Researcher Portfolio

Bohn, Stefan

Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, Plitzko, Jürgen / Cryo-EM Technology, Max Planck Institute of Biochemistry, Max Planck Society

Researcher Profile

Position: Plitzko, Jürgen / Cryo-EM Technology, Max Planck Institute of Biochemistry, Max Planck Society

Position: Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society

Researcher ID: https://pure.mpg.de/cone/persons/resource/persons77778

External references

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Publications

: Zinzula, L., Beck, F., Camasta, M., Bohn, S., Liu, C., Morado, D., Bracher, A., Plitzko, J. M., & Baumeister, W. (2024). Cryo-EM structure of single-layered nucleoprotein-RNA complex from Marburg virus. Nature Communications, 15(1): 10307. doi:10.1038/s41467-024-54431-7. [PubMan] : Wagner, J., Carvajal Alvarez, A. I., Bracher, A., Beck, F., Wan, W., Bohn, S., Körner, R., Baumeister, W., Fernandez-Busnadiego, R., & Hartl, F. U. (2024). Visualizing chaperonin function in situ by cryo-electron tomography. Nature, 633(8029), 459-464. doi:10.1038/s41586-024-07843-w. [PubMan] : Bohnacker, S., Henkel, F. D. R., Hartung, F., Geerlof, A., Riemer, S., Prodjinotho, U. F., Salah, E. B., Mourão, A. S. D., Bohn, S., Teder, T., Thomas, D., Gurke, R., Boeckel, C., Ud-Dean, M., König, A.-C., Quaranta, A., Alessandrini, F., Lechner, A., Spitzlberger, B., Kabat, A. M., Pearce, E., Haeggström, J. Z., Hauck, S. M., Wheelock, C. E., Jakobsson, P.-J., Sattler, M., Voehringer, D., Feige, M. J., da Costa, C. P., & Bieren, J.-E.-v. (2024). A helminth enzyme subverts macrophage-mediated immunity by epigenetic targeting of prostaglandin synthesis. Science Immunology, 9(102): eadl1467. doi:10.1126/sciimmunol.adl1467. [PubMan] : Zabret, J., Bohn, S., Schuller, S. K., Arnolds, O., Möller, M., Meier-Credo, J., Liauw, P., Chan, A., Tajkhorshid, E., Langer, J. D., Stoll, R., Krieger-Liszkay, A., Engel, B. D., Rudack, T., Schuller, J. M., & Nowaczyk, M. M. (2021). Structural insights into photosystem II assembly. Nature Plants, 7, 524-538. doi:10.1038/s41477-021-00895-0. [PubMan] : Zabret, J., Bohn, S., Schuller, S. K., Moeller, M., Meier-Credo, J., Liauw, P., Chan, A., Tajkhorshid, E., Langer, J. D., Krieger-Liszkay, A., Engel, B. D., Rudack, T., Schuller, J. M., & Nowaczyk, M. M. (2021). CryoEM structure of PSII assembly intermediate: insights into the role of auxiliary proteins. FEBS Open Bio, 11, 86-86. [PubMan] : Zinzula, L., Beck, F., Klumpe, S., Bohn, S., Pfeifer, G., Bollschweiler, D., Nagy, I., Plitzko, J. M., & Baumeister, W. (2021). Cryo-EM structure of the cetacean morbillivirus nucleoprotein-RNA complex. Journal of Structural Biology, 213(3): 107750. doi:10.1016/j.jsb.2021.107750. [PubMan] : Zinzula, L., Basquin, J., Bohn, S., Beck, F., Klumpe, S., Pfeifer, G., Nagy, I., Bracher, A., Hartl, F. U., & Baumeister, W. (2021). High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2 acute respiratory syndrome coronavirus 2. Biochemical and Biophysical Research Communications, 538, 54-62. doi:10.1016/j.bbrc.2020.09.131. [PubMan] : Zabret, J., Bohn, S., Schuller, S. K., Arnolds, O., Moller, M., Meier-Credo, J., Liauw, P., Chan, A., Tajkhorshid, E., Langer, J. D., Stoll, R., Krieger-Liszkay, A., Engel, B. D., Rudack, T., Schuller, J. M., & Nowaczyk, M. M. (2021). Structural insights into photosystem II assembly. Nature Plants, 7(4), 524-538. doi:10.1038/s41477-021-00895-0. [PubMan] : Braberg, H., Echeverria, I., Bohn, S., Cimermancic, P., Shiver, A., Alexander, R., Xu, J., Shales, M., Dronamraju, R., Jiang, S., Dwivedi, G., Bogdanoff, D., Chaung, K. K., Huttenhain, R., Wang, S., Mavor, D., Pellarin, R., Schneidman, D., Bader, J. S., Fraser, J. S., Morris, J., Haber, J. E., Strahl, B. D., Gross, C. A., Dai, J., Boeke, J. D., Sali, A., & Krogan, N. J. (2020). Genetic interaction mapping informs integrative structure determination of protein complexes. Science, 370(6522): eaaz4910. doi:10.1126/science.aaz4910. [PubMan] : Bohn, S., & Förster, F. (2013). The 26S Proteasome. In N. D. Rawlings, & G. S. Salvesen (Eds.), Handbook of Proteolytic Enzymes, Vol. 1 (3rd Ed., pp. 3691-3700). London: Academic Press. [PubMan] : Bohn, S., Sakata, E., Beck, F., Pathare, G. R., Schnitger, J., Nagy, I., Baumeister, W., & Förster, F. (2013). Localization of the regulatory particle subunit Semi in the 26S proteasome. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 435(2), 250-254. doi:10.1016/j.bbrc.2013.04.069. [PubMan] : Beck, F., Unverdorben, P., Bohn, S., Schweitzer, A., Pfeifer, G., Sakata, E., Nickell, S., Plitzko, J. M., Villa, E., Baumeister, W., & Förster, F. (2012). Near-atomic resolution structural model of the yeast 26S proteasome. Proceedings of the National Academy of Sciences of the United States of America, 109(37), 14870-14875. [PubMan] : Walzthoeni, T., Claassen, M., Leitner, A., Herzog, F., Bohn, S., Förster, F., Beck, M., & Aebersold, R. (2012). False discovery rate estimation for cross-linked peptides identified by mass spectrometry. NATURE METHODS, 9(9), 901-903. doi:10.1038/nmeth.2103. [PubMan] : Leitner, A., Reischl, R., Walzthoeni, T., Herzog, F., Bohn, S., Förster, F., & Aebersold, R. (2012). Expanding the Chemical Cross-Linking Toolbox by the Use of Multiple Proteases and Enrichment by Size Exclusion Chromatography. Special Issue: Prospects in Space and Time, M111.014126, pp. [1]-[12]. doi:10.1074/mcp.M111.014126. [PubMan] : Sakata, E., Bohn, S., Mihalache, O., Kiss, P., Beck, F., Nagy, I., Nickell, S., Tanaka, K., Saeki, Y., Förster, F., & Baumeister, W. (2012). Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy. Proceedings of the National Academy of Sciences of the United States of America, 109(5), 1479-1484. [PubMan] : Lasker, K., Förster, F., Bohn, S., Walzthoeni, T., Villa, E., Unverdorben, P., Beck, F., Aebersold, R., Sali, A., & Baumeister, W. (2012). Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach. Proceedings of the National Academy of Sciences of the United States of America, 109(5), 1380-1387. [PubMan] : Pathare, G. R., Nagy, I., Bohn, S., Unverdorben, P., Hubert, A., Körner, R., Nickell, S., Lasker, K., Sali, A., Tamura, T., Nishioka, T., Förster, F., Baumeister, W., & Bracher, A. (2012). The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together. Proceedings of the National Academy of Sciences of the United States of America, 109(1), 149-154. [PubMan] : Bohn, S. (2011). Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution. PhD Thesis, Technische Universität, München. [PubMan] : Bohn, S., Beck, F., Sakata, E., Walzthoeni, T., Beck, M., Aebersold, R., Förster, F., Baumeister, W., & Nickell, S. (2010). Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution. Proceedings of the National Academy of Sciences of the United States of America, 107(49), 20992-20997. [PubMan] : Kudryashev, M., Lepper, S., Stanway, R., Bohn, S., Baumeister, W., Cyrklaff, M., & Frischknecht, F. (2010). Positioning of large organelles by a membrane- associated cytoskeleton in Plasmodium sporozoites. Cellular Microbiology, 12(3), 362-371. doi:10.1111/j.1462-5822.2009.01399.x. [PubMan] : Kudryashev, M., Lepper, S., Stanway, R., Bohn, S., Baumeister, W., Cyrklaff, M., & Frischknecht, F. (2010). Positioning of large organelles by a membrane- associated cytoskeleton in Plasmodium sporozoites. Cellular Microbiology, 12(3), 362-371. [PubMan]