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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Main Authors: | Michael A. Serwetnyk (Author), Brian S.J. Blagg (Author) |
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Format: | Book |
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Elsevier,
2021-06-01T00:00:00Z.
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Online Access: | Connect to this object online. |
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