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

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,Inhibition of α-Secretase by Zinc Metalloproteinase Inhibitors, the β-amyloid (Aβ) peptide by β-secretase and at the C-terminus by one or more γ-secretases constitutes the amyloidogenic pathway. In the nonamyloidogenic pathway, α-secretase cleaves APP within the Aβ peptide between Lys16 and Leu17 (numbering from the N-terminus of the Aβ peptide) (.), thereby pr

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,Development of Neoepitope Antibodies Against the β-Secretase Cleavage Site in the Amyloid Precursorin (APP) has eluded many researchers. This is largely because the measurement of the various APP processing products is technically challenging owing to their low levels of production in in vitro and in vivo test systems. Sequence analysis of products in cell cultures, cerebrospinal fluid (CSF), and

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,Using β-Secretase Inhibitors to Distiguish the Generation of the Aβ Peptides Terminating at Val-40 c and toxicity requires the formation of amyloid fibrils similar to those found in senile plaques (.). Autosomal dominant mutations linked to Alzheimer’s disease were identified in three different genes (. .). All mutations apparently alter amyloid precursor protein (APP) metabolism to increase the

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