The Osaka FAD mutation E22Δ leads to the formation of a previously unknown type of amyloid β fibrils and modulates Aβ neurotoxicity.

@article{Ovchinnikova2011TheOF,
  title={The Osaka FAD mutation E22Δ leads to the formation of a previously unknown type of amyloid β fibrils and modulates Aβ neurotoxicity.},
  author={Oxana Yu Ovchinnikova and Verena H Finder and Ivana Vodopivec and Roger M. Nitsch and Rudi Glockshuber},
  journal={Journal of molecular biology},
  year={2011},
  volume={408 4},
  pages={780-91}
}
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by cerebral deposition of amyloid fibrils formed by the amyloid β (Aβ) peptide. Aβ has a length of 39-43 amino acid residues; the predominant Aβ isoforms are Aβ1-40 and Aβ1-42. While the majority of AD cases occur spontaneously, a subset of early-onset familial AD cases is caused by mutations in the genes encoding the Aβ precursor protein or presenilin 1/presenilin 2. Recently, a deletion of glutamic acid at position 22… CONTINUE READING
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