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rdf:type |
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|
lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2000-3-2
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pubmed:abstractText |
Histone acetylation is closely linked to gene transcription. The identification of histone acetyltransferases (HATs) and the large multiprotein complexes in which they reside has yielded important insights into how these enzymes regulate transcription. The demonstration that HAT complexes interact with sequence-specific activator proteins illustrates how these complexes target specific genes. In addition to histones, some HATs can acetylate non-histone proteins suggesting multiple roles for these enzymes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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|
pubmed:issn |
0968-0004
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10637607-Acetyltransferases,
pubmed-meshheading:10637607-Animals,
pubmed-meshheading:10637607-Gene Expression Regulation, Fungal,
pubmed-meshheading:10637607-Histone Acetyltransferases,
pubmed-meshheading:10637607-Humans,
pubmed-meshheading:10637607-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10637607-Substrate Specificity,
pubmed-meshheading:10637607-Trans-Activators,
pubmed-meshheading:10637607-Transcription, Genetic,
pubmed-meshheading:10637607-Yeasts
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|
pubmed:year |
2000
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|
pubmed:articleTitle |
The many HATs of transcription coactivators.
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|
pubmed:affiliation |
Howard Hughes Medical Institute, Dept of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802-4500, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
|
