Gcn5p is involved in the acetylation of histone H3 in nucleosomes.
about
Acetylation of histones and transcription-related factorsCharacterization of yeast histone H3-specific type B histone acetyltransferases identifies an ADA2-independent Gcn5p activityImplication of posttranslational histone modifications in nucleotide excision repairHistone H3 specific acetyltransferases are essential for cell cycle progression.Mutational analysis of the C-terminal FATC domain of Saccharomyces cerevisiae Tra1.Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction.The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae.Comprehensive analysis of interacting proteins and genome-wide location studies of the Sas3-dependent NuA3 histone acetyltransferase complexHif1 is a component of yeast histone acetyltransferase B, a complex mainly localized in the nucleus.Plasmodium falciparum histone acetyltransferase, a yeast GCN5 homologue involved in chromatin remodeling.The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway.Cluster analysis of mass spectrometry data reveals a novel component of SAGAHAT1 and HAT2 proteins are components of a yeast nuclear histone acetyltransferase enzyme specific for free histone H4.Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60Molecular genetics of the RNA polymerase II general transcriptional machineryMulti-tasking on chromatin with the SAGA coactivator complexes.The SAGA of Spt proteins and transcriptional analysis in yeast: past, present, and future.Histone acetyltransferase complexes can mediate transcriptional activation by the major glucocorticoid receptor activation domainComponents of the SAGA histone acetyltransferase complex are required for repressed transcription of ARG1 in rich medium.Processing mechanism and substrate selectivity of the core NuA4 histone acetyltransferase complex.Two Drosophila Ada2 homologues function in different multiprotein complexesRole of ZBP-89 in human globin gene regulation and erythroid differentiationExpression and purification of recombinant yeast Ada2/Ada3/Gcn5 and Piccolo NuA4 histone acetyltransferase complexesMutations in chromatin components suppress a defect of Gcn5 protein in Saccharomyces cerevisiae.Suberoylanilide hydroxamic acid (SAHA) has potent anti-glioma properties in vitro, ex vivo and in vivo.Methylation of histone H3 mediates the association of the NuA3 histone acetyltransferase with chromatinAcetylome profiling reveals overlap in the regulation of diverse processes by sirtuins, gcn5, and esa1.Che1/AATF interacts with subunits of the histone acetyltransferase core module of SAGA complexes.Gcn5p, a Transcription-related Histone Acetyltransferase, Acetylates Nucleosomes and Folded Nucleosomal Arrays in the Absence of Other Protein Subunits
P2860
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P2860
Gcn5p is involved in the acetylation of histone H3 in nucleosomes.
description
1997 nî lūn-bûn
@nan
1997 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
Gcn5p is involved in the acetylation of histone H3 in nucleosomes.
@ast
Gcn5p is involved in the acetylation of histone H3 in nucleosomes.
@en
Gcn5p is involved in the acetylation of histone H3 in nucleosomes.
@nl
type
label
Gcn5p is involved in the acetylation of histone H3 in nucleosomes.
@ast
Gcn5p is involved in the acetylation of histone H3 in nucleosomes.
@en
Gcn5p is involved in the acetylation of histone H3 in nucleosomes.
@nl
prefLabel
Gcn5p is involved in the acetylation of histone H3 in nucleosomes.
@ast
Gcn5p is involved in the acetylation of histone H3 in nucleosomes.
@en
Gcn5p is involved in the acetylation of histone H3 in nucleosomes.
@nl
P50
P1433
P1476
Gcn5p is involved in the acetylation of histone H3 in nucleosomes
@en
P2093
P304
P356
10.1016/S0014-5793(97)00049-5
P407
P577
1997-02-01T00:00:00Z