R. Hilgenfeld

Why is the Omicron main protease of SARS-CoV-2 less stable than its wild-type counterpart? A crystallographic, biophysical, and theoretical study of the free enzyme and its complex with inhibitor 13b-K

This study investigates why the Omicron variant's main protease is less stable than the wild-type by analyzing its structure, enzymatic activity, and biophysical properties.

An Integrative Approach to Dissect the Drug Resistance Mechanism of the H172Y Mutation of SARS-CoV-2 Main Protease

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.

Redox regulation of the SARS-CoV-2 main protease provides new opportunities for drug design

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

Ebselen derivatives are very potent dual inhibitors of SARS-CoV-2 proteases - PLpro and Mpro in in vitro studies

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.

Substrate specificity profiling of SARS-CoV-2 main protease enables design of activity-based probes for patient-sample imaging

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

X-ray Structure of Main Protease of the Novel Coronavirus SARS-CoV-2 Enables Design of α-Ketoamide Inhibitors

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.

Alpha-ketoamides as broad-spectrum inhibitors of coronavirus and enterovirus replication

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

Processing of the SARS-CoV pp1a/ab nsp7-10 region

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