{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Meng Q"],"funding":["Hunan Agricultural University,China","Hunan Agricultural University"],"pagination":["307"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12305901"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(1)"],"pubmed_abstract":["<h4>Background</h4>Baylisascaris procyonis is an intestinal ascarid worm that parasitizes in raccoons and causes fatal neural, visceral, and ocular larva migrans in humans. Phosphorylated proteins and protein kinases have been studied as vaccine and drug target candidates against parasitic infections. However, no data are available on protein phosphorylation in the raccoon roundworm.<h4>Methods</h4>In this study, the entire proteome of adult B. procyonis was enzymatically digested. Then, phosphopeptides were enriched using immobilized metal affinity chromatography (IMAC) and analyzed by liquid chromatography-mass spectrometry (LC-MS/MS).<h4>Results</h4>Our phosphoproteome analysis displayed 854 unique phosphorylation sites mapped to 450 proteins in B. procyonis (3308 phosphopeptides total)"],"journal":["Parasites & vectors"],"pubmed_title":["Protein phosphorylation networks in Baylisascaris procyonis revealed by phosphoproteomic analysis."],"pmcid":["PMC12305901"],"funding_grant_id":["2023XC011","2021KJC-JS223"],"pubmed_authors":["Liu X","Li Z","Tan X","Meng Q","Chen Z","Qiu Q","Chen S","Gong H","Liu W"],"additional_accession":[]},"is_claimable":false,"name":"Protein phosphorylation networks in Baylisascaris procyonis revealed by phosphoproteomic analysis.","description":"<h4>Background</h4>Baylisascaris procyonis is an intestinal ascarid worm that parasitizes in raccoons and causes fatal neural, visceral, and ocular larva migrans in humans. Phosphorylated proteins and protein kinases have been studied as vaccine and drug target candidates against parasitic infections. However, no data are available on protein phosphorylation in the raccoon roundworm.<h4>Methods</h4>In this study, the entire proteome of adult B. procyonis was enzymatically digested. Then, phosphopeptides were enriched using immobilized metal affinity chromatography (IMAC) and analyzed by liquid chromatography-mass spectrometry (LC-MS/MS).<h4>Results</h4>Our phosphoproteome analysis displayed 854 unique phosphorylation sites mapped to 450 proteins in B. procyonis (3308 phosphopeptides total)","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jul","modification":"2026-03-16T09:10:50.687Z","creation":"2025-08-15T03:06:52.566Z"},"accession":"S-EPMC12305901","cross_references":{"pubmed":["40722118"],"doi":["10.1186/s13071-025-06949-y"]}}