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1 Par-4 Is Involved In Regulation Of -secretase Cleavage Of The ... - Jbc
Get 1 Par-4 Is Involved In Regulation Of -secretase Cleavage Of The ... - Jbc
Ed online January 25, 2005 Find articles, minireviews, Reflections and Classics on similar topics on the JBC Affinity Sites. Alerts: When this article is cited When a correction for this article is posted Click here to choose from all of JBC's e-mail alerts This article cites 0 references, 0 of which can be accessed free at http://www.jbc.org/content/early/2005/01/25/jbc.M411933200.citation.full.html#ref-list-1 Downloaded from http://www.jbc.org/ by guest on September 16, 2014 Access.
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SiRNAs FAQ
BACE1, beta-secretase, is one of the two key enzymes in amyloid precursor protein (APP) processing; the other being gamma-secretase.
Amyloid precursor protein (APP) is initially cleaved by β-secretase in the extracellular space, producing a membrane-tethered, 99-residue carboxyl-terminal fragment known as APP C99 (1). Cleavage of amyloid precursor protein by an archaeal presenilin ... - PNAS pnas.org https://.pnas.org › doi › full › pnas.1502150112 pnas.org https://.pnas.org › doi › full › pnas.1502150112
Aβ is generated from β-amyloid precursor protein (APP) through sequential cleavages first by β-secretase and then by γ-secretase complex. Alternatively, APP can be cleaved by α-secretase within the Aβ domain to release soluble APPα and preclude Aβ generation. APP processing in Alzheimer's disease - Molecular Brain Molecular Brain https://molecularbrain.biomedcentral.com › articles Molecular Brain https://molecularbrain.biomedcentral.com › articles
In the amyloidogenic pathway, APP is cleaved first by β-secretase at Asp1 site to generate the secreted sAPPβ and the membrane-bound fragment C99. C99 is further cleaved by γ-secretase to generate CTFγ and Aβ. BACE1 Cleavage Site Selection Critical for Amyloidogenesis and ... nih.gov https://.ncbi.nlm.nih.gov › articles › PMC6705717 nih.gov https://.ncbi.nlm.nih.gov › articles › PMC6705717
membrane domain Now it is clear that γ-secretase catalyzes three major cleavages within the membrane domain of AβPP, namely the γ-cleavage at Aβ40/42, the ε-cleavage at Aβ49, and the ζ-cleavage at Aβ46. Studies also strongly suggest that cleavage at Aβ43 is also a necessary intermediate step. γ-Secretase Catalyzes Sequential Cleavages of the AβPP ... - NCBI nih.gov https://.ncbi.nlm.nih.gov › articles › PMC2696591 nih.gov https://.ncbi.nlm.nih.gov › articles › PMC2696591
Amyloid precursor protein (APP) is cleaved by β-secretase to produce APP C99, which undergoes additional, sequential cleavages by γ-secretase to generate amyloid-β peptides including Aβ40 and Aβ42. Increased ratios of Aβ42 over Aβ40 are thought to cause Alzheimer's disease.
In the anti-amyloidogenic pathway, APP is cleaved approximately in the middle of the Aβ region by the α-secretase activity (Esch et al.
The enzymes that cleave APP have been extensively characterized. BACE1, a transmembrane aspartic protease, is directly involved in the cleavage of APP at the +1 (prior to amino acid 1) and +11 sites of Aβ.
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