Protein folding: Chaperone embrace

@article{Cesari2008ProteinFC,
  title={Protein folding: Chaperone embrace},
  author={Francesca Cesari},
  journal={Nature Reviews Molecular Cell Biology},
  year={2008},
  volume={9},
  pages={497-497}
}
...HSP110 proteins control nucleotide exchange on HSP70 chaperones... Heat-shock protein-70 (HSP70) proteins are molecular chaperones that participate in many cellular processes, such as protein folding, transport across membranes, prevention of protein aggregation and degradation. HSP70 activity is regulated by nucleotide-exchange factors (NEFs), which accelerate the release of ADP from the HSP70 nucleotide-binding domain (NBD), allowing ATP binding; this causes the release of the substrate… CONTINUE READING