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Heat shock protein 90 has emerged as an important target in several diseases. The present review will discuss our understanding of the role played by Hsp90 in regulating and maintaining the transformed phenotype in cancers and neurodegenerative diseases, as well as recent findings on its roles in fungal and viral infections. It will also update the reader on the preclinical development and clinical...
The molecular chaperone Hsp90 has emerged as an important target in cancer treatment because of its roles in maintaining transformation and regulating the function of proteins involved in apoptotic, survival and growth pathways. Many Hsp90 inhibitors function by binding to the N-terminal ATP pocket, but the chaperone has many other vulnerable points. Agents that interact with its C-terminus or modify...
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