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Article

Client processing is altered by novel myopathy-causing mutations in the HSP40 J domain.

PloS one - 1 Jan 2020

Pullen Melanie Y, Weihl Conrad C, True Heather L

Abstract excerpt

The misfolding and aggregation of proteins is often implicated in the development and progression of degenerative diseases. Heat shock proteins (HSPs), such as the ubiquitously expressed Type II Hsp40 molecular chaperone, DNAJB6, assist in protein folding and disaggregation. Historically, mutations within the DNAJB6 G/F domain have been associated with Limb-Girdle Muscular Dystrophy type 1D, now referred to as...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 32497100
DOI: 10.1371/journal.pone.0234207
PMCID: PMC7272046

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