Protein palmitoylation, also known as S-acylation, is a reversible post-translational modification in which fatty acids are covalently attached to cysteine residues via thioester bonds. To date, prote
Table S1. Proteins identified by mass spectrometry after enrichment of palmitoylated proteins by acylRAC after 0–60 min TNF incubation. The sample processing and data analysis is described in table. (
We report here the identification of substrates of the depalmitoylating enzyme PPT1 by quantitative mass spectrometry. We utilized a stringent two-step Acyl Resin-Assisted Capture (Acyl RAC) screen in
Given our laboratory interest in IFITM3 S-fatty-acylation and antiviral activity, we sought to directly characterize fatty acids that are covalently attached to the Cys residues of IFITM3. IFITM3 comp
