PubMed:11159917 / 950-1313 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T5","span":{"begin":0,"end":363},"obj":"Sentence"},{"id":"T5","span":{"begin":0,"end":363},"obj":"Sentence"},{"id":"T5","span":{"begin":0,"end":363},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Gel filtration analysis of the pronase-resistant gC-1 O-glycan clusters from a glycoprotein mutant, lacking a site for N-linked glycosylation at Asn 73 in the vicinity of the O-glycosylation signal, suggested that one function of this N-linked glycan was to modulate the access for GalNAc transferases to one particular O-glycosylation peptide signal (aa 80-104)."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T21","span":{"begin":79,"end":91},"obj":"FMAID:62925"},{"id":"_T22","span":{"begin":79,"end":91},"obj":"FMAID:167256"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Gel filtration analysis of the pronase-resistant gC-1 O-glycan clusters from a glycoprotein mutant, lacking a site for N-linked glycosylation at Asn 73 in the vicinity of the O-glycosylation signal, suggested that one function of this N-linked glycan was to modulate the access for GalNAc transferases to one particular O-glycosylation peptide signal (aa 80-104)."}

{"project":"uniprot-human","denotations":[{"id":"T2","span":{"begin":289,"end":301},"obj":"http://www.uniprot.org/uniprot/Q99484"}],"text":"Gel filtration analysis of the pronase-resistant gC-1 O-glycan clusters from a glycoprotein mutant, lacking a site for N-linked glycosylation at Asn 73 in the vicinity of the O-glycosylation signal, suggested that one function of this N-linked glycan was to modulate the access for GalNAc transferases to one particular O-glycosylation peptide signal (aa 80-104)."}

{"project":"uniprot-mouse","denotations":[{"id":"T2","span":{"begin":289,"end":301},"obj":"http://www.uniprot.org/uniprot/P38649"},{"id":"T5","span":{"begin":145,"end":148},"obj":"http://www.uniprot.org/uniprot/Q61024"}],"text":"Gel filtration analysis of the pronase-resistant gC-1 O-glycan clusters from a glycoprotein mutant, lacking a site for N-linked glycosylation at Asn 73 in the vicinity of the O-glycosylation signal, suggested that one function of this N-linked glycan was to modulate the access for GalNAc transferases to one particular O-glycosylation peptide signal (aa 80-104)."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T8","span":{"begin":352,"end":354},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/152839"}],"text":"Gel filtration analysis of the pronase-resistant gC-1 O-glycan clusters from a glycoprotein mutant, lacking a site for N-linked glycosylation at Asn 73 in the vicinity of the O-glycosylation signal, suggested that one function of this N-linked glycan was to modulate the access for GalNAc transferases to one particular O-glycosylation peptide signal (aa 80-104)."}

{"project":"GO-BP","denotations":[{"id":"T5","span":{"begin":128,"end":141},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T6","span":{"begin":177,"end":190},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T7","span":{"begin":322,"end":335},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T14","span":{"begin":191,"end":197},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T15","span":{"begin":344,"end":350},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T16","span":{"begin":119,"end":141},"obj":"http://purl.obolibrary.org/obo/GO_0006487"}],"text":"Gel filtration analysis of the pronase-resistant gC-1 O-glycan clusters from a glycoprotein mutant, lacking a site for N-linked glycosylation at Asn 73 in the vicinity of the O-glycosylation signal, suggested that one function of this N-linked glycan was to modulate the access for GalNAc transferases to one particular O-glycosylation peptide signal (aa 80-104)."}

{"project":"EDAM-topics","denotations":[{"id":"T6","span":{"begin":336,"end":343},"obj":"http://edamontology.org/topic_0154"}],"text":"Gel filtration analysis of the pronase-resistant gC-1 O-glycan clusters from a glycoprotein mutant, lacking a site for N-linked glycosylation at Asn 73 in the vicinity of the O-glycosylation signal, suggested that one function of this N-linked glycan was to modulate the access for GalNAc transferases to one particular O-glycosylation peptide signal (aa 80-104)."}

{"project":"EDAM-DFO","denotations":[{"id":"T15","span":{"begin":15,"end":23},"obj":"http://edamontology.org/operation_2945"},{"id":"T16","span":{"begin":63,"end":71},"obj":"http://edamontology.org/operation_3432"},{"id":"T17","span":{"begin":336,"end":343},"obj":"http://edamontology.org/data_2906"}],"text":"Gel filtration analysis of the pronase-resistant gC-1 O-glycan clusters from a glycoprotein mutant, lacking a site for N-linked glycosylation at Asn 73 in the vicinity of the O-glycosylation signal, suggested that one function of this N-linked glycan was to modulate the access for GalNAc transferases to one particular O-glycosylation peptide signal (aa 80-104)."}

{"project":"Lectin","denotations":[{"id":"Lectin_T5","span":{"begin":49,"end":53},"obj":"https://acgg.asia/db/lfdb/LfDB0053"}],"text":"Gel filtration analysis of the pronase-resistant gC-1 O-glycan clusters from a glycoprotein mutant, lacking a site for N-linked glycosylation at Asn 73 in the vicinity of the O-glycosylation signal, suggested that one function of this N-linked glycan was to modulate the access for GalNAc transferases to one particular O-glycosylation peptide signal (aa 80-104)."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T2","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G23425WZ\""},{"id":"GlycanIUPAC_T8","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G02874VH\""},{"id":"GlycanIUPAC_T14","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G99699DW\""},{"id":"GlycanIUPAC_T20","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G22074RM\""},{"id":"GlycanIUPAC_T26","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G48535VZ\""},{"id":"GlycanIUPAC_T32","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G39738WL\""},{"id":"GlycanIUPAC_T38","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G42313WU\""},{"id":"GlycanIUPAC_T44","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G00393CK\""},{"id":"GlycanIUPAC_T50","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G42649EX\""},{"id":"GlycanIUPAC_T56","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G46880SB\""},{"id":"GlycanIUPAC_T62","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G75599IR\""},{"id":"GlycanIUPAC_T68","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G58985MU\""},{"id":"GlycanIUPAC_T74","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G92517PO\""},{"id":"GlycanIUPAC_T80","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G88512YL\""},{"id":"GlycanIUPAC_T86","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G41473NX\""},{"id":"GlycanIUPAC_T92","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G71089RB\""},{"id":"GlycanIUPAC_T98","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G73485GZ\""},{"id":"GlycanIUPAC_T104","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G61406KC\""},{"id":"GlycanIUPAC_T110","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G34412GZ\""},{"id":"GlycanIUPAC_T116","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G67209FP\""},{"id":"GlycanIUPAC_T122","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G61442IL\""},{"id":"GlycanIUPAC_T128","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G93729MV\""},{"id":"GlycanIUPAC_T134","span":{"begin":282,"end":288},"obj":"\"http://rdf.glycoinfo.org/glycan/G92144AE\""}],"text":"Gel filtration analysis of the pronase-resistant gC-1 O-glycan clusters from a glycoprotein mutant, lacking a site for N-linked glycosylation at Asn 73 in the vicinity of the O-glycosylation signal, suggested that one function of this N-linked glycan was to modulate the access for GalNAc transferases to one particular O-glycosylation peptide signal (aa 80-104)."}