Christopher Fröhlich

This paper investigates the molecular mechanisms of collateral sensitivity in β-lactamase evolution, showing how specific mutations alter enzyme structure and drug resistance profiles.

This paper shows how evolution improves enzyme function by shifting the rate-limiting step from substrate binding to sub-state interconversion in β-lactamase OXA-48.

The paper identifies mutations in the enzyme MbaA that enhance c-di-GMP synthesis, promoting biofilm formation in Vibrio cholerae by disrupting polyamine regulation.

This study shows that β-lactamases from different Ambler classes confer cefiderocol resistance and can evolve to increase resistance through mutations.