High-Throughput Screen of Natural Product Libraries for Hsp90 Inhibitors-Reference-Cited by-同舟云学术

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High-Throughput Screen of Natural Product Libraries for Hsp90 Inhibitors

Published:2014-02-10 Issue:1 Volume:3 Page:101-138
ISSN:2079-7737
Container-title:Biology
language:en
Short-container-title:Biology

Author:

Davenport Jason,Balch Maurie,Galam Lakshmi,Girgis Antwan,Hall Jessica,Blagg Brian,Matts Robert

Publisher

MDPI AG

Subject

General Agricultural and Biological Sciences,General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology

Link

http://www.mdpi.com/2079-7737/3/1/101/pdf

Reference200 articles.

1. Inhibition of heat shock protein hsp90-pp60v-Src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation;Whitesell;Proc. Natl. Acad. Sci. USA,1994

2. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation;Grenert;J. Biol. Chem.,1997

3. Targeting of the protein chaperone, Hsp90, by the transformation suppressing agent, radicicol;Sharma;Oncogene,1998

4. Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin

5. Structural Basis for Inhibition of the Hsp90 Molecular Chaperone by the Antitumor Antibiotics Radicicol and Geldanamycin

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