Tumor selectivity of Hsp90 inhibitors: the explanation remains elusive.

ACS chemical biology ·Vol. 1 ·No. 5 ·2006-06-20 ·Pages 279-84

Chiosis G, Neckers L

Abstract

Two recent papers attempt to solve both the tumor selectivity and the in vivo tumor accumulation profiles seen with some Hsp90 inhibitors. They spotlight the higher affinity of ansamycins' hydroquinone over the quinone form for Hsp90 and further discuss its possible contribution to ansamycins' tumor selectivity.

MeSH Terms

Animals Antineoplastic Agents/administration & dosage,classification,pharmacology HSP90 Heat-Shock Proteins/antagonists & inhibitors,physiology Humans Neoplasms/drug therapy,metabolism,pathology

Chemicals

Antineoplastic Agents HSP90 Heat-Shock Proteins

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Chiosis Gabriela

Department of Medicine and Program in Molecular Pharmacology and Chemistry, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, New York 10021, USA.

Neckers Len

Article Info

Journal

ACS chemical biology

Abbr.

ACS Chem Biol

ISSN

1554-8937

DOI

10.1021/cb600224w

Published

2006-06-20

Pages

279-84

Language

English

Region

United States

NLM ID

101282906

Subset

External Links

PubMed source DOI: 10.1021/cb600224w View journal details

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Tumor selectivity of Hsp90 inhibitors: the explanation remains elusive.

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