S. K. Kapuganti

This study uses molecular dynamics simulations and experimental validation to show that the ZIKV NS1 beta-roll domain is intrinsically disordered and the beta-ladder domain is highly flexible.

This study identifies aggregation-prone regions in the Zika virus proteome using computational tools and experimental validation, showing several viral proteins can form amyloid-like fibrils.

This study investigates protein aggregation in SARS-CoV and SARS-CoV-2 proteomes, finding that several SARS-CoV-2 proteins form cytotoxic aggregates via a nucleation-dependent mechanism.

This study investigates the aggregation behavior of the P53 TAD2 domain (38-61) in isolation, showing it forms amyloid-like aggregates under acidic pH conditions.

This paper investigates how environmental factors affect the conformation of the C-terminal domain of the SARS-CoV-2 envelope protein, showing it transitions between disordered, membrane-bound, and amyloid states.