Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-1-30
pubmed:abstractText
Since the identification of the first histone deacetylase (Taunton et al., Science 272, 408-411), several new members have been isolated. They can loosely be separated into entities on the basis of their similarity to various yeast histone deacetylases. The first class is represented by its closeness to the yeast Rpd3-like proteins, and the second most recently discovered class has similarities to yeast Hda1-like proteins. However, due to the fact that several different research groups isolated the Hda1-like histone deacetylases independently, there have been various different nomenclatures used to describe the various members, which can lead to confusion in the interpretation of this family's functions and interactions. With the discovery of another novel murine histone deacetylase, homologous to yeast Sir2, the number of members of this family is set to increase, as 7 human homologues of this gene have been isolated. In the light of these recent discoveries, we have examined the literature data and conducted a database analysis of the isolated histone deacetylases and potential candidates. The results obtained suggest that the number of histone deacetylases within the human genome may be as high as 17 and are discussed in relation to their homology to the yeast histone deacetylases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases, http://linkedlifedata.com/resource/pubmed/chemical/RPD3 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/SIR2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/SIRT1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Silent Information Regulator..., http://linkedlifedata.com/resource/pubmed/chemical/Sirtuin 1, http://linkedlifedata.com/resource/pubmed/chemical/Sirtuin 2, http://linkedlifedata.com/resource/pubmed/chemical/Sirtuins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-4827
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
75-83
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11139331-Amino Acid Sequence, pubmed-meshheading:11139331-Animals, pubmed-meshheading:11139331-Computational Biology, pubmed-meshheading:11139331-Databases, Factual, pubmed-meshheading:11139331-Histone Deacetylases, pubmed-meshheading:11139331-Humans, pubmed-meshheading:11139331-Mice, pubmed-meshheading:11139331-Molecular Sequence Data, pubmed-meshheading:11139331-Multigene Family, pubmed-meshheading:11139331-Saccharomyces cerevisiae, pubmed-meshheading:11139331-Saccharomyces cerevisiae Proteins, pubmed-meshheading:11139331-Sequence Homology, Amino Acid, pubmed-meshheading:11139331-Silent Information Regulator Proteins, Saccharomyces..., pubmed-meshheading:11139331-Sirtuin 1, pubmed-meshheading:11139331-Sirtuin 2, pubmed-meshheading:11139331-Sirtuins, pubmed-meshheading:11139331-Terminology as Topic, pubmed-meshheading:11139331-Trans-Activators, pubmed-meshheading:11139331-Transcription Factors
pubmed:year
2001
pubmed:articleTitle
The human histone deacetylase family.
pubmed:affiliation
Laboratory for Molecular Development and Tumor Biology, Centre for Molecular Medicine (CMM), Stockholm, S-171 76, Sweden. Steven.Gray@vai.org
pubmed:publicationType
Journal Article, Review