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Cited by 357

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

BACE2, a β-secretase homolog, cleaves at the β site and within the amyloid-β region of the amyloid-β precursor protein

Farzan, Michael, Schnitzler, Christine E., Vasilieva, Natalya, Leung, Doris, Choe, Hyeryun·2000·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.160115697
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Abstract

Production of amyloid-β protein (Aβ) is initiated by a β-secretase that cleaves the Aβ precursor protein (APP) at the N terminus of Aβ (the β site). A recently identified aspartyl protease, BACE, cleaves the β site and at residue 11 within the Aβ region of APP. Here we show that BACE2, a BACE homolog, cleaves at the β site and more efficiently at a different site within Aβ. The Flemish missense mutation of APP, implicated in a form of familial Alzheimer's disease, is adjacent to this latter site and markedly increases Aβ production by BACE2 but not by BACE. BACE and BACE2 respond identically to conservative β-site mutations, and alteration of a common active site Arg inhibits β-site cleavage but not cleavage within Aβ by both enzymes. These data suggest that BACE2 contributes to Aβ production in individuals bearing the Flemish mutation, and that selective inhibition of these highly similar proteases may be feasible and therapeutically advantageous.

Overview

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Registry

Crossref · 10.1073/pnas.160115697

Cites

5 of 5 references verified0 citation errors · 0 not checkable

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Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 24

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Metadata

Authors
Farzan, M., Schnitzler, C. E., Vasilieva, N., Leung, D., & Choe, H.
Affiliations
Department of Cancer Immunology and AIDS, Dana–Farber Cancer Institute, and Department of Pathology, and Perlmutter Laboratory, Children's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA 02115
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2000-08-08
Volume
97
Issue
17
Pages
9712-9717
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.160115697
Cited by
357
References
5
Language
en

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