Open AccessThe Unfolding Story of a Redox Chaperone
Author(s) -
Matthias P. Mayer
Publication year - 2012
Publication title -
cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 26.304
H-Index - 776
eISSN - 1097-4172
pISSN - 0092-8674
DOI - 10.1016/j.cell.2012.02.029
Subject(s) - biology , chaperone (clinical) , redox , biophysics , computational biology , microbiology and biotechnology , medicine , pathology , materials science , metallurgy
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.
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