Stephanie A. Moquin

This study investigates how the two active sites of SARS-CoV-2 Mpro communicate and cooperate in catalysis using enzymatic assays, crystal structures, and engineered mutations.

This study investigates drug resistance mechanisms in SARS-CoV-2 Mpro caused by E166 mutations and their compensation by L50F, revealing structural and functional impacts on inhibitor binding and catalytic efficiency.

This study identifies how NITD-688 inhibits dengue virus by binding NS4B and disrupting its interaction with NS3, reducing viral replication.

This study identifies hyperactive mutations in SARS-CoV-2 Mpro that increase enzyme activity and contribute to drug resistance, finding them more prevalent than binding-reducing mutations.

The paper identifies resistance mutations in SARS-CoV-2 main protease against nirmatrelvir and ensitrelvir using yeast screens, finding cross-resistant mutations and reduced enzyme function.

The paper performs a comprehensive mutational scan of SARS-CoV-2 Mpro to identify resistance mechanisms and guide inhibitor design.