PubMed:10704528 JSONTXT

{"project":"GlyCosmos6-UBERON","denotations":[{"id":"T1","span":{"begin":78,"end":84},"obj":"Body_part"},{"id":"T2","span":{"begin":114,"end":118},"obj":"Body_part"},{"id":"T3","span":{"begin":119,"end":126},"obj":"Body_part"},{"id":"T4","span":{"begin":160,"end":168},"obj":"Body_part"},{"id":"T5","span":{"begin":172,"end":190},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002416"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0002416"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0000483"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":675,"end":682},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":777,"end":784},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":993,"end":998},"obj":"https://glytoucan.org/Structures/Glycans/G00062MO"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":127,"end":135},"obj":"http://purl.bioontology.org/ontology/STY/T192"},{"id":"T2","span":{"begin":183,"end":190},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T1","span":{"begin":74,"end":77},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"NCBItxid:10114"},{"id":"A2","pred":"db_id","subj":"T1","obj":"NCBItxid:10116"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":675,"end":682},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":777,"end":784},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":993,"end":998},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00062MO"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":675,"end":682},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":777,"end":784},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":993,"end":998},"obj":"https://glytoucan.org/Structures/Glycans/G00062MO"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":85},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":86,"end":300},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":301,"end":408},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":409,"end":523},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":524,"end":601},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":602,"end":796},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":797,"end":860},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":861,"end":1032},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1033,"end":1170},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":85},"obj":"Sentence"},{"id":"T2","span":{"begin":86,"end":300},"obj":"Sentence"},{"id":"T3","span":{"begin":301,"end":408},"obj":"Sentence"},{"id":"T4","span":{"begin":409,"end":523},"obj":"Sentence"},{"id":"T5","span":{"begin":524,"end":601},"obj":"Sentence"},{"id":"T6","span":{"begin":602,"end":796},"obj":"Sentence"},{"id":"T7","span":{"begin":797,"end":860},"obj":"Sentence"},{"id":"T8","span":{"begin":861,"end":1032},"obj":"Sentence"},{"id":"T9","span":{"begin":1033,"end":1170},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":85},"obj":"Sentence"},{"id":"T2","span":{"begin":86,"end":300},"obj":"Sentence"},{"id":"T3","span":{"begin":301,"end":408},"obj":"Sentence"},{"id":"T4","span":{"begin":409,"end":523},"obj":"Sentence"},{"id":"T5","span":{"begin":524,"end":601},"obj":"Sentence"},{"id":"T6","span":{"begin":602,"end":796},"obj":"Sentence"},{"id":"T7","span":{"begin":797,"end":860},"obj":"Sentence"},{"id":"T8","span":{"begin":861,"end":1032},"obj":"Sentence"},{"id":"T9","span":{"begin":1033,"end":1170},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":78,"end":84},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T2","span":{"begin":153,"end":159},"obj":"http://purl.obolibrary.org/obo/MAT_0000484"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"GlyCosmos6-CLO","denotations":[{"id":"T1","span":{"begin":114,"end":118},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":172,"end":182},"obj":"http://purl.obolibrary.org/obo/CL_0000066"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":33,"end":49},"obj":"FMAID:196731"},{"id":"_T2","span":{"begin":33,"end":49},"obj":"FMAID:82742"},{"id":"_T3","span":{"begin":78,"end":84},"obj":"FMAID:7203"},{"id":"_T4","span":{"begin":78,"end":84},"obj":"FMAID:93681"},{"id":"_T5","span":{"begin":114,"end":126},"obj":"FMAID:212684"},{"id":"_T6","span":{"begin":114,"end":126},"obj":"FMAID:200942"},{"id":"_T7","span":{"begin":119,"end":126},"obj":"FMAID:50594"},{"id":"_T8","span":{"begin":119,"end":126},"obj":"FMAID:146300"},{"id":"_T9","span":{"begin":160,"end":168},"obj":"FMAID:50594"},{"id":"_T10","span":{"begin":160,"end":168},"obj":"FMAID:146300"},{"id":"_T11","span":{"begin":172,"end":190},"obj":"FMAID:97545"},{"id":"_T12","span":{"begin":183,"end":190},"obj":"FMAID:256050"},{"id":"_T13","span":{"begin":222,"end":237},"obj":"FMAID:214710"},{"id":"_T14","span":{"begin":391,"end":407},"obj":"FMAID:82742"},{"id":"_T15","span":{"begin":391,"end":407},"obj":"FMAID:196731"},{"id":"_T16","span":{"begin":556,"end":568},"obj":"FMAID:62925"},{"id":"_T17","span":{"begin":556,"end":568},"obj":"FMAID:167256"},{"id":"_T18","span":{"begin":675,"end":682},"obj":"FMAID:82801"},{"id":"_T19","span":{"begin":675,"end":682},"obj":"FMAID:196796"},{"id":"_T20","span":{"begin":777,"end":784},"obj":"FMAID:82801"},{"id":"_T21","span":{"begin":777,"end":784},"obj":"FMAID:196796"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":53,"end":60},"obj":"http://www.uniprot.org/uniprot/P98164"},{"id":"T2","span":{"begin":375,"end":382},"obj":"http://www.uniprot.org/uniprot/P98164"},{"id":"T3","span":{"begin":515,"end":522},"obj":"http://www.uniprot.org/uniprot/P98164"},{"id":"T4","span":{"begin":62,"end":67},"obj":"http://www.uniprot.org/uniprot/P98164"},{"id":"T5","span":{"begin":114,"end":135},"obj":"http://www.uniprot.org/uniprot/Q9UKJ1"},{"id":"T6","span":{"begin":114,"end":135},"obj":"http://www.uniprot.org/uniprot/Q9UKJ0"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":53,"end":60},"obj":"http://www.uniprot.org/uniprot/A2ARV4"},{"id":"T2","span":{"begin":375,"end":382},"obj":"http://www.uniprot.org/uniprot/A2ARV4"},{"id":"T3","span":{"begin":515,"end":522},"obj":"http://www.uniprot.org/uniprot/A2ARV4"},{"id":"T4","span":{"begin":62,"end":67},"obj":"http://www.uniprot.org/uniprot/A2ARV4"},{"id":"T5","span":{"begin":153,"end":159},"obj":"http://www.uniprot.org/uniprot/P28352"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":183,"end":190},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T2","span":{"begin":572,"end":587},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/691256"},{"id":"T3","span":{"begin":572,"end":587},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1113441"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":588,"end":600},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T2","span":{"begin":927,"end":937},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T3","span":{"begin":1110,"end":1122},"obj":"http://purl.obolibrary.org/obo/GO_0036065"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":210,"end":217},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":210,"end":217},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T3","span":{"begin":210,"end":217},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T4","span":{"begin":210,"end":217},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T5","span":{"begin":292,"end":299},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":114,"end":118},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":114,"end":126},"obj":"http://purl.obolibrary.org/obo/GO_0009986"},{"id":"T3","span":{"begin":1105,"end":1109},"obj":"http://purl.obolibrary.org/obo/GO_0019013"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":78,"end":84},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"T2","span":{"begin":183,"end":190},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":435,"end":453},"obj":"http://edamontology.org/topic_3520"},{"id":"T2","span":{"begin":435,"end":453},"obj":"http://edamontology.org/topic_0134"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":253,"end":265},"obj":"http://edamontology.org/data_0883"},{"id":"T2","span":{"begin":270,"end":282},"obj":"http://edamontology.org/operation_0004"},{"id":"T3","span":{"begin":318,"end":324},"obj":"http://edamontology.org/data_2048"},{"id":"T4","span":{"begin":344,"end":354},"obj":"http://edamontology.org/data_0883"},{"id":"T5","span":{"begin":435,"end":453},"obj":"http://edamontology.org/data_2536"},{"id":"T6","span":{"begin":435,"end":462},"obj":"http://edamontology.org/operation_3214"},{"id":"T7","span":{"begin":454,"end":462},"obj":"http://edamontology.org/operation_2945"},{"id":"T8","span":{"begin":484,"end":494},"obj":"http://edamontology.org/data_0883"},{"id":"T9","span":{"begin":622,"end":632},"obj":"http://edamontology.org/data_0842"},{"id":"T10","span":{"begin":622,"end":632},"obj":"http://edamontology.org/data_2611"},{"id":"T11","span":{"begin":683,"end":693},"obj":"http://edamontology.org/data_0883"},{"id":"T12","span":{"begin":711,"end":721},"obj":"http://edamontology.org/data_0883"},{"id":"T13","span":{"begin":736,"end":746},"obj":"http://edamontology.org/data_0883"},{"id":"T14","span":{"begin":785,"end":795},"obj":"http://edamontology.org/data_0883"},{"id":"T15","span":{"begin":1046,"end":1056},"obj":"http://edamontology.org/data_0883"},{"id":"T16","span":{"begin":1162,"end":1169},"obj":"http://edamontology.org/data_1756"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":861,"end":867},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":1155,"end":1161},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":78,"end":84},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T2","span":{"begin":153,"end":159},"obj":"http://purl.obolibrary.org/obo/MAT_0000484"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":502,"end":511},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T2","span":{"begin":612,"end":621},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T3","span":{"begin":670,"end":682},"obj":"http://rdf.glycoinfo.org/glycan/G00028MO"},{"id":"T4","span":{"begin":772,"end":784},"obj":"http://rdf.glycoinfo.org/glycan/G00028MO"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"GlycoGenes","denotations":[{"id":"PD-GlycoGenes-B_T1","span":{"begin":108,"end":113},"obj":"GGDB:LARGE"}],"namespaces":[{"prefix":"GGDB","uri":"http://acgg.asia/ggdb2/"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G26693XF\""},{"id":"GlycanIUPAC_T2","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G26693XF\""},{"id":"GlycanIUPAC_T3","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G01864SU\""},{"id":"GlycanIUPAC_T4","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G01864SU\""},{"id":"GlycanIUPAC_T5","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G17605FD\""},{"id":"GlycanIUPAC_T6","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G17605FD\""},{"id":"GlycanIUPAC_T7","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G41950LU\""},{"id":"GlycanIUPAC_T8","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G41950LU\""},{"id":"GlycanIUPAC_T9","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G57195RJ\""},{"id":"GlycanIUPAC_T10","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G57195RJ\""},{"id":"GlycanIUPAC_T11","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G85391SA\""},{"id":"GlycanIUPAC_T12","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G85391SA\""},{"id":"GlycanIUPAC_T13","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G89565QL\""},{"id":"GlycanIUPAC_T14","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G89565QL\""},{"id":"GlycanIUPAC_T15","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G80869MR\""},{"id":"GlycanIUPAC_T16","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G80869MR\""},{"id":"GlycanIUPAC_T17","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G55978NL\""},{"id":"GlycanIUPAC_T18","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G55978NL\""},{"id":"GlycanIUPAC_T19","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G54644LT\""},{"id":"GlycanIUPAC_T20","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G54644LT\""},{"id":"GlycanIUPAC_T21","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G25694UG\""},{"id":"GlycanIUPAC_T22","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G25694UG\""},{"id":"GlycanIUPAC_T23","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G25126RB\""},{"id":"GlycanIUPAC_T24","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G25126RB\""},{"id":"GlycanIUPAC_T25","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G51848AD\""},{"id":"GlycanIUPAC_T26","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G51848AD\""},{"id":"GlycanIUPAC_T27","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G94667GM\""},{"id":"GlycanIUPAC_T28","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G94667GM\""},{"id":"GlycanIUPAC_T29","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G30124BO\""},{"id":"GlycanIUPAC_T30","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G30124BO\""},{"id":"GlycanIUPAC_T31","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G82777EZ\""},{"id":"GlycanIUPAC_T32","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G82777EZ\""},{"id":"GlycanIUPAC_T33","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G10151YZ\""},{"id":"GlycanIUPAC_T34","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G10151YZ\""},{"id":"GlycanIUPAC_T35","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G17585ZM\""},{"id":"GlycanIUPAC_T36","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G17585ZM\""},{"id":"GlycanIUPAC_T37","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G04411CJ\""},{"id":"GlycanIUPAC_T38","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G04411CJ\""},{"id":"GlycanIUPAC_T39","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G38254HJ\""},{"id":"GlycanIUPAC_T40","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G38254HJ\""},{"id":"GlycanIUPAC_T41","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G75188FS\""},{"id":"GlycanIUPAC_T42","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G75188FS\""},{"id":"GlycanIUPAC_T43","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G70374VG\""},{"id":"GlycanIUPAC_T44","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G70374VG\""},{"id":"GlycanIUPAC_T45","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G45176LJ\""},{"id":"GlycanIUPAC_T46","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G45176LJ\""},{"id":"GlycanIUPAC_T47","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G30874VW\""},{"id":"GlycanIUPAC_T48","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G30874VW\""},{"id":"GlycanIUPAC_T49","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G69333MI\""},{"id":"GlycanIUPAC_T50","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G69333MI\""},{"id":"GlycanIUPAC_T51","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G10676XO\""},{"id":"GlycanIUPAC_T52","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G10676XO\""},{"id":"GlycanIUPAC_T53","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G14843DJ\""},{"id":"GlycanIUPAC_T54","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G14843DJ\""},{"id":"GlycanIUPAC_T55","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G47546FR\""},{"id":"GlycanIUPAC_T56","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G47546FR\""},{"id":"GlycanIUPAC_T57","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G73695ZM\""},{"id":"GlycanIUPAC_T58","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G73695ZM\""},{"id":"GlycanIUPAC_T59","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G31923TJ\""},{"id":"GlycanIUPAC_T60","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G31923TJ\""},{"id":"GlycanIUPAC_T61","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G60519EP\""},{"id":"GlycanIUPAC_T62","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G60519EP\""},{"id":"GlycanIUPAC_T63","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G07933IA\""},{"id":"GlycanIUPAC_T64","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G07933IA\""},{"id":"GlycanIUPAC_T65","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G40745NH\""},{"id":"GlycanIUPAC_T66","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G40745NH\""},{"id":"GlycanIUPAC_T67","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G54496YV\""},{"id":"GlycanIUPAC_T68","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G54496YV\""},{"id":"GlycanIUPAC_T69","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T70","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T71","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T72","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T73","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T74","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T75","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T76","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T77","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T78","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T79","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T80","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T81","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T82","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T83","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T84","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T85","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T86","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T87","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T88","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T89","span":{"begin":861,"end":867},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""},{"id":"GlycanIUPAC_T90","span":{"begin":1155,"end":1161},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":183,"end":190},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":78,"end":84},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"}],"text":"Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney.\nMegalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galbeta1-4GlcNAc (LacNAc), NeuAcalpha2-6Galbeta1-4GlcNAc (sialylated LacNAc), GalNAcbeta1-4[NeuAcalpha2-3]Galbeta1-4GlcNAc (Sd(a)) and Galalpha1-3Galbeta1-4GlcNAc. Most complex structures are characterized by the presence of (alpha1,6)-core fucosylation and the presence of a bisecting GlcNAc residue."}