The unfolding story of a redox chaperone.
basic_science · Level V
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- Record sourced from PubMed, PMID 22385952.
- Also identified by DOI 10.1016/j.cell.2012.02.029.
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Abstract
Oxidative stress, especially in combination with heat stress, poses a life-threatening challenge to many organisms by causing protein misfolding and aggregation. In this issue, Reichmann et al. demonstrate how a destabilized linker region of the bacterial chaperone Hsp33 prevents aggregation of a denatured protein by stabilizing structural elements.