Prefibrillar Amyloid Aggregates Could Be Generic Toxins in Higher Organisms

@article{Baglioni2006PrefibrillarAA,
  title={Prefibrillar Amyloid Aggregates Could Be Generic Toxins in Higher Organisms},
  author={S. Baglioni and F. Casamenti and M. Bucciantini and L. Luheshi and N. Taddei and F. Chiti and C. Dobson and M. Stefani},
  journal={The Journal of Neuroscience},
  year={2006},
  volume={26},
  pages={8160 - 8167}
}
More than 40 human diseases are associated with fibrillar deposits of specific peptides or proteins in tissue. Amyloid fibrils, or their precursors, can be highly toxic to cells, suggesting their key role in disease pathogenesis. Proteins not associated with any disease are able to form oligomers and amyloid assemblies in vitro displaying structures and cytotoxicity comparable with those of aggregates of disease-related polypeptides. In isolated cells, such toxicity has been shown to result… Expand
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A causative link between the structure of aberrant protein oligomers and their toxicity.
Annular Protofibrils Are a Structurally and Functionally Distinct Type of Amyloid Oligomer*
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