{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Herring LE"],"funding":["NSF","NIH","NIGMS NIH HHS"],"pagination":["166-74"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4489695"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["988"],"pubmed_abstract":["Phosphorylation is an important post-translational modification that is involved in regulating many signaling pathways. Of particular interest are the growth factor mediated Ras and phosphoinositide 3-kinase (PI3K) signaling pathways which, if misregulated, can contribute to the progression of cancer. Phosphoproteomic methods have been developed to study regulation of signaling pathways; however, due to the low stoichiometry of phosphorylation, understanding these pathways is still a challenge. In this study, we have developed a multi-dimensional method incorporating electrostatic repulsion-hydrophilic interaction chromatography (ERLIC) with tandem IMAC/TiO2 enrichment for subsequent phosphopeptide identification by LC/MS/MS. We applied this method to PDGF-stimulated NIH 3T3 cells to provi"],"journal":["Journal of chromatography. B, Analytical technologies in the biomedical and life sciences"],"pubmed_title":["Development of a tandem affinity phosphoproteomic method with motif selectivity and its application in analysis of signal transduction networks."],"pmcid":["PMC4489695"],"funding_grant_id":["DBI-1126244","R01GM088987","R01 GM088987"],"pubmed_authors":["Goshe MB","Grant KG","Haugh JM","Blackburn K","Herring LE"],"additional_accession":[]},"is_claimable":false,"name":"Development of a tandem affinity phosphoproteomic method with motif selectivity and its application in analysis of signal transduction networks.","description":"Phosphorylation is an important post-translational modification that is involved in regulating many signaling pathways. Of particular interest are the growth factor mediated Ras and phosphoinositide 3-kinase (PI3K) signaling pathways which, if misregulated, can contribute to the progression of cancer. Phosphoproteomic methods have been developed to study regulation of signaling pathways; however, due to the low stoichiometry of phosphorylation, understanding these pathways is still a challenge. In this study, we have developed a multi-dimensional method incorporating electrostatic repulsion-hydrophilic interaction chromatography (ERLIC) with tandem IMAC/TiO2 enrichment for subsequent phosphopeptide identification by LC/MS/MS. We applied this method to PDGF-stimulated NIH 3T3 cells to provi","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Apr","modification":"2025-04-04T02:42:59.486Z","creation":"2019-03-27T01:54:24Z"},"accession":"S-EPMC4489695","cross_references":{"pubmed":["25777480"],"doi":["10.1016/j.jchromb.2015.02.017"]}}