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- W2092508662 abstract "Insights into Amyloidogenesis The amyloid-β (Aβ) peptides associated with Alzheimer's disease are generated by cleavage of the transmembrane C-terminal domain (C99) of the amyloid precursor protein by the enzyme γ-secretase. Barrett et al. (p. 1168 ) used nuclear magnetic resonance (NMR) and electron paramagnetic resonance spectroscopy to show that C99 contains surface-associated N- and C-terminal helices and a flexibly curved transmembrane helix that is well suited to processive cleavage by γ-secretase. Elevated cholesterol levels have been found to increase Aβ generation. NMR titration together with mutagenesis revealed a binding site for cholesterol within C99 that included a motif previously implicated in protein oligomerization." @default.
- W2092508662 created "2016-06-24" @default.
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- W2092508662 date "2012-06-01" @default.
- W2092508662 modified "2023-10-11" @default.
- W2092508662 title "The Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds Cholesterol" @default.
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- W2092508662 doi "https://doi.org/10.1126/science.1219988" @default.
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