Insights into structure and function of GCN5/PCAF and yEsa 1 histone acetyltransferase domains: (Q75231779)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14712728%20AND%20SRC:MED&resulttype=core&format=json

17 November 2019

title

Insights into structure and function of GCN5/PCAF and yEsa 1 histone acetyltransferase domains: (English)

1 reference

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17 November 2019

author name string

Adrienne Clements

series ordinal

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14712728%20AND%20SRC:MED&resulttype=core&format=json

17 November 2019

Ronen Marmorstein

series ordinal

2

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17 November 2019

publication date

1 January 2003

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17 November 2019

published in

Methods in Enzymology

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17 November 2019

volume

371

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17 November 2019

page(s)

545-564

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Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome

17 November 2019

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ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation

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Acetylation of histones and transcription-related factors

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Genetic isolation of ADA2: a potential transcriptional adaptor required for function of certain acidic activation domains

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Yeast ADA2 protein binds to the VP16 protein activation domain and activates transcription.

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Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex

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7 January 2021

Expanded lysine acetylation specificity of Gcn5 in native complexes

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7 January 2021

Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines

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7 January 2021

Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates

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Histone-like TAFs within the PCAF histone acetylase complex

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Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction

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A human SPT3-TAFII31-GCN5-L acetylase complex distinct from transcription factor IID

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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 vivo

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The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein

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7 January 2021

Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases

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7 January 2021

Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator

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Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13)

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Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis

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mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila

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7 January 2021

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7 January 2021

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7 January 2021

Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator

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7 January 2021

Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A

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7 January 2021

Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide

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7 January 2021

Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A

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7 January 2021

Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator

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7 January 2021

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7 January 2021

Application of a fluorescent histone acetyltransferase assay to probe the substrate specificity of the human p300/CBP-associated factor

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7 January 2021

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Modulating acetyl-CoA binding in the GCN5 family of histone acetyltransferases

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Mutational analysis of conserved residues in the GCN5 family of histone acetyltransferases

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Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor

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HATs off: selective synthetic inhibitors of the histone acetyltransferases p300 and PCAF.

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Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14712728%20AND%20SRC:MED&resulttype=core&format=json

17 November 2019

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