Linked Life Data

12648672

Source:http://linkedlifedata.com/resource/pubmed/id/12648672

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-3-21
pubmed:abstractText
The p53 tumor suppressor exerts anti-proliferative effects, including growth arrest, apoptosis and cell senescence, in response to various types of stress. Tight regulation of p53 activation is imperative for preventing tumorigenesis and maintaining normal cell growth; p53 stabilization and transcriptional activation are crucial early events in a cell's battle against genotoxic stress. Ubiquitination, phosphorylation and acetylation are post-translational modifications to p53 that affect its overall appearance and activity. Recent findings suggest that these modifications have a profound affect on p53 stability and function. Defining the precise roles of these modifications in p53 function may show not only that they are markers of the stress response but also that they serve as the focal point in the regulation of p53.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0955-0674
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
164-71
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation.
pubmed:affiliation
Institute for Cancer Genetics and Department of Pathology College of Physicians and Surgeons, Columbia University, 1150 St. Nicholas Avenue, New York, NY 10032, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't