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Biofactors ; 6(3): 359-66, 1997.
Article in English | MEDLINE | ID: mdl-9288406

ABSTRACT

Ras, a signal-transducing protein involved in mediating growth factor-stimulated proliferation, is mutationally activated in over 30% of human tumors. To be functional Ras must bind to the inner surface of the plasma membrane, with post-translational lipid modifications being necessary for this localization. The essential, first modification of Ras is farnesylation catalyzed by the enzyme farnesyl: proteintransferase (FPTase). Inhibitors of FPTase (FTIs) are currently being tested to determine if they are capable of tumor growth inhibition. Here we describe our efforts, along with those of other groups, in testing the biological and biochemical effects of FTIs.


Subject(s)
Alkyl and Aryl Transferases , Antineoplastic Agents/therapeutic use , Enzyme Inhibitors/therapeutic use , Neoplasms/drug therapy , Transferases/antagonists & inhibitors , Animals , Genes, ras , Humans , Neoplasms/pathology , Protein Prenylation , Transferases/chemistry , Transferases/metabolism , Tumor Cells, Cultured , ras Proteins/metabolism
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