Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Abeta 42 production.

@article{Moehlmann2002Presenilin1MO,
  title={Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Abeta 42 production.},
  author={Tobias Moehlmann and Edith Winkler and Xuefeng Xia and Dieter Edbauer and Jill Murrell and Anja Capell and Christoph Kaether and Hui Zheng and Bernardino Ghetti and Christian Haass and Harald Steiner},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2002},
  volume={99 12},
  pages={
          8025-30
        }
}
The Alzheimer's disease (AD)-associated presenilin (PS) proteins are required for the gamma-secretase cleavages of the beta-amyloid precursor protein and the site 3 (S3) protease cleavage of Notch. These intramembrane cleavages release amyloid-beta peptide (Abeta), including the pathogenic 42-aa variant (Abeta(42)), as well as the beta-amyloid precursor protein and the Notch intracellular domains (AICD, NICD). Whereas Abeta is generated by endoproteolysis in the middle of the transmembrane… CONTINUE READING

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