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Original paper

Design of Disruptors of the Hsp90–Cdc37 Interface

Volume: 25, Issue: 2, Pages: 360 - 360
Published: Jan 15, 2020
Abstract
The molecular chaperone Hsp90 is a ubiquitous ATPase-directed protein responsible for the activation and structural stabilization of a large clientele of proteins. As such, Hsp90 has emerged as a suitable candidate for the treatment of a diverse set of diseases, such as cancer and neurodegeneration. The inhibition of the chaperone through ATP-competitive inhibitors, however, was shown to lead to undesirable side effects. One strategy to...
Paper Details
Title
Design of Disruptors of the Hsp90–Cdc37 Interface
Published Date
Jan 15, 2020
Journal
Volume
25
Issue
2
Pages
360 - 360
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