Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:9370292rdf:typepubmed:Citationlld:pubmed
pubmed-article:9370292lifeskim:mentionsumls-concept:C0015576lld:lifeskim
pubmed-article:9370292lifeskim:mentionsumls-concept:C0043342lld:lifeskim
pubmed-article:9370292lifeskim:mentionsumls-concept:C0014442lld:lifeskim
pubmed-article:9370292lifeskim:mentionsumls-concept:C1171362lld:lifeskim
pubmed-article:9370292lifeskim:mentionsumls-concept:C0019643lld:lifeskim
pubmed-article:9370292lifeskim:mentionsumls-concept:C0017262lld:lifeskim
pubmed-article:9370292lifeskim:mentionsumls-concept:C1515670lld:lifeskim
pubmed-article:9370292pubmed:issue1-2lld:pubmed
pubmed-article:9370292pubmed:dateCreated1997-12-9lld:pubmed
pubmed-article:9370292pubmed:databankReferencehttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9370292pubmed:abstractTextModification of core histones can alter chromatin structure, facilitating the activation and repression of genes. A key example is the acetylation of N-terminal lysines of the core histones. Recently, the mammalian histone deacetylase HD1 was cloned from Jurkat T cells, and shown to be 60% identical to the yeast global gene regulator Rpd3 (Taunton et al., 1996). Here we report the cloning of HDm, a maternally expressed putative deposition histone deacetylase from Xenopus laevis. Comparison of the amino acid sequences of histone deacetylases from diverse eukaryotes shows high levels of identity within a putative enzyme core region. Further alignment with other types of protein: acetoin-utilizing enzymes from eubacteria; acetylpolyamine hydrolases from mycoplasma and cyanobacteria; and a protein of unknown function from an archaebacterium, reveals an apparently conserved core, and suggests that histone deacetylases belong to an ancient family of enzymes with related functions.lld:pubmed
pubmed-article:9370292pubmed:languageenglld:pubmed
pubmed-article:9370292pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9370292pubmed:citationSubsetIMlld:pubmed
pubmed-article:9370292pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9370292pubmed:statusMEDLINElld:pubmed
pubmed-article:9370292pubmed:monthOctlld:pubmed
pubmed-article:9370292pubmed:issn0378-1119lld:pubmed
pubmed-article:9370292pubmed:authorpubmed-author:SommervilleJJlld:pubmed
pubmed-article:9370292pubmed:authorpubmed-author:LyonsSSlld:pubmed
pubmed-article:9370292pubmed:authorpubmed-author:LadomeryMMlld:pubmed
pubmed-article:9370292pubmed:issnTypePrintlld:pubmed
pubmed-article:9370292pubmed:day1lld:pubmed
pubmed-article:9370292pubmed:volume198lld:pubmed
pubmed-article:9370292pubmed:ownerNLMlld:pubmed
pubmed-article:9370292pubmed:authorsCompleteYlld:pubmed
pubmed-article:9370292pubmed:pagination275-80lld:pubmed
pubmed-article:9370292pubmed:dateRevised2010-11-18lld:pubmed
pubmed-article:9370292pubmed:meshHeadingpubmed-meshheading:9370292-...lld:pubmed
pubmed-article:9370292pubmed:meshHeadingpubmed-meshheading:9370292-...lld:pubmed
pubmed-article:9370292pubmed:meshHeadingpubmed-meshheading:9370292-...lld:pubmed
pubmed-article:9370292pubmed:meshHeadingpubmed-meshheading:9370292-...lld:pubmed
pubmed-article:9370292pubmed:meshHeadingpubmed-meshheading:9370292-...lld:pubmed
pubmed-article:9370292pubmed:meshHeadingpubmed-meshheading:9370292-...lld:pubmed
pubmed-article:9370292pubmed:meshHeadingpubmed-meshheading:9370292-...lld:pubmed
pubmed-article:9370292pubmed:meshHeadingpubmed-meshheading:9370292-...lld:pubmed
pubmed-article:9370292pubmed:meshHeadingpubmed-meshheading:9370292-...lld:pubmed
pubmed-article:9370292pubmed:meshHeadingpubmed-meshheading:9370292-...lld:pubmed
pubmed-article:9370292pubmed:meshHeadingpubmed-meshheading:9370292-...lld:pubmed
pubmed-article:9370292pubmed:meshHeadingpubmed-meshheading:9370292-...lld:pubmed
pubmed-article:9370292pubmed:year1997lld:pubmed
pubmed-article:9370292pubmed:articleTitleXenopus HDm, a maternally expressed histone deacetylase, belongs to an ancient family of acetyl-metabolizing enzymes.lld:pubmed
pubmed-article:9370292pubmed:affiliationDivision of Cell and Molecular Biology, School of Biological and Medical Sciences, University of St Andrews, Fife, Scotland, UK.lld:pubmed
pubmed-article:9370292pubmed:publicationTypeJournal Articlelld:pubmed
entrez-gene:397868entrezgene:pubmedpubmed-article:9370292lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9370292lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9370292lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9370292lld:pubmed