V. Smirnovas

S100A9 Inhibits and Redirects Prion Protein 89-230 Fragment Amyloid Aggregation

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

Liquid-liquid Phase Separation of Alpha-synuclein Increases the Structural Variability of Fibrils Formed during Amyloid 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.

Formation of amyloid fibrils by the regulatory 14-3-3ζ protein

This study investigates the formation of amyloid fibrils by the 14-3-3ζ protein using bioinformatics and structural analysis methods.

dGAE(297-391) tau fragment promotes formation of CTE-like full-length tau filaments

The paper shows that the dGAE tau fragment seeds the formation of CTE-like full-length tau filaments in vitro.

Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses

The paper investigates the co-aggregation of S100A9 and Aβ42 amyloids using CDMS, microscopy, and kinetic analysis, revealing templating of S100A9 fibrils on Aβ42 surfaces.