Vytautas Smirnovas

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.