Time-resolved phosphoproteomics and thermal proteome profiling reveal the Ca²⁺-responsive proteome of the model apicomplexan Taxoplasma gondii, identifying PP1 as a Ca²⁺-responsive enzyme that regulates Ca²⁺ uptake to promote parasite motility.

An approachable framework for the scalable implementation of proteome-wide thermal shift assays to assess drug mechanisms of action.

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.

Repurposing of a drug designed for pain relief can quickly and reversibly slow biochemical and metabolic activities in cells and organs and could facilitate organ transplantation and prevent tissue injury.

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.

A chemically unstable ostrich eggshell peptide survives for at least 3.8 million years at the equator, stabilized by strong mineral interactions.

Thermodynamic, kinetic, and dynamic analyses as well as solubility proteome profiling reveal that influenza A virus liquid inclusions may be selectively hardened with promising antiviral activity.

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.

Small molecule proteostasis regulators that activate the unfolded protein response transcription factor ATF6 reduce the secretion of amyloid disease-associated proteins.

The E2F/Dp transcription factors, which are key cell cycle regulators, can also mediate the regulation of carbohydrate metabolism in larva by controlling both systemic trehalose homeostasis and fat storage.