Targeted therapies induce an aberrant fucosylation of complex tumor secretomes stimulating the expansion of minority drug-resistant clones and promoting therapy resistance.

Plasmodium falciparum aminopeptidase PfA-M17 is essential to parasite survival and plays a role in hemoglobin digestion, providing a rationale for further development of inhibitors against this enzyme.

When antiviral compounds target oligomeric assemblages, the formation of chimeric oligomers within cells can negate selection for naturally occurring drug-resistant variants.

Data-driven systems biology models of signaling predict cellular response to untested perturbations and can nominate drug combinations to overcome drug resistance in cancer cells.

A genome scale model of Brugia malayi metabolism illustrates a dynamic reliance on energy production pathways across its life cycle and identifies new drugs with experimentally supported anti-parasitic properties.

HPK1 is an important immuno-oncology drug target that may induce superior anti-tumor immunity through the multiple roles HPK1 may play at multiple steps of the cancer immunity cycle.

Novel small molecule inhibitors act against Neisseria including multi-drug resistant isolates by uniquely targeting RNR thereby enabling single pathogen therapy whilst sparing the microbiome.

Slow conformational changes after drug binding rationalize selectivity, affinity and long on-target residence time for kinase inhibitors.

M1 alanyl aminopeptidase is chemically validated as an attractive antimalarial target by confirming the on-target activity of a novel selective inhibitor using chemoproteomics and metabolomics-based drug target deconvolution approaches.

Solvent shift assays such as solvent proteome profiling and solvent-PISA are valuable tools for identifying protein-ligand interactions on a proteome-wide scale and can be used to determine drug target engagement, which should benefit future drug discovery efforts.