Matthias De Vleeschouwer

This study determines the cryo-EM structures of Aβ40 and medin fibrils in vitro, revealing polymorphic remodeling and mixed amyloid interactions.

This study shows N-glycosylation prevents protein aggregation by steric hindrance, especially in proteins prone to misfolding, using computational and biochemical analyses.

This study shows heterotypic interactions between Aβ APRs and homologous protein segments accelerate Aβ assembly, alter fibril morphology, and are enriched in AD plaques but not in mouse models.

The paper identifies MOAG-4/SERF as modifiers of amyloid formation through charge complementation, showing that charge interactions drive protein aggregation and toxicity.