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Titlebook: Alzheimer‘s Disease; Methods and Protocol Nigel M. Hooper Book 2000 Humana Press 2000

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Posttranslational Modifications of the Amyloid Precursor Protein,er provides methods for analyzing the glycosylation of APP that is actively synthesized by living cells in tissue culture. These methods can be applied to primary cultures, continuous cell lines, and transfected cell lines expressing recombinant APP.
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,Development of Neoepitope Antibodies Against the β-Secretase Cleavage Site in the Amyloid Precursorptide from APP (. .). More routine identification of the secretase activities has relied on the specificity and sensitivity of antibodies raised to the predicted cleavage products and has been impeded by the difficulties associated with the generation of such reagents.
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https://doi.org/10.1007/978-3-662-02210-8 cleavages govern the level of Aβ generated from the amyloid precursor protein (APP). β- and γ-cleavages at the amino and carboxyl termini of Aβ produce amyloidogenic peptides; in contrast, α-cleavage within the Aβ domain destroys the amyloidogenic potential of APP. The proteases responsible for these cleavages have not been identified.
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