PMC:7243778 / 23153-23960 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"573","span":{"begin":97,"end":101},"obj":"Gene"},{"id":"574","span":{"begin":453,"end":457},"obj":"Gene"},{"id":"575","span":{"begin":67,"end":68},"obj":"Gene"},{"id":"576","span":{"begin":0,"end":1},"obj":"Gene"},{"id":"577","span":{"begin":13,"end":23},"obj":"Species"},{"id":"578","span":{"begin":139,"end":147},"obj":"Species"},{"id":"579","span":{"begin":373,"end":383},"obj":"Species"},{"id":"580","span":{"begin":362,"end":371},"obj":"Disease"},{"id":"581","span":{"begin":786,"end":801},"obj":"Disease"}],"attributes":[{"id":"A573","pred":"tao:has_database_id","subj":"573","obj":"Gene:59272"},{"id":"A574","pred":"tao:has_database_id","subj":"574","obj":"Gene:59272"},{"id":"A575","pred":"tao:has_database_id","subj":"575","obj":"Gene:43740575"},{"id":"A576","pred":"tao:has_database_id","subj":"576","obj":"Gene:43740568"},{"id":"A577","pred":"tao:has_database_id","subj":"577","obj":"Tax:2697049"},{"id":"A578","pred":"tao:has_database_id","subj":"578","obj":"Tax:694009"},{"id":"A579","pred":"tao:has_database_id","subj":"579","obj":"Tax:2697049"},{"id":"A580","pred":"tao:has_database_id","subj":"580","obj":"MESH:D007239"},{"id":"A581","pred":"tao:has_database_id","subj":"581","obj":"MESH:D001102"}],"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":"S protein of SARS-CoV-2 composed of 1273 amino acids [76] uses its N-terminal S1 subunit to bind ACE2 receptor with a better affinity than SARS-CoV S glycoprotein for entry [78]. Effectively, S1 subunit divides into an N-terminal domain (NTD) and a receptor-binding domain (RBD). The latter is necessary for viral binding and a potential target for nAbs. During infection, SARS-CoV-2 first binds the host cell through interaction between its S1-RBD and ACE2, triggering conformational changes in the S2 subunit that is indispensable for virus fusion and entry into the target cell [79,80]. Some recent studies also confirmed that RBD is a conformational epitope [78]. Antibodies binding RBD may sterically hinder binding to the nearby peptide S14P5 of ACE2 receptor, thereby abolishing virus infection [34]."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T96","span":{"begin":2,"end":9},"obj":"Body_part"},{"id":"T97","span":{"begin":41,"end":52},"obj":"Body_part"},{"id":"T98","span":{"begin":150,"end":162},"obj":"Body_part"},{"id":"T99","span":{"begin":405,"end":409},"obj":"Body_part"},{"id":"T100","span":{"begin":576,"end":580},"obj":"Body_part"},{"id":"T101","span":{"begin":668,"end":678},"obj":"Body_part"}],"attributes":[{"id":"A96","pred":"fma_id","subj":"T96","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A97","pred":"fma_id","subj":"T97","obj":"http://purl.org/sig/ont/fma/fma82739"},{"id":"A98","pred":"fma_id","subj":"T98","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A99","pred":"fma_id","subj":"T99","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A100","pred":"fma_id","subj":"T100","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A101","pred":"fma_id","subj":"T101","obj":"http://purl.org/sig/ont/fma/fma62871"}],"text":"S protein of SARS-CoV-2 composed of 1273 amino acids [76] uses its N-terminal S1 subunit to bind ACE2 receptor with a better affinity than SARS-CoV S glycoprotein for entry [78]. Effectively, S1 subunit divides into an N-terminal domain (NTD) and a receptor-binding domain (RBD). The latter is necessary for viral binding and a potential target for nAbs. During infection, SARS-CoV-2 first binds the host cell through interaction between its S1-RBD and ACE2, triggering conformational changes in the S2 subunit that is indispensable for virus fusion and entry into the target cell [79,80]. Some recent studies also confirmed that RBD is a conformational epitope [78]. Antibodies binding RBD may sterically hinder binding to the nearby peptide S14P5 of ACE2 receptor, thereby abolishing virus infection [34]."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T85","span":{"begin":13,"end":21},"obj":"Disease"},{"id":"T86","span":{"begin":139,"end":147},"obj":"Disease"},{"id":"T87","span":{"begin":238,"end":241},"obj":"Disease"},{"id":"T89","span":{"begin":362,"end":371},"obj":"Disease"},{"id":"T90","span":{"begin":373,"end":381},"obj":"Disease"},{"id":"T91","span":{"begin":786,"end":801},"obj":"Disease"},{"id":"T92","span":{"begin":792,"end":801},"obj":"Disease"}],"attributes":[{"id":"A85","pred":"mondo_id","subj":"T85","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A86","pred":"mondo_id","subj":"T86","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A87","pred":"mondo_id","subj":"T87","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A88","pred":"mondo_id","subj":"T87","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"},{"id":"A89","pred":"mondo_id","subj":"T89","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A90","pred":"mondo_id","subj":"T90","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A91","pred":"mondo_id","subj":"T91","obj":"http://purl.obolibrary.org/obo/MONDO_0005108"},{"id":"A92","pred":"mondo_id","subj":"T92","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"}],"text":"S protein of SARS-CoV-2 composed of 1273 amino acids [76] uses its N-terminal S1 subunit to bind ACE2 receptor with a better affinity than SARS-CoV S glycoprotein for entry [78]. Effectively, S1 subunit divides into an N-terminal domain (NTD) and a receptor-binding domain (RBD). The latter is necessary for viral binding and a potential target for nAbs. During infection, SARS-CoV-2 first binds the host cell through interaction between its S1-RBD and ACE2, triggering conformational changes in the S2 subunit that is indispensable for virus fusion and entry into the target cell [79,80]. Some recent studies also confirmed that RBD is a conformational epitope [78]. Antibodies binding RBD may sterically hinder binding to the nearby peptide S14P5 of ACE2 receptor, thereby abolishing virus infection [34]."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T288","span":{"begin":78,"end":80},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T289","span":{"begin":116,"end":117},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T290","span":{"begin":192,"end":194},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T291","span":{"begin":247,"end":248},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T292","span":{"begin":326,"end":327},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T293","span":{"begin":405,"end":409},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T294","span":{"begin":442,"end":444},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T295","span":{"begin":500,"end":502},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T296","span":{"begin":500,"end":502},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"},{"id":"T297","span":{"begin":537,"end":542},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T298","span":{"begin":576,"end":580},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T299","span":{"begin":637,"end":638},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T300","span":{"begin":735,"end":742},"obj":"http://purl.obolibrary.org/obo/PR_000018263"},{"id":"T301","span":{"begin":786,"end":791},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T302","span":{"begin":803,"end":805},"obj":"http://purl.obolibrary.org/obo/CLO_0001302"}],"text":"S protein of SARS-CoV-2 composed of 1273 amino acids [76] uses its N-terminal S1 subunit to bind ACE2 receptor with a better affinity than SARS-CoV S glycoprotein for entry [78]. Effectively, S1 subunit divides into an N-terminal domain (NTD) and a receptor-binding domain (RBD). The latter is necessary for viral binding and a potential target for nAbs. During infection, SARS-CoV-2 first binds the host cell through interaction between its S1-RBD and ACE2, triggering conformational changes in the S2 subunit that is indispensable for virus fusion and entry into the target cell [79,80]. Some recent studies also confirmed that RBD is a conformational epitope [78]. Antibodies binding RBD may sterically hinder binding to the nearby peptide S14P5 of ACE2 receptor, thereby abolishing virus infection [34]."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T134","span":{"begin":2,"end":9},"obj":"Chemical"},{"id":"T135","span":{"begin":41,"end":52},"obj":"Chemical"},{"id":"T136","span":{"begin":41,"end":46},"obj":"Chemical"},{"id":"T137","span":{"begin":47,"end":52},"obj":"Chemical"},{"id":"T138","span":{"begin":150,"end":162},"obj":"Chemical"},{"id":"T139","span":{"begin":500,"end":502},"obj":"Chemical"},{"id":"T140","span":{"begin":654,"end":661},"obj":"Chemical"},{"id":"T141","span":{"begin":735,"end":742},"obj":"Chemical"}],"attributes":[{"id":"A134","pred":"chebi_id","subj":"T134","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A135","pred":"chebi_id","subj":"T135","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"},{"id":"A136","pred":"chebi_id","subj":"T136","obj":"http://purl.obolibrary.org/obo/CHEBI_46882"},{"id":"A137","pred":"chebi_id","subj":"T137","obj":"http://purl.obolibrary.org/obo/CHEBI_37527"},{"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_29387"},{"id":"A140","pred":"chebi_id","subj":"T140","obj":"http://purl.obolibrary.org/obo/CHEBI_53000"},{"id":"A141","pred":"chebi_id","subj":"T141","obj":"http://purl.obolibrary.org/obo/CHEBI_16670"}],"text":"S protein of SARS-CoV-2 composed of 1273 amino acids [76] uses its N-terminal S1 subunit to bind ACE2 receptor with a better affinity than SARS-CoV S glycoprotein for entry [78]. Effectively, S1 subunit divides into an N-terminal domain (NTD) and a receptor-binding domain (RBD). The latter is necessary for viral binding and a potential target for nAbs. During infection, SARS-CoV-2 first binds the host cell through interaction between its S1-RBD and ACE2, triggering conformational changes in the S2 subunit that is indispensable for virus fusion and entry into the target cell [79,80]. Some recent studies also confirmed that RBD is a conformational epitope [78]. Antibodies binding RBD may sterically hinder binding to the nearby peptide S14P5 of ACE2 receptor, thereby abolishing virus infection [34]."}

{"project":"LitCovid-sentences","denotations":[{"id":"T179","span":{"begin":0,"end":178},"obj":"Sentence"},{"id":"T180","span":{"begin":179,"end":279},"obj":"Sentence"},{"id":"T181","span":{"begin":280,"end":354},"obj":"Sentence"},{"id":"T182","span":{"begin":355,"end":589},"obj":"Sentence"},{"id":"T183","span":{"begin":590,"end":667},"obj":"Sentence"},{"id":"T184","span":{"begin":668,"end":807},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"S protein of SARS-CoV-2 composed of 1273 amino acids [76] uses its N-terminal S1 subunit to bind ACE2 receptor with a better affinity than SARS-CoV S glycoprotein for entry [78]. Effectively, S1 subunit divides into an N-terminal domain (NTD) and a receptor-binding domain (RBD). The latter is necessary for viral binding and a potential target for nAbs. During infection, SARS-CoV-2 first binds the host cell through interaction between its S1-RBD and ACE2, triggering conformational changes in the S2 subunit that is indispensable for virus fusion and entry into the target cell [79,80]. Some recent studies also confirmed that RBD is a conformational epitope [78]. Antibodies binding RBD may sterically hinder binding to the nearby peptide S14P5 of ACE2 receptor, thereby abolishing virus infection [34]."}

{"project":"2_test","denotations":[{"id":"32450171-19198616-66454502","span":{"begin":582,"end":584},"obj":"19198616"},{"id":"32450171-27936982-66454503","span":{"begin":585,"end":587},"obj":"27936982"},{"id":"32450171-32065055-66454504","span":{"begin":803,"end":805},"obj":"32065055"}],"text":"S protein of SARS-CoV-2 composed of 1273 amino acids [76] uses its N-terminal S1 subunit to bind ACE2 receptor with a better affinity than SARS-CoV S glycoprotein for entry [78]. Effectively, S1 subunit divides into an N-terminal domain (NTD) and a receptor-binding domain (RBD). The latter is necessary for viral binding and a potential target for nAbs. During infection, SARS-CoV-2 first binds the host cell through interaction between its S1-RBD and ACE2, triggering conformational changes in the S2 subunit that is indispensable for virus fusion and entry into the target cell [79,80]. Some recent studies also confirmed that RBD is a conformational epitope [78]. Antibodies binding RBD may sterically hinder binding to the nearby peptide S14P5 of ACE2 receptor, thereby abolishing virus infection [34]."}