| Literature DB >> 11504487 |
Len Neckers1, Edward Mimnaugh, Theodor W. Schulte.
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.Entities:
Year: 1999 PMID: 11504487 DOI: 10.1054/drup.1999.0082
Source DB: PubMed Journal: Drug Resist Updat ISSN: 1368-7646 Impact factor: 18.500