PMC:7091888 / 723-955 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"30","span":{"begin":116,"end":147},"obj":"Gene"},{"id":"31","span":{"begin":149,"end":153},"obj":"Gene"},{"id":"35","span":{"begin":43,"end":44},"obj":"Gene"},{"id":"41","span":{"begin":32,"end":42},"obj":"Species"},{"id":"42","span":{"begin":102,"end":107},"obj":"Species"},{"id":"43","span":{"begin":166,"end":176},"obj":"Species"}],"attributes":[{"id":"A30","pred":"tao:has_database_id","subj":"30","obj":"Gene:59272"},{"id":"A31","pred":"tao:has_database_id","subj":"31","obj":"Gene:59272"},{"id":"A35","pred":"tao:has_database_id","subj":"35","obj":"Gene:43740568"},{"id":"A41","pred":"tao:has_database_id","subj":"41","obj":"Tax:2697049"},{"id":"A42","pred":"tao:has_database_id","subj":"42","obj":"Tax:9606"},{"id":"A43","pred":"tao:has_database_id","subj":"43","obj":"Tax:2697049"}],"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":"eceptor-binding domain (RBD) in SARS-CoV-2 S protein and found that the RBD protein bound strongly to human and bat angiotensin-converting enzyme 2 (ACE2) receptors. SARS-CoV-2 RBD exhibited significantly higher binding affinity to "}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T3","span":{"begin":45,"end":52},"obj":"Body_part"},{"id":"T4","span":{"begin":76,"end":83},"obj":"Body_part"}],"attributes":[{"id":"A3","pred":"fma_id","subj":"T3","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A4","pred":"fma_id","subj":"T4","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"eceptor-binding domain (RBD) in SARS-CoV-2 S protein and found that the RBD protein bound strongly to human and bat angiotensin-converting enzyme 2 (ACE2) receptors. SARS-CoV-2 RBD exhibited significantly higher binding affinity to "}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T8","span":{"begin":32,"end":40},"obj":"Disease"},{"id":"T9","span":{"begin":32,"end":36},"obj":"Disease"},{"id":"T10","span":{"begin":166,"end":174},"obj":"Disease"},{"id":"T11","span":{"begin":166,"end":170},"obj":"Disease"}],"attributes":[{"id":"A8","pred":"mondo_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A9","pred":"mondo_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A10","pred":"mondo_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A11","pred":"mondo_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"eceptor-binding domain (RBD) in SARS-CoV-2 S protein and found that the RBD protein bound strongly to human and bat angiotensin-converting enzyme 2 (ACE2) receptors. SARS-CoV-2 RBD exhibited significantly higher binding affinity to "}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T5","span":{"begin":102,"end":107},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T6","span":{"begin":112,"end":115},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9397"}],"text":"eceptor-binding domain (RBD) in SARS-CoV-2 S protein and found that the RBD protein bound strongly to human and bat angiotensin-converting enzyme 2 (ACE2) receptors. SARS-CoV-2 RBD exhibited significantly higher binding affinity to "}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T5","span":{"begin":45,"end":52},"obj":"Chemical"},{"id":"T6","span":{"begin":76,"end":83},"obj":"Chemical"},{"id":"T7","span":{"begin":116,"end":127},"obj":"Chemical"}],"attributes":[{"id":"A5","pred":"chebi_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A6","pred":"chebi_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A7","pred":"chebi_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"}],"text":"eceptor-binding domain (RBD) in SARS-CoV-2 S protein and found that the RBD protein bound strongly to human and bat angiotensin-converting enzyme 2 (ACE2) receptors. SARS-CoV-2 RBD exhibited significantly higher binding affinity to "}