PMC:7199903 / 2336-2754 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T16","span":{"begin":177,"end":184},"obj":"Body_part"}],"attributes":[{"id":"A16","pred":"fma_id","subj":"T16","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T23","span":{"begin":1,"end":9},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T24","span":{"begin":18,"end":20},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T25","span":{"begin":18,"end":20},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"},{"id":"T26","span":{"begin":31,"end":35},"obj":"http://purl.obolibrary.org/obo/CLO_0053799"},{"id":"T27","span":{"begin":188,"end":189},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T28","span":{"begin":409,"end":412},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"}],"text":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T14","span":{"begin":18,"end":20},"obj":"Chemical"},{"id":"T15","span":{"begin":101,"end":108},"obj":"Chemical"},{"id":"T16","span":{"begin":177,"end":184},"obj":"Chemical"}],"attributes":[{"id":"A14","pred":"chebi_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A15","pred":"chebi_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A16","pred":"chebi_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T21","span":{"begin":88,"end":92},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T22","span":{"begin":164,"end":169},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"}],"text":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

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membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T16","span":{"begin":177,"end":184},"obj":"Body_part"}],"attributes":[{"id":"A16","pred":"fma_id","subj":"T16","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T12","span":{"begin":101,"end":108},"obj":"Chemical"},{"id":"T13","span":{"begin":177,"end":184},"obj":"Chemical"}],"attributes":[{"id":"A12","pred":"chebi_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A13","pred":"chebi_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T21","span":{"begin":38,"end":170},"obj":"Sentence"},{"id":"T22","span":{"begin":171,"end":388},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"89","span":{"begin":66,"end":71},"obj":"Gene"},{"id":"90","span":{"begin":175,"end":184},"obj":"Gene"},{"id":"96","span":{"begin":101,"end":108},"obj":"Chemical"},{"id":"97","span":{"begin":141,"end":142},"obj":"Chemical"}],"attributes":[{"id":"A89","pred":"pubann:denotes","subj":"89","obj":"Gene:43740568"},{"id":"A90","pred":"pubann:denotes","subj":"90","obj":"Gene:43740568"},{"id":"A96","pred":"pubann:denotes","subj":"96","obj":"MESH:D011134"},{"id":"A97","pred":"pubann:denotes","subj":"97","obj":"MESH:D009584"}],"text":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T185","span":{"begin":175,"end":184},"obj":"Protein"}],"attributes":[{"id":"A185","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9UIP0"},{"id":"A186","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9UIN9"},{"id":"A187","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9UIN8"},{"id":"A188","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9UIN7"},{"id":"A189","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9UIN6"},{"id":"A190","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9UBH8"},{"id":"A191","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9NRH8"},{"id":"A192","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9NRH7"},{"id":"A193","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9NRH6"},{"id":"A194","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9NRH5"},{"id":"A195","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9NRH4"},{"id":"A196","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9NPG5"},{"id":"A197","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9NPE0"},{"id":"A198","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q9NP52"},{"id":"A199","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q95IF9"},{"id":"A200","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q8N5P3"},{"id":"A201","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q8IZU6"},{"id":"A202","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q8IZU5"},{"id":"A203","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q8IZU4"},{"id":"A204","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q86Z04"},{"id":"A205","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q7YR44"},{"id":"A206","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q7LA71"},{"id":"A207","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q7LA70"},{"id":"A208","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q5STD2"},{"id":"A209","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q5SQ85"},{"id":"A210","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q1XI16"},{"id":"A211","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q1XI12"},{"id":"A212","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/Q15517"},{"id":"A213","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/O43509"},{"id":"A214","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/O19084"},{"id":"A215","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/B0UYZ7"},{"id":"A216","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/B0S7V2"},{"id":"A217","pred":"uniprot_id","subj":"T185","obj":"https://www.uniprot.org/uniprot/A5A6L9"}],"text":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T9","span":{"begin":1,"end":16},"obj":"http://purl.obolibrary.org/obo/GO_0061025"},{"id":"T10","span":{"begin":150,"end":163},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T11","span":{"begin":254,"end":267},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T12","span":{"begin":395,"end":408},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T8","span":{"begin":1,"end":16},"obj":"http://purl.obolibrary.org/obo/GO_0061025"},{"id":"T9","span":{"begin":150,"end":163},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T10","span":{"begin":254,"end":267},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T11","span":{"begin":395,"end":408},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T8","span":{"begin":1,"end":16},"obj":"http://purl.obolibrary.org/obo/GO_0061025"},{"id":"T9","span":{"begin":141,"end":163},"obj":"http://purl.obolibrary.org/obo/GO_0006487"},{"id":"T10","span":{"begin":150,"end":163},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T11","span":{"begin":254,"end":267},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T12","span":{"begin":395,"end":408},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

{"project":"LitCovid-sentences","denotations":[{"id":"T21","span":{"begin":38,"end":170},"obj":"Sentence"},{"id":"T22","span":{"begin":171,"end":388},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}

{"project":"LitCovid-PubTator","denotations":[{"id":"89","span":{"begin":66,"end":71},"obj":"Gene"},{"id":"90","span":{"begin":175,"end":184},"obj":"Gene"},{"id":"96","span":{"begin":101,"end":108},"obj":"Chemical"},{"id":"97","span":{"begin":141,"end":142},"obj":"Chemical"}],"attributes":[{"id":"A89","pred":"tao:has_database_id","subj":"89","obj":"Gene:43740568"},{"id":"A90","pred":"tao:has_database_id","subj":"90","obj":"Gene:43740568"},{"id":"A96","pred":"tao:has_database_id","subj":"96","obj":"MESH:D011134"},{"id":"A97","pred":"tao:has_database_id","subj":"97","obj":"MESH:D009584"}],"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":" membrane fusion (S2 subunit) (4, 5). The surface of the envelope spike is dominated by host-derived glycans, with each trimer displaying 66 N-linked glycosylation sites. The S protein is a key target in vaccine design efforts (6), and understanding the glycosylation of recombinant viral spikes can reveal fundamental features of viral biology and guide vaccine design strategies (7, 8).\nViral glycosylation has wide-"}