Ontology highlight
ABSTRACT:
SUBMITTER: Hoffmann JH
PROVIDER: S-EPMC1271656 | biostudies-literature | 2004 Jan
REPOSITORIES: biostudies-literature
Hoffmann Jörg H JH Linke Katrin K Graf Paul C F PC Lilie Hauke H Jakob Ursula U
The EMBO journal 20031211 1
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 confo ...[more]