J. Collinge

Alanine replacements in the structured C-terminal domain of the prion protein reveal conformationally variable regions as major determinants for prion propagation

This study uses alanine mutagenesis to identify conformationally variable regions in PrPC that are critical for prion propagation.

Loss of the first β-strand of human prion protein generates an aggregation-competent partially "open" form

This study examines the structural and functional changes in a truncated form of human prion protein lacking a conserved membrane region, showing it forms fibrils more readily than the native form.

Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and Kinetics

This study uses super-resolution microscopy to observe competing prion protein fibril populations with distinct structures and kinetics, revealing their quasi-species behavior.

A structural basis for prion strain diversity

This paper determines the cryo-EM structure of ME7 prion fibrils and compares it to RML fibrils, revealing structural differences that explain prion strain diversity within the same species.

Mapping prion pathology in mice using quantitative imaging: an MRI study

The paper uses MRI techniques to detect early prion disease changes in mice, identifying significant alterations in brain regions before clinical symptoms appear.

Can Chemical Exchange Saturation Transfer (CEST MRI) be used as biomarker of disease progression in Prion Disease?

This study shows that CEST MRI can detect early pathological changes in prion disease before structural or clinical signs, with significant correlations between CEST metrics and histopathological findings.

2.7 A cryo-EM structure of ex vivo RML prion fibrils

The paper presents a cryo-EM structure of prion fibrils from RML prion-infected mice, revealing structural features and conformational variations that may influence prion strain diversity and propagation.

Brazilin Removes Toxic alpha-Synuclein and Seeding Competent Assemblies from Parkinson Brain by Altering Conformational Equilibrium

This paper shows Brazilin inhibits alpha-synuclein fibril formation and reduces toxicity in Parkinson's disease by altering conformational equilibrium.