Hsp90 inhibition: Elimination of shock and stress

Adam S. Duerfeldt, Brian S.J. Blagg

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

The 90 kDa heat shock proteins (Hsp90) represent a class of molecular chaperones responsible for the maturation and stabilization of many oncogenic proteins. Disrupting the ability of ATP to bind and facilitate the operation of Hsp90 has emerged as a promising approach toward cancer chemotherapeutic development. While numerous Hsp90 inhibitory scaffolds have been identified, progress through the clinic has revealed many obstacles that should be addressed in future analogue development. Recent reports of the complications, pitfalls, and downstream effects associated with Hsp90 inhibition are discussed herein, in hopes of providing a reference that can be used to guide the future design of Hsp90 inhibitory scaffolds.

Original languageEnglish (US)
Pages (from-to)4983-4987
Number of pages5
JournalBioorganic and Medicinal Chemistry Letters
Volume20
Issue number17
DOIs
StatePublished - Sep 1 2010
Externally publishedYes

Bibliographical note

Funding Information:
The authors thank the NIH/NCI CA109265, The Madison and Lila Self Graduate Fellowship (A.S.D.), and The American Foundation for Pharmaceutical Education Pre-doctoral Fellowship (A.S.D.) for financial support.

Keywords

  • Anti-cancer
  • Hsp90
  • Resistance

Fingerprint Dive into the research topics of 'Hsp90 inhibition: Elimination of shock and stress'. Together they form a unique fingerprint.

Cite this