1. Abrishami, V., et al. (2021). Localized reconstruction in Scipion expedites the analysis of symmetry mismatches in cryo-EM data. Progress in Biophysics & Molecular Biology. 160:43-52. doi: 10.1016/j.pbiomolbio.2020.05.004
  2. Alqabandi, M., et al. (2021). The ESCRT-III isoforms CHMP2A and CHMP2B display different effects on membranes upon polymerization. BMC Biology. 19(1):18. doi: 10.1186/s12915-021-00983-9
  3. Altincekic, N., et al. (2021). Large-Scale Recombinant Production of the SARS-CoV-2 Proteome for High-Throughput and Structural Biology Applications. Frontiers in Molecular Biosciences. 8:25. doi: 10.3389/fmolb.2021.653148
  4. 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
  5. 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
  6. Bally, I., et al. (2021). Functional recombinant human complement C1q with different affinity tags. Journal of Immunological Methods. 492:8. doi: 10.1016/j.jim.2021.113001
  7. Bally, I., et al. (2021). Functional recombinant human complement C1q with different affinity tags. Journal of Immunological Methods. 492:8. doi: 10.1016/j.jim.2021.113001
  8. Banchelli, M., et al. (2021). Probing the Structure of Toxic Amyloid-beta Oligomers with Electron Spin Resonance and Molecular Modeling. ACS Chemical Neuroscience. 12(7):1150-1161. doi: 10.1021/acschemneuro.0c00714
  9. 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. Jove-Journal of Visualized Experiments. (169):17. doi: 10.3791/62323
  10. Bauer, V., et al. (2021). Conformational editing of intrinsically disordered protein by alpha-methylation. Chemical Science. 12(3):1080-1089. doi: 10.1039/d0sc04482b
  11. Beinsteiner, B., et al. (2021). A structural signature motif enlightens the origin and diversification of nuclear receptors. Plos Genetics. 17(4):32. doi: 10.1371/journal.pgen.1009492
  12. Bertling, E., et al. (2021). Carbonic anhydrase seven bundles filamentous actin and regulates dendritic spine morphology and density. EMBO Reports. 22(4):17. doi: 10.15252/embr.202050145
  13. Blum, T. B., et al. (2021). Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals. Acta Crystallographica Section D: Structural Biology. 77(1):75-85. doi: doi:10.1107/S2059798320014540
  14. 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. International Journal of Biological Macromolecules. 171:89-99. doi: 10.1016/j.ijbiomac.2020.12.190
  15. Calisto, B. M., et al. (2021). Sulfotyrosine-Mediated Recognition of Human Thrombin by a Tsetse Fly Anticoagulant Mimics Physiological Substrates. Cell Chemical Biology. 28(1):26-+. doi: 10.1016/j.chembiol.2020.10.002
  16. Caulier, B., et al. (2021). Evaluation of the human type 3 adenoviral dodecahedron as a vector to target acute myeloid leukemia. Molecular Therapy-Methods & Clinical Development. 20:181-190. doi: 10.1016/j.omtm.2020.11.009
  17. Chikunova, A., et al. (2021). Conserved residues Glu37 and Trp229 play an essential role in protein folding of beta-lactamase. FEBS Journal.15. doi: 10.1111/febs.15854
  18. Conrady, M. C., et al. (2021). Structure of High-Risk Papillomavirus 31 E6 Oncogenic Protein and Characterization of E6/E6AP/p53 Complex Formation. Journal of Virology. 95(2):15. doi: 10.1128/jvi.00730-20
  19. Cussol, L., et al. (2021). Structural Basis for alpha-Helix Mimicry and Inhibition of Protein-Protein Interactions with Oligourea Foldamers. Angewandte Chemie-International Edition. 60(5):2296-2303. doi: 10.1002/anie.202008992
  20. Daniel, E., et al. (2021). IceBear: an intuitive and versatile web application for research-data tracking from crystallization experiment to PDB deposition. Acta Crystallographica Section D-Structural Biology. 77:151-163. doi: 10.1107/s2059798320015223
  21. 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
  22. 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
  23. 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
  24. 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
  25. Duraffourg, N., et al. (2021). Hybrid Amyloid-Based Redox Hydrogel for Bioelectrocatalytic H-2 Oxidation. Angewandte Chemie-International Edition.11. doi: 10.1002/anie.202101700
  26. 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
  27. Edwards, R., et al. (2021). The mitochondrial intermembrane space: the most constricted mitochondrial sub-compartment with the largest variety of protein import pathways. Open Biology. 11(3):13. doi: 10.1098/rsob.210002
  28. Felix, J., et al. (2021). Structural and functional analysis of the Francisella lysine decarboxylase as a key actor in oxidative stress resistance. Scientific Reports. 11(1):19. doi: 10.1038/s41598-020-79611-5
  29. Flatt, J. W., et al. (2021). Identification of a conserved virion-stabilizing network inside the interprotomer pocket of enteroviruses. Communications Biology. 4(1):8. doi: 10.1038/s42003-021-01779-x
  30. 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
  31. 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". Biomolecular NMR Assignments.7. doi: 10.1007/s12104-020-10000-9
  32. Gauthier, L., et al. (2021). Lectin recognition and hepatocyte endocytosis of GalNAc-decorated nanostructured lipid carriers. Journal of Drug Targeting. 29(1):99-107. doi: 10.1080/1061186x.2020.1806286
  33. 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
  34. Ghashghaei, O., et al. (2021). Extended Multicomponent Reactions with Indole Aldehydes: Access to Unprecedented Polyheterocyclic Scaffolds, Ligands of the Aryl Hydrocarbon Receptor. Angewandte Chemie-International Edition. 60(5):2603-2608. doi: 10.1002/anie.202011253
  35. Giachin, G., et al. (2021). Assembly of the mitochondrial Complex I assembly complex suggests a regulatory role for deflavination. Angewandte Chemie. 60(9):4689-4697. doi: 10.1002/anie.202011548
  36. 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
  37. Gogl, G., et al. (2021). Hierarchized phosphotarget binding by the seven human 14-3-3 isoforms. Nature Communications. 12(1):12. doi: 10.1038/s41467-021-21908-8
  38. 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. Biomolecular NMR Assignments.6. doi: 10.1007/s12104-021-10014-x
  39. 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. Journal of Biomolecular NMR.12. doi: 10.1007/s10858-021-00370-0
  40. Houser, J., et al. (2021). Development of 48-condition buffer screen for protein stability assessment. European Biophysics Journal with Biophysics Letters.11. doi: 10.1007/s00249-021-01497-6
  41. 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
  42. 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
  43. Jessop, M., et al. (2021). Supramolecular assembly of the Escherichia coli LdcI upon acid stress. Proceedings of the National Academy of Sciences of the United States of America. 118(2):11. doi: 10.1073/pnas.2014383118
  44. 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
  45. Jurasek, M., et al. (2021). Phosphorylation-induced changes in the PDZ domain of Dishevelled 3. Scientific Reports. 11(1):14. doi: 10.1038/s41598-020-79398-5
  46. 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 Journal.18. doi: 10.1111/tpj.15145
  47. Leonardo, D. A., et al. (2021). Orientational Ambiguity in Septin Coiled Coils and its Structural Basis. Journal of Molecular Biology. 433(9):19. doi: 10.1016/j.jmb.2021.166889
  48. Liu, S. S., et al. (2021). Evaluation of dsRNA delivery methods for targeting macrophage migration inhibitory factor MIF in RNAi-based aphid control. Journal of Plant Diseases and Protection.12. doi: 10.1007/s41348-021-00464-9
  49. Lopez-Mendez, B., et al. (2021). Reproducibility and accuracy of microscale thermophoresis in the NanoTemper Monolith: a multi laboratory benchmark study. European Biophysics Journal with Biophysics Letters.17. doi: 10.1007/s00249-021-01532-6
  50. 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 of Conferences. 236:03002. doi: 10.1051/epjconf/202023603002
  51. 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. Angewandte Chemie-International Edition.6. doi: 10.1002/anie.202102910
  52. 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
  53. Miele, A. E., et al. (2021). Biophysical characterization of the complex between the iron-responsive transcription factor Fep1 and DNA. European Biophysics Journal with Biophysics Letters.12. doi: 10.1007/s00249-020-01489-y
  54. Mikulasek, K., et al. (2021). SP3 Protocol for Proteomic Plant Sample Preparation Prior LC-MS/MS. Frontiers in Plant Science. 12:12. doi: 10.3389/fpls.2021.635550
  55. Mustonen, V., et al. (2021). Crystal and solution structure of NDRG1, a membrane-binding protein linked to myelination and tumour suppression. FEBS Journal.23. doi: 10.1111/febs.15660
  56. 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. Journal of the American Chemical Society. 143(9):3330-3339. doi: 10.1021/jacs.0c10053
  57. Pastucha, M., et al. (2021). Upconversion-Linked Immunoassay for the Diagnosis of Honeybee Disease American Foulbrood. Ieee Journal of Selected Topics in Quantum Electronics. 27(5):11. doi: 10.1109/jstqe.2021.3049689
  58. Perestrelo, A. R., et al. (2021). Multiscale Analysis of Extracellular Matrix Remodeling in the Failing Heart. Circulation Research. 128(1):24-38. doi: 10.1161/circresaha.120.317685
  59. Porizka, P., et al. (2021). Laser-induced breakdown spectroscopy as a readout method for immunocytochemistry with upconversion nanoparticles. Microchimica Acta. 188(5):10. doi: 10.1007/s00604-021-04816-y
  60. Pounot, K., et al. (2021). Zinc determines dynamical properties and aggregation kinetics of human insulin. Biophysical Journal. 120(5):886-898. doi: 10.1016/j.bpj.2020.11.2280
  61. Pradhan, S., et al. (2021). Stable lead-halide perovskite quantum dots as efficient visible light photocatalysts for organic transformations. Nanoscale Advances. 3(5):1464-1472. doi: 10.1039/d0na00992j
  62. Prasanna, M., et al. (2021). On the use of adenovirus dodecahedron as a carrier for glycoconjugate vaccines. Glycoconjugate Journal.10. doi: 10.1007/s10719-021-09999-3
  63. Prochazkova, M., et al. (2021). Capsid Structure of Leishmania RNA Virus 1. Journal of Virology. 95(3):12. doi: 10.1128/jvi.01957-20
  64. 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. Inorganic Chemistry. 60(3):2068-2075. doi: 10.1021/acs.inorgchem.0c03635
  65. Ravera, E., et al. (2021). A High-Resolution View of the Coordination Environment in a Paramagnetic Metalloprotein from its Magnetic Properties. Angewandte Chemie-International Edition.8. doi: 10.1002/anie.202101149
  66. Rizzo, D., et al. (2021). Origin of the MRI Contrast in Natural and Hydrogel Formulation of Pineapple Juice. Bioinorganic Chemistry and Applications. 2021:12. doi: 10.1155/2021/6666018
  67. Rizzuto, C. (2021). The ERIC Consortium a new type of EU research institution. Europhysics News. 51(3):25-27. doi: 10.1051/epn/2020305
  68. 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 Letters.9. doi: 10.1002/1873-3468.14012
  69. Rodrigues, J., et al. (2021). High Throughput Expression Screening of Arabinofuranosyltransferases from Mycobacteria. Processes. 9(4):18. doi: 10.3390/pr9040629
  70. 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
  71. Rovito, D., et al. (2021). Myod1 and GR coordinate myofiber-specific transcriptional enhancers. Nucleic Acids Research. 49(8):4472-4492. doi: 10.1093/nar/gkab226
  72. Salinas, N., et al. (2021). The amphibian antimicrobial peptide uperin 3.5 is a cross-alpha/cross-beta chameleon functional amyloid. Proceedings of the National Academy of Sciences of the United States of America. 118(3):8. doi: 10.1073/pnas.2014442118
  73. Salvi, N., et al. (2021). H-1, C-13 and N-15 backbone chemical shift assignments of SARS-CoV-2 nsp3a. Biomolecular NMR Assignments.4. doi: 10.1007/s12104-020-10001-8
  74. Schep, R., et al. (2021). Impact of chromatin context on Cas9-induced DNA double-strand break repair pathway balance. Molecular Cell. 81(10):2216-+. doi: 10.1016/j.molcel.2021.03.032
  75. Schiro, G., et al. (2021). Diffusivelike Motions in a Solvent-Free Protein-Polymer Hybrid. Physical Review Letters. 126(8):7. doi: 10.1103/PhysRevLett.126.088102
  76. Schwarzer, S., et al. (2021). Growth Phase Dependent Cell Shape of Haloarcula. Microorganisms. 9(2):14. doi: 10.3390/microorganisms9020231
  77. Signor, L., et al. (2021). Divalent cations influence the dimerization mode of murine S100A9 protein by modulating its disulfide bond pattern. Journal of Structural Biology. 213(1):16. doi: 10.1016/j.jsb.2020.107689
  78. Sopousek, J., et al. (2021). Thick nanoporous matrices of polystyrene nanoparticles and their potential for electrochemical biosensing. Electrochimica Acta. 368:9. doi: 10.1016/j.electacta.2020.137607
  79. Sorzano, C. O. S., et al. (2021). Algorithmic robustness to preferred orientations in single particle analysis by CryoEM. Journal of Structural Biology. 213(1):5. doi: 10.1016/j.jsb.2020.107695
  80. 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. Journal of Molecular Biology. 433(5):15. doi: 10.1016/j.jmb.2021.166826
  81. 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
  82. Suraci, D., et al. (2021). ISCA1 Orchestrates ISCA2 and NFU1 in the Maturation of Human Mitochondrial 4Fe-4S Proteins. Journal of Molecular Biology. 433(10):17. doi: 10.1016/j.jmb.2021.166924
  83. Tittes, C., et al. (2021). Cellular and Genomic Properties of Haloferax gibbonsii LR2-5, the Host of Euryarchaeal Virus HFTV1. Frontiers in Microbiology. 12:14. doi: 10.3389/fmicb.2021.625599
  84. Tomecek, J., et al. (2021). Modes of Micromolar Host-Guest Binding of beta-Cyclodextrin Complexes Revealed by NMR Spectroscopy in Salt Water. Journal of Organic Chemistry. 86(6):4483-4496. doi: 10.1021/acs.joc.0c02917
  85. Torner, R., et al. (2021). Backbone and methyl resonances assignment of the 87 kDa prefoldin from Pyrococcus horikoshii. Biomolecular NMR Assignments.10. doi: 10.1007/s12104-021-10029-4
  86. Torricella, F., et al. (2021). Nitroxide spin labels and EPR spectroscopy: A powerful association for protein dynamics studies. Biochimica Et Biophysica Acta-Proteins and Proteomics. 1869(7):14. doi: 10.1016/j.bbapap.2021.140653
  87. Trindade, I. B., et al. (2021). Sequence-specific assignments in NMR spectra of paramagnetic systems: A non-systematic approach. Inorganica Chimica Acta. 514:8. doi: 10.1016/j.ica.2020.119984
  88. Tully, M. D., et al. (2021). Analysis of SEC-SAXS data via EFA deconvolution and Scatter. Jove-Journal of Visualized Experiments. (167):16. doi: 10.3791/61578
  89. Uchanski, T., et al. (2021). Megabodies expand the nanobody toolkit for protein structure determination by single-particle cryo-EM. Nature Methods. 18(1):60-+. doi: 10.1038/s41592-020-01001-6
  90. Urso, M., et al. (2021). Breaking Polymer Chains with Self-Propelled Light-Controlled Navigable Hematite Microrobots. Advanced Functional Materials.10. doi: 10.1002/adfm.202101510
  91. Uwizeye, C., et al. (2021). Morphological bases of phytoplankton energy management and physiological responses unveiled by 3D subcellular imaging. Nature Communications. 12(1):12. doi: 10.1038/s41467-021-21314-0
  92. Vignoli, A., et al. (2021). Differential Network Analysis Reveals Molecular Determinants Associated with Blood Pressure and Heart Rate in Healthy Subjects. Journal of Proteome Research. 20(1):1040-1051. doi: 10.1021/acs.jproteome.0c00882
  93. Walsh, M. A., et al. (2021). Diamond Light Source: contributions to SARS-CoV-2 biology and therapeutics. Biochemical and Biophysical Research Communications. 538:40-46. doi: 10.1016/j.bbrc.2020.11.041
  94. Wang, J. M., et al. (2021). Identification of Mg2+ ions next to nucleotides in cryo-EM maps using electrostatic potential maps. Acta Crystallographica Section D-Structural Biology. 77:534-539. doi: 10.1107/s2059798321001893
  95. Wang, J. M., et al. (2021). Identification of Mg2+ ions next to nucleotides in cryo-EM maps using electrostatic potential maps. Acta Crystallographica Section D-Structural Biology. 77:534-539. doi: 10.1107/s2059798321001893
  96. 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
  97. 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. International Journal of Molecular Sciences. 22(2):24. doi: 10.3390/ijms22020530
  98. 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


  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



  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



  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



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


 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


 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


 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


 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

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

 93. 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

 94. 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.


 95. 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

 96. 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

 97. 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

 98. 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

 99. 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

 100. 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

 101. 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


 102. 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

 103. 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

 104. Luchinat, E., et al. (2017). Identification of a novel nucleophosmin-interaction motif in the tumor suppressor p14arf. Febs j. doi:10.1111/febs.14373

 105. 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

 106. 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

 107. 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

 108. 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

 109. 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

 110. 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

 111. 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

 112. 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

 113. 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

 114. Mietton, F., et al. (2017). Selective BET bromodomain inhibition as an antifungal therapeutic strategy. Nat Commun, 8, 15482. doi:10.1038/ncomms15482

 115. 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


 116. 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

 117. 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

 118. 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

 119. 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

 120. 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

 121. 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

 122. 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

 123. 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

 124. 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

 125. Natchiar, S. K., et al. (2017). Atomic model building and refinement into high-resolution cryo-EM maps.

 126. Natchiar, S. K., et al. (2017). Visualization of chemical modifications in the human 80S ribosome structure. Nature, 551(7681), 472-+. doi:10.1038/nature24482

 127. 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

 128. 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

 129. Oksanen, H. M., et al. (2017). ICTV Virus Taxonomy Profile: Corticoviridae. J Gen Virol, 98(5), 888-889. doi:10.1099/jgv.0.000795

 130. 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

 131. 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

 132. 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


 133. 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

 134. 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

 135. 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

 136. 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

 137. 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

 138. 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

 139. 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

 140. 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

 141. 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

 142. 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

 143. 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

 144. 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

 145. 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

 146. 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

 147. 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

 148. 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

 149. 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

 150. 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

151. 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

 152. 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

 153. 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

 154. 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

 155. 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

 156. 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

 157. 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

 158. 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

 159. 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

 160. 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

 161. 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

 162. 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

 163. 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

 164. 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

 165. 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

 166. 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

 167. Schubert, A. F., et al. (2017). Structure of PINK1 in complex with its substrate ubiquitin. Nature, 552(7683), 51-+. doi:10.1038/nature24645

 168. 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

 169. 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

 170. 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

 171. 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.

 172. Shevchenko, V., et al. (2017). Inward H(+) pump xenorhodopsin: Mechanism and alternative optogenetic approach. Science Advances, 3(9), e1603187. doi:10.1126/sciadv.1603187

 173. Sorrenti, A., et al. (2017). Non-equilibrium steady states in supramolecular polymerization. Nature Communications, 8, 15899. doi:10.1038/ncomms15899


 174. 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

 175. 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

 176. Steinbach, T., et al. (2017). Reversible Bioconjugation: Biodegradable Poly(phosphate)-Protein Conjugates. Macromol Biosci, 17(10). doi:10.1002/mabi.201600377

 177. 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

 178. 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

 179. 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

 180. 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

181. 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

 182. 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

 183. 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

 184. 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

 185. 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

 186. 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

 187. 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

 188. 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

189. Volkov, O., et al. (2017). Structural insights into ion conduction by channelrhodopsin 2. Science, 358(6366). doi:10.1126/science.aan8862 

190. 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

191. 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

192. 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 

193. 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


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

A with Amyloid Fibers of a Conserved 11 Residue Peptide from Androgen Receptor. Plos One, 11(9). doi:10.1371/journal.pone.0161948

 10. 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

 11. Baldoneschi, V., et al. (2016). Active-Site Targeting Paramagnetic Probe for Matrix Metalloproteinases. Chempluschem, 81(12), 1333-1338. doi:10.1002/cplu.201600375

 12. 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

 13. 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

 14. 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

 15. 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

 16. 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

nuclear RNA. Rna, 22(12), 1844-1858. doi:10.1261/rna.056523.116

 23. 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

 24. Burhan, I., et al. (2016). Interplay between transglutaminases and heparan sulphate in progressive renal scarring. Scientific Reports, 6, 31343. doi:10.1038/srep31343


 25. 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

 26. 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

 27. 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

 28. 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

 29. 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

 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

 31. 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

 32. 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

 33. 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.


 34. 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

 35. 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


 36. 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

 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. 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

 39. 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

 40. 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

 41. 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

 42. 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.

 43. 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

 44. 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


 45. 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

 46. 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

 47. 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

 48. 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

 49. 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

 50. 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

 51. 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

 52. 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

 53. 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

 54. 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

 55. 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

 56. 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

 57. 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

 58. 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

 59. 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

 60. 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

 61. 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

 62. 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

 63. Khoshouei, M., et al. (2016). Volta phase plate cryo-EM of the small protein complex Prx3. Nature Communications, 7. doi:10.1038/ncomms10534

 64. 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

 65. 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

 66. 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

 67. 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

 68. 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

 69. 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

70. Labaronne, A., et al. (2016). Binding ofRNA by the Nucleoproteins of Influenza Viruses A and B. Viruses, 8(9).doi:10.3390/v8090247

 71. Lassalle, L., et al. (2016). Newinsights into the mechanism of substrates trafficking in

Glyoxylate/Hydroxypyruvate reductases. SciRep, 6, 20629. doi:10.1038/srep20629

 72. 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

 73. 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

 74. Levy, N., et al. (2016). Production ofunstable proteins through the formation of stable core complexes. NatureCommunications, 7. doi:10.1038/ncomms10932

 75. 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

 76. 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

 77. 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


 78. 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

 79. 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

 80. 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

 81. 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

 82. Martin, F., et al. (2016). Ribosomal 18SrRNA base pairs with mRNA during eukaryotic translation initiation. NatureCommunications, 7. doi:10.1038/ncomms12622

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

 83. 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

 84. 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

 85. 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

 86. 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

 87. 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

 88. 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

 89. 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

 90. 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

91. 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

 92. 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.


 93. 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

 94. 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

 95. Ohayon, D., et al. (2016). Cytoplasmicproliferating cell nuclear antigen connects glycolysis and cell survival inacute myeloid leukemia. Scientific Reports, 6, 35561.



 96. 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

 97. Ordanini, S., et al. (2016). SolutionBehavior of Amphiphilic Glycodendrimers with a Rod-Like Core. MacromolBiosci, 16(6), 896-905. doi:10.1002/mabi.201500452

 98. Otero, R., et al. (2016).Carborane-based design of a potent vitamin D receptor agonist. ChemicalScience, 7(2), 1033-1037. doi:10.1039/c5sc03084f

 99. 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

 100. 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.

101. 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

 102. 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

 103. 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

 104. Pilsl, M., et al. (2016). Structure ofthe initiation-competent RNA polymerase I and its implication fortranscription. Nature Communications, 7. doi:10.1038/ncomms12126

 105. Podobnik, M., et al. (2016). Crystalstructure of an invertebrate cytolysin pore reveals unique properties andmechanism of assembly. Nature Communications, 7. doi:10.1038/ncomms11598

 106. Polidori, A., et al. (2016). Sparinglyfluorinated maltoside-based surfactants for membrane-protein stabilization. NewJournal of Chemistry, 40(6), 5364-5378. doi:10.1039/C5NJ03502C

 107. 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

 108.  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

 109. 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


 110. 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

 111. Ravera, E., et al. (2016). Solid-State NMRof PEGylated Proteins. Angewandte Chemie-International Edition, 55(7),2446-2449. doi:10.1002/anie.201510148

 112. 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

 113. 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

 114. 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

 115. Renner, M., et al. (2016). Nucleocapsidassembly in pneumoviruses is regulated by conformational switching of the Nprotein. Elife, 5, e12627. doi:10.7554/eLife.1262

 116. 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

 117. 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

 118. 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

 119. 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

120. 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

 121. 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

 122. 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

 123. Schrader, J., et al. (2016). The inhibition mechanism of human 20S proteasomes enables next-generation inhibitor design. Science, 353(6299), 594-598. doi:10.1126/science.aaf8993

 124. 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


 125. 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

 126. 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

 127. 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

 128. 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

 129. 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

 130. 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

 131. 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

 132. 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

 133. 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

 134. Sonawane, P. D., et al. (2016). Plant cholesterol biosynthetic pathway overlaps with phytosterol metabolism. Nat Plants, 3, 16205. doi:10.1038/nplants.2016.205

 135. 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

 136. 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

 137. 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

 138. 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

 139. 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

 140. 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

 141. 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

 142. 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

 143. 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

 144. 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

 145. 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.


 146. 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

 147. 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

 148. 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

 149. 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

 150. 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

 151. Zhao, Y., et al. (2016). Toremifene interacts with and destabilizes the Ebola virus glycoprotein. Nature, 535(7610), 169-172. doi:10.1038/nature18615

 152. 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



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


 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.


 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.


 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


 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


 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

 95. 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

 96. 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

 97. 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

 98. 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

 99. 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.


 100. 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

 101. 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

 102. 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

 103. 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

 104. 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

 105. 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

 106. 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

 107. 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

 108. 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

 109. 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

 110. 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

 111. 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

 112. 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

 113. 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

 114. 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

 115. 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

 116. 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

 117. 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

 118. van Zundert, G. C., et al. (2015). DisVis: quantifying and visualizing accessible interaction space of distance-restrained biomolecular complexes. Bioinformatics, 31(19), 3222-3224.


 119. 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

 120. Vangone, A., et al. (2015). Contacts-based prediction of binding affinity in protein-protein complexes. Elife, 4, e07454. doi:10.7554/eLife.07454

 121. 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

 122. 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

 123. 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


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, 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.


 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


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.


 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


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 


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


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


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