Melissa M. Dix

TL;DR: A robust and versatile proteomic platform is described that enables direct visualization of the topography and magnitude of proteolytic events on a global scale and generates a proteome-wide map of proteological events induced by the intrinsic apoptotic pathway.

TL;DR: Activity-based profiling platforms enable both the discovery of cancer-relevant enzymes and selective pharmacological probes to perturb and characterize these proteins in tumour cells and can provide insight into the metabolic and signalling pathways that support cancer pathogenesis and illuminate new strategies for disease diagnosis and treatment.

TL;DR: This work uses activity-based protein profiling coupled with quantitative mass spectrometry to globally map the targets, both specific and non-specific, of covalent kinase inhibitors in human cells and shows that, when these windows are exceeded, rampant proteome-wide reactivity and kinase target-independent cell death conjointly occur.

TL;DR: A chemical proteomics strategy identifies DCAF16—a poorly characterized substrate recognition component of CUL4-DDB1 E3 ubiquitin ligases—as a target of electrophilic PROTACs that promote the nuclear-restricted degradation of proteins.

TL;DR: NR0B1 is designated as a druggable transcriptional regulator that supports NRF2-dependent lung cancers and small molecules that covalently target a conserved cysteine within the NR0B 1 protein interaction domain are identified.