The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae.
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Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivoHuman Elongator facilitates RNA polymerase II transcription through chromatinHuman ADA3 regulates RARalpha transcriptional activity through direct contact between LxxLL motifs and the receptor coactivator pocketHuman papillomavirus oncoprotein E6 inactivates the transcriptional coactivator human ADA3Acetylation of histones and transcription-related factorsA multiplicity of coactivators is required by Gcn4p at individual promoters in vivoCharacterization of yeast histone H3-specific type B histone acetyltransferases identifies an ADA2-independent Gcn5p activityGenome-wide analysis of Rad52 foci reveals diverse mechanisms impacting recombination.Histone H3 specific acetyltransferases are essential for cell cycle progression.Mutational analysis of the C-terminal FATC domain of Saccharomyces cerevisiae Tra1.The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex.Multiple histone modifications in euchromatin promote heterochromatin formation by redundant mechanisms in Saccharomyces cerevisiae.Polyglutamine-expanded spinocerebellar ataxia-7 protein disrupts normal SAGA and SLIK histone acetyltransferase activity.Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities.Sds3 (suppressor of defective silencing 3) is an integral component of the yeast Sin3[middle dot]Rpd3 histone deacetylase complex and is required for histone deacetylase activity.An array of coactivators is required for optimal recruitment of TATA binding protein and RNA polymerase II by promoter-bound Gcn4p.Comprehensive analysis of interacting proteins and genome-wide location studies of the Sas3-dependent NuA3 histone acetyltransferase complexCombinatorial depletion analysis to assemble the network architecture of the SAGA and ADA chromatin remodeling complexes.Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8.The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway.Yng1p modulates the activity of Sas3p as a component of the yeast NuA3 Hhistone acetyltransferase complex.Applicability of tandem affinity purification MudPIT to pathway proteomics in yeast.Interdependent recruitment of SAGA and Srb mediator by transcriptional activator Gcn4p.Mot1-mediated control of transcription complex assembly and activity.Human papilloma virus 16 E6 oncoprotein inhibits retinoic X receptor-mediated transactivation by targeting human ADA3 coactivatorThe role of transcriptional corepressor Nif3l1 in early stage of neural differentiation via cooperation with Trip15/CSN2Histone H3K56 acetylation, Rad52, and non-DNA repair factors control double-strand break repair choice with the sister chromatidAdenovirus E1A requires the yeast SAGA histone acetyltransferase complex and associates with SAGA components Gcn5 and Tra1.Histone acetylation, acetyltransferases, and ataxia--alteration of histone acetylation and chromatin dynamics is implicated in the pathogenesis of polyglutamine-expansion disordersThe histone acetyltransferase GCN5 affects the inflorescence meristem and stamen development in Arabidopsis.Synergistic action of histone acetyltransferase GCN5 and receptor CLAVATA1 negatively affects ethylene responses in Arabidopsis thaliana.Not5-dependent co-translational assembly of Ada2 and Spt20 is essential for functional integrity of SAGAGcn5-mediated Rph1 acetylation regulates its autophagic degradation under DNA damage stress.MCL-CAw: a refinement of MCL for detecting yeast complexes from weighted PPI networks by incorporating core-attachment structure.GCN5 dependence of chromatin remodeling and transcriptional activation by the GAL4 and VP16 activation domains in budding yeast.Elongator complex influences telomeric gene silencing and DNA damage response by its role in wobble uridine tRNA modification.Cryptococcus neoformans histone acetyltransferase Gcn5 regulates fungal adaptation to the hostProteomic tools for cell biology.Components of the SAGA histone acetyltransferase complex are required for repressed transcription of ARG1 in rich medium.N-terminal domain of nuclear IL-1α shows structural similarity to the C-terminal domain of Snf1 and binds to the HAT/core module of the SAGA complex.
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Q24291710-12C4AE63-148F-4D51-B57A-93DE0122E0B4Q24292235-5AABAD0D-7DE2-40EC-A86F-15B7854B06C1Q24307654-326875F8-A2D6-4C3B-8021-40F0926E2EB2Q24537722-6533A423-E8C5-4205-B4E8-C8F0C3B8E628Q24548503-09C563A9-6317-44C0-BE6F-1DC05CDDE601Q24684851-31606C2F-3CAE-40BD-8B76-DECEBB7AEA3FQ24798328-457CF17D-C86D-48DA-A15D-AAF109FF65B4Q27929891-17EE599E-976A-48BC-8798-A705F356AF84Q27929940-DC6E232C-0C97-4628-B583-22FCEB2E4538Q27930623-8B2BCD96-64F4-4AF1-80B9-3473959C1DA2Q27930726-896338C4-54D1-4AC4-999F-644429EADB35Q27931069-D414929A-1F43-4329-A2A8-16C664ED502CQ27931763-EB88EB09-673B-485F-BF44-AD48F956C72AQ27932063-53C3CA5B-4E3D-436C-8E09-0042959F9237Q27932143-B7C5961A-8928-49EB-A7AC-D987100C618DQ27932320-5247DEC1-5CB5-4096-91AC-C86CF55081B6Q27932543-EF4F5356-B7EE-4AB2-837B-E9A3C782CEA9Q27932566-EA1BF766-4C26-4A5B-BA62-40E5299D1D16Q27933975-E8A00420-1DD0-489E-88EE-87886701F4E0Q27934606-CB132BD7-5EDD-4C9F-8132-32E9056E2762Q27935097-5EFB3A03-BF29-4DA5-865E-410D94F407D0Q27936978-D9DCA15D-C827-475E-96EF-886076FDC7C9Q27939381-953E8584-872F-4D27-B986-25C0AD58F7CEQ27939600-10D78C41-DBD9-4174-AA1A-9B118643F9DDQ28202210-CDC4072B-E3A5-42A1-ABB5-C8A892A688E3Q28202532-790DD89B-FB5F-4699-BFC2-BCBCCB6EA10CQ28563892-B6A56EC9-4449-46AF-A6AB-983A41C43153Q30308769-FFF0FC59-248A-491D-BF8F-F8AAF61542A0Q30433574-2FBEB420-A811-45AE-9018-A728E3DB868FQ33347883-7650CE95-48DF-4835-89B3-645A113834AAQ33361972-73833606-5CFD-4CA8-BA6E-4CD1901518ACQ33554086-6718B43F-E777-4265-A567-108F00AFA8B6Q33701454-9A7DD3BB-EB84-478B-BFE0-3890F9F9CDC8Q33715772-1120FAE5-56D0-4070-8259-026107B38956Q33968670-1C93D9CD-08B8-4D90-A150-A4DE1EF4EF68Q34017522-2E5150E2-A52D-470C-B6AD-3F438D8943EEQ34055174-072613D5-029D-4A9B-9B20-0041BB56510BQ34156493-7E09222A-F0E8-4AD5-BDFE-C3BD2B99DE21Q34281088-E985450D-9A41-4284-BE05-6BC40E845E44Q34374051-AD3634EE-656A-482F-A0EA-1FF133916F06
P2860
The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae.
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The ADA complex is a distinct ...... x in Saccharomyces cerevisiae.
@ast
The ADA complex is a distinct ...... x in Saccharomyces cerevisiae.
@en
The ADA complex is a distinct ...... x in Saccharomyces cerevisiae.
@nl
type
label
The ADA complex is a distinct ...... x in Saccharomyces cerevisiae.
@ast
The ADA complex is a distinct ...... x in Saccharomyces cerevisiae.
@en
The ADA complex is a distinct ...... x in Saccharomyces cerevisiae.
@nl
prefLabel
The ADA complex is a distinct ...... x in Saccharomyces cerevisiae.
@ast
The ADA complex is a distinct ...... x in Saccharomyces cerevisiae.
@en
The ADA complex is a distinct ...... x in Saccharomyces cerevisiae.
@nl
P2093
P2860
P356
P1476
The ADA complex is a distinct ...... x in Saccharomyces cerevisiae.
@en
P2093
A Eberharter
D E Sterner
D Schieltz
J L Workman
S L Berger
P2860
P304
P356
10.1128/MCB.19.10.6621
P407
P577
1999-10-01T00:00:00Z