The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones.

@article{Li2012TheHC,
  title={The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones.},
  author={Jing Li and Joanna Soroka and Johannes Buchner},
  journal={Biochimica et biophysica acta},
  year={2012},
  volume={1823 3},
  pages={624-35}
}
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 transduction pathways. This activation process is regulated by ATP-induced large conformational changes, co-chaperones and posttranslational modifications. For some co-chaperones, a detailed picture on their structures and functions exists, for others their contributions to the Hsp90 system is still unclear… CONTINUE READING
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Cpr6 and Cpr7

  • C. Mayr, K. Richter, H. Lilie, J. Buchner
  • two closely related Hsp90associated immunophilins…
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