Article ID Journal Published Year Pages File Type
2474882 Acta Pharmaceutica Sinica B 2012 8 Pages PDF
Abstract

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.

Graphical abstractThis review briefly discusses the molecular structure and biological function of Hsp90, and focuses 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.Figure optionsDownload full-size imageDownload as PowerPoint slide

Related Topics
Health Sciences Pharmacology, Toxicology and Pharmaceutical Science Drug Discovery
Authors
, , , , , , ,