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2020

  1. 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
  2. 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
  3. Achilli, S., et al. (2020). TETRALEC, Artificial Tetrameric Lectins: A Tool to Screen Ligand and Pathogen Interactions. International Journal of Molecular Sciences. 21(15):19. doi: 10.3390/ijms21155290
  4. Aguilar, P. P., et al. (2020). Capture and purification of Human Immunodeficiency Virus-1 virus-like particles: Convective media vs porous beads. Journal of Chromatography A. 1627:11. doi: 10.1016/j.chroma.2020.461378
  5. Albanese, P., et al. (2020). How paired PSII-LHCII supercomplexes mediate the stacking of plant thylakoid membranes unveiled by structural mass-spectrometry. Nature Communications. 11(1):14. doi: 10.1038/s41467-020-15184-1
  6. Alleva, C., et al. (2020). Na+-dependent gate dynamics and electrostatic attraction ensure substrate coupling in glutamate transporters. Science Advances. 6(47):12. doi: 10.1126/sciadv.aba9854
  7. Andres, G., et al. (2020). The cryo-EM structure of African swine fever virus unravels a unique architecture comprising two icosahedral protein capsids and two lipoprotein membranes. Journal of Biological Chemistry. 295(1):1-12. doi: 10.1074/jbc.AC119.011196
  8. Antonaros, F., et al. (2020). Plasma metabolome and cognitive skills in Down syndrome. Scientific Reports. 10(1):12. doi: 10.1038/s41598-020-67195-z
  9. Arias-Alpizar, G., et al. (2020). Light-triggered switching of liposome surface charge directs delivery of membrane impermeable payloads in vivo. Nature Communications. 11(1):14. doi: 10.1038/s41467-020-17360-9
  10. Arragain, B., et al. (2020). Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes. Nature Communications. 11(1):13. doi: 10.1038/s41467-020-17349-4
  11. Aumonier, S., et al. (2020). Millisecond time-resolved serial oscillation crystallography of a blue-light photoreceptor at a synchrotron. IUCrJ. 7:728-736. doi: 10.1107/s2052252520007411
  12. Ayala, I., et al. (2020). Asymmetric Synthesis of Methyl Specifically Labelled L-Threonine and Application to the NMR Studies of High Molecular Weight Proteins. Chemistryselect. 5(17):5092-5098. doi: 10.1002/slct.202000827
  13. Barylski, J., et al. (2020). Analysis of Spounaviruses as a Case Study for the Overdue Reclassification of Tailed Phages. Systematic Biology. 69(1):110-123. doi: 10.1093/sysbio/syz036
  14. Basoglu, A., et al. (2020). NMR based serum metabolomics for monitoring newborn preterm calves' health. Japanese Journal of Veterinary Research. 68(2):105-115. doi: 10.14943/jjvr.68.2.105
  15. Basoglu, A., et al. (2020). Nuclear magnetic resonance (NMR)-based metabolome profile evaluation in dairy cows with and without displaced abomasum. Veterinary Quarterly. 40(1):1-15. doi: 10.1080/01652176.2019.1707907
  16. Basoglu, A., et al. (2020). NMR based serum extracts' metabolomics for evaluation of canine Ehrlichiosis. Japanese Journal of Veterinary Research. 68(4):227-236. doi: 10.14943/jjvr.68.4.227
  17. Belorusova, A. Y., et al. (2020). Molecular determinants of MED1 interaction with the DNA bound VDR-RXR heterodimer. Nucleic Acids Research. 48(19). doi: 10.1093/nar/gkaa775
  18. Belorusova, A. Y., et al. (2020). Structural Analysis of VDR Complex with ZK168281 Antagonist. Journal of Medicinal Chemistry. 63(17):9457-9463. doi: 10.1021/acs.jmedchem.0c00656
  19. Bertin, A., et al. (2020). Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation. Nature Communications. 11(1):13. doi: 10.1038/s41467-020-16368-5
  20. Bertrand, Q., et al. (2020). Exolysin (ExlA) from Pseudomonas aeruginosa Punctures Holes into Target Membranes Using a Molten Globule Domain. Journal of Molecular Biology. 432(16):4466-4480. doi: 10.1016/j.jmb.2020.05.025
  21. Bhaskar, V., et al. (2020). Dynamics of uS19 C-Terminal Tail during the Translation Elongation Cycle in Human Ribosomes. Cell Reports. 31(1):12. doi: 10.1016/j.celrep.2020.03.037
  22. Bhattarai, M., et al. (2020). Colloidal features of softwood galactoglucomannans-rich extract. Carbohydrate Polymers. 241:10. doi: 10.1016/j.carbpol.2020.116368
  23. Bhattarai, M., et al. (2020). Time-dependent self-association of spruce galactoglucomannans depends on pH and mechanical shearing. Food Hydrocolloids. 102:12. doi: 10.1016/j.foodhyd.2019.105607
  24. Bonhoure, A., et al. (2020). Benchtop holdup assay for quantitative affinity-based analysis of sequence determinants of protein-motif interactions. Analytical Biochemistry. 603:17. doi: 10.1016/j.ab.2020.113772
  25. Boni, F., et al. (2020). Modulation of Guanylate Cyclase Activating Protein 1 (GCAP1) Dimeric Assembly by Ca2+ or Mg2+: Hints to Understand Protein Activity. Biomolecules. 10(10):17. doi: 10.3390/biom10101408
  26. Bonucci, A., et al. (2020). A combined NMR and EPR investigation on the effect of the disordered RGG regions in the structure and the activity of the RRM domain of FUS. Scientific Reports. 10(1). doi: 10.1038/s41598-020-77899-x
  27. Bouillot, S., et al. (2020). Inflammasome activation byPseudomonas aeruginosa's ExlA pore-forming toxin is detrimental for the host. Cellular Microbiology. 22(11). doi: 10.1111/cmi.13251
  28. Brams, M., et al. (2020). Modulation of the Erwinia ligand-gated ion channel (ELIC) and the 5-HT3 receptor via a common vestibule site. eLife. 9:e51511. doi: 10.7554/eLife.51511
  29. Brillet, K., et al. (2020). Different views of the dynamic landscape covered by the 5 '-hairpin of the 7SK small nuclear RNA. RNA. 26(9):1184-1197. doi: 10.1261/rna.074955.120
  30. Bruno, F., et al. (2020). Multivariate Curve Resolution for 2D Solid-State NMR spectra. Analytical Chemistry. 92(6):4451-4458. doi: 10.1021/acs.analchem.9b05420
  31. Buckles, T. C., et al. (2020). The G-Protein Rab5A Activates VPS34 Complex II, a Class III PI3K, by a Dual Regulatory Mechanism. Biophysical Journal. 119(11). doi: 10.1016/j.bpj.2020.10.028
  32. Burt, A., et al. (2020). Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain. Nature Communications. 11(1):9. doi: 10.1038/s41467-020-14350-9
  33. Camacho-Zarco, A. R., et al. (2020). Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A. Nature Communications. 11(1):12. doi: 10.1038/s41467-020-17407-x
  34. Camponeschi, F., et al. (2020). GLRX3 Acts as a 2Fe-2S Cluster Chaperone in the Cytosolic Iron- Sulfur Assembly Machinery Transferring 2Fe-2S Clusters to NUBP1. Journal of the American Chemical Society. 142(24):10794-10805. doi: 10.1021/jacs.0c02266
  35. Cantini, F., et al. (2020). H-1,C-13, and(15)N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b. Biomolecular NMR Assignments. 14(2):8. doi: 10.1007/s12104-020-09973-4
  36. Carrique, L., et al. (2020). Structure and catalytic regulation of Plasmodium falciparum IMP specific nucleotidase. Nature Communications. 11(1):11. doi: 10.1038/s41467-020-17013-x
  37. Carter, S. D., et al. (2020). Ribosome-associated vesicles: A dynamic subcompartment of the endoplasmic reticulum in secretory cells. Science Advances. 6(14):17. doi: 10.1126/sciadv.aay9572
  38. Caveney, N. A., et al. (2020). Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa. Structure. 28(6):643-+. doi: 10.1016/j.str.2020.03.012
  39. Cerofolini, L., et al. (2020). Orientation of immobilized antigens on common surfaces by a simple computational model: Exposition of SARS-CoV-2 Spike protein RBD epitopes. Biophysical Chemistry. 265:6. doi: 10.1016/j.bpc.2020.106441
  40. Cerofolini, L., et al. (2020). Mixing A beta(1-40) and A beta(1-42) peptides generates unique amyloid fibrils. Chemical Communications. 56(62):8830-8833. doi: 10.1039/d0cc02463e
  41. Chatzikonstantinou, A. V., et al. (2020). The NMR tube bioreactor. In: Shukla, A. K., ed. Chemical and Synthetic Biology Approaches to Understand Cellular Functions - Pt C. London: Academic Press Ltd-Elsevier Science Ltd 2020:71-101. doi: 10.1016/bs.mie.2019.10.032
  42. Che, T., et al. (2020). Nanobody-enabled monitoring of kappa opioid receptor states. Nature Communications. 11(1):12. doi: 10.1038/s41467-020-14889-7
  43. Chen, G. F., et al. (2020). Augmentation of Bri2 molecular chaperone activity against amyloid-beta reduces neurotoxicity in mouse hippocampus in vitro. Communications Biology. 3(1):12. doi: 10.1038/s42003-020-0757-z
  44. Chillon, I., et al. (2020). The molecular structure of long non-coding RNAs: emerging patterns and functional implications. Critical Reviews in Biochemistry and Molecular Biology. 55(6):29. doi: 10.1080/10409238.2020.1828259
  45. Ciambellotti, S., et al. (2020). Iron Biomineral Growth from the Initial Nucleation Seed in L-Ferritin. Chemistry-a European Journal. 26(26):5770-5773. doi: 10.1002/chem.202000064
  46. Cioce, A., et al. (2020). Rapid On-Chip Synthesis of Complex Glycomimetics from N-Glycan Scaffolds for Improved Lectin Targeting. Chemistry. 26(56):12809-12817. doi: 10.1002/chem.202000026
  47. 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
  48. 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
  49. da Silva, V. M., et al. (2020). High-resolution structure of a modular hyperthermostable endo-beta-1,4-mannanase from Thermotoga petrophila: The ancillary immunoglobulin-like module is a thermostabilizing domain. Biochimica Et Biophysica Acta-Proteins and Proteomics. 1868(8):8. doi: 10.1016/j.bbapap.2020.140437
  50. Dalzon, B., et al. (2020). Influences of Nanoparticles Characteristics on the Cellular Responses: The Example of Iron Oxide and Macrophages. Nanomaterials. 10(2):18. doi: 10.3390/nano10020266
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  54. 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
  55. 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
  56. 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
  57. Dekoninck, K., et al. (2020). Defining the function of OmpA in the Rcs stress response. eLife. 9. doi: 10.7554/eLife.60861
  58. 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
  59. 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
  60. 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
  61. 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
  62. 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
  63. 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
  64. Donchet, A., et al. (2020). Differential Behaviours and Preferential Bindings of Influenza Nucleoproteins on Importins-alpha. Viruses. 12(8):16. doi: 10.3390/v12080834
  65. 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
  66. 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
  67. 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
  68. Fajardo, A. S., et al. (2020). Structural Insights into the Mechanism of the Radical SAM Carbide Synthase NifB, a Key Nitrogenase Cofactor Maturating Enzyme. Journal of the American Chemical Society. 142(25):11006-11012. doi: 10.1021/jacs.0c02243
  69. Fouet, G., et al. (2020). Headless C1q: a new molecular tool to decipher its collagen-like functions. FEBS J.12. doi: 10.1111/febs.15543
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  71. 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
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  75. 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
  76. 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
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  82. 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
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  88. 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
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2018

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2013

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2012

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 9. Oksanen, H. M., et al. (2012). Monolithic ion exchange chromatographic methods for virus purification. Virology, 434(2), 271-277. doi:10.1016/j.virol.2012.09.019

 10. Perez, A. B., et al. (2012). Extraction of Glomalin and Associated Compounds with Two Chemical Solutions in Cultivated Tepetates of Mexico. Communications in Soil Science and Plant Analysis, 43(1-2), 28-35. doi:10.1080/00103624.2012.631403

 11. Ruskamo, S., et al. (2012). The C-terminal rod 2 fragment of filamin A forms a compact structure that can be extended. Biochemical Journal, 446, 261-269. doi:10.1042/bj20120361

 12. Senčilo, A., et al. (2012). Related haloarchaeal pleomorphic viruses contain different genome types. Nucleic Acids Research, 40(12), 5523-5534. doi:10.1093/nar/gks215

 13. Sun, X. Y., et al. (2012). Probing, by Self-Assembly, the Number of Potential Binding Sites for Minor Protein Subunits in the Procapsid of Double-Stranded RNA Bacteriophage phi 6. Journal

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 14. Thielmann, Y., et al. (2012). The ESFRI Instruct Core Centre Frankfurt: automated high-throughput crystallization suited for membrane proteins and more. J Struct Funct Genomics, 13(2), 63-69. doi:10.1007/s10969-011-9118-y

 15. Trowitzsch, S., et al. (2012). MultiBac complexomics. Expert Review of Proteomics, 9(4), 363-373. doi:10.1586/epr.12.32 



2011

1. Banci, L., et al. (2011). NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Diemutase. Journal of the American Chemical Society, 133(2), 345-349. doi:10.1021/ja1069689

 2. Bertini, I., et al. (2011). High-Resolution Characterization of Intrinsic Disorder in Proteins: Expanding the Suite of C-13-Detected NMR Spectroscopy Experiments to Determine Key Observables. Chembiochem, 12(15), 2347-2352. doi:10.1002/cbic.201100406

 3. Bertini, I., et al. (2011). C-13 Direct-Detection Biomolecular NMR Spectroscopy in Living Cells. Angewandte Chemie-International Edition, 50(10), 2339-2341. doi:10.1002/anie.201006636

 4. Bertini, I., et al. (2011). A New Structural Model of A beta(40) Fibrils. Journal of the American Chemical Society, 133(40), 16013-16022. doi:10.1021/ja2035859

 5. Daniel, E., et al. (2011). xtalPiMS: A PiMS-based web application for the management and monitoring of crystallization trials. Journal of Structural Biology, 175(2), 230-235. doi:10.1016/j.jsb.2011.05.008

 6. Hedderich, T., et al. (2011). PICKScreens, A New Database for the Comparison of Crystallization Screens for Biological Macromolecules. Crystal Growth & Design, 11(2), 488-491. doi:10.1021/cg101267n

 7. Imasaki, T., et al. (2011). Architecture of the Mediator head module. Nature, 475(7355), 240-U245. doi:10.1038/nature10162

 8. Morris, C., et al. (2011). The Protein Information Management System (PiMS): a generic tool for any structural biology research laboratory. Acta Crystallographica Section D-Biological Crystallography, 67, 249-260. doi:10.1107/s0907444911007943

 9. Perrakis, A., et al. (2011). From SPINE to SPINE-2 complexes and beyond. J Struct Biol, 175(2), 105. doi:10.1016/j.jsb.2011.05.013

 10. Popoff, V., et al. (2011). Several ADP-ribosylation Factor (Arf) Isoforms Support COPI Vesicle Formation. Journal of Biological Chemistry, 286(41), 35634-35642. doi:10.1074/jbc.M111.261800

 11. Praper, T., et al. (2011). Perforin activity at membranes leads to invaginations and vesicle formation. Proceedings of the National Academy of Sciences of the United States of America, 108(52), 21016-21021. doi:10.1073/pnas.1107473108

 12. Trowitzsch, S., et al. (2011). Light it up: Highly efficient multigene delivery in mammalian cells. Bioessays, 33(12), 946-955. doi:10.1002/bies.201100109

 13. Vijayachandran, L. S., et al. (2011). Robots, pipelines, polyproteins: Enabling multiprotein expression in prokaryotic and eukaryotic cells. Journal of Structural Biology, 175(2), 198-208. doi:10.1016/j.jsb.2011.03.007

 14. Yumerefendi, H., et al. (2011). Library-based methods for identification of soluble expression constructs. Methods, 55(1), 38-43. doi:10.1016/j.ymeth.2011.06.007

 15. Zhao, Y. G., et al. (2011). Automation of large scale transient protein expression in mammalian

cells. Journal of Structural Biology, 175(2), 209-215. doi:10.1016/j.jsb.2011.04.017



2010

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

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

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

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

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

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



2009

1. Bieniossek, C., et al. (2009). Towards eukaryotic structural complexomics. J Struct Funct Genomics, 10(1), 37-46. doi:10.1007/s10969-008-9047-6

 2. Bieniossek, C., et al. (2009). Automated unrestricted multigene recombineering for multiprotein complex production. Nature Methods, 6(6), 447-U468. doi:10.1038/nmeth.1326

 3. Spadiut, O., et al. (2009). Improving thermostability and catalytic activity of pyranose 2-oxidase     from Trametes multicolor by rational and semi-rational design. Febs Journal, 276(3), 776-792. Doi:10.1111/j.1742-4658.2008.06823.x