Heat shock protein 90: its inhibition and function.

@article{Zuehlke2018HeatSP,
  title={Heat shock protein 90: its inhibition and function.},
  author={Abbey D. Zuehlke and Michael A. Moses and Leonard M. Neckers},
  journal={Philosophical transactions of the Royal Society of London. Series B, Biological sciences},
  year={2018},
  volume={373 1738}
}
The molecular chaperone heat shock protein 90 (Hsp90) facilitates metastable protein maturation, stabilization of aggregation-prone proteins, quality control of misfolded proteins and assists in keeping proteins in activation-competent conformations. Proteins that rely on Hsp90 for function are delivered to Hsp90 utilizing a co-chaperone-assisted cycle. Co-chaperones play a role in client transfer to Hsp90, Hsp90 ATPase regulation and stabilization of various Hsp90 conformational states. Many… CONTINUE READING
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