Source:http://linkedlifedata.com/resource/pubmed/id/15157517
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
10
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| pubmed:dateCreated |
2004-5-25
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| pubmed:abstractText |
Increased histone acetylation has long been linked to gene activation, but little is known about how acetylation levels are regulated, largely because the histone acetyltransferase activities (HATs) responsible for this modification have been cloned only recently. Comparison of the biochemical nature of the Tetrahymena HAT A complex with the genetic and biochemical properties of the Saccharomyces Gcn5p-Ado complex leads us to propose that histone acetylase assemblies may be modular in nature and that this modularity may be an intimate part of the association of these enzymes with chromatin. The 'subunit-exchange' model provides a mechanism for the regulation and targeting of both histone acetylases and deacetylases and has implications for the control of cell growth, proliferation and tumorigenesis.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0962-8924
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
6
|
| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
371-5
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| pubmed:year |
1996
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| pubmed:articleTitle |
The subunit-exchange model of histone acetylation.
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| pubmed:affiliation |
Dept of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston, TX 77030, USA. syr@utmdacc.mda.uth.tmc.edu
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| pubmed:publicationType |
Journal Article
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