The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70

Abstract In human cells under stress conditions, misfolded polypeptides can form potentially cytotoxic insoluble aggregates. To eliminate aggregates, the HSP70 chaperone machinery extracts and resolubilizes polypeptides for triage to refolding or degradation. Yeast and bacterial chaperones of the sm...

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Bibliographic Details
Main Authors: Conrado C. Gonçalves, Itai Sharon, T. Martin Schmeing, Carlos H. I. Ramos, Jason C. Young
Format: article
Language:EN
Published: Nature Portfolio 2021
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Q
Online Access:https://doaj.org/article/da3504a65e704da49d5323a9fb4e6586
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