Hsp90 inhibition: Elimination of shock and stress

Adam S. Duerfeldt; Brian S.J. Blagg

doi:10.1016/j.bmcl.2010.06.108

Hsp90 inhibition: Elimination of shock and stress

Adam S. Duerfeldt, Brian S.J. Blagg

Research output: Contribution to journal › Article › peer-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 language	English (US)
Pages (from-to)	4983-4987
Number of pages	5
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	20
Issue number	17
DOIs	https://doi.org/10.1016/j.bmcl.2010.06.108
State	Published - Sep 1 2010
Externally published	Yes

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

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.bmcl.2010.06.108

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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.",

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AU - Blagg, Brian S.J.

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AB - 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.

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KW - Hsp90

KW - Resistance

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Hsp90 inhibition: Elimination of shock and stress

Abstract

Bibliographical note

Keywords

UN SDGs

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