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- W1567119143 abstract "Publisher Summary Senile plaques, a neuropathological feature of Alzheimer's disease (AD), consist primarily of an insoluble aggregate of amyloid-β peptide (Aβ), a 40–43 amino acid peptide. Dense core plaques of Aβ deposited in AD brain are typically surrounded by dystrophic neurites, an observation that led to the proposal that Aβ itself may be neurotoxic. Although studied intensively in the early 1990s, the biochemical mechanisms that underlie the neurotoxicity of Aβ remain uncertain. One observation that remains consistent, however, is that amyloidogenic peptides such as Aβ, human amylin, and calcitonin—at least in the aggregated state that is associated with their neurotoxicity—potently inhibit cellular reduction of the tetrazolium redox dye 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT). Despite the fact that the biochemical basis for this inhibitory activity still remains unclear, it appears to be a reliable early indicator of the mechanism of amyloid peptide cytotoxicity." @default.
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- W1567119143 date "1999-01-01" @default.
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- W1567119143 title "[45] Toxicity of protein aggregates in PC12 cells: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay" @default.
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- W1567119143 doi "https://doi.org/10.1016/s0076-6879(99)09047-3" @default.
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