PubMed:11030742 / 0-354 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":113},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":114,"end":327},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":113},"obj":"Sentence"},{"id":"T2","span":{"begin":114,"end":327},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":113},"obj":"Sentence"},{"id":"T2","span":{"begin":114,"end":327},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.\nAlthough glycosylation appears to protect prion protein (PrP(C)) from the conformational transition to the disease-associated scrapie form (PrP(Sc)), available NMR structures are for non-glycosylated PrP(C), only. To investigate the influen"}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":45,"end":52},"obj":"FMAID:165447"},{"id":"_T2","span":{"begin":45,"end":52},"obj":"FMAID:67257"},{"id":"_T3","span":{"begin":77,"end":93},"obj":"FMAID:82742"},{"id":"_T4","span":{"begin":77,"end":93},"obj":"FMAID:196731"},{"id":"_T5","span":{"begin":162,"end":169},"obj":"FMAID:165447"},{"id":"_T6","span":{"begin":162,"end":169},"obj":"FMAID:67257"},{"id":"_T7","span":{"begin":203,"end":213},"obj":"FMAID:70637"},{"id":"_T8","span":{"begin":203,"end":213},"obj":"FMAID:171495"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.\nAlthough glycosylation appears to protect prion protein (PrP(C)) from the conformational transition to the disease-associated scrapie form (PrP(Sc)), available NMR structures are for non-glycosylated PrP(C), only. To investigate the influen"}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":102,"end":105},"obj":"http://www.uniprot.org/uniprot/P06744"}],"text":"Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.\nAlthough glycosylation appears to protect prion protein (PrP(C)) from the conformational transition to the disease-associated scrapie form (PrP(Sc)), available NMR structures are for non-glycosylated PrP(C), only. To investigate the influen"}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":102,"end":105},"obj":"http://www.uniprot.org/uniprot/Q8C675"}],"text":"Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.\nAlthough glycosylation appears to protect prion protein (PrP(C)) from the conformational transition to the disease-associated scrapie form (PrP(Sc)), available NMR structures are for non-glycosylated PrP(C), only. To investigate the influen"}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":39,"end":44},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/94193"},{"id":"T2","span":{"begin":39,"end":44},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/94464"},{"id":"T3","span":{"begin":156,"end":161},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/94193"},{"id":"T4","span":{"begin":156,"end":161},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/94464"},{"id":"T5","span":{"begin":297,"end":300},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/604139"}],"text":"Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.\nAlthough glycosylation appears to protect prion protein (PrP(C)) from the conformational transition to the disease-associated scrapie form (PrP(Sc)), available NMR structures are for non-glycosylated PrP(C), only. To investigate the influen"}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":123,"end":136},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T2","span":{"begin":301,"end":313},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.\nAlthough glycosylation appears to protect prion protein (PrP(C)) from the conformational transition to the disease-associated scrapie form (PrP(Sc)), available NMR structures are for non-glycosylated PrP(C), only. To investigate the influen"}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":106,"end":112},"obj":"http://purl.obolibrary.org/obo/GO_0043495"}],"text":"Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.\nAlthough glycosylation appears to protect prion protein (PrP(C)) from the conformational transition to the disease-associated scrapie form (PrP(Sc)), available NMR structures are for non-glycosylated PrP(C), only. To investigate the influen"}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":0,"end":18},"obj":"http://edamontology.org/topic_0176"},{"id":"T2","span":{"begin":33,"end":38},"obj":"http://edamontology.org/topic_2815"},{"id":"T3","span":{"begin":45,"end":52},"obj":"http://edamontology.org/topic_0078"},{"id":"T4","span":{"begin":162,"end":169},"obj":"http://edamontology.org/topic_0078"},{"id":"T5","span":{"begin":221,"end":228},"obj":"http://edamontology.org/topic_0634"},{"id":"T6","span":{"begin":274,"end":277},"obj":"http://edamontology.org/topic_0593"}],"text":"Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.\nAlthough glycosylation appears to protect prion protein (PrP(C)) from the conformational transition to the disease-associated scrapie form (PrP(Sc)), available NMR structures are for non-glycosylated PrP(C), only. To investigate the influen"}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":0,"end":29},"obj":"http://edamontology.org/operation_2476"},{"id":"T2","span":{"begin":45,"end":52},"obj":"http://edamontology.org/data_1467"},{"id":"T3","span":{"begin":45,"end":52},"obj":"http://edamontology.org/format_1208"},{"id":"T4","span":{"begin":162,"end":169},"obj":"http://edamontology.org/data_1467"},{"id":"T5","span":{"begin":162,"end":169},"obj":"http://edamontology.org/format_1208"},{"id":"T6","span":{"begin":278,"end":288},"obj":"http://edamontology.org/data_0883"}],"text":"Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.\nAlthough glycosylation appears to protect prion protein (PrP(C)) from the conformational transition to the disease-associated scrapie form (PrP(Sc)), available NMR structures are for non-glycosylated PrP(C), only. To investigate the influen"}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":102,"end":112},"obj":"http://rdf.glycoinfo.org/glycan/G00045MO"}],"text":"Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.\nAlthough glycosylation appears to protect prion protein (PrP(C)) from the conformational transition to the disease-associated scrapie form (PrP(Sc)), available NMR structures are for non-glycosylated PrP(C), only. To investigate the influen"}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":297,"end":300},"obj":"\"http://rdf.glycoinfo.org/glycan/G02780QX\""},{"id":"GlycanIUPAC_T2","span":{"begin":297,"end":300},"obj":"\"http://rdf.glycoinfo.org/glycan/G18425DX\""},{"id":"GlycanIUPAC_T3","span":{"begin":297,"end":300},"obj":"\"http://rdf.glycoinfo.org/glycan/G18630JE\""},{"id":"GlycanIUPAC_T4","span":{"begin":297,"end":300},"obj":"\"http://rdf.glycoinfo.org/glycan/G01004IT\""},{"id":"GlycanIUPAC_T5","span":{"begin":297,"end":300},"obj":"\"http://rdf.glycoinfo.org/glycan/G87301QZ\""},{"id":"GlycanIUPAC_T6","span":{"begin":297,"end":300},"obj":"\"http://rdf.glycoinfo.org/glycan/G39790GW\""},{"id":"GlycanIUPAC_T7","span":{"begin":297,"end":300},"obj":"\"http://rdf.glycoinfo.org/glycan/G42928BB\""},{"id":"GlycanIUPAC_T8","span":{"begin":297,"end":300},"obj":"\"http://rdf.glycoinfo.org/glycan/G51134HC\""},{"id":"GlycanIUPAC_T9","span":{"begin":297,"end":300},"obj":"\"http://rdf.glycoinfo.org/glycan/G68183GR\""},{"id":"GlycanIUPAC_T10","span":{"begin":297,"end":300},"obj":"\"http://rdf.glycoinfo.org/glycan/G46883FA\""},{"id":"GlycanIUPAC_T11","span":{"begin":297,"end":300},"obj":"\"http://rdf.glycoinfo.org/glycan/G54702VY\""}],"text":"Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.\nAlthough glycosylation appears to protect prion protein (PrP(C)) from the conformational transition to the disease-associated scrapie form (PrP(Sc)), available NMR structures are for non-glycosylated PrP(C), only. To investigate the influen"}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":240,"end":247},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0006961"}],"text":"Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.\nAlthough glycosylation appears to protect prion protein (PrP(C)) from the conformational transition to the disease-associated scrapie form (PrP(Sc)), available NMR structures are for non-glycosylated PrP(C), only. To investigate the influen"}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":33,"end":38},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.\nAlthough glycosylation appears to protect prion protein (PrP(C)) from the conformational transition to the disease-associated scrapie form (PrP(Sc)), available NMR structures are for non-glycosylated PrP(C), only. To investigate the influen"}