摘要
热休克蛋白90作为分子伴侣在调节细胞生长、分化、凋亡等方面发挥重要的作用,逐渐成为肿瘤治疗的重要靶点。许多H sp90抑制剂作用于H sp90N-端ATP结合域,此外H sp90还有许多易被攻击的位点,如本文所阐述的作用于H sp90-端的抑制剂及翻译后H sp90修饰的抑制剂。
The molecular chaperone heat shock protein 90 （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 al：optotic, survival and growth pathways. Many Hsp90 inhibitors function by binding to the N-terminal ATP-binding domain, but the chaperone has many other vulnerable points. This review will discuss several emerging classes of Hsp90 inhibitors including agents that interact with its C-terminus or modify its post-translational status.
出处
《海峡药学》
2005年第6期1-5,共5页
Strait Pharmaceutical Journal
