R. Hilgenfeld

This study investigates how the H172Y mutation in SARS-CoV-2 Mpro reduces nirmatrelvir efficacy using simulations, AI, and experiments, revealing structural and functional changes in the enzyme.

This study identifies redox regulation of SARS-CoV-2 Mpro and discovers antiviral reagents that mimic redox switching, suggesting new drug targets.

This study identifies ebselen derivatives as potent inhibitors of SARS-CoV-2 proteases PLpro and Mpro in vitro, with some compounds showing greater potency than ebselen itself.

The paper profiles SARS-CoV-2 main protease substrate specificity to design activity-based probes for imaging Mpro in patient samples.

The paper determines the X-ray structure of SARS-CoV-2 main protease and uses it to design alpha-ketoamide inhibitors with improved pharmacokinetic properties.

This study identifies alpha-ketoamides as broad-spectrum inhibitors effective against coronavirus and enterovirus proteases, with compounds showing low-micromolar activity in cell cultures.

The paper uses native mass spectrometry to analyze SARS-CoV polyprotein processing, revealing cleavage order and protein interactions in the nsp7-10 region.