{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14(1)"],"submitter":["Palollathil A"],"pubmed_abstract":["<h4>Background</h4>Fibroblast growth factor receptors (FGFRs) play a crucial role in tissue homeostasis and organ development by regulating cellular processes, including proliferation, differentiation, and survival. Dysregulation of FGFRs contributes to developmental disorders and carcinogenesis. As membrane-bound receptors, they represent promising targets for therapeutic intervention and drug development.<h4>Methods</h4>This study employed a systematic in silico analysis of publicly available phosphoproteomics datasets to provide a comprehensive overview of the phosphorylation regulatory network of the FGFR family.<h4>Results</h4>We identified predominant phosphosites in FGFR1-4 that exhibited differential abundance across diverse experimental conditions, specifically, Y653 in FGFR1; S45"],"journal":["Proteomes"],"pagination":["8"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12922108"],"repository":["biostudies-literature"],"pubmed_title":["Proteome-Wide Analysis of Functional Phosphosites in the FGFR Family of Proteins: Insights from Large-Scale Phosphoproteomic Analysis."],"pmcid":["PMC12922108"],"pubmed_authors":["Sambreena A","Basthikoppa Shivamurthy P","Poojari TR","Perunelly Gopalakrishnan A","Palollathil A","Mahin A","Raju R"],"additional_accession":[]},"is_claimable":false,"name":"Proteome-Wide Analysis of Functional Phosphosites in the FGFR Family of Proteins: Insights from Large-Scale Phosphoproteomic Analysis.","description":"<h4>Background</h4>Fibroblast growth factor receptors (FGFRs) play a crucial role in tissue homeostasis and organ development by regulating cellular processes, including proliferation, differentiation, and survival. Dysregulation of FGFRs contributes to developmental disorders and carcinogenesis. As membrane-bound receptors, they represent promising targets for therapeutic intervention and drug development.<h4>Methods</h4>This study employed a systematic in silico analysis of publicly available phosphoproteomics datasets to provide a comprehensive overview of the phosphorylation regulatory network of the FGFR family.<h4>Results</h4>We identified predominant phosphosites in FGFR1-4 that exhibited differential abundance across diverse experimental conditions, specifically, Y653 in FGFR1; S45","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Feb","modification":"2026-07-09T11:43:20.617Z","creation":"2026-07-09T10:55:39.767Z"},"accession":"S-EPMC12922108","cross_references":{"pubmed":["41718090"],"doi":["10.3390/proteomes14010008"]}}