Source:http://linkedlifedata.com/resource/pubmed/id/16630806
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2006-4-24
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pubmed:abstractText |
Methylation marks on the lysine residues of histone proteins are thought to contribute to epigenetic phenomena in part because of their apparent irreversibility. Will this view change with the recent discovery of histone lysine demethylases that reversibly remove methyl marks?
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0092-8674
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
125
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
213-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16630806-Animals,
pubmed-meshheading:16630806-Chromatin,
pubmed-meshheading:16630806-Epigenesis, Genetic,
pubmed-meshheading:16630806-Histones,
pubmed-meshheading:16630806-Lysine,
pubmed-meshheading:16630806-Methylation,
pubmed-meshheading:16630806-Oxidoreductases, N-Demethylating
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pubmed:year |
2006
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pubmed:articleTitle |
Histone lysine demethylases and their impact on epigenetics.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Biochemistry, Division of Nucleic Acids Enzymology, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, NJ 08854, USA.
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pubmed:publicationType |
Journal Article
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