PubMed:14736728 / 1025-1271 JSONTXT

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    GlycoBiology-FMA

    {"project":"GlycoBiology-FMA","denotations":[{"id":"_T19","span":{"begin":149,"end":156},"obj":"FMAID:67257"},{"id":"_T20","span":{"begin":149,"end":156},"obj":"FMAID:165447"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"The electrophoretic mobility of the immunoprecipitated mutant p.Asn286Ser CLN2 was increased by approximately 2 kDa compared with the wild-type CLN2 protein, whereas deglycosylation led to the generation of polypeptides of the same apparent size."}

    GlycoBiology-NCBITAXON

    {"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T4","span":{"begin":4,"end":19},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/8004"}],"text":"The electrophoretic mobility of the immunoprecipitated mutant p.Asn286Ser CLN2 was increased by approximately 2 kDa compared with the wild-type CLN2 protein, whereas deglycosylation led to the generation of polypeptides of the same apparent size."}

    sentences

    {"project":"sentences","denotations":[{"id":"TextSentencer_T8","span":{"begin":0,"end":246},"obj":"Sentence"},{"id":"T8","span":{"begin":0,"end":246},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The electrophoretic mobility of the immunoprecipitated mutant p.Asn286Ser CLN2 was increased by approximately 2 kDa compared with the wild-type CLN2 protein, whereas deglycosylation led to the generation of polypeptides of the same apparent size."}

    EDAM-topics

    {"project":"EDAM-topics","denotations":[{"id":"T11","span":{"begin":36,"end":54},"obj":"http://edamontology.org/topic_3557"},{"id":"T12","span":{"begin":149,"end":156},"obj":"http://edamontology.org/topic_0078"}],"text":"The electrophoretic mobility of the immunoprecipitated mutant p.Asn286Ser CLN2 was increased by approximately 2 kDa compared with the wild-type CLN2 protein, whereas deglycosylation led to the generation of polypeptides of the same apparent size."}

    EDAM-DFO

    {"project":"EDAM-DFO","denotations":[{"id":"T14","span":{"begin":149,"end":156},"obj":"http://edamontology.org/format_1208"},{"id":"T15","span":{"begin":149,"end":156},"obj":"http://edamontology.org/data_1467"},{"id":"T16","span":{"begin":193,"end":203},"obj":"http://edamontology.org/operation_3429"}],"text":"The electrophoretic mobility of the immunoprecipitated mutant p.Asn286Ser CLN2 was increased by approximately 2 kDa compared with the wild-type CLN2 protein, whereas deglycosylation led to the generation of polypeptides of the same apparent size."}

    GlyCosmos600-FMA

    {"project":"GlyCosmos600-FMA","denotations":[{"id":"T7","span":{"begin":149,"end":156},"obj":"Body_part"}],"attributes":[{"id":"A7","pred":"fma_id","subj":"T7","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"The electrophoretic mobility of the immunoprecipitated mutant p.Asn286Ser CLN2 was increased by approximately 2 kDa compared with the wild-type CLN2 protein, whereas deglycosylation led to the generation of polypeptides of the same apparent size."}

    pubmed-enju-pas

    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electrophoretic mobility of the immunoprecipitated mutant p.Asn286Ser CLN2 was increased by approximately 2 kDa compared with the wild-type CLN2 protein, whereas deglycosylation led to the generation of polypeptides of the same apparent size."}