PMC:7161517 / 4247-5889 JSON TXT

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LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T9","span":{"begin":475,"end":487},"obj":"Body_part"},{"id":"T10","span":{"begin":524,"end":532},"obj":"Body_part"},{"id":"T11","span":{"begin":534,"end":549},"obj":"Body_part"},{"id":"T12","span":{"begin":551,"end":556},"obj":"Body_part"},{"id":"T13","span":{"begin":558,"end":569},"obj":"Body_part"},{"id":"T14","span":{"begin":571,"end":578},"obj":"Body_part"},{"id":"T15","span":{"begin":580,"end":588},"obj":"Body_part"},{"id":"T16","span":{"begin":594,"end":609},"obj":"Body_part"},{"id":"T17","span":{"begin":978,"end":991},"obj":"Body_part"},{"id":"T18","span":{"begin":1213,"end":1220},"obj":"Body_part"},{"id":"T19","span":{"begin":1241,"end":1251},"obj":"Body_part"},{"id":"T20","span":{"begin":1274,"end":1283},"obj":"Body_part"},{"id":"T21","span":{"begin":1292,"end":1298},"obj":"Body_part"},{"id":"T22","span":{"begin":1559,"end":1569},"obj":"Body_part"},{"id":"T23","span":{"begin":1584,"end":1595},"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":"Angiotensin-Converting Enzyme 2\nClassically, the RAS involves the conversion of angiotensinogen by renin into angiotensin I (Ang I). Ang I is metabolized to Ang II via the dipeptide carboxypeptidase ACE. The pro-inflammatory effects of Ang II (7, 8, 9) are mediated through Ang II type I (AT1) receptors. Recently, the ACE2 receptor and its signaling pathway were identified as an important counter regulatory mechanism to the classic RAS.\nACE2 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)."}

LitCovid-PD-UBERON

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T39","span":{"begin":289,"end":292},"obj":"Disease"},{"id":"T40","span":{"begin":1390,"end":1395},"obj":"Disease"}],"attributes":[{"id":"A39","pred":"mondo_id","subj":"T39","obj":"http://purl.obolibrary.org/obo/MONDO_0008840"},{"id":"A40","pred":"mondo_id","subj":"T40","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"}],"text":"Angiotensin-Converting Enzyme 2\nClassically, the RAS involves the conversion of angiotensinogen by renin into angiotensin I (Ang I). Ang I is metabolized to Ang II via the dipeptide carboxypeptidase ACE. The pro-inflammatory effects of Ang II (7, 8, 9) are mediated through Ang II type I (AT1) receptors. Recently, the ACE2 receptor and its signaling pathway were identified as an important counter regulatory mechanism to the classic RAS.\nACE2 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)."}

LitCovid-PD-CLO

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T12","span":{"begin":341,"end":358},"obj":"http://purl.obolibrary.org/obo/GO_0007165"},{"id":"T13","span":{"begin":341,"end":350},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T14","span":{"begin":1396,"end":1404},"obj":"http://purl.obolibrary.org/obo/GO_0070265"},{"id":"T15","span":{"begin":1396,"end":1404},"obj":"http://purl.obolibrary.org/obo/GO_0019835"},{"id":"T16","span":{"begin":1396,"end":1404},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T17","span":{"begin":1396,"end":1404},"obj":"http://purl.obolibrary.org/obo/GO_0001906"},{"id":"T18","span":{"begin":1507,"end":1516},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"Angiotensin-Converting Enzyme 2\nClassically, the RAS involves the conversion of angiotensinogen by renin into angiotensin I (Ang I). Ang I is metabolized to Ang II via the dipeptide carboxypeptidase ACE. The pro-inflammatory effects of Ang II (7, 8, 9) are mediated through Ang II type I (AT1) receptors. Recently, the ACE2 receptor and its signaling pathway were identified as an important counter regulatory mechanism to the classic RAS.\nACE2 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)."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T29","span":{"begin":0,"end":31},"obj":"Sentence"},{"id":"T30","span":{"begin":32,"end":132},"obj":"Sentence"},{"id":"T31","span":{"begin":133,"end":203},"obj":"Sentence"},{"id":"T32","span":{"begin":204,"end":304},"obj":"Sentence"},{"id":"T33","span":{"begin":305,"end":439},"obj":"Sentence"},{"id":"T34","span":{"begin":440,"end":615},"obj":"Sentence"},{"id":"T35","span":{"begin":616,"end":744},"obj":"Sentence"},{"id":"T36","span":{"begin":745,"end":866},"obj":"Sentence"},{"id":"T37","span":{"begin":867,"end":997},"obj":"Sentence"},{"id":"T38","span":{"begin":998,"end":1118},"obj":"Sentence"},{"id":"T39","span":{"begin":1119,"end":1307},"obj":"Sentence"},{"id":"T40","span":{"begin":1308,"end":1537},"obj":"Sentence"},{"id":"T41","span":{"begin":1538,"end":1642},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Angiotensin-Converting Enzyme 2\nClassically, the RAS involves the conversion of angiotensinogen by renin into angiotensin I (Ang I). Ang I is metabolized to Ang II via the dipeptide carboxypeptidase ACE. The pro-inflammatory effects of Ang II (7, 8, 9) are mediated through Ang II type I (AT1) receptors. Recently, the ACE2 receptor and its signaling pathway were identified as an important counter regulatory mechanism to the classic RAS.\nACE2 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)."}

LitCovid-PD-HP

{"project":"LitCovid-PD-HP","denotations":[{"id":"T7","span":{"begin":1390,"end":1395},"obj":"Phenotype"}],"attributes":[{"id":"A7","pred":"hp_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/HP_0002664"}],"text":"Angiotensin-Converting Enzyme 2\nClassically, the RAS involves the conversion of angiotensinogen by renin into angiotensin I (Ang I). Ang I is metabolized to Ang II via the dipeptide carboxypeptidase ACE. The pro-inflammatory effects of Ang II (7, 8, 9) are mediated through Ang II type I (AT1) receptors. Recently, the ACE2 receptor and its signaling pathway were identified as an important counter regulatory mechanism to the classic RAS.\nACE2 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)."}

LitCovid-PMC-OGER-BB

LitCovid-PubTator

2_test

{"project":"2_test","denotations":[{"id":"32305401-29217510-55252919","span":{"begin":244,"end":245},"obj":"29217510"},{"id":"32305401-10773230-55252920","span":{"begin":247,"end":248},"obj":"10773230"},{"id":"32305401-8307637-55252921","span":{"begin":250,"end":251},"obj":"8307637"},{"id":"32305401-24309898-55252922","span":{"begin":611,"end":613},"obj":"24309898"},{"id":"32305401-15283675-55252923","span":{"begin":740,"end":742},"obj":"15283675"},{"id":"32305401-1649623-55252924","span":{"begin":859,"end":861},"obj":"1649623"},{"id":"32305401-2849100-55252925","span":{"begin":862,"end":864},"obj":"2849100"},{"id":"32305401-11931993-55252926","span":{"begin":993,"end":995},"obj":"11931993"},{"id":"32305401-11815627-55252927","span":{"begin":1114,"end":1116},"obj":"11815627"},{"id":"32305401-18424768-55252928","span":{"begin":1303,"end":1305},"obj":"18424768"},{"id":"32305401-15983030-55252929","span":{"begin":1481,"end":1483},"obj":"15983030"},{"id":"32305401-18070603-55252930","span":{"begin":1638,"end":1640},"obj":"18070603"}],"text":"Angiotensin-Converting Enzyme 2\nClassically, the RAS involves the conversion of angiotensinogen by renin into angiotensin I (Ang I). Ang I is metabolized to Ang II via the dipeptide carboxypeptidase ACE. The pro-inflammatory effects of Ang II (7, 8, 9) are mediated through Ang II type I (AT1) receptors. Recently, the ACE2 receptor and its signaling pathway were identified as an important counter regulatory mechanism to the classic RAS.\nACE2 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)."}

PMC:7161517 / 4247-5889 JSONTXT

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PMC:7161517 / 4247-5889 JSON TXT