Amyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization.

@article{Richter2010AmyloidB4,
  title={Amyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization.},
  author={Luise Richter and Lisa Marie Munter and Julia Ness and Peter Werner Hildebrand and Muralidhar Dasari and Stephanie Unterreitmeier and Bruno Bulic and Michael Beyermann and Ronald Gust and Bernd Reif and Sascha Weggen and Dieter Langosch and Gerhard Multhaup},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 33},
  pages={14597-602}
}
Following ectodomain shedding by beta-secretase, successive proteolytic cleavages within the transmembrane sequence (TMS) of the amyloid precursor protein (APP) catalyzed by gamma-secretase result in the release of amyloid-beta (Abeta) peptides of variable length. Abeta peptides with 42 amino acids appear to be the key pathogenic species in Alzheimer's disease, as they are believed to initiate neuronal degeneration. Sulindac sulfide, which is known as a potent gamma-secretase modulator (GSM… CONTINUE READING
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