Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Yuri A. Nedialkov"'
Autor:
Fadi Assaf, Yuri A. Nedialkov, Kristopher Opron, Amanda J. Anderson, Zachary F. Burton, Robert I. Cukier, Guo-Wei Wei, Hailey L. Caudill
Publikováno v:
Transcription
Based on molecular dynamics simulations and functional studies, a conformational mechanism is posited for forward translocation by RNA polymerase (RNAP). In a simulation of a ternary elongation complex, the clamp and downstream cleft were observed to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::989ddf808590c291fda3ae54269e5d6e
http://europepmc.org/articles/PMC5791816
http://europepmc.org/articles/PMC5791816
Autor:
Zachary F. Burton, Yuri A. Nedialkov, Irina Artsimovitch, Evgeny Nudler, Kristopher Opron, Maria L. Kireeva, Fadi Assaf, Robert I. Cukier, Mikhail Kashlev
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms. 1829:187-198
The bridge α-helix in the β′ subunit of RNA polymerase (RNAP) borders the active site and may have roles in catalysis and translocation. In Escherichia coli RNAP, a bulky hydrophobic segment near the N-terminal end of the bridge helix is identifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6011ffa1e7acb68c6d2ab8eed9fb317f
https://doi.org/10.1016/j.bbagrm.2012.11.005
https://doi.org/10.1016/j.bbagrm.2012.11.005
Autor:
Xue Qian Gong, Yalin Xiong, Chunfen Zhang, Zachary F. Burton, Mikhail Kashlev, Woo Moon, Maria L. Kireeva, Yuri A. Nedialkov
Publikováno v:
Methods. 48:333-345
Strategies for assembly and analysis of human, yeast, and bacterial RNA polymerase elongation complexes are described, and methods are shown for millisecond phase kinetic analyses of elongation using rapid chemical quench flow. Human, yeast, and bact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35312854ae50d323638215c384a4f18d
https://doi.org/10.1016/j.ymeth.2009.04.008
https://doi.org/10.1016/j.ymeth.2009.04.008
Autor:
Jordan D. Irvin, Jeffrey N. Strathern, Maria L. Kireeva, Lucyna Lubkowska, Francisco Malagon, Mikhail Kashlev, Yuri A. Nedialkov, Celine Walmacq
Publikováno v:
Journal of Biological Chemistry. 284:19601-19612
Rpb9 is a small non-essential subunit of yeast RNA polymerase II located on the surface on the enzyme. Deletion of the RPB9 gene shows synthetic lethality with the low fidelity rpb1-E1103G mutation localized in the trigger loop, a mobile element of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33e9189bfa47986b355cdaebec993f9d
https://doi.org/10.1074/jbc.m109.006908
https://doi.org/10.1074/jbc.m109.006908
Autor:
Gina H. Cremona, Mikhail Kashlev, Francisco Malagon, Zachary F. Burton, Yuri A. Purtov, Yuri A. Nedialkov, Maria L. Kireeva, Jeffrey N. Strathern, Lucyna Lubkowska
Publikováno v:
Mol Cell
To study fidelity of RNA polymerase II (Pol II), we analyzed properties of the 6-azauracil-sensitive and TFIIS-dependent E1103G mutant of rbp1 (rpo21), the gene encoding the catalytic subunit of Pol II in Saccharomyces cerevisiae. Using an in vivo re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03ddac9d8f16acca0f2d00a5d9cdf047
https://doi.org/10.1016/j.molcel.2008.04.017
https://doi.org/10.1016/j.molcel.2008.04.017
Publikováno v:
Biochemistry and Cell Biology. 83:486-496
Multi-subunit RNA polymerases bind nucleotide triphosphate (NTP) substrates in the pretranslocated state and carry the dNMPNTP base pair into the active site for phosphoryl transfer. NTP-driven translocation requires that NTP substrates enter the m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df24356da8aa54001684411a441e4755
https://doi.org/10.1139/o05-059
https://doi.org/10.1139/o05-059
Publikováno v:
Journal of Biological Chemistry. 279:27422-27427
Our laboratory has developed methods for transient state kinetic analysis of human RNA polymerase II elongation. In these studies, multiple conformations of the RNA polymerase II elongation complex were revealed by their distinct elongation potential
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::307f638d3c81d416d5759c438a914230
https://doi.org/10.1074/jbc.m402163200
https://doi.org/10.1074/jbc.m402163200
Publikováno v:
Archives of Biochemistry and Biophysics. 425:77-86
Models of mechanisms of transcriptional activation in eukaryotes frequently invoke direct interactions of transcriptional activation domains with target proteins including general transcription factors or coactivators such as chromatin modifying comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::466e53d2d9e8da0342b88b74307d03d6
https://doi.org/10.1016/j.abb.2004.03.002
https://doi.org/10.1016/j.abb.2004.03.002
Publikováno v:
Journal of Biological Chemistry. 277:46998-47003
RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II. Mutations within or adjacent to the alpha1 helix of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4e7c65193b2d3eafc4c447cd9f8d0d5
https://doi.org/10.1074/jbc.m206249200
https://doi.org/10.1074/jbc.m206249200
Publikováno v:
The FASEB Journal. 28
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::78545927505df1f1a591d4cd8cf281f6
https://doi.org/10.1096/fasebj.28.1_supplement.944.2
https://doi.org/10.1096/fasebj.28.1_supplement.944.2