Comment
doi: 10.1016/j.cell.2012.02.029.
The unfolding story of a redox chaperone
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- PMID: 22385952
- DOI: 10.1016/j.cell.2012.02.029
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Comment
The unfolding story of a redox chaperone
Cell.
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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.
Copyright © 2012 Elsevier Inc. All rights reserved.
Comment on
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Order out of disorder: working cycle of an intrinsically unfolded chaperone.Cell. 2012 Mar 2;148(5):947-57. doi: 10.1016/j.cell.2012.01.045. Cell. 2012. PMID: 22385960 Free PMC article.
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