Molecular structure of an N-terminal phosphorylated β-amyloid fibril

This is the authors' abstract. We don't add key points for this paper.

fibrils may potentially dominate the polymorphisms in the mixture of wild-type and phosphorylated Aβ deposits. Our results imply that Aβ subtypes with "seeding-prone" properties may influence the polymorphisms of amyloid plaques through the cross-seeding process.