A yeast-based genomic strategy highlights the cell protein networks altered by FTase inhibitor peptidomimetics.

ABSTRACT:

Background

Farnesyltransferase inhibitors (FTIs) are anticancer agents developed to inhibit Ras oncoprotein activities. FTIs of different chemical structure act via a conserved mechanism in eukaryotic cells. They have low toxicity and are active on a wide range of tumors in cellular and animal models, independently of the Ras activation state. Their ultimate mechanism of action, however, remains undetermined. FTase has hundred of substrates in human cells, many of which play a pivotal role in either tumorigenesis or in pro-survival pathways. This lack of knowledge probably accounts for the failure of FTIs at clinical stage III for most of the malignancies treated, with the notable exception of haematological malignancies. Understanding which cellular pathways are the ultimate targe

SUBMITTER: Porcu G 

PROVIDER: S-EPMC2925370 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature