{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chen Y"],"funding":["National Natural Science Foundation of China"],"pagination":["1320-1324"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9627732"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["3(11)"],"pubmed_abstract":["Post-translational modifications (PTMs) play important roles in modulating the biological functions of proteins. Stoichiometry, which quantifies the modification percentage, is a critical factor for any given PTM. In this work, we developed a chemoproteomic strategy called \"STO-MS\" to systematically quantify the PTM stoichiometry in complex biological samples. This strategy employs a resolvable mass tag to differentiate proteoforms with different numbers of modifications and utilizes liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS) techniques to measure PTM stoichiometry at the proteomic level. As a proof-of-concept, we successfully determined the stoichiometry of 197 proteins modified by 4-hydroxynonenal (HNE), a well-characterized lipid-derived electrophile and biom"],"journal":["RSC chemical biology"],"pubmed_title":["Quantitative profiling of PTM stoichiometry by resolvable mass tags."],"pmcid":["PMC9627732"],"funding_grant_id":["91953109","21925701","92153301"],"pubmed_authors":["Liu Y","Li Y","Quan B","Wang C","Chen Y","Qin W"],"additional_accession":[]},"is_claimable":false,"name":"Quantitative profiling of PTM stoichiometry by resolvable mass tags.","description":"Post-translational modifications (PTMs) play important roles in modulating the biological functions of proteins. Stoichiometry, which quantifies the modification percentage, is a critical factor for any given PTM. In this work, we developed a chemoproteomic strategy called \"STO-MS\" to systematically quantify the PTM stoichiometry in complex biological samples. This strategy employs a resolvable mass tag to differentiate proteoforms with different numbers of modifications and utilizes liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS) techniques to measure PTM stoichiometry at the proteomic level. As a proof-of-concept, we successfully determined the stoichiometry of 197 proteins modified by 4-hydroxynonenal (HNE), a well-characterized lipid-derived electrophile and biom","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2025-04-21T23:35:16.595Z","creation":"2025-04-05T19:11:21.284Z"},"accession":"S-EPMC9627732","cross_references":{"pubmed":["36349223"],"doi":["10.1039/d2cb00179a"]}}