HSP90 and its inhibitors.
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.
Hao
Huifang
H
Department of Gastroenterological Surgery, Transplant and Surgical Oncology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Naomoto
Yoshio
Y
Bao
Xiaohong
X
Watanabe
Nobuyuki
N
Sakurama
Kazufumi
K
Noma
Kazuhiro
K
Motoki
Takayuki
T
Tomono
Yasuko
Y
Fukazawa
Takuya
T
Shirakawa
Yasuhiro
Y
Yamatsuji
Tomoki
T
Matsuoka
Junji
J
Takaoka
Munenori
M
D000970:Antineoplastic Agents / Q000494:pharmacology*; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors* / Q000378:metabolism; D006801:Humans; D009369:Neoplasms / Q000188:drug therapy* / Q000378:metabolism
D000970:Antineoplastic Agents; D018841:HSP90 Heat-Shock Proteins