Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Dmitry V. Lesnyak"'
Publikováno v:
Известия Томского политехнического университета: Инжиниринг георесурсов, Vol 333, Iss 8, Pp 60-72 (2022)
The relevance of the research. Poor knowledge and economic attractiveness make the problem of forecasting and prospecting for epithermal high-sulfidation gold-silver deposits within the volcanogenic belts of the Russian Federation topical. The main g
Externí odkaz:
https://doaj.org/article/94dd71ee48bb4d29a208b0443476f19a
Publikováno v:
Известия Томского политехнического университета: Инжиниринг георесурсов, Vol 332, Iss 10, Pp 17-32 (2021)
The relevance of the study is determined by obtaining new data concerning mineral composition, textural and structural features, hydrothermal-metasomatic zoning, fluid regime, and types of gold mineralization of two most contrasting areas of the Svet
Externí odkaz:
https://doaj.org/article/29e3fcdbcc1346e293a69ac591dd1faf
Autor:
Roman Yu. Gavrilov, Alexey Ruban, Olesya Savinova, Dmitry V. Lesnyak, Yury S. Ananyev, Tamara Yu. Yakich, Maksim Andreevich Rudmin, Darya V. Levochskaia
Publikováno v:
Ore Geology Reviews. 136:104257
The Svetloye epithermal district (SED) is located within the Okhotsk-Chukotka volcanic belt (OCVB), 220 km southwest of Okhotsk. The OCVB, which formed during the Cretaceous with ore potential, is a large marginal volcanic rock belt associated with c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5245a9b88b451b5217329a3d70984891
https://doi.org/10.1016/j.oregeorev.2021.104257
https://doi.org/10.1016/j.oregeorev.2021.104257
Autor:
Dmitry V. Lesnyak, Irina A. Demina, Maxim S. Svetlov, Dmitry E. Burakovsky, Petr V. Sergiev, Marina V. Serebryakova, Alexey A. Bogdanov, Vadim M. Govorun, Vyacheslav A. Kolb, Olga A. Dontsova
Publikováno v:
Journal of Molecular Biology. 416:656-667
Catalysis of peptide bond formation in the peptidyl transferase center is a major enzymatic activity of the ribosome. Mutations limiting peptidyl transferase activity are mostly lethal. However, cellular processes triggered by peptidyl transferase de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f7aa6ee19a25bf6dfae476d9f888106
https://doi.org/10.1016/j.jmb.2012.01.005
https://doi.org/10.1016/j.jmb.2012.01.005
Autor:
Andrei A. Leonov, Sergey V. Kiparisov, Olga A. Dontsova, Petr V. Sergiev, A. S. Smirnova, Dmitry V. Lesnyak, Dmitry E. Burakovsky, Alexey A. Bogdanov
Publikováno v:
Molecular Biology. 41:939-948
The noncanonical pairing of C2475 with G2529 links 23S rRNA helices 89 and 91 in the Escherichia coli ribosome. These nucleotides are at the intersection of the peptidyltransferase center, the sarcin-ricin loop, and the GTPase-associated center of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5410a1b4206d5f396b1c7c76554289b0
https://doi.org/10.1134/s0026893307060118
https://doi.org/10.1134/s0026893307060118
Autor:
Petr V. Sergiev, Alexey A. Bogdanov, Jerzy Osipiuk, Aled M. Edwards, Tatiana Skarina, Alexei Savchenko, Olga A. Dontsova, Dmitry V. Lesnyak, Andrzej Joachimiak
Publikováno v:
Journal of Biological Chemistry. 282:5880-5887
N2-Methylguanine 966 is located in the loop of Escherichia coli 16 S rRNA helix 31, forming a part of the P-site tRNA-binding pocket. We found yhhF to be a gene encoding for m2G966 specific 16 S rRNA methyltransferase. Disruption of the yhhF gene by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::071ac315317c8301722cf1bf1fb4dda6
https://doi.org/10.1074/jbc.m608214200
https://doi.org/10.1074/jbc.m608214200
Autor:
Sergey V. Kiparisov, Alexey A. Bogdanov, Dmitry E. Burakovsky, Olga A. Dontsova, Dmitry V. Lesnyak, Petr V. Sergiev, Andrei A. Leonov
Publikováno v:
Journal of Molecular Biology. 353:116-123
During the translocation of tRNAs and mRNA relative to the ribosome, the B1a, B1b and B1c bridges undergo the most extensive conformational changes among the bridges between the large and the small ribosomal subunits. The B1a bridge, also called the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::403a461f612c169d21c5060196c66b9c
https://doi.org/10.1016/j.jmb.2005.08.006
https://doi.org/10.1016/j.jmb.2005.08.006
Autor:
Dmitry V. Lesnyak, Alexey A. Bogdanov, Dmitry E. Burakovsky, Sergey V. Kiparisov, Petr V. Sergiev, Olga A. Dontsova, Andrei A. Leonov, Richard Brimacombe
Publikováno v:
Journal of Biological Chemistry. 280:31882-31889
Translocation catalyzed by elongation factor G occurs after the peptidyltransferase reaction on the large ribosomal subunit. Deacylated tRNA in the P-site stimulates multiple turnover GTPase activity of EF-G. We suggest that the allosteric signal fro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2949051309cc0ca3358d29f1509d691c
https://doi.org/10.1074/jbc.m505670200
https://doi.org/10.1074/jbc.m505670200
Autor:
Dmitry V, Lesnyak, Jerzy, Osipiuk, Tatiana, Skarina, Petr V, Sergiev, Alexey A, Bogdanov, Aled, Edwards, Alexei, Savchenko, Andrzej, Joachimiak, Olga A, Dontsova
Publikováno v:
The Journal of biological chemistry. 282(8)
N(2)-Methylguanine 966 is located in the loop of Escherichia coli 16 S rRNA helix 31, forming a part of the P-site tRNA-binding pocket. We found yhhF to be a gene encoding for m(2)G966 specific 16 S rRNA methyltransferase. Disruption of the yhhF gene
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2da3313b94bb557cfc2b2393c7b5beb4
https://pubmed.ncbi.nlm.nih.gov/17189261
https://pubmed.ncbi.nlm.nih.gov/17189261
Publikováno v:
Journal of molecular biology. 364(1)
Escherichia coli ribosomal RNA contains five guanosine residues methylated at N2. The ygjO gene was previously predicted to methylate 16 S rRNA residue G966 due to its high sequence homology with the protein RsmC, responsible for G1207 methylation. W
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8ad8e5c63c3e2831a3c087479ea9ca7
https://pubmed.ncbi.nlm.nih.gov/17010380
https://pubmed.ncbi.nlm.nih.gov/17010380