Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Vladislav Kljashtorny"'
Autor:
Vladislav Kljashtorny, Stanislav Nikonov, Lev Ovchinnikov, Dmitry Lyabin, Nicolas Vodovar, Patrick Curmi, Philippe Manivet
Publikováno v:
PLoS ONE, Vol 10, Iss 7, p e0130318 (2015)
The human YB-1 protein plays multiple cellular roles, of which many are dictated by its binding to RNA and DNA through its Cold Shock Domain (CSD). Using molecular dynamics simulation approaches validated by experimental assays, the YB1 CSD was found
Externí odkaz:
https://doaj.org/article/0139f4be3a6a41b9b630c4c9a4d48e3e
Autor:
Irina Strazhesko, Olga Tkacheva, Daria Kashtanova, Mikhail Ivanov, Vladislav Kljashtorny, Antonina Esakova, Maria Karnaushkina, Cassandra Guillemette, Amber Hewett, Véronique Legault, Lilit Maytesian, Maria Litvinova, Alan Cohen, Alexey Moskalev
Publikováno v:
Aging. 14(4)
Old age is a crucial risk factor for severe coronavirus disease 2019 (COVID-19), with serious or fatal outcomes disproportionately affecting older adults compared with the rest of the population. We proposed that the physiological health status and b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2042b159aca336244d3a4fbef201a8fa
https://pubmed.ncbi.nlm.nih.gov/35213841
https://pubmed.ncbi.nlm.nih.gov/35213841
Publikováno v:
Crystallography Reports. 62:584-588
The halophilic archaeon Haloarcula marismortui proliferates in the Dead Sea at extremely high salt concentrations (higher than 3 M). This is the only archaeon, for which the crystal structure of the ribosomal 50S subunit was determined. However, the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3f87fd29e8b759325055052f8f00e20c
https://doi.org/10.1134/s1063774517040137
https://doi.org/10.1134/s1063774517040137
Autor:
O. G. Korotkova, Arkady P. Sinitsyn, Svetlana Tishchenko, Alexander V. Gusakov, Azat Gabdulkhakov, Anna Vakhrusheva, V. A. Nemashkalov, O. V. Kravchenko, Vladislav Kljashtorny
Publikováno v:
Crystallography Reports. 62:254-259
Enzyme additives capable of degrading non-starch polysaccharides of cereal cell walls, which are major ingredients used in animal feed, can improve the efficiency of livestock production. Non-starch polysaccharides have antinutritional properties tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f3f2798b829eb2b6846ab871a01afda1
https://doi.org/10.1134/s1063774517020304
https://doi.org/10.1134/s1063774517020304
Autor:
Elena Stolboushkina, Oleg Nikonov, Udo Bläsi, O. V. Kravchenko, V.I. Arkhipova, Maria Garber, Stanislav Nikonov, Azat Gabdulkhakov, Vladislav Kljashtorny, Birgit Märtens
Publikováno v:
Journal of Molecular Biology. 427:3086-3095
The heterotrimeric archaeal IF2 orthologue of eukaryotic translation initiation factor 2 consists of the α-subunit, β-subunit and γ-subunit. Previous studies showed that the γ-subunit of aIF2, besides its central role in Met-tRNAi binding, has an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f1bdab7a3c7691d40925fc1655efe98
https://doi.org/10.1016/j.jmb.2015.07.020
https://doi.org/10.1016/j.jmb.2015.07.020
Autor:
Alexei Nikulin, N. Nevskaya, Svetlana Tishchenko, Wolfgang Piendl, O. S. Kostareva, P. V. Gulak, Maria Garber, Vladislav Kljashtorny, Stanislav Nikonov
Publikováno v:
Journal of Molecular Biology. 383:301-305
The two-domain ribosomal protein L1 has a dual function as a primary rRNA-binding ribosomal protein and as a translational repressor that binds its own mRNA. Here, we report the crystal structure of a complex between the isolated domain I of L1 from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6aee7942c8095c2d7febe6fc89115a52
https://doi.org/10.1016/j.jmb.2008.08.058
https://doi.org/10.1016/j.jmb.2008.08.058
Autor:
Natalia Davydova, Natalia Nevskaya, Maria Garber, Vladislav Kljashtorny, Svetlana Tishchenko, Stanislav Nikonov, Olga Kostareva, Victor Streltsov, Ekaterina Nikonova, Wolfgang Piendl
Publikováno v:
Nucleic Acids Research
Ribosomal protein L1 has a dual function as a ribosomal protein binding 23S rRNA and as a translational repressor binding its mRNA. L1 is a two-domain protein with N- and C-termini located in domain I. Earlier it was shown that L1 interacts with the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a96d3762d366bd29260280cfd51a6d6
http://europepmc.org/articles/PMC2175363
http://europepmc.org/articles/PMC2175363
Autor:
Robert A. Zimmermann, Alexei Nikulin, S. Volchkov, Oleg Nikonov, N. Nevskaya, Caroline Köhrer, Stanislav Nikonov, Ekaterina Nikonova, Maria Garber, Peter G. Stockley, Vladislav Kljashtorny, Svetlana Tishchenko, Wolfgang Piendl
Publikováno v:
Journal of Molecular Biology. 355:747-759
The RNA-binding ability of ribosomal protein L1 is of profound interest, since L1 has a dual function as a ribosomal structural protein that binds rRNA and as a translational repressor that binds its own mRNA. Here, we report the crystal structure at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55d1a9868e4a8199d8a88bece433b3b0
https://doi.org/10.1016/j.jmb.2005.10.084
https://doi.org/10.1016/j.jmb.2005.10.084
Autor:
A. P. Korepanov, Vladislav Kljashtorny, Wolfgang Piendl, Stanislav Nikonov, G.M. Gongadze, M. B. Garber, A. Y. Anikaev, A. V. Korobeinikova
Publikováno v:
Biochemistry. Biokhimiia. 79(8)
5S rRNA-binding ribosomal proteins of the L25 family are an evolutional acquisition of bacteria. Earlier we showed that (i) single replacements in the RNA-binding module of the protein of this family result in destabilization or complete impossibilit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5637492cfadf4c4f1101a9c72dd29bd
https://pubmed.ncbi.nlm.nih.gov/25365493
https://pubmed.ncbi.nlm.nih.gov/25365493
Autor:
Anna Sycheva, Svetlana Tishchenko, Wolfgang Piendl, Alexei Nikulin, N. Nevskaya, Maria Garber, Ekaterina Nikonova, O. S. Kostareva, Vladislav Kljashtorny, Sergei A. Moshkovskii, Stanislav Nikonov
Publikováno v:
Journal of molecular recognition : JMR. 24(4)
The formation of a specific and stable complex between two (macro)molecules implies complementary contact surface regions. We used ribosomal protein L1, which specifically binds a target site on 23S rRNA, to study the influence of surface modificatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de4c6140dcf3a1816ee9392946bbb129
https://pubmed.ncbi.nlm.nih.gov/20740692
https://pubmed.ncbi.nlm.nih.gov/20740692