PMC:7205724 / 26957-28042 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"982","span":{"begin":422,"end":426},"obj":"Gene"},{"id":"983","span":{"begin":896,"end":901},"obj":"Gene"},{"id":"984","span":{"begin":830,"end":831},"obj":"Gene"},{"id":"985","span":{"begin":553,"end":558},"obj":"Gene"},{"id":"986","span":{"begin":347,"end":352},"obj":"Gene"},{"id":"987","span":{"begin":4,"end":21},"obj":"Species"},{"id":"988","span":{"begin":23,"end":32},"obj":"Species"},{"id":"989","span":{"begin":86,"end":92},"obj":"Species"},{"id":"990","span":{"begin":111,"end":116},"obj":"Species"},{"id":"991","span":{"begin":126,"end":135},"obj":"Species"},{"id":"992","span":{"begin":337,"end":346},"obj":"Species"},{"id":"993","span":{"begin":441,"end":446},"obj":"Species"},{"id":"994","span":{"begin":543,"end":552},"obj":"Species"},{"id":"995","span":{"begin":662,"end":671},"obj":"Species"},{"id":"996","span":{"begin":751,"end":760},"obj":"Species"},{"id":"997","span":{"begin":820,"end":829},"obj":"Species"},{"id":"998","span":{"begin":935,"end":944},"obj":"Species"},{"id":"999","span":{"begin":996,"end":1005},"obj":"Species"},{"id":"1000","span":{"begin":762,"end":771},"obj":"Chemical"},{"id":"1001","span":{"begin":776,"end":785},"obj":"Chemical"},{"id":"1002","span":{"begin":58,"end":71},"obj":"Disease"},{"id":"1003","span":{"begin":73,"end":81},"obj":"Disease"},{"id":"1004","span":{"begin":98,"end":107},"obj":"Disease"},{"id":"1005","span":{"begin":1068,"end":1076},"obj":"Disease"}],"attributes":[{"id":"A982","pred":"tao:has_database_id","subj":"982","obj":"Gene:59272"},{"id":"A983","pred":"tao:has_database_id","subj":"983","obj":"Gene:3309"},{"id":"A984","pred":"tao:has_database_id","subj":"984","obj":"Gene:43740568"},{"id":"A985","pred":"tao:has_database_id","subj":"985","obj":"Gene:43740568"},{"id":"A986","pred":"tao:has_database_id","subj":"986","obj":"Gene:43740568"},{"id":"A987","pred":"tao:has_database_id","subj":"987","obj":"Tax:2697049"},{"id":"A988","pred":"tao:has_database_id","subj":"988","obj":"Tax:2697049"},{"id":"A989","pred":"tao:has_database_id","subj":"989","obj":"Tax:9606"},{"id":"A990","pred":"tao:has_database_id","subj":"990","obj":"Tax:9606"},{"id":"A991","pred":"tao:has_database_id","subj":"991","obj":"Tax:2697049"},{"id":"A992","pred":"tao:has_database_id","subj":"992","obj":"Tax:2697049"},{"id":"A993","pred":"tao:has_database_id","subj":"993","obj":"Tax:9606"},{"id":"A994","pred":"tao:has_database_id","subj":"994","obj":"Tax:2697049"},{"id":"A995","pred":"tao:has_database_id","subj":"995","obj":"Tax:2697049"},{"id":"A996","pred":"tao:has_database_id","subj":"996","obj":"Tax:2697049"},{"id":"A997","pred":"tao:has_database_id","subj":"997","obj":"Tax:2697049"},{"id":"A998","pred":"tao:has_database_id","subj":"998","obj":"Tax:2697049"},{"id":"A999","pred":"tao:has_database_id","subj":"999","obj":"Tax:2697049"},{"id":"A1002","pred":"tao:has_database_id","subj":"1002","obj":"MESH:D034062"},{"id":"A1003","pred":"tao:has_database_id","subj":"1003","obj":"MESH:C000657245"},{"id":"A1004","pred":"tao:has_database_id","subj":"1004","obj":"MESH:D007239"},{"id":"A1005","pred":"tao:has_database_id","subj":"1005","obj":"MESH:C000657245"}],"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 novel coronavirus, SARS-CoV2, can cause a potentially fatal disease, COVID-19, in humans. The infection of human cells by SARS-CoV2 includes two sequential steps: attachment of the virus to the surface receptor of target cells and the fusion of viral and host membranes. The former requires at least a receptor-binding domain on the SARS-CoV2 Spike protein that can interact with a cell surface receptor, for example, ACE2, expressed on human cells. The latter requires at least the host protease(s) to mediate proteolytic cleavage of the SARS-CoV2 Spike protein into S1 and S2 subunits and consequently promote the fusion of viral and host membranes. Also, SARS-CoV2 possesses a polybasic cleavage site that can explain the high pathogenicity of SARS-CoV2, N-glycans and O-glycans that make the dense decoration of SARS-CoV2 S protein, and cyclic regions that can interact with cell-surface GRP78. Essential elements that process SARS-CoV2 cell entry and specific characteristics that allow SARS-CoV2 to escape the immune system have the potential as targets for COVID-19 therapy."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T192","span":{"begin":117,"end":122},"obj":"Body_part"},{"id":"T193","span":{"begin":225,"end":230},"obj":"Body_part"},{"id":"T194","span":{"begin":353,"end":360},"obj":"Body_part"},{"id":"T195","span":{"begin":386,"end":398},"obj":"Body_part"},{"id":"T196","span":{"begin":386,"end":390},"obj":"Body_part"},{"id":"T197","span":{"begin":447,"end":452},"obj":"Body_part"},{"id":"T198","span":{"begin":559,"end":566},"obj":"Body_part"},{"id":"T199","span":{"begin":832,"end":839},"obj":"Body_part"},{"id":"T200","span":{"begin":883,"end":895},"obj":"Body_part"},{"id":"T201","span":{"begin":883,"end":887},"obj":"Body_part"},{"id":"T202","span":{"begin":945,"end":949},"obj":"Body_part"},{"id":"T203","span":{"begin":1020,"end":1033},"obj":"Body_part"}],"attributes":[{"id":"A192","pred":"fma_id","subj":"T192","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A193","pred":"fma_id","subj":"T193","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A194","pred":"fma_id","subj":"T194","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A195","pred":"fma_id","subj":"T195","obj":"http://purl.org/sig/ont/fma/fma67653"},{"id":"A196","pred":"fma_id","subj":"T196","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A197","pred":"fma_id","subj":"T197","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A198","pred":"fma_id","subj":"T198","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A199","pred":"fma_id","subj":"T199","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A200","pred":"fma_id","subj":"T200","obj":"http://purl.org/sig/ont/fma/fma67653"},{"id":"A201","pred":"fma_id","subj":"T201","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A202","pred":"fma_id","subj":"T202","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A203","pred":"fma_id","subj":"T203","obj":"http://purl.org/sig/ont/fma/fma9825"}],"text":"The novel coronavirus, SARS-CoV2, can cause a potentially fatal disease, COVID-19, in humans. The infection of human cells by SARS-CoV2 includes two sequential steps: attachment of the virus to the surface receptor of target cells and the fusion of viral and host membranes. The former requires at least a receptor-binding domain on the SARS-CoV2 Spike protein that can interact with a cell surface receptor, for example, ACE2, expressed on human cells. The latter requires at least the host protease(s) to mediate proteolytic cleavage of the SARS-CoV2 Spike protein into S1 and S2 subunits and consequently promote the fusion of viral and host membranes. Also, SARS-CoV2 possesses a polybasic cleavage site that can explain the high pathogenicity of SARS-CoV2, N-glycans and O-glycans that make the dense decoration of SARS-CoV2 S protein, and cyclic regions that can interact with cell-surface GRP78. Essential elements that process SARS-CoV2 cell entry and specific characteristics that allow SARS-CoV2 to escape the immune system have the potential as targets for COVID-19 therapy."}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T33","span":{"begin":1020,"end":1033},"obj":"Body_part"}],"attributes":[{"id":"A33","pred":"uberon_id","subj":"T33","obj":"http://purl.obolibrary.org/obo/UBERON_0002405"}],"text":"The novel coronavirus, SARS-CoV2, can cause a potentially fatal disease, COVID-19, in humans. The infection of human cells by SARS-CoV2 includes two sequential steps: attachment of the virus to the surface receptor of target cells and the fusion of viral and host membranes. The former requires at least a receptor-binding domain on the SARS-CoV2 Spike protein that can interact with a cell surface receptor, for example, ACE2, expressed on human cells. The latter requires at least the host protease(s) to mediate proteolytic cleavage of the SARS-CoV2 Spike protein into S1 and S2 subunits and consequently promote the fusion of viral and host membranes. Also, SARS-CoV2 possesses a polybasic cleavage site that can explain the high pathogenicity of SARS-CoV2, N-glycans and O-glycans that make the dense decoration of SARS-CoV2 S protein, and cyclic regions that can interact with cell-surface GRP78. Essential elements that process SARS-CoV2 cell entry and specific characteristics that allow SARS-CoV2 to escape the immune system have the potential as targets for COVID-19 therapy."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T197","span":{"begin":23,"end":27},"obj":"Disease"},{"id":"T198","span":{"begin":73,"end":81},"obj":"Disease"},{"id":"T199","span":{"begin":98,"end":107},"obj":"Disease"},{"id":"T200","span":{"begin":126,"end":130},"obj":"Disease"},{"id":"T201","span":{"begin":337,"end":341},"obj":"Disease"},{"id":"T202","span":{"begin":543,"end":547},"obj":"Disease"},{"id":"T203","span":{"begin":662,"end":666},"obj":"Disease"},{"id":"T204","span":{"begin":751,"end":755},"obj":"Disease"},{"id":"T205","span":{"begin":820,"end":824},"obj":"Disease"},{"id":"T206","span":{"begin":935,"end":939},"obj":"Disease"},{"id":"T207","span":{"begin":996,"end":1000},"obj":"Disease"},{"id":"T208","span":{"begin":1068,"end":1076},"obj":"Disease"}],"attributes":[{"id":"A197","pred":"mondo_id","subj":"T197","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A198","pred":"mondo_id","subj":"T198","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A199","pred":"mondo_id","subj":"T199","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A200","pred":"mondo_id","subj":"T200","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A201","pred":"mondo_id","subj":"T201","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A202","pred":"mondo_id","subj":"T202","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A203","pred":"mondo_id","subj":"T203","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A204","pred":"mondo_id","subj":"T204","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A205","pred":"mondo_id","subj":"T205","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A206","pred":"mondo_id","subj":"T206","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A207","pred":"mondo_id","subj":"T207","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A208","pred":"mondo_id","subj":"T208","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"The novel coronavirus, SARS-CoV2, can cause a potentially fatal disease, COVID-19, in humans. The infection of human cells by SARS-CoV2 includes two sequential steps: attachment of the virus to the surface receptor of target cells and the fusion of viral and host membranes. The former requires at least a receptor-binding domain on the SARS-CoV2 Spike protein that can interact with a cell surface receptor, for example, ACE2, expressed on human cells. The latter requires at least the host protease(s) to mediate proteolytic cleavage of the SARS-CoV2 Spike protein into S1 and S2 subunits and consequently promote the fusion of viral and host membranes. Also, SARS-CoV2 possesses a polybasic cleavage site that can explain the high pathogenicity of SARS-CoV2, N-glycans and O-glycans that make the dense decoration of SARS-CoV2 S protein, and cyclic regions that can interact with cell-surface GRP78. Essential elements that process SARS-CoV2 cell entry and specific characteristics that allow SARS-CoV2 to escape the immune system have the potential as targets for COVID-19 therapy."}

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{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T127","span":{"begin":64,"end":71},"obj":"http://purl.obolibrary.org/obo/OGMS_0000031"},{"id":"T128","span":{"begin":98,"end":107},"obj":"http://purl.obolibrary.org/obo/IDO_0000586"},{"id":"T129","span":{"begin":117,"end":122},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T130","span":{"begin":185,"end":190},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T131","span":{"begin":225,"end":230},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T132","span":{"begin":259,"end":263},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T133","span":{"begin":386,"end":390},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T134","span":{"begin":447,"end":452},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T135","span":{"begin":487,"end":491},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T136","span":{"begin":640,"end":644},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T137","span":{"begin":703,"end":707},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T138","span":{"begin":734,"end":747},"obj":"http://purl.obolibrary.org/obo/IDO_0000450"},{"id":"T139","span":{"begin":883,"end":887},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T140","span":{"begin":945,"end":949},"obj":"http://purl.obolibrary.org/obo/CL_0000000"}],"text":"The novel coronavirus, SARS-CoV2, can cause a potentially fatal disease, COVID-19, in humans. The infection of human cells by SARS-CoV2 includes two sequential steps: attachment of the virus to the surface receptor of target cells and the fusion of viral and host membranes. The former requires at least a receptor-binding domain on the SARS-CoV2 Spike protein that can interact with a cell surface receptor, for example, ACE2, expressed on human cells. The latter requires at least the host protease(s) to mediate proteolytic cleavage of the SARS-CoV2 Spike protein into S1 and S2 subunits and consequently promote the fusion of viral and host membranes. Also, SARS-CoV2 possesses a polybasic cleavage site that can explain the high pathogenicity of SARS-CoV2, N-glycans and O-glycans that make the dense decoration of SARS-CoV2 S protein, and cyclic regions that can interact with cell-surface GRP78. Essential elements that process SARS-CoV2 cell entry and specific characteristics that allow SARS-CoV2 to escape the immune system have the potential as targets for COVID-19 therapy."}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T144","span":{"begin":353,"end":360},"obj":"Chemical"},{"id":"T145","span":{"begin":559,"end":566},"obj":"Chemical"},{"id":"T146","span":{"begin":762,"end":771},"obj":"Chemical"},{"id":"T147","span":{"begin":776,"end":785},"obj":"Chemical"},{"id":"T148","span":{"begin":832,"end":839},"obj":"Chemical"}],"attributes":[{"id":"A144","pred":"chebi_id","subj":"T144","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A145","pred":"chebi_id","subj":"T145","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A146","pred":"chebi_id","subj":"T146","obj":"http://purl.obolibrary.org/obo/CHEBI_59520"},{"id":"A147","pred":"chebi_id","subj":"T147","obj":"http://purl.obolibrary.org/obo/CHEBI_59521"},{"id":"A148","pred":"chebi_id","subj":"T148","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"The novel coronavirus, SARS-CoV2, can cause a potentially fatal disease, COVID-19, in humans. The infection of human cells by SARS-CoV2 includes two sequential steps: attachment of the virus to the surface receptor of target cells and the fusion of viral and host membranes. The former requires at least a receptor-binding domain on the SARS-CoV2 Spike protein that can interact with a cell surface receptor, for example, ACE2, expressed on human cells. The latter requires at least the host protease(s) to mediate proteolytic cleavage of the SARS-CoV2 Spike protein into S1 and S2 subunits and consequently promote the fusion of viral and host membranes. Also, SARS-CoV2 possesses a polybasic cleavage site that can explain the high pathogenicity of SARS-CoV2, N-glycans and O-glycans that make the dense decoration of SARS-CoV2 S protein, and cyclic regions that can interact with cell-surface GRP78. Essential elements that process SARS-CoV2 cell entry and specific characteristics that allow SARS-CoV2 to escape the immune system have the potential as targets for COVID-19 therapy."}

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novel coronavirus, SARS-CoV2, can cause a potentially fatal disease, COVID-19, in humans. The infection of human cells by SARS-CoV2 includes two sequential steps: attachment of the virus to the surface receptor of target cells and the fusion of viral and host membranes. The former requires at least a receptor-binding domain on the SARS-CoV2 Spike protein that can interact with a cell surface receptor, for example, ACE2, expressed on human cells. The latter requires at least the host protease(s) to mediate proteolytic cleavage of the SARS-CoV2 Spike protein into S1 and S2 subunits and consequently promote the fusion of viral and host membranes. Also, SARS-CoV2 possesses a polybasic cleavage site that can explain the high pathogenicity of SARS-CoV2, N-glycans and O-glycans that make the dense decoration of SARS-CoV2 S protein, and cyclic regions that can interact with cell-surface GRP78. Essential elements that process SARS-CoV2 cell entry and specific characteristics that allow SARS-CoV2 to escape the immune system have the potential as targets for COVID-19 therapy."}

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novel coronavirus, SARS-CoV2, can cause a potentially fatal disease, COVID-19, in humans. The infection of human cells by SARS-CoV2 includes two sequential steps: attachment of the virus to the surface receptor of target cells and the fusion of viral and host membranes. The former requires at least a receptor-binding domain on the SARS-CoV2 Spike protein that can interact with a cell surface receptor, for example, ACE2, expressed on human cells. The latter requires at least the host protease(s) to mediate proteolytic cleavage of the SARS-CoV2 Spike protein into S1 and S2 subunits and consequently promote the fusion of viral and host membranes. Also, SARS-CoV2 possesses a polybasic cleavage site that can explain the high pathogenicity of SARS-CoV2, N-glycans and O-glycans that make the dense decoration of SARS-CoV2 S protein, and cyclic regions that can interact with cell-surface GRP78. Essential elements that process SARS-CoV2 cell entry and specific characteristics that allow SARS-CoV2 to escape the immune system have the potential as targets for COVID-19 therapy."}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T192","span":{"begin":117,"end":122},"obj":"Body_part"},{"id":"T193","span":{"begin":225,"end":230},"obj":"Body_part"},{"id":"T194","span":{"begin":353,"end":360},"obj":"Body_part"},{"id":"T195","span":{"begin":386,"end":398},"obj":"Body_part"},{"id":"T196","span":{"begin":386,"end":390},"obj":"Body_part"},{"id":"T197","span":{"begin":447,"end":452},"obj":"Body_part"},{"id":"T198","span":{"begin":559,"end":566},"obj":"Body_part"},{"id":"T199","span":{"begin":832,"end":839},"obj":"Body_part"},{"id":"T200","span":{"begin":883,"end":895},"obj":"Body_part"},{"id":"T201","span":{"begin":883,"end":887},"obj":"Body_part"},{"id":"T202","span":{"begin":945,"end":949},"obj":"Body_part"},{"id":"T203","span":{"begin":1020,"end":1033},"obj":"Body_part"}],"attributes":[{"id":"A199","pred":"fma_id","subj":"T199","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A196","pred":"fma_id","subj":"T196","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A198","pred":"fma_id","subj":"T198","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A200","pred":"fma_id","subj":"T200","obj":"http://purl.org/sig/ont/fma/fma67653"},{"id":"A202","pred":"fma_id","subj":"T202","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A194","pred":"fma_id","subj":"T194","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A193","pred":"fma_id","subj":"T193","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A203","pred":"fma_id","subj":"T203","obj":"http://purl.org/sig/ont/fma/fma9825"},{"id":"A195","pred":"fma_id","subj":"T195","obj":"http://purl.org/sig/ont/fma/fma67653"},{"id":"A197","pred":"fma_id","subj":"T197","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A192","pred":"fma_id","subj":"T192","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A201","pred":"fma_id","subj":"T201","obj":"http://purl.org/sig/ont/fma/fma68646"}],"text":"The novel coronavirus, SARS-CoV2, can cause a potentially fatal disease, COVID-19, in humans. The infection of human cells by SARS-CoV2 includes two sequential steps: attachment of the virus to the surface receptor of target cells and the fusion of viral and host membranes. The former requires at least a receptor-binding domain on the SARS-CoV2 Spike protein that can interact with a cell surface receptor, for example, ACE2, expressed on human cells. The latter requires at least the host protease(s) to mediate proteolytic cleavage of the SARS-CoV2 Spike protein into S1 and S2 subunits and consequently promote the fusion of viral and host membranes. Also, SARS-CoV2 possesses a polybasic cleavage site that can explain the high pathogenicity of SARS-CoV2, N-glycans and O-glycans that make the dense decoration of SARS-CoV2 S protein, and cyclic regions that can interact with cell-surface GRP78. Essential elements that process SARS-CoV2 cell entry and specific characteristics that allow SARS-CoV2 to escape the immune system have the potential as targets for COVID-19 therapy."}

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T187","span":{"begin":23,"end":32},"obj":"Disease"},{"id":"T188","span":{"begin":73,"end":81},"obj":"Disease"},{"id":"T189","span":{"begin":98,"end":107},"obj":"Disease"},{"id":"T190","span":{"begin":126,"end":135},"obj":"Disease"},{"id":"T191","span":{"begin":337,"end":346},"obj":"Disease"},{"id":"T192","span":{"begin":543,"end":552},"obj":"Disease"},{"id":"T193","span":{"begin":662,"end":671},"obj":"Disease"},{"id":"T194","span":{"begin":751,"end":760},"obj":"Disease"},{"id":"T195","span":{"begin":820,"end":829},"obj":"Disease"},{"id":"T196","span":{"begin":935,"end":944},"obj":"Disease"},{"id":"T197","span":{"begin":996,"end":1005},"obj":"Disease"},{"id":"T198","span":{"begin":1068,"end":1076},"obj":"Disease"}],"attributes":[{"id":"A187","pred":"mondo_id","subj":"T187","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A189","pred":"mondo_id","subj":"T189","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A198","pred":"mondo_id","subj":"T198","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A188","pred":"mondo_id","subj":"T188","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A195","pred":"mondo_id","subj":"T195","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A194","pred":"mondo_id","subj":"T194","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A193","pred":"mondo_id","subj":"T193","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A192","pred":"mondo_id","subj":"T192","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A197","pred":"mondo_id","subj":"T197","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A191","pred":"mondo_id","subj":"T191","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A190","pred":"mondo_id","subj":"T190","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A196","pred":"mondo_id","subj":"T196","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"The novel coronavirus, SARS-CoV2, can cause a potentially fatal disease, COVID-19, in humans. The infection of human cells by SARS-CoV2 includes two sequential steps: attachment of the virus to the surface receptor of target cells and the fusion of viral and host membranes. The former requires at least a receptor-binding domain on the SARS-CoV2 Spike protein that can interact with a cell surface receptor, for example, ACE2, expressed on human cells. The latter requires at least the host protease(s) to mediate proteolytic cleavage of the SARS-CoV2 Spike protein into S1 and S2 subunits and consequently promote the fusion of viral and host membranes. Also, SARS-CoV2 possesses a polybasic cleavage site that can explain the high pathogenicity of SARS-CoV2, N-glycans and O-glycans that make the dense decoration of SARS-CoV2 S protein, and cyclic regions that can interact with cell-surface GRP78. Essential elements that process SARS-CoV2 cell entry and specific characteristics that allow SARS-CoV2 to escape the immune system have the potential as targets for COVID-19 therapy."}

{"project":"LitCovid-sentences","denotations":[{"id":"T221","span":{"begin":0,"end":93},"obj":"Sentence"},{"id":"T222","span":{"begin":94,"end":274},"obj":"Sentence"},{"id":"T223","span":{"begin":275,"end":453},"obj":"Sentence"},{"id":"T224","span":{"begin":454,"end":655},"obj":"Sentence"},{"id":"T225","span":{"begin":656,"end":902},"obj":"Sentence"},{"id":"T226","span":{"begin":903,"end":1085},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The novel coronavirus, SARS-CoV2, can cause a potentially fatal disease, COVID-19, in humans. The infection of human cells by SARS-CoV2 includes two sequential steps: attachment of the virus to the surface receptor of target cells and the fusion of viral and host membranes. The former requires at least a receptor-binding domain on the SARS-CoV2 Spike protein that can interact with a cell surface receptor, for example, ACE2, expressed on human cells. The latter requires at least the host protease(s) to mediate proteolytic cleavage of the SARS-CoV2 Spike protein into S1 and S2 subunits and consequently promote the fusion of viral and host membranes. Also, SARS-CoV2 possesses a polybasic cleavage site that can explain the high pathogenicity of SARS-CoV2, N-glycans and O-glycans that make the dense decoration of SARS-CoV2 S protein, and cyclic regions that can interact with cell-surface GRP78. Essential elements that process SARS-CoV2 cell entry and specific characteristics that allow SARS-CoV2 to escape the immune system have the potential as targets for COVID-19 therapy."}