Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2004-6-28
pubmed:abstractText
Ras and Rho GTPases are prominent participants in malignant transformation. They possess an essential prenyl group (farnesyl or geranylgeranyl) that endows them with membrane-tethering ability and functional specificity. Accumulating evidence suggests that prenyl groups are involved primarily in lipid-protein interactions, and recent experiments point to prenyl-binding hydrophobic pockets in proteins regulating Ras and Rho in normal cells and cancer cells. This review presents the evidence for such prenyl-binding domains as significant players in the control of Ras-like GTPases, and the emerging concept of prenyl-binding domains as potential targets for Ras inhibitors and anti-cancer drugs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1044-579X
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
253-61
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Prenyl-binding domains: potential targets for Ras inhibitors and anti-cancer drugs.
pubmed:affiliation
Department of Neurobiochemistry, The George S. Wise Faculty of Life Sciences, Tel-Aviv University, 69978 Tel-Aviv, Israel. yoelk@taunex.tau.ac.il
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Review, Research Support, Non-U.S. Gov't