Source:http://linkedlifedata.com/resource/pubmed/id/16261189
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2005-11-1
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pubmed:abstractText |
Covalent modifications of histone tails have fundamental roles in chromatin structure and function. One such modification, lysine methylation, has important functions in many biological processes that include heterochromatin formation, X-chromosome inactivation and transcriptional regulation. Here, we summarize recent advances in our understanding of how lysine methylation functions in these diverse biological processes, and raise questions that need to be addressed in the future.
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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 |
Nov
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pubmed:issn |
1471-0072
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
838-49
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:16261189-Animals,
pubmed-meshheading:16261189-Gene Silencing,
pubmed-meshheading:16261189-Heterochromatin,
pubmed-meshheading:16261189-Histone-Lysine N-Methyltransferase,
pubmed-meshheading:16261189-Histones,
pubmed-meshheading:16261189-Lysine,
pubmed-meshheading:16261189-Methylation,
pubmed-meshheading:16261189-Transcription, Genetic,
pubmed-meshheading:16261189-Transcriptional Activation
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pubmed:year |
2005
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pubmed:articleTitle |
The diverse functions of histone lysine methylation.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Biochemistry & Biophysics, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, North Carolina 27599-7295, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, N.I.H., Extramural
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