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The heat shock response: life on the verge of death.
This Review summarizes the concepts of the protective Hsp network, and the most conserved Hsps are molecular chaperones that prevent the formation of nonspecific protein aggregates and assist proteins in the acquisition of their native structures. Expand
Some like it hot: the structure and function of small heat-shock proteins
Small heat-shock proteins are a widespread and diverse class of molecular chaperones that maintain protein homeostasis by binding proteins in non-native conformations, thereby preventing substrate aggregation. Expand
Small heat shock proteins are molecular chaperones.
It is shown that all sHsps investigated act as molecular chaperones in these folding reactions and at stoichiometric amounts they maximally prevent the aggregation of citrate synthase and alpha-glucosidase under heat shock conditions and stabilize the proteins. Expand
Binding of non‐native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
The task of sHsps in this context is to efficiently trap a large number of unfolding proteins in a folding‐competent state and thus create a reservoir of non‐native proteins for an extended period of time, allowing refolding after restoration of physiological conditions in cooperation with other chaperones. Expand
Regulation of Hsp27 Oligomerization, Chaperone Function, and Protective Activity against Oxidative Stress/Tumor Necrosis Factor α by Phosphorylation*
It is demonstrated that large oligomers of sHsps are necessary for chaperone action and resistance against oxidative stress whereas phosphorylation down-regulates these activities by dissociation of s Hsps complexes to tetramers. Expand
The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones.
Hsp90 is a dimeric molecular chaperone required for the activation and stabilization of numerous client proteins many of which are involved in essential cellular processes like signal transductionExpand
Hsp26: a temperature‐regulated chaperone
The temperature‐dependent dissociation of the large storage form of Hsp26 into a smaller, active species and the subsequent re‐association to a defined large chaperone–substrate complex represents a novel mechanism for the functional activation of a molecular chaperones. Expand
The Hsp90 Chaperone Machinery*
The current knowledge on the functional principles of this molecular machine, including the ATPdriven chaperone cycle of Hsp90 and its regulation by co-chaperones and post-translational modifications are summarized. Expand
Hsp70 and Hsp90--a relay team for protein folding.
This review summarizes the current knowledge in the field, including the ATP-dependent regulation of the Hsp70/Hsp90 multichaperone cycle and elucidates the complex interplay and their synergistic interaction. Expand
Hsp90 & Co. - a holding for folding.
  • J. Buchner
  • Biology, Medicine
  • Trends in biochemical sciences
  • 1 April 1999
In vitro experiments suggest that Hsp90 contains two different binding sites for non-native proteins, which allow it to combine the properties of a promiscuous chaperone with those of a dedicated folding-helper protein. Expand