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Substrate and Inhibitor Profile of BACE (β-Secretase) and Comparison with Other Mammalian Aspartic Proteases
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BACE1 preferentially cleaves C-terminally to leucine or other hydrophobic amino acids.
“but BACE1 preferentially cleaves C-terminally to leucine or other hydrophobic amino acids [40].”
From Seizure protein 6 and its homolog seizure 6-like protein are physiological substrates of BACE1 in neurons (2016) · cites this paper as [40]
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Pigoni, M., Wanngren, J., Kuhn, P.-H., Munro, K. M., Gunnersen, J. M., Takeshima, H., Feederle, R., Voytyuk, I., De Strooper, B., Levasseur, M. D., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0134-z · Cited by 125
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Metadata
- Authors
- Grüninger-Leitch, F., Schlatter, D., Küng, E., Nelböck, P., & Döbeli, H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-02
- Volume
- 277
- Issue
- 7
- Pages
- 4687-4693
- ISSN
- 0021-9258
- Cited by
- 211
- References
- 1
- Language
- en
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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