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LitCovid-sample-PD-NCBITaxon

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T46","span":{"begin":1081,"end":1091},"obj":"Species"}],"attributes":[{"id":"A46","pred":"ncbi_taxonomy_id","subj":"T46","obj":"NCBItxid:2697049"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"Beside undergoing post-translational modifications by glycosylation and phosphorylation, ACE2 is also post-translationally regulated by shedding from cell membrane through the action of the metalloproteinase ADAM17. The proteolysis of ACE2 releases a soluble, enzymatically active form which corresponds to the ACE2 ectodomain (Jia et al., 2009; Xiao et al., 2014; Conrad et al., 2016). The function, if any, of soluble ACE2 is still obscure, but the shedding mechanism is under strict molecular control. Lambert et al. (2008) highlighted that calmodulin associates with ACE2 to prevent its shedding, while calmodulin inhibitors increase the cellular release of ACE2. Patel identified a positive feedback in the RAAS: Ang II activates ADAM17, thereby increasing the release of ACE2, its negative regulator (Patel et al., 2016b). It is worth noting that high levels of plasma-soluble ACE2 have been associated with myocardial dysfunction (Epelman et al., 2009). The potential pathophysiological role of ADAM17 is further discussed in paragraph ACE2 and the Inflammatory Response to Sars-CoV-2."}

LitCovid-sample-sentences

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T112","span":{"begin":0,"end":215},"obj":"Sentence"},{"id":"T113","span":{"begin":216,"end":386},"obj":"Sentence"},{"id":"T114","span":{"begin":387,"end":504},"obj":"Sentence"},{"id":"T115","span":{"begin":505,"end":667},"obj":"Sentence"},{"id":"T116","span":{"begin":668,"end":717},"obj":"Sentence"},{"id":"T117","span":{"begin":718,"end":828},"obj":"Sentence"},{"id":"T118","span":{"begin":829,"end":960},"obj":"Sentence"},{"id":"T119","span":{"begin":961,"end":1092},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Beside undergoing post-translational modifications by glycosylation and phosphorylation, ACE2 is also post-translationally regulated by shedding from cell membrane through the action of the metalloproteinase ADAM17. The proteolysis of ACE2 releases a soluble, enzymatically active form which corresponds to the ACE2 ectodomain (Jia et al., 2009; Xiao et al., 2014; Conrad et al., 2016). The function, if any, of soluble ACE2 is still obscure, but the shedding mechanism is under strict molecular control. Lambert et al. (2008) highlighted that calmodulin associates with ACE2 to prevent its shedding, while calmodulin inhibitors increase the cellular release of ACE2. Patel identified a positive feedback in the RAAS: Ang II activates ADAM17, thereby increasing the release of ACE2, its negative regulator (Patel et al., 2016b). It is worth noting that high levels of plasma-soluble ACE2 have been associated with myocardial dysfunction (Epelman et al., 2009). The potential pathophysiological role of ADAM17 is further discussed in paragraph ACE2 and the Inflammatory Response to Sars-CoV-2."}

LitCovid-sample-Pubtator

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"521","span":{"begin":89,"end":93},"obj":"Gene"},{"id":"522","span":{"begin":235,"end":239},"obj":"Gene"},{"id":"523","span":{"begin":311,"end":315},"obj":"Gene"},{"id":"524","span":{"begin":420,"end":424},"obj":"Gene"},{"id":"525","span":{"begin":571,"end":575},"obj":"Gene"},{"id":"526","span":{"begin":662,"end":666},"obj":"Gene"},{"id":"527","span":{"begin":718,"end":724},"obj":"Gene"},{"id":"528","span":{"begin":735,"end":741},"obj":"Gene"},{"id":"529","span":{"begin":777,"end":781},"obj":"Gene"},{"id":"530","span":{"begin":883,"end":887},"obj":"Gene"},{"id":"531","span":{"begin":1002,"end":1008},"obj":"Gene"},{"id":"532","span":{"begin":1043,"end":1047},"obj":"Gene"},{"id":"533","span":{"begin":607,"end":617},"obj":"Gene"},{"id":"534","span":{"begin":544,"end":554},"obj":"Gene"},{"id":"535","span":{"begin":102,"end":106},"obj":"Gene"},{"id":"536","span":{"begin":18,"end":22},"obj":"Gene"},{"id":"537","span":{"begin":155,"end":163},"obj":"Gene"},{"id":"538","span":{"begin":1081,"end":1091},"obj":"Species"},{"id":"539","span":{"begin":914,"end":936},"obj":"Disease"}],"attributes":[{"id":"A528","pred":"pubann:denotes","subj":"528","obj":"Gene:6868"},{"id":"A533","pred":"pubann:denotes","subj":"533","obj":"Gene:801"},{"id":"A521","pred":"pubann:denotes","subj":"521","obj":"Gene:59272"},{"id":"A539","pred":"pubann:denotes","subj":"539","obj":"MESH:D009202"},{"id":"A535","pred":"pubann:denotes","subj":"535","obj":"Gene:159371"},{"id":"A525","pred":"pubann:denotes","subj":"525","obj":"Gene:59272"},{"id":"A529","pred":"pubann:denotes","subj":"529","obj":"Gene:59272"},{"id":"A523","pred":"pubann:denotes","subj":"523","obj":"Gene:59272"},{"id":"A532","pred":"pubann:denotes","subj":"532","obj":"Gene:59272"},{"id":"A537","pred":"pubann:denotes","subj":"537","obj":"Gene:43740571"},{"id":"A536","pred":"pubann:denotes","subj":"536","obj":"Gene:159371"},{"id":"A526","pred":"pubann:denotes","subj":"526","obj":"Gene:59272"},{"id":"A522","pred":"pubann:denotes","subj":"522","obj":"Gene:59272"},{"id":"A538","pred":"pubann:denotes","subj":"538","obj":"Tax:2697049"},{"id":"A530","pred":"pubann:denotes","subj":"530","obj":"Gene:59272"},{"id":"A527","pred":"pubann:denotes","subj":"527","obj":"Gene:24179"},{"id":"A524","pred":"pubann:denotes","subj":"524","obj":"Gene:59272"},{"id":"A531","pred":"pubann:denotes","subj":"531","obj":"Gene:6868"},{"id":"A534","pred":"pubann:denotes","subj":"534","obj":"Gene:801"}],"text":"Beside undergoing post-translational modifications by glycosylation and phosphorylation, ACE2 is also post-translationally regulated by shedding from cell membrane through the action of the metalloproteinase ADAM17. The proteolysis of ACE2 releases a soluble, enzymatically active form which corresponds to the ACE2 ectodomain (Jia et al., 2009; Xiao et al., 2014; Conrad et al., 2016). The function, if any, of soluble ACE2 is still obscure, but the shedding mechanism is under strict molecular control. Lambert et al. (2008) highlighted that calmodulin associates with ACE2 to prevent its shedding, while calmodulin inhibitors increase the cellular release of ACE2. Patel identified a positive feedback in the RAAS: Ang II activates ADAM17, thereby increasing the release of ACE2, its negative regulator (Patel et al., 2016b). It is worth noting that high levels of plasma-soluble ACE2 have been associated with myocardial dysfunction (Epelman et al., 2009). The potential pathophysiological role of ADAM17 is further discussed in paragraph ACE2 and the Inflammatory Response to Sars-CoV-2."}

LitCovid-sample-UniProt

LitCovid-sample-PD-IDO

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T40","span":{"begin":150,"end":154},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T41","span":{"begin":391,"end":399},"obj":"http://purl.obolibrary.org/obo/BFO_0000034"}],"text":"Beside undergoing post-translational modifications by glycosylation and phosphorylation, ACE2 is also post-translationally regulated by shedding from cell membrane through the action of the metalloproteinase ADAM17. The proteolysis of ACE2 releases a soluble, enzymatically active form which corresponds to the ACE2 ectodomain (Jia et al., 2009; Xiao et al., 2014; Conrad et al., 2016). The function, if any, of soluble ACE2 is still obscure, but the shedding mechanism is under strict molecular control. Lambert et al. (2008) highlighted that calmodulin associates with ACE2 to prevent its shedding, while calmodulin inhibitors increase the cellular release of ACE2. Patel identified a positive feedback in the RAAS: Ang II activates ADAM17, thereby increasing the release of ACE2, its negative regulator (Patel et al., 2016b). It is worth noting that high levels of plasma-soluble ACE2 have been associated with myocardial dysfunction (Epelman et al., 2009). The potential pathophysiological role of ADAM17 is further discussed in paragraph ACE2 and the Inflammatory Response to Sars-CoV-2."}

LitCovid-sample-PD-FMA

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T92","span":{"begin":150,"end":163},"obj":"Body_part"},{"id":"T93","span":{"begin":150,"end":154},"obj":"Body_part"},{"id":"T94","span":{"begin":544,"end":554},"obj":"Body_part"},{"id":"T95","span":{"begin":607,"end":617},"obj":"Body_part"},{"id":"T96","span":{"begin":868,"end":874},"obj":"Body_part"}],"attributes":[{"id":"A92","pred":"fma_id","subj":"T92","obj":"http://purl.org/sig/ont/fma/fma63841"},{"id":"A95","pred":"fma_id","subj":"T95","obj":"http://purl.org/sig/ont/fma/fma62343"},{"id":"A96","pred":"fma_id","subj":"T96","obj":"http://purl.org/sig/ont/fma/fma62970"},{"id":"A94","pred":"fma_id","subj":"T94","obj":"http://purl.org/sig/ont/fma/fma62343"},{"id":"A93","pred":"fma_id","subj":"T93","obj":"http://purl.org/sig/ont/fma/fma68646"}],"text":"Beside undergoing post-translational modifications by glycosylation and phosphorylation, ACE2 is also post-translationally regulated by shedding from cell membrane through the action of the metalloproteinase ADAM17. The proteolysis of ACE2 releases a soluble, enzymatically active form which corresponds to the ACE2 ectodomain (Jia et al., 2009; Xiao et al., 2014; Conrad et al., 2016). The function, if any, of soluble ACE2 is still obscure, but the shedding mechanism is under strict molecular control. Lambert et al. (2008) highlighted that calmodulin associates with ACE2 to prevent its shedding, while calmodulin inhibitors increase the cellular release of ACE2. Patel identified a positive feedback in the RAAS: Ang II activates ADAM17, thereby increasing the release of ACE2, its negative regulator (Patel et al., 2016b). It is worth noting that high levels of plasma-soluble ACE2 have been associated with myocardial dysfunction (Epelman et al., 2009). The potential pathophysiological role of ADAM17 is further discussed in paragraph ACE2 and the Inflammatory Response to Sars-CoV-2."}

LitCovid-sample-PD-MONDO

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T56","span":{"begin":1081,"end":1091},"obj":"Disease"}],"attributes":[{"id":"A56","pred":"mondo_id","subj":"T56","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"Beside undergoing post-translational modifications by glycosylation and phosphorylation, ACE2 is also post-translationally regulated by shedding from cell membrane through the action of the metalloproteinase ADAM17. The proteolysis of ACE2 releases a soluble, enzymatically active form which corresponds to the ACE2 ectodomain (Jia et al., 2009; Xiao et al., 2014; Conrad et al., 2016). The function, if any, of soluble ACE2 is still obscure, but the shedding mechanism is under strict molecular control. Lambert et al. (2008) highlighted that calmodulin associates with ACE2 to prevent its shedding, while calmodulin inhibitors increase the cellular release of ACE2. Patel identified a positive feedback in the RAAS: Ang II activates ADAM17, thereby increasing the release of ACE2, its negative regulator (Patel et al., 2016b). It is worth noting that high levels of plasma-soluble ACE2 have been associated with myocardial dysfunction (Epelman et al., 2009). The potential pathophysiological role of ADAM17 is further discussed in paragraph ACE2 and the Inflammatory Response to Sars-CoV-2."}

LitCovid-sample-PD-GO-BP-0

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T49","span":{"begin":18,"end":50},"obj":"http://purl.obolibrary.org/obo/GO_0043687"},{"id":"T50","span":{"begin":54,"end":67},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T51","span":{"begin":72,"end":87},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T52","span":{"begin":107,"end":122},"obj":"http://purl.obolibrary.org/obo/GO_0006412"},{"id":"T53","span":{"begin":220,"end":231},"obj":"http://purl.obolibrary.org/obo/GO_0006508"},{"id":"T54","span":{"begin":1056,"end":1077},"obj":"http://purl.obolibrary.org/obo/GO_0006954"}],"text":"Beside undergoing post-translational modifications by glycosylation and phosphorylation, ACE2 is also post-translationally regulated by shedding from cell membrane through the action of the metalloproteinase ADAM17. The proteolysis of ACE2 releases a soluble, enzymatically active form which corresponds to the ACE2 ectodomain (Jia et al., 2009; Xiao et al., 2014; Conrad et al., 2016). The function, if any, of soluble ACE2 is still obscure, but the shedding mechanism is under strict molecular control. Lambert et al. (2008) highlighted that calmodulin associates with ACE2 to prevent its shedding, while calmodulin inhibitors increase the cellular release of ACE2. Patel identified a positive feedback in the RAAS: Ang II activates ADAM17, thereby increasing the release of ACE2, its negative regulator (Patel et al., 2016b). It is worth noting that high levels of plasma-soluble ACE2 have been associated with myocardial dysfunction (Epelman et al., 2009). The potential pathophysiological role of ADAM17 is further discussed in paragraph ACE2 and the Inflammatory Response to Sars-CoV-2."}

LitCovid-sample-GO-BP

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T51","span":{"begin":18,"end":50},"obj":"http://purl.obolibrary.org/obo/GO_0043687"},{"id":"T52","span":{"begin":54,"end":67},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T53","span":{"begin":72,"end":87},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T54","span":{"begin":107,"end":122},"obj":"http://purl.obolibrary.org/obo/GO_0006412"},{"id":"T55","span":{"begin":220,"end":231},"obj":"http://purl.obolibrary.org/obo/GO_0006508"},{"id":"T56","span":{"begin":1056,"end":1077},"obj":"http://purl.obolibrary.org/obo/GO_0006954"}],"text":"Beside undergoing post-translational modifications by glycosylation and phosphorylation, ACE2 is also post-translationally regulated by shedding from cell membrane through the action of the metalloproteinase ADAM17. The proteolysis of ACE2 releases a soluble, enzymatically active form which corresponds to the ACE2 ectodomain (Jia et al., 2009; Xiao et al., 2014; Conrad et al., 2016). The function, if any, of soluble ACE2 is still obscure, but the shedding mechanism is under strict molecular control. Lambert et al. (2008) highlighted that calmodulin associates with ACE2 to prevent its shedding, while calmodulin inhibitors increase the cellular release of ACE2. Patel identified a positive feedback in the RAAS: Ang II activates ADAM17, thereby increasing the release of ACE2, its negative regulator (Patel et al., 2016b). It is worth noting that high levels of plasma-soluble ACE2 have been associated with myocardial dysfunction (Epelman et al., 2009). The potential pathophysiological role of ADAM17 is further discussed in paragraph ACE2 and the Inflammatory Response to Sars-CoV-2."}

LitCovid-PubTator

{"project":"LitCovid-PubTator","denotations":[{"id":"521","span":{"begin":89,"end":93},"obj":"Gene"},{"id":"522","span":{"begin":235,"end":239},"obj":"Gene"},{"id":"523","span":{"begin":311,"end":315},"obj":"Gene"},{"id":"524","span":{"begin":420,"end":424},"obj":"Gene"},{"id":"525","span":{"begin":571,"end":575},"obj":"Gene"},{"id":"526","span":{"begin":662,"end":666},"obj":"Gene"},{"id":"527","span":{"begin":718,"end":724},"obj":"Gene"},{"id":"528","span":{"begin":735,"end":741},"obj":"Gene"},{"id":"529","span":{"begin":777,"end":781},"obj":"Gene"},{"id":"530","span":{"begin":883,"end":887},"obj":"Gene"},{"id":"531","span":{"begin":1002,"end":1008},"obj":"Gene"},{"id":"532","span":{"begin":1043,"end":1047},"obj":"Gene"},{"id":"533","span":{"begin":607,"end":617},"obj":"Gene"},{"id":"534","span":{"begin":544,"end":554},"obj":"Gene"},{"id":"535","span":{"begin":102,"end":106},"obj":"Gene"},{"id":"536","span":{"begin":18,"end":22},"obj":"Gene"},{"id":"537","span":{"begin":155,"end":163},"obj":"Gene"},{"id":"538","span":{"begin":1081,"end":1091},"obj":"Species"},{"id":"539","span":{"begin":914,"end":936},"obj":"Disease"}],"attributes":[{"id":"A521","pred":"tao:has_database_id","subj":"521","obj":"Gene:59272"},{"id":"A522","pred":"tao:has_database_id","subj":"522","obj":"Gene:59272"},{"id":"A523","pred":"tao:has_database_id","subj":"523","obj":"Gene:59272"},{"id":"A524","pred":"tao:has_database_id","subj":"524","obj":"Gene:59272"},{"id":"A525","pred":"tao:has_database_id","subj":"525","obj":"Gene:59272"},{"id":"A526","pred":"tao:has_database_id","subj":"526","obj":"Gene:59272"},{"id":"A527","pred":"tao:has_database_id","subj":"527","obj":"Gene:24179"},{"id":"A528","pred":"tao:has_database_id","subj":"528","obj":"Gene:6868"},{"id":"A529","pred":"tao:has_database_id","subj":"529","obj":"Gene:59272"},{"id":"A530","pred":"tao:has_database_id","subj":"530","obj":"Gene:59272"},{"id":"A531","pred":"tao:has_database_id","subj":"531","obj":"Gene:6868"},{"id":"A532","pred":"tao:has_database_id","subj":"532","obj":"Gene:59272"},{"id":"A533","pred":"tao:has_database_id","subj":"533","obj":"Gene:801"},{"id":"A534","pred":"tao:has_database_id","subj":"534","obj":"Gene:801"},{"id":"A535","pred":"tao:has_database_id","subj":"535","obj":"Gene:159371"},{"id":"A536","pred":"tao:has_database_id","subj":"536","obj":"Gene:159371"},{"id":"A537","pred":"tao:has_database_id","subj":"537","obj":"Gene:43740571"},{"id":"A538","pred":"tao:has_database_id","subj":"538","obj":"Tax:2697049"},{"id":"A539","pred":"tao:has_database_id","subj":"539","obj":"MESH:D009202"}],"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":"Beside undergoing post-translational modifications by glycosylation and phosphorylation, ACE2 is also post-translationally regulated by shedding from cell membrane through the action of the metalloproteinase ADAM17. The proteolysis of ACE2 releases a soluble, enzymatically active form which corresponds to the ACE2 ectodomain (Jia et al., 2009; Xiao et al., 2014; Conrad et al., 2016). The function, if any, of soluble ACE2 is still obscure, but the shedding mechanism is under strict molecular control. Lambert et al. (2008) highlighted that calmodulin associates with ACE2 to prevent its shedding, while calmodulin inhibitors increase the cellular release of ACE2. Patel identified a positive feedback in the RAAS: Ang II activates ADAM17, thereby increasing the release of ACE2, its negative regulator (Patel et al., 2016b). It is worth noting that high levels of plasma-soluble ACE2 have been associated with myocardial dysfunction (Epelman et al., 2009). The potential pathophysiological role of ADAM17 is further discussed in paragraph ACE2 and the Inflammatory Response to Sars-CoV-2."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T112","span":{"begin":0,"end":215},"obj":"Sentence"},{"id":"T113","span":{"begin":216,"end":386},"obj":"Sentence"},{"id":"T114","span":{"begin":387,"end":504},"obj":"Sentence"},{"id":"T115","span":{"begin":505,"end":667},"obj":"Sentence"},{"id":"T116","span":{"begin":668,"end":717},"obj":"Sentence"},{"id":"T117","span":{"begin":718,"end":828},"obj":"Sentence"},{"id":"T118","span":{"begin":829,"end":960},"obj":"Sentence"},{"id":"T119","span":{"begin":961,"end":1092},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Beside undergoing post-translational modifications by glycosylation and phosphorylation, ACE2 is also post-translationally regulated by shedding from cell membrane through the action of the metalloproteinase ADAM17. The proteolysis of ACE2 releases a soluble, enzymatically active form which corresponds to the ACE2 ectodomain (Jia et al., 2009; Xiao et al., 2014; Conrad et al., 2016). The function, if any, of soluble ACE2 is still obscure, but the shedding mechanism is under strict molecular control. Lambert et al. (2008) highlighted that calmodulin associates with ACE2 to prevent its shedding, while calmodulin inhibitors increase the cellular release of ACE2. Patel identified a positive feedback in the RAAS: Ang II activates ADAM17, thereby increasing the release of ACE2, its negative regulator (Patel et al., 2016b). It is worth noting that high levels of plasma-soluble ACE2 have been associated with myocardial dysfunction (Epelman et al., 2009). The potential pathophysiological role of ADAM17 is further discussed in paragraph ACE2 and the Inflammatory Response to Sars-CoV-2."}

PMC:7556165 / 16975-18067 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:7556165 / 16975-18067 JSON TXT