Mantas Žiaunys

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

This study investigates the phase separation and amyloid aggregation properties of 14-3-3 protein isoforms, finding that some forms can accelerate α-synuclein aggregation and form heterotypical droplets with α-synuclein.

This study shows that artificial cerebrospinal fluid (aCSF) forms distinct aSyn fibrils with unique structural features that change when key CSF components are removed.

This study investigates the calcium-dependent interactions and amyloid co-aggregation of S100A1 and S100A8 proteins, revealing their aggregation behavior is regulated by calcium ion concentrations.

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.