Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2009-6-23
pubmed:abstractText
Modulation of chromatin structure has emerged as a critical molecular device to control gene expression. Histones undergo different post-translational modifications that increase chromatin accessibility to a number of regulatory factors. Among them, histone ubiquitination appears relevant in nuclear processes that govern gene silencing, either by inhibiting or activating transcription, and maintain genome stability, acting as scaffold to properly organize the DNA damage response. Thus, it is of paramount importance the identification and the characterization of new ubiquitin ligases that address histones.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-10804500, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-11007473, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-11395416, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-14993289, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-16462746, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-16499958, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-16633336, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-17034365, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-17355622, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-17525341, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-17525342, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-17552281, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-17914355, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-17940005, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-18001824, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-18001825, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-18006705, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-18082599, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-18206970, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-18344985, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-18374642, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-18471973, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-18483401, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-18724939, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-18832071, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-19203578, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-19203579, http://linkedlifedata.com/resource/pubmed/commentcorrection/19500350-19217402
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1471-2199
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
55
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
RNF168, a new RING finger, MIU-containing protein that modifies chromatin by ubiquitination of histones H2A and H2AX.
pubmed:affiliation
Department of DISCAFF and DFB Center, University of Piemonte Orientale A, Avogadro, Novara, Italy. sabrina.pinato@pharm.unipmn.it
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't