PMC:7121452 / 4184-5159 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"125","span":{"begin":151,"end":155},"obj":"Gene"},{"id":"126","span":{"begin":204,"end":218},"obj":"Gene"},{"id":"127","span":{"begin":335,"end":349},"obj":"Gene"},{"id":"128","span":{"begin":378,"end":382},"obj":"Gene"},{"id":"129","span":{"begin":409,"end":422},"obj":"Gene"},{"id":"130","span":{"begin":568,"end":572},"obj":"Gene"},{"id":"131","span":{"begin":807,"end":811},"obj":"Gene"},{"id":"132","span":{"begin":847,"end":851},"obj":"Gene"},{"id":"133","span":{"begin":514,"end":520},"obj":"Species"},{"id":"134","span":{"begin":676,"end":686},"obj":"Species"},{"id":"135","span":{"begin":294,"end":300},"obj":"Chemical"},{"id":"136","span":{"begin":426,"end":443},"obj":"Chemical"},{"id":"137","span":{"begin":488,"end":496},"obj":"Chemical"},{"id":"138","span":{"begin":316,"end":324},"obj":"Disease"},{"id":"139","span":{"begin":704,"end":719},"obj":"Disease"}],"attributes":[{"id":"A125","pred":"tao:has_database_id","subj":"125","obj":"Gene:59272"},{"id":"A126","pred":"tao:has_database_id","subj":"126","obj":"Gene:183"},{"id":"A127","pred":"tao:has_database_id","subj":"127","obj":"Gene:183"},{"id":"A128","pred":"tao:has_database_id","subj":"128","obj":"Gene:59272"},{"id":"A129","pred":"tao:has_database_id","subj":"129","obj":"Gene:183"},{"id":"A130","pred":"tao:has_database_id","subj":"130","obj":"Gene:59272"},{"id":"A131","pred":"tao:has_database_id","subj":"131","obj":"Gene:59272"},{"id":"A132","pred":"tao:has_database_id","subj":"132","obj":"Gene:59272"},{"id":"A133","pred":"tao:has_database_id","subj":"133","obj":"Tax:9606"},{"id":"A134","pred":"tao:has_database_id","subj":"134","obj":"Tax:2697049"},{"id":"A135","pred":"tao:has_database_id","subj":"135","obj":"MESH:D012964"},{"id":"A137","pred":"tao:has_database_id","subj":"137","obj":"MESH:D010455"},{"id":"A138","pred":"tao:has_database_id","subj":"138","obj":"MESH:D005355"},{"id":"A139","pred":"tao:has_database_id","subj":"139","obj":"MESH:D014947"}],"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":"Tissue-specific and circulating components of the RAAS make up a complex intersecting network of regulatory and counterregulatory peptides (Figure 1). ACE2 is a key counterregulatory enzyme that degrades angiotensin II to angiotensin-(1–7), thereby attenuating its effects on vasoconstriction, sodium retention, and fibrosis. Although angiotensin II is the primary substrate of ACE2, that enzyme also cleaves angiotensin I to angiotensin-(1–9) and participates in the hydrolysis of other peptides.16 In studies in humans, tissue samples from 15 organs have shown that ACE2 is expressed broadly, including in the heart and kidneys, as well as on the principal target cells for SARS-CoV-2 (and the site of dominant injury), the lung alveolar epithelial cells.17 Of interest, the circulating levels of soluble ACE2 are low and the functional role of ACE2 in the lungs appears to be relatively minimal under normal conditions18 but may be up-regulated in certain clinical states."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T3","span":{"begin":0,"end":6},"obj":"Body_part"},{"id":"T4","span":{"begin":522,"end":528},"obj":"Body_part"},{"id":"T5","span":{"begin":612,"end":617},"obj":"Body_part"},{"id":"T6","span":{"begin":622,"end":629},"obj":"Body_part"},{"id":"T7","span":{"begin":666,"end":671},"obj":"Body_part"},{"id":"T8","span":{"begin":726,"end":730},"obj":"Body_part"},{"id":"T9","span":{"begin":731,"end":756},"obj":"Body_part"},{"id":"T10","span":{"begin":751,"end":756},"obj":"Body_part"},{"id":"T11","span":{"begin":859,"end":864},"obj":"Body_part"}],"attributes":[{"id":"A3","pred":"fma_id","subj":"T3","obj":"http://purl.org/sig/ont/fma/fma9637"},{"id":"A4","pred":"fma_id","subj":"T4","obj":"http://purl.org/sig/ont/fma/fma9637"},{"id":"A5","pred":"fma_id","subj":"T5","obj":"http://purl.org/sig/ont/fma/fma7088"},{"id":"A6","pred":"fma_id","subj":"T6","obj":"http://purl.org/sig/ont/fma/fma7203"},{"id":"A7","pred":"fma_id","subj":"T7","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A8","pred":"fma_id","subj":"T8","obj":"http://purl.org/sig/ont/fma/fma7195"},{"id":"A9","pred":"fma_id","subj":"T9","obj":"http://purl.org/sig/ont/fma/fma62499"},{"id":"A10","pred":"fma_id","subj":"T10","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A11","pred":"fma_id","subj":"T11","obj":"http://purl.org/sig/ont/fma/fma68877"}],"text":"Tissue-specific and circulating components of the RAAS make up a complex intersecting network of regulatory and counterregulatory peptides (Figure 1). ACE2 is a key counterregulatory enzyme that degrades angiotensin II to angiotensin-(1–7), thereby attenuating its effects on vasoconstriction, sodium retention, and fibrosis. Although angiotensin II is the primary substrate of ACE2, that enzyme also cleaves angiotensin I to angiotensin-(1–9) and participates in the hydrolysis of other peptides.16 In studies in humans, tissue samples from 15 organs have shown that ACE2 is expressed broadly, including in the heart and kidneys, as well as on the principal target cells for SARS-CoV-2 (and the site of dominant injury), the lung alveolar epithelial cells.17 Of interest, the circulating levels of soluble ACE2 are low and the functional role of ACE2 in the lungs appears to be relatively minimal under normal conditions18 but may be up-regulated in certain clinical states."}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T2","span":{"begin":0,"end":6},"obj":"Body_part"},{"id":"T3","span":{"begin":522,"end":528},"obj":"Body_part"},{"id":"T4","span":{"begin":545,"end":551},"obj":"Body_part"},{"id":"T5","span":{"begin":612,"end":617},"obj":"Body_part"},{"id":"T6","span":{"begin":726,"end":730},"obj":"Body_part"}],"attributes":[{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000062"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0000948"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"}],"text":"Tissue-specific and circulating components of the RAAS make up a complex intersecting network of regulatory and counterregulatory peptides (Figure 1). ACE2 is a key counterregulatory enzyme that degrades angiotensin II to angiotensin-(1–7), thereby attenuating its effects on vasoconstriction, sodium retention, and fibrosis. Although angiotensin II is the primary substrate of ACE2, that enzyme also cleaves angiotensin I to angiotensin-(1–9) and participates in the hydrolysis of other peptides.16 In studies in humans, tissue samples from 15 organs have shown that ACE2 is expressed broadly, including in the heart and kidneys, as well as on the principal target cells for SARS-CoV-2 (and the site of dominant injury), the lung alveolar epithelial cells.17 Of interest, the circulating levels of soluble ACE2 are low and the functional role of ACE2 in the lungs appears to be relatively minimal under normal conditions18 but may be up-regulated in certain clinical states."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T15","span":{"begin":676,"end":684},"obj":"Disease"},{"id":"T16","span":{"begin":713,"end":719},"obj":"Disease"}],"attributes":[{"id":"A15","pred":"mondo_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A16","pred":"mondo_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/MONDO_0021178"}],"text":"Tissue-specific and circulating components of the RAAS make up a complex intersecting network of regulatory and counterregulatory peptides (Figure 1). ACE2 is a key counterregulatory enzyme that degrades angiotensin II to angiotensin-(1–7), thereby attenuating its effects on vasoconstriction, sodium retention, and fibrosis. Although angiotensin II is the primary substrate of ACE2, that enzyme also cleaves angiotensin I to angiotensin-(1–9) and participates in the hydrolysis of other peptides.16 In studies in humans, tissue samples from 15 organs have shown that ACE2 is expressed broadly, including in the heart and kidneys, as well as on the principal target cells for SARS-CoV-2 (and the site of dominant injury), the lung alveolar epithelial cells.17 Of interest, the circulating levels of soluble ACE2 are low and the functional role of ACE2 in the lungs appears to be relatively minimal under normal conditions18 but may be up-regulated in certain clinical states."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T18","span":{"begin":63,"end":64},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T19","span":{"begin":130,"end":138},"obj":"http://purl.obolibrary.org/obo/PR_000018263"},{"id":"T20","span":{"begin":159,"end":160},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T21","span":{"begin":488,"end":496},"obj":"http://purl.obolibrary.org/obo/PR_000018263"},{"id":"T22","span":{"begin":514,"end":520},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T23","span":{"begin":545,"end":551},"obj":"http://purl.obolibrary.org/obo/UBERON_0003103"},{"id":"T24","span":{"begin":612,"end":617},"obj":"http://purl.obolibrary.org/obo/UBERON_0000948"},{"id":"T25","span":{"begin":612,"end":617},"obj":"http://purl.obolibrary.org/obo/UBERON_0007100"},{"id":"T26","span":{"begin":612,"end":617},"obj":"http://purl.obolibrary.org/obo/UBERON_0015228"},{"id":"T27","span":{"begin":612,"end":617},"obj":"http://www.ebi.ac.uk/efo/EFO_0000815"},{"id":"T28","span":{"begin":622,"end":629},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"T29","span":{"begin":622,"end":629},"obj":"http://www.ebi.ac.uk/efo/EFO_0000927"},{"id":"T30","span":{"begin":622,"end":629},"obj":"http://www.ebi.ac.uk/efo/EFO_0000929"},{"id":"T31","span":{"begin":666,"end":671},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T32","span":{"begin":726,"end":730},"obj":"http://purl.obolibrary.org/obo/UBERON_0002048"},{"id":"T33","span":{"begin":726,"end":730},"obj":"http://www.ebi.ac.uk/efo/EFO_0000934"},{"id":"T34","span":{"begin":740,"end":750},"obj":"http://purl.obolibrary.org/obo/CL_0000066"},{"id":"T35","span":{"begin":751,"end":756},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T36","span":{"begin":859,"end":864},"obj":"http://www.ebi.ac.uk/efo/EFO_0000934"}],"text":"Tissue-specific and circulating components of the RAAS make up a complex intersecting network of regulatory and counterregulatory peptides (Figure 1). ACE2 is a key counterregulatory enzyme that degrades angiotensin II to angiotensin-(1–7), thereby attenuating its effects on vasoconstriction, sodium retention, and fibrosis. Although angiotensin II is the primary substrate of ACE2, that enzyme also cleaves angiotensin I to angiotensin-(1–9) and participates in the hydrolysis of other peptides.16 In studies in humans, tissue samples from 15 organs have shown that ACE2 is expressed broadly, including in the heart and kidneys, as well as on the principal target cells for SARS-CoV-2 (and the site of dominant injury), the lung alveolar epithelial cells.17 Of interest, the circulating levels of soluble ACE2 are low and the functional role of ACE2 in the lungs appears to be relatively minimal under normal conditions18 but may be up-regulated in certain clinical states."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T22","span":{"begin":130,"end":138},"obj":"Chemical"},{"id":"T23","span":{"begin":204,"end":218},"obj":"Chemical"},{"id":"T26","span":{"begin":204,"end":215},"obj":"Chemical"},{"id":"T27","span":{"begin":216,"end":218},"obj":"Chemical"},{"id":"T28","span":{"begin":222,"end":233},"obj":"Chemical"},{"id":"T29","span":{"begin":294,"end":300},"obj":"Chemical"},{"id":"T30","span":{"begin":335,"end":349},"obj":"Chemical"},{"id":"T33","span":{"begin":335,"end":346},"obj":"Chemical"},{"id":"T34","span":{"begin":347,"end":349},"obj":"Chemical"},{"id":"T35","span":{"begin":409,"end":420},"obj":"Chemical"},{"id":"T36","span":{"begin":426,"end":437},"obj":"Chemical"},{"id":"T37","span":{"begin":488,"end":496},"obj":"Chemical"}],"attributes":[{"id":"A22","pred":"chebi_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/CHEBI_16670"},{"id":"A23","pred":"chebi_id","subj":"T23","obj":"http://purl.obolibrary.org/obo/CHEBI_2719"},{"id":"A24","pred":"chebi_id","subj":"T23","obj":"http://purl.obolibrary.org/obo/CHEBI_48432"},{"id":"A25","pred":"chebi_id","subj":"T23","obj":"http://purl.obolibrary.org/obo/CHEBI_58506"},{"id":"A26","pred":"chebi_id","subj":"T26","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A27","pred":"chebi_id","subj":"T27","obj":"http://purl.obolibrary.org/obo/CHEBI_74067"},{"id":"A28","pred":"chebi_id","subj":"T28","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A29","pred":"chebi_id","subj":"T29","obj":"http://purl.obolibrary.org/obo/CHEBI_26708"},{"id":"A30","pred":"chebi_id","subj":"T30","obj":"http://purl.obolibrary.org/obo/CHEBI_2719"},{"id":"A31","pred":"chebi_id","subj":"T30","obj":"http://purl.obolibrary.org/obo/CHEBI_48432"},{"id":"A32","pred":"chebi_id","subj":"T30","obj":"http://purl.obolibrary.org/obo/CHEBI_58506"},{"id":"A33","pred":"chebi_id","subj":"T33","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A34","pred":"chebi_id","subj":"T34","obj":"http://purl.obolibrary.org/obo/CHEBI_74067"},{"id":"A35","pred":"chebi_id","subj":"T35","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A36","pred":"chebi_id","subj":"T36","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A37","pred":"chebi_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/CHEBI_16670"}],"text":"Tissue-specific and circulating components of the RAAS make up a complex intersecting network of regulatory and counterregulatory peptides (Figure 1). ACE2 is a key counterregulatory enzyme that degrades angiotensin II to angiotensin-(1–7), thereby attenuating its effects on vasoconstriction, sodium retention, and fibrosis. Although angiotensin II is the primary substrate of ACE2, that enzyme also cleaves angiotensin I to angiotensin-(1–9) and participates in the hydrolysis of other peptides.16 In studies in humans, tissue samples from 15 organs have shown that ACE2 is expressed broadly, including in the heart and kidneys, as well as on the principal target cells for SARS-CoV-2 (and the site of dominant injury), the lung alveolar epithelial cells.17 Of interest, the circulating levels of soluble ACE2 are low and the functional role of ACE2 in the lungs appears to be relatively minimal under normal conditions18 but may be up-regulated in certain clinical states."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T3","span":{"begin":276,"end":292},"obj":"http://purl.obolibrary.org/obo/GO_0042310"},{"id":"T4","span":{"begin":301,"end":310},"obj":"http://purl.obolibrary.org/obo/GO_0051235"}],"text":"Tissue-specific and circulating components of the RAAS make up a complex intersecting network of regulatory and counterregulatory peptides (Figure 1). ACE2 is a key counterregulatory enzyme that degrades angiotensin II to angiotensin-(1–7), thereby attenuating its effects on vasoconstriction, sodium retention, and fibrosis. Although angiotensin II is the primary substrate of ACE2, that enzyme also cleaves angiotensin I to angiotensin-(1–9) and participates in the hydrolysis of other peptides.16 In studies in humans, tissue samples from 15 organs have shown that ACE2 is expressed broadly, including in the heart and kidneys, as well as on the principal target cells for SARS-CoV-2 (and the site of dominant injury), the lung alveolar epithelial cells.17 Of interest, the circulating levels of soluble ACE2 are low and the functional role of ACE2 in the lungs appears to be relatively minimal under normal conditions18 but may be up-regulated in certain clinical states."}

{"project":"LitCovid-sentences","denotations":[{"id":"T19","span":{"begin":0,"end":150},"obj":"Sentence"},{"id":"T20","span":{"begin":151,"end":325},"obj":"Sentence"},{"id":"T21","span":{"begin":326,"end":975},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Tissue-specific and circulating components of the RAAS make up a complex intersecting network of regulatory and counterregulatory peptides (Figure 1). ACE2 is a key counterregulatory enzyme that degrades angiotensin II to angiotensin-(1–7), thereby attenuating its effects on vasoconstriction, sodium retention, and fibrosis. Although angiotensin II is the primary substrate of ACE2, that enzyme also cleaves angiotensin I to angiotensin-(1–9) and participates in the hydrolysis of other peptides.16 In studies in humans, tissue samples from 15 organs have shown that ACE2 is expressed broadly, including in the heart and kidneys, as well as on the principal target cells for SARS-CoV-2 (and the site of dominant injury), the lung alveolar epithelial cells.17 Of interest, the circulating levels of soluble ACE2 are low and the functional role of ACE2 in the lungs appears to be relatively minimal under normal conditions18 but may be up-regulated in certain clinical states."}

{"project":"2_test","denotations":[{"id":"32227760-11815627-75177413","span":{"begin":497,"end":499},"obj":"11815627"},{"id":"32227760-15141377-75177414","span":{"begin":757,"end":759},"obj":"15141377"},{"id":"32227760-31786979-75177415","span":{"begin":921,"end":923},"obj":"31786979"}],"text":"Tissue-specific and circulating components of the RAAS make up a complex intersecting network of regulatory and counterregulatory peptides (Figure 1). ACE2 is a key counterregulatory enzyme that degrades angiotensin II to angiotensin-(1–7), thereby attenuating its effects on vasoconstriction, sodium retention, and fibrosis. Although angiotensin II is the primary substrate of ACE2, that enzyme also cleaves angiotensin I to angiotensin-(1–9) and participates in the hydrolysis of other peptides.16 In studies in humans, tissue samples from 15 organs have shown that ACE2 is expressed broadly, including in the heart and kidneys, as well as on the principal target cells for SARS-CoV-2 (and the site of dominant injury), the lung alveolar epithelial cells.17 Of interest, the circulating levels of soluble ACE2 are low and the functional role of ACE2 in the lungs appears to be relatively minimal under normal conditions18 but may be up-regulated in certain clinical states."}