{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lopes M"],"funding":["Crohn's and Colitis Foundation of America","National Institute of Allergy and Infectious Diseases","Eunice Kennedy Shriver National Institute of Child Health and Human Development","NICHD NIH HHS","NIAID NIH HHS","NHLBI NIH HHS","National Cancer Institute","NCI NIH HHS"],"pagination":["5405-5420"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11932154"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(12)"],"pubmed_abstract":["The eukaryotic genome is packaged around histone proteins, which are subject to a myriad of post-translational modifications. By controlling DNA accessibility and the recruitment of protein complexes that mediate chromatin-related processes, these modifications constitute a key mechanism of epigenetic regulation. Since mass spectrometry can easily distinguish between these different modifications, it has become an essential technique in deciphering the histone code. Although robust LC-MS/MS methods are available to analyze modifications on the histone N-terminal tails, routine methods for characterizing ubiquitin marks on histone C-terminal regions, especially H2AK119ub, are less robust. Here, we report the development of a simple workflow for the detection and improved quantification of t"],"journal":["Journal of proteome research"],"pubmed_title":["Optimized and Robust Workflow for Quantifying the Canonical Histone Ubiquitination Marks H2AK119ub and H2BK120ub by LC-MS/MS."],"pmcid":["PMC11932154"],"funding_grant_id":["T32CA009140","R01 HL177113","R01 HD106051","R01HD106051","T32 CA009140","P01 CA196539","P01CA196539","RFA 598467","R01AI118891","R01 AI118891"],"pubmed_authors":["Lopes M","Lund PJ","Garcia BA"],"additional_accession":[]},"is_claimable":false,"name":"Optimized and Robust Workflow for Quantifying the Canonical Histone Ubiquitination Marks H2AK119ub and H2BK120ub by LC-MS/MS.","description":"The eukaryotic genome is packaged around histone proteins, which are subject to a myriad of post-translational modifications. By controlling DNA accessibility and the recruitment of protein complexes that mediate chromatin-related processes, these modifications constitute a key mechanism of epigenetic regulation. Since mass spectrometry can easily distinguish between these different modifications, it has become an essential technique in deciphering the histone code. Although robust LC-MS/MS methods are available to analyze modifications on the histone N-terminal tails, routine methods for characterizing ubiquitin marks on histone C-terminal regions, especially H2AK119ub, are less robust. Here, we report the development of a simple workflow for the detection and improved quantification of t","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2026-06-01T14:44:19.119Z","creation":"2025-07-05T03:05:26.838Z"},"accession":"S-EPMC11932154","cross_references":{"pubmed":["39556659"],"doi":["10.1021/acs.jproteome.4c00519"]}}