HSP90 and its inhibitors

被引：29

作者：

Hao, Huifang ^{[1
]}

Naomoto, Yoshio ^{[1
]}

Bao, Xiaohong ^{[1
]}

Watanabe, Nobuyuki ^{[1
]}

Sakurama, Kazufumi ^{[1
]}

Noma, Kazuhiro ^{[1
]}

Motoki, Takayuki ^{[1
]}

Tomono, Yasuko ^{[2
]}

Fukazawa, Takuya ^{[1
]}

Shirakawa, Yasuhiro ^{[1
]}

Yamatsuji, Tomoki ^{[1
]}

Matsuoka, Junji ^{[1
]}

Takaoka, Munenori ^{[1
]}

机构：

[1] Okayama Univ, Grad Sch Med Dent & Pharmaceut Sci, Dept Gastroenterol Surg Transplant & Surg Oncol, Okayama 7008558, Japan

[2] Shigei Med Res Inst, Okayama, Japan

来源：

ONCOLOGY REPORTS | 2010年 / 23卷 / 06期

关键词：

heat shock protein 90; chaperone; inhibitors; HEAT-SHOCK PROTEINS; N-TERMINAL DOMAIN; IMPORTANT BIOLOGIC ACTIVITIES; MOLECULAR CHAPERONE HSP90; ESCHERICHIA-COLI HSP90; PHASE-II TRIAL; ATP-BINDING; IN-VIVO; CRYSTAL-STRUCTURE; DNA GYRASE;

D O I：

10.3892/or_00000787

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

The HSP90 molecular chaperone family is highly conserved and expressed in various organisms ranging from prokaryotes to eukaryotes. HSP90 proteins play essential housekeeping functions, such as controlling the activity, turnover and trafficking of various proteins, promoting cell survival through maintaining the structural and functional integrity of some client proteins which control cell survival, proliferation and apoptosis, and play an important role in the progression of malignant disease. HSP90 proteins are ATP-dependent chaperones and the binding and hydrolysis of ATP are coupled to conformation changes of HSP90, which facilitate client protein folding and maturation. Many natural and synthetic molecular compounds have been proposed as promising cancer therapy via disrupting the formation of complex ATP-HSP90-client proteins.

引用

页码：1483 / 1492

页数：10

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