Charline Giroud

The paper identifies fragment binders and mutationally intolerant sites in Zika virus NS2B-NS3 protease to develop resistance-resilient antiviral inhibitors.

This study identifies fragments binding to EV-D68 3C protease through crystallography and expands them into lead-like compounds, revealing novel binding modes and structural insights for drug design.

The paper identifies 75 fragments that bind to Coxsackievirus A16 2A protease, including 38 unique compounds in the active site, offering a path for broad-spectrum anti-enteroviral inhibitors.

This study uses high-throughput crystallographic fragment screening to identify 46 fragment binding poses on ZIKV NS3Hel, providing templates for antiviral drug design.