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- W2085241860 abstract "One of the features of Alzheimer's disease (AD) is the formation of senile plaques, of which the main component is a 42 amino acid β-protein (βP). Molecular cloning of βP revealed the presence of a 90–130 kDa precursor, amyloid precursor protein (APP). Since APP is expressed in normal brain without producing βP, some abnormal processing is the cause of the formation of βP in AD. Two kinds of mutations of APP, Glu693 to Gln and Val717 to Ile, were reported in AD-related diseases. Site-directed mutagenesis was applied, and the mutated APPs were expressed in COS-1 cells by cDNA transfection. They showed apparently the same processing as wild APP. This means that these mutations might not be a direct cause for the abnormal processing of APP or the formation of βP in AD." @default.
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- W2085241860 date "1991-10-01" @default.
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- W2085241860 title "Mutation of Glu693 to Gln or Val717 to Ile has no effect on the processing of Alzheimer amyloid precursor protein expressed in COS-1 cells by cDNA transfection" @default.
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- W2085241860 doi "https://doi.org/10.1016/0304-3940(91)90442-v" @default.
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