F. Trost

This paper resolves the mechanism of covalent bond formation in a LOV photoreceptor using time-resolved crystallography and spectroscopy, revealing a water-mediated proton transfer that accelerates the reaction by fourteen orders of magnitude.

This study identifies three natural compounds that inhibit SARS-CoV-2 PLpro by binding to the ISG15/Ub-S2 allosteric site, showing antiviral activity and potential for drug design.

The paper identifies 37 compounds binding to SARS-CoV-2 main protease through X-ray crystallography, with five non-peptidic compounds showing antiviral activity in cell-based assays.

The paper presents the crystal structure of SARS-CoV-2 main protease covalently bound to a metabolite of HEAT, revealing a pro-drug mechanism and potential for non-peptidic inhibitors.