PMC:7352545 / 18413-19469 JSONTXT

{"project":"LitCovid_Glycan-Motif-Structure","denotations":[{"id":"T34","span":{"begin":312,"end":314},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T35","span":{"begin":344,"end":346},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T36","span":{"begin":543,"end":545},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T37","span":{"begin":674,"end":676},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T38","span":{"begin":766,"end":768},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"HE hemagglutinates and destroys receptors. As RNA viruses, CoVs bear RDEs, which are used in effective attachment to hosts and also reversely in detachment from the hosts. For example, enveloped RNA viruses evade the hosts via their RDEs. Currently, RDE-related functional enzymes such as neuraminidase (NA) and SA-O-acetyl-esterase are known. SA-O-acetyl-esterase was originally identified in influenza C virus and in nidoviruses (CoV and torovirus) as well as in salmon anemia virus (teleost orthomyxovirus). The origin and evolution of CoV SA-O-acetylesterases are correlated to other viruses. The fusion event of S glycoprotein and HE is specific for HCoV attachment to SA-associated receptors in the host [25]. The HE has acetylesterase activity [26]. In early SA-related biology, influenza A/B viruses were found to recognize chicken erythrocytes in 1942 [27]. They caused hemagglutination through clumping by virus-borne hemagglutinin. These phenomena were widely found in influenza viruses, paramyxoviruses, Newcastle disease (NDV) and mumps virus."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T201","span":{"begin":46,"end":49},"obj":"Body_part"},{"id":"T202","span":{"begin":195,"end":198},"obj":"Body_part"},{"id":"T203","span":{"begin":619,"end":631},"obj":"Body_part"},{"id":"T204","span":{"begin":840,"end":852},"obj":"Body_part"}],"attributes":[{"id":"A201","pred":"fma_id","subj":"T201","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A202","pred":"fma_id","subj":"T202","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A203","pred":"fma_id","subj":"T203","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A204","pred":"fma_id","subj":"T204","obj":"http://purl.org/sig/ont/fma/fma62845"}],"text":"HE hemagglutinates and destroys receptors. As RNA viruses, CoVs bear RDEs, which are used in effective attachment to hosts and also reversely in detachment from the hosts. For example, enveloped RNA viruses evade the hosts via their RDEs. Currently, RDE-related functional enzymes such as neuraminidase (NA) and SA-O-acetyl-esterase are known. SA-O-acetyl-esterase was originally identified in influenza C virus and in nidoviruses (CoV and torovirus) as well as in salmon anemia virus (teleost orthomyxovirus). The origin and evolution of CoV SA-O-acetylesterases are correlated to other viruses. The fusion event of S glycoprotein and HE is specific for HCoV attachment to SA-associated receptors in the host [25]. The HE has acetylesterase activity [26]. In early SA-related biology, influenza A/B viruses were found to recognize chicken erythrocytes in 1942 [27]. They caused hemagglutination through clumping by virus-borne hemagglutinin. These phenomena were widely found in influenza viruses, paramyxoviruses, Newcastle disease (NDV) and mumps virus."}

{"project":"LitCovid-PubTator","denotations":[{"id":"552","span":{"begin":766,"end":768},"obj":"Gene"},{"id":"553","span":{"begin":59,"end":63},"obj":"Species"},{"id":"554","span":{"begin":394,"end":411},"obj":"Species"},{"id":"555","span":{"begin":432,"end":435},"obj":"Species"},{"id":"556","span":{"begin":539,"end":542},"obj":"Species"},{"id":"557","span":{"begin":832,"end":839},"obj":"Species"},{"id":"558","span":{"begin":980,"end":997},"obj":"Species"},{"id":"559","span":{"begin":1044,"end":1055},"obj":"Species"},{"id":"560","span":{"begin":786,"end":795},"obj":"Species"},{"id":"561","span":{"begin":1016,"end":1025},"obj":"Species"},{"id":"562","span":{"begin":0,"end":18},"obj":"Chemical"},{"id":"563","span":{"begin":465,"end":484},"obj":"Disease"}],"attributes":[{"id":"A552","pred":"tao:has_database_id","subj":"552","obj":"Gene:6296"},{"id":"A553","pred":"tao:has_database_id","subj":"553","obj":"Tax:11118"},{"id":"A554","pred":"tao:has_database_id","subj":"554","obj":"Tax:11552"},{"id":"A555","pred":"tao:has_database_id","subj":"555","obj":"Tax:11118"},{"id":"A556","pred":"tao:has_database_id","subj":"556","obj":"Tax:11118"},{"id":"A557","pred":"tao:has_database_id","subj":"557","obj":"Tax:9031"},{"id":"A558","pred":"tao:has_database_id","subj":"558","obj":"Tax:11308"},{"id":"A559","pred":"tao:has_database_id","subj":"559","obj":"Tax:11161"},{"id":"A560","pred":"tao:has_database_id","subj":"560","obj":"Tax:11552"},{"id":"A561","pred":"tao:has_database_id","subj":"561","obj":"Tax:11176"},{"id":"A563","pred":"tao:has_database_id","subj":"563","obj":"MESH:D000740"}],"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":"HE hemagglutinates and destroys receptors. As RNA viruses, CoVs bear RDEs, which are used in effective attachment to hosts and also reversely in detachment from the hosts. For example, enveloped RNA viruses evade the hosts via their RDEs. Currently, RDE-related functional enzymes such as neuraminidase (NA) and SA-O-acetyl-esterase are known. SA-O-acetyl-esterase was originally identified in influenza C virus and in nidoviruses (CoV and torovirus) as well as in salmon anemia virus (teleost orthomyxovirus). The origin and evolution of CoV SA-O-acetylesterases are correlated to other viruses. The fusion event of S glycoprotein and HE is specific for HCoV attachment to SA-associated receptors in the host [25]. The HE has acetylesterase activity [26]. In early SA-related biology, influenza A/B viruses were found to recognize chicken erythrocytes in 1942 [27]. They caused hemagglutination through clumping by virus-borne hemagglutinin. These phenomena were widely found in influenza viruses, paramyxoviruses, Newcastle disease (NDV) and mumps virus."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T78","span":{"begin":394,"end":403},"obj":"Disease"},{"id":"T79","span":{"begin":472,"end":478},"obj":"Disease"},{"id":"T80","span":{"begin":786,"end":795},"obj":"Disease"},{"id":"T81","span":{"begin":980,"end":989},"obj":"Disease"},{"id":"T82","span":{"begin":1016,"end":1033},"obj":"Disease"},{"id":"T83","span":{"begin":1044,"end":1049},"obj":"Disease"}],"attributes":[{"id":"A78","pred":"mondo_id","subj":"T78","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A79","pred":"mondo_id","subj":"T79","obj":"http://purl.obolibrary.org/obo/MONDO_0002280"},{"id":"A80","pred":"mondo_id","subj":"T80","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A81","pred":"mondo_id","subj":"T81","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A82","pred":"mondo_id","subj":"T82","obj":"http://purl.obolibrary.org/obo/MONDO_0005875"},{"id":"A83","pred":"mondo_id","subj":"T83","obj":"http://purl.obolibrary.org/obo/MONDO_0000989"}],"text":"HE hemagglutinates and destroys receptors. As RNA viruses, CoVs bear RDEs, which are used in effective attachment to hosts and also reversely in detachment from the hosts. For example, enveloped RNA viruses evade the hosts via their RDEs. Currently, RDE-related functional enzymes such as neuraminidase (NA) and SA-O-acetyl-esterase are known. SA-O-acetyl-esterase was originally identified in influenza C virus and in nidoviruses (CoV and torovirus) as well as in salmon anemia virus (teleost orthomyxovirus). The origin and evolution of CoV SA-O-acetylesterases are correlated to other viruses. The fusion event of S glycoprotein and HE is specific for HCoV attachment to SA-associated receptors in the host [25]. The HE has acetylesterase activity [26]. In early SA-related biology, influenza A/B viruses were found to recognize chicken erythrocytes in 1942 [27]. They caused hemagglutination through clumping by virus-borne hemagglutinin. These phenomena were widely found in influenza viruses, paramyxoviruses, Newcastle disease (NDV) and mumps virus."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T211","span":{"begin":50,"end":57},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T212","span":{"begin":69,"end":73},"obj":"http://purl.obolibrary.org/obo/CLO_0008774"},{"id":"T213","span":{"begin":199,"end":206},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T214","span":{"begin":233,"end":237},"obj":"http://purl.obolibrary.org/obo/CLO_0008774"},{"id":"T215","span":{"begin":406,"end":411},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T216","span":{"begin":479,"end":484},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T217","span":{"begin":588,"end":595},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T218","span":{"begin":723,"end":726},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T219","span":{"begin":742,"end":750},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T220","span":{"begin":796,"end":797},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T221","span":{"begin":798,"end":799},"obj":"http://purl.obolibrary.org/obo/CLO_0001021"},{"id":"T222","span":{"begin":800,"end":807},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T223","span":{"begin":832,"end":839},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9031"},{"id":"T224","span":{"begin":840,"end":852},"obj":"http://purl.obolibrary.org/obo/CL_0000232"},{"id":"T225","span":{"begin":862,"end":864},"obj":"http://purl.obolibrary.org/obo/CLO_0050509"},{"id":"T226","span":{"begin":916,"end":921},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T227","span":{"begin":990,"end":997},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T228","span":{"begin":1050,"end":1055},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"}],"text":"HE hemagglutinates and destroys receptors. As RNA viruses, CoVs bear RDEs, which are used in effective attachment to hosts and also reversely in detachment from the hosts. For example, enveloped RNA viruses evade the hosts via their RDEs. Currently, RDE-related functional enzymes such as neuraminidase (NA) and SA-O-acetyl-esterase are known. SA-O-acetyl-esterase was originally identified in influenza C virus and in nidoviruses (CoV and torovirus) as well as in salmon anemia virus (teleost orthomyxovirus). The origin and evolution of CoV SA-O-acetylesterases are correlated to other viruses. The fusion event of S glycoprotein and HE is specific for HCoV attachment to SA-associated receptors in the host [25]. The HE has acetylesterase activity [26]. In early SA-related biology, influenza A/B viruses were found to recognize chicken erythrocytes in 1942 [27]. They caused hemagglutination through clumping by virus-borne hemagglutinin. These phenomena were widely found in influenza viruses, paramyxoviruses, Newcastle disease (NDV) and mumps virus."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T365","span":{"begin":304,"end":306},"obj":"Chemical"},{"id":"T366","span":{"begin":312,"end":314},"obj":"Chemical"},{"id":"T371","span":{"begin":317,"end":323},"obj":"Chemical"},{"id":"T373","span":{"begin":344,"end":346},"obj":"Chemical"},{"id":"T378","span":{"begin":349,"end":355},"obj":"Chemical"},{"id":"T380","span":{"begin":543,"end":545},"obj":"Chemical"},{"id":"T385","span":{"begin":619,"end":631},"obj":"Chemical"},{"id":"T386","span":{"begin":674,"end":676},"obj":"Chemical"},{"id":"T391","span":{"begin":766,"end":768},"obj":"Chemical"}],"attributes":[{"id":"A365","pred":"chebi_id","subj":"T365","obj":"http://purl.obolibrary.org/obo/CHEBI_33696"},{"id":"A366","pred":"chebi_id","subj":"T366","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A367","pred":"chebi_id","subj":"T366","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A368","pred":"chebi_id","subj":"T366","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A369","pred":"chebi_id","subj":"T366","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A370","pred":"chebi_id","subj":"T366","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A371","pred":"chebi_id","subj":"T371","obj":"http://purl.obolibrary.org/obo/CHEBI_40574"},{"id":"A372","pred":"chebi_id","subj":"T371","obj":"http://purl.obolibrary.org/obo/CHEBI_46887"},{"id":"A373","pred":"chebi_id","subj":"T373","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A374","pred":"chebi_id","subj":"T373","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A375","pred":"chebi_id","subj":"T373","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A376","pred":"chebi_id","subj":"T373","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A377","pred":"chebi_id","subj":"T373","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A378","pred":"chebi_id","subj":"T378","obj":"http://purl.obolibrary.org/obo/CHEBI_40574"},{"id":"A379","pred":"chebi_id","subj":"T378","obj":"http://purl.obolibrary.org/obo/CHEBI_46887"},{"id":"A380","pred":"chebi_id","subj":"T380","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A381","pred":"chebi_id","subj":"T380","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A382","pred":"chebi_id","subj":"T380","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A383","pred":"chebi_id","subj":"T380","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A384","pred":"chebi_id","subj":"T380","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A385","pred":"chebi_id","subj":"T385","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A386","pred":"chebi_id","subj":"T386","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A387","pred":"chebi_id","subj":"T386","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A388","pred":"chebi_id","subj":"T386","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A389","pred":"chebi_id","subj":"T386","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A390","pred":"chebi_id","subj":"T386","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A391","pred":"chebi_id","subj":"T391","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A392","pred":"chebi_id","subj":"T391","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A393","pred":"chebi_id","subj":"T391","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A394","pred":"chebi_id","subj":"T391","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A395","pred":"chebi_id","subj":"T391","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"}],"text":"HE hemagglutinates and destroys receptors. As RNA viruses, CoVs bear RDEs, which are used in effective attachment to hosts and also reversely in detachment from the hosts. For example, enveloped RNA viruses evade the hosts via their RDEs. Currently, RDE-related functional enzymes such as neuraminidase (NA) and SA-O-acetyl-esterase are known. SA-O-acetyl-esterase was originally identified in influenza C virus and in nidoviruses (CoV and torovirus) as well as in salmon anemia virus (teleost orthomyxovirus). The origin and evolution of CoV SA-O-acetylesterases are correlated to other viruses. The fusion event of S glycoprotein and HE is specific for HCoV attachment to SA-associated receptors in the host [25]. The HE has acetylesterase activity [26]. In early SA-related biology, influenza A/B viruses were found to recognize chicken erythrocytes in 1942 [27]. They caused hemagglutination through clumping by virus-borne hemagglutinin. These phenomena were widely found in influenza viruses, paramyxoviruses, Newcastle disease (NDV) and mumps virus."}

{"project":"LitCovid-sentences","denotations":[{"id":"T172","span":{"begin":0,"end":42},"obj":"Sentence"},{"id":"T173","span":{"begin":43,"end":171},"obj":"Sentence"},{"id":"T174","span":{"begin":172,"end":238},"obj":"Sentence"},{"id":"T175","span":{"begin":239,"end":343},"obj":"Sentence"},{"id":"T176","span":{"begin":344,"end":510},"obj":"Sentence"},{"id":"T177","span":{"begin":511,"end":596},"obj":"Sentence"},{"id":"T178","span":{"begin":597,"end":715},"obj":"Sentence"},{"id":"T179","span":{"begin":716,"end":756},"obj":"Sentence"},{"id":"T180","span":{"begin":757,"end":866},"obj":"Sentence"},{"id":"T181","span":{"begin":867,"end":942},"obj":"Sentence"},{"id":"T182","span":{"begin":943,"end":1056},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"HE hemagglutinates and destroys receptors. As RNA viruses, CoVs bear RDEs, which are used in effective attachment to hosts and also reversely in detachment from the hosts. For example, enveloped RNA viruses evade the hosts via their RDEs. Currently, RDE-related functional enzymes such as neuraminidase (NA) and SA-O-acetyl-esterase are known. SA-O-acetyl-esterase was originally identified in influenza C virus and in nidoviruses (CoV and torovirus) as well as in salmon anemia virus (teleost orthomyxovirus). The origin and evolution of CoV SA-O-acetylesterases are correlated to other viruses. The fusion event of S glycoprotein and HE is specific for HCoV attachment to SA-associated receptors in the host [25]. The HE has acetylesterase activity [26]. In early SA-related biology, influenza A/B viruses were found to recognize chicken erythrocytes in 1942 [27]. They caused hemagglutination through clumping by virus-borne hemagglutinin. These phenomena were widely found in influenza viruses, paramyxoviruses, Newcastle disease (NDV) and mumps virus."}

{"project":"2_test","denotations":[{"id":"32604730-25926653-51943968","span":{"begin":752,"end":754},"obj":"25926653"},{"id":"32604730-19871229-51943969","span":{"begin":862,"end":864},"obj":"19871229"},{"id":"T97535","span":{"begin":752,"end":754},"obj":"25926653"},{"id":"T59612","span":{"begin":862,"end":864},"obj":"19871229"}],"text":"HE hemagglutinates and destroys receptors. As RNA viruses, CoVs bear RDEs, which are used in effective attachment to hosts and also reversely in detachment from the hosts. For example, enveloped RNA viruses evade the hosts via their RDEs. Currently, RDE-related functional enzymes such as neuraminidase (NA) and SA-O-acetyl-esterase are known. SA-O-acetyl-esterase was originally identified in influenza C virus and in nidoviruses (CoV and torovirus) as well as in salmon anemia virus (teleost orthomyxovirus). The origin and evolution of CoV SA-O-acetylesterases are correlated to other viruses. The fusion event of S glycoprotein and HE is specific for HCoV attachment to SA-associated receptors in the host [25]. The HE has acetylesterase activity [26]. In early SA-related biology, influenza A/B viruses were found to recognize chicken erythrocytes in 1942 [27]. They caused hemagglutination through clumping by virus-borne hemagglutinin. These phenomena were widely found in influenza viruses, paramyxoviruses, Newcastle disease (NDV) and mumps virus."}

{"project":"LitCovid-PD-HP","denotations":[{"id":"T6","span":{"begin":472,"end":478},"obj":"Phenotype"}],"attributes":[{"id":"A6","pred":"hp_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/HP_0001903"}],"text":"HE hemagglutinates and destroys receptors. As RNA viruses, CoVs bear RDEs, which are used in effective attachment to hosts and also reversely in detachment from the hosts. For example, enveloped RNA viruses evade the hosts via their RDEs. Currently, RDE-related functional enzymes such as neuraminidase (NA) and SA-O-acetyl-esterase are known. SA-O-acetyl-esterase was originally identified in influenza C virus and in nidoviruses (CoV and torovirus) as well as in salmon anemia virus (teleost orthomyxovirus). The origin and evolution of CoV SA-O-acetylesterases are correlated to other viruses. The fusion event of S glycoprotein and HE is specific for HCoV attachment to SA-associated receptors in the host [25]. The HE has acetylesterase activity [26]. In early SA-related biology, influenza A/B viruses were found to recognize chicken erythrocytes in 1942 [27]. They caused hemagglutination through clumping by virus-borne hemagglutinin. These phenomena were widely found in influenza viruses, paramyxoviruses, Newcastle disease (NDV) and mumps virus."}