Vladimir V. Egorov

This study investigates peptide fibrils as vaccine candidates using an Ebola virus fragment, showing they induce immune response without toxicity.

This study shows that recombinant alpha-synuclein can form different fibril types under the same conditions, and these fibrils can act as seeds to produce similar fibrils.

This study investigates how an amyloidogenic peptide binds to DNA, showing its structural interactions and effects on DNA function.

The paper predicts and validates that mangiferin inhibits transthyretin fibrillogenesis using in silico docking and in vitro assays.

The paper investigates how an influenza NS1 peptide interacts with TCR intramembrane domains to suppress immune responses using structural and biophysical methods.

The paper analyzes the primary structure of the NSP7 protein to identify potential amyloidogenic determinants and shows that synthesized peptides can form amyloid-like fibrils in vitro.

This study shows that influenza A NS1 protein can form amyloid-like fibrils in vitro, with structural changes detected by proteolysis and mass spectrometry.