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Thermal stabilization of proteins after ligand binding provides an efficient means to assess the binding of small molecules to proteins. We show here that in combination with quantitative mass spectrometry, the approach allows for the systematic survey of protein engagement by cellular metabolites and drugs. We profiled the targets of the drugs methotrexate and (S)-crizotinib and the metabolite 2'3'-cGAMP in intact cells and identified the 2'3'-cGAMP cognate transmembrane receptor STING, involved in immune signaling.

Original publication




Journal article


Nat Methods

Publication Date





1055 - 1057


Animals, Carrier Proteins, Cell Line, Cell Line, Tumor, Computational Biology, Crizotinib, Drug Design, Humans, Immune System, K562 Cells, Ligands, Mass Spectrometry, Methotrexate, Mice, Protein Binding, Protein Kinase Inhibitors, Proteome, Proteomics, Pyrazoles, Pyridines, Signal Transduction, Systems Biology, Temperature