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ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation

ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_bbe3b18cb62b4560996ac9f25bb15fdb

ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation

About this item

Full title

ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2016-10, Vol.7 (1), p.12882-12882, Article 12882

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Heat shock protein (Hsp)70 is a molecular chaperone that maintains protein homoeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. However, the mechanisms by which Hsp70 balances these opposing functions under stress conditions remain unknown. Here, we demonstrate that Hsp70 preferentially facilitates...

Alternative Titles

Full title

ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_bbe3b18cb62b4560996ac9f25bb15fdb

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_bbe3b18cb62b4560996ac9f25bb15fdb

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms12882

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