Hsp90 as an anti-cancer target

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 sur...

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Veröffentlicht in:Drug resistance updates 1999-06, Vol.2 (3), p.165-172
Hauptverfasser: Neckers, Len, Mimnaugh, Edward, Schulte, Theodor W
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:1368-7646
1532-2084
DOI:10.1054/drup.1999.0082