PMC:7435837 / 4972-6183 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T39","span":{"begin":81,"end":88},"obj":"Body_part"},{"id":"T40","span":{"begin":116,"end":131},"obj":"Body_part"},{"id":"T41","span":{"begin":126,"end":131},"obj":"Body_part"},{"id":"T42","span":{"begin":144,"end":149},"obj":"Body_part"},{"id":"T43","span":{"begin":217,"end":230},"obj":"Body_part"},{"id":"T44","span":{"begin":238,"end":251},"obj":"Body_part"},{"id":"T45","span":{"begin":268,"end":275},"obj":"Body_part"},{"id":"T46","span":{"begin":293,"end":300},"obj":"Body_part"},{"id":"T47","span":{"begin":324,"end":329},"obj":"Body_part"},{"id":"T48","span":{"begin":338,"end":343},"obj":"Body_part"},{"id":"T49","span":{"begin":481,"end":489},"obj":"Body_part"},{"id":"T50","span":{"begin":571,"end":574},"obj":"Body_part"},{"id":"T51","span":{"begin":1053,"end":1061},"obj":"Body_part"},{"id":"T52","span":{"begin":1100,"end":1104},"obj":"Body_part"},{"id":"T53","span":{"begin":1205,"end":1210},"obj":"Body_part"}],"attributes":[{"id":"A39","pred":"fma_id","subj":"T39","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A40","pred":"fma_id","subj":"T40","obj":"http://purl.org/sig/ont/fma/fma273565"},{"id":"A41","pred":"fma_id","subj":"T41","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A42","pred":"fma_id","subj":"T42","obj":"http://purl.org/sig/ont/fma/fma9670"},{"id":"A43","pred":"fma_id","subj":"T43","obj":"http://purl.org/sig/ont/fma/fma82784"},{"id":"A44","pred":"fma_id","subj":"T44","obj":"http://purl.org/sig/ont/fma/fma82784"},{"id":"A45","pred":"fma_id","subj":"T45","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A46","pred":"fma_id","subj":"T46","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A47","pred":"fma_id","subj":"T47","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A48","pred":"fma_id","subj":"T48","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A49","pred":"fma_id","subj":"T49","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A50","pred":"fma_id","subj":"T50","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A51","pred":"fma_id","subj":"T51","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A52","pred":"fma_id","subj":"T52","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A53","pred":"fma_id","subj":"T53","obj":"http://purl.org/sig/ont/fma/fma68646"}],"text":"As part of the human host immune responses, the glycans of the coronavirus spike protein subunits are recognized by dendritic cells [11] in the blood which binds to the glycan and subsequently expresses CD4+ and CD8+ glycopeptides. These glycopeptides label the spike protein and this labeled protein is then presented to T-cells [12]. T-cells subsequently recognize the labels, phagocytose these antigen-marked viruses, and degrade them. It has been found that the glycan-binding proteins, also known as lectins [5], can impart broad-spectrum binding properties against HIV-1, SARS-CoV, and human cytomegalovirus. The lectin which is capable of showing broad interaction via oligomannosyl antigens is known as lectin GNA (Galanthus nivalis agglutinin). The N-oligomannosyl cores are embedded in N-glycans which are commonly expressed on the surface of numerous viral pathogens [13]. Once the lectin binds to the glycan, the virus structure may undergo conformational changes that result in the fusion of the virus and host to facilitate virus entry. S-proteins are specifically responsible for host cell entry by coronaviruses [14]. Figure 1 depicts a simplified entry mechanism of the viruses into host cells."}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T2","span":{"begin":144,"end":149},"obj":"Body_part"}],"attributes":[{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"As part of the human host immune responses, the glycans of the coronavirus spike protein subunits are recognized by dendritic cells [11] in the blood which binds to the glycan and subsequently expresses CD4+ and CD8+ glycopeptides. These glycopeptides label the spike protein and this labeled protein is then presented to T-cells [12]. T-cells subsequently recognize the labels, phagocytose these antigen-marked viruses, and degrade them. It has been found that the glycan-binding proteins, also known as lectins [5], can impart broad-spectrum binding properties against HIV-1, SARS-CoV, and human cytomegalovirus. The lectin which is capable of showing broad interaction via oligomannosyl antigens is known as lectin GNA (Galanthus nivalis agglutinin). The N-oligomannosyl cores are embedded in N-glycans which are commonly expressed on the surface of numerous viral pathogens [13]. Once the lectin binds to the glycan, the virus structure may undergo conformational changes that result in the fusion of the virus and host to facilitate virus entry. S-proteins are specifically responsible for host cell entry by coronaviruses [14]. Figure 1 depicts a simplified entry mechanism of the viruses into host cells."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T6","span":{"begin":578,"end":586},"obj":"Disease"}],"attributes":[{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"As part of the human host immune responses, the glycans of the coronavirus spike protein subunits are recognized by dendritic cells [11] in the blood which binds to the glycan and subsequently expresses CD4+ and CD8+ glycopeptides. These glycopeptides label the spike protein and this labeled protein is then presented to T-cells [12]. T-cells subsequently recognize the labels, phagocytose these antigen-marked viruses, and degrade them. It has been found that the glycan-binding proteins, also known as lectins [5], can impart broad-spectrum binding properties against HIV-1, SARS-CoV, and human cytomegalovirus. The lectin which is capable of showing broad interaction via oligomannosyl antigens is known as lectin GNA (Galanthus nivalis agglutinin). The N-oligomannosyl cores are embedded in N-glycans which are commonly expressed on the surface of numerous viral pathogens [13]. Once the lectin binds to the glycan, the virus structure may undergo conformational changes that result in the fusion of the virus and host to facilitate virus entry. S-proteins are specifically responsible for host cell entry by coronaviruses [14]. Figure 1 depicts a simplified entry mechanism of the viruses into host cells."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T58","span":{"begin":15,"end":20},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T59","span":{"begin":116,"end":131},"obj":"http://purl.obolibrary.org/obo/CL_0000451"},{"id":"T60","span":{"begin":133,"end":135},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T61","span":{"begin":144,"end":149},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"T62","span":{"begin":144,"end":149},"obj":"http://www.ebi.ac.uk/efo/EFO_0000296"},{"id":"T63","span":{"begin":203,"end":206},"obj":"http://purl.obolibrary.org/obo/PR_000001004"},{"id":"T64","span":{"begin":212,"end":215},"obj":"http://purl.obolibrary.org/obo/CLO_0053438"},{"id":"T65","span":{"begin":252,"end":257},"obj":"http://purl.obolibrary.org/obo/CLO_0007225"},{"id":"T66","span":{"begin":285,"end":292},"obj":"http://purl.obolibrary.org/obo/CLO_0007225"},{"id":"T67","span":{"begin":322,"end":329},"obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"T68","span":{"begin":336,"end":343},"obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"T69","span":{"begin":371,"end":377},"obj":"http://purl.obolibrary.org/obo/CLO_0007225"},{"id":"T70","span":{"begin":412,"end":419},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T71","span":{"begin":442,"end":445},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T72","span":{"begin":592,"end":597},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T73","span":{"begin":925,"end":930},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T74","span":{"begin":1009,"end":1014},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T75","span":{"begin":1038,"end":1043},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T76","span":{"begin":1100,"end":1104},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T77","span":{"begin":1151,"end":1152},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T78","span":{"begin":1187,"end":1194},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T79","span":{"begin":1205,"end":1210},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"As part of the human host immune responses, the glycans of the coronavirus spike protein subunits are recognized by dendritic cells [11] in the blood which binds to the glycan and subsequently expresses CD4+ and CD8+ glycopeptides. These glycopeptides label the spike protein and this labeled protein is then presented to T-cells [12]. T-cells subsequently recognize the labels, phagocytose these antigen-marked viruses, and degrade them. It has been found that the glycan-binding proteins, also known as lectins [5], can impart broad-spectrum binding properties against HIV-1, SARS-CoV, and human cytomegalovirus. The lectin which is capable of showing broad interaction via oligomannosyl antigens is known as lectin GNA (Galanthus nivalis agglutinin). The N-oligomannosyl cores are embedded in N-glycans which are commonly expressed on the surface of numerous viral pathogens [13]. Once the lectin binds to the glycan, the virus structure may undergo conformational changes that result in the fusion of the virus and host to facilitate virus entry. S-proteins are specifically responsible for host cell entry by coronaviruses [14]. Figure 1 depicts a simplified entry mechanism of the viruses into host cells."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T40","span":{"begin":48,"end":55},"obj":"Chemical"},{"id":"T41","span":{"begin":81,"end":88},"obj":"Chemical"},{"id":"T42","span":{"begin":217,"end":230},"obj":"Chemical"},{"id":"T43","span":{"begin":238,"end":251},"obj":"Chemical"},{"id":"T44","span":{"begin":252,"end":257},"obj":"Chemical"},{"id":"T45","span":{"begin":268,"end":275},"obj":"Chemical"},{"id":"T46","span":{"begin":293,"end":300},"obj":"Chemical"},{"id":"T47","span":{"begin":397,"end":404},"obj":"Chemical"},{"id":"T48","span":{"begin":481,"end":489},"obj":"Chemical"},{"id":"T49","span":{"begin":690,"end":698},"obj":"Chemical"},{"id":"T50","span":{"begin":718,"end":721},"obj":"Chemical"},{"id":"T51","span":{"begin":796,"end":805},"obj":"Chemical"},{"id":"T52","span":{"begin":798,"end":805},"obj":"Chemical"},{"id":"T53","span":{"begin":1053,"end":1061},"obj":"Chemical"}],"attributes":[{"id":"A40","pred":"chebi_id","subj":"T40","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A41","pred":"chebi_id","subj":"T41","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A42","pred":"chebi_id","subj":"T42","obj":"http://purl.obolibrary.org/obo/CHEBI_24396"},{"id":"A43","pred":"chebi_id","subj":"T43","obj":"http://purl.obolibrary.org/obo/CHEBI_24396"},{"id":"A44","pred":"chebi_id","subj":"T44","obj":"http://purl.obolibrary.org/obo/CHEBI_35209"},{"id":"A45","pred":"chebi_id","subj":"T45","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A46","pred":"chebi_id","subj":"T46","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A47","pred":"chebi_id","subj":"T47","obj":"http://purl.obolibrary.org/obo/CHEBI_59132"},{"id":"A48","pred":"chebi_id","subj":"T48","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A49","pred":"chebi_id","subj":"T49","obj":"http://purl.obolibrary.org/obo/CHEBI_59132"},{"id":"A50","pred":"chebi_id","subj":"T50","obj":"http://purl.obolibrary.org/obo/CHEBI_48015"},{"id":"A51","pred":"chebi_id","subj":"T51","obj":"http://purl.obolibrary.org/obo/CHEBI_59520"},{"id":"A52","pred":"chebi_id","subj":"T52","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A53","pred":"chebi_id","subj":"T53","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"As part of the human host immune responses, the glycans of the coronavirus spike protein subunits are recognized by dendritic cells [11] in the blood which binds to the glycan and subsequently expresses CD4+ and CD8+ glycopeptides. These glycopeptides label the spike protein and this labeled protein is then presented to T-cells [12]. T-cells subsequently recognize the labels, phagocytose these antigen-marked viruses, and degrade them. It has been found that the glycan-binding proteins, also known as lectins [5], can impart broad-spectrum binding properties against HIV-1, SARS-CoV, and human cytomegalovirus. The lectin which is capable of showing broad interaction via oligomannosyl antigens is known as lectin GNA (Galanthus nivalis agglutinin). The N-oligomannosyl cores are embedded in N-glycans which are commonly expressed on the surface of numerous viral pathogens [13]. Once the lectin binds to the glycan, the virus structure may undergo conformational changes that result in the fusion of the virus and host to facilitate virus entry. S-proteins are specifically responsible for host cell entry by coronaviruses [14]. Figure 1 depicts a simplified entry mechanism of the viruses into host cells."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T5","span":{"begin":26,"end":42},"obj":"http://purl.obolibrary.org/obo/GO_0006955"}],"text":"As part of the human host immune responses, the glycans of the coronavirus spike protein subunits are recognized by dendritic cells [11] in the blood which binds to the glycan and subsequently expresses CD4+ and CD8+ glycopeptides. These glycopeptides label the spike protein and this labeled protein is then presented to T-cells [12]. T-cells subsequently recognize the labels, phagocytose these antigen-marked viruses, and degrade them. It has been found that the glycan-binding proteins, also known as lectins [5], can impart broad-spectrum binding properties against HIV-1, SARS-CoV, and human cytomegalovirus. The lectin which is capable of showing broad interaction via oligomannosyl antigens is known as lectin GNA (Galanthus nivalis agglutinin). The N-oligomannosyl cores are embedded in N-glycans which are commonly expressed on the surface of numerous viral pathogens [13]. Once the lectin binds to the glycan, the virus structure may undergo conformational changes that result in the fusion of the virus and host to facilitate virus entry. S-proteins are specifically responsible for host cell entry by coronaviruses [14]. Figure 1 depicts a simplified entry mechanism of the viruses into host cells."}

{"project":"LitCovid-PubTator","denotations":[{"id":"88","span":{"begin":262,"end":267},"obj":"Gene"},{"id":"89","span":{"begin":75,"end":80},"obj":"Gene"},{"id":"90","span":{"begin":15,"end":20},"obj":"Species"},{"id":"91","span":{"begin":63,"end":74},"obj":"Species"},{"id":"92","span":{"begin":571,"end":576},"obj":"Species"},{"id":"93","span":{"begin":578,"end":586},"obj":"Species"},{"id":"94","span":{"begin":592,"end":613},"obj":"Species"},{"id":"95","span":{"begin":723,"end":740},"obj":"Species"},{"id":"96","span":{"begin":1114,"end":1127},"obj":"Species"},{"id":"97","span":{"begin":48,"end":55},"obj":"Chemical"},{"id":"98","span":{"begin":169,"end":175},"obj":"Chemical"},{"id":"99","span":{"begin":217,"end":230},"obj":"Chemical"},{"id":"100","span":{"begin":238,"end":251},"obj":"Chemical"},{"id":"101","span":{"begin":466,"end":472},"obj":"Chemical"},{"id":"102","span":{"begin":796,"end":805},"obj":"Chemical"},{"id":"103","span":{"begin":913,"end":919},"obj":"Chemical"}],"attributes":[{"id":"A88","pred":"tao:has_database_id","subj":"88","obj":"Gene:43740568"},{"id":"A89","pred":"tao:has_database_id","subj":"89","obj":"Gene:43740568"},{"id":"A90","pred":"tao:has_database_id","subj":"90","obj":"Tax:9606"},{"id":"A91","pred":"tao:has_database_id","subj":"91","obj":"Tax:11118"},{"id":"A92","pred":"tao:has_database_id","subj":"92","obj":"Tax:11676"},{"id":"A93","pred":"tao:has_database_id","subj":"93","obj":"Tax:694009"},{"id":"A94","pred":"tao:has_database_id","subj":"94","obj":"Tax:10359"},{"id":"A95","pred":"tao:has_database_id","subj":"95","obj":"Tax:4670"},{"id":"A96","pred":"tao:has_database_id","subj":"96","obj":"Tax:11118"},{"id":"A97","pred":"tao:has_database_id","subj":"97","obj":"MESH:D011134"},{"id":"A98","pred":"tao:has_database_id","subj":"98","obj":"MESH:D011134"},{"id":"A99","pred":"tao:has_database_id","subj":"99","obj":"MESH:D006020"},{"id":"A100","pred":"tao:has_database_id","subj":"100","obj":"MESH:D006020"},{"id":"A101","pred":"tao:has_database_id","subj":"101","obj":"MESH:D011134"},{"id":"A103","pred":"tao:has_database_id","subj":"103","obj":"MESH:D011134"}],"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":"As part of the human host immune responses, the glycans of the coronavirus spike protein subunits are recognized by dendritic cells [11] in the blood which binds to the glycan and subsequently expresses CD4+ and CD8+ glycopeptides. These glycopeptides label the spike protein and this labeled protein is then presented to T-cells [12]. T-cells subsequently recognize the labels, phagocytose these antigen-marked viruses, and degrade them. It has been found that the glycan-binding proteins, also known as lectins [5], can impart broad-spectrum binding properties against HIV-1, SARS-CoV, and human cytomegalovirus. The lectin which is capable of showing broad interaction via oligomannosyl antigens is known as lectin GNA (Galanthus nivalis agglutinin). The N-oligomannosyl cores are embedded in N-glycans which are commonly expressed on the surface of numerous viral pathogens [13]. Once the lectin binds to the glycan, the virus structure may undergo conformational changes that result in the fusion of the virus and host to facilitate virus entry. S-proteins are specifically responsible for host cell entry by coronaviruses [14]. Figure 1 depicts a simplified entry mechanism of the viruses into host cells."}

{"project":"LitCovid-sentences","denotations":[{"id":"T42","span":{"begin":0,"end":231},"obj":"Sentence"},{"id":"T43","span":{"begin":232,"end":335},"obj":"Sentence"},{"id":"T44","span":{"begin":336,"end":438},"obj":"Sentence"},{"id":"T45","span":{"begin":439,"end":614},"obj":"Sentence"},{"id":"T46","span":{"begin":615,"end":753},"obj":"Sentence"},{"id":"T47","span":{"begin":754,"end":883},"obj":"Sentence"},{"id":"T48","span":{"begin":884,"end":1050},"obj":"Sentence"},{"id":"T49","span":{"begin":1051,"end":1133},"obj":"Sentence"},{"id":"T50","span":{"begin":1134,"end":1211},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"As part of the human host immune responses, the glycans of the coronavirus spike protein subunits are recognized by dendritic cells [11] in the blood which binds to the glycan and subsequently expresses CD4+ and CD8+ glycopeptides. These glycopeptides label the spike protein and this labeled protein is then presented to T-cells [12]. T-cells subsequently recognize the labels, phagocytose these antigen-marked viruses, and degrade them. It has been found that the glycan-binding proteins, also known as lectins [5], can impart broad-spectrum binding properties against HIV-1, SARS-CoV, and human cytomegalovirus. The lectin which is capable of showing broad interaction via oligomannosyl antigens is known as lectin GNA (Galanthus nivalis agglutinin). The N-oligomannosyl cores are embedded in N-glycans which are commonly expressed on the surface of numerous viral pathogens [13]. Once the lectin binds to the glycan, the virus structure may undergo conformational changes that result in the fusion of the virus and host to facilitate virus entry. S-proteins are specifically responsible for host cell entry by coronaviruses [14]. Figure 1 depicts a simplified entry mechanism of the viruses into host cells."}

{"project":"2_test","denotations":[{"id":"32731428-18799140-71421251","span":{"begin":133,"end":135},"obj":"18799140"},{"id":"32731428-32328406-71421252","span":{"begin":331,"end":333},"obj":"32328406"},{"id":"32731428-24188132-71421253","span":{"begin":514,"end":515},"obj":"24188132"},{"id":"32731428-25774492-71421254","span":{"begin":879,"end":881},"obj":"25774492"},{"id":"32731428-16258152-71421255","span":{"begin":1129,"end":1131},"obj":"16258152"}],"text":"As part of the human host immune responses, the glycans of the coronavirus spike protein subunits are recognized by dendritic cells [11] in the blood which binds to the glycan and subsequently expresses CD4+ and CD8+ glycopeptides. These glycopeptides label the spike protein and this labeled protein is then presented to T-cells [12]. T-cells subsequently recognize the labels, phagocytose these antigen-marked viruses, and degrade them. It has been found that the glycan-binding proteins, also known as lectins [5], can impart broad-spectrum binding properties against HIV-1, SARS-CoV, and human cytomegalovirus. The lectin which is capable of showing broad interaction via oligomannosyl antigens is known as lectin GNA (Galanthus nivalis agglutinin). The N-oligomannosyl cores are embedded in N-glycans which are commonly expressed on the surface of numerous viral pathogens [13]. Once the lectin binds to the glycan, the virus structure may undergo conformational changes that result in the fusion of the virus and host to facilitate virus entry. S-proteins are specifically responsible for host cell entry by coronaviruses [14]. Figure 1 depicts a simplified entry mechanism of the viruses into host cells."}