Linked Life Data

19571682

Source:http://linkedlifedata.com/resource/pubmed/id/19571682

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2009-9-8
pubmed:abstractText
Residue and degree-specific methylation of histone lysines along with other epigenetic modifications organizes chromatin into distinct domains and regulates almost every aspect of DNA metabolism. Identification of histone methyltransferases and demethylases, as well as proteins that recognize methylated lysines, has clarified the role of each methylation event in regulating different biological pathways. Methylation of histone H4 lysine 20 (H4K20me) plays critical roles in diverse cellular processes such as gene expression, cell cycle progression and DNA damage repair, with each of the three degrees of methylation (mono-, di- and tri-methylation) making a unique contribution. Here we discuss recent studies of H4K20me that have greatly improved our understanding of the regulation and function of this fascinating histone modification.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1559-2308
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
273-6
pubmed:dateRevised
2010-8-6
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Degrees make all the difference: the multifunctionality of histone H4 lysine 20 methylation.
pubmed:affiliation
Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural