Discovery and development of natural heat shock protein 90 inhibitors in cancer treatment

Discovery and development of natural heat shock protein 90 inhibitors in cancer treatment

Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that plays a vital role in the signal transduction of cancers. Hsp90 inhibitors are able to inhibit Hsp90 or the complex of Hsp90 and co-chaperones resulting in the degradation of Hsp90-dependent client proteins through the ubiq...

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Bibliografiske detaljer
Main Authors: Yong Li, Dongmei Zhang, Jun Xu, Junmin Shi, Lei Jiang, Nan Yao, Wencai Ye
Format: Article
Sprog:English
Udgivet: Elsevier 2012-06-01
Serier:Acta Pharmaceutica Sinica B
Fag:
Heat shock protein 90 (Hsp90)
Tumor
Hsp90 inhibitors
Geldanamycin
Online adgang:http://www.sciencedirect.com/science/article/pii/S2211383512000639
Beskrivelse
Summary:Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that plays a vital role in the signal transduction of cancers. Hsp90 inhibitors are able to inhibit Hsp90 or the complex of Hsp90 and co-chaperones resulting in the degradation of Hsp90-dependent client proteins through the ubiquitination-proteasome pathway, thereby leading to the growth inhibition of tumor cells. This review will briefly discuss the molecular structure and biological function of Hsp90, and focus on a summary of recent progress in the development and testing of natural Hsp90 inhibitors and their different means by which they interact with Hsp90.
ISSN:2211-3835
2211-3843

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