2020
- Aarestrup, F. M., et al. (2020). Towards a European health research and innovation cloud (HRIC). Genome Medicine. 12(1):14. doi: 10.1186/s13073-020-0713-z
- Abelein, A., et al. (2020). High-yield Production of Amyloid-beta Peptide Enabled by a Customized Spider Silk Domain. Scientific Reports. 10(1):10. doi: 10.1038/s41598-019-57143-x
- 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
- 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. 1627:11. doi: 10.1016/j.chroma.2020.461378
- 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):14. doi: 10.1038/s41467-020-15184-1
- 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
- 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
- Antonaros, F., et al. (2020). Plasma metabolome and cognitive skills in Down syndrome. Scientific Reports. 10(1):12. doi: 10.1038/s41598-020-67195-z
- 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):14. doi: 10.1038/s41467-020-17360-9
- 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):13. doi: 10.1038/s41467-020-17349-4
- Aumonier, S., et al. (2020). Millisecond time-resolved serial oscillation crystallography of a blue-light photoreceptor at a synchrotron. IUCrJ. 7:728-736. doi: 10.1107/s2052252520007411
- 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
- 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
- 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
- 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
- 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
- Belorusova, A. Y., et al. (2020). Molecular determinants of MED1 interaction with the DNA bound VDR-RXR heterodimer. Nucleic Acids Research. 48(19). doi: 10.1093/nar/gkaa775
- 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
- Bertin, A., et al. (2020). Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation. Nature Communications. 11(1):13. doi: 10.1038/s41467-020-16368-5
- 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
- Bhaskar, V., et al. (2020). Dynamics of uS19 C-Terminal Tail during the Translation Elongation Cycle in Human Ribosomes. Cell Reports. 31(1):12. doi: 10.1016/j.celrep.2020.03.037
- Bhattarai, M., et al. (2020). Colloidal features of softwood galactoglucomannans-rich extract. Carbohydrate Polymers. 241:10. doi: 10.1016/j.carbpol.2020.116368
- 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
- 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
- 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
- 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). doi: 10.1038/s41598-020-77899-x
- Bouillot, S., et al. (2020). Inflammasome activation byPseudomonas aeruginosa's ExlA pore-forming toxin is detrimental for the host. Cellular Microbiology. 22(11). doi: 10.1111/cmi.13251
- 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
- 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
- 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
- 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). doi: 10.1016/j.bpj.2020.10.028
- Burt, A., et al. (2020). Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain. Nature Communications. 11(1):9. doi: 10.1038/s41467-020-14350-9
- 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):12. doi: 10.1038/s41467-020-17407-x
- 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
- 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):8. doi: 10.1007/s12104-020-09973-4
- Carrique, L., et al. (2020). Structure and catalytic regulation of Plasmodium falciparum IMP specific nucleotidase. Nature Communications. 11(1):11. doi: 10.1038/s41467-020-17013-x
- Carter, S. D., et al. (2020). Ribosome-associated vesicles: A dynamic subcompartment of the endoplasmic reticulum in secretory cells. Science Advances. 6(14):17. doi: 10.1126/sciadv.aay9572
- Caveney, N. A., et al. (2020). Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa. Structure. 28(6):643-+. doi: 10.1016/j.str.2020.03.012
- 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. 265:6. doi: 10.1016/j.bpc.2020.106441
- 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
- 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
- Che, T., et al. (2020). Nanobody-enabled monitoring of kappa opioid receptor states. Nature Communications. 11(1):12. doi: 10.1038/s41467-020-14889-7
- 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):12. doi: 10.1038/s42003-020-0757-z
- 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):29. doi: 10.1080/10409238.2020.1828259
- 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
- Cioce, A., et al. (2020). Rapid On-Chip Synthesis of Complex Glycomimetics from N-Glycan Scaffolds for Improved Lectin Targeting. Chemistry. 26(56):12809-12817. doi: 10.1002/chem.202000026
- Cussol, L., et al. (2020). Structural Basis for alpha-Helix Mimicry and Inhibition of Protein-Protein Interactions with Oligourea Foldamers. Angewandte Chemie-International Edition.9. doi: 10.1002/anie.202008992
- Cuveillier, C., et al. (2020). MAP6 is an intraluminal protein that induces neuronal microtubules to coil. Science Advances. 6(14):11. doi: 10.1126/sciadv.aaz4344
- 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):8. doi: 10.1016/j.bbapap.2020.140437
- 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
- 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
- de Muizon, C. J., et al. (2020). Self-organization Properties of a GPCR-Binding Peptide with a Fluorinated Tail Studied by Fluorine NMR Spectroscopy. ChemBioChem.6. doi: 10.1002/cbic.202000601
- 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
- 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
- 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
- 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
- Dekoninck, K., et al. (2020). Defining the function of OmpA in the Rcs stress response. eLife. 9. doi: 10.7554/eLife.60861
- 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
- Demina, T. A., et al. (2020). Pleomorphic archaeal viruses: the familyPleolipoviridaeis expanding by seven new species. Archives of Virology.9. doi: 10.1007/s00705-020-04689-1
- 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
- Di Mattia, T., et al. (2020). FFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts. Embo Journal. 39(23):29. doi: 10.15252/embj.2019104369
- Di Mattia, T., et al. (2020). FFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts. EMBO Journal. 39(23):29. doi: 10.15252/embj.2019104369
- 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
- Donchet, A., et al. (2020). Differential Behaviours and Preferential Bindings of Influenza Nucleoproteins on Importins-alpha. Viruses. 12(8):16. doi: 10.3390/v12080834
- El Masri, R., et al. (2020). HS and Inflammation: A Potential Playground for the Sulfs? Frontiers in Immunology. 11:8. doi: 10.3389/fimmu.2020.00570
- Engelberg, Y., et al. (2020). The Human LL-37(17-29) antimicrobial peptide reveals a functional supramolecular structure. Nature Communications. 11(1):10. doi: 10.1038/s41467-020-17736-x
- Erba, E. B., et al. (2020). Exploring the structure and dynamics of macromolecular complexes by native mass spectrometry. Journal of Proteomics. 222:17. doi: 10.1016/j.jprot.2020.103799
- 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
- Fouet, G., et al. (2020). Headless C1q: a new molecular tool to decipher its collagen-like functions. FEBS J.12. doi: 10.1111/febs.15543
- Fouet, G., et al. (2020). Headless C1q: a new molecular tool to decipher its collagen-like functions. FEBS Journal. doi: 10.1111/febs.15543
- 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. 11:17. doi: 10.3389/fimmu.2020.583754
- 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
- 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
- Ghashghaei, O., et al. (2020). Extended Multicomponent Reactions with Indole Aldehydes: Access to Unprecedented Polyheterocyclic Scaffolds, Ligands of the Aryl Hydrocarbon Receptor. Angewandte Chemie-International Edition.7. doi: 10.1002/anie.202011253
- 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
- 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). doi: 10.1038/s41467-020-18770-5
- Gogl, G., et al. (2020). Dual Specificity PDZ- and 14-3-3-Binding Motifs: A Structural and Interactomics Study. Structure. 28(7):747-+. doi: 10.1016/j.str.2020.03.010
- 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
- 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
- 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
- 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
- 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
- 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
- Hennicke, J., et al. (2020). Transient pentameric IgM fulfill biological function-Effect of expression host and transfection on IgM properties. Plos One. 15(3):12. doi: 10.1371/journal.pone.0229992
- 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
- 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
- Hosek, T., et al. (2020). Structural features of the interaction of MapZ with FtsZ and membranes in Streptococcus pneumoniae. Scientific Reports. 10(1):13. doi: 10.1038/s41598-020-61036-9
- 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):13. doi: 10.1038/s41467-020-19013-3
- 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
- Huo, J., et al. (2020). Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2. Nature Struct Mol Biol. 27(9):846-854. doi: 10.1038/s41594-020-0469-6
- Huo, J. D., et al. (2020). Neutralization of SARS-CoV-2 by Destruction of the Prefusion Spike. Cell Host & Microbe. 28(3):445-+. doi: 10.1016/j.chom.2020.06.010
- Invernici, M., et al. (2020). Measuring transverse relaxation in highly paramagnetic systems. J Biomol NMR.12. doi: 10.1007/s10858-020-00334-w
- 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
- 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):14. doi: 10.1038/s42003-020-0772-0
- Jones, R., et al. (2020). Capping pores of alphavirus nsP1 gate membranous viral replication factories. Nature.28. doi: 10.1038/s41586-020-3036-8
- 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
- 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
- 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
- Karki, S., et al. (2020). Structural basis of SALM3 dimerization and synaptic adhesion complex formation with PTP sigma. Scientific Reports. 10(1):13. doi: 10.1038/s41598-020-68502-4
- 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
- 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):15. doi: 10.1038/s41598-020-62069-w
- Kovalev, K., et al. (2020). Molecular mechanism of light-driven sodium pumping. Nature Communications. 11(1):11. doi: 10.1038/s41467-020-16032-y
- 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
- Kumar, H., et al. (2020). Diversity in kinetics correlated with structure in nano body-stabilized LacY. Plos One. 15(5):14. doi: 10.1371/journal.pone.0232846
- 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
- 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
- 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):11. doi: 10.1038/s41598-020-76613-1
- 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
- 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
- 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. 182:8. doi: 10.1016/j.antiviral.2020.104916
- 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. 8:8. doi: 10.3389/fcell.2020.00556
- Liebers, M., et al. (2020). Nucleo-plastidic PAP8/pTAC6 couples chloroplast formation with photomorphogenesis. EMBO Journal.17. doi: 10.15252/embj.2020104941
- Liebers, M., et al. (2020). Nucleo-plastidic PAP8/pTAC6 couples chloroplast formation with photomorphogenesis. EMBO Journal. 39(22):17. doi:
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Manigrasso, J., et al. (2020). Visualizing group II intron dynamics between the first and second steps of splicing. Nature Communications. 11(1):15. doi: 10.1038/s41467-020-16741-4
- Mantynen, S., et al. (2020). ICTV Virus Taxonomy Profile: Finnlakeviridae. Journal of General Virology. 101(9):894-895. doi: 10.1099/jgv.0.001488
- 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
- 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
- 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
- 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
- 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
- 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):10. doi: 10.1038/s41467-020-14943-4
- 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
- Melero, R., et al. (2020). Continuous flexibility analysis of SARS-CoV-2 spike prefusion structures. Iucrj. 7:1059-1069. doi: 10.1107/s2052252520012725
- 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
- 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
- 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. 11:15. doi: 10.3389/fmicb.2020.00909
- Murrali, M. G., et al. (2020). Adenoviral E1A Exploits Flexibility and Disorder to Target Cellular Proteins. Biomolecules. 10(11). doi: 10.3390/biom10111541
- 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
- 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
- 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
- Ouaguia, L., et al. (2020). Hepatitis B virus exploits C-type lectin receptors to hijack cDC1s, cDC2s and pDCs. Clinical & Translational Immunology. 9(12). doi: 10.1002/cti2.1208
- Papai, G., et al. (2020). Structure of SAGA and mechanism of TBP deposition on gene promoters. Nature. 577(7792):711-+. doi: 10.1038/s41586-020-1944-2
- 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.10. doi: 10.1002/cssc.202001951
- 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
- Peissert, S., et al. (2020). In TFIIH the Arch domain of XPD is mechanistically essential for transcription and DNA repair. Nature Communications. 11(1):13. doi: 10.1038/s41467-020-15241-9
- 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
- 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):16. doi: 10.1038/s41467-020-16872-8
- 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):46. doi: 10.3390/magnetochemistry6040046
- Polykretis, P., et al. (2020). Methylglyoxal interaction with superoxide dismutase 1. Redox Biology. 30:10. doi: 10.1016/j.redox.2019.101421
- 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.9. doi: 10.1002/anie.202008079
- 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
- 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
- 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
- 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
- Rampelt, H., et al. (2020). The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments. BMC Biol. 18(1):2. doi: 10.1186/s12915-019-0733-6
- 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
- Rathner, P., et al. (2020). Interhelical interactions within the STIM1 CC1 domain modulate CRAC channel activation. Nature Chemical Biology.19. doi: 10.1038/s41589-020-00672-8
- 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
- Salomon, E., et al. (2020). Aminobenzosuberone derivatives as PfA-M1 inhibitors: Molecular recognition and antiplasmodial evaluation. Bioorganic Chemistry. 98:11. doi: 10.1016/j.bioorg.2020.103750
- Sanchez-Garcia, R., et al. (2020). MicrographCleaner: A python package for cryo-EM micrograph cleaning using deep learning. Journal of Structural Biology. 210(3):7. doi: 10.1016/j.jsb.2020.107498
- 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):13. doi: 10.1038/s41598-020-76522-3
- 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
- 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
- Selegato, D. M., et al. (2020). Comparison of Different Reweighting Approaches for the Calculation of Conformational Variability of Macromolecules from Molecular Simulations. ChemPhysChem.13. doi: 10.1002/cphc.202000714
- 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
- Setyawati, I., et al. (2020). In vitro reconstitution of dynamically interacting integral membrane subunits of energy-coupling factor transporters. eLife. doi: 10.7554/eLife.64389
- 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
- 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
- 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
- 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
- Silva, Y. R. O., et al. (2020). Bacterial secretins: Mechanisms of assembly and membrane targeting. Protein Sci. 29(4):893-904. doi: 10.1002/pro.3835
- 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
- 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
- Skorepa, O., et al. (2020). Natural Killer Cell Activation Receptor NKp30 Oligomerization Depends on ItsN-Glycosylation. Cancers. 12(7):24. doi: 10.3390/cancers12071998
- Sorzano, C. O. S., et al. (2020). Improvements on marker-free images alignment for electron tomography,. Journal of Structural Biology: X. 4. doi: 10.1016/j.yjsbx.2020.100037
- 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):12. doi: 10.1038/s41598-020-69229-y
- 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
- Spehner, D., et al. (2020). Cryo-FIB-SEM as a promising tool for localizing proteins in 3D. Journal of Structural Biology. 211(1):10. doi: 10.1016/j.jsb.2020.107528
- 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. 76:1256-1269. doi: 10.1107/s2059798320013819
- 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
- 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
- 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
- Sutton, G., et al. (2020). Assembly intermediates of orthoreovirus captured in the cell. Nature Communications. 11(1):7. doi: 10.1038/s41467-020-18243-9
- 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
- Talsma, D. T., et al. (2020). MASP-2 Is a Heparin-Binding Protease, Identification of Blocking Oligosaccharides. Frontiers in Immunology. 11:17. doi: 10.3389/fimmu.2020.00732
- Tetreau, G., et al. (2020). Serial femtosecond crystallography on in vivo-grown crystals drives elucidation of mosquitocidal Cyt1Aa bioactivation cascade. Nature Communications. 11(1):16. doi: 10.1038/s41467-020-14894-w
- 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
- 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
- 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. Biomol NMR Assign. 14(2):211-215. doi: 10.1007/s12104-020-09947-6
- 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
- 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
- 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-+. doi: 10.1016/j.str.2020.04.008
- 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
- 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):7. doi: 10.1016/j.jsb.2019.107408
- 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
- Vauclare, P., et al. (2020). Surviving salt fluctuations: stress and recovery in Halobacterium salinarum, an extreme halophilic Archaeon. Scientific Reports. 10(1):10. doi: 10.1038/s41598-020-59681-1
- 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
- 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
- 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
- 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
- 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
- Vilas, J. L., et al. (2020). Measuring local-directional resolution and local anisotropy in cryo-EM maps. Nature Communications. 11(1):7. doi: 10.1038/s41467-019-13742-w
- 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):11. doi: 10.1016/j.jsb.2020.107447
- Vrettos, E. I., et al. (2020). Single Peptide Backbone Surrogate Mutations to Regulate Angiotensin GPCR Subtype Selectivity. Chemistry.7. doi: 10.1002/chem.202000924
- Wagemans, J., et al. (2020). Structural Analysis of Jumbo Coliphage phAPEC6. International Journal of Molecular Sciences. 21(9):13. doi: 10.3390/ijms21093119
- 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):8. doi: 10.1016/j.bbalip.2020.158769
- 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
- Wandzik, J. M., et al. (2020). A Structure-Based Model for the Complete Transcription Cycle of Influenza Polymerase. Cell. 181(4):877-+. doi: 10.1016/j.cell.2020.03.061
- Wazir, S., et al. (2020). Multiple crystal forms of human MacroD2. Acta Crystallographica Section F-Structural Biology Communications. 76:477-482. doi: 10.1107/s2053230x20011309
- Webster, M. W., et al. (2020). Structural basis of transcription-translation coupling and collision in bacteria. Science. 369(6509):1355-+. doi: 10.1126/science.abb5036
- 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. 11:15. doi: 10.3389/fimmu.2020.00544
- Woodhouse, J., et al. (2020). Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy. Nature Communications. 11(1):11. doi: 10.1038/s41467-020-14537-0
- Zabelskii, D., et al. (2020). Viral rhodopsins 1 are an unique family of light-gated cation channels. Nature Communications. 11(1):16. doi: 10.1038/s41467-020-19457-7
- Zarate-Potes, A., et al. (2020). TheC.elegansGATA transcription factorelt-2mediates distinct transcriptional responses and opposite infection outcomes towards differentBacillus thuringiensisstrains. Plos Pathogens. 16(9):32. doi: 10.1371/journal.ppat.1008826
- Zarkadas, E., et al. (2020). The Binding of Palonosetron and Other Antiemetic Drugs to the Serotonin 5-HT3 Receptor. Structure. 28(10):1131-+. doi: 10.1016/j.str.2020.07.004
- Zarzecka, U., et al. (2020). Functional analysis and cryo-electron microscopy of Campylobacter jejuni serine protease HtrA. Gut Microbes. 12(1). doi: 10.1080/19490976.2020.1810532
- Zhao, Y. G., et al. (2020). Caffeine inhibits Notum activity by binding at the catalytic pocket. Communications Biology. 3(1):8. doi: 10.1038/s42003-020-01286-5
- 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):8. doi: 10.1038/s41467-019-13936-2
- 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
- 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-+. doi: 10.1038/s41594-020-0480-y
- Zinn, T., et al. (2020). Phoretic dynamics of colloids in a phase separating critical liquid mixture. Physical Review Research. 2. doi: 10.1103/PhysRevResearch.2.033177
2019
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Bratanov, D., et al. (2019). Unique structure and function of viral rhodopsins. Nature Communications. 10:13. doi: 10.1038/s41467-019-12718-0
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Cerofolini, L., et al. (2019). Mechanism and Inhibition of Matrix Metalloproteinases. Current Medicinal Chemistry. 26(15):2609-2633. doi: 10.2174/0929867325666180326163523
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Davey, N. E., et al. (2019). An intrinsically disordered proteins community for ELIXIR. F1000Research. 8. doi: 10.12688/f1000research.20136.1
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Garratt, R. C. (2019). A brief history of protein crystallography in Brazil. Biophysical Reviews.509-511. doi: 10.1007/s12551-019-00562-x
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Kovalev, K., et al. (2019). Structure and mechanisms of sodium-pumping KR2 rhodopsin. Science Advances. 5(4):10. doi: 10.1126/sciadv.aav2671
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Machon, C., et al. (2019). Atomic structure of the Epstein-Barr virus portal. Nature Communications. 10:7. doi: 10.1038/s41467-019-11706-8
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Maurice, F., et al. (2019). In vitro dimerization of human RIO2 kinase. RNA Biology. 16(11):1633-1642. doi: 10.1080/15476286.2019.1653679
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Teulon, J. M., et al. (2019). On the Operational Aspects of Measuring Nanoparticle Sizes. Nanomaterials. 9(1):29. doi: 10.3390/nano9010018
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Yee, A. W., et al. (2019). A molecular mechanism for transthyretin amyloidogenesis. Nature Communications. 10:10. doi: 10.1038/s41467-019-08609-z
- Zhou, D. M., et al. (2019). Unexpected mode of engagement between enterovirus 71 and its receptor SCARB2. Nature Microbiology. 4(3):414-419. doi: 10.1038/s41564-018-0319-z
2018
- 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
- 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
- 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
- Andronov, L., et al. (2018). 3DClusterViSu: 3D clustering analysis of super-resolution microscopy data by 3D Voronoi tessellations. Bioinformatics. doi: 10.1093/bioinformatics/bty200
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Cerofolini, L., et al. (2018). Mechanism and Inhibition of Matrix Metalloproteinases. Curr Med Chem. doi: 10.2174/0929867325666180326163523
- Cerofolini, L., et al. (2018). Characterization of PEGylated asparaginase: new opportunities from NMR analysis of large pegylated therapeutics. Chemistry. doi: 10.1002/chem.201804488
- 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
- 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
- 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
- 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
- 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
- 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
- Colin, P., et al. (2018). CCR5 structural plasticity shapes HIV-1 phenotypic properties. PLoS Pathog. 14(12):e1007432. doi: 10.1371/journal.ppat.1007432
- 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
- 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
- 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
- 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
- Duyvesteyn, H. M. E., et al. (2018). Towards in cellulo virus crystallography. Scientific Reports. 8(1):3771. doi: 10.1038/s41598-018-21693-3
- 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
- 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
- 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
- Faridounnia, M., et al. (2018). Function and Interactions of ERCC1-XPF in DNA Damage Response. Molecules. 23(12). doi: 10.3390/molecules23123205
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Grimes, J. M., et al. (2018). Where is crystallography going? Acta Crystallographica Section D. 74(2):152-166. doi: doi:10.1107/S2059798317016709
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Kolesnikova, O., et al. (2018). Molecular structure of promoter-bound yeast TFIID. Nature Communications. 9(1):4666. doi: 10.1038/s41467-018-07096-y
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Louka, A., et al. (2018). Engineering l-asparaginase for spontaneous formation of calcium phosphate bioinspired microreactors. Phys Chem Chem Phys. doi: 10.1039/c8cp00419f
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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:
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Monte, D., et al. (2018). Crystal structure of human Mediator subunit MED23. Nature Communications. 9:7. doi: 10.1038/s41467-018-05967-y
- Moroni, A., et al. (2018). Structure-guided design of a cell penetrating peptide preventing cAMP modulation of HCN channels. bioRxiv. doi: 10.1101/253096
- 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
- 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
- Murrali, M. G., et al. (2018). Proline Fingerprint in Intrinsically Disordered Proteins. Chembiochem. 19(15):1625-1629. doi: 10.1002/cbic.201800172
- 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
- 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
- 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
- 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
- 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
- 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:
- 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
- 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
- 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
- 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
- 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
- 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
- Ravera, E., et al. (2018). Paramagnetic NMR as a new tool in structural biology. Emerging Topics in Life Sciences. doi: 10.1042/etls20170084
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Suarez, I., et al. (2018). Structural Insights in Multifunctional Papillomavirus Oncoproteins. Viruses-Basel. 10(1):22. doi: 10.3390/v10010037
- 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
- Szekely, O., et al. (2018). High-Resolution 2D NMR of Disordered Proteins Enhanced by Hyperpolarized Water. Anal Chem. doi: 10.1021/acs.analchem.8b00585
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Wang, Y., et al. (2018). The cellular economy of the Saccharomyces cerevisiae zinc proteome. Metallomics. doi: 10.1039/C8MT00269J
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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