about
Structural analysis and dimerization potential of the human TAF5 subunit of TFIIDThe nuclear import of TAF10 is regulated by one of its three histone fold domain-containing interaction partnersTAF9b (formerly TAF9L) is a bona fide TAF that has unique and overlapping roles with TAF9In vivo functional analysis of the histone 3-like TAF9 and a TAF9-related factor, TAF9LCore promoter binding by histone-like TAF complexesSUMO-1 modification of human transcription factor (TF) IID complex subunits: inhibition of TFIID promoter-binding activity through SUMO-1 modification of hsTAF5Prediction of the general transcription factors associated with RNA polymerase II in Plasmodium falciparum: conserved features and differences relative to other eukaryotesZooming in on Transcription PreinitiationdTAF10- and dTAF10b-Containing Complexes Are Required for Ecdysone-Driven Larval-Pupal Morphogenesis in Drosophila melanogasterCrystal structure of a subcomplex of human transcription factor TFIID formed by TATA binding protein-associated factors hTAF4 (hTAF(II)135) and hTAF12 (hTAF(II)20)Mediator head subcomplex Med11/22 contains a common helix bundle building block with a specific function in transcription initiation complex stabilizationTFIID TAF6-TAF9 Complex Formation Involves the HEAT Repeat-containing C-terminal Domain of TAF6 and Is Modulated by TAF5 ProteinStructural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II DUse of a genetically introduced cross-linker to identify interaction sites of acidic activators within native transcription factor IID and SAGA.Protein-protein interaction map for yeast TFIID.Mutations in the histone fold domain of the TAF12 gene show synthetic lethality with the TAF1 gene lacking the TAF N-terminal domain (TAND) by different mechanisms from those in the SPT15 gene encoding the TATA box-binding protein (TBP)Purification of active TFIID from Saccharomyces cerevisiae. Extensive promoter contacts and co-activator function.TFIIA and the transactivator Rap1 cooperate to commit TFIID for transcription initiationMolecular and genetic characterization of a Taf1p domain essential for yeast TFIID assembly.Structure of promoter-bound TFIID and model of human pre-initiation complex assemblyFunctional analysis of the TFIID-specific yeast TAF4 (yTAF(II)48) reveals an unexpected organization of its histone-fold domainMultivalent engagement of TFIID to nucleosomes.Identification of a small TAF complex and its role in the assembly of TAF-containing complexes.Structure, assembly and dynamics of macromolecular complexes by single particle cryo-electron microscopy.Direct transactivator-transcription factor IID (TFIID) contacts drive yeast ribosomal protein gene transcriptionMolecular architecture of the basal transcription factor B-TFIID.Distinct regulatory mechanisms of eukaryotic transcriptional activation by SAGA and TFIID.Transcriptional regulation in Saccharomyces cerevisiae: transcription factor regulation and function, mechanisms of initiation, and roles of activators and coactivators.TAF10 Interacts with the GATA1 Transcription Factor and Controls Mouse Erythropoiesis.Structure and mechanism of the RNA polymerase II transcription machinery.Human TFIID binds to core promoter DNA in a reorganized structural state.Direct TFIIA-TFIID protein contacts drive budding yeast ribosomal protein gene transcription.Mapping the initiator binding Taf2 subunit in the structure of hydrated yeast TFIIDStructures of three distinct activator-TFIID complexesMapping key functional sites within yeast TFIIDProteomics reveals a physical and functional link between hepatocyte nuclear factor 4alpha and transcription factor IID.The basal initiation machinery: beyond the general transcription factors.Structural dynamics and DNA interaction of human TFIID.New insights into the function of transcription factor TFIID from recent structural studies.Self-association of the amino-terminal domain of the yeast TATA-binding protein.
P2860
Q24293225-00E38910-6F7B-405D-AFAE-93F724EE9602Q24301379-7B6E8C8E-2A47-4241-A0EE-6DDAADC64E46Q24302399-93A5E98F-A09B-4B18-B5F3-3779ED087613Q24306731-E81DB365-1E21-449A-A0E3-5638BC4222B3Q24322695-1249F862-41E3-455D-90E5-28287288AA16Q24337572-17A25335-7E87-46D8-B099-089331CB177FQ24811411-B49EA218-B2C7-4D33-BE85-E01947DB1796Q26749291-03ECB130-2B3B-472A-BF28-411CE5B6B5C0Q27346614-A7C8504D-294F-454F-8563-4EA912605D28Q27639666-F435BE71-3C4A-41F8-8416-AB7793945294Q27667533-B3FFA37A-E942-43C2-8705-29C3B2F13474Q27681162-9ABE90B1-FDEE-41E5-9B84-57DE38FC1340Q27684318-AE189A3D-5A58-4D0B-AA2A-B9A77A7CD147Q27929763-E4DEB988-A8D4-48BC-872A-A6BD4F571EE6Q27930749-34AE5523-56D0-4462-BEC4-0581652FF804Q27932095-FA578227-D079-4A80-A513-41A3C5997D9DQ27932723-35DE4A24-19AE-4D92-908E-8DFDF5F63DB1Q27933367-41263847-0977-43CA-9B43-F741DF22106BQ27940055-BA7BBCAE-3FCD-4775-BE58-E3F6A4162422Q28115645-FE2B663E-B403-45F7-A0B3-19213B3FD0CCQ28202398-62BECBEA-7D68-4BB8-89FF-FBE9489A8E92Q31139142-451EAA5D-DF0D-40B0-8E2B-C646773DE911Q33279534-D7D43099-6F04-459B-82FA-4C2E659B08A4Q33640811-B293B475-9A59-433E-BC3C-AF372C88CDB2Q33832637-29374C16-4FE8-4E22-A9C9-8B9B93D7EE09Q34301663-8FFB2913-2E74-4C10-B082-DC5CC3807840Q34478777-BA9C69EC-D01E-45DF-99D6-54CF6872F57DQ35542072-1B57A63E-1C29-4046-B656-1590C5826BF0Q35626108-06DBBF86-B296-421C-A1BA-F755E37E3C97Q35758805-8034DA7F-D5AD-48E1-B439-3ADE7ADB035CQ36554764-24C31C35-9420-4E1D-8F08-E786D1AC93C0Q37095433-12A77456-30A6-4E7C-B441-CDBD419E6A0BQ37180231-3DED76D5-7820-4708-92FA-7D7DF02D1285Q37247127-B543C4C0-1745-4CF4-BFCF-80A3CD2F323CQ37260390-FBA33D9D-16A2-465D-B07F-E16EE92BF0D3Q37431978-F2AD392C-84D0-4D7E-B836-A38F66FE322DQ37467909-C388795A-63BA-4796-AF5B-4DF4B2AEDF90Q37613614-D2D5A31E-9728-448A-B613-D737B6EA6B26Q37855183-1D9EA1B7-A736-4B6F-87AA-910B8E84F659Q38349446-C90D4C5F-32D5-4BA3-B22C-015D62A8C130
P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Mapping histone fold TAFs within yeast TFIID.
@ast
Mapping histone fold TAFs within yeast TFIID.
@en
Mapping histone fold TAFs within yeast TFIID.
@nl
type
label
Mapping histone fold TAFs within yeast TFIID.
@ast
Mapping histone fold TAFs within yeast TFIID.
@en
Mapping histone fold TAFs within yeast TFIID.
@nl
prefLabel
Mapping histone fold TAFs within yeast TFIID.
@ast
Mapping histone fold TAFs within yeast TFIID.
@en
Mapping histone fold TAFs within yeast TFIID.
@nl
P2093
P2860
P356
P1433
P1476
Mapping histone fold TAFs within yeast TFIID.
@en
P2093
Christine Ruhlmann
Claire Leurent
Doris B Kirschner
P Anthony Weil
Steven Sanders
Véronique Mallouh
P2860
P304
P356
10.1093/EMBOJ/CDF342
P407
P577
2002-07-01T00:00:00Z