PMC:7556165 / 69222-70499 JSONTXT

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T191","span":{"begin":234,"end":242},"obj":"Chemical"},{"id":"T192","span":{"begin":498,"end":536},"obj":"Chemical"},{"id":"T193","span":{"begin":845,"end":852},"obj":"Chemical"}],"attributes":[{"id":"A192","pred":"chebi_id","subj":"T192","obj":"http://purl.obolibrary.org/obo/CHEBI_145998"},{"id":"A193","pred":"chebi_id","subj":"T193","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A191","pred":"chebi_id","subj":"T191","obj":"http://purl.obolibrary.org/obo/CHEBI_16670"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T386","span":{"begin":411,"end":419},"obj":"Species"},{"id":"T387","span":{"begin":411,"end":415},"obj":"Species"},{"id":"T388","span":{"begin":633,"end":641},"obj":"Species"},{"id":"T389","span":{"begin":633,"end":637},"obj":"Species"},{"id":"T390","span":{"begin":936,"end":940},"obj":"Species"},{"id":"T391","span":{"begin":1091,"end":1107},"obj":"Species"},{"id":"T392","span":{"begin":1091,"end":1095},"obj":"Species"}],"attributes":[{"id":"A386","pred":"ncbi_taxonomy_id","subj":"T386","obj":"NCBItxid:694009"},{"id":"A387","pred":"ncbi_taxonomy_id","subj":"T387","obj":"NCBItxid:694009"},{"id":"A391","pred":"ncbi_taxonomy_id","subj":"T391","obj":"NCBItxid:694009"},{"id":"A389","pred":"ncbi_taxonomy_id","subj":"T389","obj":"NCBItxid:694009"},{"id":"A392","pred":"ncbi_taxonomy_id","subj":"T392","obj":"NCBItxid:694009"},{"id":"A390","pred":"ncbi_taxonomy_id","subj":"T390","obj":"NCBItxid:694009"},{"id":"A388","pred":"ncbi_taxonomy_id","subj":"T388","obj":"NCBItxid:694009"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T412","span":{"begin":0,"end":13},"obj":"Sentence"},{"id":"T413","span":{"begin":14,"end":264},"obj":"Sentence"},{"id":"T414","span":{"begin":265,"end":453},"obj":"Sentence"},{"id":"T415","span":{"begin":454,"end":781},"obj":"Sentence"},{"id":"T416","span":{"begin":782,"end":980},"obj":"Sentence"},{"id":"T417","span":{"begin":981,"end":1277},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-sample-PD-UBERON","denotations":[{"id":"T149","span":{"begin":1060,"end":1064},"obj":"Body_part"}],"attributes":[{"id":"A149","pred":"uberon_id","subj":"T149","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"1891","span":{"begin":0,"end":4},"obj":"Gene"},{"id":"1907","span":{"begin":26,"end":30},"obj":"Gene"},{"id":"1908","span":{"begin":550,"end":554},"obj":"Gene"},{"id":"1909","span":{"begin":802,"end":806},"obj":"Gene"},{"id":"1910","span":{"begin":908,"end":912},"obj":"Gene"},{"id":"1911","span":{"begin":1018,"end":1022},"obj":"Gene"},{"id":"1912","span":{"begin":1207,"end":1211},"obj":"Gene"},{"id":"1913","span":{"begin":411,"end":419},"obj":"Species"},{"id":"1914","span":{"begin":633,"end":641},"obj":"Species"},{"id":"1915","span":{"begin":1091,"end":1107},"obj":"Species"},{"id":"1916","span":{"begin":843,"end":852},"obj":"Gene"},{"id":"1917","span":{"begin":498,"end":536},"obj":"Chemical"},{"id":"1918","span":{"begin":538,"end":542},"obj":"Chemical"},{"id":"1919","span":{"begin":869,"end":873},"obj":"Chemical"},{"id":"1920","span":{"begin":1054,"end":1071},"obj":"Disease"},{"id":"1921","span":{"begin":1075,"end":1085},"obj":"Disease"}],"attributes":[{"id":"A1908","pred":"pubann:denotes","subj":"1908","obj":"Gene:59272"},{"id":"A1913","pred":"pubann:denotes","subj":"1913","obj":"Tax:694009"},{"id":"A1911","pred":"pubann:denotes","subj":"1911","obj":"Gene:59272"},{"id":"A1921","pred":"pubann:denotes","subj":"1921","obj":"MESH:D007239"},{"id":"A1891","pred":"pubann:denotes","subj":"1891","obj":"Gene:59272"},{"id":"A1914","pred":"pubann:denotes","subj":"1914","obj":"Tax:694009"},{"id":"A1909","pred":"pubann:denotes","subj":"1909","obj":"Gene:59272"},{"id":"A1912","pred":"pubann:denotes","subj":"1912","obj":"Gene:59272"},{"id":"A1910","pred":"pubann:denotes","subj":"1910","obj":"Gene:59272"},{"id":"A1907","pred":"pubann:denotes","subj":"1907","obj":"Gene:59272"},{"id":"A1916","pred":"pubann:denotes","subj":"1916","obj":"Gene:43740568"},{"id":"A1920","pred":"pubann:denotes","subj":"1920","obj":"MESH:D055371"},{"id":"A1915","pred":"pubann:denotes","subj":"1915","obj":"Tax:694009"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T6161","span":{"begin":0,"end":4},"obj":"Protein"},{"id":"T6162","span":{"begin":26,"end":30},"obj":"Protein"},{"id":"T6163","span":{"begin":550,"end":554},"obj":"Protein"},{"id":"T6164","span":{"begin":802,"end":806},"obj":"Protein"},{"id":"T6165","span":{"begin":843,"end":852},"obj":"Protein"},{"id":"T6176","span":{"begin":908,"end":912},"obj":"Protein"},{"id":"T6177","span":{"begin":1018,"end":1022},"obj":"Protein"},{"id":"T6178","span":{"begin":1207,"end":1211},"obj":"Protein"}],"attributes":[{"id":"A6161","pred":"uniprot_id","subj":"T6161","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"},{"id":"A6162","pred":"uniprot_id","subj":"T6162","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"},{"id":"A6163","pred":"uniprot_id","subj":"T6163","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"},{"id":"A6164","pred":"uniprot_id","subj":"T6164","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"},{"id":"A6165","pred":"uniprot_id","subj":"T6165","obj":"https://www.uniprot.org/uniprot/Q9D080"},{"id":"A6166","pred":"uniprot_id","subj":"T6165","obj":"https://www.uniprot.org/uniprot/Q9BSH7"},{"id":"A6167","pred":"uniprot_id","subj":"T6165","obj":"https://www.uniprot.org/uniprot/Q91X32"},{"id":"A6168","pred":"uniprot_id","subj":"T6165","obj":"https://www.uniprot.org/uniprot/Q8VII4"},{"id":"A6169","pred":"uniprot_id","subj":"T6165","obj":"https://www.uniprot.org/uniprot/Q5SYG4"},{"id":"A6170","pred":"uniprot_id","subj":"T6165","obj":"https://www.uniprot.org/uniprot/P48819"},{"id":"A6171","pred":"uniprot_id","subj":"T6165","obj":"https://www.uniprot.org/uniprot/P29788"},{"id":"A6172","pred":"uniprot_id","subj":"T6165","obj":"https://www.uniprot.org/uniprot/P22458"},{"id":"A6173","pred":"uniprot_id","subj":"T6165","obj":"https://www.uniprot.org/uniprot/P04004"},{"id":"A6174","pred":"uniprot_id","subj":"T6165","obj":"https://www.uniprot.org/uniprot/P01141"},{"id":"A6175","pred":"uniprot_id","subj":"T6165","obj":"https://www.uniprot.org/uniprot/B2R7G0"},{"id":"A6176","pred":"uniprot_id","subj":"T6176","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"},{"id":"A6177","pred":"uniprot_id","subj":"T6177","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"},{"id":"A6178","pred":"uniprot_id","subj":"T6178","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T279","span":{"begin":562,"end":566},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T280","span":{"begin":738,"end":742},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T281","span":{"begin":743,"end":747},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T282","span":{"begin":817,"end":821},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T283","span":{"begin":1040,"end":1045},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T284","span":{"begin":1075,"end":1085},"obj":"http://purl.obolibrary.org/obo/IDO_0000586"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T452","span":{"begin":738,"end":742},"obj":"Body_part"},{"id":"T453","span":{"begin":743,"end":747},"obj":"Body_part"},{"id":"T454","span":{"begin":845,"end":852},"obj":"Body_part"},{"id":"T455","span":{"begin":1060,"end":1064},"obj":"Body_part"}],"attributes":[{"id":"A455","pred":"fma_id","subj":"T455","obj":"http://purl.org/sig/ont/fma/fma7195"},{"id":"A453","pred":"fma_id","subj":"T453","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A452","pred":"fma_id","subj":"T452","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A454","pred":"fma_id","subj":"T454","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T407","span":{"begin":411,"end":419},"obj":"Disease"},{"id":"T408","span":{"begin":411,"end":415},"obj":"Disease"},{"id":"T409","span":{"begin":633,"end":641},"obj":"Disease"},{"id":"T410","span":{"begin":633,"end":637},"obj":"Disease"},{"id":"T411","span":{"begin":936,"end":940},"obj":"Disease"},{"id":"T412","span":{"begin":1054,"end":1071},"obj":"Disease"},{"id":"T414","span":{"begin":1075,"end":1085},"obj":"Disease"},{"id":"T415","span":{"begin":1091,"end":1095},"obj":"Disease"}],"attributes":[{"id":"A409","pred":"mondo_id","subj":"T409","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A414","pred":"mondo_id","subj":"T414","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A415","pred":"mondo_id","subj":"T415","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A407","pred":"mondo_id","subj":"T407","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A412","pred":"mondo_id","subj":"T412","obj":"http://purl.obolibrary.org/obo/MONDO_0006502"},{"id":"A413","pred":"mondo_id","subj":"T412","obj":"http://purl.obolibrary.org/obo/MONDO_0015796"},{"id":"A408","pred":"mondo_id","subj":"T408","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A410","pred":"mondo_id","subj":"T410","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A411","pred":"mondo_id","subj":"T411","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-sample-PD-MAT","denotations":[{"id":"T135","span":{"begin":1060,"end":1064},"obj":"http://purl.obolibrary.org/obo/MAT_0000135"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T147","span":{"begin":738,"end":754},"obj":"http://purl.obolibrary.org/obo/GO_0000768"},{"id":"T148","span":{"begin":738,"end":754},"obj":"http://purl.obolibrary.org/obo/GO_0045026"},{"id":"T149","span":{"begin":743,"end":754},"obj":"http://purl.obolibrary.org/obo/GO_0000747"},{"id":"T150","span":{"begin":913,"end":931},"obj":"http://purl.obolibrary.org/obo/GO_0003824"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T152","span":{"begin":738,"end":754},"obj":"http://purl.obolibrary.org/obo/GO_0140253"},{"id":"T153","span":{"begin":738,"end":754},"obj":"http://purl.obolibrary.org/obo/GO_0045026"},{"id":"T154","span":{"begin":743,"end":754},"obj":"http://purl.obolibrary.org/obo/GO_0000768"},{"id":"T155","span":{"begin":743,"end":754},"obj":"http://purl.obolibrary.org/obo/GO_0000747"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-PD-HP","denotations":[{"id":"T77","span":{"begin":1054,"end":1071},"obj":"Phenotype"}],"attributes":[{"id":"A77","pred":"hp_id","subj":"T77","obj":"http://www.orpha.net/ORDO/Orphanet_178320"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-PubTator","denotations":[{"id":"1891","span":{"begin":0,"end":4},"obj":"Gene"},{"id":"1907","span":{"begin":26,"end":30},"obj":"Gene"},{"id":"1908","span":{"begin":550,"end":554},"obj":"Gene"},{"id":"1909","span":{"begin":802,"end":806},"obj":"Gene"},{"id":"1910","span":{"begin":908,"end":912},"obj":"Gene"},{"id":"1911","span":{"begin":1018,"end":1022},"obj":"Gene"},{"id":"1912","span":{"begin":1207,"end":1211},"obj":"Gene"},{"id":"1913","span":{"begin":411,"end":419},"obj":"Species"},{"id":"1914","span":{"begin":633,"end":641},"obj":"Species"},{"id":"1915","span":{"begin":1091,"end":1107},"obj":"Species"},{"id":"1916","span":{"begin":843,"end":852},"obj":"Gene"},{"id":"1917","span":{"begin":498,"end":536},"obj":"Chemical"},{"id":"1918","span":{"begin":538,"end":542},"obj":"Chemical"},{"id":"1919","span":{"begin":869,"end":873},"obj":"Chemical"},{"id":"1920","span":{"begin":1054,"end":1071},"obj":"Disease"},{"id":"1921","span":{"begin":1075,"end":1085},"obj":"Disease"}],"attributes":[{"id":"A1891","pred":"tao:has_database_id","subj":"1891","obj":"Gene:59272"},{"id":"A1907","pred":"tao:has_database_id","subj":"1907","obj":"Gene:59272"},{"id":"A1908","pred":"tao:has_database_id","subj":"1908","obj":"Gene:59272"},{"id":"A1909","pred":"tao:has_database_id","subj":"1909","obj":"Gene:59272"},{"id":"A1910","pred":"tao:has_database_id","subj":"1910","obj":"Gene:59272"},{"id":"A1911","pred":"tao:has_database_id","subj":"1911","obj":"Gene:59272"},{"id":"A1912","pred":"tao:has_database_id","subj":"1912","obj":"Gene:59272"},{"id":"A1913","pred":"tao:has_database_id","subj":"1913","obj":"Tax:694009"},{"id":"A1914","pred":"tao:has_database_id","subj":"1914","obj":"Tax:694009"},{"id":"A1915","pred":"tao:has_database_id","subj":"1915","obj":"Tax:694009"},{"id":"A1916","pred":"tao:has_database_id","subj":"1916","obj":"Gene:43740568"},{"id":"A1920","pred":"tao:has_database_id","subj":"1920","obj":"MESH:D055371"},{"id":"A1921","pred":"tao:has_database_id","subj":"1921","obj":"MESH:D007239"}],"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 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}

{"project":"LitCovid-sentences","denotations":[{"id":"T412","span":{"begin":0,"end":13},"obj":"Sentence"},{"id":"T413","span":{"begin":14,"end":264},"obj":"Sentence"},{"id":"T414","span":{"begin":265,"end":453},"obj":"Sentence"},{"id":"T415","span":{"begin":454,"end":781},"obj":"Sentence"},{"id":"T416","span":{"begin":782,"end":980},"obj":"Sentence"},{"id":"T417","span":{"begin":981,"end":1277},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"ACE2 Blockers\nBlockade of ACE2 receptor could be achieved through specific antibodies (Li et al., 2003), rationally designed small molecules (Dales et al., 2002; Huentelman et al., 2004; Gross et al., 2020; Pillaiyar et al., 2020) or peptides (Huang et al., 2003). Although their efficacy needs to be confirmed, some of these agents are currently available on the market and have been show to effectively block SARS-CoV invasion (Li S.-R. et al., 2020). For instance, the small synthetic inhibitor N-(2-aminoethyl)-1aziridine-ethanamine (NAAE) binds ACE2 active site in its closed conformation; this contact triggers the shifting of SARS-CoV S binding residues preventing the molecular interaction with targeted enzyme and the subsequent cell-cell fusion (Huentelman et al., 2004). Therefore, although ACE2 catalytic site is distinct from the S-protein-binding domain, NAAE exerts dual inhibitory effects on ACE2 catalytic activity and SARS binding (Adedeji and Sarafianos, 2014). However, since a protecting role for ACE2 receptor against virus-induced acute lung injury in infections with SARS coronavirus has not been excluded (Imai et al., 2005; Kuba et al., 2005; Li S.-R. et al., 2020), the choice of ACE2 inhibition as therapeutic approach should be carefully evaluated."}