G.F. Schroeder

This study shows that stochastic misfolding leads to the formation of distinct α-synuclein strains both in vitro and in vivo, resulting in different disease phenotypes.

This paper introduces new DIBMA-based copolymers for extracting GPCRs into native lipid-bilayer nanodiscs, showing improved performance over existing polymers like SMA.

This paper shows lecanemab binds to amyloid-β fibrils from Alzheimer's disease mouse models with flexible N-termini, including type-I, type-II, and Arctic folds, but not those with fixed N-termini like in tg-SwDI mice.

This paper shows that anle138b binds to a cavity in lipidic Aβ fibrils and reduces fibril formation by 75%, suggesting a potential therapeutic mechanism for Alzheimer's disease.

This study identifies two binding sites of the PET tracer MODAG-005 on lipidic α-synuclein fibrils, with the cavity site being more stable and selectively occupied under certain conditions.

The paper determines the structure of amyloid-β (Aβ40) fibrils bound to lipids using cryo-EM, showing lipid binding and potential relevance to Alzheimer's disease pathogenesis.

The paper presents cryo-EM structures of Aβ fibrils from Alzheimer's disease mouse models and compares them to human fibrils.

The paper presents six atomic structures of α-synuclein fibrils in the presence of phospholipids, revealing how phospholipids influence fibril morphology and lipid interactions.

This study compares α-synuclein fibril structures from Parkinson's disease and Multiple System Atrophy patients, showing differences in their quaternary arrangement and effects on oligodendroglial cells.