Source:http://linkedlifedata.com/resource/pubmed/id/15219618
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2004-6-28
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1044-579X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
253-61
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:15219618-Animals,
pubmed-meshheading:15219618-Binding Sites,
pubmed-meshheading:15219618-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:15219618-Humans,
pubmed-meshheading:15219618-Neoplasms,
pubmed-meshheading:15219618-Protein Prenylation,
pubmed-meshheading:15219618-ras Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
Prenyl-binding domains: potential targets for Ras inhibitors and anti-cancer drugs.
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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
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Review,
Research Support, Non-U.S. Gov't
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