Kamilė Mikalauskaitė

This study shows that prion proteins and S100A9 form heterotypic condensates, enhancing their aggregation and amyloid formation under molecular crowding conditions.

This study investigates how S100A9 and alpha-synuclein form heterotypic droplets through LLPS and how this affects alpha-synuclein aggregation and fibril stability.

This study investigates how different fluorescent labels affect alpha-synuclein condensate formation during liquid-liquid phase separation, finding label type and concentration influence droplet size and aggregation.

This study compares alpha-synuclein aggregation under conditions that promote or negate liquid-liquid phase separation, showing that phase separation leads to more structurally variable and toxic fibrils.

This study investigates how S100A9 interacts with prion protein 89-230 fragment, showing it modulates aggregation pathways and inhibits nucleation.