2019

1. Abdelkareem, M., et al. (2019). Structural Basis of Transcription: RNA Polymerase Backtracking and Its Reactivation. Mol Cell, 75(2), 298-309.e294. doi:10.1016/j.molcel.2019.04.029
 
2. Abdelkareem, M. m., et al. (2019). Structural Basis of Transcription: RNA Polymerase Backtracking and Its Reactivation. Molecular Cell, 75(2), 298-309.e294. doi:https://doi.org/10.1016/j.molcel.2019.04.029
 
3. 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
 
4. Barbieri, L., et al. (2019). Backbone resonance assignment of human DJ-1 in the reduced state and in the cysteine sulfinic acid state. Biomol NMR Assign. doi:10.1007/s12104-019-09908-8
 
5. Becatti, M., et al. (2019). Different Antioxidant Efficacy of Two MnII-Containing Superoxide Anion Scavengers on Hypoxia/Reoxygenation-Exposed Cardiac Muscle Cells. Scientific Reports, 9(1), 10320. doi:10.1038/s41598-019-46476-2
 
6. 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. J Phys Chem B, 123(20), 4380-4386. doi:10.1021/acs.jpcb.9b02381
 
7. Brennecke, P. e. a. (2019). EU-OPENSCREEN: A Novel Collaborative Approach to Facilitate Chemical Biology. Life Sciences R&D, 24(3), 398-413. doi:https://doi.org/10.1177/2472555218816276
 
8. Brenzinger, S., et al. (2019). Structural and Proteomic Changes in Viable but Non-culturable Vibrio cholerae. Front Microbiol, 10, 793. doi:10.3389/fmicb.2019.00793
 
9. Camponeschi, F. (2019). Metal cofactors trafficking and assembly in the cell: a molecular view. Pure and Applied Chemistry, 91(2), 231-245. doi: https://doi.org/10.1515/pac-2018-0720
 
10. 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
 
11. 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
 
12. 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:https://doi.org/10.1016/j.bpj.2018.11.3132
 
13. Cerofolini, L., et al. (2019). Structural characterization of a protein adsorbed on aluminum hydroxide adjuvant in vaccine formulation. NPJ Vaccines, 4, 20. doi:10.1038/s41541-019-0115-7
 
14. 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. J Phys Chem Lett, 10(13), 3610-3614. doi:10.1021/acs.jpclett.9b01128
 
15. 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
 
16. 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
 
17. 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
 
18. De Colibus, L., et al. (2019). Assembly of complex viruses exemplified by a halophilic euryarchaeal virus. Nat Commun, 10(1), 1456. doi:10.1038/s41467-019-09451-z
 
19. 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
 
20. Decelle, J., et al. (2019). Algal Remodeling in a Ubiquitous Planktonic Photosymbiosis. Curr Biol, 29(6), 968-978.e964. doi:10.1016/j.cub.2019.01.073
 
21. 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, 116(10), 4256. doi:10.1073/pnas.1816417116
 
22. Desfosses, A., et al. (2019). Atomic structures of an entire contractile injection system in both the extended and contracted states. Nat Microbiol. doi:10.1038/s41564-019-0530-6
 
23. 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. Sci Rep, 9(1), 600. doi:10.1038/s41598-018-37306-y
 
24. Errasti-Murugarren, E., et al. (2019). L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction. Nature Communications, 10(1), 1807. doi:10.1038/s41467-019-09837-z
 
25. 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:https://doi.org/10.1016/j.kint.2019.02.017
 
26. Favier, A., et al. (2019). NMRlib: user-friendly pulse sequence tools for Bruker NMR spectrometers. J Biomol NMR, 73(5), 199-211. doi:10.1007/s10858-019-00249-1
 
27. Fenwick, C., et al. (2019). Tumor suppression of novel anti-PD-1 antibodies mediated through CD28 costimulatory pathway. J Exp Med, 216(7), 1525-1541. doi:10.1084/jem.20182359
 
28. Gabel, F. E., S.; Perez, J.; Girard, E. (2019). Medical contrast media as possible tools for SAXS contrast variation. Iucrj, 6(4), 521-525. doi:doi:10.1107/S2052252519005943
 
29. Galves, M., et al. (2019). Ubiquitin Signaling and Degradation of Aggregate-Prone Proteins. Trends in Biochemical Sciences. doi:https://doi.org/10.1016/j.tibs.2019.04.007
 
30. Garratt, R. C. (2019). A brief history of protein crystallography in Brazil. Biophys Rev, 509-511. doi:10.1007/s12551-019-00562-x
 
31. Gauto, D. F., et al. (2019). Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications, 10(1), 2697. doi:10.1038/s41467-019-10490-9
 
32. Ghini, V., et al. (2019). About the use of (13)C-(13)C NOESY in bioinorganic chemistry. J Inorg Biochem, 192, 25-32. doi:10.1016/j.jinorgbio.2018.12.006
 
33. 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 Crystallogr D Biol Crystallogr, 75(3), 317-324. doi:https://doi.org/10.1107/S2059798319000214
 
34. 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
 
35. 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
 
36. 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. The Journal of Physical Chemistry B, 123(24), 5048-5058. doi:10.1021/acs.jpcb.9b02293
 
37. 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
 
38. Howard, S. P., et al. (2019). Structure and assembly of pilotin-dependent and -independent secretins of the type II secretion system. PLoS Pathog, 15(5), e1007731. doi:10.1371/journal.ppat.1007731
 
39. Ilca, S. L., et al. (2019). Multiple Liquid Crystalline Geometries of Highly Complicated Nucleic Acid in a dsRNA Virus. Nature, 570(7760), 252-256. doi: 10.1038/s41586-019-1229-9
 
40. Ivic, N., et al. (2019). Fuzzy Interactions Form and Shape the Histone Transport Complex. Molecular Cell, 73(6), 1191-1203.e1196. doi:https://doi.org/10.1016/j.molcel.2019.01.032
 
41. 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
 
42. Kolesnikova, O., et al. (2019). TFIIH: A multi-subunit complex at the cross-roads of transcription and DNA repair. Adv Protein Chem Struct Biol, 115, 21-67. doi:10.1016/bs.apcsb.2019.01.003
 
43. 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), 5822. doi:10.1038/s41598-019-41925-4
 
44. Kuzina, E. S., et al. (2019). Structures of ligand-occupied beta-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity. Proc Natl Acad Sci U S A, 116(16), 7819-7824. doi:10.1073/pnas.1822055116
 
45. 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), 4656. doi:10.1038/s41598-019-40966-z
 
46. Laverty, D., et al. (2019). Cryo-EM structure of the human α1β3γ2 GABAA receptor in a lipid bilayer. Nature, 565(7740), 516-520. doi:10.1038/s41586-018-0833-4
 
47. 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
 
48. Lombardi, C., et al. (2019). Structural and Functional Characterization of the Type Three Secretion System (T3SS) Needle of Pseudomonas aeruginosa. Front Microbiol, 10, 573. doi:10.3389/fmicb.2019.00573
 
49. Lombardo, C. M., et al. (2019). Design and Structure Determination of a Composite Zinc Finger Containing a Nonpeptide Foldamer Helical Domain. J Am Chem Soc, 141(6), 2516-2525. doi:10.1021/jacs.8b12240
 
50. 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 Crystallogr D Biol Crystallogr, 75, 79-89. doi:doi:10.1107/S2059798318016959
 
51. Malanho Silva, J., et al. (2019). Metal centers in biomolecular solid-state NMR. Journal of Structural Biology, 206(1), 99-109. doi:https://doi.org/10.1016/j.jsb.2018.11.013
 
52. Mantynen, S., et al. (2019). Half a Century of Research on Membrane-Containing Bacteriophages: Bringing New Concepts to Modern Virology. Viruses, 11(1). doi:10.3390/v11010076
 
53. Masiulis, S., et al. (2019). GABAA receptor signalling mechanisms revealed by structural pharmacology. Nature, 565(7740), 454-459. doi:10.1038/s41586-018-0832-5
 
54. Maurice, F., et al. (2019). In vitro dimerization of human RIO2 kinase. Rna Biology, 1-10. doi:10.1080/15476286.2019.1653679
 
55. 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
 
56. 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(1), 
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57. Morris, C., et al. (2019). West-Life: A Virtual Research Environment for structural biology. Journal of Structural Biology: X, 1, 100006. doi:https://doi.org/10.1016/j.yjsbx.2019.100006
 
58. 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:https://doi.org/10.1016/j.jcis.2019.06.071
 
59. Njume, F. N., et al. (2019). Identification and characterization of the Onchocerca volvulus Excretory Secretory Product Ov28CRP, a putative GM2 activator protein. PLoS Negl Trop Dis, 13(7), e0007591. doi:10.1371/journal.pntd.0007591
 
60. 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
 
61. Pereira Aguilar, P., et al. (2019). Polymer-grafted chromatography media for the purification of enveloped virus-like particles, exemplified with HIV-1 gag VLP. Vaccine. doi:https://doi.org/10.1016/j.vaccine.2019.07.001
 
62. Polykretis, P., et al. (2019). Cadmium effects on superoxide dismutase 1 in human cells revealed by NMR. Redox Biol, 21, 101102. doi:10.1016/j.redox.2019.101102
 
63. Pozzi, C., et al. (2019). Effect of the point mutation H54N on the ferroxidase process of Rana catesbeiana H' ferritin. J Inorg Biochem, 197, 110697. doi:10.1016/j.jinorgbio.2019.110697
 
64. 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.e1636. doi:https://doi.org/10.1016/j.cub.2019.04.032
 
65. Ravera, E., et al. (2019). What are the methodological and theoretical prospects for paramagnetic NMR in structural biology? A glimpse into the crystal ball. J Magn Reson, 306, 173-179. doi:10.1016/j.jmr.2019.07.027
 
66. Rochel, N., et al. (2019). Recurrent activating mutations of PPARγ associated with luminal bladder tumors. Nature Communications, 10(1), 253. doi:10.1038/s41467-018-08157-y
 
67. Ruprecht, J. J., et al. (2019). The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier. Cell, 176(3), 435-447.e415. doi:10.1016/j.cell.2018.11.025
 
68. Salvador, D., et al. (2019). Minimal nanodisc without exogenous lipids for stabilizing membrane proteins in detergent-free buffer. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1861(4), 852-860. doi:https://doi.org/10.1016/j.bbamem.2019.01.013
 
69. Schiavina, M., et al. (2019). Taking Simultaneous Snapshots of Intrinsically Disordered Proteins in Action. Biophysical Journal, 117(1), 46-55. doi:https://doi.org/10.1016/j.bpj.2019.05.017
 
70. Sigoillot, M., et al. (2019). Domain-interface dynamics of CFTR revealed by stabilizing nanobodies. Nature Communications, 10(1), 2636. doi:10.1038/s41467-019-10714-y
 
71. 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
 
72. Skalova, T. B., J.; Stransky, J.; Koval T.; Duskova, J.; Zhao, Y.; Harlos, K.; Vanek, O.; Dohnalek, J. (2019). Structure of human natural killer cell receptor NKR-P1 in complex with its ligand LLT1. Acta Crystallographica Section A Foundations and Advances(74), e225. doi: 10.1107/S2053273318091775
 
73. Strokappe, M. N. H., Miriam; Rutten, Lucy; Mccoy, E. Laura; Back, W. Jaap; Caillat, Christophe; Haffke, Matthias; Weiss, A. Robin; Weissenhorn, Winfried; Verrips, Theo. (2019). Super Potent Bispecific Llama VHH Antibodies Neutralize HIV via a Combination of gp41 and gp120 Epitopes. Antibodies, 8(2), 38. doi:https://doi.org/10.3390/antib8020038
 
74. 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, 100168. doi:https://doi.org/10.1016/j.impact.2019.100168
 
75. Teulon, J.-M. G., Christian; Chantalat, Louis; Moriscot, Christine; Cambedouzou, Julien; Odorico, Michael; Ravaux, Johann; Podor, Renaud; Gerdil, Adèle; Habert, Aurélie; Herlin-Boime, Nathalie; Chen, W. Shu-wen; Pellequer, Jean-Luc. (2019). On the Operational Aspects of Measuring Nanoparticle Sizes. Nanomaterials, 9(1), 18. doi:doi:10.3390/nano9010018
 
76. Torra, J., et al. (2019). Tailing miniSOG: structural bases of the complex photophysics of a flavin-binding singlet oxygen photosensitizing protein. Scientific Reports, 9(1), 2428. doi:10.1038/s41598-019-38955-3
 
77. Uchański, T., et al. (2019). An improved yeast surface display platform for the screening of nanobody immune libraries. Scientific Reports, 9(1), 382. doi:10.1038/s41598-018-37212-3
 
78. 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
 
79. Urzhumtseva, L., et al. (2019). {\it py_convrot}: rotation conventions, to understand and to apply. J Appl Crystallogr, 52(4), 869-881. doi:10.1107/S1600576719007313
 
80. 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. J Med Chem. doi:10.1021/acs.jmedchem.9b00931
 
81. 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
 
82. 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(1), 1181. doi:10.1038/s41467-019-09220-y
 
83. 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
 
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2018 

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 18. Capper, M. J., et al. (2018). Thecysteine-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 andurinary metabolomic profiles of Down syndrome correlate with alteration ofmitochondrial metabolism. Scientific Reports, 8(1), 2977.doi:10.1038/s41598-018-20834-y

 20. Carlon, A., et al. (2018). JointX-ray/NMR structure refinement of multidomain/multisubunit systems. J BiomolNMR. doi:10.1007/s10858-018-0212-3

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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

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 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

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 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

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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.  Bermel, W., et al. (2010). Exclusively Heteronuclear NMR Experiments to Obtain Structural and Dynamic Information on Proteins. Chemphyschem, 11(3), 689-695. doi:10.1002/cphc.200900772

 2. Borsi, V., et al. (2010). Entropic Contribution to the Linking Coefficient in Fragment Based Drug Design: A Case Study. Journal of Medicinal Chemistry, 53(10), 4285-4289. doi:10.1021/jm901723z

 3. Krah, A., et al. (2010). Structural and energetic basis for H+ versus Na+ binding selectivity in ATP synthase Fo rotors. Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1797(6), 763-772. doi:https://doi.org/10.1016/j.bbabio.2010.04.014

 4. Marcia, M., et al. (2010). Characterizing a monotopic membrane enzyme. Biochemical, enzymatic and crystallization studies on Aquifex aeolicus sulfide:quinone oxidoreductase. Biochimica Et Biophysica Acta-Biomembranes, 1798(11), 2114-2123. doi:10.1016/j.bbamem.2010.07.033

 5. Pogoryelov, D., et al. (2010). Microscopic rotary mechanism of ion translocation in the F-0 complex of ATP synthases. Nature Chemical Biology, 6(12), 891-899. doi:10.1038/nchembio.457

 6. Trowitzsch, S., et al. (2010). New baculovirus expression tools for recombinant protein complex production. Journal of Structural Biology, 172(1), 45-54. doi:10.1016/j.jsb.2010.02.010



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