{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Li X"],"funding":["NCRR NIH HHS","NIGMS NIH HHS"],"pagination":["1982-5"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3520067"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["134(4)"],"pubmed_abstract":["Post-translational modifications (PTMs) (e.g., acetylation, methylation, and phosphorylation) play crucial roles in regulating the diverse protein-protein interactions involved in essentially every cellular process. While significant progress has been made to detect PTMs, profiling protein-protein interactions mediated by these PTMs remains a challenge. Here, we report a method that combines a photo-cross-linking strategy with stable isotope labeling in cell culture (SILAC)-based quantitative mass spectrometry to identify PTM-dependent protein-protein interactions. To develop and apply this approach, we focused on trimethylated lysine-4 at the histone H3 N-terminus (H3K4Me(3)), a PTM linked to actively transcribed gene promoters. Our approach identified proteins previously known to recogni"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Quantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions."],"pmcid":["PMC3520067"],"funding_grant_id":["R01 GM098579-01","RR00862","R01 GM098579","R01 GM098579-02","GM98579"],"pubmed_authors":["Li X","Li Y","Chait BT","Kapoor TM","Molloy KR","Foley EA"],"additional_accession":[]},"is_claimable":false,"name":"Quantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions.","description":"Post-translational modifications (PTMs) (e.g., acetylation, methylation, and phosphorylation) play crucial roles in regulating the diverse protein-protein interactions involved in essentially every cellular process. While significant progress has been made to detect PTMs, profiling protein-protein interactions mediated by these PTMs remains a challenge. Here, we report a method that combines a photo-cross-linking strategy with stable isotope labeling in cell culture (SILAC)-based quantitative mass spectrometry to identify PTM-dependent protein-protein interactions. To develop and apply this approach, we focused on trimethylated lysine-4 at the histone H3 N-terminus (H3K4Me(3)), a PTM linked to actively transcribed gene promoters. Our approach identified proteins previously known to recogni","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Feb","modification":"2025-04-26T10:45:10.206Z","creation":"2019-03-27T01:01:42Z"},"accession":"S-EPMC3520067","cross_references":{"pubmed":["22239320"],"doi":["10.1021/ja210528v"]}}