PMC:7253482 / 11710-12426 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"379","span":{"begin":520,"end":524},"obj":"Gene"},{"id":"380","span":{"begin":552,"end":556},"obj":"Gene"},{"id":"381","span":{"begin":210,"end":226},"obj":"Chemical"},{"id":"382","span":{"begin":442,"end":449},"obj":"Chemical"},{"id":"383","span":{"begin":475,"end":487},"obj":"Chemical"},{"id":"384","span":{"begin":115,"end":119},"obj":"Disease"},{"id":"385","span":{"begin":144,"end":148},"obj":"Disease"},{"id":"386","span":{"begin":232,"end":236},"obj":"Disease"},{"id":"387","span":{"begin":243,"end":247},"obj":"Disease"},{"id":"388","span":{"begin":373,"end":377},"obj":"Disease"},{"id":"389","span":{"begin":400,"end":404},"obj":"Disease"},{"id":"390","span":{"begin":584,"end":588},"obj":"Disease"},{"id":"391","span":{"begin":593,"end":597},"obj":"Disease"}],"attributes":[{"id":"A379","pred":"tao:has_database_id","subj":"379","obj":"Gene:1803"},{"id":"A380","pred":"tao:has_database_id","subj":"380","obj":"Gene:59272"},{"id":"A382","pred":"tao:has_database_id","subj":"382","obj":"MESH:D011134"},{"id":"A384","pred":"tao:has_database_id","subj":"384","obj":"MESH:D018352"},{"id":"A385","pred":"tao:has_database_id","subj":"385","obj":"MESH:D045169"},{"id":"A386","pred":"tao:has_database_id","subj":"386","obj":"MESH:D018352"},{"id":"A387","pred":"tao:has_database_id","subj":"387","obj":"MESH:D045169"},{"id":"A388","pred":"tao:has_database_id","subj":"388","obj":"MESH:D018352"},{"id":"A389","pred":"tao:has_database_id","subj":"389","obj":"MESH:D045169"},{"id":"A390","pred":"tao:has_database_id","subj":"390","obj":"MESH:D018352"},{"id":"A391","pred":"tao:has_database_id","subj":"391","obj":"MESH:D045169"}],"namespaces":[{"prefix":"Tax","uri":"https://www.ncbi.nlm.nih.gov/taxonomy/"},{"prefix":"MESH","uri":"https://id.nlm.nih.gov/mesh/"},{"prefix":"Gene","uri":"https://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"CVCL","uri":"https://web.expasy.org/cellosaurus/CVCL_"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T71","span":{"begin":167,"end":180},"obj":"Body_part"},{"id":"T72","span":{"begin":250,"end":258},"obj":"Body_part"},{"id":"T73","span":{"begin":423,"end":436},"obj":"Body_part"}],"attributes":[{"id":"A71","pred":"fma_id","subj":"T71","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A72","pred":"fma_id","subj":"T72","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A73","pred":"fma_id","subj":"T73","obj":"http://purl.org/sig/ont/fma/fma62925"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T42","span":{"begin":144,"end":148},"obj":"Disease"},{"id":"T43","span":{"begin":243,"end":247},"obj":"Disease"},{"id":"T44","span":{"begin":400,"end":404},"obj":"Disease"},{"id":"T45","span":{"begin":593,"end":597},"obj":"Disease"}],"attributes":[{"id":"A42","pred":"mondo_id","subj":"T42","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A43","pred":"mondo_id","subj":"T43","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A44","pred":"mondo_id","subj":"T44","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A45","pred":"mondo_id","subj":"T45","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T67","span":{"begin":113,"end":114},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T68","span":{"begin":135,"end":137},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T69","span":{"begin":142,"end":143},"obj":"http://purl.obolibrary.org/obo/CLO_0001021"},{"id":"T70","span":{"begin":164,"end":166},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T71","span":{"begin":230,"end":231},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T72","span":{"begin":241,"end":242},"obj":"http://purl.obolibrary.org/obo/CLO_0001021"},{"id":"T73","span":{"begin":393,"end":395},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T74","span":{"begin":420,"end":422},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T75","span":{"begin":646,"end":648},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T76","span":{"begin":653,"end":655},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T77","span":{"begin":653,"end":655},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T131","span":{"begin":127,"end":129},"obj":"Chemical"},{"id":"T132","span":{"begin":156,"end":158},"obj":"Chemical"},{"id":"T133","span":{"begin":167,"end":180},"obj":"Chemical"},{"id":"T134","span":{"begin":219,"end":226},"obj":"Chemical"},{"id":"T135","span":{"begin":250,"end":258},"obj":"Chemical"},{"id":"T136","span":{"begin":385,"end":387},"obj":"Chemical"},{"id":"T137","span":{"begin":412,"end":414},"obj":"Chemical"},{"id":"T138","span":{"begin":423,"end":436},"obj":"Chemical"},{"id":"T139","span":{"begin":442,"end":449},"obj":"Chemical"},{"id":"T140","span":{"begin":653,"end":655},"obj":"Chemical"}],"attributes":[{"id":"A131","pred":"chebi_id","subj":"T131","obj":"http://purl.obolibrary.org/obo/CHEBI_141439"},{"id":"A132","pred":"chebi_id","subj":"T132","obj":"http://purl.obolibrary.org/obo/CHEBI_141439"},{"id":"A133","pred":"chebi_id","subj":"T133","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A134","pred":"chebi_id","subj":"T134","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A135","pred":"chebi_id","subj":"T135","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A136","pred":"chebi_id","subj":"T136","obj":"http://purl.obolibrary.org/obo/CHEBI_141439"},{"id":"A137","pred":"chebi_id","subj":"T137","obj":"http://purl.obolibrary.org/obo/CHEBI_141439"},{"id":"A138","pred":"chebi_id","subj":"T138","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A139","pred":"chebi_id","subj":"T139","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A140","pred":"chebi_id","subj":"T140","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T31","span":{"begin":542,"end":547},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T32","span":{"begin":574,"end":579},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-sample-Enju","denotations":[{"id":"T33108","span":{"begin":0,"end":3},"obj":"DT"},{"id":"T5164","span":{"begin":4,"end":13},"obj":"NN"},{"id":"T85081","span":{"begin":14,"end":16},"obj":"IN"},{"id":"T78202","span":{"begin":17,"end":20},"obj":"DT"},{"id":"T60050","span":{"begin":21,"end":35},"obj":"RB"},{"id":"T4820","span":{"begin":36,"end":44},"obj":"VBN"},{"id":"T14194","span":{"begin":45,"end":58},"obj":"NN"},{"id":"T67945","span":{"begin":59,"end":61},"obj":"VBZ"},{"id":"T60933","span":{"begin":62,"end":73},"obj":"VBN"},{"id":"T74928","span":{"begin":74,"end":76},"obj":"IN"},{"id":"T84730","span":{"begin":77,"end":80},"obj":"DT"},{"id":"T26156","span":{"begin":81,"end":90},"obj":"NN"},{"id":"T35915","span":{"begin":91,"end":100},"obj":"NN"},{"id":"T38149","span":{"begin":101,"end":103},"obj":"IN"},{"id":"T82839","span":{"begin":104,"end":112},"obj":"JJ"},{"id":"T8210","span":{"begin":113,"end":114},"obj":"DT"},{"id":"T24421","span":{"begin":115,"end":119},"obj":"NN"},{"id":"T35489","span":{"begin":120,"end":121},"obj":"NN"},{"id":"T78652","span":{"begin":122,"end":123},"obj":"-LRB-"},{"id":"T68425","span":{"begin":123,"end":126},"obj":"NN"},{"id":"T70607","span":{"begin":127,"end":129},"obj":"NN"},{"id":"T28784","span":{"begin":130,"end":134},"obj":"NN"},{"id":"T45890","span":{"begin":134,"end":135},"obj":"-RRB-"},{"id":"T7560","span":{"begin":135,"end":141},"obj":"CD"},{"id":"T76185","span":{"begin":142,"end":143},"obj":"NN"},{"id":"T79009","span":{"begin":144,"end":148},"obj":"NNP"},{"id":"T30776","span":{"begin":149,"end":150},"obj":"NNP"},{"id":"T73014","span":{"begin":151,"end":152},"obj":"-LRB-"},{"id":"T68521","span":{"begin":152,"end":155},"obj":"NN"},{"id":"T15706","span":{"begin":156,"end":158},"obj":"NN"},{"id":"T11708","span":{"begin":159,"end":163},"obj":"NN"},{"id":"T3010","span":{"begin":163,"end":164},"obj":"-RRB-"},{"id":"T27583","span":{"begin":164,"end":198},"obj":"JJ"},{"id":"T28741","span":{"begin":199,"end":206},"obj":"NN"},{"id":"T83177","span":{"begin":207,"end":209},"obj":"IN"},{"id":"T70681","span":{"begin":210,"end":218},"obj":"JJ"},{"id":"T92110","span":{"begin":219,"end":226},"obj":"NNS"},{"id":"T35748","span":{"begin":227,"end":229},"obj":"IN"},{"id":"T9158","span":{"begin":230,"end":231},"obj":"DT"},{"id":"T59935","span":{"begin":232,"end":236},"obj":"NN"},{"id":"T12304","span":{"begin":237,"end":240},"obj":"CC"},{"id":"T82313","span":{"begin":241,"end":242},"obj":"NN"},{"id":"T61347","span":{"begin":243,"end":247},"obj":"NNP"},{"id":"T24930","span":{"begin":248,"end":249},"obj":"NNP"},{"id":"T68640","span":{"begin":250,"end":258},"obj":"NNS"},{"id":"T58506","span":{"begin":260,"end":263},"obj":"DT"},{"id":"T30217","span":{"begin":264,"end":273},"obj":"NN"},{"id":"T24446","span":{"begin":274,"end":276},"obj":"IN"},{"id":"T64701","span":{"begin":277,"end":280},"obj":"DT"},{"id":"T32032","span":{"begin":281,"end":295},"obj":"RB"},{"id":"T87865","span":{"begin":296,"end":304},"obj":"VBN"},{"id":"T41472","span":{"begin":305,"end":318},"obj":"NN"},{"id":"T75169","span":{"begin":319,"end":321},"obj":"VBZ"},{"id":"T85671","span":{"begin":322,"end":333},"obj":"VBN"},{"id":"T14723","span":{"begin":334,"end":336},"obj":"IN"},{"id":"T33006","span":{"begin":337,"end":340},"obj":"DT"},{"id":"T74197","span":{"begin":341,"end":350},"obj":"NN"},{"id":"T74594","span":{"begin":351,"end":360},"obj":"NN"},{"id":"T32963","span":{"begin":361,"end":363},"obj":"IN"},{"id":"T41739","span":{"begin":364,"end":372},"obj":"JJ"},{"id":"T10224","span":{"begin":373,"end":377},"obj":"NNS"},{"id":"T21879","span":{"begin":378,"end":379},"obj":"NN"},{"id":"T97449","span":{"begin":380,"end":381},"obj":"-LRB-"},{"id":"T53301","span":{"begin":381,"end":384},"obj":"NN"},{"id":"T9349","span":{"begin":385,"end":387},"obj":"NN"},{"id":"T99864","span":{"begin":388,"end":392},"obj":"NN"},{"id":"T96751","span":{"begin":392,"end":393},"obj":"-RRB-"},{"id":"T41923","span":{"begin":393,"end":395},"obj":"CD"},{"id":"T4404","span":{"begin":396,"end":399},"obj":"CC"},{"id":"T91868","span":{"begin":400,"end":404},"obj":"NNP"},{"id":"T72317","span":{"begin":405,"end":406},"obj":"NNP"},{"id":"T2448","span":{"begin":407,"end":408},"obj":"-LRB-"},{"id":"T71010","span":{"begin":408,"end":411},"obj":"NN"},{"id":"T12743","span":{"begin":412,"end":414},"obj":"NN"},{"id":"T88079","span":{"begin":415,"end":419},"obj":"NN"},{"id":"T86576","span":{"begin":419,"end":420},"obj":"-RRB-"},{"id":"T3017","span":{"begin":420,"end":422},"obj":"CD"},{"id":"T99799","span":{"begin":423,"end":436},"obj":"NNS"},{"id":"T93818","span":{"begin":438,"end":441},"obj":"DT"},{"id":"T88390","span":{"begin":442,"end":449},"obj":"NNS"},{"id":"T27490","span":{"begin":450,"end":453},"obj":"VBP"},{"id":"T93961","span":{"begin":454,"end":461},"obj":"VBN"},{"id":"T72784","span":{"begin":462,"end":471},"obj":"VBG"},{"id":"T77097","span":{"begin":472,"end":474},"obj":"TO"},{"id":"T64192","span":{"begin":475,"end":487},"obj":"NN"},{"id":"T65168","span":{"begin":488,"end":495},"obj":"NN"},{"id":"T6760","span":{"begin":495,"end":496},"obj":"-COMMA-"},{"id":"T9745","span":{"begin":497,"end":499},"obj":"IN"},{"id":"T86418","span":{"begin":500,"end":507},"obj":"VBN"},{"id":"T30404","span":{"begin":508,"end":510},"obj":"IN"},{"id":"T37495","span":{"begin":511,"end":514},"obj":"DT"},{"id":"T79747","span":{"begin":515,"end":518},"obj":"NN"},{"id":"T59664","span":{"begin":520,"end":524},"obj":"NN"},{"id":"T85817","span":{"begin":525,"end":541},"obj":"JJ"},{"id":"T40508","span":{"begin":542,"end":547},"obj":"NNS"},{"id":"T52910","span":{"begin":548,"end":551},"obj":"CC"},{"id":"T7086","span":{"begin":552,"end":556},"obj":"NN"},{"id":"T75407","span":{"begin":557,"end":573},"obj":"JJ"},{"id":"T46887","span":{"begin":574,"end":579},"obj":"NNS"},{"id":"T73267","span":{"begin":580,"end":583},"obj":"IN"},{"id":"T33037","span":{"begin":584,"end":588},"obj":"NNS"},{"id":"T82290","span":{"begin":589,"end":592},"obj":"CC"},{"id":"T38470","span":{"begin":593,"end":597},"obj":"NNS"},{"id":"T11920","span":{"begin":597,"end":598},"obj":"-COMMA-"},{"id":"T13712","span":{"begin":599,"end":611},"obj":"RB"},{"id":"T3547","span":{"begin":611,"end":612},"obj":"-COMMA-"},{"id":"T34630","span":{"begin":613,"end":616},"obj":"VBP"},{"id":"T48779","span":{"begin":617,"end":626},"obj":"VBN"},{"id":"T50978","span":{"begin":627,"end":629},"obj":"IN"},{"id":"T62580","span":{"begin":630,"end":635},"obj":"NN"},{"id":"T99144","span":{"begin":636,"end":640},"obj":"NN"},{"id":"T43036","span":{"begin":642,"end":645},"obj":"DT"},{"id":"T72864","span":{"begin":646,"end":648},"obj":"NN"},{"id":"T60407","span":{"begin":649,"end":652},"obj":"CC"},{"id":"T63087","span":{"begin":653,"end":655},"obj":"NN"},{"id":"T35349","span":{"begin":656,"end":664},"obj":"NNS"},{"id":"T29813","span":{"begin":665,"end":668},"obj":"VBP"},{"id":"T72291","span":{"begin":669,"end":676},"obj":"VBN"},{"id":"T28888","span":{"begin":677,"end":682},"obj":"JJ"},{"id":"T2559","span":{"begin":683,"end":687},"obj":"JJ"},{"id":"T24147","span":{"begin":688,"end":691},"obj":"CC"},{"id":"T73178","span":{"begin":692,"end":696},"obj":"JJ"},{"id":"T95495","span":{"begin":697,"end":701},"obj":"NN"},{"id":"T87030","span":{"begin":701,"end":702},"obj":"-COMMA-"},{"id":"T42416","span":{"begin":703,"end":715},"obj":"RB"}],"relations":[{"id":"R23985","pred":"arg1Of","subj":"T5164","obj":"T33108"},{"id":"R42024","pred":"arg1Of","subj":"T5164","obj":"T85081"},{"id":"R2979","pred":"arg2Of","subj":"T14194","obj":"T85081"},{"id":"R71341","pred":"arg1Of","subj":"T14194","obj":"T78202"},{"id":"R15611","pred":"arg1Of","subj":"T4820","obj":"T60050"},{"id":"R91207","pred":"arg1Of","subj":"T14194","obj":"T4820"},{"id":"R91364","pred":"arg1Of","subj":"T5164","obj":"T67945"},{"id":"R57657","pred":"arg2Of","subj":"T60933","obj":"T67945"},{"id":"R64641","pred":"arg2Of","subj":"T5164","obj":"T60933"},{"id":"R71202","pred":"arg1Of","subj":"T60933","obj":"T74928"},{"id":"R25467","pred":"arg2Of","subj":"T35915","obj":"T74928"},{"id":"R14182","pred":"arg1Of","subj":"T35915","obj":"T84730"},{"id":"R71520","pred":"arg1Of","subj":"T35915","obj":"T26156"},{"id":"R60786","pred":"arg1Of","subj":"T35915","obj":"T38149"},{"id":"R11447","pred":"arg2Of","subj":"T28741","obj":"T38149"},{"id":"R19445","pred":"arg1Of","subj":"T24421","obj":"T82839"},{"id":"R34175","pred":"arg1Of","subj":"T24421","obj":"T8210"},{"id":"R25874","pred":"arg1Of","subj":"T76185","obj":"T24421"},{"id":"R20473","pred":"arg1Of","subj":"T76185","obj":"T35489"},{"id":"R94261","pred":"arg1Of","subj":"T35489","obj":"T78652"},{"id":"R39195","pred":"arg2Of","subj":"T28784","obj":"T78652"},{"id":"R19115","pred":"arg3Of","subj":"T45890","obj":"T78652"},{"id":"R34457","pred":"arg1Of","subj":"T28784","obj":"T68425"},{"id":"R12595","pred":"arg1Of","subj":"T28784","obj":"T70607"},{"id":"R20784","pred":"arg1Of","subj":"T76185","obj":"T7560"},{"id":"R30047","pred":"arg1Of","subj":"T28741","obj":"T76185"},{"id":"R27001","pred":"arg1Of","subj":"T30776","obj":"T79009"},{"id":"R7735","pred":"arg1Of","subj":"T28741","obj":"T30776"},{"id":"R64829","pred":"arg1Of","subj":"T30776","obj":"T73014"},{"id":"R80551","pred":"arg2Of","subj":"T11708","obj":"T73014"},{"id":"R94295","pred":"arg3Of","subj":"T3010","obj":"T73014"},{"id":"R24335","pred":"arg1Of","subj":"T11708","obj":"T68521"},{"id":"R78811","pred":"arg1Of","subj":"T11708","obj":"T15706"},{"id":"R15238","pred":"arg1Of","subj":"T28741","obj":"T27583"},{"id":"R13295","pred":"arg1Of","subj":"T28741","obj":"T83177"},{"id":"R50333","pred":"arg2Of","subj":"T12304","obj":"T83177"},{"id":"R59811","pred":"arg1Of","subj":"T92110","obj":"T70681"},{"id":"R18918","pred":"arg1Of","subj":"T92110","obj":"T35748"},{"id":"R55957","pred":"arg2Of","subj":"T59935","obj":"T35748"},{"id":"R59063","pred":"arg1Of","subj":"T59935","obj":"T9158"},{"id":"R39844","pred":"arg1Of","subj":"T92110","obj":"T12304"},{"id":"R44359","pred":"arg2Of","subj":"T68640","obj":"T12304"},{"id":"R1966","pred":"arg1Of","subj":"T68640","obj":"T82313"},{"id":"R38468","pred":"arg1Of","subj":"T24930","obj":"T61347"},{"id":"R85546","pred":"arg1Of","subj":"T68640","obj":"T24930"},{"id":"R40464","pred":"arg1Of","subj":"T30217","obj":"T58506"},{"id":"R8332","pred":"arg1Of","subj":"T30217","obj":"T24446"},{"id":"R34633","pred":"arg2Of","subj":"T41472","obj":"T24446"},{"id":"R65984","pred":"arg1Of","subj":"T41472","obj":"T64701"},{"id":"R15545","pred":"arg1Of","subj":"T87865","obj":"T32032"},{"id":"R55106","pred":"arg1Of","subj":"T41472","obj":"T87865"},{"id":"R43509","pred":"arg1Of","subj":"T30217","obj":"T75169"},{"id":"R61258","pred":"arg2Of","subj":"T85671","obj":"T75169"},{"id":"R50646","pred":"arg2Of","subj":"T30217","obj":"T85671"},{"id":"R71664","pred":"arg1Of","subj":"T85671","obj":"T14723"},{"id":"R49912","pred":"arg2Of","subj":"T74594","obj":"T14723"},{"id":"R42808","pred":"arg1Of","subj":"T74594","obj":"T33006"},{"id":"R97100","pred":"arg1Of","subj":"T74594","obj":"T74197"},{"id":"R17970","pred":"arg1Of","subj":"T74594","obj":"T32963"},{"id":"R69282","pred":"arg2Of","subj":"T4404","obj":"T32963"},{"id":"R76425","pred":"arg1Of","subj":"T10224","obj":"T41739"},{"id":"R29816","pred":"arg1Of","subj":"T4404","obj":"T10224"},{"id":"R25583","pred":"arg1Of","subj":"T41923","obj":"T21879"},{"id":"R46556","pred":"arg1Of","subj":"T21879","obj":"T97449"},{"id":"R93979","pred":"arg2Of","subj":"T99864","obj":"T97449"},{"id":"R9284","pred":"arg3Of","subj":"T96751","obj":"T97449"},{"id":"R65072","pred":"arg1Of","subj":"T99864","obj":"T53301"},{"id":"R87543","pred":"arg1Of","subj":"T99864","obj":"T9349"},{"id":"R90800","pred":"arg1Of","subj":"T41923","obj":"T4404"},{"id":"R85455","pred":"arg2Of","subj":"T99799","obj":"T4404"},{"id":"R63130","pred":"arg1Of","subj":"T72317","obj":"T91868"},{"id":"R52854","pred":"arg1Of","subj":"T99799","obj":"T72317"},{"id":"R70729","pred":"arg1Of","subj":"T72317","obj":"T2448"},{"id":"R17073","pred":"arg2Of","subj":"T88079","obj":"T2448"},{"id":"R90881","pred":"arg3Of","subj":"T86576","obj":"T2448"},{"id":"R91530","pred":"arg1Of","subj":"T88079","obj":"T71010"},{"id":"R18293","pred":"arg1Of","subj":"T88079","obj":"T12743"},{"id":"R83861","pred":"arg1Of","subj":"T99799","obj":"T3017"},{"id":"R66917","pred":"arg1Of","subj":"T88390","obj":"T93818"},{"id":"R61214","pred":"arg1Of","subj":"T88390","obj":"T27490"},{"id":"R20308","pred":"arg2Of","subj":"T93961","obj":"T27490"},{"id":"R75632","pred":"arg2Of","subj":"T88390","obj":"T93961"},{"id":"R23537","pred":"arg1Of","subj":"T93961","obj":"T72784"},{"id":"R38629","pred":"arg2Of","subj":"T77097","obj":"T72784"},{"id":"R36773","pred":"arg2Of","subj":"T65168","obj":"T77097"},{"id":"R91605","pred":"arg1Of","subj":"T65168","obj":"T64192"},{"id":"R29363","pred":"arg1Of","subj":"T93961","obj":"T6760"},{"id":"R55821","pred":"arg1Of","subj":"T93961","obj":"T9745"},{"id":"R18556","pred":"arg2Of","subj":"T86418","obj":"T9745"},{"id":"R84962","pred":"arg1Of","subj":"T79747","obj":"T86418"},{"id":"R75695","pred":"arg2Of","subj":"T79747","obj":"T30404"},{"id":"R74158","pred":"arg1Of","subj":"T79747","obj":"T37495"},{"id":"R92325","pred":"arg1Of","subj":"T40508","obj":"T59664"},{"id":"R39154","pred":"arg1Of","subj":"T40508","obj":"T85817"},{"id":"R98876","pred":"arg1Of","subj":"T40508","obj":"T52910"},{"id":"R33747","pred":"arg2Of","subj":"T46887","obj":"T52910"},{"id":"R93852","pred":"arg1Of","subj":"T46887","obj":"T7086"},{"id":"R40335","pred":"arg1Of","subj":"T46887","obj":"T75407"},{"id":"R47551","pred":"arg1Of","subj":"T52910","obj":"T73267"},{"id":"R71577","pred":"arg2Of","subj":"T82290","obj":"T73267"},{"id":"R41263","pred":"arg1Of","subj":"T33037","obj":"T82290"},{"id":"R35928","pred":"arg2Of","subj":"T38470","obj":"T82290"},{"id":"R91411","pred":"arg1Of","subj":"T48779","obj":"T11920"},{"id":"R38554","pred":"arg1Of","subj":"T48779","obj":"T13712"},{"id":"R33721","pred":"arg1Of","subj":"T48779","obj":"T3547"},{"id":"R64648","pred":"arg1Of","subj":"T52910","obj":"T34630"},{"id":"R36430","pred":"arg2Of","subj":"T48779","obj":"T34630"},{"id":"R70838","pred":"arg2Of","subj":"T52910","obj":"T48779"},{"id":"R48801","pred":"arg1Of","subj":"T48779","obj":"T50978"},{"id":"R99054","pred":"arg2Of","subj":"T99144","obj":"T50978"},{"id":"R9602","pred":"arg1Of","subj":"T99144","obj":"T62580"},{"id":"R40578","pred":"arg1Of","subj":"T35349","obj":"T43036"},{"id":"R13402","pred":"arg1Of","subj":"T35349","obj":"T72864"},{"id":"R82455","pred":"arg1Of","subj":"T72864","obj":"T60407"},{"id":"R25568","pred":"arg2Of","subj":"T63087","obj":"T60407"},{"id":"R41821","pred":"arg1Of","subj":"T35349","obj":"T63087"},{"id":"R87779","pred":"arg1Of","subj":"T35349","obj":"T29813"},{"id":"R25857","pred":"arg2Of","subj":"T72291","obj":"T29813"},{"id":"R18448","pred":"arg2Of","subj":"T35349","obj":"T72291"},{"id":"R98204","pred":"arg3Of","subj":"T95495","obj":"T72291"},{"id":"R35270","pred":"arg1Of","subj":"T95495","obj":"T28888"},{"id":"R10534","pred":"arg1Of","subj":"T95495","obj":"T2559"},{"id":"R4632","pred":"arg1Of","subj":"T2559","obj":"T24147"},{"id":"R22049","pred":"arg2Of","subj":"T73178","obj":"T24147"},{"id":"R15613","pred":"arg1Of","subj":"T95495","obj":"T73178"},{"id":"R18285","pred":"arg1Of","subj":"T72291","obj":"T87030"},{"id":"R49825","pred":"arg1Of","subj":"T72291","obj":"T42416"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T70","span":{"begin":167,"end":180},"obj":"Body_part"},{"id":"T71","span":{"begin":250,"end":258},"obj":"Body_part"},{"id":"T72","span":{"begin":423,"end":436},"obj":"Body_part"}],"attributes":[{"id":"A70","pred":"fma_id","subj":"T70","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A71","pred":"fma_id","subj":"T71","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A72","pred":"fma_id","subj":"T72","obj":"http://purl.org/sig/ont/fma/fma62925"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T102","span":{"begin":167,"end":180},"obj":"Chemical"},{"id":"T103","span":{"begin":219,"end":226},"obj":"Chemical"},{"id":"T104","span":{"begin":250,"end":258},"obj":"Chemical"},{"id":"T105","span":{"begin":423,"end":436},"obj":"Chemical"},{"id":"T106","span":{"begin":442,"end":449},"obj":"Chemical"}],"attributes":[{"id":"A102","pred":"chebi_id","subj":"T102","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A103","pred":"chebi_id","subj":"T103","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A104","pred":"chebi_id","subj":"T104","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A105","pred":"chebi_id","subj":"T105","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A106","pred":"chebi_id","subj":"T106","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T76","span":{"begin":115,"end":119},"obj":"Species"},{"id":"T77","span":{"begin":144,"end":148},"obj":"Species"},{"id":"T78","span":{"begin":232,"end":236},"obj":"Species"},{"id":"T79","span":{"begin":243,"end":247},"obj":"Species"},{"id":"T80","span":{"begin":373,"end":377},"obj":"Species"},{"id":"T81","span":{"begin":400,"end":404},"obj":"Species"},{"id":"T82","span":{"begin":584,"end":588},"obj":"Species"},{"id":"T83","span":{"begin":593,"end":597},"obj":"Species"}],"attributes":[{"id":"A82","pred":"ncbi_taxonomy_id","subj":"T82","obj":"NCBItxid:1335626"},{"id":"A81","pred":"ncbi_taxonomy_id","subj":"T81","obj":"NCBItxid:694009"},{"id":"A76","pred":"ncbi_taxonomy_id","subj":"T76","obj":"NCBItxid:1335626"},{"id":"A77","pred":"ncbi_taxonomy_id","subj":"T77","obj":"NCBItxid:694009"},{"id":"A79","pred":"ncbi_taxonomy_id","subj":"T79","obj":"NCBItxid:694009"},{"id":"A80","pred":"ncbi_taxonomy_id","subj":"T80","obj":"NCBItxid:1335626"},{"id":"A78","pred":"ncbi_taxonomy_id","subj":"T78","obj":"NCBItxid:1335626"},{"id":"A83","pred":"ncbi_taxonomy_id","subj":"T83","obj":"NCBItxid:694009"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T70","span":{"begin":0,"end":259},"obj":"Sentence"},{"id":"T71","span":{"begin":260,"end":437},"obj":"Sentence"},{"id":"T72","span":{"begin":438,"end":519},"obj":"Sentence"},{"id":"T73","span":{"begin":520,"end":641},"obj":"Sentence"},{"id":"T74","span":{"begin":642,"end":716},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T37","span":{"begin":144,"end":148},"obj":"Disease"},{"id":"T38","span":{"begin":243,"end":247},"obj":"Disease"},{"id":"T39","span":{"begin":400,"end":404},"obj":"Disease"},{"id":"T40","span":{"begin":593,"end":597},"obj":"Disease"}],"attributes":[{"id":"A37","pred":"mondo_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A38","pred":"mondo_id","subj":"T38","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A39","pred":"mondo_id","subj":"T39","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A40","pred":"mondo_id","subj":"T40","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"384","span":{"begin":115,"end":119},"obj":"Disease"},{"id":"385","span":{"begin":144,"end":148},"obj":"Disease"},{"id":"381","span":{"begin":210,"end":226},"obj":"Chemical"},{"id":"386","span":{"begin":232,"end":236},"obj":"Disease"},{"id":"387","span":{"begin":243,"end":247},"obj":"Disease"},{"id":"388","span":{"begin":373,"end":377},"obj":"Disease"},{"id":"389","span":{"begin":400,"end":404},"obj":"Disease"},{"id":"382","span":{"begin":442,"end":449},"obj":"Chemical"},{"id":"383","span":{"begin":475,"end":487},"obj":"Chemical"},{"id":"379","span":{"begin":520,"end":524},"obj":"Gene"},{"id":"380","span":{"begin":552,"end":556},"obj":"Gene"},{"id":"390","span":{"begin":584,"end":588},"obj":"Disease"},{"id":"391","span":{"begin":593,"end":597},"obj":"Disease"}],"attributes":[{"id":"A386","pred":"pubann:denotes","subj":"386","obj":"MESH:D018352"},{"id":"A380","pred":"pubann:denotes","subj":"380","obj":"Gene:59272"},{"id":"A391","pred":"pubann:denotes","subj":"391","obj":"MESH:D045169"},{"id":"A379","pred":"pubann:denotes","subj":"379","obj":"Gene:1803"},{"id":"A385","pred":"pubann:denotes","subj":"385","obj":"MESH:D045169"},{"id":"A384","pred":"pubann:denotes","subj":"384","obj":"MESH:D018352"},{"id":"A389","pred":"pubann:denotes","subj":"389","obj":"MESH:D045169"},{"id":"A382","pred":"pubann:denotes","subj":"382","obj":"MESH:D011134"},{"id":"A388","pred":"pubann:denotes","subj":"388","obj":"MESH:D018352"},{"id":"A387","pred":"pubann:denotes","subj":"387","obj":"MESH:D045169"},{"id":"A390","pred":"pubann:denotes","subj":"390","obj":"MESH:D018352"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T3398","span":{"begin":167,"end":180},"obj":"Protein"},{"id":"T3483","span":{"begin":248,"end":258},"obj":"Protein"},{"id":"T3516","span":{"begin":423,"end":436},"obj":"Protein"},{"id":"T3601","span":{"begin":520,"end":524},"obj":"Protein"},{"id":"T3602","span":{"begin":552,"end":556},"obj":"Protein"}],"attributes":[{"id":"A3398","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q9QSP1"},{"id":"A3399","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q9QJT6"},{"id":"A3400","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q9JGT4"},{"id":"A3401","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q9IPJ6"},{"id":"A3402","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q9DIC6"},{"id":"A3403","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q91DS0"},{"id":"A3404","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q91C28"},{"id":"A3405","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q8QQA2"},{"id":"A3406","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q8QPE5"},{"id":"A3407","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q8QPE4"},{"id":"A3408","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q8QPE3"},{"id":"A3409","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q8JTH0"},{"id":"A3410","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q8BDV6"},{"id":"A3411","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q8B6J6"},{"id":"A3412","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q8B0I1"},{"id":"A3413","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q8B0H6"},{"id":"A3414","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q8B0H1"},{"id":"A3415","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q89669"},{"id":"A3416","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q85213"},{"id":"A3417","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q82706"},{"id":"A3418","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q82683"},{"id":"A3419","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q82020"},{"id":"A3420","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q787B5"},{"id":"A3421","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q77SK0"},{"id":"A3422","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q77N36"},{"id":"A3423","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q76G52"},{"id":"A3424","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q75T09"},{"id":"A3425","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q6X1D5"},{"id":"A3426","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q6X1D1"},{"id":"A3427","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q6TYA0"},{"id":"A3428","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q6E0W7"},{"id":"A3429","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q66T62"},{"id":"A3430","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q5VKP3"},{"id":"A3431","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q5VKN9"},{"id":"A3432","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q5K2K4"},{"id":"A3433","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q5IX93"},{"id":"A3434","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q5IX92"},{"id":"A3435","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q5IX91"},{"id":"A3436","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q5IX90"},{"id":"A3437","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q5IX89"},{"id":"A3438","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q5IX88"},{"id":"A3439","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q5IX87"},{"id":"A3440","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q5GA86"},{"id":"A3441","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q58FH1"},{"id":"A3442","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q4VKV3"},{"id":"A3443","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q4F900"},{"id":"A3444","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q49LL3"},{"id":"A3445","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q49IU2"},{"id":"A3446","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q49IU1"},{"id":"A3447","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q49IT9"},{"id":"A3448","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q49IT8"},{"id":"A3449","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q49AV0"},{"id":"A3450","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q0GBY1"},{"id":"A3451","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q0GBX6"},{"id":"A3452","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/Q08089"},{"id":"A3453","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P32595"},{"id":"A3454","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P32550"},{"id":"A3455","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P19462"},{"id":"A3456","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P16288"},{"id":"A3457","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P15199"},{"id":"A3458","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P13180"},{"id":"A3459","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P0C572"},{"id":"A3460","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P08667"},{"id":"A3461","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P08163"},{"id":"A3462","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P07923"},{"id":"A3463","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P04884"},{"id":"A3464","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P04883"},{"id":"A3465","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P04882"},{"id":"A3466","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P03524"},{"id":"A3467","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/P03522"},{"id":"A3468","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/O92284"},{"id":"A3469","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/O56677"},{"id":"A3470","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/O10236"},{"id":"A3471","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/J7HBH4"},{"id":"A3472","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/D8V075"},{"id":"A3473","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/A7WNB3"},{"id":"A3474","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/A4UHQ6"},{"id":"A3475","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/A4UHQ1"},{"id":"A3476","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/A3RM22"},{"id":"A3477","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/A3F5R8"},{"id":"A3478","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/A3F5R3"},{"id":"A3479","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/A3F5Q8"},{"id":"A3480","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/A3F5N3"},{"id":"A3481","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/A3F5M3"},{"id":"A3482","pred":"uniprot_id","subj":"T3398","obj":"https://www.uniprot.org/uniprot/A3F5L8"},{"id":"A3483","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9UIP0"},{"id":"A3484","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9UIN9"},{"id":"A3485","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9UIN8"},{"id":"A3486","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9UIN7"},{"id":"A3487","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9UIN6"},{"id":"A3488","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9UBH8"},{"id":"A3489","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9NRH8"},{"id":"A3490","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9NRH7"},{"id":"A3491","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9NRH6"},{"id":"A3492","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9NRH5"},{"id":"A3493","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9NRH4"},{"id":"A3494","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9NPG5"},{"id":"A3495","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9NPE0"},{"id":"A3496","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q9NP52"},{"id":"A3497","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q95IF9"},{"id":"A3498","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q8N5P3"},{"id":"A3499","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q8IZU6"},{"id":"A3500","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q8IZU5"},{"id":"A3501","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q8IZU4"},{"id":"A3502","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q86Z04"},{"id":"A3503","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q7YR44"},{"id":"A3504","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q7LA71"},{"id":"A3505","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q7LA70"},{"id":"A3506","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q5STD2"},{"id":"A3507","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q5SQ85"},{"id":"A3508","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q1XI16"},{"id":"A3509","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q1XI12"},{"id":"A3510","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/Q15517"},{"id":"A3511","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/O43509"},{"id":"A3512","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/O19084"},{"id":"A3513","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/B0UYZ7"},{"id":"A3514","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/B0S7V2"},{"id":"A3515","pred":"uniprot_id","subj":"T3483","obj":"https://www.uniprot.org/uniprot/A5A6L9"},{"id":"A3516","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q9QSP1"},{"id":"A3517","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q9QJT6"},{"id":"A3518","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q9JGT4"},{"id":"A3519","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q9IPJ6"},{"id":"A3520","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q9DIC6"},{"id":"A3521","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q91DS0"},{"id":"A3522","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q91C28"},{"id":"A3523","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q8QQA2"},{"id":"A3524","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q8QPE5"},{"id":"A3525","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q8QPE4"},{"id":"A3526","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q8QPE3"},{"id":"A3527","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q8JTH0"},{"id":"A3528","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q8BDV6"},{"id":"A3529","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q8B6J6"},{"id":"A3530","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q8B0I1"},{"id":"A3531","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q8B0H6"},{"id":"A3532","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q8B0H1"},{"id":"A3533","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q89669"},{"id":"A3534","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q85213"},{"id":"A3535","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q82706"},{"id":"A3536","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q82683"},{"id":"A3537","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q82020"},{"id":"A3538","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q787B5"},{"id":"A3539","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q77SK0"},{"id":"A3540","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q77N36"},{"id":"A3541","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q76G52"},{"id":"A3542","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q75T09"},{"id":"A3543","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q6X1D5"},{"id":"A3544","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q6X1D1"},{"id":"A3545","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q6TYA0"},{"id":"A3546","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q6E0W7"},{"id":"A3547","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q66T62"},{"id":"A3548","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q5VKP3"},{"id":"A3549","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q5VKN9"},{"id":"A3550","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q5K2K4"},{"id":"A3551","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q5IX93"},{"id":"A3552","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q5IX92"},{"id":"A3553","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q5IX91"},{"id":"A3554","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q5IX90"},{"id":"A3555","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q5IX89"},{"id":"A3556","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q5IX88"},{"id":"A3557","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q5IX87"},{"id":"A3558","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q5GA86"},{"id":"A3559","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q58FH1"},{"id":"A3560","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q4VKV3"},{"id":"A3561","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q4F900"},{"id":"A3562","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q49LL3"},{"id":"A3563","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q49IU2"},{"id":"A3564","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q49IU1"},{"id":"A3565","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q49IT9"},{"id":"A3566","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q49IT8"},{"id":"A3567","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q49AV0"},{"id":"A3568","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q0GBY1"},{"id":"A3569","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q0GBX6"},{"id":"A3570","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/Q08089"},{"id":"A3571","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P32595"},{"id":"A3572","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P32550"},{"id":"A3573","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P19462"},{"id":"A3574","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P16288"},{"id":"A3575","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P15199"},{"id":"A3576","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P13180"},{"id":"A3577","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P0C572"},{"id":"A3578","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P08667"},{"id":"A3579","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P08163"},{"id":"A3580","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P07923"},{"id":"A3581","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P04884"},{"id":"A3582","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P04883"},{"id":"A3583","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P04882"},{"id":"A3584","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P03524"},{"id":"A3585","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/P03522"},{"id":"A3586","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/O92284"},{"id":"A3587","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/O56677"},{"id":"A3588","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/O10236"},{"id":"A3589","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/J7HBH4"},{"id":"A3590","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/D8V075"},{"id":"A3591","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/A7WNB3"},{"id":"A3592","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/A4UHQ6"},{"id":"A3593","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/A4UHQ1"},{"id":"A3594","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/A3RM22"},{"id":"A3595","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/A3F5R8"},{"id":"A3596","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/A3F5R3"},{"id":"A3597","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/A3F5Q8"},{"id":"A3598","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/A3F5N3"},{"id":"A3599","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/A3F5M3"},{"id":"A3600","pred":"uniprot_id","subj":"T3516","obj":"https://www.uniprot.org/uniprot/A3F5L8"},{"id":"A3601","pred":"uniprot_id","subj":"T3601","obj":"https://www.uniprot.org/uniprot/Q9N2I7"},{"id":"A3602","pred":"uniprot_id","subj":"T3602","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T31","span":{"begin":45,"end":58},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T32","span":{"begin":305,"end":318},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T28","span":{"begin":45,"end":58},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T29","span":{"begin":305,"end":318},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T32","span":{"begin":45,"end":58},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T33","span":{"begin":305,"end":318},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}

{"project":"LitCovid-sentences","denotations":[{"id":"T70","span":{"begin":0,"end":259},"obj":"Sentence"},{"id":"T71","span":{"begin":260,"end":437},"obj":"Sentence"},{"id":"T72","span":{"begin":438,"end":519},"obj":"Sentence"},{"id":"T73","span":{"begin":520,"end":641},"obj":"Sentence"},{"id":"T74","span":{"begin":642,"end":716},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric a MERS S (PDB ID 5X59)11 and b SARS S (PDB ID 5X58)11 glycoproteins. Structural-based mapping of N-linked glycans on a MERS and b SARS S proteins. The modelling of the experimentally observed glycosylation is illustrated on the prefusion structure of trimeric MERS S (PDB ID 5X59)11 and SARS S (PDB ID 5X58)11 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor-binding sites and ACE2 receptor-binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively."}