Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein.

@article{Lichtenthaler1999MechanismOT,
  title={Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein.},
  author={Stefan F. Lichtenthaler and Rong Wang and H. Grimm and Sacha N Uljon and Colin L. Masters and Konrad Beyreuther},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 6},
  pages={3053-8}
}
Proteolytic processing of the amyloid precursor protein by beta-secretase yields A4CT (C99), which is cleaved further by the as yet unknown gamma-secretase, yielding the beta-amyloid (Abeta) peptide with 40 (Abeta40) or 42 residues (Abeta42). Because the position of gamma-secretase cleavage is crucial for the pathogenesis of Alzheimer's disease, we individually replaced all membrane-domain residues of A4CT outside the Abeta domain with phenylalanine, stably transfected the constructs in COS7… CONTINUE READING

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