Sandra Röhm

This paper introduces kinetic fingerprints to evaluate KIT inhibitors, showing that residence time and dissociation rates predict clinical success and resistance.

The paper identifies inhibitor-induced kinase destabilization as a common phenomenon and reveals that it occurs through endogenous proteolytic mechanisms rather than classical ubiquitination.

This study develops a covalent LIMK1 inhibitor that selectively targets a unique cysteine, enabling isoform-specific studies of LIMK1 function.

The paper repurposes a benzoxazepinone scaffold originally designed for RIPK1 inhibition to develop a novel type-III LIMK1/2 inhibitor with high selectivity.

The paper assesses current chemical coverage of the human Reactome, finding that 3% of proteins are targeted by chemical probes, but they cover 53% of pathways due to pathway overlap.