Do amyloid oligomers act as traps for misfolded proteins? A hypothesis.

@article{Gruschus2008DoAO,
  title={Do amyloid oligomers act as traps for misfolded proteins? A hypothesis.},
  author={James M. Gruschus},
  journal={Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis},
  year={2008},
  volume={15 3},
  pages={160-5}
}
Mounting evidence points to soluble peptide oligomers as the primary agents in various amyloid and prion diseases. Multiple mechanisms appear to contribute to the cytotoxic effects of these oligomers. Here, an additional, general mechanism is proposed - that soluble amyloid peptide oligomers serve as "all-purpose"beta strands that can interact with transiently unfolded or nascent proteins where interior beta-sheet edges are exposed. The proteins, trapped in misfolded states through this… CONTINUE READING

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