2009

  1. Bieniossek, C., et al. (2009). Towards eukaryotic structural complexomics. J Struct Funct Genomics, 10(1), 37-46. doi:10.1007/s10969-008-9047-6
  2. Bieniossek, C., et al. (2009). Automated unrestricted multigene recombineering for multiprotein complex production. Nature Methods, 6(6), 447-U468. doi:10.1038/nmeth.1326
  3. Spadiut, O., et al. (2009). Improving thermostability and catalytic activity of pyranose 2-oxidase     from Trametes multicolor by rational and semi-rational design. Febs Journal, 276(3), 776-792. Doi:10.1111/j.1742-4658.2008.06823.x