Source:http://linkedlifedata.com/resource/pubmed/id/11311229
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2001-4-20
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pubmed:abstractText |
Recent investigations have allowed the identification of an increasing number of distinct nuclear multi-component complexes containing several types of enzymatic activity. Many of the complexes containing histone deacetylases are believed to control transcription and chromatin remodeling. We suggest here that at least some of these abundant complexes are likely to be "molecular reservoirs" of dynamic composition that exchange factors with other less abundant and functional complexes, according to specific required activities.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
494
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
141-4
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11311229-Cell Nucleus,
pubmed-meshheading:11311229-Histone Deacetylases,
pubmed-meshheading:11311229-Macromolecular Substances,
pubmed-meshheading:11311229-Models, Biological,
pubmed-meshheading:11311229-Multienzyme Complexes,
pubmed-meshheading:11311229-Protein Subunits,
pubmed-meshheading:11311229-Protein Transport
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pubmed:year |
2001
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pubmed:articleTitle |
Histone deacetylase complexes: functional entities or molecular reservoirs.
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pubmed:affiliation |
Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation, INSERM U309, Equipe chromatine et expression des gènes, Institut Albert Bonniot, Faculté de Médecine, Domaine de la Merci, 38706 La Tronche Cedex, France. khochbin@ujf-grenoble.fr
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pubmed:publicationType |
Journal Article
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