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- W1973025287 abstract "Immunocytochemical, biochemical, and molecular genetic studies indicate that apolipoprotein E (apoE) plays an important role in the process of amyloidogenesis-β. However, there is still no clear translation of these data into the pathogenesis of amyloidosis-β. Previous studies demonstrated sodium dodecyl sulfate (SDS)-resistant binding of apoE to the main component of Alzheimer’s amyloid-Aβ and modulation of Aβ aggregation by apoE in vitro. To more closely characterize apoE-Aβ interactions, we have studied the binding of thrombolytic fragments of apoE3 to Aβ in vitro by using SDS-polyacrylamide gel electrophoresis and intrinsic fluorescence quenching. Here we demonstrate that SDS-resistant binding of Aβ is mediated by the receptor-binding, N-terminal domain of apoE3. Under native conditions, both the N- and C-terminal domains of apoE3 bind Aβ; however, the former does so with higher affinity. We propose that the modulation of Aβ binding to the N-terminal domain of apoE is a potential therapeutic target for the treatment of amyloidosis-β." @default.
- W1973025287 created "2016-06-24" @default.
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- W1973025287 date "2000-08-01" @default.
- W1973025287 modified "2023-10-02" @default.
- W1973025287 title "Sodium Dodecyl Sulfate-Resistant Complexes of Alzheimer’s Amyloid β-Peptide with the N-Terminal, Receptor Binding Domain of Apolipoprotein E" @default.
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- W1973025287 doi "https://doi.org/10.1016/s0006-3495(00)76354-5" @default.
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