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• W1975472033 abstract "Significance Apolipoprotein (apo) A-II is the most important protein associated with senile amyloidosis. Because some variants of apoA-II protein have been found among inbred strains of mice, we hypothesized that investigating amyloidogenesis of the variants would improve our understanding of the molecular and biological mechanisms of senile amyloidosis. Here, we demonstrate that mice with type F apoA-II (APOA2F) protein were absolutely resistant to senile amyloidosis. Moreover, a selective C-terminal APOA2F peptide inhibited fibril formation of amyloidogenic apoA-II in vitro and prevented senile amyloidosis in mice. We propose an inhibitory model in which the C-terminal APOA2F peptide prevents further fibril extension by blocking the active ends of seeds. This approach could provide a novel therapeutic option for the treatment of senile amyloidosis." @default.
• W1975472033 created "2016-06-24" @default.
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• W1975472033 date "2015-02-09" @default.
• W1975472033 modified "2023-10-15" @default.
• W1975472033 title "C-terminal sequence of amyloid-resistant type F apolipoprotein A-II inhibits amyloid fibril formation of apolipoprotein A-II in mice" @default.
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• W1975472033 doi "https://doi.org/10.1073/pnas.1416363112" @default.
• W1975472033 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4345559" @default.
• W1975472033 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25675489" @default.
• W1975472033 hasPublicationYear "2015" @default.
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