PMC:7253482 / 11630-12426 JSONTXT

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    LitCovid-PubTator

    {"project":"LitCovid-PubTator","denotations":[{"id":"363","span":{"begin":34,"end":50},"obj":"Chemical"},{"id":"364","span":{"begin":54,"end":58},"obj":"Disease"},{"id":"365","span":{"begin":63,"end":67},"obj":"Disease"},{"id":"379","span":{"begin":600,"end":604},"obj":"Gene"},{"id":"380","span":{"begin":632,"end":636},"obj":"Gene"},{"id":"381","span":{"begin":290,"end":306},"obj":"Chemical"},{"id":"382","span":{"begin":522,"end":529},"obj":"Chemical"},{"id":"383","span":{"begin":555,"end":567},"obj":"Chemical"},{"id":"384","span":{"begin":195,"end":199},"obj":"Disease"},{"id":"385","span":{"begin":224,"end":228},"obj":"Disease"},{"id":"386","span":{"begin":312,"end":316},"obj":"Disease"},{"id":"387","span":{"begin":323,"end":327},"obj":"Disease"},{"id":"388","span":{"begin":453,"end":457},"obj":"Disease"},{"id":"389","span":{"begin":480,"end":484},"obj":"Disease"},{"id":"390","span":{"begin":664,"end":668},"obj":"Disease"},{"id":"391","span":{"begin":673,"end":677},"obj":"Disease"}],"attributes":[{"id":"A364","pred":"tao:has_database_id","subj":"364","obj":"MESH:D018352"},{"id":"A365","pred":"tao:has_database_id","subj":"365","obj":"MESH:D045169"},{"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":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-PD-FMA-UBERON

    {"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T70","span":{"begin":70,"end":78},"obj":"Body_part"},{"id":"T71","span":{"begin":247,"end":260},"obj":"Body_part"},{"id":"T72","span":{"begin":330,"end":338},"obj":"Body_part"},{"id":"T73","span":{"begin":503,"end":516},"obj":"Body_part"}],"attributes":[{"id":"A70","pred":"fma_id","subj":"T70","obj":"http://purl.org/sig/ont/fma/fma67257"},{"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":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-PD-MONDO

    {"project":"LitCovid-PD-MONDO","denotations":[{"id":"T41","span":{"begin":63,"end":67},"obj":"Disease"},{"id":"T42","span":{"begin":224,"end":228},"obj":"Disease"},{"id":"T43","span":{"begin":323,"end":327},"obj":"Disease"},{"id":"T44","span":{"begin":480,"end":484},"obj":"Disease"},{"id":"T45","span":{"begin":673,"end":677},"obj":"Disease"}],"attributes":[{"id":"A41","pred":"mondo_id","subj":"T41","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"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":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-PD-CLO

    {"project":"LitCovid-PD-CLO","denotations":[{"id":"T67","span":{"begin":193,"end":194},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T68","span":{"begin":215,"end":217},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T69","span":{"begin":222,"end":223},"obj":"http://purl.obolibrary.org/obo/CLO_0001021"},{"id":"T70","span":{"begin":244,"end":246},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T71","span":{"begin":310,"end":311},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T72","span":{"begin":321,"end":322},"obj":"http://purl.obolibrary.org/obo/CLO_0001021"},{"id":"T73","span":{"begin":473,"end":475},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T74","span":{"begin":500,"end":502},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T75","span":{"begin":726,"end":728},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T76","span":{"begin":733,"end":735},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T77","span":{"begin":733,"end":735},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"}],"text":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-PD-CHEBI

    {"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T129","span":{"begin":43,"end":50},"obj":"Chemical"},{"id":"T130","span":{"begin":70,"end":78},"obj":"Chemical"},{"id":"T131","span":{"begin":207,"end":209},"obj":"Chemical"},{"id":"T132","span":{"begin":236,"end":238},"obj":"Chemical"},{"id":"T133","span":{"begin":247,"end":260},"obj":"Chemical"},{"id":"T134","span":{"begin":299,"end":306},"obj":"Chemical"},{"id":"T135","span":{"begin":330,"end":338},"obj":"Chemical"},{"id":"T136","span":{"begin":465,"end":467},"obj":"Chemical"},{"id":"T137","span":{"begin":492,"end":494},"obj":"Chemical"},{"id":"T138","span":{"begin":503,"end":516},"obj":"Chemical"},{"id":"T139","span":{"begin":522,"end":529},"obj":"Chemical"},{"id":"T140","span":{"begin":733,"end":735},"obj":"Chemical"}],"attributes":[{"id":"A129","pred":"chebi_id","subj":"T129","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A130","pred":"chebi_id","subj":"T130","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"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":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-sample-PD-IDO

    {"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T31","span":{"begin":622,"end":627},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T32","span":{"begin":654,"end":659},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"}],"text":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-sample-Enju

    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3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-sample-PD-FMA

    {"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T69","span":{"begin":70,"end":78},"obj":"Body_part"},{"id":"T70","span":{"begin":247,"end":260},"obj":"Body_part"},{"id":"T71","span":{"begin":330,"end":338},"obj":"Body_part"},{"id":"T72","span":{"begin":503,"end":516},"obj":"Body_part"}],"attributes":[{"id":"A72","pred":"fma_id","subj":"T72","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A70","pred":"fma_id","subj":"T70","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A69","pred":"fma_id","subj":"T69","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A71","pred":"fma_id","subj":"T71","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-sample-CHEBI

    {"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T100","span":{"begin":43,"end":50},"obj":"Chemical"},{"id":"T101","span":{"begin":70,"end":78},"obj":"Chemical"},{"id":"T102","span":{"begin":247,"end":260},"obj":"Chemical"},{"id":"T103","span":{"begin":299,"end":306},"obj":"Chemical"},{"id":"T104","span":{"begin":330,"end":338},"obj":"Chemical"},{"id":"T105","span":{"begin":503,"end":516},"obj":"Chemical"},{"id":"T106","span":{"begin":522,"end":529},"obj":"Chemical"}],"attributes":[{"id":"A106","pred":"chebi_id","subj":"T106","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A101","pred":"chebi_id","subj":"T101","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A104","pred":"chebi_id","subj":"T104","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A103","pred":"chebi_id","subj":"T103","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A105","pred":"chebi_id","subj":"T105","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A100","pred":"chebi_id","subj":"T100","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A102","pred":"chebi_id","subj":"T102","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"}],"text":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-sample-PD-NCBITaxon

    {"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T74","span":{"begin":54,"end":58},"obj":"Species"},{"id":"T75","span":{"begin":63,"end":67},"obj":"Species"},{"id":"T76","span":{"begin":195,"end":199},"obj":"Species"},{"id":"T77","span":{"begin":224,"end":228},"obj":"Species"},{"id":"T78","span":{"begin":312,"end":316},"obj":"Species"},{"id":"T79","span":{"begin":323,"end":327},"obj":"Species"},{"id":"T80","span":{"begin":453,"end":457},"obj":"Species"},{"id":"T81","span":{"begin":480,"end":484},"obj":"Species"},{"id":"T82","span":{"begin":664,"end":668},"obj":"Species"},{"id":"T83","span":{"begin":673,"end":677},"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":"A74","pred":"ncbi_taxonomy_id","subj":"T74","obj":"NCBItxid:1335626"},{"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":"A75","pred":"ncbi_taxonomy_id","subj":"T75","obj":"NCBItxid:694009"},{"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":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-sample-sentences

    {"project":"LitCovid-sample-sentences","denotations":[{"id":"T69","span":{"begin":0,"end":79},"obj":"Sentence"},{"id":"T70","span":{"begin":80,"end":339},"obj":"Sentence"},{"id":"T71","span":{"begin":340,"end":517},"obj":"Sentence"},{"id":"T72","span":{"begin":518,"end":599},"obj":"Sentence"},{"id":"T73","span":{"begin":600,"end":721},"obj":"Sentence"},{"id":"T74","span":{"begin":722,"end":796},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-sample-PD-MONDO

    {"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T36","span":{"begin":63,"end":67},"obj":"Disease"},{"id":"T37","span":{"begin":224,"end":228},"obj":"Disease"},{"id":"T38","span":{"begin":323,"end":327},"obj":"Disease"},{"id":"T39","span":{"begin":480,"end":484},"obj":"Disease"},{"id":"T40","span":{"begin":673,"end":677},"obj":"Disease"}],"attributes":[{"id":"A40","pred":"mondo_id","subj":"T40","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A38","pred":"mondo_id","subj":"T38","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A37","pred":"mondo_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A36","pred":"mondo_id","subj":"T36","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A39","pred":"mondo_id","subj":"T39","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-sample-Pubtator

    {"project":"LitCovid-sample-Pubtator","denotations":[{"id":"363","span":{"begin":34,"end":50},"obj":"Chemical"},{"id":"364","span":{"begin":54,"end":58},"obj":"Disease"},{"id":"365","span":{"begin":63,"end":67},"obj":"Disease"},{"id":"384","span":{"begin":195,"end":199},"obj":"Disease"},{"id":"385","span":{"begin":224,"end":228},"obj":"Disease"},{"id":"381","span":{"begin":290,"end":306},"obj":"Chemical"},{"id":"386","span":{"begin":312,"end":316},"obj":"Disease"},{"id":"387","span":{"begin":323,"end":327},"obj":"Disease"},{"id":"388","span":{"begin":453,"end":457},"obj":"Disease"},{"id":"389","span":{"begin":480,"end":484},"obj":"Disease"},{"id":"382","span":{"begin":522,"end":529},"obj":"Chemical"},{"id":"383","span":{"begin":555,"end":567},"obj":"Chemical"},{"id":"379","span":{"begin":600,"end":604},"obj":"Gene"},{"id":"380","span":{"begin":632,"end":636},"obj":"Gene"},{"id":"390","span":{"begin":664,"end":668},"obj":"Disease"},{"id":"391","span":{"begin":673,"end":677},"obj":"Disease"}],"attributes":[{"id":"A386","pred":"pubann:denotes","subj":"386","obj":"MESH:D018352"},{"id":"A364","pred":"pubann:denotes","subj":"364","obj":"MESH:D018352"},{"id":"A380","pred":"pubann:denotes","subj":"380","obj":"Gene:59272"},{"id":"A391","pred":"pubann:denotes","subj":"391","obj":"MESH:D045169"},{"id":"A365","pred":"pubann:denotes","subj":"365","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":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-sample-UniProt

    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3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-sample-PD-GO-BP-0

    {"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T31","span":{"begin":125,"end":138},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T32","span":{"begin":385,"end":398},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-sample-GO-BP

    {"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T28","span":{"begin":125,"end":138},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T29","span":{"begin":385,"end":398},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-PD-GO-BP

    {"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T32","span":{"begin":125,"end":138},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T33","span":{"begin":385,"end":398},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}

    LitCovid-sentences

    {"project":"LitCovid-sentences","denotations":[{"id":"T69","span":{"begin":0,"end":79},"obj":"Sentence"},{"id":"T70","span":{"begin":80,"end":339},"obj":"Sentence"},{"id":"T71","span":{"begin":340,"end":517},"obj":"Sentence"},{"id":"T72","span":{"begin":518,"end":599},"obj":"Sentence"},{"id":"T73","span":{"begin":600,"end":721},"obj":"Sentence"},{"id":"T74","span":{"begin":722,"end":796},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Fig. 3 Structure-based mapping of N-linked glycans on MERS and SARS S proteins.\nThe 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."}