Distinct sites of intracellular production for Alzheimer's disease Aβ40/42 amyloid peptides

@article{Hartmann1997DistinctSO,
  title={Distinct sites of intracellular production for Alzheimer's disease A$\beta$40/42 amyloid peptides},
  author={Tobias Hartmann and Sophie Bieger and Babara Br{\"u}hl and Pentti J. Tienari and Nobuo Ida and David Allsop and Gareth W. Roberts and Colin L. Masters and Carlos G Dotti and Klaus Unsicker and Konrad T. Beyreuther},
  journal={Nature Medicine},
  year={1997},
  volume={3},
  pages={1016-1020}
}
The Alzheimer amyloid precursor protein (APP) is cleaved by several proteases, the most studied, but still unidentified ones, are those involved in the release of a fragment of APP, the amyloidogenic β-protein Aβ. Proteolysis by γ-secretase is the last processing step resulting in release of Aβ. Cleavage occurs after residue 40 of Aβ [Aβ(1–40)], occasionally after residue 42 [Aβ(1–42)]. Even slightly increased amounts of this Aβ(1–42) might be sufficient to cause Alzheimer's disease (AD… 
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