Targeting the dynamic HSP90 complex in cancer

被引：1250

作者：

Trepel, Jane ^{[2
]}

Mollapour, Mehdi ^{[1
]}

Giaccone, Giuseppe

Neckers, Len ^{[1
,2
]}

机构：

[1] NCI, Urol Oncol Branch, Ctr Canc Res, Bethesda, MD 20892 USA

[2] NCI, Med Oncol Branch, Bethesda, MD 20892 USA

来源：

NATURE REVIEWS CANCER | 2010年 / 10卷 / 08期

关键词：

HEAT-SHOCK-PROTEIN; PHASE-II TRIAL; MOLECULAR CHAPERONE; BCR-ABL; THERAPEUTIC TARGET; CELL RECOGNITION; STRUCTURAL BASIS; ATPASE ACTIVITY; IN-VITRO; B-RAF;

D O I：

10.1038/nrc2887

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

The molecular chaperone heat shock protein 90 (HSP90) has been used by cancer cells to facilitate the function of numerous oncoproteins, and it can be argued that cancer cells are 'addicted' to HSP90. However, although recent reports of the early clinical efficacy of HSP90 inhibitors are encouraging, the optimal use of HSP90-targeted therapeutics will depend on understanding the complexity of HSP90 regulation and the degree to which HSP90 participates in both neoplastic and normal cellular physiology.

引用

页码：537 / 549

页数：13

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