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- W2275101314 abstract "Mutation of ras protein is involved in 30% of human cancers. This protein is synthesized in the cytosol and localized to the membrane after farnesylation of Cys at the C-terminal tetrapeptide CAAX. This prenylation is catalyzed by farnesyltransferase (FTase). Therefore, an inhibitor of this enzyme can block cell transforming activity and act as a potential anticancer agent. A tetrapeptide, Cys-Val-Phe-Met-OH, has been identified to inhibit FTase. Moreover, two conformational models for bioactivity of the tetrapeptide turn and extended structure) have been suggested. During the last 3 or 4 years, we have refined these models and have designed peptidomimetic inhibitors. Among these efforts, this paper focuses on the design of a hydantoin based inhibitor series." @default.
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- W2275101314 date "2006-05-16" @default.
- W2275101314 modified "2023-09-22" @default.
- W2275101314 title "Design of peptidomimetic farnesyltransferase inhibitors as anticancer agents" @default.
- W2275101314 doi "https://doi.org/10.1007/0-306-46881-6_183" @default.
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