Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Liliya I. Nurullina"'
Autor:
E.A. Klochkova, Dmitry S. Blokhin, Alexander Golubev, Aydar Bikmullin, Sh Z Validov, I.Sh. Khusainov, Natalia Garaeva, Marat Yusupov, Liliya I. Nurullina, Konstantin S. Usachev
Publikováno v:
Biochemistry (Moscow). 85:545-552
Ribosome-binding factor A (RbfA) from Staphylococcus aureus is a cold adaptation protein that is required for the growth of pathogenic cells at low temperatures (10-15°C). RbfA is involved in the processing of 16S rRNA, as well as in the assembly an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcfea360c9be4698418c933150dfdbf5
https://doi.org/10.1134/s000629792005003x
https://doi.org/10.1134/s000629792005003x
Autor:
Albert V. Aganov, Marat Yusupov, I. Khusainov, Liliya I. Nurullina, Aydar Bikmullin, Vladimir V. Klochkov, Daut R. Islamov, Konstantin S. Usachev, Gulnara Yusupova, Azat Gabdulkhakov, Natalia Garaeva, Bulat Fatkhullin, Alexander Golubev, Shamil Validov, E.A. Klochkova
Publikováno v:
European Biophysics Journal. 49:223-230
Elongation factor P (EF-P) is a translation protein factor that plays an important role in specialized translation of consecutive proline amino acid motifs. EF-P is an essential protein for cell fitness in native environmental conditions. It regulate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f133c5b4fb6205f04f3bf1357fdd91ed
https://doi.org/10.1007/s00249-020-01428-x
https://doi.org/10.1007/s00249-020-01428-x
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:
I. Khusainov, Albert V. Aganov, Konstantin S. Usachev, Liliya I. Nurullina, Shamil Validov, Marat Yusupov, Natalia Garaeva, Aydar Bikmullin, Dmitriy S. Blokhin, Vladimir V. Klochkov
Publikováno v:
Biomolecular NMR Assignments
Biomolecular NMR Assignments, Springer, 2019, 13 (1), pp.27-30. ⟨10.1007/s12104-018-9845-0⟩
Biomolecular NMR Assignments, Springer, 2019, 13 (1), pp.27-30. ⟨10.1007/s12104-018-9845-0⟩
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bb84b06754bb1b18b04a3e265297d39
https://doi.org/10.1007/s12104-018-9845-0
https://doi.org/10.1007/s12104-018-9845-0
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::65d4dcc864aea4a5ac253c56a1bae099
https://pubmed.ncbi.nlm.nih.gov/30225569
https://pubmed.ncbi.nlm.nih.gov/30225569