Abstract
Heat shock protein 90 is one of the most abundant cellular proteins. Although its functions are still being characterized, it appears to serve as a chaperone for a growing list of cell signaling proteins, including many tyrosine and serine/threonine kinases, involved in cell proliferation and/or survival. The recent discovery of natural products which are able to inhibit Hsp90 function have allowed for both identification of its client proteins and for a better understanding of its role in their activity. Accumulating data have suggested that targeting Hsp90 in cancer cells may be of clinical benefit. Copyright 1999 Harcourt Publishers Ltd.
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