PubMed:1820197 JSON TXT

Annnotations TAB JSON ListView MergeView

Glycan-Motif

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":144,"end":167},"obj":"https://glytoucan.org/Structures/Glycans/G50850NI"},{"id":"T2","span":{"begin":144,"end":167},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

GlyCosmos6-Glycan-Motif-Image

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":144,"end":167},"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":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G50850NI"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":128},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":129,"end":284},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":285,"end":446},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":447,"end":525},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":526,"end":639},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":640,"end":805},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":128},"obj":"Sentence"},{"id":"T2","span":{"begin":129,"end":446},"obj":"Sentence"},{"id":"T3","span":{"begin":447,"end":525},"obj":"Sentence"},{"id":"T4","span":{"begin":526,"end":639},"obj":"Sentence"},{"id":"T5","span":{"begin":640,"end":805},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":128},"obj":"Sentence"},{"id":"T2","span":{"begin":129,"end":284},"obj":"Sentence"},{"id":"T3","span":{"begin":285,"end":446},"obj":"Sentence"},{"id":"T4","span":{"begin":447,"end":525},"obj":"Sentence"},{"id":"T5","span":{"begin":526,"end":639},"obj":"Sentence"},{"id":"T6","span":{"begin":640,"end":805},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":144,"end":167},"obj":"https://glytoucan.org/Structures/Glycans/G50850NI"},{"id":"T2","span":{"begin":144,"end":167},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

GlycoBiology-PACDB

GlycoBiology-FMA

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":9,"end":19},"obj":"FMAID:196729"},{"id":"_T2","span":{"begin":9,"end":19},"obj":"FMAID:82740"},{"id":"_T3","span":{"begin":32,"end":39},"obj":"FMAID:67257"},{"id":"_T4","span":{"begin":32,"end":39},"obj":"FMAID:165447"},{"id":"_T5","span":{"begin":144,"end":167},"obj":"FMAID:196782"},{"id":"_T6","span":{"begin":144,"end":167},"obj":"FMAID:82789"},{"id":"_T7","span":{"begin":144,"end":167},"obj":"FMAID:196783"},{"id":"_T8","span":{"begin":144,"end":167},"obj":"FMAID:82799"},{"id":"_T9","span":{"begin":144,"end":167},"obj":"FMAID:82788"},{"id":"_T10","span":{"begin":144,"end":167},"obj":"FMAID:196794"},{"id":"_T11","span":{"begin":301,"end":311},"obj":"FMAID:167608"},{"id":"_T12","span":{"begin":301,"end":311},"obj":"FMAID:30322"},{"id":"_T13","span":{"begin":301,"end":311},"obj":"FMAID:7145"},{"id":"_T14","span":{"begin":301,"end":311},"obj":"FMAID:93573"},{"id":"_T15","span":{"begin":530,"end":534},"obj":"FMAID:198663"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":52,"end":55},"obj":"http://www.uniprot.org/uniprot/P21941"},{"id":"T2","span":{"begin":312,"end":315},"obj":"http://www.uniprot.org/uniprot/P21941"},{"id":"T3","span":{"begin":125,"end":127},"obj":"http://www.uniprot.org/uniprot/P04264"},{"id":"T4","span":{"begin":252,"end":254},"obj":"http://www.uniprot.org/uniprot/P04264"},{"id":"T5","span":{"begin":296,"end":298},"obj":"http://www.uniprot.org/uniprot/P04264"},{"id":"T6","span":{"begin":144,"end":167},"obj":"http://www.uniprot.org/uniprot/Q9BXD5"},{"id":"T7","span":{"begin":144,"end":167},"obj":"http://www.uniprot.org/uniprot/Q9NR45"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":125,"end":127},"obj":"http://www.uniprot.org/uniprot/P04104"},{"id":"T2","span":{"begin":252,"end":254},"obj":"http://www.uniprot.org/uniprot/P04104"},{"id":"T3","span":{"begin":296,"end":298},"obj":"http://www.uniprot.org/uniprot/P04104"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":108,"end":119},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/561"},{"id":"T2","span":{"begin":235,"end":246},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/561"},{"id":"T3","span":{"begin":259,"end":268},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/482"},{"id":"T4","span":{"begin":259,"end":268},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/481"},{"id":"T5","span":{"begin":259,"end":268},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/206351"},{"id":"T6","span":{"begin":259,"end":281},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/487"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":194,"end":203},"obj":"http://purl.obolibrary.org/obo/GO_0009405"},{"id":"T2","span":{"begin":194,"end":203},"obj":"http://purl.obolibrary.org/obo/GO_0016032"},{"id":"T3","span":{"begin":411,"end":420},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T4","span":{"begin":747,"end":756},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T5","span":{"begin":474,"end":480},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T6","span":{"begin":505,"end":514},"obj":"http://purl.obolibrary.org/obo/GO_0042638"},{"id":"T7","span":{"begin":785,"end":794},"obj":"http://purl.obolibrary.org/obo/GO_0042638"},{"id":"T8","span":{"begin":654,"end":666},"obj":"http://purl.obolibrary.org/obo/GO_0006309"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":301,"end":311},"obj":"http://purl.obolibrary.org/obo/GO_0016020"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

EDAM-topics

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":32,"end":39},"obj":"http://edamontology.org/topic_0078"},{"id":"T2","span":{"begin":32,"end":48},"obj":"http://edamontology.org/topic_3043"},{"id":"T3","span":{"begin":32,"end":48},"obj":"http://edamontology.org/topic_0741"},{"id":"T4","span":{"begin":32,"end":51},"obj":"http://edamontology.org/topic_0623"},{"id":"T5","span":{"begin":40,"end":48},"obj":"http://edamontology.org/topic_0080"},{"id":"T6","span":{"begin":40,"end":48},"obj":"http://edamontology.org/topic_3168"},{"id":"T7","span":{"begin":621,"end":629},"obj":"http://edamontology.org/topic_0080"},{"id":"T8","span":{"begin":621,"end":629},"obj":"http://edamontology.org/topic_3168"},{"id":"T9","span":{"begin":621,"end":638},"obj":"http://edamontology.org/topic_0080"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

EDAM-DFO

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":9,"end":19},"obj":"http://edamontology.org/format_1207"},{"id":"T2","span":{"begin":32,"end":39},"obj":"http://edamontology.org/data_1467"},{"id":"T3","span":{"begin":32,"end":39},"obj":"http://edamontology.org/format_1208"},{"id":"T4","span":{"begin":32,"end":48},"obj":"http://edamontology.org/data_2976"},{"id":"T5","span":{"begin":32,"end":48},"obj":"http://edamontology.org/data_2974"},{"id":"T6","span":{"begin":32,"end":51},"obj":"http://edamontology.org/data_2071"},{"id":"T7","span":{"begin":40,"end":48},"obj":"http://edamontology.org/operation_3218"},{"id":"T8","span":{"begin":40,"end":48},"obj":"http://edamontology.org/data_2044"},{"id":"T9","span":{"begin":588,"end":598},"obj":"http://edamontology.org/data_2611"},{"id":"T10","span":{"begin":588,"end":598},"obj":"http://edamontology.org/data_0842"},{"id":"T11","span":{"begin":613,"end":638},"obj":"http://edamontology.org/operation_0317"},{"id":"T12","span":{"begin":621,"end":629},"obj":"http://edamontology.org/operation_3218"},{"id":"T13","span":{"begin":621,"end":629},"obj":"http://edamontology.org/data_2044"},{"id":"T14","span":{"begin":621,"end":638},"obj":"http://edamontology.org/operation_0258"},{"id":"T15","span":{"begin":621,"end":638},"obj":"http://edamontology.org/operation_3229"},{"id":"T16","span":{"begin":621,"end":638},"obj":"http://edamontology.org/operation_2403"},{"id":"T17","span":{"begin":621,"end":638},"obj":"http://edamontology.org/operation_2408"},{"id":"T18","span":{"begin":621,"end":638},"obj":"http://edamontology.org/operation_2404"},{"id":"T19","span":{"begin":621,"end":638},"obj":"http://edamontology.org/operation_3197"},{"id":"T20","span":{"begin":630,"end":638},"obj":"http://edamontology.org/operation_2945"},{"id":"T21","span":{"begin":698,"end":712},"obj":"http://edamontology.org/data_0844"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

mondo_disease

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":214,"end":251},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0020920"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

Glycan-GlyCosmos

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":56,"end":61},"obj":"Glycan"},{"id":"T2","span":{"begin":316,"end":321},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

GlyCosmos15-MONDO

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":214,"end":251},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0020920"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

GlyCosmos15-NCBITAXON

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":108,"end":124},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":235,"end":251},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":259,"end":281},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":288,"end":295},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":571,"end":578},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"562"},{"id":"A2","pred":"db_id","subj":"T2","obj":"562"},{"id":"A3","pred":"db_id","subj":"T3","obj":"487"},{"id":"A4","pred":"db_id","subj":"T4","obj":"562"},{"id":"A5","pred":"db_id","subj":"T5","obj":"562"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

GlyCosmos15-CL

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":63,"end":67},"obj":"Cell"},{"id":"T3","span":{"begin":129,"end":133},"obj":"Cell"},{"id":"T5","span":{"begin":323,"end":327},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A2","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A4","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A6","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000775"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

sentences

GlyCosmos15-Sentences

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":128},"obj":"Sentence"},{"id":"T2","span":{"begin":129,"end":446},"obj":"Sentence"},{"id":"T3","span":{"begin":447,"end":525},"obj":"Sentence"},{"id":"T4","span":{"begin":526,"end":639},"obj":"Sentence"},{"id":"T5","span":{"begin":640,"end":805},"obj":"Sentence"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

GlyCosmos15-Glycan

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":56,"end":61},"obj":"Glycan"},{"id":"T2","span":{"begin":316,"end":321},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":108,"end":124},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":235,"end":251},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":259,"end":281},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":288,"end":295},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":571,"end":578},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"562"},{"id":"A2","pred":"db_id","subj":"T2","obj":"562"},{"id":"A3","pred":"db_id","subj":"T3","obj":"487"},{"id":"A4","pred":"db_id","subj":"T4","obj":"562"},{"id":"A5","pred":"db_id","subj":"T5","obj":"562"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}

CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":63,"end":67},"obj":"Cell"},{"id":"T3","span":{"begin":129,"end":133},"obj":"Cell"},{"id":"T5","span":{"begin":323,"end":327},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A2","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A4","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A6","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000775"}],"text":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.\nPoly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors."}