Unfolding of Metastable Linker Region Is at the Core of Hsp33 Activation as a Redox-regulated Chaperone

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 presenc...

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Bibliografiske detaljer
Main Authors: Cremers, Claudia M., Reichmann, Dana, Hausmann, Jens, Ilbert, Marianne, Jakob, Ursula
Format: Artigo
Sprog:Inglês
Udgivet: American Society for Biochemistry and Molecular Biology 2010
Fag:
Protein Structure and Folding
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2857002/
https://ncbi.nlm.nih.gov/pubmed/20139072
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.084350
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