PMC:7605337 / 6600-7287 JSONTXT

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T47","span":{"begin":26,"end":30},"obj":"Disease"},{"id":"T48","span":{"begin":119,"end":123},"obj":"Disease"},{"id":"T49","span":{"begin":177,"end":181},"obj":"Disease"},{"id":"T50","span":{"begin":265,"end":269},"obj":"Disease"},{"id":"T51","span":{"begin":337,"end":341},"obj":"Disease"},{"id":"T52","span":{"begin":385,"end":389},"obj":"Disease"},{"id":"T53","span":{"begin":606,"end":610},"obj":"Disease"}],"attributes":[{"id":"A47","pred":"mondo_id","subj":"T47","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A48","pred":"mondo_id","subj":"T48","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A49","pred":"mondo_id","subj":"T49","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A50","pred":"mondo_id","subj":"T50","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A51","pred":"mondo_id","subj":"T51","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A52","pred":"mondo_id","subj":"T52","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A53","pred":"mondo_id","subj":"T53","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Residues K479 and S487 in SARS-Civet are in close proximity with these hotspots and mutations at these residues caused SARS to bind ACE2 with significantly higher affinity than SARS-civet and played a major role in civet-to-human and human-to-human transmission of SARS coronavirus in 2002.3,13−15 Numerous mutations in the interface of SARS-COV RBD and ACE2 from different strains of SARS isolated from humans in 2002 have been identified and the effect of these mutations on binding ACE2 has been investigated by SPR.14,16 Two identified RBD mutations (Y442F and L472F) increased the binding affinity of SARS-COV to ACE2 and two mutations (N479K, T487S) decreased the binding affinity."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T61","span":{"begin":199,"end":200},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T62","span":{"begin":224,"end":229},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T63","span":{"begin":234,"end":239},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T64","span":{"begin":243,"end":248},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T65","span":{"begin":404,"end":410},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T66","span":{"begin":490,"end":493},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"}],"text":"Residues K479 and S487 in SARS-Civet are in close proximity with these hotspots and mutations at these residues caused SARS to bind ACE2 with significantly higher affinity than SARS-civet and played a major role in civet-to-human and human-to-human transmission of SARS coronavirus in 2002.3,13−15 Numerous mutations in the interface of SARS-COV RBD and ACE2 from different strains of SARS isolated from humans in 2002 have been identified and the effect of these mutations on binding ACE2 has been investigated by SPR.14,16 Two identified RBD mutations (Y442F and L472F) increased the binding affinity of SARS-COV to ACE2 and two mutations (N479K, T487S) decreased the binding affinity."}

{"project":"LitCovid-sentences","denotations":[{"id":"T37","span":{"begin":0,"end":687},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Residues K479 and S487 in SARS-Civet are in close proximity with these hotspots and mutations at these residues caused SARS to bind ACE2 with significantly higher affinity than SARS-civet and played a major role in civet-to-human and human-to-human transmission of SARS coronavirus in 2002.3,13−15 Numerous mutations in the interface of SARS-COV RBD and ACE2 from different strains of SARS isolated from humans in 2002 have been identified and the effect of these mutations on binding ACE2 has been investigated by SPR.14,16 Two identified RBD mutations (Y442F and L472F) increased the binding affinity of SARS-COV to ACE2 and two mutations (N479K, T487S) decreased the binding affinity."}

{"project":"LitCovid-PubTator","denotations":[{"id":"207","span":{"begin":132,"end":136},"obj":"Gene"},{"id":"208","span":{"begin":354,"end":358},"obj":"Gene"},{"id":"209","span":{"begin":485,"end":489},"obj":"Gene"},{"id":"210","span":{"begin":618,"end":622},"obj":"Gene"},{"id":"224","span":{"begin":224,"end":229},"obj":"Species"},{"id":"225","span":{"begin":234,"end":239},"obj":"Species"},{"id":"226","span":{"begin":243,"end":248},"obj":"Species"},{"id":"227","span":{"begin":265,"end":281},"obj":"Species"},{"id":"228","span":{"begin":337,"end":345},"obj":"Species"},{"id":"229","span":{"begin":404,"end":410},"obj":"Species"},{"id":"230","span":{"begin":606,"end":614},"obj":"Species"}],"attributes":[{"id":"A207","pred":"tao:has_database_id","subj":"207","obj":"Gene:59272"},{"id":"A208","pred":"tao:has_database_id","subj":"208","obj":"Gene:59272"},{"id":"A209","pred":"tao:has_database_id","subj":"209","obj":"Gene:59272"},{"id":"A210","pred":"tao:has_database_id","subj":"210","obj":"Gene:59272"},{"id":"A224","pred":"tao:has_database_id","subj":"224","obj":"Tax:9606"},{"id":"A225","pred":"tao:has_database_id","subj":"225","obj":"Tax:9606"},{"id":"A226","pred":"tao:has_database_id","subj":"226","obj":"Tax:9606"},{"id":"A227","pred":"tao:has_database_id","subj":"227","obj":"Tax:694009"},{"id":"A228","pred":"tao:has_database_id","subj":"228","obj":"Tax:694009"},{"id":"A229","pred":"tao:has_database_id","subj":"229","obj":"Tax:9606"},{"id":"A230","pred":"tao:has_database_id","subj":"230","obj":"Tax:694009"}],"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":"Residues K479 and S487 in SARS-Civet are in close proximity with these hotspots and mutations at these residues caused SARS to bind ACE2 with significantly higher affinity than SARS-civet and played a major role in civet-to-human and human-to-human transmission of SARS coronavirus in 2002.3,13−15 Numerous mutations in the interface of SARS-COV RBD and ACE2 from different strains of SARS isolated from humans in 2002 have been identified and the effect of these mutations on binding ACE2 has been investigated by SPR.14,16 Two identified RBD mutations (Y442F and L472F) increased the binding affinity of SARS-COV to ACE2 and two mutations (N479K, T487S) decreased the binding affinity."}