Aspirin reshapes acetylomes in inflammatory and cancer cells via CoA-dependent and –independent

We used a deuterium-labeled aspirin (D-aspirin) together with mass spectrometry-based acetylomic analysis, termed “DAcMS”, to investigate the landscape of protein acetylation induced by aspirin. And we further demonstrated that aspirin acetylates proteins through both acetyl-CoA-dependent and -independent pathways, and the accessible lysine residues at the protein surface are major acetylation targets of aspirin.