PubMed:9639536 JSONTXT

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    Glycan-Motif

    {"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":21,"end":36},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T2","span":{"begin":227,"end":242},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T3","span":{"begin":504,"end":519},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T4","span":{"begin":727,"end":742},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T5","span":{"begin":1130,"end":1145},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T6","span":{"begin":1365,"end":1380},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T7","span":{"begin":1468,"end":1483},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GlyCosmos6-Glycan-Motif-Image

    {"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":21,"end":36},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":227,"end":242},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":504,"end":519},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":727,"end":742},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":1130,"end":1145},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":1365,"end":1380},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":1468,"end":1483},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00054MO"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00054MO"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00054MO"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00054MO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00054MO"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00054MO"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00054MO"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    Glycosmos6-GlycoEpitope

    {"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":21,"end":36},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T2","span":{"begin":227,"end":242},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T3","span":{"begin":504,"end":519},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T4","span":{"begin":727,"end":742},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T5","span":{"begin":1130,"end":1145},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T6","span":{"begin":1365,"end":1380},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T7","span":{"begin":1468,"end":1483},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GlyCosmos6-Glycan-Motif-Structure

    {"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":21,"end":36},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T2","span":{"begin":227,"end":242},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T3","span":{"begin":504,"end":519},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T4","span":{"begin":727,"end":742},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T5","span":{"begin":1130,"end":1145},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T6","span":{"begin":1365,"end":1380},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T7","span":{"begin":1468,"end":1483},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    sentences

    {"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":147,"end":279},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":280,"end":528},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":529,"end":645},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":646,"end":885},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":886,"end":1011},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1012,"end":1155},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1156,"end":1306},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1307,"end":1444},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1445,"end":1588},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"T2","span":{"begin":147,"end":279},"obj":"Sentence"},{"id":"T3","span":{"begin":280,"end":528},"obj":"Sentence"},{"id":"T4","span":{"begin":529,"end":645},"obj":"Sentence"},{"id":"T5","span":{"begin":646,"end":885},"obj":"Sentence"},{"id":"T6","span":{"begin":886,"end":1155},"obj":"Sentence"},{"id":"T7","span":{"begin":1156,"end":1306},"obj":"Sentence"},{"id":"T8","span":{"begin":1307,"end":1444},"obj":"Sentence"},{"id":"T9","span":{"begin":1445,"end":1588},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"T2","span":{"begin":147,"end":279},"obj":"Sentence"},{"id":"T3","span":{"begin":280,"end":528},"obj":"Sentence"},{"id":"T4","span":{"begin":529,"end":645},"obj":"Sentence"},{"id":"T5","span":{"begin":646,"end":885},"obj":"Sentence"},{"id":"T6","span":{"begin":886,"end":1011},"obj":"Sentence"},{"id":"T7","span":{"begin":1012,"end":1155},"obj":"Sentence"},{"id":"T8","span":{"begin":1156,"end":1306},"obj":"Sentence"},{"id":"T9","span":{"begin":1307,"end":1444},"obj":"Sentence"},{"id":"T10","span":{"begin":1445,"end":1588},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GlycoBiology-FMA

    {"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":60,"end":72},"obj":"FMAID:62925"},{"id":"_T2","span":{"begin":60,"end":72},"obj":"FMAID:167256"},{"id":"_T3","span":{"begin":93,"end":99},"obj":"FMAID:85815"},{"id":"_T4","span":{"begin":266,"end":278},"obj":"FMAID:167256"},{"id":"_T5","span":{"begin":266,"end":278},"obj":"FMAID:62925"},{"id":"_T6","span":{"begin":297,"end":303},"obj":"FMAID:85815"},{"id":"_T7","span":{"begin":441,"end":447},"obj":"FMAID:162307"},{"id":"_T8","span":{"begin":460,"end":472},"obj":"FMAID:167256"},{"id":"_T9","span":{"begin":460,"end":472},"obj":"FMAID:62925"},{"id":"_T10","span":{"begin":835,"end":847},"obj":"FMAID:179268"},{"id":"_T11","span":{"begin":835,"end":847},"obj":"FMAID:74531"},{"id":"_T12","span":{"begin":1430,"end":1443},"obj":"FMAID:196778"},{"id":"_T13","span":{"begin":1430,"end":1443},"obj":"FMAID:82784"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    uniprot-human

    {"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":356,"end":359},"obj":"http://www.uniprot.org/uniprot/P19957"},{"id":"T2","span":{"begin":638,"end":641},"obj":"http://www.uniprot.org/uniprot/P19957"},{"id":"T3","span":{"begin":871,"end":874},"obj":"http://www.uniprot.org/uniprot/P19957"},{"id":"T4","span":{"begin":890,"end":893},"obj":"http://www.uniprot.org/uniprot/P19957"},{"id":"T5","span":{"begin":1061,"end":1064},"obj":"http://www.uniprot.org/uniprot/P19957"},{"id":"T6","span":{"begin":360,"end":362},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T7","span":{"begin":642,"end":644},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T8","span":{"begin":894,"end":896},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T9","span":{"begin":1065,"end":1067},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T10","span":{"begin":1068,"end":1070},"obj":"http://www.uniprot.org/uniprot/Q99707"},{"id":"T11","span":{"begin":487,"end":490},"obj":"http://www.uniprot.org/uniprot/Q99983"},{"id":"T12","span":{"begin":529,"end":532},"obj":"http://www.uniprot.org/uniprot/Q99983"},{"id":"T13","span":{"begin":1323,"end":1326},"obj":"http://www.uniprot.org/uniprot/Q99983"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    uniprot-mouse

    {"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":360,"end":362},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"},{"id":"T2","span":{"begin":642,"end":644},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"},{"id":"T3","span":{"begin":894,"end":896},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"},{"id":"T4","span":{"begin":1065,"end":1067},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"},{"id":"T5","span":{"begin":1068,"end":1070},"obj":"http://www.uniprot.org/uniprot/A6H5Y3"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GO-BP

    {"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":5,"end":17},"obj":"http://purl.obolibrary.org/obo/GO_0051179"},{"id":"T2","span":{"begin":21,"end":27},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T3","span":{"begin":227,"end":233},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T4","span":{"begin":504,"end":510},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T5","span":{"begin":727,"end":733},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T6","span":{"begin":1130,"end":1136},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T7","span":{"begin":1365,"end":1371},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T8","span":{"begin":1468,"end":1474},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T9","span":{"begin":157,"end":161},"obj":"http://purl.obolibrary.org/obo/GO_0033867"},{"id":"T10","span":{"begin":166,"end":175},"obj":"http://purl.obolibrary.org/obo/GO_0046960"},{"id":"T11","span":{"begin":187,"end":196},"obj":"http://purl.obolibrary.org/obo/GO_0032502"},{"id":"T12","span":{"begin":403,"end":425},"obj":"http://purl.obolibrary.org/obo/GO_0006487"},{"id":"T13","span":{"begin":412,"end":425},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T14","span":{"begin":537,"end":545},"obj":"http://purl.obolibrary.org/obo/GO_0007586"},{"id":"T15","span":{"begin":897,"end":903},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T16","span":{"begin":1350,"end":1356},"obj":"http://purl.obolibrary.org/obo/GO_0023052"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    NGLY1-deficiency

    {"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":995,"end":1001},"obj":"chem:24139"},{"id":"T1","span":{"begin":995,"end":1001},"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":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GlycoBiology-Motifs

    {"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":21,"end":33},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T2","span":{"begin":227,"end":239},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T3","span":{"begin":504,"end":516},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T4","span":{"begin":727,"end":739},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T5","span":{"begin":1130,"end":1142},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T6","span":{"begin":1365,"end":1377},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T7","span":{"begin":1468,"end":1480},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T8","span":{"begin":21,"end":35},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T9","span":{"begin":227,"end":241},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T10","span":{"begin":504,"end":518},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T11","span":{"begin":727,"end":741},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T12","span":{"begin":1130,"end":1144},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T13","span":{"begin":1365,"end":1379},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T14","span":{"begin":1468,"end":1482},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T15","span":{"begin":28,"end":33},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T16","span":{"begin":234,"end":239},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T17","span":{"begin":511,"end":516},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T18","span":{"begin":734,"end":739},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T19","span":{"begin":1137,"end":1142},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T20","span":{"begin":1372,"end":1377},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T21","span":{"begin":1475,"end":1480},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T22","span":{"begin":28,"end":35},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T23","span":{"begin":234,"end":241},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T24","span":{"begin":511,"end":518},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T25","span":{"begin":734,"end":741},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T26","span":{"begin":1137,"end":1144},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T27","span":{"begin":1372,"end":1379},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T28","span":{"begin":1475,"end":1482},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GlycoBiology-Epitope

    {"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":28,"end":35},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":234,"end":241},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":511,"end":518},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T4","span":{"begin":734,"end":741},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T5","span":{"begin":1137,"end":1144},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T6","span":{"begin":1372,"end":1379},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T7","span":{"begin":1475,"end":1482},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T8","span":{"begin":21,"end":33},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T9","span":{"begin":227,"end":239},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T10","span":{"begin":504,"end":516},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T11","span":{"begin":727,"end":739},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T12","span":{"begin":1130,"end":1142},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T13","span":{"begin":1365,"end":1377},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T14","span":{"begin":1468,"end":1480},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T15","span":{"begin":21,"end":35},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T16","span":{"begin":227,"end":241},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T17","span":{"begin":504,"end":518},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T18","span":{"begin":727,"end":741},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T19","span":{"begin":1130,"end":1144},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T20","span":{"begin":1365,"end":1379},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T21","span":{"begin":1468,"end":1482},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GlyTouCan-IUPAC

    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:"\"http://rdf.glycoinfo.org/glycan/G67363FK\""},{"id":"GlycanIUPAC_T47","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G17562KT\""},{"id":"GlycanIUPAC_T48","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G24774YJ\""},{"id":"GlycanIUPAC_T49","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G32162UO\""},{"id":"GlycanIUPAC_T50","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G89163RR\""},{"id":"GlycanIUPAC_T51","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G99522DY\""},{"id":"GlycanIUPAC_T52","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G59246IF\""},{"id":"GlycanIUPAC_T53","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G95321NT\""},{"id":"GlycanIUPAC_T54","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G17531ZI\""},{"id":"GlycanIUPAC_T55","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G54322SU\""},{"id":"GlycanIUPAC_T56","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G72010DO\""},{"id":"GlycanIUPAC_T57","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G44269EP\""},{"id":"GlycanIUPAC_T58","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G57335AD\""},{"id":"GlycanIUPAC_T59","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G60837LL\""},{"id":"GlycanIUPAC_T60","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G61929XX\""},{"id":"GlycanIUPAC_T61","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G88747RA\""},{"id":"GlycanIUPAC_T62","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G47955HA\""},{"id":"GlycanIUPAC_T63","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G60982WS\""},{"id":"GlycanIUPAC_T64","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G37035KG\""},{"id":"GlycanIUPAC_T65","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G46297FI\""},{"id":"GlycanIUPAC_T66","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G35475KI\""},{"id":"GlycanIUPAC_T67","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G29771JN\""},{"id":"GlycanIUPAC_T68","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G61285YR\""},{"id":"GlycanIUPAC_T69","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G54785MW\""},{"id":"GlycanIUPAC_T70","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G53039GT\""},{"id":"GlycanIUPAC_T71","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G00601HK\""},{"id":"GlycanIUPAC_T72","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G10485IJ\""},{"id":"GlycanIUPAC_T73","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G16393IB\""},{"id":"GlycanIUPAC_T74","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G98436FZ\""},{"id":"GlycanIUPAC_T75","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G18825IA\""},{"id":"GlycanIUPAC_T76","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G61281HQ\""},{"id":"GlycanIUPAC_T77","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G07798TI\""},{"id":"GlycanIUPAC_T78","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G55921QA\""},{"id":"GlycanIUPAC_T79","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G99066DL\""},{"id":"GlycanIUPAC_T80","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G33451PQ\""},{"id":"GlycanIUPAC_T81","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G02111XU\""},{"id":"GlycanIUPAC_T82","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G85193OM\""},{"id":"GlycanIUPAC_T83","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G89174YQ\""},{"id":"GlycanIUPAC_T84","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G28802LE\""},{"id":"GlycanIUPAC_T85","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G56061JK\""},{"id":"GlycanIUPAC_T86","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G68941BC\""},{"id":"GlycanIUPAC_T87","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G55436FC\""},{"id":"GlycanIUPAC_T88","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G24002PU\""},{"id":"GlycanIUPAC_T89","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G61387SV\""},{"id":"GlycanIUPAC_T90","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G31834HW\""},{"id":"GlycanIUPAC_T91","span":{"begin":990,"end":993},"obj":"\"http://rdf.glycoinfo.org/glycan/G35324RT\""},{"id":"GlycanIUPAC_T92","span":{"begin":990,"e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org/glycan/G80869MR\""},{"id":"GlycanIUPAC_T138","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G55978NL\""},{"id":"GlycanIUPAC_T139","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G54644LT\""},{"id":"GlycanIUPAC_T140","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G25694UG\""},{"id":"GlycanIUPAC_T141","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G25126RB\""},{"id":"GlycanIUPAC_T142","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G51848AD\""},{"id":"GlycanIUPAC_T143","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G94667GM\""},{"id":"GlycanIUPAC_T144","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G30124BO\""},{"id":"GlycanIUPAC_T145","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G82777EZ\""},{"id":"GlycanIUPAC_T146","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G10151YZ\""},{"id":"GlycanIUPAC_T147","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G17585ZM\""},{"id":"GlycanIUPAC_T148","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G04411CJ\""},{"id":"GlycanIUPAC_T149","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G38254HJ\""},{"id":"GlycanIUPAC_T150","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G75188FS\""},{"id":"GlycanIUPAC_T151","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G70374VG\""},{"id":"GlycanIUPAC_T152","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G45176LJ\""},{"id":"GlycanIUPAC_T153","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G30874VW\""},{"id":"GlycanIUPAC_T154","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G69333MI\""},{"id":"GlycanIUPAC_T155","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G10676XO\""},{"id":"GlycanIUPAC_T156","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G14843DJ\""},{"id":"GlycanIUPAC_T157","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G47546FR\""},{"id":"GlycanIUPAC_T158","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G73695ZM\""},{"id":"GlycanIUPAC_T159","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G31923TJ\""},{"id":"GlycanIUPAC_T160","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G60519EP\""},{"id":"GlycanIUPAC_T161","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G07933IA\""},{"id":"GlycanIUPAC_T162","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G40745NH\""},{"id":"GlycanIUPAC_T163","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G54496YV\""},{"id":"GlycanIUPAC_T164","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T165","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T166","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T167","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T168","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T169","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T170","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T171","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T172","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T173","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T174","span":{"begin":995,"end":1001},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""},{"id":"GlycanIUPAC_T175","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G49112ZN\""},{"id":"GlycanIUPAC_T176","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G50059AJ\""},{"id":"GlycanIUPAC_T177","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G76218YK\""},{"id":"GlycanIUPAC_T178","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G50102KR\""},{"id":"GlycanIUPAC_T179","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G10717VS\""},{"id":"GlycanIUPAC_T180","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G60524RK\""},{"id":"GlycanIUPAC_T181","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G84407TT\""},{"id":"GlycanIUPAC_T182","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G64717JT\""},{"id":"GlycanIUPAC_T183","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G45003TT\""},{"id":"GlycanIUPAC_T184","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G73923FP\""},{"id":"GlycanIUPAC_T185","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G78231MB\""},{"id":"GlycanIUPAC_T186","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G80487UG\""},{"id":"GlycanIUPAC_T187","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G29758MI\""},{"id":"GlycanIUPAC_T188","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G02671KD\""},{"id":"GlycanIUPAC_T189","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G57926TZ\""},{"id":"GlycanIUPAC_T190","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G41718FD\""},{"id":"GlycanIUPAC_T191","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G99840FL\""},{"id":"GlycanIUPAC_T192","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G64321UX\""},{"id":"GlycanIUPAC_T193","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G11231EG\""},{"id":"GlycanIUPAC_T194","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G62741TN\""},{"id":"GlycanIUPAC_T195","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G51576ZQ\""},{"id":"GlycanIUPAC_T196","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G66056LD\""},{"id":"GlycanIUPAC_T197","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G02768BF\""},{"id":"GlycanIUPAC_T198","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G26168RO\""},{"id":"GlycanIUPAC_T199","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G42890HL\""},{"id":"GlycanIUPAC_T200","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G17533VU\""},{"id":"GlycanIUPAC_T201","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G34306RG\""},{"id":"GlycanIUPAC_T202","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G88735KU\""},{"id":"GlycanIUPAC_T203","span":{"begin":1007,"end":1010},"obj":"\"http://rdf.glycoinfo.org/glycan/G82605UA\""}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    mondo_disease

    {"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":487,"end":490},"obj":"Disease"},{"id":"T2","span":{"begin":529,"end":532},"obj":"Disease"},{"id":"T3","span":{"begin":642,"end":647},"obj":"Disease"},{"id":"T5","span":{"begin":1323,"end":1326},"obj":"Disease"},{"id":"T6","span":{"begin":1566,"end":1587},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0013316"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0013316"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0007803"},{"id":"A4","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0010892"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0013316"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0021166"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    Glycan-GlyCosmos

    {"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":21,"end":36},"obj":"Glycan"},{"id":"T2","span":{"begin":227,"end":242},"obj":"Glycan"},{"id":"T3","span":{"begin":504,"end":519},"obj":"Glycan"},{"id":"T4","span":{"begin":727,"end":742},"obj":"Glycan"},{"id":"T5","span":{"begin":983,"end":988},"obj":"Glycan"},{"id":"T6","span":{"begin":1130,"end":1145},"obj":"Glycan"},{"id":"T7","span":{"begin":1365,"end":1380},"obj":"Glycan"},{"id":"T8","span":{"begin":1468,"end":1483},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A9","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A10","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A11","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A12","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A13","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A14","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A15","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A16","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GlyCosmos-GlycoEpitope

    {"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":21,"end":36},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":227,"end":242},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":504,"end":519},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":727,"end":742},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":1130,"end":1145},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":1365,"end":1380},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":1468,"end":1483},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0012"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GlyCosmos15-MONDO

    {"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":487,"end":490},"obj":"Disease"},{"id":"T2","span":{"begin":529,"end":532},"obj":"Disease"},{"id":"T3","span":{"begin":642,"end":647},"obj":"Disease"},{"id":"T5","span":{"begin":1323,"end":1326},"obj":"Disease"},{"id":"T6","span":{"begin":1566,"end":1587},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0013316"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0013316"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0007803"},{"id":"A4","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0010892"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0013316"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0021166"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GlyCosmos15-NCBITAXON

    {"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":435,"end":440},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GlyCosmos15-UBERON

    {"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":441,"end":447},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001969"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    sentences

    {"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":147,"end":279},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":280,"end":528},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":529,"end":645},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":646,"end":885},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":886,"end":1011},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1012,"end":1155},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1156,"end":1306},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1307,"end":1444},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1445,"end":1588},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"T2","span":{"begin":147,"end":279},"obj":"Sentence"},{"id":"T3","span":{"begin":280,"end":528},"obj":"Sentence"},{"id":"T4","span":{"begin":529,"end":645},"obj":"Sentence"},{"id":"T5","span":{"begin":646,"end":885},"obj":"Sentence"},{"id":"T6","span":{"begin":886,"end":1155},"obj":"Sentence"},{"id":"T7","span":{"begin":1156,"end":1306},"obj":"Sentence"},{"id":"T8","span":{"begin":1307,"end":1444},"obj":"Sentence"},{"id":"T9","span":{"begin":1445,"end":1588},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"T2","span":{"begin":147,"end":279},"obj":"Sentence"},{"id":"T3","span":{"begin":280,"end":528},"obj":"Sentence"},{"id":"T4","span":{"begin":529,"end":645},"obj":"Sentence"},{"id":"T5","span":{"begin":646,"end":885},"obj":"Sentence"},{"id":"T6","span":{"begin":886,"end":1011},"obj":"Sentence"},{"id":"T7","span":{"begin":1012,"end":1155},"obj":"Sentence"},{"id":"T8","span":{"begin":1156,"end":1306},"obj":"Sentence"},{"id":"T9","span":{"begin":1307,"end":1444},"obj":"Sentence"},{"id":"T10","span":{"begin":1445,"end":1588},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GlyCosmos15-Sentences

    {"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"T2","span":{"begin":147,"end":279},"obj":"Sentence"},{"id":"T3","span":{"begin":280,"end":528},"obj":"Sentence"},{"id":"T4","span":{"begin":529,"end":645},"obj":"Sentence"},{"id":"T5","span":{"begin":646,"end":885},"obj":"Sentence"},{"id":"T6","span":{"begin":886,"end":1155},"obj":"Sentence"},{"id":"T7","span":{"begin":1156,"end":1306},"obj":"Sentence"},{"id":"T8","span":{"begin":1307,"end":1444},"obj":"Sentence"},{"id":"T9","span":{"begin":1445,"end":1588},"obj":"Sentence"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GlyCosmos15-Glycan

    {"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":21,"end":36},"obj":"Glycan"},{"id":"T2","span":{"begin":227,"end":242},"obj":"Glycan"},{"id":"T3","span":{"begin":504,"end":519},"obj":"Glycan"},{"id":"T4","span":{"begin":727,"end":742},"obj":"Glycan"},{"id":"T5","span":{"begin":983,"end":988},"obj":"Glycan"},{"id":"T6","span":{"begin":1130,"end":1145},"obj":"Glycan"},{"id":"T7","span":{"begin":1365,"end":1380},"obj":"Glycan"},{"id":"T8","span":{"begin":1468,"end":1483},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A9","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A10","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A11","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A12","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A13","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A14","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A15","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A16","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    GlyCosmos15-GlycoEpitope

    {"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":21,"end":36},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":227,"end":242},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":504,"end":519},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":727,"end":742},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":1130,"end":1145},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":1365,"end":1380},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":1468,"end":1483},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0012"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    NCBITAXON

    {"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":435,"end":440},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}

    Anatomy-UBERON

    {"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":441,"end":447},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001969"}],"text":"Site localization of sialyl Lewis(x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry.\nA simple, fast and sensitive method was developed to verify the presence of the sialyl Lewis(x) antigen on an N-linked glycoprotein. High performance liquid chromatography-electrospray mass spectrometry (HPLC-ESI/MS) was used to identify which of the five N-linked glycosylation sites of human plasma alpha1-acid-glycoprotein (orosomucoid, OMD) contain the sialyl Lewis(x) antigen. OMD was digested with proteolytic enzymes and analyzed by reversed phase chromatography coupled with on-line ESI/MS. A tandem mass spectrometry experiment was designed to detect the presence of the sialyl Lewis(x) antigen based on the observation of an 803 mass to charge ratio ( m/z ) ion produced in the intermediate pressure region of the ESI interface. The ESI/MS signal at m/z 803 is consistent with an oxonium ion for a glycan structure containing NeuAc, Gal, GlcNAc, and Fuc. The identity of the m/z 803 ion was confirmed by ESI/MS/MS analysis of the m/z 803 fragment ion and comparison with a sialyl Lewis(x) standard. The stereochemistry and linkage positions were assigned using previous NMR analysis but could be determined with permethylation analysis if necessary. The analysis of OMD gave a pattern showing signal for the sialyl Lewis(x) antigen coeluting with each of the five N-linked glycopeptides. The ability to monitor sialyl Lewis(x) expression at each of the five sites is of interest in the study of OMD's role in inflammatory diseases."}