The disruption of protein−protein interactions with co-chaperones and client substrates as a strategy towards Hsp90 inhibition

The disruption of protein−protein interactions with co-chaperones and client substrates as a strategy towards Hsp90 inhibition

The 90-kiloDalton (kD) heat shock protein (Hsp90) is a ubiquitous, ATP-dependent molecular chaperone whose primary function is to ensure the proper folding of several hundred client protein substrates. Because many of these clients are overexpressed or become mutated during cancer progression, Hsp90...

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Bibliographic Details
Main Authors: Michael A. Serwetnyk, Brian S.J. Blagg
Format: Article
Language:English
Published: Elsevier 2021-06-01
Series:Acta Pharmaceutica Sinica B
Subjects:
Hsp90
Protein−protein interactions
Disruptors
Natural products
Small molecules
Peptidomimetics
Online Access:http://www.sciencedirect.com/science/article/pii/S2211383520308054

Internet

http://www.sciencedirect.com/science/article/pii/S2211383520308054

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