HSP90 and the chaperoning of cancer

被引：2007

作者：

Whitesell, L ^{[1
]}

Lindquist, SL

机构：

[1] Univ Arizona, Steele Mem Childrens Res Ctr, Tucson, AZ 85724 USA

[2] Whitehead Inst Biomed Res, Cambridge, MA 02142 USA

来源：

NATURE REVIEWS CANCER | 2005年 / 5卷 / 10期

关键词：

D O I：

10.1038/nrc1716

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

Standing watch over the proteome, molecular chaperones are an ancient and evolutionarily conserved class of proteins that guide the normal folding, intracellular disposition and proteolytic turnover of many of the key regulators of cell growth, differentiation and survival. This essential guardian function is subverted during oncogenesis to allow malignant transformation and to facilitate rapid somatic evolution. Pharmacologically 'bribing' the essential guard duty of the chaperone HSP90 (heat-shock protein of 90 kDa) seems to offer a unique anticancer strategy of considerable promise.

引用

页码：761 / 772

页数：12

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