Publications

Found 11 results
Filters: Author is Syroegin, Egor A  [Clear All Filters]
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Mitcheltree, M. J., Pisipati, A., Syroegin, E. A., Silvestre, K. J., Klepacki, D., Mason, J. D., Terwilliger, D. W., Testolin, G., Pote, A. R., J Y Wu, K., Ladley, R. Porter, Chatman, K., Mankin, A. S., Polikanov, Y. S., and Myers, A. G. (2021) A synthetic antibiotic class overcoming bacterial multidrug resistance. Nature. 10.1038/s41586-021-04045-6
Svetlov, M. S., Syroegin, E. A., Aleksandrova, E. V., Atkinson, G. C., Gregory, S. T., Mankin, A. S., and Polikanov, Y. S. (2021) Structure of Erm-modified 70S ribosome reveals the mechanism of macrolide resistance. Nat Chem Biol. 10.1038/s41589-020-00715-0
Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18
Chen, C. - W., Leimer, N., Syroegin, E. A., Dunand, C., Bulman, Z. P., Lewis, K., Polikanov, Y. S., and Svetlov, M. S. (2023) Structural insights into the mechanism of overcoming Erm-mediated resistance by macrolides acting together with hygromycin-A. Nat Commun. 14, 4196
Aleksandrova, E. V., J Y Wu, K., Tresco, B. I. C., Syroegin, E. A., Killeavy, E. E., Balasanyants, S. M., Svetlov, M. S., Gregory, S. T., Atkinson, G. C., Myers, A. G., and Polikanov, Y. S. (2024) Structural basis of Cfr-mediated antimicrobial resistance and mechanisms to evade it. Nat Chem Biol. 20, 867-876
Syroegin, E. A., Aleksandrova, E. V., and Polikanov, Y. S. (2022) Structural basis for the inability of chloramphenicol to inhibit peptide bond formation in the presence of A-site glycine. Nucleic Acids Res. 50, 7669-7679
Syroegin, E. A., Flemmich, L., Klepacki, D., Vázquez-Laslop, N., Micura, R., and Polikanov, Y. S. (2022) Structural basis for the context-specific action of the classic peptidyl transferase inhibitor chloramphenicol. Nat Struct Mol Biol. 29, 152-161