Noriyuki Nishida

The paper investigates how hydrophobic amino acid mutations affect the stability of β-sheet amyloids in α-synuclein and a PrPSc model, revealing their role in prion strain diversity.

The paper uses molecular dynamics simulations to show how codon 129 polymorphism affects PrPSc structure and propagation by comparing V129 and M129 models.

The paper uses molecular dynamics simulations to show that methionine uniquely stabilizes a beta-arch structure in an in-register parallel beta-sheet amyloid, suggesting its role in prion strain diversity.

The paper reviews advances in understanding the structures of Tau and Syn amyloids and discusses their implications for prion strain diversity mechanisms.

The paper uses molecular dynamics simulations to show that mutant α-synuclein amyloids have switchable β-sheet structures that may explain their strain-like properties.

This study uses disulfide-crosslink scanning to reveal strain-specific structural changes in PrPSc, showing that prion strain diversity is encoded in conformational differences in specific regions of the protein.

The paper uses secondary-structure prediction to analyze interspecies prion transmission by examining Pβ and Pc values, showing their utility in explaining structural phenomena.