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

Cleavage of Amyloid-β Precursor Protein and Amyloid-β Precursor-like Protein by BACE 1

Li, Qiming, Südhof, Thomas C.·2004·Journal of Biological Chemistry
DOI 10.1074/jbc.m310001200
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  • VPS35 deficiency leads to a similar increase in APP-related proteins APLP1 and APLP2 at the cell surface, which are thought to be processed by secretases in the same way as APP.

    “As has been shown previously, VPS35 deficiency also leads to a similar increase in APP-related proteins APLP1 and APLP2 at the cell surface, which are thought to be processed by secretases in the same way as APP [79,93,141].”

    From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [93]

    The Discussion reports that APP, APLP1, and APLP2 are cleaved by BACE 1, supporting the secretase-processing portion of the claim. The paper does not report VPS35 deficiency or an increase in APLP1 and APLP2 at the cell surface. (LLM, conf=0.88)

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  • Besides APP, identified BACE substrates include APLP1 and -2, PSGL-1, and a membrane-bound sialyltransferase.

    “Besides APP, the few BACE substrates that have been identi-fied include the APP homologues APLP1 and -2 (5), P-selectin glycoprotein ligand-1 (PSGL-1), and a membrane-bound sialyltransferase (6).”

    From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [5]

  • In addition to APP, there was an increase in the surface expression of several proteins involved in APP processing and amyloid-β response in VPS35-suppressed neuronal cultures, including BACE1, APLP1, APLP2, ABCC1, EPHA4, IGFR1, and SYP.

    “In addition to APP, we found an increase in the surface expression of several proteins involved in APP processing and amyloid-β response in the VPS35 suppressed neuronal cultures.These included βsecretase 1 (BACE1), [92], APP-like β-secretase substrates APLP1 and APLP2 [93], transporter ABCC1 [94][95][96], ephrin type-A receptor 4 (EPHA4) [97,98], and insulin-like growth factor-1 (IGFR1) [99], and”

    From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [93]

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Metadata

Authors
Li, Q., & Südhof, T. C.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2004-03
Volume
279
Issue
11
Pages
10542-10550
ISSN
0021-9258
DOI
10.1074/jbc.m310001200
Cited by
180
References
5
Language
en
Licence

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