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- W2334933842 abstract "Formation of amyloid- () aggregates is a core process in the pathogenesis of Alzheimer's disease. Importance of interaction of the length variants, and in the process and consequent cytotoxicity has been pointed out for wild-type previously. In addition to confirming the findings, the current study demonstrates that the potential interaction is also important for cytotoxicity of the Flemish and Dutch sequence variants. The interaction could strengthen or inhibit cytotoxicity of mixture, depending on interaction time of the length variants as well as the ratio and amyloidogenic property. The inhibitory effect was prominent at the early stage of aggregate formation in less amyloidogenic Flemish mixture, while strengthened cytotoxicity was exhibited at the stage in potently amyloidogenic Dutch variant and at the later stage in wild-type and the Flemish variant. The samples showing relatively robust cytotoxicity were those enriched in protofibril-like structures, implying strong correlation of the structure with cytotoxicity. The different consequence of the interaction on sequence variants is likely due to differential amyloidogenic property of each variant, rather than that of , because aggregation rates and levels of variants are greatly variable depending on the sequence, compared to variants. These studies may highlight a potential role of in the cytotoxicity, providing a novel mechanistic insight into the pathogenesis of each FAD-associated variant." @default.
- W2334933842 created "2016-06-24" @default.
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- W2334933842 date "2014-03-30" @default.
- W2334933842 modified "2023-09-25" @default.
- W2334933842 title "A Study on Cytotoxicities of Aβ40 to Aβ42 in Contract to Time and Concentration with the Comparison of Wild-Type and Mutants" @default.
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- W2334933842 doi "https://doi.org/10.13160/ricns.2014.7.1.11" @default.
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