{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lauc G"],"funding":["Medical Research Council","Chief Scientist Office","Wellcome Trust"],"pagination":["e1003225"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3561084"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(1)"],"pubmed_abstract":["Glycosylation of immunoglobulin G (IgG) influences IgG effector function by modulating binding to Fc receptors. To identify genetic loci associated with IgG glycosylation, we quantitated N-linked IgG glycans using two approaches. After isolating IgG from human plasma, we performed 77 quantitative measurements of N-glycosylation using ultra-performance liquid chromatography (UPLC) in 2,247 individuals from four European discovery populations. In parallel, we measured IgG N-glycans using MALDI-TOF mass spectrometry (MS) in a replication cohort of 1,848 Europeans. Meta-analysis of genome-wide association study (GWAS) results identified 9 genome-wide significant loci (P<2.27 × 10(-9)) in the discovery analysis and two of the same loci (B4GALT1 and MGAT3) in the replication cohort. Four loci co"],"journal":["PLoS genetics"],"pubmed_title":["Loci associated with N-glycosylation of human immunoglobulin G show pleiotropy with autoimmune diseases and haematological cancers."],"pmcid":["PMC3561084"],"funding_grant_id":["CZB/4/710","CZB/4/728","MC_PC_U127561128","095831"],"pubmed_authors":["Zgaga L","Uh HW","Deelder AM","Adamczyk B","Polasek O","Huffman JE","Kolcic I","Slagboom PE","Keser T","Beekman M","Ruhaak LR","Swann O","Wilson JF","Wuhrer M","Rudd PM","Scheijen B","van Leeuwen FN","de Craen AJ","Pucic M","Lukic IK","Gornik O","Wang W","Houwing-Duistermaat JJ","Hayward C","Zeng Q","Rudan I","McKeigue P","Hastie ND","Wright AF","Patrick AL","Novokmet M","Vitart V","Molokhia M","Muzinic A","Gyllensten U","Campbell H","Aulchenko Y","Kristic J","Lauc G"],"additional_accession":[]},"is_claimable":false,"name":"Loci associated with N-glycosylation of human immunoglobulin G show pleiotropy with autoimmune diseases and haematological cancers.","description":"Glycosylation of immunoglobulin G (IgG) influences IgG effector function by modulating binding to Fc receptors. To identify genetic loci associated with IgG glycosylation, we quantitated N-linked IgG glycans using two approaches. After isolating IgG from human plasma, we performed 77 quantitative measurements of N-glycosylation using ultra-performance liquid chromatography (UPLC) in 2,247 individuals from four European discovery populations. In parallel, we measured IgG N-glycans using MALDI-TOF mass spectrometry (MS) in a replication cohort of 1,848 Europeans. Meta-analysis of genome-wide association study (GWAS) results identified 9 genome-wide significant loci (P<2.27 × 10(-9)) in the discovery analysis and two of the same loci (B4GALT1 and MGAT3) in the replication cohort. Four loci co","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013","modification":"2026-04-08T04:19:05.006Z","creation":"2026-04-07T21:53:07.516Z"},"accession":"S-EPMC3561084","cross_references":{"pubmed":["23382691"],"doi":["10.1371/journal.pgen.1003225"]}}