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Model for the assembly and pathological aggregation of U1-70K and other RNA-binding proteins with BAD domains in AD. RNA-binding proteins with BAD domains reciprocally interact to form dimers, oligomers, and RNA granules (via LLPS) under normal endogenous conditions. In AD, RBPs with BAD domains and Tau aberrantly interact in the cytoplasm to form aggregates under pathological conditions, with a mechanism likely influenced by Aβ-directed signaling events.
