PMC:7161517 / 4687-5889 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T9","span":{"begin":35,"end":47},"obj":"Body_part"},{"id":"T10","span":{"begin":84,"end":92},"obj":"Body_part"},{"id":"T11","span":{"begin":94,"end":109},"obj":"Body_part"},{"id":"T12","span":{"begin":111,"end":116},"obj":"Body_part"},{"id":"T13","span":{"begin":118,"end":129},"obj":"Body_part"},{"id":"T14","span":{"begin":131,"end":138},"obj":"Body_part"},{"id":"T15","span":{"begin":140,"end":148},"obj":"Body_part"},{"id":"T16","span":{"begin":154,"end":169},"obj":"Body_part"},{"id":"T17","span":{"begin":538,"end":551},"obj":"Body_part"},{"id":"T18","span":{"begin":773,"end":780},"obj":"Body_part"},{"id":"T19","span":{"begin":801,"end":811},"obj":"Body_part"},{"id":"T20","span":{"begin":834,"end":843},"obj":"Body_part"},{"id":"T21","span":{"begin":852,"end":858},"obj":"Body_part"},{"id":"T22","span":{"begin":1119,"end":1129},"obj":"Body_part"},{"id":"T23","span":{"begin":1144,"end":1155},"obj":"Body_part"}],"attributes":[{"id":"A9","pred":"fma_id","subj":"T9","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A10","pred":"fma_id","subj":"T10","obj":"http://purl.org/sig/ont/fma/fma7409"},{"id":"A11","pred":"fma_id","subj":"T11","obj":"http://purl.org/sig/ont/fma/fma27360"},{"id":"A12","pred":"fma_id","subj":"T12","obj":"http://purl.org/sig/ont/fma/fma7088"},{"id":"A13","pred":"fma_id","subj":"T13","obj":"http://purl.org/sig/ont/fma/fma63916"},{"id":"A14","pred":"fma_id","subj":"T14","obj":"http://purl.org/sig/ont/fma/fma7203"},{"id":"A15","pred":"fma_id","subj":"T15","obj":"http://purl.org/sig/ont/fma/fma7206"},{"id":"A16","pred":"fma_id","subj":"T16","obj":"http://purl.org/sig/ont/fma/fma7200"},{"id":"A17","pred":"fma_id","subj":"T17","obj":"http://purl.org/sig/ont/fma/fma82754"},{"id":"A18","pred":"fma_id","subj":"T18","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A19","pred":"fma_id","subj":"T19","obj":"http://purl.org/sig/ont/fma/fma82739"},{"id":"A20","pred":"fma_id","subj":"T20","obj":"http://purl.org/sig/ont/fma/fma7199"},{"id":"A21","pred":"fma_id","subj":"T21","obj":"http://purl.org/sig/ont/fma/fma7203"},{"id":"A22","pred":"fma_id","subj":"T22","obj":"http://purl.org/sig/ont/fma/fma62343"},{"id":"A23","pred":"fma_id","subj":"T23","obj":"http://purl.org/sig/ont/fma/fma66835"}],"text":"ACE2 is a type I integral membrane glycoprotein (15) expressed predominantly in the bronchus, lung parenchyma, heart, endothelium, kidneys, duodenum, and small intestine (16). ACE2 is a monocarboxypeptidase, unlike its homolog, ACE, which is a dipeptidase; ACE2 is not antagonized by ACE inhibitors (17). Although ACE contains 2 active catalytic domains, ACE2 has a single catalytic domain with 42% identical residues (18,19). The major substrate of ACE2 is Ang II, which upon C-terminus cleavage, produces angiotensin 1-7 (Ang1-7) and L-phenylalanine (20). Other substrates for ACE2 include Ang I, apelin-13, and dynorphin-13, which are catalyzed at much lower affinities (21). The non-catalytic C-terminal domain of ACE2 shares a 48% sequence homology with collectrin, a protein involved in neutral amino acid reabsorption from the intestine and the kidney (22,23). In the presence of a disintegrin and metalloproteinase 17 (ADAM17), also known as tumor necrosis factor (TNF)-α−converting enzyme (TACE), ACE2 exhibits ectodomain shedding (24), which results in the formation of a soluble enzyme. ACE2 also contains a calmodulin domain on its cytoplasmic tail that influences ectodomain shedding (25)."}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T16","span":{"begin":84,"end":92},"obj":"Body_part"},{"id":"T17","span":{"begin":94,"end":109},"obj":"Body_part"},{"id":"T18","span":{"begin":94,"end":98},"obj":"Body_part"},{"id":"T19","span":{"begin":99,"end":109},"obj":"Body_part"},{"id":"T20","span":{"begin":111,"end":129},"obj":"Body_part"},{"id":"T21","span":{"begin":111,"end":116},"obj":"Body_part"},{"id":"T22","span":{"begin":118,"end":129},"obj":"Body_part"},{"id":"T23","span":{"begin":140,"end":148},"obj":"Body_part"},{"id":"T24","span":{"begin":154,"end":169},"obj":"Body_part"},{"id":"T25","span":{"begin":160,"end":169},"obj":"Body_part"},{"id":"T26","span":{"begin":834,"end":843},"obj":"Body_part"},{"id":"T27","span":{"begin":852,"end":858},"obj":"Body_part"},{"id":"T28","span":{"begin":1156,"end":1160},"obj":"Body_part"}],"attributes":[{"id":"A16","pred":"uberon_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/UBERON_0002185"},{"id":"A17","pred":"uberon_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/UBERON_0008946"},{"id":"A18","pred":"uberon_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"},{"id":"A19","pred":"uberon_id","subj":"T19","obj":"http://purl.obolibrary.org/obo/UBERON_0000353"},{"id":"A20","pred":"uberon_id","subj":"T20","obj":"http://purl.obolibrary.org/obo/UBERON_0008307"},{"id":"A21","pred":"uberon_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/UBERON_0000948"},{"id":"A22","pred":"uberon_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/UBERON_0001986"},{"id":"A23","pred":"uberon_id","subj":"T23","obj":"http://purl.obolibrary.org/obo/UBERON_0002114"},{"id":"A24","pred":"uberon_id","subj":"T24","obj":"http://purl.obolibrary.org/obo/UBERON_0002108"},{"id":"A25","pred":"uberon_id","subj":"T25","obj":"http://purl.obolibrary.org/obo/UBERON_0000160"},{"id":"A26","pred":"uberon_id","subj":"T26","obj":"http://purl.obolibrary.org/obo/UBERON_0000160"},{"id":"A27","pred":"uberon_id","subj":"T27","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A28","pred":"uberon_id","subj":"T28","obj":"http://purl.obolibrary.org/obo/UBERON_0002415"}],"text":"ACE2 is a type I integral membrane glycoprotein (15) expressed predominantly in the bronchus, lung parenchyma, heart, endothelium, kidneys, duodenum, and small intestine (16). ACE2 is a monocarboxypeptidase, unlike its homolog, ACE, which is a dipeptidase; ACE2 is not antagonized by ACE inhibitors (17). Although ACE contains 2 active catalytic domains, ACE2 has a single catalytic domain with 42% identical residues (18,19). The major substrate of ACE2 is Ang II, which upon C-terminus cleavage, produces angiotensin 1-7 (Ang1-7) and L-phenylalanine (20). Other substrates for ACE2 include Ang I, apelin-13, and dynorphin-13, which are catalyzed at much lower affinities (21). The non-catalytic C-terminal domain of ACE2 shares a 48% sequence homology with collectrin, a protein involved in neutral amino acid reabsorption from the intestine and the kidney (22,23). In the presence of a disintegrin and metalloproteinase 17 (ADAM17), also known as tumor necrosis factor (TNF)-α−converting enzyme (TACE), ACE2 exhibits ectodomain shedding (24), which results in the formation of a soluble enzyme. ACE2 also contains a calmodulin domain on its cytoplasmic tail that influences ectodomain shedding (25)."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T40","span":{"begin":950,"end":955},"obj":"Disease"}],"attributes":[{"id":"A40","pred":"mondo_id","subj":"T40","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"}],"text":"ACE2 is a type I integral membrane glycoprotein (15) expressed predominantly in the bronchus, lung parenchyma, heart, endothelium, kidneys, duodenum, and small intestine (16). ACE2 is a monocarboxypeptidase, unlike its homolog, ACE, which is a dipeptidase; ACE2 is not antagonized by ACE inhibitors (17). Although ACE contains 2 active catalytic domains, ACE2 has a single catalytic domain with 42% identical residues (18,19). The major substrate of ACE2 is Ang II, which upon C-terminus cleavage, produces angiotensin 1-7 (Ang1-7) and L-phenylalanine (20). Other substrates for ACE2 include Ang I, apelin-13, and dynorphin-13, which are catalyzed at much lower affinities (21). The non-catalytic C-terminal domain of ACE2 shares a 48% sequence homology with collectrin, a protein involved in neutral amino acid reabsorption from the intestine and the kidney (22,23). In the presence of a disintegrin and metalloproteinase 17 (ADAM17), also known as tumor necrosis factor (TNF)-α−converting enzyme (TACE), ACE2 exhibits ectodomain shedding (24), which results in the formation of a soluble enzyme. ACE2 also contains a calmodulin domain on its cytoplasmic tail that influences ectodomain shedding (25)."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T31","span":{"begin":8,"end":9},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T32","span":{"begin":26,"end":34},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T33","span":{"begin":84,"end":92},"obj":"http://purl.obolibrary.org/obo/UBERON_0002185"},{"id":"T34","span":{"begin":94,"end":98},"obj":"http://purl.obolibrary.org/obo/UBERON_0002048"},{"id":"T35","span":{"begin":94,"end":98},"obj":"http://www.ebi.ac.uk/efo/EFO_0000934"},{"id":"T36","span":{"begin":111,"end":116},"obj":"http://purl.obolibrary.org/obo/UBERON_0000948"},{"id":"T37","span":{"begin":111,"end":116},"obj":"http://purl.obolibrary.org/obo/UBERON_0007100"},{"id":"T38","span":{"begin":111,"end":116},"obj":"http://purl.obolibrary.org/obo/UBERON_0015228"},{"id":"T39","span":{"begin":111,"end":116},"obj":"http://www.ebi.ac.uk/efo/EFO_0000815"},{"id":"T40","span":{"begin":118,"end":129},"obj":"http://purl.obolibrary.org/obo/UBERON_0001986"},{"id":"T41","span":{"begin":131,"end":138},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"T42","span":{"begin":131,"end":138},"obj":"http://www.ebi.ac.uk/efo/EFO_0000927"},{"id":"T43","span":{"begin":131,"end":138},"obj":"http://www.ebi.ac.uk/efo/EFO_0000929"},{"id":"T44","span":{"begin":154,"end":169},"obj":"http://purl.obolibrary.org/obo/UBERON_0002108"},{"id":"T45","span":{"begin":184,"end":185},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T46","span":{"begin":242,"end":243},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T47","span":{"begin":329,"end":335},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T48","span":{"begin":360,"end":363},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T49","span":{"begin":364,"end":365},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T50","span":{"begin":730,"end":731},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T51","span":{"begin":732,"end":734},"obj":"http://purl.obolibrary.org/obo/CLO_0001382"},{"id":"T52","span":{"begin":771,"end":772},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T53","span":{"begin":834,"end":843},"obj":"http://purl.obolibrary.org/obo/UBERON_0000160"},{"id":"T54","span":{"begin":834,"end":843},"obj":"http://www.ebi.ac.uk/efo/EFO_0000834"},{"id":"T55","span":{"begin":852,"end":858},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"T56","span":{"begin":852,"end":858},"obj":"http://www.ebi.ac.uk/efo/EFO_0000927"},{"id":"T57","span":{"begin":852,"end":858},"obj":"http://www.ebi.ac.uk/efo/EFO_0000929"},{"id":"T58","span":{"begin":887,"end":888},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T59","span":{"begin":1080,"end":1081},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T60","span":{"begin":1117,"end":1118},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T61","span":{"begin":1156,"end":1160},"obj":"http://purl.obolibrary.org/obo/UBERON_0002415"}],"text":"ACE2 is a type I integral membrane glycoprotein (15) expressed predominantly in the bronchus, lung parenchyma, heart, endothelium, kidneys, duodenum, and small intestine (16). ACE2 is a monocarboxypeptidase, unlike its homolog, ACE, which is a dipeptidase; ACE2 is not antagonized by ACE inhibitors (17). Although ACE contains 2 active catalytic domains, ACE2 has a single catalytic domain with 42% identical residues (18,19). The major substrate of ACE2 is Ang II, which upon C-terminus cleavage, produces angiotensin 1-7 (Ang1-7) and L-phenylalanine (20). Other substrates for ACE2 include Ang I, apelin-13, and dynorphin-13, which are catalyzed at much lower affinities (21). The non-catalytic C-terminal domain of ACE2 shares a 48% sequence homology with collectrin, a protein involved in neutral amino acid reabsorption from the intestine and the kidney (22,23). In the presence of a disintegrin and metalloproteinase 17 (ADAM17), also known as tumor necrosis factor (TNF)-α−converting enzyme (TACE), ACE2 exhibits ectodomain shedding (24), which results in the formation of a soluble enzyme. ACE2 also contains a calmodulin domain on its cytoplasmic tail that influences ectodomain shedding (25)."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T51","span":{"begin":35,"end":47},"obj":"Chemical"},{"id":"T52","span":{"begin":284,"end":298},"obj":"Chemical"},{"id":"T53","span":{"begin":288,"end":298},"obj":"Chemical"},{"id":"T54","span":{"begin":462,"end":464},"obj":"Chemical"},{"id":"T55","span":{"begin":507,"end":518},"obj":"Chemical"},{"id":"T56","span":{"begin":536,"end":551},"obj":"Chemical"},{"id":"T59","span":{"begin":538,"end":551},"obj":"Chemical"},{"id":"T60","span":{"begin":773,"end":780},"obj":"Chemical"},{"id":"T61","span":{"begin":801,"end":811},"obj":"Chemical"},{"id":"T62","span":{"begin":801,"end":806},"obj":"Chemical"},{"id":"T63","span":{"begin":807,"end":811},"obj":"Chemical"}],"attributes":[{"id":"A51","pred":"chebi_id","subj":"T51","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A52","pred":"chebi_id","subj":"T52","obj":"http://purl.obolibrary.org/obo/CHEBI_35457"},{"id":"A53","pred":"chebi_id","subj":"T53","obj":"http://purl.obolibrary.org/obo/CHEBI_35222"},{"id":"A54","pred":"chebi_id","subj":"T54","obj":"http://purl.obolibrary.org/obo/CHEBI_74067"},{"id":"A55","pred":"chebi_id","subj":"T55","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A56","pred":"chebi_id","subj":"T56","obj":"http://purl.obolibrary.org/obo/CHEBI_17295"},{"id":"A57","pred":"chebi_id","subj":"T56","obj":"http://purl.obolibrary.org/obo/CHEBI_29997"},{"id":"A58","pred":"chebi_id","subj":"T56","obj":"http://purl.obolibrary.org/obo/CHEBI_58095"},{"id":"A59","pred":"chebi_id","subj":"T59","obj":"http://purl.obolibrary.org/obo/CHEBI_28044"},{"id":"A60","pred":"chebi_id","subj":"T60","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A61","pred":"chebi_id","subj":"T61","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"},{"id":"A62","pred":"chebi_id","subj":"T62","obj":"http://purl.obolibrary.org/obo/CHEBI_46882"},{"id":"A63","pred":"chebi_id","subj":"T63","obj":"http://purl.obolibrary.org/obo/CHEBI_37527"}],"text":"ACE2 is a type I integral membrane glycoprotein (15) expressed predominantly in the bronchus, lung parenchyma, heart, endothelium, kidneys, duodenum, and small intestine (16). ACE2 is a monocarboxypeptidase, unlike its homolog, ACE, which is a dipeptidase; ACE2 is not antagonized by ACE inhibitors (17). Although ACE contains 2 active catalytic domains, ACE2 has a single catalytic domain with 42% identical residues (18,19). The major substrate of ACE2 is Ang II, which upon C-terminus cleavage, produces angiotensin 1-7 (Ang1-7) and L-phenylalanine (20). Other substrates for ACE2 include Ang I, apelin-13, and dynorphin-13, which are catalyzed at much lower affinities (21). The non-catalytic C-terminal domain of ACE2 shares a 48% sequence homology with collectrin, a protein involved in neutral amino acid reabsorption from the intestine and the kidney (22,23). In the presence of a disintegrin and metalloproteinase 17 (ADAM17), also known as tumor necrosis factor (TNF)-α−converting enzyme (TACE), ACE2 exhibits ectodomain shedding (24), which results in the formation of a soluble enzyme. ACE2 also contains a calmodulin domain on its cytoplasmic tail that influences ectodomain shedding (25)."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T14","span":{"begin":956,"end":964},"obj":"http://purl.obolibrary.org/obo/GO_0070265"},{"id":"T15","span":{"begin":956,"end":964},"obj":"http://purl.obolibrary.org/obo/GO_0019835"},{"id":"T16","span":{"begin":956,"end":964},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T17","span":{"begin":956,"end":964},"obj":"http://purl.obolibrary.org/obo/GO_0001906"},{"id":"T18","span":{"begin":1067,"end":1076},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"ACE2 is a type I integral membrane glycoprotein (15) expressed predominantly in the bronchus, lung parenchyma, heart, endothelium, kidneys, duodenum, and small intestine (16). ACE2 is a monocarboxypeptidase, unlike its homolog, ACE, which is a dipeptidase; ACE2 is not antagonized by ACE inhibitors (17). Although ACE contains 2 active catalytic domains, ACE2 has a single catalytic domain with 42% identical residues (18,19). The major substrate of ACE2 is Ang II, which upon C-terminus cleavage, produces angiotensin 1-7 (Ang1-7) and L-phenylalanine (20). Other substrates for ACE2 include Ang I, apelin-13, and dynorphin-13, which are catalyzed at much lower affinities (21). The non-catalytic C-terminal domain of ACE2 shares a 48% sequence homology with collectrin, a protein involved in neutral amino acid reabsorption from the intestine and the kidney (22,23). In the presence of a disintegrin and metalloproteinase 17 (ADAM17), also known as tumor necrosis factor (TNF)-α−converting enzyme (TACE), ACE2 exhibits ectodomain shedding (24), which results in the formation of a soluble enzyme. ACE2 also contains a calmodulin domain on its cytoplasmic tail that influences ectodomain shedding (25)."}

{"project":"LitCovid-sentences","denotations":[{"id":"T34","span":{"begin":0,"end":175},"obj":"Sentence"},{"id":"T35","span":{"begin":176,"end":304},"obj":"Sentence"},{"id":"T36","span":{"begin":305,"end":426},"obj":"Sentence"},{"id":"T37","span":{"begin":427,"end":557},"obj":"Sentence"},{"id":"T38","span":{"begin":558,"end":678},"obj":"Sentence"},{"id":"T39","span":{"begin":679,"end":867},"obj":"Sentence"},{"id":"T40","span":{"begin":868,"end":1097},"obj":"Sentence"},{"id":"T41","span":{"begin":1098,"end":1202},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"ACE2 is a type I integral membrane glycoprotein (15) expressed predominantly in the bronchus, lung parenchyma, heart, endothelium, kidneys, duodenum, and small intestine (16). ACE2 is a monocarboxypeptidase, unlike its homolog, ACE, which is a dipeptidase; ACE2 is not antagonized by ACE inhibitors (17). Although ACE contains 2 active catalytic domains, ACE2 has a single catalytic domain with 42% identical residues (18,19). The major substrate of ACE2 is Ang II, which upon C-terminus cleavage, produces angiotensin 1-7 (Ang1-7) and L-phenylalanine (20). Other substrates for ACE2 include Ang I, apelin-13, and dynorphin-13, which are catalyzed at much lower affinities (21). The non-catalytic C-terminal domain of ACE2 shares a 48% sequence homology with collectrin, a protein involved in neutral amino acid reabsorption from the intestine and the kidney (22,23). In the presence of a disintegrin and metalloproteinase 17 (ADAM17), also known as tumor necrosis factor (TNF)-α−converting enzyme (TACE), ACE2 exhibits ectodomain shedding (24), which results in the formation of a soluble enzyme. ACE2 also contains a calmodulin domain on its cytoplasmic tail that influences ectodomain shedding (25)."}

{"project":"LitCovid-PD-HP","denotations":[{"id":"T7","span":{"begin":950,"end":955},"obj":"Phenotype"}],"attributes":[{"id":"A7","pred":"hp_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/HP_0002664"}],"text":"ACE2 is a type I integral membrane glycoprotein (15) expressed predominantly in the bronchus, lung parenchyma, heart, endothelium, kidneys, duodenum, and small intestine (16). ACE2 is a monocarboxypeptidase, unlike its homolog, ACE, which is a dipeptidase; ACE2 is not antagonized by ACE inhibitors (17). Although ACE contains 2 active catalytic domains, ACE2 has a single catalytic domain with 42% identical residues (18,19). The major substrate of ACE2 is Ang II, which upon C-terminus cleavage, produces angiotensin 1-7 (Ang1-7) and L-phenylalanine (20). Other substrates for ACE2 include Ang I, apelin-13, and dynorphin-13, which are catalyzed at much lower affinities (21). The non-catalytic C-terminal domain of ACE2 shares a 48% sequence homology with collectrin, a protein involved in neutral amino acid reabsorption from the intestine and the kidney (22,23). In the presence of a disintegrin and metalloproteinase 17 (ADAM17), also known as tumor necrosis factor (TNF)-α−converting enzyme (TACE), ACE2 exhibits ectodomain shedding (24), which results in the formation of a soluble enzyme. ACE2 also contains a calmodulin domain on its cytoplasmic tail that influences ectodomain shedding (25)."}

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is a type I integral membrane glycoprotein (15) expressed predominantly in the bronchus, lung parenchyma, heart, endothelium, kidneys, duodenum, and small intestine (16). ACE2 is a monocarboxypeptidase, unlike its homolog, ACE, which is a dipeptidase; ACE2 is not antagonized by ACE inhibitors (17). Although ACE contains 2 active catalytic domains, ACE2 has a single catalytic domain with 42% identical residues (18,19). The major substrate of ACE2 is Ang II, which upon C-terminus cleavage, produces angiotensin 1-7 (Ang1-7) and L-phenylalanine (20). Other substrates for ACE2 include Ang I, apelin-13, and dynorphin-13, which are catalyzed at much lower affinities (21). The non-catalytic C-terminal domain of ACE2 shares a 48% sequence homology with collectrin, a protein involved in neutral amino acid reabsorption from the intestine and the kidney (22,23). In the presence of a disintegrin and metalloproteinase 17 (ADAM17), also known as tumor necrosis factor (TNF)-α−converting enzyme (TACE), ACE2 exhibits ectodomain shedding (24), which results in the formation of a soluble enzyme. ACE2 also contains a calmodulin domain on its cytoplasmic tail that influences ectodomain shedding (25)."}

{"project":"LitCovid-PubTator","denotations":[{"id":"191","span":{"begin":0,"end":4},"obj":"Gene"},{"id":"192","span":{"begin":176,"end":180},"obj":"Gene"},{"id":"193","span":{"begin":228,"end":231},"obj":"Gene"},{"id":"194","span":{"begin":257,"end":261},"obj":"Gene"},{"id":"195","span":{"begin":284,"end":287},"obj":"Gene"},{"id":"196","span":{"begin":355,"end":359},"obj":"Gene"},{"id":"197","span":{"begin":450,"end":454},"obj":"Gene"},{"id":"198","span":{"begin":458,"end":464},"obj":"Gene"},{"id":"199","span":{"begin":524,"end":530},"obj":"Gene"},{"id":"200","span":{"begin":579,"end":583},"obj":"Gene"},{"id":"201","span":{"begin":592,"end":597},"obj":"Gene"},{"id":"202","span":{"begin":718,"end":722},"obj":"Gene"},{"id":"203","span":{"begin":759,"end":769},"obj":"Gene"},{"id":"204","span":{"begin":927,"end":933},"obj":"Gene"},{"id":"205","span":{"begin":950,"end":997},"obj":"Gene"},{"id":"206","span":{"begin":999,"end":1003},"obj":"Gene"},{"id":"207","span":{"begin":1006,"end":1010},"obj":"Gene"},{"id":"208","span":{"begin":1098,"end":1102},"obj":"Gene"},{"id":"209","span":{"begin":314,"end":317},"obj":"Gene"},{"id":"210","span":{"begin":1119,"end":1129},"obj":"Gene"},{"id":"211","span":{"begin":536,"end":551},"obj":"Chemical"}],"attributes":[{"id":"A191","pred":"tao:has_database_id","subj":"191","obj":"Gene:59272"},{"id":"A192","pred":"tao:has_database_id","subj":"192","obj":"Gene:59272"},{"id":"A193","pred":"tao:has_database_id","subj":"193","obj":"Gene:1636"},{"id":"A194","pred":"tao:has_database_id","subj":"194","obj":"Gene:59272"},{"id":"A195","pred":"tao:has_database_id","subj":"195","obj":"Gene:1636"},{"id":"A196","pred":"tao:has_database_id","subj":"196","obj":"Gene:59272"},{"id":"A197","pred":"tao:has_database_id","subj":"197","obj":"Gene:59272"},{"id":"A198","pred":"tao:has_database_id","subj":"198","obj":"Gene:183"},{"id":"A199","pred":"tao:has_database_id","subj":"199","obj":"Gene:284"},{"id":"A200","pred":"tao:has_database_id","subj":"200","obj":"Gene:59272"},{"id":"A201","pred":"tao:has_database_id","subj":"201","obj":"Gene:183"},{"id":"A202","pred":"tao:has_database_id","subj":"202","obj":"Gene:59272"},{"id":"A203","pred":"tao:has_database_id","subj":"203","obj":"Gene:57393"},{"id":"A204","pred":"tao:has_database_id","subj":"204","obj":"Gene:6868"},{"id":"A205","pred":"tao:has_database_id","subj":"205","obj":"Gene:6868"},{"id":"A206","pred":"tao:has_database_id","subj":"206","obj":"Gene:6868"},{"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:1636"},{"id":"A210","pred":"tao:has_database_id","subj":"210","obj":"Gene:801"},{"id":"A211","pred":"tao:has_database_id","subj":"211","obj":"MESH:D010649"}],"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":"ACE2 is a type I integral membrane glycoprotein (15) expressed predominantly in the bronchus, lung parenchyma, heart, endothelium, kidneys, duodenum, and small intestine (16). ACE2 is a monocarboxypeptidase, unlike its homolog, ACE, which is a dipeptidase; ACE2 is not antagonized by ACE inhibitors (17). Although ACE contains 2 active catalytic domains, ACE2 has a single catalytic domain with 42% identical residues (18,19). The major substrate of ACE2 is Ang II, which upon C-terminus cleavage, produces angiotensin 1-7 (Ang1-7) and L-phenylalanine (20). Other substrates for ACE2 include Ang I, apelin-13, and dynorphin-13, which are catalyzed at much lower affinities (21). The non-catalytic C-terminal domain of ACE2 shares a 48% sequence homology with collectrin, a protein involved in neutral amino acid reabsorption from the intestine and the kidney (22,23). In the presence of a disintegrin and metalloproteinase 17 (ADAM17), also known as tumor necrosis factor (TNF)-α−converting enzyme (TACE), ACE2 exhibits ectodomain shedding (24), which results in the formation of a soluble enzyme. ACE2 also contains a calmodulin domain on its cytoplasmic tail that influences ectodomain shedding (25)."}

{"project":"2_test","denotations":[{"id":"32305401-24309898-55252922","span":{"begin":171,"end":173},"obj":"24309898"},{"id":"32305401-15283675-55252923","span":{"begin":300,"end":302},"obj":"15283675"},{"id":"32305401-1649623-55252924","span":{"begin":419,"end":421},"obj":"1649623"},{"id":"32305401-2849100-55252925","span":{"begin":422,"end":424},"obj":"2849100"},{"id":"32305401-11931993-55252926","span":{"begin":553,"end":555},"obj":"11931993"},{"id":"32305401-11815627-55252927","span":{"begin":674,"end":676},"obj":"11815627"},{"id":"32305401-18424768-55252928","span":{"begin":863,"end":865},"obj":"18424768"},{"id":"32305401-15983030-55252929","span":{"begin":1041,"end":1043},"obj":"15983030"},{"id":"32305401-18070603-55252930","span":{"begin":1198,"end":1200},"obj":"18070603"}],"text":"ACE2 is a type I integral membrane glycoprotein (15) expressed predominantly in the bronchus, lung parenchyma, heart, endothelium, kidneys, duodenum, and small intestine (16). ACE2 is a monocarboxypeptidase, unlike its homolog, ACE, which is a dipeptidase; ACE2 is not antagonized by ACE inhibitors (17). Although ACE contains 2 active catalytic domains, ACE2 has a single catalytic domain with 42% identical residues (18,19). The major substrate of ACE2 is Ang II, which upon C-terminus cleavage, produces angiotensin 1-7 (Ang1-7) and L-phenylalanine (20). Other substrates for ACE2 include Ang I, apelin-13, and dynorphin-13, which are catalyzed at much lower affinities (21). The non-catalytic C-terminal domain of ACE2 shares a 48% sequence homology with collectrin, a protein involved in neutral amino acid reabsorption from the intestine and the kidney (22,23). In the presence of a disintegrin and metalloproteinase 17 (ADAM17), also known as tumor necrosis factor (TNF)-α−converting enzyme (TACE), ACE2 exhibits ectodomain shedding (24), which results in the formation of a soluble enzyme. ACE2 also contains a calmodulin domain on its cytoplasmic tail that influences ectodomain shedding (25)."}