Protein prenylation: from discovery to prospects for cancer treatment

被引：75

作者：

Gelb, MH

Scholten, JD

Sebolt-Leopold, JS

机构：

[1] Univ Washington, Dept Chem, Seattle, WA 98195 USA

[2] Univ Washington, Dept Biochem, Seattle, WA 98195 USA

[3] Warner Lambert Co, Parke Davis Pharmaceut Res Div, Dept Biochem, Ann Arbor, MI 48105 USA

[4] Warner Lambert Co, Parke Davis Pharmaceut Res Div, Dept Cell Biol, Ann Arbor, MI 48105 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 1998年 / 2卷 / 01期

关键词：

D O I：

10.1016/S1367-5931(98)80034-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A specific set of proteins in eukaryotic cells contain covalently attached carboxy-terminal prenyl groups (15-carbon farnesyl and 20-carbon geranylgeranyl). Many of them are signaling proteins including Ras, heterotrimeric G proteins and Rab proteins. The protein prenyltransferases which attach prenyl groups to proteins have been well characterized, and an X-ray structure is available for protein farnesyltransferase. Inhibitors of protein farnesyltransferase are showing sufficient promise in preclinical trials as anti-cancer drugs to warrant widespread interest in the pharmaceutical industry.

引用

页码：40 / 48

页数：9

共 95 条

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