PubMed:33122196 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T1","span":{"begin":42,"end":49},"obj":"Body_part"},{"id":"T2","span":{"begin":530,"end":537},"obj":"Body_part"},{"id":"T3","span":{"begin":661,"end":668},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"fma_id","subj":"T1","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A2","pred":"fma_id","subj":"T2","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A3","pred":"fma_id","subj":"T3","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity.\nThe novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T1","span":{"begin":25,"end":33},"obj":"Disease"},{"id":"T2","span":{"begin":101,"end":134},"obj":"Disease"},{"id":"T3","span":{"begin":148,"end":156},"obj":"Disease"},{"id":"T4","span":{"begin":311,"end":319},"obj":"Disease"},{"id":"T5","span":{"begin":513,"end":521},"obj":"Disease"},{"id":"T6","span":{"begin":635,"end":643},"obj":"Disease"},{"id":"T7","span":{"begin":875,"end":883},"obj":"Disease"},{"id":"T8","span":{"begin":948,"end":956},"obj":"Disease"},{"id":"T9","span":{"begin":959,"end":968},"obj":"Disease"},{"id":"T10","span":{"begin":1064,"end":1072},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A7","pred":"mondo_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"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_0005550"},{"id":"A10","pred":"mondo_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity.\nThe novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T1","span":{"begin":81,"end":89},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T2","span":{"begin":160,"end":163},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T3","span":{"begin":175,"end":176},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T4","span":{"begin":226,"end":231},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T5","span":{"begin":326,"end":327},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T6","span":{"begin":603,"end":611},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T7","span":{"begin":696,"end":704},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T8","span":{"begin":730,"end":737},"obj":"http://purl.obolibrary.org/obo/PR_000018263"},{"id":"T9","span":{"begin":985,"end":993},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"}],"text":"High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity.\nThe novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T1","span":{"begin":42,"end":49},"obj":"Chemical"},{"id":"T2","span":{"begin":232,"end":243},"obj":"Chemical"},{"id":"T3","span":{"begin":394,"end":408},"obj":"Chemical"},{"id":"T6","span":{"begin":394,"end":405},"obj":"Chemical"},{"id":"T7","span":{"begin":406,"end":408},"obj":"Chemical"},{"id":"T8","span":{"begin":530,"end":537},"obj":"Chemical"},{"id":"T9","span":{"begin":661,"end":668},"obj":"Chemical"},{"id":"T10","span":{"begin":730,"end":737},"obj":"Chemical"}],"attributes":[{"id":"A1","pred":"chebi_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A2","pred":"chebi_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A3","pred":"chebi_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CHEBI_2719"},{"id":"A4","pred":"chebi_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CHEBI_48432"},{"id":"A5","pred":"chebi_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CHEBI_58506"},{"id":"A6","pred":"chebi_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A7","pred":"chebi_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CHEBI_74067"},{"id":"A8","pred":"chebi_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A9","pred":"chebi_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A10","pred":"chebi_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/CHEBI_16670"}],"text":"High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity.\nThe novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T1","span":{"begin":64,"end":89},"obj":"http://purl.obolibrary.org/obo/GO_0004180"},{"id":"T2","span":{"begin":420,"end":434},"obj":"http://purl.obolibrary.org/obo/GO_0042311"}],"text":"High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity.\nThe novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19."}

{"project":"LitCovid-PubTator","denotations":[{"id":"3","span":{"begin":25,"end":35},"obj":"Species"},{"id":"4","span":{"begin":36,"end":41},"obj":"Gene"},{"id":"5","span":{"begin":59,"end":63},"obj":"Gene"},{"id":"30","span":{"begin":101,"end":146},"obj":"Species"},{"id":"31","span":{"begin":148,"end":158},"obj":"Species"},{"id":"32","span":{"begin":226,"end":231},"obj":"Species"},{"id":"33","span":{"begin":232,"end":263},"obj":"Gene"},{"id":"34","span":{"begin":264,"end":268},"obj":"Gene"},{"id":"35","span":{"begin":311,"end":321},"obj":"Species"},{"id":"36","span":{"begin":346,"end":350},"obj":"Gene"},{"id":"37","span":{"begin":394,"end":408},"obj":"Gene"},{"id":"38","span":{"begin":504,"end":508},"obj":"Gene"},{"id":"39","span":{"begin":513,"end":523},"obj":"Species"},{"id":"40","span":{"begin":524,"end":529},"obj":"Gene"},{"id":"41","span":{"begin":615,"end":619},"obj":"Gene"},{"id":"42","span":{"begin":635,"end":645},"obj":"Species"},{"id":"43","span":{"begin":655,"end":660},"obj":"Gene"},{"id":"44","span":{"begin":679,"end":683},"obj":"Gene"},{"id":"45","span":{"begin":758,"end":767},"obj":"Gene"},{"id":"46","span":{"begin":782,"end":792},"obj":"Gene"},{"id":"47","span":{"begin":820,"end":824},"obj":"Gene"},{"id":"48","span":{"begin":875,"end":885},"obj":"Species"},{"id":"49","span":{"begin":886,"end":891},"obj":"Gene"},{"id":"50","span":{"begin":948,"end":968},"obj":"Disease"},{"id":"51","span":{"begin":980,"end":984},"obj":"Gene"},{"id":"52","span":{"begin":1024,"end":1047},"obj":"Disease"},{"id":"53","span":{"begin":1064,"end":1072},"obj":"Disease"}],"attributes":[{"id":"A3","pred":"tao:has_database_id","subj":"3","obj":"Tax:2697049"},{"id":"A4","pred":"tao:has_database_id","subj":"4","obj":"Gene:43740568"},{"id":"A5","pred":"tao:has_database_id","subj":"5","obj":"Gene:59272"},{"id":"A30","pred":"tao:has_database_id","subj":"30","obj":"Tax:694009"},{"id":"A31","pred":"tao:has_database_id","subj":"31","obj":"Tax:2697049"},{"id":"A32","pred":"tao:has_database_id","subj":"32","obj":"Tax:9606"},{"id":"A33","pred":"tao:has_database_id","subj":"33","obj":"Gene:59272"},{"id":"A34","pred":"tao:has_database_id","subj":"34","obj":"Gene:59272"},{"id":"A35","pred":"tao:has_database_id","subj":"35","obj":"Tax:2697049"},{"id":"A36","pred":"tao:has_database_id","subj":"36","obj":"Gene:59272"},{"id":"A37","pred":"tao:has_database_id","subj":"37","obj":"Gene:183"},{"id":"A38","pred":"tao:has_database_id","subj":"38","obj":"Gene:59272"},{"id":"A39","pred":"tao:has_database_id","subj":"39","obj":"Tax:2697049"},{"id":"A40","pred":"tao:has_database_id","subj":"40","obj":"Gene:43740568"},{"id":"A41","pred":"tao:has_database_id","subj":"41","obj":"Gene:59272"},{"id":"A42","pred":"tao:has_database_id","subj":"42","obj":"Tax:2697049"},{"id":"A43","pred":"tao:has_database_id","subj":"43","obj":"Gene:43740568"},{"id":"A44","pred":"tao:has_database_id","subj":"44","obj":"Gene:59272"},{"id":"A45","pred":"tao:has_database_id","subj":"45","obj":"Gene:834"},{"id":"A46","pred":"tao:has_database_id","subj":"46","obj":"Gene:3827"},{"id":"A47","pred":"tao:has_database_id","subj":"47","obj":"Gene:59272"},{"id":"A48","pred":"tao:has_database_id","subj":"48","obj":"Tax:2697049"},{"id":"A49","pred":"tao:has_database_id","subj":"49","obj":"Gene:43740568"},{"id":"A50","pred":"tao:has_database_id","subj":"50","obj":"MESH:C000657245"},{"id":"A51","pred":"tao:has_database_id","subj":"51","obj":"Gene:59272"},{"id":"A52","pred":"tao:has_database_id","subj":"52","obj":"MESH:D051271"},{"id":"A53","pred":"tao:has_database_id","subj":"53","obj":"MESH:C000657245"}],"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":"High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity.\nThe novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19."}

{"project":"LitCovid-sentences","denotations":[{"id":"T1","span":{"begin":0,"end":90},"obj":"Sentence"},{"id":"T2","span":{"begin":91,"end":225},"obj":"Sentence"},{"id":"T3","span":{"begin":226,"end":322},"obj":"Sentence"},{"id":"T4","span":{"begin":323,"end":461},"obj":"Sentence"},{"id":"T5","span":{"begin":462,"end":620},"obj":"Sentence"},{"id":"T6","span":{"begin":621,"end":800},"obj":"Sentence"},{"id":"T7","span":{"begin":801,"end":903},"obj":"Sentence"},{"id":"T8","span":{"begin":904,"end":1073},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity.\nThe novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19."}

{"project":"LitCovid_AGAC_only","denotations":[{"id":"p261841s11","span":{"begin":50,"end":58},"obj":"PosReg"},{"id":"p261841s12","span":{"begin":59,"end":80},"obj":"MPA"},{"id":"p261841s14","span":{"begin":81,"end":89},"obj":"MPA"},{"id":"p261846s10","span":{"begin":669,"end":678},"obj":"PosReg"},{"id":"p261846s11","span":{"begin":679,"end":704},"obj":"MPA"}],"text":"High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity.\nThe novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":90},"obj":"Sentence"},{"id":"T2","span":{"begin":91,"end":225},"obj":"Sentence"},{"id":"T3","span":{"begin":226,"end":322},"obj":"Sentence"},{"id":"T4","span":{"begin":323,"end":461},"obj":"Sentence"},{"id":"T5","span":{"begin":462,"end":620},"obj":"Sentence"},{"id":"T6","span":{"begin":621,"end":800},"obj":"Sentence"},{"id":"T7","span":{"begin":801,"end":903},"obj":"Sentence"},{"id":"T8","span":{"begin":904,"end":1073},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity.\nThe novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":25,"end":35},"obj":"Disease"},{"id":"T2","span":{"begin":101,"end":134},"obj":"Disease"},{"id":"T3","span":{"begin":148,"end":158},"obj":"Disease"},{"id":"T4","span":{"begin":311,"end":321},"obj":"Disease"},{"id":"T5","span":{"begin":513,"end":523},"obj":"Disease"},{"id":"T6","span":{"begin":635,"end":645},"obj":"Disease"},{"id":"T7","span":{"begin":875,"end":885},"obj":"Disease"},{"id":"T8","span":{"begin":948,"end":958},"obj":"Disease"},{"id":"T9","span":{"begin":959,"end":968},"obj":"Disease"},{"id":"T10","span":{"begin":1064,"end":1072},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A7","pred":"mondo_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A8","pred":"mondo_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A9","pred":"mondo_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A10","pred":"mondo_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity.\nThe novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":892,"end":895},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:5200291"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity.\nThe novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":25,"end":33},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":101,"end":134},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":148,"end":156},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":226,"end":231},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":311,"end":319},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":513,"end":521},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":635,"end":643},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":875,"end":883},"obj":"OrganismTaxon"},{"id":"T9","span":{"begin":948,"end":956},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"694009"},{"id":"A2","pred":"db_id","subj":"T2","obj":"694009"},{"id":"A3","pred":"db_id","subj":"T3","obj":"694009"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"},{"id":"A5","pred":"db_id","subj":"T5","obj":"694009"},{"id":"A6","pred":"db_id","subj":"T6","obj":"694009"},{"id":"A7","pred":"db_id","subj":"T7","obj":"694009"},{"id":"A8","pred":"db_id","subj":"T8","obj":"694009"},{"id":"A9","pred":"db_id","subj":"T9","obj":"694009"}],"text":"High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity.\nThe novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19."}