Prion Diseases and Protein Misfolding

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 shows that structurally diverse PrPSc assemblies complement each other to cross species barriers, supporting the quasi-species concept in prions.

The paper investigates the role of small endogenous RNAs in scrapie-infected hamster brains but finds no scrapie-specific variants in eight candidate RNA species.

The paper examines how prion diseases alter region-specific glial homeostatic signatures, finding that these signatures are replaced by a region-independent neuroinflammation signature during disease progression.

The paper shows that a specific amino acid at position 163 in canine PrPC confers resistance to prion infection, confirmed through transgenic mouse 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.

This study analyzes the structure of the native human Prion Protein and compares it with the toxic form causing Sporadic Fatal Insomnia, finding increased flexibility in the mutant form.

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.