PubMed:1983782 / 1112-1311 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T8","span":{"begin":0,"end":199},"obj":"Sentence"},{"id":"T8","span":{"begin":0,"end":199},"obj":"Sentence"},{"id":"T8","span":{"begin":0,"end":199},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Our results indicate that both single-site mutant prion proteins are glycosylated at non-mutated sites and they suggest that both potential sites for Asn-linked glycosylation are utilized in wt PrPC."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T50","span":{"begin":56,"end":64},"obj":"FMAID:165447"},{"id":"_T51","span":{"begin":56,"end":64},"obj":"FMAID:67257"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Our results indicate that both single-site mutant prion proteins are glycosylated at non-mutated sites and they suggest that both potential sites for Asn-linked glycosylation are utilized in wt PrPC."}

{"project":"uniprot-mouse","denotations":[{"id":"T5","span":{"begin":150,"end":153},"obj":"http://www.uniprot.org/uniprot/Q61024"}],"text":"Our results indicate that both single-site mutant prion proteins are glycosylated at non-mutated sites and they suggest that both potential sites for Asn-linked glycosylation are utilized in wt PrPC."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T8","span":{"begin":50,"end":55},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/94193"},{"id":"T9","span":{"begin":50,"end":55},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/94464"},{"id":"T10","span":{"begin":85,"end":88},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/604139"}],"text":"Our results indicate that both single-site mutant prion proteins are glycosylated at non-mutated sites and they suggest that both potential sites for Asn-linked glycosylation are utilized in wt PrPC."}

{"project":"GO-BP","denotations":[{"id":"T5","span":{"begin":69,"end":81},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T7","span":{"begin":56,"end":81},"obj":"http://purl.obolibrary.org/obo/GO_0006486"}],"text":"Our results indicate that both single-site mutant prion proteins are glycosylated at non-mutated sites and they suggest that both potential sites for Asn-linked glycosylation are utilized in wt PrPC."}

{"project":"EDAM-topics","denotations":[{"id":"T13","span":{"begin":56,"end":64},"obj":"http://edamontology.org/topic_0078"},{"id":"T14","span":{"begin":89,"end":96},"obj":"http://edamontology.org/topic_0199"}],"text":"Our results indicate that both single-site mutant prion proteins are glycosylated at non-mutated sites and they suggest that both potential sites for Asn-linked glycosylation are utilized in wt PrPC."}

{"project":"EDAM-DFO","denotations":[{"id":"T14","span":{"begin":56,"end":64},"obj":"http://edamontology.org/data_1467"},{"id":"T15","span":{"begin":56,"end":64},"obj":"http://edamontology.org/format_1208"}],"text":"Our results indicate that both single-site mutant prion proteins are glycosylated at non-mutated sites and they suggest that both potential sites for Asn-linked glycosylation are utilized in wt PrPC."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T523","span":{"begin":85,"end":88},"obj":"\"http://rdf.glycoinfo.org/glycan/G02780QX\""},{"id":"GlycanIUPAC_T524","span":{"begin":85,"end":88},"obj":"\"http://rdf.glycoinfo.org/glycan/G18425DX\""},{"id":"GlycanIUPAC_T525","span":{"begin":85,"end":88},"obj":"\"http://rdf.glycoinfo.org/glycan/G18630JE\""},{"id":"GlycanIUPAC_T526","span":{"begin":85,"end":88},"obj":"\"http://rdf.glycoinfo.org/glycan/G01004IT\""},{"id":"GlycanIUPAC_T527","span":{"begin":85,"end":88},"obj":"\"http://rdf.glycoinfo.org/glycan/G87301QZ\""},{"id":"GlycanIUPAC_T528","span":{"begin":85,"end":88},"obj":"\"http://rdf.glycoinfo.org/glycan/G39790GW\""},{"id":"GlycanIUPAC_T529","span":{"begin":85,"end":88},"obj":"\"http://rdf.glycoinfo.org/glycan/G42928BB\""},{"id":"GlycanIUPAC_T530","span":{"begin":85,"end":88},"obj":"\"http://rdf.glycoinfo.org/glycan/G51134HC\""},{"id":"GlycanIUPAC_T531","span":{"begin":85,"end":88},"obj":"\"http://rdf.glycoinfo.org/glycan/G68183GR\""},{"id":"GlycanIUPAC_T532","span":{"begin":85,"end":88},"obj":"\"http://rdf.glycoinfo.org/glycan/G46883FA\""},{"id":"GlycanIUPAC_T533","span":{"begin":85,"end":88},"obj":"\"http://rdf.glycoinfo.org/glycan/G54702VY\""}],"text":"Our results indicate that both single-site mutant prion proteins are glycosylated at non-mutated sites and they suggest that both potential sites for Asn-linked glycosylation are utilized in wt PrPC."}