ASP1 (BACE2) Cleaves the Amyloid Precursor Protein at the β-Secretase Site
✍ Scribed by I. Hussain; D.J. Powell; D.R. Howlett; G.A. Chapman; L. Gilmour; P.R. Murdock; D.G. Tew; T.D. Meek; C. Chapman; K. Schneider; S.J. Ratcliffe; D. Tattersall; T.T. Testa; C. Southan; D.M. Ryan; D.L. Simmons; F.S. Walsh; C. Dingwall; G. Christie
- Book ID
- 115637672
- Publisher
- Elsevier Science
- Year
- 2000
- Tongue
- English
- Weight
- 680 KB
- Volume
- 16
- Category
- Article
- ISSN
- 1044-7431
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## Abstract One of the pathologic hallmarks of Alzheimer's disease is the excessive deposition of β‐amyloid peptides (Aβ) in senile plaques. Aβ is generated when β‐amyloid precursor protein (APP) is cleaved sequentially by β‐secretase, identified as β‐site APP‐cleaving enzyme 1 (BACE1), and γ‐secre
BACE1 cleaves the amyloid precursor protein (APP) at the b-cleavage site (Met 671 -Asp 672 ) to initiate the generation of amyloid peptide Ab. BACE1 is also known to cleave APP at a much less well-characterized b 0 -cleavage site (Tyr 681 -Glu 682 ). We describe here the identification of a novel AP