PubMed:7620333 JSONTXT

{"project":"GlyCosmos600-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":136,"end":147},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T2","span":{"begin":354,"end":357},"obj":"https://glytoucan.org/Structures/Glycans/G91237TK"},{"id":"T3","span":{"begin":354,"end":357},"obj":"https://glytoucan.org/Structures/Glycans/G56516VH"},{"id":"T4","span":{"begin":382,"end":388},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T5","span":{"begin":427,"end":433},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T6","span":{"begin":542,"end":548},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T7","span":{"begin":622,"end":628},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T8","span":{"begin":657,"end":661},"obj":"https://glytoucan.org/Structures/Glycans/G03277YI"},{"id":"T9","span":{"begin":663,"end":666},"obj":"https://glytoucan.org/Structures/Glycans/G91237TK"},{"id":"T10","span":{"begin":663,"end":666},"obj":"https://glytoucan.org/Structures/Glycans/G56516VH"},{"id":"T11","span":{"begin":671,"end":690},"obj":"https://glytoucan.org/Structures/Glycans/G83513YI"},{"id":"T12","span":{"begin":808,"end":814},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T13","span":{"begin":831,"end":837},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T14","span":{"begin":901,"end":907},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T15","span":{"begin":1019,"end":1025},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T16","span":{"begin":1039,"end":1045},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T17","span":{"begin":1097,"end":1103},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T18","span":{"begin":1276,"end":1287},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T19","span":{"begin":1393,"end":1399},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":136,"end":147},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":354,"end":357},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":382,"end":388},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":427,"end":433},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":542,"end":548},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":622,"end":628},"obj":"Glycan_Motif"},{"id":"T8","span":{"begin":657,"end":661},"obj":"Glycan_Motif"},{"id":"T9","span":{"begin":663,"end":666},"obj":"Glycan_Motif"},{"id":"T11","span":{"begin":671,"end":690},"obj":"Glycan_Motif"},{"id":"T12","span":{"begin":808,"end":814},"obj":"Glycan_Motif"},{"id":"T13","span":{"begin":831,"end":837},"obj":"Glycan_Motif"},{"id":"T14","span":{"begin":901,"end":907},"obj":"Glycan_Motif"},{"id":"T15","span":{"begin":1019,"end":1025},"obj":"Glycan_Motif"},{"id":"T16","span":{"begin":1039,"end":1045},"obj":"Glycan_Motif"},{"id":"T17","span":{"begin":1097,"end":1103},"obj":"Glycan_Motif"},{"id":"T18","span":{"begin":1276,"end":1287},"obj":"Glycan_Motif"},{"id":"T19","span":{"begin":1393,"end":1399},"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/G91237TK"},{"id":"A3","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G56516VH"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"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"},{"id":"A8","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G03277YI"},{"id":"A9","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G91237TK"},{"id":"A10","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G56516VH"},{"id":"A11","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G83513YI"},{"id":"A12","pred":"image","subj":"T12","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A13","pred":"image","subj":"T13","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A14","pred":"image","subj":"T14","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A15","pred":"image","subj":"T15","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A16","pred":"image","subj":"T16","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A17","pred":"image","subj":"T17","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A18","pred":"image","subj":"T18","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A19","pred":"image","subj":"T19","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":136,"end":147},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T2","span":{"begin":354,"end":357},"obj":"https://glytoucan.org/Structures/Glycans/G56516VH"},{"id":"T3","span":{"begin":354,"end":357},"obj":"https://glytoucan.org/Structures/Glycans/G91237TK"},{"id":"T4","span":{"begin":382,"end":388},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T5","span":{"begin":427,"end":433},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T6","span":{"begin":542,"end":548},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T7","span":{"begin":622,"end":628},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T8","span":{"begin":657,"end":661},"obj":"https://glytoucan.org/Structures/Glycans/G03277YI"},{"id":"T9","span":{"begin":663,"end":666},"obj":"https://glytoucan.org/Structures/Glycans/G56516VH"},{"id":"T10","span":{"begin":663,"end":666},"obj":"https://glytoucan.org/Structures/Glycans/G91237TK"},{"id":"T11","span":{"begin":671,"end":690},"obj":"https://glytoucan.org/Structures/Glycans/G83513YI"},{"id":"T12","span":{"begin":808,"end":814},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T13","span":{"begin":831,"end":837},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T14","span":{"begin":901,"end":907},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T15","span":{"begin":1019,"end":1025},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T16","span":{"begin":1039,"end":1045},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T17","span":{"begin":1097,"end":1103},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T18","span":{"begin":1276,"end":1287},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T19","span":{"begin":1393,"end":1399},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":175},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":176,"end":456},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":457,"end":651},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":652,"end":1117},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":1118,"end":1507},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":175},"obj":"Sentence"},{"id":"T2","span":{"begin":176,"end":456},"obj":"Sentence"},{"id":"T3","span":{"begin":457,"end":651},"obj":"Sentence"},{"id":"T4","span":{"begin":652,"end":1117},"obj":"Sentence"},{"id":"T5","span":{"begin":1118,"end":1507},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":657,"end":661},"obj":"http://www.glycoepitope.jp/epitopes/EP0048"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"GlyCosmos600-GlycoEpitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":657,"end":661},"obj":"http://www.glycoepitope.jp/epitopes/EP0048"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"GlyCosmos600-FMA","denotations":[{"id":"T1","span":{"begin":358,"end":370},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"fma_id","subj":"T1","obj":"http://purl.org/sig/ont/fma/fma82816"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"GlyCosmos600-GlycoGenes2","denotations":[{"id":"T1","span":{"begin":354,"end":357},"obj":"https://acgg.asia/db/ggdb/info/gg052"},{"id":"T2","span":{"begin":663,"end":666},"obj":"https://acgg.asia/db/ggdb/info/gg052"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"glycosmos-test-glycan-structure","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":354,"end":357},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa15/trivialname"},{"id":"PD-GlycanStructures-B_T2","span":{"begin":663,"end":666},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa15/trivialname"},{"id":"PD-GlycanStructures-B_T3","span":{"begin":354,"end":357},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa50/trivialname"},{"id":"PD-GlycanStructures-B_T4","span":{"begin":663,"end":666},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa50/trivialname"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"glycosmos-test-structure-v1","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":354,"end":357},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa15/trivialname"},{"id":"PD-GlycanStructures-B_T3","span":{"begin":354,"end":357},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa50/trivialname"},{"id":"PD-GlycanStructures-B_T2","span":{"begin":663,"end":666},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa15/trivialname"},{"id":"PD-GlycanStructures-B_T4","span":{"begin":663,"end":666},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa50/trivialname"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"GlyCosmos600-MAT","denotations":[{"id":"PD-MAT-B_T1","span":{"begin":313,"end":320},"obj":"http://purl.obolibrary.org/obo/MAT_0000343"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

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of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":13,"end":28},"obj":"Disease"},{"id":"T2","span":{"begin":193,"end":208},"obj":"Disease"},{"id":"T3","span":{"begin":1197,"end":1212},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005460"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005460"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0005460"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":354,"end":357},"obj":"Glycan"},{"id":"T2","span":{"begin":382,"end":388},"obj":"Glycan"},{"id":"T3","span":{"begin":427,"end":433},"obj":"Glycan"},{"id":"T4","span":{"begin":542,"end":548},"obj":"Glycan"},{"id":"T5","span":{"begin":622,"end":628},"obj":"Glycan"},{"id":"T6","span":{"begin":657,"end":661},"obj":"Glycan"},{"id":"T7","span":{"begin":663,"end":666},"obj":"Glycan"},{"id":"T8","span":{"begin":808,"end":814},"obj":"Glycan"},{"id":"T9","span":{"begin":831,"end":837},"obj":"Glycan"},{"id":"T10","span":{"begin":901,"end":907},"obj":"Glycan"},{"id":"T11","span":{"begin":1019,"end":1025},"obj":"Glycan"},{"id":"T12","span":{"begin":1039,"end":1045},"obj":"Glycan"},{"id":"T13","span":{"begin":1097,"end":1103},"obj":"Glycan"},{"id":"T14","span":{"begin":1393,"end":1399},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G91237TK"},{"id":"A15","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G91237TK"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A16","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/G76685HR"},{"id":"A17","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A18","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A19","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/G03277YI"},{"id":"A20","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G03277YI"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G91237TK"},{"id":"A21","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G91237TK"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A22","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A23","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A24","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A11","pred":"glycosmos_id","subj":"T11","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A25","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A12","pred":"glycosmos_id","subj":"T12","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A26","pred":"image","subj":"T12","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A13","pred":"glycosmos_id","subj":"T13","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A27","pred":"image","subj":"T13","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A14","pred":"glycosmos_id","subj":"T14","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A28","pred":"image","subj":"T14","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":657,"end":661},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0048"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":13,"end":28},"obj":"Disease"},{"id":"T2","span":{"begin":193,"end":208},"obj":"Disease"},{"id":"T3","span":{"begin":1197,"end":1212},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005460"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005460"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0005460"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":13,"end":18},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":19,"end":38},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":193,"end":198},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":199,"end":218},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1197,"end":1202},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":1203,"end":1222},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9823"},{"id":"A2","pred":"db_id","subj":"T2","obj":"11320"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9823"},{"id":"A4","pred":"db_id","subj":"T4","obj":"11320"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9823"},{"id":"A6","pred":"db_id","subj":"T6","obj":"11320"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":175},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":176,"end":456},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":457,"end":651},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":652,"end":1117},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":1118,"end":1507},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":175},"obj":"Sentence"},{"id":"T2","span":{"begin":176,"end":456},"obj":"Sentence"},{"id":"T3","span":{"begin":457,"end":651},"obj":"Sentence"},{"id":"T4","span":{"begin":652,"end":1117},"obj":"Sentence"},{"id":"T5","span":{"begin":1118,"end":1507},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":175},"obj":"Sentence"},{"id":"T2","span":{"begin":176,"end":456},"obj":"Sentence"},{"id":"T3","span":{"begin":457,"end":651},"obj":"Sentence"},{"id":"T4","span":{"begin":652,"end":1117},"obj":"Sentence"},{"id":"T5","span":{"begin":1118,"end":1507},"obj":"Sentence"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":354,"end":357},"obj":"Glycan"},{"id":"T2","span":{"begin":382,"end":388},"obj":"Glycan"},{"id":"T3","span":{"begin":427,"end":433},"obj":"Glycan"},{"id":"T4","span":{"begin":542,"end":548},"obj":"Glycan"},{"id":"T5","span":{"begin":622,"end":628},"obj":"Glycan"},{"id":"T6","span":{"begin":657,"end":661},"obj":"Glycan"},{"id":"T7","span":{"begin":663,"end":666},"obj":"Glycan"},{"id":"T8","span":{"begin":808,"end":814},"obj":"Glycan"},{"id":"T9","span":{"begin":831,"end":837},"obj":"Glycan"},{"id":"T10","span":{"begin":901,"end":907},"obj":"Glycan"},{"id":"T11","span":{"begin":1019,"end":1025},"obj":"Glycan"},{"id":"T12","span":{"begin":1039,"end":1045},"obj":"Glycan"},{"id":"T13","span":{"begin":1097,"end":1103},"obj":"Glycan"},{"id":"T14","span":{"begin":1393,"end":1399},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G91237TK"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"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/G03277YI"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G91237TK"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A11","pred":"glycosmos_id","subj":"T11","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A12","pred":"glycosmos_id","subj":"T12","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A13","pred":"glycosmos_id","subj":"T13","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A14","pred":"glycosmos_id","subj":"T14","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A15","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G91237TK"},{"id":"A16","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A17","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A18","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A19","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A20","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G03277YI"},{"id":"A21","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G91237TK"},{"id":"A22","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A23","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A24","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A25","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A26","pred":"image","subj":"T12","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A27","pred":"image","subj":"T13","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A28","pred":"image","subj":"T14","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":657,"end":661},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0048"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":13,"end":18},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":19,"end":38},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":193,"end":198},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":199,"end":218},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1197,"end":1202},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":1203,"end":1222},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9823"},{"id":"A2","pred":"db_id","subj":"T2","obj":"11320"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9823"},{"id":"A4","pred":"db_id","subj":"T4","obj":"11320"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9823"},{"id":"A6","pred":"db_id","subj":"T6","obj":"11320"}],"text":"Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation.\nThe sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930."}