Identification of a redox-regulated chaperone network.

@article{Hoffmann2004IdentificationOA,
  title={Identification of a redox-regulated chaperone network.},
  author={J{\"o}rg H. Hoffmann and Katrin Linke and Paul C. F. Graf and Hauke Lilie and Ursula Jakob},
  journal={The EMBO journal},
  year={2004},
  volume={23 1},
  pages={160-8}
}
We have identified and reconstituted a multicomponent redox-chaperone network that appears to be designed to protect proteins against stress-induced unfolding and to refold proteins when conditions return to normal. The central player is Hsp33, a redox-regulated molecular chaperone. Hsp33, which is activated by disulfide bond formation and subsequent dimerization, works as an efficient chaperone holdase that binds to unfolding protein intermediates and maintains them in a folding competent… CONTINUE READING
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