
Ning Liu, Oleg Mikhailovskii, Nikolai R. Skrynnikovb, and Yi Xue
https://journals.iucr.org/m/issues/2023/01/00/lz5062/index.html
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Ning Liu, Oleg Mikhailovskii, Nikolai R. Skrynnikovb, and Yi Xue
https://journals.iucr.org/m/issues/2023/01/00/lz5062/index.html
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Ivan S.Podkorytov, Nikolai R.Skrynnikov
https://doi.org/10.1016/j.jmr.2022.107303
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Boris B. Kharkov
https://events.spbu.ru/events/translational-biomedicine-2022
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D.A. Case, H.M. Aktulga, K. Belfon, I.Y. Ben-Shalom, J.T. Berryman, S.R. Brozell, D.S. Cerutti, T.E. Cheatham, III, G.A. Cisneros, V.W.D. Cruzeiro, T.A. Darden, R.E. Duke, G. Giambasu, M.K. Gilson, H. Gohlke, A.W. Goetz, R. Harris, S. Izadi, S.A. Izmailov, K. Kasavajhala, M.C. Kaymak, E. King, A. Kovalenko, T. Kurtzman, T.S. Lee, S. LeGrand, P. Li, C. Lin, J. Liu, T. Luchko, R. Luo, M. Machado, V. Man, M. Manathunga, K.M. Merz, Y. Miao, O. Mikhailovskii, G. Monard, H. Nguyen, K.A. O’Hearn, A. Onufriev, F. Pan, S. Pantano, R. Qi, A. Rahnamoun, D.R. Roe, A. Roitberg, C. Sagui, S. Schott-Verdugo, A. Shajan, J. Shen, C.L. Simmerling, N.R. Skrynnikov, J. Smith, J. Swails, R.C. Walker, J. Wang, J. Wang, H. Wei, R.M. Wolf, X. Wu, Y. Xiong, Y. Xue, D.M. York, S. Zhao, and P.A. Kollman
https://ambermd.org/doc12/Amber22.pdf
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B. Kharkov, X. Duan, J. Rantaharju, M. Sabba, M.H. Levitt, J.W. Canary, A. Jerschow
https://pubs.rsc.org/en/content/articlelanding/2022/cp/d1cp05537b
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Oleg Mikhailovskii, Yi Xue, and Nikolai R. Skrynnikov.
https://doi.org/10.1107/S2052252521011891.
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Dr. Boris B. Kharkov, Ivan S. Podkorytov, Dr. Stanislav A. Bondarev, Dr. Mikhail V. Belousov, Vladislav A. Salikov, Prof. Dr. Galina A. Zhouravleva, Prof. Dr. Nikolai R. Skrynnikov
https://doi.org/10.1002/anie.202102408
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Sevastyan O. Rabdano, Matthew D. Shannon, Sergei A. Izmailov, Nicole Gonzalez Salguero, Mohamad Zandian, Rudra N. Purusottam, Michael G. Poirier, Nikolai R. Skrynnikov and Christopher P. Jaroniec
https://doi.org/10.1002/anie.202012046
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Bolgov, A., Korban, S., Luzik, D., Zhemkov, V., Kim, M., Rogacheva, O., & Bezprozvanny, I. Crystal structure of the SH3 domain of growth factor receptor-bound protein 2. Acta Crystallographica Section F: Structural Biology Communications, 76(6), 263-270, 2020.
This study presents the crystal structure of the N-terminal SH3 (SH3N) domain of growth factor receptor-bound protein 2 (Grb2) at 2.5 Å resolution. Grb2 is a small (215-amino-acid) adaptor protein that is widely expressed and involved in signal transduction/cell communication. The crystal structure of full-length Grb2 has previously been reported (PDB entry 1gri). The structure of the isolated SH3N domain is consistent with the full-length structure. The structure of the isolated SH3N domain was solved at a higher resolution (2.5 Å compared with 3.1 Å for the previously deposited structure) and made it possible to resolve some of the loops that were missing in the full-length structure. In addition, interactions between the carboxy-terminal region of the SH3N domain and the Sos1-binding sites were observed in the structure of the isolated domain. Analysis of these interactions provided new information about the ligand-binding properties of the SH3N domain of Grb2.
Izmailov, S.A, Rabdano, S.O., Hasanbasri, Z., Podkorytov, I.S., Saxena, S., Skrynnikov, N.R. Structural and dynamic origins of ESR lineshapes in spin-labeled GB1 domain: the insights from spin dynamics simulations based on long MD trajectories. Scientific Reports 2020.
DOI: 10.1038/s41598-019-56750-y
Tags: Izmailov, Podkorytov, Rabdano, Skrynnikov