• DOI:10.1038/nature10317
Corpus ID: 4337671

Molecular chaperones in protein folding and proteostasis

@article{Hartl2011MolecularCI,
  title={Molecular chaperones in protein folding and proteostasis},
  author={F. U. Hartl and A. Bracher and M. Hayer-Hartl},
  journal={Nature},
  year={2011},
  volume={475},
  pages={324-332}
}

F. U. Hartl, A. Bracher, M. Hayer-Hartl

Published 2011

Biology, Medicine

Nature

Most proteins must fold into defined three-dimensional structures to gain functional activity. But in the cellular environment, newly synthesized proteins are at great risk of aberrant folding and aggregation, potentially forming toxic species. To avoid these dangers, cells invest in a complex network of molecular chaperones, which use ingenious mechanisms to prevent aggregation and promote efficient folding. Because protein molecules are highly dynamic, constant chaperone surveillance is… CONTINUE READING

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