| pubmed-article:9663395 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9663395 | lifeskim:mentions | umls-concept:C0043343 | lld:lifeskim |
| pubmed-article:9663395 | lifeskim:mentions | umls-concept:C0019643 | lld:lifeskim |
| pubmed-article:9663395 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:9663395 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:9663395 | lifeskim:mentions | umls-concept:C1335843 | lld:lifeskim |
| pubmed-article:9663395 | lifeskim:mentions | umls-concept:C1335841 | lld:lifeskim |
| pubmed-article:9663395 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:9663395 | lifeskim:mentions | umls-concept:C1440961 | lld:lifeskim |
| pubmed-article:9663395 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:9663395 | lifeskim:mentions | umls-concept:C1883220 | lld:lifeskim |
| pubmed-article:9663395 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:9663395 | pubmed:dateCreated | 1998-10-1 | lld:pubmed |
| pubmed-article:9663395 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9663395 | pubmed:abstractText | Chromatin structure plays a crucial regulatory role in the control of gene expression. In eukaryotic nuclei, enzymatic complexes can alter this structure by both targeted covalent modification and ATP-dependent chromatin remodeling. Modification of histone amino termini by acetyltransferases and deacetylases correlates with transcriptional activation and repression [1-3], cell growth [4], and tumorigenesis [5]. Chromatin-remodeling enzymes of the Snf2 superfamily use ATP hydrolysis to restructure nucleosomes and chromatin, events which correlate with activation of transcription [6,7]. We purified a multi-subunit complex from Xenopus laevis eggs which contains six putative subunits including the known deacetylase subunits Rpd3 and RbAp48/p46 [8] as well as substoichiometric quantities of the deacetylase-associated protein Sin3 [9-13]. In addition, we identified one of the other components of the complex to be Mi-2, a Snf2 superfamily member previously identified as an autoantigen in the human connective tissue disease dermatomyositis [14,15]. We found that nucleosome-stimulated ATPase activity precisely copurified with both histone deacetylase activity and the deacetylase enzyme complex. This association of a histone deacetylase with a Snf2 superfamily ATPase suggests a functional link between these two disparate classes of chromatin regulators. | lld:pubmed |
| pubmed-article:9663395 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9663395 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9663395 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9663395 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9663395 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:9663395 | pubmed:issn | 0960-9822 | lld:pubmed |
| pubmed-article:9663395 | pubmed:author | pubmed-author:JonesP LPL | lld:pubmed |
| pubmed-article:9663395 | pubmed:author | pubmed-author:WolffeA PAP | lld:pubmed |
| pubmed-article:9663395 | pubmed:author | pubmed-author:WadeP APA | lld:pubmed |
| pubmed-article:9663395 | pubmed:author | pubmed-author:VermaakDD | lld:pubmed |
| pubmed-article:9663395 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9663395 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:9663395 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:9663395 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9663395 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9663395 | pubmed:pagination | 843-6 | lld:pubmed |
| pubmed-article:9663395 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:9663395 | pubmed:meshHeading | pubmed-meshheading:9663395-... | lld:pubmed |
| pubmed-article:9663395 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9663395 | pubmed:articleTitle | A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase. | lld:pubmed |
| pubmed-article:9663395 | pubmed:affiliation | Laboratory of Molecular Embryology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA. | lld:pubmed |
| pubmed-article:9663395 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9663395 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9663395 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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