PMC:7352545 / 56696-57846 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T500","span":{"begin":57,"end":70},"obj":"Body_part"},{"id":"T501","span":{"begin":57,"end":61},"obj":"Body_part"},{"id":"T502","span":{"begin":236,"end":244},"obj":"Body_part"},{"id":"T503","span":{"begin":350,"end":362},"obj":"Body_part"},{"id":"T504","span":{"begin":494,"end":500},"obj":"Body_part"},{"id":"T505","span":{"begin":669,"end":682},"obj":"Body_part"},{"id":"T506","span":{"begin":732,"end":744},"obj":"Body_part"},{"id":"T507","span":{"begin":934,"end":942},"obj":"Body_part"},{"id":"T508","span":{"begin":1031,"end":1036},"obj":"Body_part"}],"attributes":[{"id":"A500","pred":"fma_id","subj":"T500","obj":"http://purl.org/sig/ont/fma/fma63841"},{"id":"A501","pred":"fma_id","subj":"T501","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A502","pred":"fma_id","subj":"T502","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A503","pred":"fma_id","subj":"T503","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A504","pred":"fma_id","subj":"T504","obj":"http://purl.org/sig/ont/fma/fma9637"},{"id":"A505","pred":"fma_id","subj":"T505","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A506","pred":"fma_id","subj":"T506","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A507","pred":"fma_id","subj":"T507","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A508","pred":"fma_id","subj":"T508","obj":"http://purl.org/sig/ont/fma/fma68646"}],"text":"Both raft and non-raft CEACAMs are involved in the virus–cell membrane fusion event. Formation of CEACAM-associated MHV particles or CEACAM-induced MHV fusion is possible by GPI-anchored CEACAMs through the binding between CEACAM and S proteins. However, MHV can bind to both GPI- and TM-anchored CEACAMs. In addition, soluble CEACAMs also mediate S glycoprotein-driven fusion [104]. This implies that membrane anchors are not intrinsically necessary. In fact, CEACAMs are present in different tissue-specific isoforms [105]. Nevertheless, GPI-anchored CEACAMs are more effective for MHV infection than TM-anchored CEACAMs. Soluble CEACAM receptors can bind to viral S glycoproteins and induce conformational shifts to acceptable S glycoprotein-involved membrane fusions [106]. For example, soluble CEACAM forms interacts with S1 fragments [107] and alters the S1–S2 association stability [108] and S1 oxidation confirmation [109]. S proteins are structurally shifted prior to membrane fusion. For the cross-linking of viruses and cells, integral hydrophobic peptides of the S2 chain are embedded into membranes via membrane hydrophobic cholesterols."}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T28","span":{"begin":494,"end":500},"obj":"Body_part"}],"attributes":[{"id":"A28","pred":"uberon_id","subj":"T28","obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"Both raft and non-raft CEACAMs are involved in the virus–cell membrane fusion event. Formation of CEACAM-associated MHV particles or CEACAM-induced MHV fusion is possible by GPI-anchored CEACAMs through the binding between CEACAM and S proteins. However, MHV can bind to both GPI- and TM-anchored CEACAMs. In addition, soluble CEACAMs also mediate S glycoprotein-driven fusion [104]. This implies that membrane anchors are not intrinsically necessary. In fact, CEACAMs are present in different tissue-specific isoforms [105]. Nevertheless, GPI-anchored CEACAMs are more effective for MHV infection than TM-anchored CEACAMs. Soluble CEACAM receptors can bind to viral S glycoproteins and induce conformational shifts to acceptable S glycoprotein-involved membrane fusions [106]. For example, soluble CEACAM forms interacts with S1 fragments [107] and alters the S1–S2 association stability [108] and S1 oxidation confirmation [109]. S proteins are structurally shifted prior to membrane fusion. For the cross-linking of viruses and cells, integral hydrophobic peptides of the S2 chain are embedded into membranes via membrane hydrophobic cholesterols."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T230","span":{"begin":588,"end":597},"obj":"Disease"}],"attributes":[{"id":"A230","pred":"mondo_id","subj":"T230","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"}],"text":"Both raft and non-raft CEACAMs are involved in the virus–cell membrane fusion event. Formation of CEACAM-associated MHV particles or CEACAM-induced MHV fusion is possible by GPI-anchored CEACAMs through the binding between CEACAM and S proteins. However, MHV can bind to both GPI- and TM-anchored CEACAMs. In addition, soluble CEACAMs also mediate S glycoprotein-driven fusion [104]. This implies that membrane anchors are not intrinsically necessary. In fact, CEACAMs are present in different tissue-specific isoforms [105]. Nevertheless, GPI-anchored CEACAMs are more effective for MHV infection than TM-anchored CEACAMs. Soluble CEACAM receptors can bind to viral S glycoproteins and induce conformational shifts to acceptable S glycoprotein-involved membrane fusions [106]. For example, soluble CEACAM forms interacts with S1 fragments [107] and alters the S1–S2 association stability [108] and S1 oxidation confirmation [109]. S proteins are structurally shifted prior to membrane fusion. For the cross-linking of viruses and cells, integral hydrophobic peptides of the S2 chain are embedded into membranes via membrane hydrophobic cholesterols."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T809","span":{"begin":51,"end":56},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T810","span":{"begin":57,"end":61},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T811","span":{"begin":62,"end":70},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T812","span":{"begin":402,"end":410},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T813","span":{"begin":754,"end":762},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T814","span":{"begin":827,"end":829},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T815","span":{"begin":861,"end":863},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T816","span":{"begin":864,"end":866},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T817","span":{"begin":864,"end":866},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"},{"id":"T818","span":{"begin":899,"end":901},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T819","span":{"begin":977,"end":985},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T820","span":{"begin":1019,"end":1026},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T821","span":{"begin":1031,"end":1036},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T822","span":{"begin":1059,"end":1067},"obj":"http://purl.obolibrary.org/obo/PR_000018263"},{"id":"T823","span":{"begin":1075,"end":1077},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T824","span":{"begin":1075,"end":1077},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"},{"id":"T825","span":{"begin":1102,"end":1111},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T826","span":{"begin":1116,"end":1124},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"}],"text":"Both raft and non-raft CEACAMs are involved in the virus–cell membrane fusion event. Formation of CEACAM-associated MHV particles or CEACAM-induced MHV fusion is possible by GPI-anchored CEACAMs through the binding between CEACAM and S proteins. However, MHV can bind to both GPI- and TM-anchored CEACAMs. In addition, soluble CEACAMs also mediate S glycoprotein-driven fusion [104]. This implies that membrane anchors are not intrinsically necessary. In fact, CEACAMs are present in different tissue-specific isoforms [105]. Nevertheless, GPI-anchored CEACAMs are more effective for MHV infection than TM-anchored CEACAMs. Soluble CEACAM receptors can bind to viral S glycoproteins and induce conformational shifts to acceptable S glycoprotein-involved membrane fusions [106]. For example, soluble CEACAM forms interacts with S1 fragments [107] and alters the S1–S2 association stability [108] and S1 oxidation confirmation [109]. S proteins are structurally shifted prior to membrane fusion. For the cross-linking of viruses and cells, integral hydrophobic peptides of the S2 chain are embedded into membranes via membrane hydrophobic cholesterols."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T145","span":{"begin":174,"end":177},"obj":"Chemical"},{"id":"T147","span":{"begin":236,"end":244},"obj":"Chemical"},{"id":"T13373","span":{"begin":276,"end":279},"obj":"Chemical"},{"id":"T78904","span":{"begin":285,"end":287},"obj":"Chemical"},{"id":"T82009","span":{"begin":350,"end":362},"obj":"Chemical"},{"id":"T45392","span":{"begin":540,"end":543},"obj":"Chemical"},{"id":"T53957","span":{"begin":603,"end":605},"obj":"Chemical"},{"id":"T23174","span":{"begin":669,"end":682},"obj":"Chemical"},{"id":"T158","span":{"begin":732,"end":744},"obj":"Chemical"},{"id":"T8007","span":{"begin":864,"end":866},"obj":"Chemical"},{"id":"T4434","span":{"begin":934,"end":942},"obj":"Chemical"},{"id":"T8852","span":{"begin":1059,"end":1067},"obj":"Chemical"},{"id":"T69566","span":{"begin":1075,"end":1077},"obj":"Chemical"}],"attributes":[{"id":"A10704","pred":"chebi_id","subj":"T145","obj":"http://purl.obolibrary.org/obo/CHEBI_36315"},{"id":"A10771","pred":"chebi_id","subj":"T145","obj":"http://purl.obolibrary.org/obo/CHEBI_59682"},{"id":"A52394","pred":"chebi_id","subj":"T147","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A76391","pred":"chebi_id","subj":"T13373","obj":"http://purl.obolibrary.org/obo/CHEBI_36315"},{"id":"A7206","pred":"chebi_id","subj":"T13373","obj":"http://purl.obolibrary.org/obo/CHEBI_59682"},{"id":"A65661","pred":"chebi_id","subj":"T78904","obj":"http://purl.obolibrary.org/obo/CHEBI_55460"},{"id":"A79162","pred":"chebi_id","subj":"T78904","obj":"http://purl.obolibrary.org/obo/CHEBI_74861"},{"id":"A69257","pred":"chebi_id","subj":"T82009","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A48022","pred":"chebi_id","subj":"T45392","obj":"http://purl.obolibrary.org/obo/CHEBI_36315"},{"id":"A80252","pred":"chebi_id","subj":"T45392","obj":"http://purl.obolibrary.org/obo/CHEBI_59682"},{"id":"A66264","pred":"chebi_id","subj":"T53957","obj":"http://purl.obolibrary.org/obo/CHEBI_55460"},{"id":"A80706","pred":"chebi_id","subj":"T53957","obj":"http://purl.obolibrary.org/obo/CHEBI_74861"},{"id":"A8761","pred":"chebi_id","subj":"T23174","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A26653","pred":"chebi_id","subj":"T158","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A7792","pred":"chebi_id","subj":"T8007","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A90204","pred":"chebi_id","subj":"T4434","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A16976","pred":"chebi_id","subj":"T8852","obj":"http://purl.obolibrary.org/obo/CHEBI_16670"},{"id":"A33038","pred":"chebi_id","subj":"T69566","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"}],"text":"Both raft and non-raft CEACAMs are involved in the virus–cell membrane fusion event. Formation of CEACAM-associated MHV particles or CEACAM-induced MHV fusion is possible by GPI-anchored CEACAMs through the binding between CEACAM and S proteins. However, MHV can bind to both GPI- and TM-anchored CEACAMs. In addition, soluble CEACAMs also mediate S glycoprotein-driven fusion [104]. This implies that membrane anchors are not intrinsically necessary. In fact, CEACAMs are present in different tissue-specific isoforms [105]. Nevertheless, GPI-anchored CEACAMs are more effective for MHV infection than TM-anchored CEACAMs. Soluble CEACAM receptors can bind to viral S glycoproteins and induce conformational shifts to acceptable S glycoprotein-involved membrane fusions [106]. For example, soluble CEACAM forms interacts with S1 fragments [107] and alters the S1–S2 association stability [108] and S1 oxidation confirmation [109]. S proteins are structurally shifted prior to membrane fusion. For the cross-linking of viruses and cells, integral hydrophobic peptides of the S2 chain are embedded into membranes via membrane hydrophobic cholesterols."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T92","span":{"begin":62,"end":77},"obj":"http://purl.obolibrary.org/obo/GO_0061025"},{"id":"T93","span":{"begin":85,"end":94},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T94","span":{"begin":754,"end":770},"obj":"http://purl.obolibrary.org/obo/GO_0061025"},{"id":"T95","span":{"begin":977,"end":992},"obj":"http://purl.obolibrary.org/obo/GO_0061025"}],"text":"Both raft and non-raft CEACAMs are involved in the virus–cell membrane fusion event. Formation of CEACAM-associated MHV particles or CEACAM-induced MHV fusion is possible by GPI-anchored CEACAMs through the binding between CEACAM and S proteins. However, MHV can bind to both GPI- and TM-anchored CEACAMs. In addition, soluble CEACAMs also mediate S glycoprotein-driven fusion [104]. This implies that membrane anchors are not intrinsically necessary. In fact, CEACAMs are present in different tissue-specific isoforms [105]. Nevertheless, GPI-anchored CEACAMs are more effective for MHV infection than TM-anchored CEACAMs. Soluble CEACAM receptors can bind to viral S glycoproteins and induce conformational shifts to acceptable S glycoprotein-involved membrane fusions [106]. For example, soluble CEACAM forms interacts with S1 fragments [107] and alters the S1–S2 association stability [108] and S1 oxidation confirmation [109]. S proteins are structurally shifted prior to membrane fusion. For the cross-linking of viruses and cells, integral hydrophobic peptides of the S2 chain are embedded into membranes via membrane hydrophobic cholesterols."}

{"project":"LitCovid-sentences","denotations":[{"id":"T549","span":{"begin":0,"end":84},"obj":"Sentence"},{"id":"T550","span":{"begin":85,"end":245},"obj":"Sentence"},{"id":"T551","span":{"begin":246,"end":383},"obj":"Sentence"},{"id":"T552","span":{"begin":384,"end":451},"obj":"Sentence"},{"id":"T553","span":{"begin":452,"end":525},"obj":"Sentence"},{"id":"T554","span":{"begin":526,"end":777},"obj":"Sentence"},{"id":"T555","span":{"begin":778,"end":931},"obj":"Sentence"},{"id":"T556","span":{"begin":932,"end":993},"obj":"Sentence"},{"id":"T557","span":{"begin":994,"end":1150},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Both raft and non-raft CEACAMs are involved in the virus–cell membrane fusion event. Formation of CEACAM-associated MHV particles or CEACAM-induced MHV fusion is possible by GPI-anchored CEACAMs through the binding between CEACAM and S proteins. However, MHV can bind to both GPI- and TM-anchored CEACAMs. In addition, soluble CEACAMs also mediate S glycoprotein-driven fusion [104]. This implies that membrane anchors are not intrinsically necessary. In fact, CEACAMs are present in different tissue-specific isoforms [105]. Nevertheless, GPI-anchored CEACAMs are more effective for MHV infection than TM-anchored CEACAMs. Soluble CEACAM receptors can bind to viral S glycoproteins and induce conformational shifts to acceptable S glycoprotein-involved membrane fusions [106]. For example, soluble CEACAM forms interacts with S1 fragments [107] and alters the S1–S2 association stability [108] and S1 oxidation confirmation [109]. S proteins are structurally shifted prior to membrane fusion. For the cross-linking of viruses and cells, integral hydrophobic peptides of the S2 chain are embedded into membranes via membrane hydrophobic cholesterols."}

{"project":"2_test","denotations":[{"id":"32604730-11773370-51944068","span":{"begin":378,"end":381},"obj":"11773370"},{"id":"32604730-11994468-51944069","span":{"begin":520,"end":523},"obj":"11994468"},{"id":"32604730-12414924-51944070","span":{"begin":772,"end":775},"obj":"12414924"},{"id":"32604730-7520090-51944071","span":{"begin":841,"end":844},"obj":"7520090"},{"id":"32604730-11222703-51944072","span":{"begin":890,"end":893},"obj":"11222703"},{"id":"T65492","span":{"begin":378,"end":381},"obj":"11773370"},{"id":"T46798","span":{"begin":520,"end":523},"obj":"11994468"},{"id":"T91956","span":{"begin":772,"end":775},"obj":"12414924"},{"id":"T88769","span":{"begin":841,"end":844},"obj":"7520090"},{"id":"T88164","span":{"begin":890,"end":893},"obj":"11222703"}],"text":"Both raft and non-raft CEACAMs are involved in the virus–cell membrane fusion event. Formation of CEACAM-associated MHV particles or CEACAM-induced MHV fusion is possible by GPI-anchored CEACAMs through the binding between CEACAM and S proteins. However, MHV can bind to both GPI- and TM-anchored CEACAMs. In addition, soluble CEACAMs also mediate S glycoprotein-driven fusion [104]. This implies that membrane anchors are not intrinsically necessary. In fact, CEACAMs are present in different tissue-specific isoforms [105]. Nevertheless, GPI-anchored CEACAMs are more effective for MHV infection than TM-anchored CEACAMs. Soluble CEACAM receptors can bind to viral S glycoproteins and induce conformational shifts to acceptable S glycoprotein-involved membrane fusions [106]. For example, soluble CEACAM forms interacts with S1 fragments [107] and alters the S1–S2 association stability [108] and S1 oxidation confirmation [109]. S proteins are structurally shifted prior to membrane fusion. For the cross-linking of viruses and cells, integral hydrophobic peptides of the S2 chain are embedded into membranes via membrane hydrophobic cholesterols."}