{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ma J"],"funding":["NCI NIH HHS","National Institutes of Health","NIH HHS"],"pagination":["67-74"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6350774"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["189"],"pubmed_abstract":["Aberrant core fucosylation of proteins has been linked to liver diseases. In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3). To minimize variability associated with the preparatory steps, the analysis was performed without enrichment of glycopeptides or fractionation of serum besides the nanoRP chromatography. Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow. We find increased core fu"],"journal":["Journal of proteomics"],"pubmed_title":["Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM."],"pmcid":["PMC6350774"],"funding_grant_id":["UO1 CA168926","RO1 CA135069","R01 CA135069","P30 CA051008","U01 CA168926","U01 CA230692","S10 OD023557"],"pubmed_authors":["Sanda M","Wei R","Ma J","Zhang L","Goldman R"],"additional_accession":[]},"is_claimable":false,"name":"Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.","description":"Aberrant core fucosylation of proteins has been linked to liver diseases. In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3). To minimize variability associated with the preparatory steps, the analysis was performed without enrichment of glycopeptides or fractionation of serum besides the nanoRP chromatography. Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow. We find increased core fu","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Oct","modification":"2026-04-15T23:40:56.719Z","creation":"2019-03-26T22:42:01Z"},"accession":"S-EPMC6350774","cross_references":{"pubmed":["29427759"],"doi":["10.1016/j.jprot.2018.02.003"]}}