about
Purification and characterization of the human elongator complexTAF7: a possible transcription initiation check-point regulatorRNA polymerase II complexes in the very early phase of transcription are not susceptible to TFIIS-induced exonucleolytic cleavage.Evidence that negative elongation factor represses transcription elongation through binding to a DRB sensitivity-inducing factor/RNA polymerase II complex and RNA.Splicing and transcription-associated proteins PSF and p54nrb/nonO bind to the RNA polymerase II CTDFCP1, a phosphatase specific for the heptapeptide repeat of the largest subunit of RNA polymerase II, stimulates transcription elongation.The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNPMolecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIFThe C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylationRole of the C-terminal domain of RNA polymerase II in U2 snRNA transcription and 3' processingATP bound to the origin recognition complex is important for preRC formationRNA polymerase stalling at developmental control genes in the Drosophila melanogaster embryoThe murine G+C-rich promoter binding protein mGPBP is required for promoter-specific transcriptionHuman CRSP interacts with RNA polymerase II CTD and adopts a specific CTD-bound conformationELL and EAF1 are Cajal body components that are disrupted in MLL-ELL leukemiaCrystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9The highly conserved glutamic acid 791 of Rpb2 is involved in the binding of NTP and Mg(B) in the active center of human RNA polymerase II.Control of eukaryotic transcription elongation.Comparative overview of RNA polymerase II and III transcription cycles, with focus on RNA polymerase III termination and reinitiationRNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approachRPAP1, a novel human RNA polymerase II-associated protein affinity purified with recombinant wild-type and mutated polymerase subunitsThe yeast RNA polymerase II-associated factor Iwr1p is involved in the basal and regulated transcription of specific genes.A Rad26-Def1 complex coordinates repair and RNA pol II proteolysis in response to DNA damage.The Rpb9 subunit of RNA polymerase II binds transcription factor TFIIE and interferes with the SAGA and elongator histone acetyltransferases.Structure-function analysis of human Spt4: evidence that hSpt4 and hSpt5 exert their roles in transcriptional elongation as parts of the DSIF complexPITSLRE p110 protein kinases associate with transcription complexes and affect their activityAndrogen receptor interacts with the positive elongation factor P-TEFb and enhances the efficiency of transcriptional elongationA highly purified RNA polymerase II elongation control systemIdentification and biochemical characterization of a novel transcription elongation factor, Elongin A3Identification of proteins interacting with the RNAPII FCP1 phosphatase: FCP1 forms a complex with arginine methyltransferase PRMT5 and it is a substrate for PRMT5-mediated methylationUp-regulation of P-TEFb by the MEK1-extracellular signal-regulated kinase signaling pathway contributes to stimulated transcription elongation of immediate early genes in neuroendocrine cellsThe positive transcription elongation factor b is an essential cofactor for the activation of transcription by myocyte enhancer factor 2Analysis of the open region of RNA polymerase II transcription complexes in the early phase of elongationA chromatin landmark and transcription initiation at most promoters in human cellsDrosophila melanogaster positive transcriptional elongation factors regulate metabolic and sex-biased expression in adults.The YEATS domain of Taf14 in Saccharomyces cerevisiae has a negative impact on cell growth.The glucocorticoid receptor blocks P-TEFb recruitment by NFkappaB to effect promoter-specific transcriptional repression.Gene-specific repression of the p53 target gene PUMA via intragenic CTCF-Cohesin binding.AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia.C-terminal domain phosphatase-like family members (AtCPLs) differentially regulate Arabidopsis thaliana abiotic stress signaling, growth, and development.
P2860
Q24291914-9EBFEE9F-520B-4B9C-AC75-5B4C3F78C1B7Q24300763-B5439670-218C-4D36-BB2E-20249BEDA6AAQ24530031-F753280F-8D45-4B71-BB7C-C09943595F47Q24537283-9C334F97-CFF0-40EF-9699-297654B82E98Q24540125-D2182D9D-CDF3-43B3-A73E-59DA183DEBFBQ24540277-2F6B9FE9-3373-4A92-B377-1895D525FAA1Q24550508-367935C1-CFE0-4F0A-A11F-35EEAC4A5CD5Q24553649-AC81F501-58B5-4561-81B4-6909807982B5Q24553772-7B926BCC-DBA0-418C-B2ED-58E8DC542C11Q24603743-A24ECD31-8F11-4D80-8577-0AC07E2BFBD9Q24630973-8B633177-F107-4DB4-BEA6-0F604BD35593Q24645367-1BC7CFBA-470B-4552-BE7E-3D2D9E3A6CBFQ24648807-0AD6F6FF-524D-498D-B95A-2DD19DA97D0FQ24675260-7B992E42-C85B-4C00-B3C7-1F1DDEEAF60BQ24683043-76C9229E-710B-4AB7-B7B8-22A03A75FA00Q24683471-70F613E3-4A96-4131-9E42-E739C424B1C8Q24801059-4C8E1425-6193-4FE5-86FE-45B28195ABADQ24805136-77F85961-34D5-4FFF-BC47-855363071FB7Q26830937-14906BB0-2349-4E7E-B83E-3CE3DC2DE29FQ27931237-61BB27B8-1C45-46C7-B040-0E5F8A5FFA7BQ27934170-408852AC-A925-44F7-9288-553DC31D66B5Q27934967-0EDB5637-F780-49E8-BD4C-2285A7143B23Q27937572-49FB77DE-4D12-43F4-89BB-F3514F633698Q27940159-1BF44BEE-6BAD-476C-A527-DD58C2996A2EQ28185959-E063038A-E9AA-4CBB-B797-0C951F8935A6Q28205514-48E6920F-EA02-4D8A-973B-AC282E2E82B3Q28206488-D54D62D8-62C2-4309-8189-3C66C416DF90Q28216031-4D7CB3B6-225F-4C70-AD10-5ACD0DCFE59AQ28216741-949FFBD3-1573-48DD-A517-845826742172Q28304227-D1EE9EFF-309B-41D1-84B3-4E503F91415AQ28572356-D14D8D66-B097-416C-89E2-7A2F48F32DCAQ28595060-4BEC7523-C008-44E9-84F4-8A21712D3B8FQ28646683-1B047A0A-CEB7-4B4A-A928-F30EDDC732AFQ29547180-D675000D-8304-4C6E-94EB-D24402A353D0Q33702832-EB1E0CD1-78D5-4652-B7AB-C5AA8DEDC61EQ33731470-46EB6A82-7C38-4E57-83DA-D2F5753FEE63Q33780734-9B578832-8CC3-44F3-B7E7-88B4CF5847AAQ33839575-B283A596-280E-416B-9432-E7E2A41ACD87Q33857407-7E0B6FD3-2211-4FD8-9E06-8626D4BECD9AQ34076319-6A01E7ED-5C0A-4F9E-830C-10D38E9F360C
P2860
description
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2000
@ast
im August 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2000/08/01)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/08/01)
@nl
наукова стаття, опублікована в серпні 2000
@uk
مقالة علمية (نشرت في أغسطس 2000)
@ar
name
Control of elongation by RNA polymerase II
@ast
Control of elongation by RNA polymerase II
@en
Control of elongation by RNA polymerase II
@nl
type
label
Control of elongation by RNA polymerase II
@ast
Control of elongation by RNA polymerase II
@en
Control of elongation by RNA polymerase II
@nl
prefLabel
Control of elongation by RNA polymerase II
@ast
Control of elongation by RNA polymerase II
@en
Control of elongation by RNA polymerase II
@nl
P2093
P1476
Control of elongation by RNA polymerase II
@en
P2093
A. Shilatifard
J. W. Conaway
R. C. Conaway
P304
P356
10.1016/S0968-0004(00)01615-7
P577
2000-08-01T00:00:00Z