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Article

Proteome-wide identification of HSP70/HSC70 chaperone clients in human cells.

PLoS biology - 1 Jul 2020

Ryu Seung W, Stewart Rose, Pectol D Chase, Ender Nicolette A, Wimalarathne Oshadi, Lee Ji-Hoon, Zanini Carlos P, Harvey Antony, Huibregtse Jon M, Mueller Peter, Paull Tanya T

Abstract excerpt

The 70 kDa heat shock protein (HSP70) family of chaperones are the front line of protection from stress-induced misfolding and aggregation of polypeptides in most organisms and are responsible for promoting the stability, folding, and degradation of clients to maintain cellular protein homeostasis. Here, we demonstrate quantitative identification of HSP70 and 71 kDa heat shock cognate (HSC70) clients using a...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 32687490
DOI: 10.1371/journal.pbio.3000606
PMCID: PMC7392334

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