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LitCovid-PD-FMA-UBERON

LitCovid-PD-UBERON

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T22","span":{"begin":1477,"end":1481},"obj":"Body_part"},{"id":"T23","span":{"begin":1587,"end":1596},"obj":"Body_part"},{"id":"T24","span":{"begin":1798,"end":1802},"obj":"Body_part"}],"attributes":[{"id":"A22","pred":"uberon_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"},{"id":"A23","pred":"uberon_id","subj":"T23","obj":"http://purl.obolibrary.org/obo/UBERON_0000160"},{"id":"A24","pred":"uberon_id","subj":"T24","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"}],"text":"A disintegrin and metallopeptidase domain (ADAM) family of Zn-metalloproteinases belongs to membrane proteins. The well-known ADAM17 is a TNF-α-converting enzyme (TACE), called the sheddase for TNF-α. Other ADAM sheddase family members include ADAM9, ADAM10 and ADAM12. ADAM17 mediates ACE2 shedding. SARS-CoV S glycoprotein activates cellular TACE and consequently facilitates virus entry. Soluble ACE2 as the N-terminal carboxypeptidase domain form is derived from the original ACE2 form by an ADAM17 metalloprotease in the membrane [89]. ADAM17 is indeed an enzyme that can convert membrane type pro-TNF-α to soluble TNF-α, a functional proinflammatory cytokine. Therefore, ADAM17 inhibition indicates an anti-inflammatory response and ADAM17 inhibitors are promising candidates for TNF-α-induced inflammatory diseases. The short C-terminal domain of ACE2 is removed by ADAM17 and TMPRSS2. However, TMPRSS2 cleaves ACE2 competitively with the ADAM17 metalloprotease. SARS-S protein-ACE2 binding leads to ADAM17/TNF-α-converting enzyme (TACE)-cleavage of ACE2, facilitating extracellular ACE2 shedding and consequent SARS-CoV entry into host cells [90,91]. Only TMPRSS2 cleavage allows SARS-CoV entry into host cells through endocytosis and fusion. Soluble ACE2 also recognizes the virus and prevents SARS-CoV-2 infection. SARS-CoV-2 infection requires membrane ACE2 and TMPRSS2. The ACE2–B0AT1 complex binds to the S glycoprotein of SARS-CoV-2. Intestinal membrane ACE2 and lung TMPRSS2-shedded ACE2 can act as alternative entry sites for SARS-CoV-2. SARS-CoV-2 infects the lungs and intestine via TMPRSS2-cleaved ACE2. If TMPRSS2 is engaged in SARS-CoV-2 entry and ACE2 downregulation, TMPRSS2 inhibition would lead to COVID-19 prevention. Although ACE2 is expressed both in type I and type II lung alveolar epithelial cells, SARS-CoV and SARS-CoV-2 target only type II epithelial cells due to the ACE2–TMPRSS2 interaction. Therefore, supplementation of ACE2 (soluble ACE2) or Ang-1 to Ang-7 should be a way to reduce SARS-CoV-2-related symptoms."}

LitCovid-PD-MONDO

LitCovid-PD-CLO

LitCovid-PD-CHEBI

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T52126","span":{"begin":59,"end":61},"obj":"Chemical"},{"id":"T21109","span":{"begin":101,"end":109},"obj":"Chemical"},{"id":"T46115","span":{"begin":312,"end":324},"obj":"Chemical"},{"id":"T4","span":{"begin":746,"end":756},"obj":"Chemical"},{"id":"T5","span":{"begin":977,"end":984},"obj":"Chemical"},{"id":"T6","span":{"begin":1420,"end":1432},"obj":"Chemical"},{"id":"T7","span":{"begin":1795,"end":1797},"obj":"Chemical"},{"id":"T77723","span":{"begin":1871,"end":1873},"obj":"Chemical"}],"attributes":[{"id":"A93838","pred":"chebi_id","subj":"T52126","obj":"http://purl.obolibrary.org/obo/CHEBI_27363"},{"id":"A4933","pred":"chebi_id","subj":"T21109","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A83274","pred":"chebi_id","subj":"T46115","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A94839","pred":"chebi_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CHEBI_35222"},{"id":"A31580","pred":"chebi_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A6598","pred":"chebi_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A66855","pred":"chebi_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CHEBI_74067"},{"id":"A57241","pred":"chebi_id","subj":"T77723","obj":"http://purl.obolibrary.org/obo/CHEBI_74067"}],"text":"A disintegrin and metallopeptidase domain (ADAM) family of Zn-metalloproteinases belongs to membrane proteins. The well-known ADAM17 is a TNF-α-converting enzyme (TACE), called the sheddase for TNF-α. Other ADAM sheddase family members include ADAM9, ADAM10 and ADAM12. ADAM17 mediates ACE2 shedding. SARS-CoV S glycoprotein activates cellular TACE and consequently facilitates virus entry. Soluble ACE2 as the N-terminal carboxypeptidase domain form is derived from the original ACE2 form by an ADAM17 metalloprotease in the membrane [89]. ADAM17 is indeed an enzyme that can convert membrane type pro-TNF-α to soluble TNF-α, a functional proinflammatory cytokine. Therefore, ADAM17 inhibition indicates an anti-inflammatory response and ADAM17 inhibitors are promising candidates for TNF-α-induced inflammatory diseases. The short C-terminal domain of ACE2 is removed by ADAM17 and TMPRSS2. However, TMPRSS2 cleaves ACE2 competitively with the ADAM17 metalloprotease. SARS-S protein-ACE2 binding leads to ADAM17/TNF-α-converting enzyme (TACE)-cleavage of ACE2, facilitating extracellular ACE2 shedding and consequent SARS-CoV entry into host cells [90,91]. Only TMPRSS2 cleavage allows SARS-CoV entry into host cells through endocytosis and fusion. Soluble ACE2 also recognizes the virus and prevents SARS-CoV-2 infection. SARS-CoV-2 infection requires membrane ACE2 and TMPRSS2. The ACE2–B0AT1 complex binds to the S glycoprotein of SARS-CoV-2. Intestinal membrane ACE2 and lung TMPRSS2-shedded ACE2 can act as alternative entry sites for SARS-CoV-2. SARS-CoV-2 infects the lungs and intestine via TMPRSS2-cleaved ACE2. If TMPRSS2 is engaged in SARS-CoV-2 entry and ACE2 downregulation, TMPRSS2 inhibition would lead to COVID-19 prevention. Although ACE2 is expressed both in type I and type II lung alveolar epithelial cells, SARS-CoV and SARS-CoV-2 target only type II epithelial cells due to the ACE2–TMPRSS2 interaction. Therefore, supplementation of ACE2 (soluble ACE2) or Ang-1 to Ang-7 should be a way to reduce SARS-CoV-2-related symptoms."}

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T77","span":{"begin":708,"end":734},"obj":"http://purl.obolibrary.org/obo/GO_0050728"},{"id":"T78","span":{"begin":713,"end":734},"obj":"http://purl.obolibrary.org/obo/GO_0006954"},{"id":"T79","span":{"begin":1128,"end":1143},"obj":"http://purl.obolibrary.org/obo/GO_0044409"},{"id":"T80","span":{"begin":1197,"end":1212},"obj":"http://purl.obolibrary.org/obo/GO_0044409"},{"id":"T81","span":{"begin":1227,"end":1238},"obj":"http://purl.obolibrary.org/obo/GO_0006897"}],"text":"A disintegrin and metallopeptidase domain (ADAM) family of Zn-metalloproteinases belongs to membrane proteins. The well-known ADAM17 is a TNF-α-converting enzyme (TACE), called the sheddase for TNF-α. Other ADAM sheddase family members include ADAM9, ADAM10 and ADAM12. ADAM17 mediates ACE2 shedding. SARS-CoV S glycoprotein activates cellular TACE and consequently facilitates virus entry. Soluble ACE2 as the N-terminal carboxypeptidase domain form is derived from the original ACE2 form by an ADAM17 metalloprotease in the membrane [89]. ADAM17 is indeed an enzyme that can convert membrane type pro-TNF-α to soluble TNF-α, a functional proinflammatory cytokine. Therefore, ADAM17 inhibition indicates an anti-inflammatory response and ADAM17 inhibitors are promising candidates for TNF-α-induced inflammatory diseases. The short C-terminal domain of ACE2 is removed by ADAM17 and TMPRSS2. However, TMPRSS2 cleaves ACE2 competitively with the ADAM17 metalloprotease. SARS-S protein-ACE2 binding leads to ADAM17/TNF-α-converting enzyme (TACE)-cleavage of ACE2, facilitating extracellular ACE2 shedding and consequent SARS-CoV entry into host cells [90,91]. Only TMPRSS2 cleavage allows SARS-CoV entry into host cells through endocytosis and fusion. Soluble ACE2 also recognizes the virus and prevents SARS-CoV-2 infection. SARS-CoV-2 infection requires membrane ACE2 and TMPRSS2. The ACE2–B0AT1 complex binds to the S glycoprotein of SARS-CoV-2. Intestinal membrane ACE2 and lung TMPRSS2-shedded ACE2 can act as alternative entry sites for SARS-CoV-2. SARS-CoV-2 infects the lungs and intestine via TMPRSS2-cleaved ACE2. If TMPRSS2 is engaged in SARS-CoV-2 entry and ACE2 downregulation, TMPRSS2 inhibition would lead to COVID-19 prevention. Although ACE2 is expressed both in type I and type II lung alveolar epithelial cells, SARS-CoV and SARS-CoV-2 target only type II epithelial cells due to the ACE2–TMPRSS2 interaction. Therefore, supplementation of ACE2 (soluble ACE2) or Ang-1 to Ang-7 should be a way to reduce SARS-CoV-2-related symptoms."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T466","span":{"begin":0,"end":110},"obj":"Sentence"},{"id":"T467","span":{"begin":111,"end":200},"obj":"Sentence"},{"id":"T468","span":{"begin":201,"end":269},"obj":"Sentence"},{"id":"T469","span":{"begin":270,"end":300},"obj":"Sentence"},{"id":"T470","span":{"begin":301,"end":390},"obj":"Sentence"},{"id":"T471","span":{"begin":391,"end":540},"obj":"Sentence"},{"id":"T472","span":{"begin":541,"end":665},"obj":"Sentence"},{"id":"T473","span":{"begin":666,"end":822},"obj":"Sentence"},{"id":"T474","span":{"begin":823,"end":892},"obj":"Sentence"},{"id":"T475","span":{"begin":893,"end":969},"obj":"Sentence"},{"id":"T476","span":{"begin":970,"end":1158},"obj":"Sentence"},{"id":"T477","span":{"begin":1159,"end":1250},"obj":"Sentence"},{"id":"T478","span":{"begin":1251,"end":1324},"obj":"Sentence"},{"id":"T479","span":{"begin":1325,"end":1381},"obj":"Sentence"},{"id":"T480","span":{"begin":1382,"end":1447},"obj":"Sentence"},{"id":"T481","span":{"begin":1448,"end":1553},"obj":"Sentence"},{"id":"T482","span":{"begin":1554,"end":1622},"obj":"Sentence"},{"id":"T483","span":{"begin":1623,"end":1743},"obj":"Sentence"},{"id":"T484","span":{"begin":1744,"end":1927},"obj":"Sentence"},{"id":"T485","span":{"begin":1928,"end":2050},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"A disintegrin and metallopeptidase domain (ADAM) family of Zn-metalloproteinases belongs to membrane proteins. The well-known ADAM17 is a TNF-α-converting enzyme (TACE), called the sheddase for TNF-α. Other ADAM sheddase family members include ADAM9, ADAM10 and ADAM12. ADAM17 mediates ACE2 shedding. SARS-CoV S glycoprotein activates cellular TACE and consequently facilitates virus entry. Soluble ACE2 as the N-terminal carboxypeptidase domain form is derived from the original ACE2 form by an ADAM17 metalloprotease in the membrane [89]. ADAM17 is indeed an enzyme that can convert membrane type pro-TNF-α to soluble TNF-α, a functional proinflammatory cytokine. Therefore, ADAM17 inhibition indicates an anti-inflammatory response and ADAM17 inhibitors are promising candidates for TNF-α-induced inflammatory diseases. The short C-terminal domain of ACE2 is removed by ADAM17 and TMPRSS2. However, TMPRSS2 cleaves ACE2 competitively with the ADAM17 metalloprotease. SARS-S protein-ACE2 binding leads to ADAM17/TNF-α-converting enzyme (TACE)-cleavage of ACE2, facilitating extracellular ACE2 shedding and consequent SARS-CoV entry into host cells [90,91]. Only TMPRSS2 cleavage allows SARS-CoV entry into host cells through endocytosis and fusion. Soluble ACE2 also recognizes the virus and prevents SARS-CoV-2 infection. SARS-CoV-2 infection requires membrane ACE2 and TMPRSS2. The ACE2–B0AT1 complex binds to the S glycoprotein of SARS-CoV-2. Intestinal membrane ACE2 and lung TMPRSS2-shedded ACE2 can act as alternative entry sites for SARS-CoV-2. SARS-CoV-2 infects the lungs and intestine via TMPRSS2-cleaved ACE2. If TMPRSS2 is engaged in SARS-CoV-2 entry and ACE2 downregulation, TMPRSS2 inhibition would lead to COVID-19 prevention. Although ACE2 is expressed both in type I and type II lung alveolar epithelial cells, SARS-CoV and SARS-CoV-2 target only type II epithelial cells due to the ACE2–TMPRSS2 interaction. Therefore, supplementation of ACE2 (soluble ACE2) or Ang-1 to Ang-7 should be a way to reduce SARS-CoV-2-related symptoms."}

2_test

{"project":"2_test","denotations":[{"id":"32604730-10924499-51944047","span":{"begin":536,"end":538},"obj":"10924499"},{"id":"32604730-24227843-51944048","span":{"begin":1151,"end":1153},"obj":"24227843"},{"id":"32604730-19995578-51944049","span":{"begin":1154,"end":1156},"obj":"19995578"},{"id":"T58896","span":{"begin":536,"end":538},"obj":"10924499"},{"id":"T39582","span":{"begin":1151,"end":1153},"obj":"24227843"},{"id":"T57089","span":{"begin":1154,"end":1156},"obj":"19995578"}],"text":"A disintegrin and metallopeptidase domain (ADAM) family of Zn-metalloproteinases belongs to membrane proteins. The well-known ADAM17 is a TNF-α-converting enzyme (TACE), called the sheddase for TNF-α. Other ADAM sheddase family members include ADAM9, ADAM10 and ADAM12. ADAM17 mediates ACE2 shedding. SARS-CoV S glycoprotein activates cellular TACE and consequently facilitates virus entry. Soluble ACE2 as the N-terminal carboxypeptidase domain form is derived from the original ACE2 form by an ADAM17 metalloprotease in the membrane [89]. ADAM17 is indeed an enzyme that can convert membrane type pro-TNF-α to soluble TNF-α, a functional proinflammatory cytokine. Therefore, ADAM17 inhibition indicates an anti-inflammatory response and ADAM17 inhibitors are promising candidates for TNF-α-induced inflammatory diseases. The short C-terminal domain of ACE2 is removed by ADAM17 and TMPRSS2. However, TMPRSS2 cleaves ACE2 competitively with the ADAM17 metalloprotease. SARS-S protein-ACE2 binding leads to ADAM17/TNF-α-converting enzyme (TACE)-cleavage of ACE2, facilitating extracellular ACE2 shedding and consequent SARS-CoV entry into host cells [90,91]. Only TMPRSS2 cleavage allows SARS-CoV entry into host cells through endocytosis and fusion. Soluble ACE2 also recognizes the virus and prevents SARS-CoV-2 infection. SARS-CoV-2 infection requires membrane ACE2 and TMPRSS2. The ACE2–B0AT1 complex binds to the S glycoprotein of SARS-CoV-2. Intestinal membrane ACE2 and lung TMPRSS2-shedded ACE2 can act as alternative entry sites for SARS-CoV-2. SARS-CoV-2 infects the lungs and intestine via TMPRSS2-cleaved ACE2. If TMPRSS2 is engaged in SARS-CoV-2 entry and ACE2 downregulation, TMPRSS2 inhibition would lead to COVID-19 prevention. Although ACE2 is expressed both in type I and type II lung alveolar epithelial cells, SARS-CoV and SARS-CoV-2 target only type II epithelial cells due to the ACE2–TMPRSS2 interaction. Therefore, supplementation of ACE2 (soluble ACE2) or Ang-1 to Ang-7 should be a way to reduce SARS-CoV-2-related symptoms."}

PMC:7352545 / 48153-50203 JSONTXT

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PMC:7352545 / 48153-50203 JSON TXT