Proteome-wide drug and metabolite interaction mapping by thermal-stability profiling

Abstract : 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.
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https://hal.umontpellier.fr/hal-02329771
Contributeur : Amandine Michel-Avella <>
Soumis le : mercredi 23 octobre 2019 - 16:39:50
Dernière modification le : jeudi 24 octobre 2019 - 01:33:50

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Kilian Huber, Karin Olek, André Müller, Chris Soon Heng Tan, Keiryn Bennett, et al.. Proteome-wide drug and metabolite interaction mapping by thermal-stability profiling. Nature Methods, Nature Publishing Group, 2015, 12 (11), pp.1055-1057. ⟨10.1038/nmeth.3590⟩. ⟨hal-02329771⟩

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