Martin Austin Walsh

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.

This study investigates how the P2' proline residue affects SARS-CoV-2 PLpro catalytic efficiency using molecular dynamics and substrate analysis.

xia2.multiplex merges multi-crystal data sets in macromolecular crystallography to improve data quality and facilitate analysis.

The paper models SARS-CoV-2 Mpro substrate and ligand binding to identify new inhibitor opportunities through computational analysis of binding interactions.

This study reports structural and functional insights into Mfd's role in DNA translocation and evolution, revealing its mechanism and implications for antimicrobial resistance.