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K. Thurber

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Open access Aug 2026

Brain-seeded 42-residue amyloid-β fibrils that resemble fibrils directly extracted from Alzheimer’s disease brain tissue

Two new brain-seeded Aβ42 fibril polymorphs that share certain structural features with previously characterized polymorphs extracted from AD brain tissue are reported, contributing to understanding of the relationships between brain-seeded and brain-extracted fibril structures and expanding the understanding of the fu...

K. Thurber, Myungwoon Lee, R. Tycko · 0 citations
Open access Aug 2026

Polymorphic structures of rapidly twisting 40-residue amyloid-β fibrils

Cryogenic electron microscopy is used to characterize the structure of rapidly twisting Aβ40 fibrils, for which the distance between apparent width minima in electron microscope images (“cross-over distances”) is approximately 25 nm, and contributes to the understanding of amyloid polymorphism, connections between morp...

M. G. Larimi, K. Thurber, R. Tycko · 0 citations

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