Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Shamil Z. Validov"'
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
Autor:
Lulu Li, Hong-Nan Sun, Miao Zhang, Tai-Hua Mu, Nasir Mehmood Khan, Shujaat Ahmad, Shamil Z. Validov
Publikováno v:
Postharvest Biology and Technology. 201:112366
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(2)
The ribosomal maturation factor (RimP) is a 17.7 kDa protein and is the assembly factor of the 30S subunit. RimP is essential for efficient processing of 16S rRNA and maturation (assembly) of the 30S ribosome. It was suggested that RimP takes part in
Autor:
Keremli Saparmyradov, Rezeda I. Tukhbatova, Maria N. Filimonova, Shamil' Z. Validov, Farida K. Alimova
Publikováno v:
Journal of Computational and Theoretical Nanoscience. 16:216-222
Antifungal Properties, Abiotic Stress Resistance, and Biocontrol Ability of Bacillus mojavensis PS17
Autor:
Roderic Gilles C, Diabankana, Daniel M, Afordoanyi, Radik I, Safin, Rustam M, Nizamov, Lilia Z, Karimova, Shamil Z, Validov
Publikováno v:
Current microbiology. 78(8)
Plant-protecting Bacillus sp. strains used as biocontrol agents frequently produce metabolites inhibiting phytopathogenic fungi. Recently, the search for a novel biocontrol agent with a wide spectrum of disease control drew attention to Bacillus subt
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