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Article

Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone.

The Journal of biological chemistry - 9 Apr 2010

Cremers Claudia M, Reichmann Dana, Hausmann Jens, Ilbert Marianne, Jakob Ursula

Abstract excerpt

Hsp33, a molecular chaperone specifically activated by oxidative stress conditions that lead to protein unfolding, protects cells against oxidative protein aggregation. Stress sensing in Hsp33 occurs via its C-terminal redox switch domain, which consists of a zinc center that responds to the pres...

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Share to Heat-Shock Proteins
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 20139072
DOI: 10.1074/jbc.M109.084350
PMCID: PMC2857002

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20139072-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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