Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

@article{Bucciantini2002InherentTO,
  title={Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases},
  author={M. Bucciantini and E. Giannoni and F. Chiti and F. Baroni and L. Formigli and J. Zurdo and N. Taddei and G. Ramponi and C. Dobson and M. Stefani},
  journal={Nature},
  year={2002},
  volume={416},
  pages={507-511}
}
A range of human degenerative conditions, including Alzheimer's disease, light-chain amyloidosis and the spongiform encephalopathies, is associated with the deposition in tissue of proteinaceous aggregates known as amyloid fibrils or plaques. It has been shown previously that fibrillar aggregates that are closely similar to those associated with clinical amyloidoses can be formed in vitro from proteins not connected with these diseases, including the SH3 domain from bovine phosphatidyl-inositol… Expand
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