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RISS 인기검색어
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- 발행기관 : The Research Institute of Chosun Natural Science (검색결과 2 건)
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Tuyet, Pham Thi Dieu The Research Institute of Chosun Natural Science 2014 조선자연과학논문집 Vol.7 No.1
Formation of amyloid-${\beta}$ ($A{\beta}$) aggregates is a core process in the pathogenesis of Alzheimer's disease. Importance of interaction of the length variants, $A{\beta}42$ and $A{\beta}40$ in the process and consequent cytotoxicity has been pointed out for wild-type $A{\beta}$ 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 $A{\beta}42/A{\beta}40$ 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 $A{\beta}42/A{\beta}40$ 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 $A{\beta}$ 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 $A{\beta}40$ variant, rather than that of $A{\beta}42$, because aggregation rates and levels of $A{\beta}40$ variants are greatly variable depending on the sequence, compared to $A{\beta}42$ variants. These studies may highlight a potential role of $A{\beta}40$ in the cytotoxicity, providing a novel mechanistic insight into the pathogenesis of each FAD-associated variant.
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Merlin Jayalal, L.P. The Research Institute of Chosun Natural Science 2013 조선자연과학논문집 Vol.6 No.1
Formation of amyloid-${\beta}$ ($A{\beta}$) aggregates is a core process in the pathogenesis of Alzheimer's disease. Importance of interaction of the length variants, $A{\beta}42$ and $A{\beta}40$ in the process and consequent cytotoxicity has been pointed out for wild-type $A{\beta}$ 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 $A{\beta}42/A{\beta}40$ 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 $A{\beta}42/A{\beta}40$ 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 $A{\beta}$ 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 $A{\beta}40$ variant, rather than that of $A{\beta}42$, because aggregation rates and levels of $A{\beta}40$ variants are greatly variable depending on the sequence, compared to $A{\beta}42$ variants. These studies may highlight a potential role of $A{\beta}40$ in the cytotoxicity, providing a novel mechanistic insight into the pathogenesis of each FAD-associated variant.
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