Abstract
Mutated ras genes are implicated in 20-30% of all human tumors, including 50% of colon, 30% of lung and 90% of pancreatic cancer [1,2]. The Ras protein is initially synthesized as an inactive cytosolic precursor that requires a series of posttranslational modifications in order to associate to the cell membrane and perform its normal and oncogenic functions. The key step in these modifications is farnesylation of a cysteine residue in the C-terminal motif of the Ras protein. Since this prenylation is catalyzed by farnesyl-protein transferase (FTase), inhibition of FTase should indirectly regulate oncogenic ras function. Therefore, inhibitors of FTase represent potential anticancer agents.
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