New approaches to anticancer drug design based on the inhibition of farnesyltransferase

Saïd M. Sebti, Andrew Hamilton

Research output: Contribution to journalArticle

Abstract

Mutated forms of the GTP-binding protein Ras are found in 30% of human cancers, with particularly high prevalence in colon and pancreatic carcinomas. Ras function in growth factor signaling requires post- translational farnesylation of a cysteine residue present as part of the CA1A2X carboxyl terminal tetrapeptide. The enzyme farnesyltransferase has become an important target for the design of potential new antitumor agents. The authors outline the major new approaches to inhibition of farnesyltransferase and describe how certain peptidomimetics have been shown to block oncogenic signaling and tumor growth in various animal models.

Original languageEnglish (US)
Pages (from-to)26-33
Number of pages8
JournalDrug Discovery Today
Volume3
Issue number1
DOIs
StatePublished - 1998

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Farnesyltranstransferase
Drug Design
Peptidomimetics
Prenylation
GTP-Binding Proteins
Antineoplastic Agents
Cysteine
Neoplasms
Intercellular Signaling Peptides and Proteins
Colon
Animal Models
Enzymes
Growth
Pancreatic Carcinoma

ASJC Scopus subject areas

  • Drug Discovery
  • Pharmacology

Cite this

New approaches to anticancer drug design based on the inhibition of farnesyltransferase. / Sebti, Saïd M.; Hamilton, Andrew.

In: Drug Discovery Today, Vol. 3, No. 1, 1998, p. 26-33.

Research output: Contribution to journalArticle

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