Linked Life Data

14585352

Source:http://linkedlifedata.com/resource/pubmed/id/14585352

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-10-30
pubmed:abstractText
Ubiquitin-dependent proteolysis ensures that specific protein functions are turned off at the right time, in the right place, and in a unidirectional fashion. The high substrate specificity of the system is determined by a large family of ubiquitin ligases, which competes with the protein kinases to be the largest family of enzymes in mammals. Given the crucial function of the proteolytic machinery, altered degradation of cellular regulators contributes to the unchecked proliferation typical of cancer cells. Here we review the aberrant activity of a variety of ubiquitin ligases in human cancer, hence the prospect of targeting them in cancer therapy.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1535-6108
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
251-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
When protein destruction runs amok, malignancy is on the loose.
pubmed:affiliation
Department of Pathology and NYU Cancer Institute, MSB 599, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA. michele.pagano@med.nyu.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review