Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers.

@article{Mannini2012MolecularMU,
  title={Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers.},
  author={Benedetta Mannini and Roberta Cascella and Mariagioia Zampagni and Maria A W H van Waarde-Verhagen and Sarah Meehan and Cintia Roodveldt and Silvia Campioni and Matilde Boninsegna and Amanda Penco and Annalisa Relini and Harm H. Kampinga and Christopher M. Dobson and Mark R. Wilson and Cristina Cecchi and Fabrizio Chiti},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2012},
  volume={109 31},
  pages={12479-84}
}
Chaperones are the primary regulators of the proteostasis network and are known to facilitate protein folding, inhibit protein aggregation, and promote disaggregation and clearance of misfolded aggregates inside cells. We have tested the effects of five chaperones on the toxicity of misfolded oligomers preformed from three different proteins added extracellularly to cultured cells. All the chaperones were found to decrease oligomer toxicity significantly, even at very low chaperone/protein… CONTINUE READING
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