A presenilin dimer at the core of the gamma-secretase enzyme: insights from parallel analysis of Notch 1 and APP proteolysis.

@article{Schroeter2003APD,
  title={A presenilin dimer at the core of the gamma-secretase enzyme: insights from parallel analysis of Notch 1 and APP proteolysis.},
  author={Eric H. Schroeter and Ma. Xenia G. Ilagan and Anne L Brunkan and Silva Hecimovic and Yue-Ming Li and Min Xu and Huw D. Lewis and Meera T. Saxena and Bart De Strooper and Archie Coonrod and Taisuke Tomita and Takeshi Iwatsubo and Chad L. Moore and Alison M. Goate and Michael S Wolfe and Mark Shearman and Raphael Kopan},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 22},
  pages={13075-80}
}
Notch receptors and the amyloid precursor protein are type I membrane proteins that are proteolytically cleaved within their transmembrane domains by a presenilin (PS)-dependent gamma-secretase activity. In both proteins, two peptide bonds are hydrolyzed: one near the inner leaflet and the other in the middle of the transmembrane domain. Under saturating conditions the substrates compete with each other for proteolysis, but not for binding to PS. At least some Alzheimer's disease-causing PS… CONTINUE READING

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