Molecular chaperones in cellular protein folding

@article{Hartl1996MolecularCI,
  title={Molecular chaperones in cellular protein folding},
  author={F. Hartl},
  journal={Nature},
  year={1996},
  volume={381},
  pages={571-580}
}
  • F. Hartl
  • Published 1996
  • Biology, Medicine
  • Nature
  • The folding of many newly synthesized proteins in the cell depends on a set of conserved proteins known as molecular chaperones. These prevent the formation of misfolded protein structures, both under normal conditions and when cells are exposed to stresses such as high temperature. Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide… CONTINUE READING
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    References

    SHOWING 1-10 OF 153 REFERENCES
    Proper and improper folding of proteins in the cellular environment.
    • 70
    Protein folding in the cell
    • 3,836
    Calnexin: a membrane-bound chaperone of the endoplasmic reticulum.
    • 495
    Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones.
    • 370
    Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides.
    • 148
    • PDF