PMC:7346000 / 3907-4984 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T2","span":{"begin":245,"end":261},"obj":"Body_part"},{"id":"T3","span":{"begin":256,"end":261},"obj":"Body_part"},{"id":"T4","span":{"begin":274,"end":285},"obj":"Body_part"},{"id":"T5","span":{"begin":320,"end":327},"obj":"Body_part"},{"id":"T6","span":{"begin":501,"end":508},"obj":"Body_part"},{"id":"T7","span":{"begin":564,"end":568},"obj":"Body_part"},{"id":"T8","span":{"begin":697,"end":701},"obj":"Body_part"},{"id":"T9","span":{"begin":920,"end":925},"obj":"Body_part"}],"attributes":[{"id":"A2","pred":"fma_id","subj":"T2","obj":"http://purl.org/sig/ont/fma/fma66768"},{"id":"A3","pred":"fma_id","subj":"T3","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A4","pred":"fma_id","subj":"T4","obj":"http://purl.org/sig/ont/fma/fma62499"},{"id":"A5","pred":"fma_id","subj":"T5","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A6","pred":"fma_id","subj":"T6","obj":"http://purl.org/sig/ont/fma/fma67257"},{"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/fma68646"}],"text":"Dissecting the complex pathogenesis of CAPA requires a molecular understanding of the physiological processes whereby infection with SARS-CoV-2 facilitates fungal pathogenesis. Similar to other SARS coronaviruses, SARS-CoV-2 targets and invades epithelial cells and type II pneumocytes through binding of the SARS spike protein to the angiotensin-converting enzyme 2 (ACE2) receptors [11]. Cleavage of the S1/S2 domain by the type 2 transmembrane protease TMPRSS2 leads to the activation of the spike protein [12], thereby facilitating viral entry into the target cell via ACE2. Besides its role as a SARS virus receptor, ACE2 was also demonstrated to be required for protection from severe acute lung injury in ARDS [13]. In support of this, an insertion/deletion polymorphism that affects ACE activity was associated with ARDS susceptibility and outcome [14]. Whether the preceding interaction of SARS-CoV-2 with host cells, by disrupting the regulation of the renin-angiotensin system and or the kallikrein-kinin system, contributes to the development of CAPA, is not known."}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T2","span":{"begin":697,"end":701},"obj":"Body_part"},{"id":"T3","span":{"begin":963,"end":987},"obj":"Body_part"}],"attributes":[{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0018229"}],"text":"Dissecting the complex pathogenesis of CAPA requires a molecular understanding of the physiological processes whereby infection with SARS-CoV-2 facilitates fungal pathogenesis. Similar to other SARS coronaviruses, SARS-CoV-2 targets and invades epithelial cells and type II pneumocytes through binding of the SARS spike protein to the angiotensin-converting enzyme 2 (ACE2) receptors [11]. Cleavage of the S1/S2 domain by the type 2 transmembrane protease TMPRSS2 leads to the activation of the spike protein [12], thereby facilitating viral entry into the target cell via ACE2. Besides its role as a SARS virus receptor, ACE2 was also demonstrated to be required for protection from severe acute lung injury in ARDS [13]. In support of this, an insertion/deletion polymorphism that affects ACE activity was associated with ARDS susceptibility and outcome [14]. Whether the preceding interaction of SARS-CoV-2 with host cells, by disrupting the regulation of the renin-angiotensin system and or the kallikrein-kinin system, contributes to the development of CAPA, is not known."}

{"project":"LitCovid-PubTator","denotations":[{"id":"144","span":{"begin":335,"end":366},"obj":"Gene"},{"id":"145","span":{"begin":368,"end":372},"obj":"Gene"},{"id":"146","span":{"begin":456,"end":463},"obj":"Gene"},{"id":"147","span":{"begin":573,"end":577},"obj":"Gene"},{"id":"148","span":{"begin":622,"end":626},"obj":"Gene"},{"id":"149","span":{"begin":791,"end":794},"obj":"Gene"},{"id":"150","span":{"begin":999,"end":1009},"obj":"Gene"},{"id":"151","span":{"begin":133,"end":143},"obj":"Species"},{"id":"152","span":{"begin":194,"end":212},"obj":"Species"},{"id":"153","span":{"begin":214,"end":224},"obj":"Species"},{"id":"154","span":{"begin":601,"end":611},"obj":"Species"},{"id":"155","span":{"begin":899,"end":909},"obj":"Species"},{"id":"156","span":{"begin":118,"end":127},"obj":"Disease"},{"id":"157","span":{"begin":697,"end":708},"obj":"Disease"},{"id":"158","span":{"begin":712,"end":716},"obj":"Disease"},{"id":"159","span":{"begin":824,"end":828},"obj":"Disease"}],"attributes":[{"id":"A144","pred":"tao:has_database_id","subj":"144","obj":"Gene:59272"},{"id":"A145","pred":"tao:has_database_id","subj":"145","obj":"Gene:59272"},{"id":"A146","pred":"tao:has_database_id","subj":"146","obj":"Gene:7113"},{"id":"A147","pred":"tao:has_database_id","subj":"147","obj":"Gene:59272"},{"id":"A148","pred":"tao:has_database_id","subj":"148","obj":"Gene:59272"},{"id":"A149","pred":"tao:has_database_id","subj":"149","obj":"Gene:1636"},{"id":"A150","pred":"tao:has_database_id","subj":"150","obj":"Gene:9622"},{"id":"A151","pred":"tao:has_database_id","subj":"151","obj":"Tax:2697049"},{"id":"A152","pred":"tao:has_database_id","subj":"152","obj":"Tax:694009"},{"id":"A153","pred":"tao:has_database_id","subj":"153","obj":"Tax:2697049"},{"id":"A154","pred":"tao:has_database_id","subj":"154","obj":"Tax:694009"},{"id":"A155","pred":"tao:has_database_id","subj":"155","obj":"Tax:2697049"},{"id":"A156","pred":"tao:has_database_id","subj":"156","obj":"MESH:D007239"},{"id":"A157","pred":"tao:has_database_id","subj":"157","obj":"MESH:D055370"},{"id":"A158","pred":"tao:has_database_id","subj":"158","obj":"MESH:D012128"},{"id":"A159","pred":"tao:has_database_id","subj":"159","obj":"MESH:D012128"}],"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":"Dissecting the complex pathogenesis of CAPA requires a molecular understanding of the physiological processes whereby infection with SARS-CoV-2 facilitates fungal pathogenesis. Similar to other SARS coronaviruses, SARS-CoV-2 targets and invades epithelial cells and type II pneumocytes through binding of the SARS spike protein to the angiotensin-converting enzyme 2 (ACE2) receptors [11]. Cleavage of the S1/S2 domain by the type 2 transmembrane protease TMPRSS2 leads to the activation of the spike protein [12], thereby facilitating viral entry into the target cell via ACE2. Besides its role as a SARS virus receptor, ACE2 was also demonstrated to be required for protection from severe acute lung injury in ARDS [13]. In support of this, an insertion/deletion polymorphism that affects ACE activity was associated with ARDS susceptibility and outcome [14]. Whether the preceding interaction of SARS-CoV-2 with host cells, by disrupting the regulation of the renin-angiotensin system and or the kallikrein-kinin system, contributes to the development of CAPA, is not known."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T52","span":{"begin":39,"end":43},"obj":"Disease"},{"id":"T53","span":{"begin":118,"end":127},"obj":"Disease"},{"id":"T54","span":{"begin":133,"end":141},"obj":"Disease"},{"id":"T55","span":{"begin":194,"end":198},"obj":"Disease"},{"id":"T56","span":{"begin":214,"end":222},"obj":"Disease"},{"id":"T57","span":{"begin":309,"end":313},"obj":"Disease"},{"id":"T58","span":{"begin":601,"end":605},"obj":"Disease"},{"id":"T59","span":{"begin":691,"end":708},"obj":"Disease"},{"id":"T61","span":{"begin":702,"end":708},"obj":"Disease"},{"id":"T62","span":{"begin":712,"end":716},"obj":"Disease"},{"id":"T63","span":{"begin":824,"end":828},"obj":"Disease"},{"id":"T64","span":{"begin":899,"end":907},"obj":"Disease"},{"id":"T65","span":{"begin":1058,"end":1062},"obj":"Disease"}],"attributes":[{"id":"A52","pred":"mondo_id","subj":"T52","obj":"http://purl.obolibrary.org/obo/MONDO_0007163"},{"id":"A53","pred":"mondo_id","subj":"T53","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A54","pred":"mondo_id","subj":"T54","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A55","pred":"mondo_id","subj":"T55","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A56","pred":"mondo_id","subj":"T56","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A57","pred":"mondo_id","subj":"T57","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A58","pred":"mondo_id","subj":"T58","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A59","pred":"mondo_id","subj":"T59","obj":"http://purl.obolibrary.org/obo/MONDO_0006502"},{"id":"A60","pred":"mondo_id","subj":"T59","obj":"http://purl.obolibrary.org/obo/MONDO_0015796"},{"id":"A61","pred":"mondo_id","subj":"T61","obj":"http://purl.obolibrary.org/obo/MONDO_0021178"},{"id":"A62","pred":"mondo_id","subj":"T62","obj":"http://purl.obolibrary.org/obo/MONDO_0006502"},{"id":"A63","pred":"mondo_id","subj":"T63","obj":"http://purl.obolibrary.org/obo/MONDO_0006502"},{"id":"A64","pred":"mondo_id","subj":"T64","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A65","pred":"mondo_id","subj":"T65","obj":"http://purl.obolibrary.org/obo/MONDO_0007163"}],"text":"Dissecting the complex pathogenesis of CAPA requires a molecular understanding of the physiological processes whereby infection with SARS-CoV-2 facilitates fungal pathogenesis. Similar to other SARS coronaviruses, SARS-CoV-2 targets and invades epithelial cells and type II pneumocytes through binding of the SARS spike protein to the angiotensin-converting enzyme 2 (ACE2) receptors [11]. Cleavage of the S1/S2 domain by the type 2 transmembrane protease TMPRSS2 leads to the activation of the spike protein [12], thereby facilitating viral entry into the target cell via ACE2. Besides its role as a SARS virus receptor, ACE2 was also demonstrated to be required for protection from severe acute lung injury in ARDS [13]. In support of this, an insertion/deletion polymorphism that affects ACE activity was associated with ARDS susceptibility and outcome [14]. Whether the preceding interaction of SARS-CoV-2 with host cells, by disrupting the regulation of the renin-angiotensin system and or the kallikrein-kinin system, contributes to the development of CAPA, is not known."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T22","span":{"begin":53,"end":54},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T23","span":{"begin":245,"end":255},"obj":"http://purl.obolibrary.org/obo/CL_0000066"},{"id":"T24","span":{"begin":256,"end":270},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T25","span":{"begin":385,"end":387},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T26","span":{"begin":406,"end":408},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T27","span":{"begin":409,"end":411},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T28","span":{"begin":409,"end":411},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"},{"id":"T29","span":{"begin":477,"end":487},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T30","span":{"begin":564,"end":568},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T31","span":{"begin":599,"end":600},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T32","span":{"begin":606,"end":611},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T33","span":{"begin":697,"end":701},"obj":"http://purl.obolibrary.org/obo/UBERON_0002048"},{"id":"T34","span":{"begin":697,"end":701},"obj":"http://www.ebi.ac.uk/efo/EFO_0000934"},{"id":"T35","span":{"begin":795,"end":803},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T36","span":{"begin":920,"end":925},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Dissecting the complex pathogenesis of CAPA requires a molecular understanding of the physiological processes whereby infection with SARS-CoV-2 facilitates fungal pathogenesis. Similar to other SARS coronaviruses, SARS-CoV-2 targets and invades epithelial cells and type II pneumocytes through binding of the SARS spike protein to the angiotensin-converting enzyme 2 (ACE2) receptors [11]. Cleavage of the S1/S2 domain by the type 2 transmembrane protease TMPRSS2 leads to the activation of the spike protein [12], thereby facilitating viral entry into the target cell via ACE2. Besides its role as a SARS virus receptor, ACE2 was also demonstrated to be required for protection from severe acute lung injury in ARDS [13]. In support of this, an insertion/deletion polymorphism that affects ACE activity was associated with ARDS susceptibility and outcome [14]. Whether the preceding interaction of SARS-CoV-2 with host cells, by disrupting the regulation of the renin-angiotensin system and or the kallikrein-kinin system, contributes to the development of CAPA, is not known."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T20","span":{"begin":271,"end":273},"obj":"Chemical"},{"id":"T21","span":{"begin":320,"end":327},"obj":"Chemical"},{"id":"T22","span":{"begin":335,"end":346},"obj":"Chemical"},{"id":"T23","span":{"begin":409,"end":411},"obj":"Chemical"},{"id":"T24","span":{"begin":501,"end":508},"obj":"Chemical"},{"id":"T25","span":{"begin":969,"end":980},"obj":"Chemical"}],"attributes":[{"id":"A20","pred":"chebi_id","subj":"T20","obj":"http://purl.obolibrary.org/obo/CHEBI_74067"},{"id":"A21","pred":"chebi_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A22","pred":"chebi_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A23","pred":"chebi_id","subj":"T23","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A24","pred":"chebi_id","subj":"T24","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A25","pred":"chebi_id","subj":"T25","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"}],"text":"Dissecting the complex pathogenesis of CAPA requires a molecular understanding of the physiological processes whereby infection with SARS-CoV-2 facilitates fungal pathogenesis. Similar to other SARS coronaviruses, SARS-CoV-2 targets and invades epithelial cells and type II pneumocytes through binding of the SARS spike protein to the angiotensin-converting enzyme 2 (ACE2) receptors [11]. Cleavage of the S1/S2 domain by the type 2 transmembrane protease TMPRSS2 leads to the activation of the spike protein [12], thereby facilitating viral entry into the target cell via ACE2. Besides its role as a SARS virus receptor, ACE2 was also demonstrated to be required for protection from severe acute lung injury in ARDS [13]. In support of this, an insertion/deletion polymorphism that affects ACE activity was associated with ARDS susceptibility and outcome [14]. Whether the preceding interaction of SARS-CoV-2 with host cells, by disrupting the regulation of the renin-angiotensin system and or the kallikrein-kinin system, contributes to the development of CAPA, is not known."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T3","span":{"begin":23,"end":35},"obj":"http://purl.obolibrary.org/obo/GO_0009405"},{"id":"T4","span":{"begin":163,"end":175},"obj":"http://purl.obolibrary.org/obo/GO_0009405"},{"id":"T5","span":{"begin":945,"end":955},"obj":"http://purl.obolibrary.org/obo/GO_0065007"}],"text":"Dissecting the complex pathogenesis of CAPA requires a molecular understanding of the physiological processes whereby infection with SARS-CoV-2 facilitates fungal pathogenesis. Similar to other SARS coronaviruses, SARS-CoV-2 targets and invades epithelial cells and type II pneumocytes through binding of the SARS spike protein to the angiotensin-converting enzyme 2 (ACE2) receptors [11]. Cleavage of the S1/S2 domain by the type 2 transmembrane protease TMPRSS2 leads to the activation of the spike protein [12], thereby facilitating viral entry into the target cell via ACE2. Besides its role as a SARS virus receptor, ACE2 was also demonstrated to be required for protection from severe acute lung injury in ARDS [13]. In support of this, an insertion/deletion polymorphism that affects ACE activity was associated with ARDS susceptibility and outcome [14]. Whether the preceding interaction of SARS-CoV-2 with host cells, by disrupting the regulation of the renin-angiotensin system and or the kallikrein-kinin system, contributes to the development of CAPA, is not known."}

{"project":"LitCovid-PD-HP","denotations":[{"id":"T13","span":{"begin":691,"end":708},"obj":"Phenotype"}],"attributes":[{"id":"A13","pred":"hp_id","subj":"T13","obj":"http://www.orpha.net/ORDO/Orphanet_178320"}],"text":"Dissecting the complex pathogenesis of CAPA requires a molecular understanding of the physiological processes whereby infection with SARS-CoV-2 facilitates fungal pathogenesis. Similar to other SARS coronaviruses, SARS-CoV-2 targets and invades epithelial cells and type II pneumocytes through binding of the SARS spike protein to the angiotensin-converting enzyme 2 (ACE2) receptors [11]. Cleavage of the S1/S2 domain by the type 2 transmembrane protease TMPRSS2 leads to the activation of the spike protein [12], thereby facilitating viral entry into the target cell via ACE2. Besides its role as a SARS virus receptor, ACE2 was also demonstrated to be required for protection from severe acute lung injury in ARDS [13]. In support of this, an insertion/deletion polymorphism that affects ACE activity was associated with ARDS susceptibility and outcome [14]. Whether the preceding interaction of SARS-CoV-2 with host cells, by disrupting the regulation of the renin-angiotensin system and or the kallikrein-kinin system, contributes to the development of CAPA, is not known."}

{"project":"LitCovid-sentences","denotations":[{"id":"T23","span":{"begin":0,"end":176},"obj":"Sentence"},{"id":"T24","span":{"begin":177,"end":389},"obj":"Sentence"},{"id":"T25","span":{"begin":390,"end":578},"obj":"Sentence"},{"id":"T26","span":{"begin":579,"end":722},"obj":"Sentence"},{"id":"T27","span":{"begin":723,"end":861},"obj":"Sentence"},{"id":"T28","span":{"begin":862,"end":1077},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Dissecting the complex pathogenesis of CAPA requires a molecular understanding of the physiological processes whereby infection with SARS-CoV-2 facilitates fungal pathogenesis. Similar to other SARS coronaviruses, SARS-CoV-2 targets and invades epithelial cells and type II pneumocytes through binding of the SARS spike protein to the angiotensin-converting enzyme 2 (ACE2) receptors [11]. Cleavage of the S1/S2 domain by the type 2 transmembrane protease TMPRSS2 leads to the activation of the spike protein [12], thereby facilitating viral entry into the target cell via ACE2. Besides its role as a SARS virus receptor, ACE2 was also demonstrated to be required for protection from severe acute lung injury in ARDS [13]. In support of this, an insertion/deletion polymorphism that affects ACE activity was associated with ARDS susceptibility and outcome [14]. Whether the preceding interaction of SARS-CoV-2 with host cells, by disrupting the regulation of the renin-angiotensin system and or the kallikrein-kinin system, contributes to the development of CAPA, is not known."}

{"project":"2_test","denotations":[{"id":"32599813-16007097-60095066","span":{"begin":385,"end":387},"obj":"16007097"},{"id":"32599813-21325420-60095067","span":{"begin":510,"end":512},"obj":"21325420"},{"id":"32599813-16001071-60095068","span":{"begin":718,"end":720},"obj":"16001071"},{"id":"32599813-12204859-60095069","span":{"begin":857,"end":859},"obj":"12204859"}],"text":"Dissecting the complex pathogenesis of CAPA requires a molecular understanding of the physiological processes whereby infection with SARS-CoV-2 facilitates fungal pathogenesis. Similar to other SARS coronaviruses, SARS-CoV-2 targets and invades epithelial cells and type II pneumocytes through binding of the SARS spike protein to the angiotensin-converting enzyme 2 (ACE2) receptors [11]. Cleavage of the S1/S2 domain by the type 2 transmembrane protease TMPRSS2 leads to the activation of the spike protein [12], thereby facilitating viral entry into the target cell via ACE2. Besides its role as a SARS virus receptor, ACE2 was also demonstrated to be required for protection from severe acute lung injury in ARDS [13]. In support of this, an insertion/deletion polymorphism that affects ACE activity was associated with ARDS susceptibility and outcome [14]. Whether the preceding interaction of SARS-CoV-2 with host cells, by disrupting the regulation of the renin-angiotensin system and or the kallikrein-kinin system, contributes to the development of CAPA, is not known."}