Zobrazeno 1 - 10
of 73
pro vyhledávání: '"Marat M, Yusupov"'
Autor:
Natalia S. Garaeva, Aydar G. Bikmullin, Bulat F. Fatkhullin, Shamil Z. Validov, Bruno Keiffer, Marat M. Yusupov, Konstantin S. Usachev
Publikováno v:
Biomolecular NMR Assignments. 16:373-377
Publikováno v:
Biochemistry. Biokhimiia. 87(6)
Solving the structures of bacterial, archaeal, and eukaryotic ribosomes by crystallography and cryo-electron microscopy has given an impetus for studying intracellular regulatory proteins affecting various stages of protein translation. Among them ar
Autor:
Konstantin S. Usachev, Bulat F. Fatkhullin, Evelina A. Klochkova, Aynur K. Miftakhov, Alexander A. Golubev, Aidar G. Bikmullin, Liliya I. Nurullina, Natalia S. Garaeva, Daut R. Islamov, Azat G. Gabdulkhakov, Natalia V. Lekontseva, Svetlana V. Tishchenko, Vitaly A. Balobanov, Iskander Sh. Khusainov, Marat M. Yusupov, Shamil Z. Validov
Publikováno v:
Journal of Structural Biology
Journal of Structural Biology, Elsevier, 2020, 209, pp.107408-. ⟨10.1016/j.jsb.2019.107408⟩
Journal of Structural Biology, 2020, 209 (1), pp.107408-. ⟨10.1016/j.jsb.2019.107408⟩
Journal of Structural Biology, Elsevier, 2020, 209, pp.107408-. ⟨10.1016/j.jsb.2019.107408⟩
Journal of Structural Biology, 2020, 209 (1), pp.107408-. ⟨10.1016/j.jsb.2019.107408⟩
International audience; Staphylococcus aureus hibernation promoting factor (SaHPF) is responsible for the formation of 100S ribosome dimers, which in turn help this pathogen to reduce energy spent under unfavorable conditions. Ribosome dimer formatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78cefd1383a536f1a4480a9a89686b36
https://hal.archives-ouvertes.fr/hal-03489916
https://hal.archives-ouvertes.fr/hal-03489916
Autor:
Konstantin S, Usachev, Shamil Z, Validov, Iskander Sh, Khusainov, Alexander A, Varfolomeev, Vladimir V, Klochkov, Albert V, Aganov, Marat M, Yusupov
Publikováno v:
Journal of biomolecular NMR. 73(5)
Staphylococcus aureus hibernation promoting factor (SaHPF) is a 22,2 kDa protein which plays a crucial role in 100S Staphylococcus aureus ribosome formation during stress. SaHPF consists of N-terminal domain (NTD) that prevents proteins synthesis by
Autor:
Dmitriy S, Blokhin, Aydar G, Bikmullin, Liliya I, Nurullina, Natalia S, Garaeva, Shamil Z, Validov, Vladimir V, Klochkov, Albert V, Aganov, Iskander Sh, Khusainov, Marat M, Yusupov, Konstantin S, Usachev
Publikováno v:
Biomolecular NMR assignments. 13(1)
Ribosome binding factor A (RbfA) is a 14.9 kDa adaptive protein of cold shock, which is important for bacterial growth at low temperatures. RbfA can bind to the free 30S ribosomal subunit and interacts with the 5'-terminal helix (helix I) of 16S rRNA
Autor:
Konstantin S, Usachev, Rustam Kh, Ayupov, Shamil Z, Validov, Iskander Sh, Khusainov, Marat M, Yusupov
Publikováno v:
Biomolecular NMR assignments. 12(1)
Staphylococcus aureus: hibernation-promoting factor (SaHPF) is a 22.2 kDa stationary-phase protein that binds to the ribosome and turns it to the inactive form favoring survival under stress. Sequence analysis has shown that this protein is combinati
Autor:
Klochkova E; Kazan Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russian Federation., Biktimirov A; Kazan Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russian Federation., Islamov D; Kazan Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russian Federation., Belousov A; Moscow Institute of Physics and Technology, Dolgoprudny 141701, Russian Federation; Sao Carlos Institute of Physics, University of Sao Paulo, poloTErRA, 13563-120, Sao Carlos, São Paolo, Brazil., Validov S; Federal Research Center «Kazan Scientific Center of Russian Academy of Sciences», Kazan, 420111, Russian Federation., Yusupov M; National Research Centre Kurchatov Institute, Kurchatov Sq. 2, 123182, Moscow, Russian Federation; Institute of Genetics, Molecular and Cellular Biology, CNRS UMR7104, INSERM U964, Universit'e de Strasbourg, Illkirch, F-67400, France., Usachev K; Kazan Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russian Federation. Electronic address: k.usachev@kpfu.ru.
Publikováno v:
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2024 Nov 26; Vol. 735, pp. 150852. Date of Electronic Publication: 2024 Oct 18.
Autor:
Biktimirov A; Kazan Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russian Federation., Islamov D; Kazan Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russian Federation; Federal Research Center «Kazan Scientific Center of Russian Academy of Sciences», Kazan, 420111, Russian Federation., Fatkhullin B; Institute of Genetics, Molecular and Cellular Biology, CNRS UMR7104, INSERM U964, Université de Strasbourg, Illkirch, F-67400, France., Lazarenko V; National Research Centre Kurchatov Institute, Kurchatov Sq. 2, 123182, Moscow, Russian Federation., Validov S; Federal Research Center «Kazan Scientific Center of Russian Academy of Sciences», Kazan, 420111, Russian Federation., Yusupov M; Institute of Genetics, Molecular and Cellular Biology, CNRS UMR7104, INSERM U964, Université de Strasbourg, Illkirch, F-67400, France., Usachev K; Kazan Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russian Federation. Electronic address: k.usachev@kpfu.ru.
Publikováno v:
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2024 Mar 05; Vol. 699, pp. 149545. Date of Electronic Publication: 2024 Jan 17.
Autor:
Nurullina L; Integrated Structural Biology, IGBMC - IGBMC - CNRS UMR 7104, Inserm, France., Terrosu S; Integrated Structural Biology, IGBMC - IGBMC - CNRS UMR 7104, Inserm, France., Myasnikov AG; Dubochet Center for Imaging (DCI), EPFL, Lausanne, Switzerland., Jenner LB; Integrated Structural Biology, IGBMC - IGBMC - CNRS UMR 7104, Inserm, France., Yusupov M; Integrated Structural Biology, IGBMC - IGBMC - CNRS UMR 7104, Inserm, France.; Regulatory Genomics Research Center, Institute of Fundamental Medicine and Biology, Kazan Federal University, Russia.
Publikováno v:
FEBS letters [FEBS Lett] 2024 Mar; Vol. 598 (5), pp. 537-547. Date of Electronic Publication: 2024 Feb 23.
Autor:
Garaeva N; Laboratory for Structural Analysis of Biomacromolecules, Federal Research Center «Kazan Scientific Center of Russian Academy of Sciences», Kazan 420111, Russian Federation; Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan 420008, Russian Federation., Fatkhullin B; Department of Integrated Structural Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS UMR7104, INSERM U964, Université de Strasbourg, 67400 Illkirch, France; Institute of Protein Research RAS, 4 Institutskaya, Pushchino 142290, Russian Federation., Murzakhanov F; Institute of Physics, Kazan Federal University, Kazan 420008, Russian Federation., Gafurov M; Institute of Physics, Kazan Federal University, Kazan 420008, Russian Federation., Golubev A; Laboratory for Structural Analysis of Biomacromolecules, Federal Research Center «Kazan Scientific Center of Russian Academy of Sciences», Kazan 420111, Russian Federation., Bikmullin A; Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan 420008, Russian Federation., Glazyrin M; Laboratory for Structural Analysis of Biomacromolecules, Federal Research Center «Kazan Scientific Center of Russian Academy of Sciences», Kazan 420111, Russian Federation., Kieffer B; Department of Integrated Structural Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS UMR7104, INSERM U964, Université de Strasbourg, 67400 Illkirch, France., Jenner L; Department of Integrated Structural Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS UMR7104, INSERM U964, Université de Strasbourg, 67400 Illkirch, France., Klochkov V; NMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kazan 420008, Russian Federation., Aganov A; NMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kazan 420008, Russian Federation., Rogachev A; Moscow Institute of Physics and Technology, Dolgoprudny 141701, Russian Federation; Joint Institute for Nuclear Research, Dubna 141980, Russian Federation., Ivankov O; Joint Institute for Nuclear Research, Dubna 141980, Russian Federation., Validov S; Laboratory for Structural Analysis of Biomacromolecules, Federal Research Center «Kazan Scientific Center of Russian Academy of Sciences», Kazan 420111, Russian Federation; Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan 420008, Russian Federation., Yusupov M; Laboratory for Structural Analysis of Biomacromolecules, Federal Research Center «Kazan Scientific Center of Russian Academy of Sciences», Kazan 420111, Russian Federation; Department of Integrated Structural Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS UMR7104, INSERM U964, Université de Strasbourg, 67400 Illkirch, France. Electronic address: marat@igbmc.fr., Usachev K; Laboratory for Structural Analysis of Biomacromolecules, Federal Research Center «Kazan Scientific Center of Russian Academy of Sciences», Kazan 420111, Russian Federation; Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan 420008, Russian Federation. Electronic address: k.usachev@knc.ru.
Publikováno v:
Structure (London, England : 1993) [Structure] 2024 Jan 04; Vol. 32 (1), pp. 74-82.e5. Date of Electronic Publication: 2023 Nov 23.