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2020

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  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
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  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
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  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
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  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
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  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
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  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
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  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
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2018

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2013

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2012

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 8. Kliefoth, M., et al. (2012). Genetic analysis of MA4079, an aldehyde dehydrogenase homolog, in Methanosarcina acetivorans. Archives of Microbiology, 194(2), 75-85. doi:10.1007/s00203-011-0727-4

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

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

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

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

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

of Virology, 86(22), 12208-12216. doi:10.1128/jvi.01505-12

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

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



2011

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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



2010

1.  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 




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