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Heat Shock Protein 90 and Role of Its Chemical Inhibitors in Treatment of Hematologic Malignancies

Division of Hematology and Oncology, Department of Medicine, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605, USA
Author to whom correspondence should be addressed.
Adam Li is currently a high school student at Xaverian Brothers High School, 800 Clapboardtree Street, Westwood, MA 02090, USA.
Pharmaceuticals 2012, 5(8), 779-801;
Received: 4 June 2012 / Revised: 9 July 2012 / Accepted: 16 July 2012 / Published: 25 July 2012
(This article belongs to the Special Issue Hsp90 Inhibitors)
Heat shock protein 90 (Hsp90) is a conserved and constitutively expressed molecular chaperone and it has been shown to stabilize oncoproteins and facilitate cancer development. Hsp90 has been considered as a therapeutic target for cancers and three classes of Hsp90 inhibitors have been developed: (1) benzoquinone ansamycin and its derivatives, (2) radicicol and its derivates, and (3) small synthetic inhibitors. The roles of these inhibitors in cancer treatment have been studied in laboratories and clinical trials, and some encouraging results have been obtained. Interestingly, targeting of Hsp90 has been shown to be effective in inhibition of cancer stem cells responsible for leukemia initiation and progression, providing a strategy for finding a cure. Because cancer stem cells are well defined in some human leukemias, we will focus on hematologic malignancies in this review. View Full-Text
Keywords: heat shock protein 90; chemical inhibitors; hematologic malignancies heat shock protein 90; chemical inhibitors; hematologic malignancies
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MDPI and ACS Style

Ho, N.; Li, A.; Li, S.; Zhang, H. Heat Shock Protein 90 and Role of Its Chemical Inhibitors in Treatment of Hematologic Malignancies. Pharmaceuticals 2012, 5, 779-801.

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