{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9(1)"],"submitter":["Boersema PJ"],"pubmed_abstract":["Several mass spectrometry-based assays have emerged for the quantitative profiling of cellular tyrosine phosphorylation. Ideally, these methods should reveal the exact sites of tyrosine phosphorylation, be quantitative, and not be cost-prohibitive. The latter is often an issue as typically several milligrams of (stable isotope-labeled) starting protein material are required to enable the detection of low abundance phosphotyrosine peptides. Here, we adopted and refined a peptidecentric immunoaffinity purification approach for the quantitative analysis of tyrosine phosphorylation by combining it with a cost-effective stable isotope dimethyl labeling method. We were able to identify by mass spectrometry, using just two LC-MS/MS runs, more than 1100 unique non-redundant phosphopeptides in HeLa"],"journal":["Molecular & cellular proteomics : MCP"],"pagination":["84-99"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2808269"],"repository":["biostudies-literature"],"pubmed_title":["In-depth qualitative and quantitative profiling of tyrosine phosphorylation using a combination of phosphopeptide immunoaffinity purification and stable isotope dimethyl labeling."],"pmcid":["PMC2808269"],"pubmed_authors":["den Hertog J","Foong LY","Philp R","Choo AB","van Breukelen B","Boekhorst J","Heck AJ","Ding VM","Snel B","Boersema PJ","Lemeer S"],"additional_accession":[]},"is_claimable":false,"name":"In-depth qualitative and quantitative profiling of tyrosine phosphorylation using a combination of phosphopeptide immunoaffinity purification and stable isotope dimethyl labeling.","description":"Several mass spectrometry-based assays have emerged for the quantitative profiling of cellular tyrosine phosphorylation. Ideally, these methods should reveal the exact sites of tyrosine phosphorylation, be quantitative, and not be cost-prohibitive. The latter is often an issue as typically several milligrams of (stable isotope-labeled) starting protein material are required to enable the detection of low abundance phosphotyrosine peptides. Here, we adopted and refined a peptidecentric immunoaffinity purification approach for the quantitative analysis of tyrosine phosphorylation by combining it with a cost-effective stable isotope dimethyl labeling method. We were able to identify by mass spectrometry, using just two LC-MS/MS runs, more than 1100 unique non-redundant phosphopeptides in HeLa","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Jan","modification":"2026-04-30T21:55:31.405Z","creation":"2026-04-07T16:22:53.961Z"},"accession":"S-EPMC2808269","cross_references":{"pubmed":["19770167"],"doi":["10.1074/mcp.m900291-mcp200","10.1074/mcp.M900291-MCP200"]}}