Linked Life Data

16175177

Source:http://linkedlifedata.com/resource/pubmed/id/16175177

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2005-9-30
pubmed:abstractText
Standing watch over the proteome, molecular chaperones are an ancient and evolutionarily conserved class of proteins that guide the normal folding, intracellular disposition and proteolytic turnover of many of the key regulators of cell growth, differentiation and survival. This essential guardian function is subverted during oncogenesis to allow malignant transformation and to facilitate rapid somatic evolution. Pharmacologically 'bribing' the essential guard duty of the chaperone HSP90 (heat-shock protein of 90 kDa) seems to offer a unique anticancer strategy of considerable promise.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1474-175X
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
761-72
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
HSP90 and the chaperoning of cancer.
pubmed:affiliation
Steele Memorial Children's Research Center, University of Arizona, Tucson, Arizona 85724, USA. Whitesell@wi.mit.edu
pubmed:publicationType
Journal Article, Review