The biological and pathological function of the presenilin-1 Deltaexon 9 mutation is independent of its defect to undergo proteolytic processing.

@article{Steiner1999TheBA,
  title={The biological and pathological function of the presenilin-1 Deltaexon 9 mutation is independent of its defect to undergo proteolytic processing.},
  author={Harald Steiner and Helmut Romig and Melissa G. Grim and Ute Philipp and Brigitte Pesold and Martin Citron and Ralf Baumeister and Christian Haass},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 12},
  pages={7615-8}
}
The two homologous presenilins are key factors for the generation of amyloid beta-peptide (Abeta), since Alzheimer's disease (AD)-associated mutations enhance the production of the pathologically relevant 42-amino acid Abeta (Abeta42), and a gene knockout of presenilin-1 (PS1) significantly inhibits total Abeta production. Presenilins undergo proteolytic processing within the domain encoded by exon 9, a process that may be closely related to their biological and pathological activity. An AD… CONTINUE READING

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