Linked Life Data

9667866

Source:http://linkedlifedata.com/resource/pubmed/id/9667866

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-9-3
pubmed:abstractText
Reversible acetylation of lysines on the amino-terminal tails of nucleosomal histones is correlated with changes in chromatin structure and transcription. The recent characterization of enzymes directly responsible for regulating histone acetylation and deacetylation and the cloning of their encoding cDNAs have provided insights into the possible functional and regulatory mechanisms of these classes of molecules. Nuclear histone acetylases have been shown to be transcriptional coactivators and coactivator-associated proteins, while histone deacetylases have been identified as components of nuclear co-repressor complexes. These findings confirm previous studies linking histone acetylation and transcriptional regulation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1367-5931
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
300-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Nuclear histone acetylases and deacetylases and transcriptional regulation: HATs off to HDACs.
pubmed:affiliation
Howard Hughes Medical Institute, Harvard University Department of Chemistry, 12 Oxford Street, Cambridge, MA 02138, USA. hassig@slsiris harvard.edu.
pubmed:publicationType
Journal Article, Review