Alzheimer’s disease-linked Flemish APP mutation defines a distinct amyloid-β fold
Cryogenic electron microscopy shows that the rare Flemish mutation in the amyloid-β precursor protein drives Aβ40 (an amyloid-β peptide) to assemble into a distinct filament fold. By exposing a phenylalanine residue, this fold creates a molecular feature that might explain the vascular accumulation of Aβ40 and associated cerebral hemorrhage in individuals carrying the Flemish mutation.
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Cryogenic electron microscopy shows that the rare Flemish mutation in the amyloid-β precursor protein drives Aβ40 (an amyloid-β peptide) to assemble into a distinct filament fold. By exposing a phenylalanine residue, this fold creates a molecular feature that might explain the vascular accumulation of Aβ40 and associated cerebral hemorrhage in individuals carrying the Flemish mutation.
Long, J. M. & Holtzman, D. M. Alzheimer disease: an update on pathobiology and treatment strategies. Cell 179, 312–339 (2019). This review provides a broad overview of Alzheimer’s disease pathobiology.