摘要
背景和目的:Hsp90伴侣蛋白调节各种癌蛋白的折叠,成熟和稳定性。近年来,许多Hsp90抑制剂已经进入临床试验,而所有这些都靶向了具有相似结合能力和副作用的ATP酶,所以没有一种进入到市场。在调节进程期间,涉及许多蛋白质 - 蛋白质相互作用(PPI),如Hsp90和客户蛋白质或辅酶。随着Hsp90-伴侣蛋白PPI网络越来越清楚,许多癌蛋白被报道与Hsp90-伴侣PPI密切相关。其中,Hsp90-Cdc37 PPI已广泛报道与许多蛋白激酶相关联,使其成为治疗癌症的新靶点。 结果与结论:本文简要回顾了靶向Hsp90-Cdc37复合物的策略和调节剂,包括直接和间接调控机制。通过这些讨论,我们期待为新的见解提供灵感,以替代方法来抑制Hsp90伴侣功能。
关键词: Hsp90 / Cdc37,蛋白质 - 蛋白质相互作用,PPI抑制剂,靶向策略,蛋白激酶。
Current Drug Targets
Title:Targeting Hsp90-Cdc37: A Promising Therapeutic Strategy by Inhibiting Hsp90 Chaperone Function
Volume: 18 Issue: 13
关键词: Hsp90 / Cdc37,蛋白质 - 蛋白质相互作用,PPI抑制剂,靶向策略,蛋白激酶。
摘要: Background & Objective: The Hsp90 chaperone protein regulates the folding, maturation and stability of a wide variety of oncoproteins. In recent years, many Hsp90 inhibitors have entered into the clinical trials while all of them target ATPase showing similar binding capacity and kinds of side-effects so that none have reached to the market. During the regulation progress, numerous protein- protein interactions (PPI) such as Hsp90 and client proteins or cochaperones are involved. With the Hsp90-cochaperones PPI networks being more and more clear, many cancerous proteins have been reported to be tightly correlated to Hsp90-cochaperones PPI. Among them, Hsp90-Cdc37 PPI has been widely reported to associate with numerous protein kinases, making it a novel target for the treatment of cancers.
Results and Conclusion: In this paper, we briefly review the strategies and modulators targeting Hsp90-Cdc37 complex including direct and indirect regulation mechanism. Through these discussions we expect to present inspirations for new insights into an alternative way to inhibit Hsp90 chaperone function.Export Options
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Cite this article as:
Targeting Hsp90-Cdc37: A Promising Therapeutic Strategy by Inhibiting Hsp90 Chaperone Function, Current Drug Targets 2017; 18 (13) . https://dx.doi.org/10.2174/1389450117666160527125522
DOI https://dx.doi.org/10.2174/1389450117666160527125522 |
Print ISSN 1389-4501 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-5592 |
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