Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils

By A. Paravastu, Richard Leapman, Wai-Ming Yau, R. Tycko. Proceedings of the National Academy of Sciences of the United States of America, 2008

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Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, methodology): “Such structure has generally been shown to involve both antiparallel (174, 181) and parallel and out-of-register strands (176), compared with the structure of the fibrils in which the β-strands are arranged in a parallel and in-register manner (72, 82, 83, 85, 122).”
Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils (2010, positive): “The side-chain packing registry within the β -turn- β motif of A β 42 fibrils is similar to that observed in A β 40 fibrils by Tycko and co-workers 19 , 20 (Fig.”