PMC:7105881 / 60738-61526 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T334","span":{"begin":38,"end":46},"obj":"Body_part"},{"id":"T335","span":{"begin":111,"end":119},"obj":"Body_part"},{"id":"T336","span":{"begin":267,"end":274},"obj":"Body_part"},{"id":"T337","span":{"begin":336,"end":343},"obj":"Body_part"},{"id":"T338","span":{"begin":455,"end":463},"obj":"Body_part"}],"attributes":[{"id":"A334","pred":"fma_id","subj":"T334","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A335","pred":"fma_id","subj":"T335","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A336","pred":"fma_id","subj":"T336","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A337","pred":"fma_id","subj":"T337","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A338","pred":"fma_id","subj":"T338","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"Structures of SARS-CoV and MERS-CoV S proteins, RBDs, and their complexes with respective receptor. Trimeric S proteins of SARS-CoV (PDB: 5×5b) (A) and MERS-CoV (PDB: 5×5f) (C) are colored differently for each monomer. Two conformations of the RBD in each trimeric S protein are labeled as standing and lying states. The RBDs of each S protein are shown as light blue on the right panel. ACE2 and DPP4 receptors are respectively modeled to the trimeric S proteins by match-alignment of SARS-CoV RBD-ACE2 complex (PDB: 2AJF) to SARS-CoV S trimer (B) or MERS-CoV RBD-DPP4 complex (PDB: 4kr0) to MERS-CoV S trimer (D). Each of the RBD-receptor complexes is shown on the right panel. ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase 4; RBD, receptor-binding domain; S, spike."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T285","span":{"begin":14,"end":22},"obj":"Disease"},{"id":"T286","span":{"begin":123,"end":131},"obj":"Disease"},{"id":"T287","span":{"begin":133,"end":139},"obj":"Disease"},{"id":"T288","span":{"begin":162,"end":168},"obj":"Disease"},{"id":"T289","span":{"begin":486,"end":494},"obj":"Disease"},{"id":"T290","span":{"begin":527,"end":535},"obj":"Disease"}],"attributes":[{"id":"A285","pred":"mondo_id","subj":"T285","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A286","pred":"mondo_id","subj":"T286","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A287","pred":"mondo_id","subj":"T287","obj":"http://purl.obolibrary.org/obo/MONDO_0009394"},{"id":"A288","pred":"mondo_id","subj":"T288","obj":"http://purl.obolibrary.org/obo/MONDO_0009394"},{"id":"A289","pred":"mondo_id","subj":"T289","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A290","pred":"mondo_id","subj":"T290","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Structures of SARS-CoV and MERS-CoV S proteins, RBDs, and their complexes with respective receptor. Trimeric S proteins of SARS-CoV (PDB: 5×5b) (A) and MERS-CoV (PDB: 5×5f) (C) are colored differently for each monomer. Two conformations of the RBD in each trimeric S protein are labeled as standing and lying states. The RBDs of each S protein are shown as light blue on the right panel. ACE2 and DPP4 receptors are respectively modeled to the trimeric S proteins by match-alignment of SARS-CoV RBD-ACE2 complex (PDB: 2AJF) to SARS-CoV S trimer (B) or MERS-CoV RBD-DPP4 complex (PDB: 4kr0) to MERS-CoV S trimer (D). Each of the RBD-receptor complexes is shown on the right panel. ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase 4; RBD, receptor-binding domain; S, spike."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T681","span":{"begin":145,"end":146},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T682","span":{"begin":279,"end":286},"obj":"http://purl.obolibrary.org/obo/CLO_0007225"},{"id":"T683","span":{"begin":546,"end":547},"obj":"http://purl.obolibrary.org/obo/CLO_0001021"},{"id":"T684","span":{"begin":632,"end":650},"obj":"http://purl.obolibrary.org/obo/GO_0043235"}],"text":"Structures of SARS-CoV and MERS-CoV S proteins, RBDs, and their complexes with respective receptor. Trimeric S proteins of SARS-CoV (PDB: 5×5b) (A) and MERS-CoV (PDB: 5×5f) (C) are colored differently for each monomer. Two conformations of the RBD in each trimeric S protein are labeled as standing and lying states. The RBDs of each S protein are shown as light blue on the right panel. ACE2 and DPP4 receptors are respectively modeled to the trimeric S proteins by match-alignment of SARS-CoV RBD-ACE2 complex (PDB: 2AJF) to SARS-CoV S trimer (B) or MERS-CoV RBD-DPP4 complex (PDB: 4kr0) to MERS-CoV S trimer (D). Each of the RBD-receptor complexes is shown on the right panel. ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase 4; RBD, receptor-binding domain; S, spike."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T88377","span":{"begin":38,"end":46},"obj":"Chemical"},{"id":"T67552","span":{"begin":111,"end":119},"obj":"Chemical"},{"id":"T11071","span":{"begin":267,"end":274},"obj":"Chemical"},{"id":"T81908","span":{"begin":336,"end":343},"obj":"Chemical"},{"id":"T18364","span":{"begin":455,"end":463},"obj":"Chemical"},{"id":"T2754","span":{"begin":686,"end":697},"obj":"Chemical"}],"attributes":[{"id":"A78194","pred":"chebi_id","subj":"T88377","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A47066","pred":"chebi_id","subj":"T67552","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A55443","pred":"chebi_id","subj":"T11071","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A45232","pred":"chebi_id","subj":"T81908","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A74662","pred":"chebi_id","subj":"T18364","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A86544","pred":"chebi_id","subj":"T2754","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"}],"text":"Structures of SARS-CoV and MERS-CoV S proteins, RBDs, and their complexes with respective receptor. Trimeric S proteins of SARS-CoV (PDB: 5×5b) (A) and MERS-CoV (PDB: 5×5f) (C) are colored differently for each monomer. Two conformations of the RBD in each trimeric S protein are labeled as standing and lying states. The RBDs of each S protein are shown as light blue on the right panel. ACE2 and DPP4 receptors are respectively modeled to the trimeric S proteins by match-alignment of SARS-CoV RBD-ACE2 complex (PDB: 2AJF) to SARS-CoV S trimer (B) or MERS-CoV RBD-DPP4 complex (PDB: 4kr0) to MERS-CoV S trimer (D). Each of the RBD-receptor complexes is shown on the right panel. ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase 4; RBD, receptor-binding domain; S, spike."}

{"project":"LitCovid-sentences","denotations":[{"id":"T335","span":{"begin":100,"end":137},"obj":"Sentence"},{"id":"T336","span":{"begin":138,"end":166},"obj":"Sentence"},{"id":"T337","span":{"begin":167,"end":218},"obj":"Sentence"},{"id":"T338","span":{"begin":219,"end":316},"obj":"Sentence"},{"id":"T339","span":{"begin":317,"end":387},"obj":"Sentence"},{"id":"T340","span":{"begin":388,"end":517},"obj":"Sentence"},{"id":"T341","span":{"begin":518,"end":583},"obj":"Sentence"},{"id":"T342","span":{"begin":584,"end":615},"obj":"Sentence"},{"id":"T343","span":{"begin":616,"end":679},"obj":"Sentence"},{"id":"T344","span":{"begin":680,"end":788},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Structures of SARS-CoV and MERS-CoV S proteins, RBDs, and their complexes with respective receptor. Trimeric S proteins of SARS-CoV (PDB: 5×5b) (A) and MERS-CoV (PDB: 5×5f) (C) are colored differently for each monomer. Two conformations of the RBD in each trimeric S protein are labeled as standing and lying states. The RBDs of each S protein are shown as light blue on the right panel. ACE2 and DPP4 receptors are respectively modeled to the trimeric S proteins by match-alignment of SARS-CoV RBD-ACE2 complex (PDB: 2AJF) to SARS-CoV S trimer (B) or MERS-CoV RBD-DPP4 complex (PDB: 4kr0) to MERS-CoV S trimer (D). Each of the RBD-receptor complexes is shown on the right panel. ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase 4; RBD, receptor-binding domain; S, spike."}