Hsp90 chaperones protein folding in vitro

@article{Wiech1992Hsp90CP,
  title={Hsp90 chaperones protein folding in vitro},
  author={Hans Wiech and Johannes Buchner and Richard Zimmermann and Ursula Jakob},
  journal={Nature},
  year={1992},
  volume={358},
  pages={169-170}
}
THE heat-shock protein Hsp90 is the most abundant constitutively expressed stress protein in the cytosol of eukaryotic cells1,2, where it participates in the maturation of other proteins, modulation of protein activity in the case of hormone-free steroid receptors, and intracellular transport of some newly synthesized kinases3–5. A feature of all these processes could be their dependence on the formation of protein structure. If Hsp90 is a molecular chaperone involved in maintaining a certain… 
Heat shock proteins: molecular chaperones of protein biogenesis
TLDR
Results of experiments are discussed within the context of experiments with other organisms in an attempt to describe the current state of understanding of these ubiquitous and important proteins.
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In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone.
TLDR
The data suggest that Hsp90 is not required for the de novo folding of most proteins, but it is required for a specific subset of proteins that have greater difficulty reaching their native conformations.
Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence.
TLDR
It is proposed that the existence of two functionally different chaperone sites together with a substrate-selecting set of cochaperones allows Hsp90 to guide the folding of a subset of target proteins and, at the same time, to exhibit general chaper one functions.
The Hsp90 Chaperone Machinery*
TLDR
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.
Hsp90: Chaperoning signal transduction
TLDR
Hsp90 is an ATP dependent molecular chaperone involved in the folding and activation of an unknown number of substrate proteins that are critical elements in signal transduction and seems to introduce an additional level of regulation.
In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis
TLDR
It is shown that both ATP binding and hydrolysis are required for Hsp82 function in vivo, and the results establish Hsp90 as an ATP-dependent chaperone.
A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90.
TLDR
It is shown that Cisplatin [cis-diamminedichloroplatinum (II), CDDP], an antineoplastic agent, associates with HSP90 and reduces its chaperone activity.
Chaperone Function of Hsp90-Associated Proteins
TLDR
Results suggest the existence of a super-chaperone complex in the cytosol of eukaryotic cells and include members of the prolyl isomerase family.
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