PubMed:8490243 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":478,"end":497},"obj":"https://glytoucan.org/Structures/Glycans/G64581RP"},{"id":"T2","span":{"begin":516,"end":522},"obj":"https://glytoucan.org/Structures/Glycans/G82576YO"},{"id":"T3","span":{"begin":537,"end":544},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T4","span":{"begin":549,"end":558},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T5","span":{"begin":549,"end":558},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T6","span":{"begin":814,"end":820},"obj":"https://glytoucan.org/Structures/Glycans/G82576YO"},{"id":"T7","span":{"begin":1033,"end":1039},"obj":"https://glytoucan.org/Structures/Glycans/G82576YO"}],"text":"Cell differentiation in Dictyostelium discoideum controls assembly of protein-linked glycans.\nThe prestalk and prespore cells from the Dictyostelium discoideum multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc alpha-linked to N-acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by beta-elimination and include a glycoantigen dependent on the modB genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":478,"end":497},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":516,"end":522},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":537,"end":544},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":549,"end":558},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":814,"end":820},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":1033,"end":1039},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G64581RP"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G82576YO"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A5","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G82576YO"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G82576YO"}],"text":"Cell differentiation in Dictyostelium discoideum controls assembly of protein-linked glycans.\nThe prestalk and prespore cells from the Dictyostelium discoideum multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc alpha-linked to N-acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by beta-elimination and include a glycoantigen dependent on the modB genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":478,"end":497},"obj":"https://glytoucan.org/Structures/Glycans/G64581RP"},{"id":"T2","span":{"begin":516,"end":522},"obj":"https://glytoucan.org/Structures/Glycans/G82576YO"},{"id":"T3","span":{"begin":537,"end":544},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T4","span":{"begin":549,"end":558},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T5","span":{"begin":549,"end":558},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T6","span":{"begin":814,"end":820},"obj":"https://glytoucan.org/Structures/Glycans/G82576YO"},{"id":"T7","span":{"begin":1033,"end":1039},"obj":"https://glytoucan.org/Structures/Glycans/G82576YO"}],"text":"Cell differentiation in Dictyostelium discoideum controls assembly of protein-linked glycans.\nThe prestalk and prespore cells from the Dictyostelium discoideum multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc alpha-linked to N-acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by beta-elimination and include a glycoantigen dependent on the modB genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":70,"end":77},"obj":"FMAID:165447"},{"id":"_T2","span":{"begin":70,"end":77},"obj":"FMAID:67257"},{"id":"_T3","span":{"begin":120,"end":125},"obj":"FMAID:68646"},{"id":"_T4","span":{"begin":120,"end":125},"obj":"FMAID:169002"},{"id":"_T5","span":{"begin":222,"end":237},"obj":"FMAID:196776"},{"id":"_T6","span":{"begin":222,"end":237},"obj":"FMAID:82782"},{"id":"_T7","span":{"begin":248,"end":253},"obj":"FMAID:68646"},{"id":"_T8","span":{"begin":248,"end":253},"obj":"FMAID:169002"},{"id":"_T9","span":{"begin":297,"end":302},"obj":"FMAID:169002"},{"id":"_T10","span":{"begin":297,"end":302},"obj":"FMAID:68646"},{"id":"_T11","span":{"begin":400,"end":405},"obj":"FMAID:68646"},{"id":"_T12","span":{"begin":400,"end":405},"obj":"FMAID:169002"},{"id":"_T13","span":{"begin":478,"end":497},"obj":"FMAID:196781"},{"id":"_T14","span":{"begin":478,"end":497},"obj":"FMAID:82787"},{"id":"_T15","span":{"begin":516,"end":522},"obj":"FMAID:196784"},{"id":"_T16","span":{"begin":516,"end":522},"obj":"FMAID:82790"},{"id":"_T17","span":{"begin":524,"end":535},"obj":"FMAID:196792"},{"id":"_T18","span":{"begin":524,"end":535},"obj":"FMAID:82797"},{"id":"_T19","span":{"begin":537,"end":544},"obj":"FMAID:196796"},{"id":"_T20","span":{"begin":537,"end":544},"obj":"FMAID:82801"},{"id":"_T21","span":{"begin":549,"end":558},"obj":"FMAID:82794"},{"id":"_T22","span":{"begin":549,"end":558},"obj":"FMAID:196789"},{"id":"_T23","span":{"begin":588,"end":603},"obj":"FMAID:82782"},{"id":"_T24","span":{"begin":588,"end":603},"obj":"FMAID:196776"},{"id":"_T25","span":{"begin":641,"end":646},"obj":"FMAID:169002"},{"id":"_T26","span":{"begin":641,"end":646},"obj":"FMAID:68646"},{"id":"_T27","span":{"begin":653,"end":664},"obj":"FMAID:82797"},{"id":"_T28","span":{"begin":653,"end":664},"obj":"FMAID:196792"},{"id":"_T29","span":{"begin":674,"end":689},"obj":"FMAID:196776"},{"id":"_T30","span":{"begin":674,"end":689},"obj":"FMAID:82782"},{"id":"_T31","span":{"begin":814,"end":820},"obj":"FMAID:82790"},{"id":"_T32","span":{"begin":814,"end":820},"obj":"FMAID:196784"},{"id":"_T33","span":{"begin":830,"end":845},"obj":"FMAID:196776"},{"id":"_T34","span":{"begin":830,"end":845},"obj":"FMAID:82782"},{"id":"_T35","span":{"begin":885,"end":901},"obj":"FMAID:82742"},{"id":"_T36","span":{"begin":885,"end":901},"obj":"FMAID:196731"},{"id":"_T37","span":{"begin":938,"end":945},"obj":"FMAID:165447"},{"id":"_T38","span":{"begin":938,"end":945},"obj":"FMAID:67257"},{"id":"_T39","span":{"begin":984,"end":1000},"obj":"FMAID:82742"},{"id":"_T40","span":{"begin":984,"end":1000},"obj":"FMAID:196731"},{"id":"_T41","span":{"begin":1033,"end":1039},"obj":"FMAID:82790"},{"id":"_T42","span":{"begin":1033,"end":1039},"obj":"FMAID:196784"},{"id":"_T43","span":{"begin":1106,"end":1117},"obj":"FMAID:199757"},{"id":"_T44","span":{"begin":1106,"end":1117},"obj":"FMAID:62900"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Cell differentiation in Dictyostelium discoideum controls assembly of protein-linked glycans.\nThe prestalk and prespore cells from the Dictyostelium discoideum multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc alpha-linked to N-acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by beta-elimination and include a glycoantigen dependent on the modB genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":174,"end":178},"obj":"http://www.uniprot.org/uniprot/P97469"}],"text":"Cell differentiation in Dictyostelium discoideum controls assembly of protein-linked glycans.\nThe prestalk and prespore cells from the Dictyostelium discoideum multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc alpha-linked to N-acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by beta-elimination and include a glycoantigen dependent on the modB genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/361072"},{"id":"T2","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1037912"},{"id":"T3","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1037920"},{"id":"T4","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1037580"},{"id":"T5","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/306026"},{"id":"T6","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/217135"},{"id":"T7","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/361082"},{"id":"T8","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/5782"},{"id":"T9","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1037946"},{"id":"T10","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1037943"},{"id":"T11","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/882401"},{"id":"T12","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/361067"},{"id":"T13","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/361070"},{"id":"T14","span":{"begin":24,"end":37},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/741935"},{"id":"T15","span":{"begin":120,"end":125},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T16","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/361082"},{"id":"T17","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/882401"},{"id":"T18","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/741935"},{"id":"T19","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/361072"},{"id":"T20","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/5782"},{"id":"T21","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1037946"},{"id":"T22","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1037943"},{"id":"T23","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/217135"},{"id":"T24","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/306026"},{"id":"T25","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1037580"},{"id":"T26","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/361067"},{"id":"T27","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1037920"},{"id":"T28","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/361070"},{"id":"T29","span":{"begin":135,"end":148},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1037912"},{"id":"T30","span":{"begin":248,"end":253},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T31","span":{"begin":297,"end":302},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T32","span":{"begin":400,"end":405},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T33","span":{"begin":641,"end":646},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T34","span":{"begin":714,"end":718},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T35","span":{"begin":714,"end":718},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"}],"text":"Cell differentiation in Dictyostelium discoideum controls assembly of protein-linked glycans.\nThe prestalk and prespore cells from the Dictyostelium discoideum multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc alpha-linked to N-acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by beta-elimination and include a glycoantigen dependent on the modB genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":0,"end":20},"obj":"http://purl.obolibrary.org/obo/GO_0030154"},{"id":"T2","span":{"begin":188,"end":199},"obj":"http://purl.obolibrary.org/obo/GO_0032502"},{"id":"T3","span":{"begin":372,"end":384},"obj":"http://purl.obolibrary.org/obo/GO_0036065"},{"id":"T4","span":{"begin":963,"end":974},"obj":"http://purl.obolibrary.org/obo/GO_0036065"},{"id":"T5","span":{"begin":1068,"end":1076},"obj":"http://purl.obolibrary.org/obo/GO_0051179"}],"text":"Cell differentiation in Dictyostelium discoideum controls assembly of protein-linked glycans.\nThe prestalk and prespore cells from the Dictyostelium discoideum multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc alpha-linked to N-acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by beta-elimination and include a glycoantigen dependent on the modB genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":0,"end":4},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":120,"end":125},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":248,"end":253},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":297,"end":302},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":400,"end":405},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":641,"end":646},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7","span":{"begin":927,"end":937},"obj":"http://purl.obolibrary.org/obo/GO_0031160"},{"id":"T8","span":{"begin":1125,"end":1135},"obj":"http://purl.obolibrary.org/obo/GO_0031160"},{"id":"T9","span":{"begin":1089,"end":1097},"obj":"http://purl.obolibrary.org/obo/GO_0031982"}],"text":"Cell differentiation in Dictyostelium discoideum controls assembly of protein-linked glycans.\nThe prestalk and prespore cells from the Dictyostelium discoideum multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc alpha-linked to N-acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by beta-elimination and include a glycoantigen dependent on the modB genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":93},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":94,"end":238},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":239,"end":385},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":386,"end":498},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":499,"end":647},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":648,"end":794},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":795,"end":922},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":923,"end":1136},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":93},"obj":"Sentence"},{"id":"T2","span":{"begin":94,"end":238},"obj":"Sentence"},{"id":"T3","span":{"begin":239,"end":385},"obj":"Sentence"},{"id":"T4","span":{"begin":386,"end":498},"obj":"Sentence"},{"id":"T5","span":{"begin":499,"end":647},"obj":"Sentence"},{"id":"T6","span":{"begin":648,"end":794},"obj":"Sentence"},{"id":"T7","span":{"begin":795,"end":922},"obj":"Sentence"},{"id":"T8","span":{"begin":923,"end":1136},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":93},"obj":"Sentence"},{"id":"T2","span":{"begin":94,"end":238},"obj":"Sentence"},{"id":"T3","span":{"begin":239,"end":385},"obj":"Sentence"},{"id":"T4","span":{"begin":386,"end":498},"obj":"Sentence"},{"id":"T5","span":{"begin":499,"end":647},"obj":"Sentence"},{"id":"T6","span":{"begin":648,"end":794},"obj":"Sentence"},{"id":"T7","span":{"begin":795,"end":922},"obj":"Sentence"},{"id":"T8","span":{"begin":923,"end":1136},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Cell differentiation in Dictyostelium discoideum controls assembly of protein-linked glycans.\nThe prestalk and prespore cells from the Dictyostelium discoideum multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc alpha-linked to N-acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by beta-elimination and include a glycoantigen dependent on the modB genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":665,"end":673},"obj":"id"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":821,"end":829},"obj":"id"}],"text":"Cell differentiation in Dictyostelium discoideum controls assembly of protein-linked glycans.\nThe prestalk and prespore cells from the Dictyostelium discoideum multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc alpha-linked to N-acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by beta-elimination and include a glycoantigen dependent on the modB genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G49112ZN\""},{"id":"GlycanIUPAC_T2","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G50059AJ\""},{"id":"GlycanIUPAC_T3","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G76218YK\""},{"id":"GlycanIUPAC_T4","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G50102KR\""},{"id":"GlycanIUPAC_T5","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G10717VS\""},{"id":"GlycanIUPAC_T6","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G60524RK\""},{"id":"GlycanIUPAC_T7","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G84407TT\""},{"id":"GlycanIUPAC_T8","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G64717JT\""},{"id":"GlycanIUPAC_T9","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G45003TT\""},{"id":"GlycanIUPAC_T10","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G73923FP\""},{"id":"GlycanIUPAC_T11","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G78231MB\""},{"id":"GlycanIUPAC_T12","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G80487UG\""},{"id":"GlycanIUPAC_T13","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G29758MI\""},{"id":"GlycanIUPAC_T14","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G02671KD\""},{"id":"GlycanIUPAC_T15","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G57926TZ\""},{"id":"GlycanIUPAC_T16","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G41718FD\""},{"id":"GlycanIUPAC_T17","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G99840FL\""},{"id":"GlycanIUPAC_T18","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G64321UX\""},{"id":"GlycanIUPAC_T19","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G11231EG\""},{"id":"GlycanIUPAC_T20","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G62741TN\""},{"id":"GlycanIUPAC_T21","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G51576ZQ\""},{"id":"GlycanIUPAC_T22","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G66056LD\""},{"id":"GlycanIUPAC_T23","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G02768BF\""},{"id":"GlycanIUPAC_T24","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G26168RO\""},{"id":"GlycanIUPAC_T25","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G42890HL\""},{"id":"GlycanIUPAC_T26","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G17533VU\""},{"id":"GlycanIUPAC_T27","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G34306RG\""},{"id":"GlycanIUPAC_T28","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G88735KU\""},{"id":"GlycanIUPAC_T29","span":{"begin":458,"end":461},"obj":"\"http://rdf.glycoinfo.org/glycan/G82605UA\""}],"text":"Cell differentiation in Dictyostelium discoideum controls assembly of protein-linked glycans.\nThe prestalk and prespore cells from the Dictyostelium discoideum multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc alpha-linked to N-acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by beta-elimination and include a glycoantigen dependent on the modB genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":24,"end":48},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":135,"end":159},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"44689"},{"id":"A2","pred":"db_id","subj":"T2","obj":"44689"}],"text":"Cell differentiation in Dictyostelium discoideum controls assembly of protein-linked glycans.\nThe prestalk and prespore cells from the Dictyostelium discoideum multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc alpha-linked to N-acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by beta-elimination and include a glycoantigen dependent on the modB genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":1112,"end":1117},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000119"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0022303"}],"text":"Cell differentiation in Dictyostelium discoideum controls assembly of protein-linked glycans.\nThe prestalk and prespore cells from the Dictyostelium discoideum multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc alpha-linked to N-acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by beta-elimination and include a glycoantigen dependent on the modB genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat."}