HSP90 and its inhibitors

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

doi:10.3892/or-00000787

HSP90 and its inhibitors

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

Research output: Contribution to journal › Review article › peer-review

30 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	1483-1492
Number of pages	10
Journal	Oncology reports
Volume	23
Issue number	6
DOIs	https://doi.org/10.3892/or-00000787
Publication status	Published - Jun 2010

Keywords

Chaperone
Heat shock protein 90
Inhibitors

ASJC Scopus subject areas

Oncology
Cancer Research

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.3892/or-00000787

Cite this

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title = "HSP90 and its inhibitors",

abstract = "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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doi = "10.3892/or-00000787",

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T1 - HSP90 and its inhibitors

AU - Hao, Huifang

AU - Naomoto, Yoshio

AU - Bao, Xiaohong

AU - Watanabe, Nobuyuki

AU - Sakurama, Kazufumi

AU - Noma, Kazuhiro

AU - Motoki, Takayuki

AU - Tomono, Yasuko

AU - Fukazawa, Takuya

AU - Shirakawa, Yasuhiro

AU - Yamatsuji, Tomoki

AU - Matsuoka, Junji

AU - Takaoka, Munenori

PY - 2010/6

Y1 - 2010/6

N2 - 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.

AB - 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.

KW - Chaperone

KW - Heat shock protein 90

KW - Inhibitors

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M3 - Review article

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VL - 23

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EP - 1492

JO - Oncology Reports

JF - Oncology Reports

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ER -

HSP90 and its inhibitors

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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