Chiosis Gabriela, Vilenchik Maria, Kim Joungnam, Solit David
Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
Drug Discov Today. 2004 Oct 15;9(20):881-8. doi: 10.1016/S1359-6446(04)03245-3.
The molecular chaperone Hsp90 has emerged as an important target in cancer treatment because of its roles in maintaining transformation and regulating the function of proteins involved in apoptotic, survival and growth pathways. Many Hsp90 inhibitors function by binding to the N-terminal ATP pocket, but the chaperone has many other vulnerable points. Agents that interact with its C-terminus or modify its post-translational status represent additional ways of interfering with chaperone activity. This review will discuss several emerging classes of Hsp90 inhibitors and their modes of action.
分子伴侣热休克蛋白90（Hsp90）已成为癌症治疗中的一个重要靶点，因为它在维持细胞转化以及调节参与凋亡、生存和生长途径的蛋白质功能方面发挥作用。许多Hsp90抑制剂通过与N端ATP口袋结合发挥作用，但该分子伴侣还有许多其他易受影响的位点。与它的C端相互作用或改变其翻译后状态的药物代表了干扰分子伴侣活性的其他方式。本综述将讨论几类新兴的Hsp90抑制剂及其作用模式。
