HSP90 and its inhibitors (Review) | Zendy

Huifang Hao | Zendy; Yoshio Naomoto | Zendy; Xiaohong Bao | Zendy; Nobuyuki Watanabe | Zendy; Kazufumi Sakurama | Zendy; Kazuhiro Noma | Zendy; Takayuki Motoki | Zendy; Yasuko Tomono | Zendy; Takuya Fukazawa | Zendy; Yasuhiro Shirakawa | Zendy; Tomoki Yamatsuji | Zendy; Junji Matsuoka | Zendy; Munenori Takaoka | Zendy

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HSP90 and its inhibitors (Review)

Author(s) -

Huifang Hao,

Yoshio Naomoto,

Xiaohong Bao,

Nobuyuki Watanabe,

Kazufumi Sakurama,

Kazuhiro Noma,

Takayuki Motoki,

Yasuko Tomono,

Takuya Fukazawa,

Yasuhiro Shirakawa,

Tomoki Yamatsuji,

Junji Matsuoka,

Munenori Takaoka

Publication year - 2010

Publication title -

oncology reports

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.094

H-Index - 96

eISSN - 1791-2431

pISSN - 1021-335X

DOI - 10.3892/or_00000787

Subject(s) - hsp90 , biology , protein folding , chaperone (clinical) , microbiology and biotechnology , oncogene , atp hydrolysis , cell cycle , cell , biochemistry , heat shock protein , enzyme , gene , medicine , atpase , pathology

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.

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