Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A (Q27618997)

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

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instance of

scholarly article

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title

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

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main subject

solution structure

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based on heuristic

inferred from title

author name string

Y Lin

series ordinal

1

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C M Fletcher

series ordinal

2

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J Zhou

series ordinal

3

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C D Allis

series ordinal

4

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G Wagner

series ordinal

5

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language of work or name

English

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publication date

1 July 1999

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published in

Nature

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volume

400

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issue

6739

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page(s)

86-9

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cites work

Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

The CBP co-activator is a histone acetyltransferase

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

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7 January 2021

based on heuristic

inferred from DOI database lookup

The TAF(II)250 subunit of TFIID has histone acetyltransferase activity

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

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7 January 2021

based on heuristic

inferred from DOI database lookup

The transcriptional coactivators p300 and CBP are histone acetyltransferases

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Histone-like TAFs within the PCAF histone acetylase complex

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

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7 January 2021

based on heuristic

inferred from DOI database lookup

A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A

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Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

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7 January 2021

based on heuristic

inferred from DOI database lookup

Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo.

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein.

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

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7 January 2021

based on heuristic

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

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Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

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7 January 2021

based on heuristic

inferred from DOI database lookup

Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Structure of translation factor eIF4E bound to m7GDP and interaction with 4E-binding protein

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Structure and interactions of the translation initiation factor eIF1

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F21922

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7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

DOI

10.1038/21922

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

547919

Dimensions Publication ID

1020565835

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Fatcat ID

release_5ihupoyu4jd33bqrracdiiuxsa

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OpenCitations bibliographic resource ID

547919

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

547919

PubMed publication ID

10403255

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

547919

ResearchGate publication ID

12896582

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