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Updated: Aug 30, 2026
06:51
Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
Published on: July 21, 2021
Synthesis of novel fluorescent probes for the molecular chaperone Hsp90
Laura Llauger-Bufi1, Sara J Felts, Henri Huezo
1Program in Cell Biology and Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
Bioorganic & Medicinal Chemistry Letters
|November 1, 2003
Abstract:
Heat shock protein 90 (Hsp90) is a molecular chaperone necessary for maintaining oncogenic transformation. There is substantial interest in developing novel agents that bind to the N-terminal of the chaperone. Here we report the synthesis and characterization of two fluorescent Hsp90 inhibitors and probe their use in an Hsp90 fluorescent polarization assay.
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