PubMed:9592119 JSONTXT

{"project":"GlyCosmos15-Species-PubTator","denotations":[{"id":"6","span":{"begin":51,"end":74},"obj":"Species"},{"id":"43","span":{"begin":163,"end":186},"obj":"Species"},{"id":"44","span":{"begin":196,"end":208},"obj":"Species"},{"id":"45","span":{"begin":210,"end":214},"obj":"Species"},{"id":"46","span":{"begin":231,"end":235},"obj":"Species"},{"id":"49","span":{"begin":313,"end":325},"obj":"Species"},{"id":"67","span":{"begin":834,"end":857},"obj":"Species"},{"id":"72","span":{"begin":1055,"end":1067},"obj":"Species"},{"id":"73","span":{"begin":1069,"end":1073},"obj":"Species"}],"attributes":[{"id":"A6","pred":"db_id","subj":"6","obj":"11320"},{"id":"A43","pred":"db_id","subj":"43","obj":"11320"},{"id":"A45","pred":"db_id","subj":"45","obj":"119210"},{"id":"A46","pred":"db_id","subj":"46","obj":"114727"},{"id":"A67","pred":"db_id","subj":"67","obj":"11320"},{"id":"A73","pred":"db_id","subj":"73","obj":"119210"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":602,"end":608},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T2","span":{"begin":629,"end":632},"obj":"https://glytoucan.org/Structures/Glycans/G61168WC"},{"id":"T3","span":{"begin":629,"end":632},"obj":"https://glytoucan.org/Structures/Glycans/G79389NT"},{"id":"T4","span":{"begin":675,"end":678},"obj":"https://glytoucan.org/Structures/Glycans/G30207PZ"},{"id":"T5","span":{"begin":675,"end":678},"obj":"https://glytoucan.org/Structures/Glycans/G77824XV"},{"id":"T6","span":{"begin":1015,"end":1026},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T7","span":{"begin":1113,"end":1124},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":602,"end":608},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":629,"end":632},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":675,"end":678},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":1015,"end":1026},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":1113,"end":1124},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G79389NT"},{"id":"A3","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G61168WC"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G77824XV"},{"id":"A5","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G30207PZ"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":602,"end":608},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T2","span":{"begin":629,"end":632},"obj":"https://glytoucan.org/Structures/Glycans/G61168WC"},{"id":"T3","span":{"begin":629,"end":632},"obj":"https://glytoucan.org/Structures/Glycans/G79389NT"},{"id":"T4","span":{"begin":675,"end":678},"obj":"https://glytoucan.org/Structures/Glycans/G30207PZ"},{"id":"T5","span":{"begin":675,"end":678},"obj":"https://glytoucan.org/Structures/Glycans/G77824XV"},{"id":"T6","span":{"begin":1015,"end":1026},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T7","span":{"begin":1113,"end":1124},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":675,"end":678},"obj":"http://www.glycoepitope.jp/epitopes/EP0055"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GlycoBiology-PACDB","denotations":[{"id":"_T1","span":{"begin":57,"end":74},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC780"},{"id":"_T2","span":{"begin":169,"end":186},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC780"},{"id":"_T3","span":{"begin":840,"end":857},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC780"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":101,"end":113},"obj":"FMAID:82816"},{"id":"_T2","span":{"begin":101,"end":113},"obj":"FMAID:196811"},{"id":"_T3","span":{"begin":278,"end":290},"obj":"FMAID:82816"},{"id":"_T4","span":{"begin":278,"end":290},"obj":"FMAID:196811"},{"id":"_T5","span":{"begin":456,"end":467},"obj":"FMAID:82816"},{"id":"_T6","span":{"begin":456,"end":467},"obj":"FMAID:196811"},{"id":"_T7","span":{"begin":745,"end":757},"obj":"FMAID:196811"},{"id":"_T8","span":{"begin":745,"end":757},"obj":"FMAID:82816"},{"id":"_T9","span":{"begin":926,"end":938},"obj":"FMAID:196811"},{"id":"_T10","span":{"begin":926,"end":938},"obj":"FMAID:82816"},{"id":"_T11","span":{"begin":965,"end":977},"obj":"FMAID:196811"},{"id":"_T12","span":{"begin":965,"end":977},"obj":"FMAID:82816"},{"id":"_T13","span":{"begin":1175,"end":1180},"obj":"FMAID:196724"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":19,"end":21},"obj":"http://www.uniprot.org/uniprot/P10163"},{"id":"T2","span":{"begin":798,"end":800},"obj":"http://www.uniprot.org/uniprot/P10163"},{"id":"T3","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/P63128"},{"id":"T4","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/P10265"},{"id":"T5","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/P63119"},{"id":"T6","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/P63120"},{"id":"T7","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/P63121"},{"id":"T8","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/P63122"},{"id":"T9","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/P63123"},{"id":"T10","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/P63124"},{"id":"T11","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/P63125"},{"id":"T12","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/P63127"},{"id":"T13","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/P63129"},{"id":"T14","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/P63131"},{"id":"T15","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/Q9Y6I0"},{"id":"T16","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/Q8WXS4"},{"id":"T17","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/P06401"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":222,"end":224},"obj":"http://www.uniprot.org/uniprot/Q00175"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":57,"end":74},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/11320"},{"id":"T2","span":{"begin":57,"end":74},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/11520"},{"id":"T3","span":{"begin":69,"end":74},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/184751"},{"id":"T4","span":{"begin":169,"end":186},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/11320"},{"id":"T5","span":{"begin":169,"end":186},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/11520"},{"id":"T6","span":{"begin":181,"end":186},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/184751"},{"id":"T7","span":{"begin":840,"end":857},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/11520"},{"id":"T8","span":{"begin":840,"end":857},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/11320"},{"id":"T9","span":{"begin":852,"end":857},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/184751"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":114},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":115,"end":291},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":292,"end":572},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":573,"end":674},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":675,"end":793},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":794,"end":939},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":940,"end":1187},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":114},"obj":"Sentence"},{"id":"T2","span":{"begin":115,"end":291},"obj":"Sentence"},{"id":"T3","span":{"begin":292,"end":572},"obj":"Sentence"},{"id":"T4","span":{"begin":573,"end":674},"obj":"Sentence"},{"id":"T5","span":{"begin":675,"end":793},"obj":"Sentence"},{"id":"T6","span":{"begin":794,"end":939},"obj":"Sentence"},{"id":"T7","span":{"begin":940,"end":1187},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":114},"obj":"Sentence"},{"id":"T2","span":{"begin":115,"end":291},"obj":"Sentence"},{"id":"T3","span":{"begin":292,"end":572},"obj":"Sentence"},{"id":"T4","span":{"begin":573,"end":674},"obj":"Sentence"},{"id":"T5","span":{"begin":675,"end":793},"obj":"Sentence"},{"id":"T6","span":{"begin":794,"end":939},"obj":"Sentence"},{"id":"T7","span":{"begin":940,"end":1187},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":115,"end":121},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T2","span":{"begin":1168,"end":1174},"obj":"http://purl.obolibrary.org/obo/GO_0097503"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":222,"end":224},"obj":"http://purl.obolibrary.org/obo/GO_0039721"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":675,"end":678},"obj":"http://www.glycoepitope.jp/epitopes/EP0055"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T2","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T3","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T4","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T5","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T6","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T7","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T8","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T9","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"GlycanIUPAC_T10","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"GlycanIUPAC_T11","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G09864UE\""},{"id":"GlycanIUPAC_T12","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G09864UE\""},{"id":"GlycanIUPAC_T13","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G28032MC\""},{"id":"GlycanIUPAC_T14","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G28032MC\""},{"id":"GlycanIUPAC_T15","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G28005UP\""},{"id":"GlycanIUPAC_T16","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G28005UP\""},{"id":"GlycanIUPAC_T17","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G92708AT\""},{"id":"GlycanIUPAC_T18","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G92708AT\""},{"id":"GlycanIUPAC_T19","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G73757UC\""},{"id":"GlycanIUPAC_T20","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G73757UC\""},{"id":"GlycanIUPAC_T21","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G51062DM\""},{"id":"GlycanIUPAC_T22","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G51062DM\""},{"id":"GlycanIUPAC_T23","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G05866BJ\""},{"id":"GlycanIUPAC_T24","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G05866BJ\""},{"id":"GlycanIUPAC_T25","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G87394FZ\""},{"id":"GlycanIUPAC_T26","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G87394FZ\""},{"id":"GlycanIUPAC_T27","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G03871NF\""},{"id":"GlycanIUPAC_T28","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G03871NF\""},{"id":"GlycanIUPAC_T29","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G29377VE\""},{"id":"GlycanIUPAC_T30","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G29377VE\""},{"id":"GlycanIUPAC_T31","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G33457CX\""},{"id":"GlycanIUPAC_T32","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G33457CX\""},{"id":"GlycanIUPAC_T33","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G97368GU\""},{"id":"GlycanIUPAC_T34","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G97368GU\""},{"id":"GlycanIUPAC_T35","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G18512EL\""},{"id":"GlycanIUPAC_T36","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G18512EL\""},{"id":"GlycanIUPAC_T37","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G41137VS\""},{"id":"GlycanIUPAC_T38","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G41137VS\""},{"id":"GlycanIUPAC_T39","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G30521NA\""},{"id":"GlycanIUPAC_T40","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G30521NA\""},{"id":"GlycanIUPAC_T41","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G19388CD\""},{"id":"GlycanIUPAC_T42","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G19388CD\""},{"id":"GlycanIUPAC_T43","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G53151FU\""},{"id":"GlycanIUPAC_T44","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G53151FU\""},{"id":"GlycanIUPAC_T45","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G27105XC\""},{"id":"GlycanIUPAC_T46","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G27105XC\""},{"id":"GlycanIUPAC_T47","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G91210VM\""},{"id":"GlycanIUPAC_T48","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G91210VM\""},{"id":"GlycanIUPAC_T49","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G40841DE\""},{"id":"GlycanIUPAC_T50","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G40841DE\""},{"id":"GlycanIUPAC_T51","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G71241HP\""},{"id":"GlycanIUPAC_T52","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G71241HP\""},{"id":"GlycanIUPAC_T53","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G84636BJ\""},{"id":"GlycanIUPAC_T54","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G84636BJ\""},{"id":"GlycanIUPAC_T55","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G47905LJ\""},{"id":"GlycanIUPAC_T56","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G47905LJ\""},{"id":"GlycanIUPAC_T57","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G39340DV\""},{"id":"GlycanIUPAC_T58","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G39340DV\""},{"id":"GlycanIUPAC_T59","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G48801AQ\""},{"id":"GlycanIUPAC_T60","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G48801AQ\""},{"id":"GlycanIUPAC_T61","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G14573NX\""},{"id":"GlycanIUPAC_T62","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G14573NX\""},{"id":"GlycanIUPAC_T63","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G56762TR\""},{"id":"GlycanIUPAC_T64","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G56762TR\""},{"id":"GlycanIUPAC_T65","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G20013XO\""},{"id":"GlycanIUPAC_T66","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G20013XO\""},{"id":"GlycanIUPAC_T67","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G39504DR\""},{"id":"GlycanIUPAC_T68","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G39504DR\""},{"id":"GlycanIUPAC_T69","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G35218RQ\""},{"id":"GlycanIUPAC_T70","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G35218RQ\""},{"id":"GlycanIUPAC_T71","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G53048SH\""},{"id":"GlycanIUPAC_T72","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G53048SH\""},{"id":"GlycanIUPAC_T73","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G78418IX\""},{"id":"GlycanIUPAC_T74","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G78418IX\""},{"id":"GlycanIUPAC_T75","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G09780OD\""},{"id":"GlycanIUPAC_T76","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G09780OD\""},{"id":"GlycanIUPAC_T77","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G56359GL\""},{"id":"GlycanIUPAC_T78","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G56359GL\""},{"id":"GlycanIUPAC_T79","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G78941YC\""},{"id":"GlycanIUPAC_T80","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G78941YC\""},{"id":"GlycanIUPAC_T81","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G26829FC\""},{"id":"GlycanIUPAC_T82","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G26829FC\""},{"id":"GlycanIUPAC_T83","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G88538ZC\""},{"id":"GlycanIUPAC_T84","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G88538ZC\""},{"id":"GlycanIUPAC_T85","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G46593ZR\""},{"id":"GlycanIUPAC_T86","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G46593ZR\""},{"id":"GlycanIUPAC_T87","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G43523TH\""},{"id":"GlycanIUPAC_T88","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G43523TH\""},{"id":"GlycanIUPAC_T89","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G36445ON\""},{"id":"GlycanIUPAC_T90","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G36445ON\""},{"id":"GlycanIUPAC_T91","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G67363FK\""},{"id":"GlycanIUPAC_T92","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G67363FK\""},{"id":"GlycanIUPAC_T93","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G17562KT\""},{"id":"GlycanIUPAC_T94","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G17562KT\""},{"id":"GlycanIUPAC_T95","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G24774YJ\""},{"id":"GlycanIUPAC_T96","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G24774YJ\""},{"id":"GlycanIUPAC_T97","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G32162UO\""},{"id":"GlycanIUPAC_T98","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G32162UO\""},{"id":"GlycanIUPAC_T99","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G89163RR\""},{"id":"GlycanIUPAC_T100","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G89163RR\""},{"id":"GlycanIUPAC_T101","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G99522DY\""},{"id":"GlycanIUPAC_T102","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G99522DY\""},{"id":"GlycanIUPAC_T103","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G59246IF\""},{"id":"GlycanIUPAC_T104","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G59246IF\""},{"id":"GlycanIUPAC_T105","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G95321NT\""},{"id":"GlycanIUPAC_T106","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G95321NT\""},{"id":"GlycanIUPAC_T107","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G17531ZI\""},{"id":"GlycanIUPAC_T108","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G17531ZI\""},{"id":"GlycanIUPAC_T109","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G54322SU\""},{"id":"GlycanIUPAC_T110","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G54322SU\""},{"id":"GlycanIUPAC_T111","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G72010DO\""},{"id":"GlycanIUPAC_T112","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G72010DO\""},{"id":"GlycanIUPAC_T113","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G44269EP\""},{"id":"GlycanIUPAC_T114","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G44269EP\""},{"id":"GlycanIUPAC_T115","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G57335AD\""},{"id":"GlycanIUPAC_T116","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G57335AD\""},{"id":"GlycanIUPAC_T117","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G60837LL\""},{"id":"GlycanIUPAC_T118","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G60837LL\""},{"id":"GlycanIUPAC_T119","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G61929XX\""},{"id":"GlycanIUPAC_T120","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G61929XX\""},{"id":"GlycanIUPAC_T121","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G88747RA\""},{"id":"GlycanIUPAC_T122","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G88747RA\""},{"id":"GlycanIUPAC_T123","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G47955HA\""},{"id":"GlycanIUPAC_T124","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G47955HA\""},{"id":"GlycanIUPAC_T125","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G60982WS\""},{"id":"GlycanIUPAC_T126","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G60982WS\""},{"id":"GlycanIUPAC_T127","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G37035KG\""},{"id":"GlycanIUPAC_T128","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G37035KG\""},{"id":"GlycanIUPAC_T129","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G46297FI\""},{"id":"GlycanIUPAC_T130","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G46297FI\""},{"id":"GlycanIUPAC_T131","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G35475KI\""},{"id":"GlycanIUPAC_T132","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G35475KI\""},{"id":"GlycanIUPAC_T133","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G29771JN\""},{"id":"GlycanIUPAC_T134","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G29771JN\""},{"id":"GlycanIUPAC_T135","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G61285YR\""},{"id":"GlycanIUPAC_T136","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G61285YR\""},{"id":"GlycanIUPAC_T137","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G54785MW\""},{"id":"GlycanIUPAC_T138","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G54785MW\""},{"id":"GlycanIUPAC_T139","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G53039GT\""},{"id":"GlycanIUPAC_T140","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G53039GT\""},{"id":"GlycanIUPAC_T141","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G00601HK\""},{"id":"GlycanIUPAC_T142","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G00601HK\""},{"id":"GlycanIUPAC_T143","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G10485IJ\""},{"id":"GlycanIUPAC_T144","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G10485IJ\""},{"id":"GlycanIUPAC_T145","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G16393IB\""},{"id":"GlycanIUPAC_T146","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G16393IB\""},{"id":"GlycanIUPAC_T147","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G98436FZ\""},{"id":"GlycanIUPAC_T148","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G98436FZ\""},{"id":"GlycanIUPAC_T149","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G18825IA\""},{"id":"GlycanIUPAC_T150","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G18825IA\""},{"id":"GlycanIUPAC_T151","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G61281HQ\""},{"id":"GlycanIUPAC_T152","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G61281HQ\""},{"id":"GlycanIUPAC_T153","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G07798TI\""},{"id":"GlycanIUPAC_T154","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G07798TI\""},{"id":"GlycanIUPAC_T155","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G55921QA\""},{"id":"GlycanIUPAC_T156","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G55921QA\""},{"id":"GlycanIUPAC_T157","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G99066DL\""},{"id":"GlycanIUPAC_T158","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G99066DL\""},{"id":"GlycanIUPAC_T159","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G33451PQ\""},{"id":"GlycanIUPAC_T160","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G33451PQ\""},{"id":"GlycanIUPAC_T161","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G02111XU\""},{"id":"GlycanIUPAC_T162","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G02111XU\""},{"id":"GlycanIUPAC_T163","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G85193OM\""},{"id":"GlycanIUPAC_T164","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G85193OM\""},{"id":"GlycanIUPAC_T165","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G89174YQ\""},{"id":"GlycanIUPAC_T166","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G89174YQ\""},{"id":"GlycanIUPAC_T167","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G28802LE\""},{"id":"GlycanIUPAC_T168","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G28802LE\""},{"id":"GlycanIUPAC_T169","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G56061JK\""},{"id":"GlycanIUPAC_T170","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G56061JK\""},{"id":"GlycanIUPAC_T171","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G68941BC\""},{"id":"GlycanIUPAC_T172","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G68941BC\""},{"id":"GlycanIUPAC_T173","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G55436FC\""},{"id":"GlycanIUPAC_T174","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G55436FC\""},{"id":"GlycanIUPAC_T175","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G24002PU\""},{"id":"GlycanIUPAC_T176","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G24002PU\""},{"id":"GlycanIUPAC_T177","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G61387SV\""},{"id":"GlycanIUPAC_T178","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G61387SV\""},{"id":"GlycanIUPAC_T179","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G31834HW\""},{"id":"GlycanIUPAC_T180","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G31834HW\""},{"id":"GlycanIUPAC_T181","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G35324RT\""},{"id":"GlycanIUPAC_T182","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G35324RT\""},{"id":"GlycanIUPAC_T183","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G34803QO\""},{"id":"GlycanIUPAC_T184","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G34803QO\""},{"id":"GlycanIUPAC_T185","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G92898FF\""},{"id":"GlycanIUPAC_T186","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G92898FF\""},{"id":"GlycanIUPAC_T187","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G01318VX\""},{"id":"GlycanIUPAC_T188","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G01318VX\""},{"id":"GlycanIUPAC_T189","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G83200MX\""},{"id":"GlycanIUPAC_T190","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G83200MX\""},{"id":"GlycanIUPAC_T191","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G56286UC\""},{"id":"GlycanIUPAC_T192","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G56286UC\""},{"id":"GlycanIUPAC_T193","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G07304QA\""},{"id":"GlycanIUPAC_T194","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G07304QA\""},{"id":"GlycanIUPAC_T195","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G06868OU\""},{"id":"GlycanIUPAC_T196","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G06868OU\""},{"id":"GlycanIUPAC_T197","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G12647BS\""},{"id":"GlycanIUPAC_T198","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G12647BS\""},{"id":"GlycanIUPAC_T199","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G51841DF\""},{"id":"GlycanIUPAC_T200","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G51841DF\""},{"id":"GlycanIUPAC_T201","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G32122AJ\""},{"id":"GlycanIUPAC_T202","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G32122AJ\""},{"id":"GlycanIUPAC_T203","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G41125MN\""},{"id":"GlycanIUPAC_T204","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G41125MN\""},{"id":"GlycanIUPAC_T205","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G16093XS\""},{"id":"GlycanIUPAC_T206","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G16093XS\""},{"id":"GlycanIUPAC_T207","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G62425IX\""},{"id":"GlycanIUPAC_T208","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G62425IX\""},{"id":"GlycanIUPAC_T209","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G15673TO\""},{"id":"GlycanIUPAC_T210","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G15673TO\""},{"id":"GlycanIUPAC_T211","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G32857IK\""},{"id":"GlycanIUPAC_T212","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G32857IK\""},{"id":"GlycanIUPAC_T213","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G60047CJ\""},{"id":"GlycanIUPAC_T214","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G60047CJ\""},{"id":"GlycanIUPAC_T215","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G55718ZB\""},{"id":"GlycanIUPAC_T216","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G55718ZB\""},{"id":"GlycanIUPAC_T217","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G88355ZE\""},{"id":"GlycanIUPAC_T218","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G88355ZE\""},{"id":"GlycanIUPAC_T219","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G11283PA\""},{"id":"GlycanIUPAC_T220","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G11283PA\""},{"id":"GlycanIUPAC_T221","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G71737IZ\""},{"id":"GlycanIUPAC_T222","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G71737IZ\""},{"id":"GlycanIUPAC_T223","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G60912WZ\""},{"id":"GlycanIUPAC_T224","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G60912WZ\""},{"id":"GlycanIUPAC_T225","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G99655SO\""},{"id":"GlycanIUPAC_T226","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G99655SO\""},{"id":"GlycanIUPAC_T227","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G10300TW\""},{"id":"GlycanIUPAC_T228","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G10300TW\""},{"id":"GlycanIUPAC_T229","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G89509FL\""},{"id":"GlycanIUPAC_T230","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G89509FL\""},{"id":"GlycanIUPAC_T231","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G31465TH\""},{"id":"GlycanIUPAC_T232","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G31465TH\""},{"id":"GlycanIUPAC_T233","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G94101LU\""},{"id":"GlycanIUPAC_T234","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G94101LU\""},{"id":"GlycanIUPAC_T235","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G38610BB\""},{"id":"GlycanIUPAC_T236","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G38610BB\""},{"id":"GlycanIUPAC_T237","span":{"begin":432,"end":435},"obj":"\"http://rdf.glycoinfo.org/glycan/G85893UF\""},{"id":"GlycanIUPAC_T238","span":{"begin":622,"end":625},"obj":"\"http://rdf.glycoinfo.org/glycan/G85893UF\""},{"id":"GlycanIUPAC_T239","span":{"begin":602,"end":608},"obj":"\"http://rdf.glycoinfo.org/glycan/G76685HR\""},{"id":"GlycanIUPAC_T240","span":{"begin":602,"end":608},"obj":"\"http://rdf.glycoinfo.org/glycan/G65881BF\""},{"id":"GlycanIUPAC_T241","span":{"begin":602,"end":608},"obj":"\"http://rdf.glycoinfo.org/glycan/G82702MH\""},{"id":"GlycanIUPAC_T242","span":{"begin":602,"end":608},"obj":"\"http://rdf.glycoinfo.org/glycan/G51494MY\""},{"id":"GlycanIUPAC_T243","span":{"begin":602,"end":608},"obj":"\"http://rdf.glycoinfo.org/glycan/G37109XL\""},{"id":"GlycanIUPAC_T244","span":{"begin":602,"end":608},"obj":"\"http://rdf.glycoinfo.org/glycan/G47427MX\""},{"id":"GlycanIUPAC_T245","span":{"begin":602,"end":608},"obj":"\"http://rdf.glycoinfo.org/glycan/G89927NS\""},{"id":"GlycanIUPAC_T246","span":{"begin":1175,"end":1180},"obj":"\"http://rdf.glycoinfo.org/glycan/G59665TO\""},{"id":"GlycanIUPAC_T247","span":{"begin":1175,"end":1180},"obj":"\"http://rdf.glycoinfo.org/glycan/G32915EI\""},{"id":"GlycanIUPAC_T248","span":{"begin":1175,"end":1180},"obj":"\"http://rdf.glycoinfo.org/glycan/G60625TS\""}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":57,"end":66},"obj":"Disease"},{"id":"T2","span":{"begin":169,"end":178},"obj":"Disease"},{"id":"T3","span":{"begin":840,"end":849},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":439,"end":443},"obj":"Glycan"},{"id":"T2","span":{"begin":602,"end":608},"obj":"Glycan"},{"id":"T3","span":{"begin":629,"end":632},"obj":"Glycan"},{"id":"T4","span":{"begin":675,"end":678},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G48558GR"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A6","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G30207PZ"},{"id":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G30207PZ"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":439,"end":443},"obj":"Glycan"},{"id":"T2","span":{"begin":602,"end":608},"obj":"Glycan"},{"id":"T3","span":{"begin":629,"end":632},"obj":"Glycan"},{"id":"T4","span":{"begin":675,"end":678},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G48558GR"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A6","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G79389NT"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G79389NT"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G30207PZ"},{"id":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G30207PZ"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"IAV-Glycan_IAV_human_2","denotations":[{"id":"T1","span":{"begin":39,"end":47},"obj":"subtype"},{"id":"T2","span":{"begin":210,"end":214},"obj":"H3N2"},{"id":"T3","span":{"begin":231,"end":235},"obj":"H1N1"},{"id":"T4","span":{"begin":432,"end":435},"obj":"Gal"},{"id":"T5","span":{"begin":622,"end":625},"obj":"Gal"},{"id":"T6","span":{"begin":818,"end":826},"obj":"subtype"},{"id":"T7","span":{"begin":1015,"end":1026},"obj":"sialic acid"},{"id":"T8","span":{"begin":1069,"end":1073},"obj":"H3N2"},{"id":"T9","span":{"begin":1113,"end":1124},"obj":"sialic acid"},{"id":"T10","span":{"begin":1151,"end":1160},"obj":"structure"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":675,"end":678},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0055"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":57,"end":74},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":169,"end":186},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":840,"end":857},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"11320"},{"id":"A2","pred":"db_id","subj":"T2","obj":"11320"},{"id":"A3","pred":"db_id","subj":"T3","obj":"11320"}],"namespaces":[{"prefix":"_base","uri":"https://glycosmos.org/organisms/"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":57,"end":66},"obj":"Disease"},{"id":"T2","span":{"begin":169,"end":178},"obj":"Disease"},{"id":"T3","span":{"begin":840,"end":849},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"MONDO:0005812"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"MONDO:0005812"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"MONDO:0005812"}],"namespaces":[{"prefix":"MONDO","uri":"http://purl.obolibrary.org/obo/MONDO_"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":114},"obj":"Sentence"},{"id":"T2","span":{"begin":115,"end":291},"obj":"Sentence"},{"id":"T3","span":{"begin":292,"end":572},"obj":"Sentence"},{"id":"T4","span":{"begin":573,"end":674},"obj":"Sentence"},{"id":"T5","span":{"begin":675,"end":793},"obj":"Sentence"},{"id":"T6","span":{"begin":794,"end":939},"obj":"Sentence"},{"id":"T7","span":{"begin":940,"end":1187},"obj":"Sentence"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":675,"end":678},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0055"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":57,"end":74},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":169,"end":186},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":840,"end":857},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"11320"},{"id":"A2","pred":"db_id","subj":"T2","obj":"11320"},{"id":"A3","pred":"db_id","subj":"T3","obj":"11320"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"IAV-Glycan_IAV_H1N1_H3N2_human","denotations":[{"id":"T1","span":{"begin":432,"end":435},"obj":"Gal"},{"id":"T2","span":{"begin":622,"end":625},"obj":"Gal"},{"id":"T3","span":{"begin":1015,"end":1026},"obj":"sialic acid"},{"id":"T4","span":{"begin":1113,"end":1124},"obj":"sialic acid"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"IAV-Glycan_IAV_H1N1_human","denotations":[{"id":"T1","span":{"begin":432,"end":435},"obj":"Gal"},{"id":"T2","span":{"begin":622,"end":625},"obj":"Gal"},{"id":"T3","span":{"begin":1015,"end":1026},"obj":"sialic acid"},{"id":"T4","span":{"begin":1113,"end":1124},"obj":"sialic acid"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"IAV-Glycan_IAV_H3N2_human","denotations":[{"id":"T1","span":{"begin":432,"end":435},"obj":"Gal"},{"id":"T2","span":{"begin":622,"end":625},"obj":"Gal"},{"id":"T3","span":{"begin":1015,"end":1026},"obj":"sialic acid"},{"id":"T4","span":{"begin":1113,"end":1124},"obj":"sialic acid"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}

{"project":"IAV-Glycan_IAV_human","denotations":[{"id":"T1","span":{"begin":432,"end":435},"obj":"Gal"},{"id":"T2","span":{"begin":622,"end":625},"obj":"Gal"},{"id":"T3","span":{"begin":1015,"end":1026},"obj":"sialic acid"},{"id":"T4","span":{"begin":1113,"end":1124},"obj":"sialic acid"}],"text":"Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.\nSialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4-(Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain."}