Linked Life Data

14593721

Source:http://linkedlifedata.com/resource/pubmed/id/14593721

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2003-11-3
pubmed:abstractText
It is becoming increasingly clear that reversible acetylation of proteins is a signal directly controlling the activity of key cellular regulators. The enzymes controlling protein acetylation were identified as histone acetyltransferases (HATs) and histone deacetylases (HDACs). Following the discovery of HATs and HDACs, a number of non-histone proteins have been identified as substrates for these enzymes. HDACs play important roles in transcriptional regulation and pathogenesis of cancer through removing acetyl groups from histones and other transcriptional regulators. HDAC inhibitors case cell cycle arrest, differentiation and/or apoptosis of many tumors, suggesting their usefulness for chemotherapy and differentiation therapy. Since recent studies have revealed that HDACs are structurally and functionally diverse, it should be possible to develop inhibitors specific to individual HDACs as more promising agents for cancer therapy.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1087-2957
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
269-78
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Protein deacetylases: enzymes with functional diversity as novel therapeutic targets.
pubmed:affiliation
Chemical Genetics Laboratory, RIKEN, Saitama, Japan.
pubmed:publicationType
Journal Article, Review