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LitCovid-PD-FMA-UBERON

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T16","span":{"begin":453,"end":462},"obj":"Disease"},{"id":"T17","span":{"begin":628,"end":637},"obj":"Disease"},{"id":"T18","span":{"begin":774,"end":783},"obj":"Disease"},{"id":"T19","span":{"begin":788,"end":792},"obj":"Disease"},{"id":"T20","span":{"begin":980,"end":989},"obj":"Disease"},{"id":"T21","span":{"begin":1024,"end":1028},"obj":"Disease"},{"id":"T22","span":{"begin":1278,"end":1287},"obj":"Disease"},{"id":"T23","span":{"begin":1403,"end":1407},"obj":"Disease"},{"id":"T24","span":{"begin":1478,"end":1487},"obj":"Disease"},{"id":"T25","span":{"begin":1492,"end":1496},"obj":"Disease"},{"id":"T26","span":{"begin":1547,"end":1556},"obj":"Disease"},{"id":"T27","span":{"begin":1592,"end":1601},"obj":"Disease"}],"attributes":[{"id":"A16","pred":"mondo_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A17","pred":"mondo_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A18","pred":"mondo_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A19","pred":"mondo_id","subj":"T19","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A20","pred":"mondo_id","subj":"T20","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A21","pred":"mondo_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A22","pred":"mondo_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A23","pred":"mondo_id","subj":"T23","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A24","pred":"mondo_id","subj":"T24","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A25","pred":"mondo_id","subj":"T25","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A26","pred":"mondo_id","subj":"T26","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A27","pred":"mondo_id","subj":"T27","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"In all coronaviruses, a homotrimeric spike glycoprotein on the virion’s envelope mediates coronavirus entry into host cells through a mechanism of receptor binding followed by fusion of viral and host membranes.3,6 Coronavirus spike protein contains two functional subunits S1 and S2. The S1 subunit is responsible for binding to host cell receptor, and the S2 subunit is responsible for fusion of viral and host cell membranes.3,7 The spike protein in nCOV-2019 exists in a meta-stable pre-fusion conformation that undergoes a substantial conformational rearrangement to fuse the viral membrane with the host cell membrane.7,8 nCOV-2019 is closely related to bat coronavirus RaTG13 with about 93.1% sequence similarity in the spike protein gene. The sequence similarity of nCOV-2019 and SARS-COV is less than 80% in the spike sequence.2 The S1 subunit in the spike protein includes a receptor binding domain (RBD) that recognizes and binds to the host cells receptor. The RBD of nCOV-2019 shares 72.8% sequence identity to SARS-COV RBD and the root mean squared deviation (RMSD) for the structure between the two proteins is 1.2Å, which shows the high structural similarity.4,8,9 Experimental binding affinity measurements using surface plasmon resonance (SPR) have shown that nCOV-2019 spike protein binds its receptor human angiotensin converter enzyme (ACE2) with 10 to 20 fold higher affinity than SARS-COV binding to ACE2.7 Based on the sequence similarity between RBD of nCOV-2019 and SARS-COV and also the tight binding between the RBD of nCOV-2019 and ACE2, it is most probable that nCOV-2019 uses this receptor on human cells to gain entry into the body.3,6,7,10"}

LitCovid-PD-CLO

LitCovid-PD-CHEBI

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T13","span":{"begin":43,"end":55},"obj":"Chemical"},{"id":"T14","span":{"begin":233,"end":240},"obj":"Chemical"},{"id":"T15","span":{"begin":281,"end":283},"obj":"Chemical"},{"id":"T16","span":{"begin":358,"end":360},"obj":"Chemical"},{"id":"T17","span":{"begin":442,"end":449},"obj":"Chemical"},{"id":"T18","span":{"begin":733,"end":740},"obj":"Chemical"},{"id":"T19","span":{"begin":866,"end":873},"obj":"Chemical"},{"id":"T20","span":{"begin":1114,"end":1122},"obj":"Chemical"},{"id":"T21","span":{"begin":1294,"end":1301},"obj":"Chemical"},{"id":"T22","span":{"begin":1327,"end":1338},"obj":"Chemical"}],"attributes":[{"id":"A13","pred":"chebi_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A14","pred":"chebi_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A15","pred":"chebi_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A16","pred":"chebi_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A17","pred":"chebi_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A18","pred":"chebi_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A19","pred":"chebi_id","subj":"T19","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A20","pred":"chebi_id","subj":"T20","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A21","pred":"chebi_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A22","pred":"chebi_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"}],"text":"In all coronaviruses, a homotrimeric spike glycoprotein on the virion’s envelope mediates coronavirus entry into host cells through a mechanism of receptor binding followed by fusion of viral and host membranes.3,6 Coronavirus spike protein contains two functional subunits S1 and S2. The S1 subunit is responsible for binding to host cell receptor, and the S2 subunit is responsible for fusion of viral and host cell membranes.3,7 The spike protein in nCOV-2019 exists in a meta-stable pre-fusion conformation that undergoes a substantial conformational rearrangement to fuse the viral membrane with the host cell membrane.7,8 nCOV-2019 is closely related to bat coronavirus RaTG13 with about 93.1% sequence similarity in the spike protein gene. The sequence similarity of nCOV-2019 and SARS-COV is less than 80% in the spike sequence.2 The S1 subunit in the spike protein includes a receptor binding domain (RBD) that recognizes and binds to the host cells receptor. The RBD of nCOV-2019 shares 72.8% sequence identity to SARS-COV RBD and the root mean squared deviation (RMSD) for the structure between the two proteins is 1.2Å, which shows the high structural similarity.4,8,9 Experimental binding affinity measurements using surface plasmon resonance (SPR) have shown that nCOV-2019 spike protein binds its receptor human angiotensin converter enzyme (ACE2) with 10 to 20 fold higher affinity than SARS-COV binding to ACE2.7 Based on the sequence similarity between RBD of nCOV-2019 and SARS-COV and also the tight binding between the RBD of nCOV-2019 and ACE2, it is most probable that nCOV-2019 uses this receptor on human cells to gain entry into the body.3,6,7,10"}

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T2","span":{"begin":102,"end":117},"obj":"http://purl.obolibrary.org/obo/GO_0044409"}],"text":"In all coronaviruses, a homotrimeric spike glycoprotein on the virion’s envelope mediates coronavirus entry into host cells through a mechanism of receptor binding followed by fusion of viral and host membranes.3,6 Coronavirus spike protein contains two functional subunits S1 and S2. The S1 subunit is responsible for binding to host cell receptor, and the S2 subunit is responsible for fusion of viral and host cell membranes.3,7 The spike protein in nCOV-2019 exists in a meta-stable pre-fusion conformation that undergoes a substantial conformational rearrangement to fuse the viral membrane with the host cell membrane.7,8 nCOV-2019 is closely related to bat coronavirus RaTG13 with about 93.1% sequence similarity in the spike protein gene. The sequence similarity of nCOV-2019 and SARS-COV is less than 80% in the spike sequence.2 The S1 subunit in the spike protein includes a receptor binding domain (RBD) that recognizes and binds to the host cells receptor. The RBD of nCOV-2019 shares 72.8% sequence identity to SARS-COV RBD and the root mean squared deviation (RMSD) for the structure between the two proteins is 1.2Å, which shows the high structural similarity.4,8,9 Experimental binding affinity measurements using surface plasmon resonance (SPR) have shown that nCOV-2019 spike protein binds its receptor human angiotensin converter enzyme (ACE2) with 10 to 20 fold higher affinity than SARS-COV binding to ACE2.7 Based on the sequence similarity between RBD of nCOV-2019 and SARS-COV and also the tight binding between the RBD of nCOV-2019 and ACE2, it is most probable that nCOV-2019 uses this receptor on human cells to gain entry into the body.3,6,7,10"}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T18","span":{"begin":0,"end":284},"obj":"Sentence"},{"id":"T19","span":{"begin":285,"end":746},"obj":"Sentence"},{"id":"T20","span":{"begin":747,"end":968},"obj":"Sentence"},{"id":"T21","span":{"begin":969,"end":1672},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"In all coronaviruses, a homotrimeric spike glycoprotein on the virion’s envelope mediates coronavirus entry into host cells through a mechanism of receptor binding followed by fusion of viral and host membranes.3,6 Coronavirus spike protein contains two functional subunits S1 and S2. The S1 subunit is responsible for binding to host cell receptor, and the S2 subunit is responsible for fusion of viral and host cell membranes.3,7 The spike protein in nCOV-2019 exists in a meta-stable pre-fusion conformation that undergoes a substantial conformational rearrangement to fuse the viral membrane with the host cell membrane.7,8 nCOV-2019 is closely related to bat coronavirus RaTG13 with about 93.1% sequence similarity in the spike protein gene. The sequence similarity of nCOV-2019 and SARS-COV is less than 80% in the spike sequence.2 The S1 subunit in the spike protein includes a receptor binding domain (RBD) that recognizes and binds to the host cells receptor. The RBD of nCOV-2019 shares 72.8% sequence identity to SARS-COV RBD and the root mean squared deviation (RMSD) for the structure between the two proteins is 1.2Å, which shows the high structural similarity.4,8,9 Experimental binding affinity measurements using surface plasmon resonance (SPR) have shown that nCOV-2019 spike protein binds its receptor human angiotensin converter enzyme (ACE2) with 10 to 20 fold higher affinity than SARS-COV binding to ACE2.7 Based on the sequence similarity between RBD of nCOV-2019 and SARS-COV and also the tight binding between the RBD of nCOV-2019 and ACE2, it is most probable that nCOV-2019 uses this receptor on human cells to gain entry into the body.3,6,7,10"}

LitCovid-PubTator