Molecular chaperones in cellular protein folding

@article{Hartl1996MolecularCI,
  title={Molecular chaperones in cellular protein folding},
  author={F. Ulrich Hartl},
  journal={Nature},
  year={1996},
  volume={381},
  pages={571-580}
}
  • F. Hartl
  • Published 13 June 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… 
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The identification and characterization of the cellular substrates of chaperones will be instrumental in understanding how proteins fold in vivo.
Chaperone-assisted protein folding.
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Highlights of the past year include the X-ray crystallographic analysis of the peptide-binding domain of the Escherichia coli Hsp70 homolog, DnaK, the direct demonstration of protein folding in the central cavity of the chaperonin GroEL, and the visualization of conformational changes in GroEL during the chacheronin folding cycle.
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
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Understanding how the thousands of different proteins synthesized in a cell use this chaperone machinery has profound implications for biotechnology and medicine.
Protein Folding and Chaperones
The specific conformation characteristic of each protein is determined by the amino acid sequence of that protein by the process of protein folding. Molecular chaperones use two distinct mechanisms…
The 70 kDa stress-related proteins as molecular chaperones
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The need to reconcile the in vitro and in vivo differences in protein folding rate and efficiency led to a modification of the self-assembly hypothesis — the molecular chaperone concept, a specific group of proteins that assist in the assembly of other proteins by suppressing nonproductive side reactions.
From the cradle to the grave: molecular chaperones that may choose between folding and degradation
TLDR
A novel concept for the regulation of the eukaryotic Hsp70 and Hsp90 chaperone systems during protein folding and protein degradation is presented.
Chaperones, Chaperonin and Heat‐Shock Proteins
The protein folding of a nascent polypeptide is the decoding of the linear information contained in the primary sequence into the native three-dimensional conformation. Chaperone proteins and folding…
Protein folding: Who chaperones nascent chains in bacteria?
TLDR
Two new studies have shown that molecular chaperones trigger factor and DnaK perform essential, yet partially redundant, functions in chaperoning nascent protein chains in bacteria.
Structures and Functions of Chaperones and Chaperonins (Review)
TLDR
Molecular chaperones are a group of relatively recently discovered proteins that control the assembling of native structures and remodel protein molecules that have wrong conformations.
Molecular chaperone functions in protein folding and proteostasis.
TLDR
This review focuses on recent advances in understanding the mechanisms of chaperone action in promoting and regulating protein folding and on the pathological consequences of protein misfolding and aggregation.
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References

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TLDR
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TLDR
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TLDR
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