PMC:7029759 / 32756-33050 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"858","span":{"begin":108,"end":112},"obj":"Gene"},{"id":"859","span":{"begin":232,"end":236},"obj":"Gene"},{"id":"872","span":{"begin":58,"end":67},"obj":"Chemical"},{"id":"875","span":{"begin":202,"end":206},"obj":"Disease"}],"attributes":[{"id":"A858","pred":"tao:has_database_id","subj":"858","obj":"Gene:59272"},{"id":"A859","pred":"tao:has_database_id","subj":"859","obj":"Gene:59272"},{"id":"A872","pred":"tao:has_database_id","subj":"872","obj":"MESH:D006639"},{"id":"A875","pred":"tao:has_database_id","subj":"875","obj":"MESH:D045169"}],"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":"E2 and IgG1 fusion protein, which showed that mutation of histidine residues at position 374 and 378 of the ACE2 extracellular domain abolished peptidase activity, but retained high affinity binding to SARS S protein 56. Of course, ACE2 peptidase mutation would eliminate the beneficial effects"}

{"project":"LitCovid-PMC-OGER-BB","denotations":[{"id":"T420","span":{"begin":108,"end":112},"obj":"G_3;PG_10;PR:000003622"},{"id":"T419","span":{"begin":113,"end":126},"obj":"GO:0005576"},{"id":"T418","span":{"begin":127,"end":133},"obj":"SO:0000417"},{"id":"T417","span":{"begin":202,"end":206},"obj":"PR:000014459;SP_10;PG_9"},{"id":"T416","span":{"begin":207,"end":208},"obj":"PG_9;PG_1;PR:000005292"},{"id":"T415","span":{"begin":209,"end":216},"obj":"PG_1;PR:000005292"},{"id":"T414","span":{"begin":232,"end":236},"obj":"G_3;PG_10;PR:000003622"}],"text":"E2 and IgG1 fusion protein, which showed that mutation of histidine residues at position 374 and 378 of the ACE2 extracellular domain abolished peptidase activity, but retained high affinity binding to SARS S protein 56. Of course, ACE2 peptidase mutation would eliminate the beneficial effects"}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T211","span":{"begin":19,"end":26},"obj":"Body_part"},{"id":"T212","span":{"begin":58,"end":67},"obj":"Body_part"},{"id":"T213","span":{"begin":209,"end":216},"obj":"Body_part"}],"attributes":[{"id":"A211","pred":"fma_id","subj":"T211","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A212","pred":"fma_id","subj":"T212","obj":"http://purl.org/sig/ont/fma/fma82755"},{"id":"A213","pred":"fma_id","subj":"T213","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"E2 and IgG1 fusion protein, which showed that mutation of histidine residues at position 374 and 378 of the ACE2 extracellular domain abolished peptidase activity, but retained high affinity binding to SARS S protein 56. Of course, ACE2 peptidase mutation would eliminate the beneficial effects"}

{"project":"LitCovid_AGAC","denotations":[{"id":"p4596s33","span":{"begin":134,"end":143},"obj":"NegReg"},{"id":"p4596s34","span":{"begin":144,"end":153},"obj":"Enzyme"},{"id":"p4596s35","span":{"begin":154,"end":162},"obj":"MPA"},{"id":"p4596s39","span":{"begin":177,"end":181},"obj":"MPA"},{"id":"p4596s40","span":{"begin":182,"end":190},"obj":"MPA"},{"id":"p4596s41","span":{"begin":191,"end":198},"obj":"Interaction"}],"text":"E2 and IgG1 fusion protein, which showed that mutation of histidine residues at position 374 and 378 of the ACE2 extracellular domain abolished peptidase activity, but retained high affinity binding to SARS S protein 56. Of course, ACE2 peptidase mutation would eliminate the beneficial effects"}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T118","span":{"begin":202,"end":206},"obj":"Disease"}],"attributes":[{"id":"A118","pred":"mondo_id","subj":"T118","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"E2 and IgG1 fusion protein, which showed that mutation of histidine residues at position 374 and 378 of the ACE2 extracellular domain abolished peptidase activity, but retained high affinity binding to SARS S protein 56. Of course, ACE2 peptidase mutation would eliminate the beneficial effects"}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T339","span":{"begin":154,"end":162},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"}],"text":"E2 and IgG1 fusion protein, which showed that mutation of histidine residues at position 374 and 378 of the ACE2 extracellular domain abolished peptidase activity, but retained high affinity binding to SARS S protein 56. Of course, ACE2 peptidase mutation would eliminate the beneficial effects"}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T148","span":{"begin":19,"end":26},"obj":"Chemical"},{"id":"T149","span":{"begin":58,"end":67},"obj":"Chemical"},{"id":"T150","span":{"begin":209,"end":216},"obj":"Chemical"}],"attributes":[{"id":"A148","pred":"chebi_id","subj":"T148","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A149","pred":"chebi_id","subj":"T149","obj":"http://purl.obolibrary.org/obo/CHEBI_27570"},{"id":"A150","pred":"chebi_id","subj":"T150","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"E2 and IgG1 fusion protein, which showed that mutation of histidine residues at position 374 and 378 of the ACE2 extracellular domain abolished peptidase activity, but retained high affinity binding to SARS S protein 56. Of course, ACE2 peptidase mutation would eliminate the beneficial effects"}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T21","span":{"begin":144,"end":162},"obj":"http://purl.obolibrary.org/obo/GO_0008233"}],"text":"E2 and IgG1 fusion protein, which showed that mutation of histidine residues at position 374 and 378 of the ACE2 extracellular domain abolished peptidase activity, but retained high affinity binding to SARS S protein 56. Of course, ACE2 peptidase mutation would eliminate the beneficial effects"}