High-throughput assay for the identification of Hsp90 inhibitors based on Hsp90-dependent refolding of firefly luciferase
- 4 January 2007
- journal article
- Published by Elsevier in Bioorganic & Medicinal Chemistry
- Vol. 15 (5) , 1939-1946
- https://doi.org/10.1016/j.bmc.2007.01.004
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- High-throughput screening for Hsp90 ATPase inhibitorsBioorganic & Medicinal Chemistry Letters, 2006
- 4-Amino derivatives of the Hsp90 inhibitor CCT018159Bioorganic & Medicinal Chemistry Letters, 2006
- Geldanamycin Induces Heat Shock Protein 70 and Protects against MPTP-induced Dopaminergic Neurotoxicity in MiceJournal of Biological Chemistry, 2005
- 3-(5-chloro-2,4-dihydroxyphenyl)-Pyrazole-4-carboxamides as inhibitors of the Hsp90 molecular chaperoneBioorganic & Medicinal Chemistry Letters, 2005
- Dissection of the Contribution of Individual Domains to the ATPase Mechanism of Hsp90Journal of Biological Chemistry, 2003
- A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitorsNature, 2003
- The Heat Shock Protein 90 Antagonist Novobiocin Interacts with a Previously Unrecognized ATP-binding Domain in the Carboxyl Terminus of the ChaperoneJournal of Biological Chemistry, 2000
- Hop Modulates hsp70/hsp90 Interactions in Protein FoldingJournal of Biological Chemistry, 1998
- Cooperative Action of Hsp70, Hsp90, and DnaJ Proteins in Protein RenaturationBiochemistry, 1996
- Effect of Geldanamycin on the Kinetics of Chaperone-Mediated Renaturation of Firefly Luciferase in Rabbit Reticulocyte LysateBiochemistry, 1996