Truncated carboxyl-terminal fragments of beta-amyloid precursor protein are processed to amyloid beta-proteins 40 and 42.

@article{Funamoto2004TruncatedCF,
  title={Truncated carboxyl-terminal fragments of beta-amyloid precursor protein are processed to amyloid beta-proteins 40 and 42.},
  author={Satoru Funamoto and Maho Morishima-Kawashima and Yu Tanimura and Naoko Hirotani and Takaomi C Saido and Yasuo Ihara},
  journal={Biochemistry},
  year={2004},
  volume={43 42},
  pages={13532-40}
}
We previously showed that beta-amyloid precursor protein (APP) is cleaved not only in the middle of the membrane (gamma-cleavage) but also at novel cleavage sites close to the membrane/cytoplasmic boundary (epsilon-cleavage), releasing APP intracellular domains (AICDs) 49-99 and 50-99. To learn more about the relationship between gamma- and epsilon-cleavage, C-terminally truncated carboxyl-terminal fragments (CTFs) of APP, especially CTFs1-48 and 1-49 (the postulated products that are generated… CONTINUE READING

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