PMC:7647877 / 10781-13161 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T200","span":{"begin":172,"end":179},"obj":"Body_part"},{"id":"T201","span":{"begin":212,"end":229},"obj":"Body_part"},{"id":"T202","span":{"begin":224,"end":229},"obj":"Body_part"},{"id":"T203","span":{"begin":237,"end":248},"obj":"Body_part"},{"id":"T204","span":{"begin":260,"end":269},"obj":"Body_part"},{"id":"T205","span":{"begin":277,"end":282},"obj":"Body_part"},{"id":"T206","span":{"begin":284,"end":293},"obj":"Body_part"},{"id":"T207","span":{"begin":295,"end":300},"obj":"Body_part"},{"id":"T208","span":{"begin":302,"end":307},"obj":"Body_part"},{"id":"T209","span":{"begin":312,"end":318},"obj":"Body_part"},{"id":"T210","span":{"begin":342,"end":346},"obj":"Body_part"},{"id":"T211","span":{"begin":416,"end":420},"obj":"Body_part"},{"id":"T212","span":{"begin":612,"end":615},"obj":"Body_part"},{"id":"T213","span":{"begin":643,"end":653},"obj":"Body_part"},{"id":"T214","span":{"begin":696,"end":706},"obj":"Body_part"},{"id":"T215","span":{"begin":762,"end":769},"obj":"Body_part"},{"id":"T216","span":{"begin":1029,"end":1042},"obj":"Body_part"},{"id":"T217","span":{"begin":1558,"end":1565},"obj":"Body_part"},{"id":"T218","span":{"begin":1665,"end":1669},"obj":"Body_part"},{"id":"T219","span":{"begin":1813,"end":1830},"obj":"Body_part"},{"id":"T220","span":{"begin":1825,"end":1830},"obj":"Body_part"},{"id":"T221","span":{"begin":1864,"end":1873},"obj":"Body_part"},{"id":"T222","span":{"begin":2019,"end":2026},"obj":"Body_part"},{"id":"T223","span":{"begin":2063,"end":2069},"obj":"Body_part"},{"id":"T224","span":{"begin":2143,"end":2148},"obj":"Body_part"}],"attributes":[{"id":"A200","pred":"fma_id","subj":"T200","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A201","pred":"fma_id","subj":"T201","obj":"http://purl.org/sig/ont/fma/fma66772"},{"id":"A202","pred":"fma_id","subj":"T202","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A203","pred":"fma_id","subj":"T203","obj":"http://purl.org/sig/ont/fma/fma69050"},{"id":"A204","pred":"fma_id","subj":"T204","obj":"http://purl.org/sig/ont/fma/fma9639"},{"id":"A205","pred":"fma_id","subj":"T205","obj":"http://purl.org/sig/ont/fma/fma68877"},{"id":"A206","pred":"fma_id","subj":"T206","obj":"http://purl.org/sig/ont/fma/fma7199"},{"id":"A207","pred":"fma_id","subj":"T207","obj":"http://purl.org/sig/ont/fma/fma7088"},{"id":"A208","pred":"fma_id","subj":"T208","obj":"http://purl.org/sig/ont/fma/fma50801"},{"id":"A209","pred":"fma_id","subj":"T209","obj":"http://purl.org/sig/ont/fma/fma7203"},{"id":"A210","pred":"fma_id","subj":"T210","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A211","pred":"fma_id","subj":"T211","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A212","pred":"fma_id","subj":"T212","obj":"http://purl.org/sig/ont/fma/fma7199"},{"id":"A213","pred":"fma_id","subj":"T213","obj":"http://purl.org/sig/ont/fma/fma82739"},{"id":"A214","pred":"fma_id","subj":"T214","obj":"http://purl.org/sig/ont/fma/fma7199"},{"id":"A215","pred":"fma_id","subj":"T215","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A216","pred":"fma_id","subj":"T216","obj":"http://purl.org/sig/ont/fma/fma9825"},{"id":"A217","pred":"fma_id","subj":"T217","obj":"http://purl.org/sig/ont/fma/fma9637"},{"id":"A218","pred":"fma_id","subj":"T218","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A219","pred":"fma_id","subj":"T219","obj":"http://purl.org/sig/ont/fma/fma66772"},{"id":"A220","pred":"fma_id","subj":"T220","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A221","pred":"fma_id","subj":"T221","obj":"http://purl.org/sig/ont/fma/fma84050"},{"id":"A222","pred":"fma_id","subj":"T222","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A223","pred":"fma_id","subj":"T223","obj":"http://purl.org/sig/ont/fma/fma82764"},{"id":"A224","pred":"fma_id","subj":"T224","obj":"http://purl.org/sig/ont/fma/fma9670"}],"text":"The access route of SARS-CoV-2 is represented by a hydrophobic pocket of the extracellular catalytic domain of Angiotensin-converting enzyme 2 (ACE2) [18]. SARS-CoV peak S protein trimers bind ACE2, expressed in endothelial cells of the vasculature and in the epithelia of the lungs, intestine, heart, brain and kidney. SARS-CoV-2 enters the cell for endocytosis and membrane fusion. Once the virus has infected the cell, it follows a downregulation of ACE2 with a consequent local increase in the levels of Ang II, and the development of acute respiratory distress syndrome (ARDS) [19]. The role of ACE2 in the gut, for expression of neutral amino acid transporters, could explain diarrhoea and intestinal inflammation observed in COVID-19. Moreover, SARS-CoV2 protein E activates the NFκB inflammatory pathway with the consequent activation of MAPK p38, resulting in exacerbation of inflammation and immunopathology [20]. Following the SARS-CoV-2 infection, in the incubation stage and in the non-serious form of COVID-19, the immune system activates the specific adaptive immune response to eliminate the virus, which should be sufficient to block viral propagation and disease progression. The antiviral system functions well in the presence of general good health and an adequate genetic background. However, the presence of concomitant pathologies (obesity, cardiovascular diseases, diabetes, neurodegenerative diseases and cancer), malnutrition, and impaired immune response determine the spread of the virus and a massive destruction of the affected tissues, especially in organs that have high ACE2 expression [21]. As noted earlier, SARS-CoV-2 enters the cell via ACE2; that inactivates des-Arg bradykinin, which is a potent ligand of the bradykinin receptor type 1 (BDKRB1).This receptor, localized on endothelial cells, is up-regulated by inflammatory cytokines, which is unlike the B2 receptor, that is constituently expressed and is the receptor for bradykinin (BDK). BDK is produced from an inactive pre-protein kininogen through activation by the serine protease kallikrein; in addition, it is considered a potent regulator of blood pressure [22], because it induces vasodilation, natriuresis, and hypotension upon activation of the BDKRB2 receptor. BDK is strongly integrated with the RAS, and the BDK receptor signaling is increased by angiotensin’s action [23]."}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T35","span":{"begin":237,"end":248},"obj":"Body_part"},{"id":"T36","span":{"begin":260,"end":269},"obj":"Body_part"},{"id":"T37","span":{"begin":284,"end":293},"obj":"Body_part"},{"id":"T38","span":{"begin":295,"end":300},"obj":"Body_part"},{"id":"T39","span":{"begin":302,"end":307},"obj":"Body_part"},{"id":"T40","span":{"begin":312,"end":318},"obj":"Body_part"},{"id":"T41","span":{"begin":1029,"end":1042},"obj":"Body_part"},{"id":"T42","span":{"begin":1581,"end":1587},"obj":"Body_part"},{"id":"T43","span":{"begin":2143,"end":2148},"obj":"Body_part"}],"attributes":[{"id":"A35","pred":"uberon_id","subj":"T35","obj":"http://purl.obolibrary.org/obo/UBERON_0002049"},{"id":"A36","pred":"uberon_id","subj":"T36","obj":"http://purl.obolibrary.org/obo/UBERON_0000483"},{"id":"A37","pred":"uberon_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/UBERON_0000160"},{"id":"A38","pred":"uberon_id","subj":"T38","obj":"http://purl.obolibrary.org/obo/UBERON_0000948"},{"id":"A39","pred":"uberon_id","subj":"T39","obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"A40","pred":"uberon_id","subj":"T40","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A41","pred":"uberon_id","subj":"T41","obj":"http://purl.obolibrary.org/obo/UBERON_0002405"},{"id":"A42","pred":"uberon_id","subj":"T42","obj":"http://purl.obolibrary.org/obo/UBERON_0000062"},{"id":"A43","pred":"uberon_id","subj":"T43","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"The access route of SARS-CoV-2 is represented by a hydrophobic pocket of the extracellular catalytic domain of Angiotensin-converting enzyme 2 (ACE2) [18]. SARS-CoV peak S protein trimers bind ACE2, expressed in endothelial cells of the vasculature and in the epithelia of the lungs, intestine, heart, brain and kidney. SARS-CoV-2 enters the cell for endocytosis and membrane fusion. Once the virus has infected the cell, it follows a downregulation of ACE2 with a consequent local increase in the levels of Ang II, and the development of acute respiratory distress syndrome (ARDS) [19]. The role of ACE2 in the gut, for expression of neutral amino acid transporters, could explain diarrhoea and intestinal inflammation observed in COVID-19. Moreover, SARS-CoV2 protein E activates the NFκB inflammatory pathway with the consequent activation of MAPK p38, resulting in exacerbation of inflammation and immunopathology [20]. Following the SARS-CoV-2 infection, in the incubation stage and in the non-serious form of COVID-19, the immune system activates the specific adaptive immune response to eliminate the virus, which should be sufficient to block viral propagation and disease progression. The antiviral system functions well in the presence of general good health and an adequate genetic background. However, the presence of concomitant pathologies (obesity, cardiovascular diseases, diabetes, neurodegenerative diseases and cancer), malnutrition, and impaired immune response determine the spread of the virus and a massive destruction of the affected tissues, especially in organs that have high ACE2 expression [21]. As noted earlier, SARS-CoV-2 enters the cell via ACE2; that inactivates des-Arg bradykinin, which is a potent ligand of the bradykinin receptor type 1 (BDKRB1).This receptor, localized on endothelial cells, is up-regulated by inflammatory cytokines, which is unlike the B2 receptor, that is constituently expressed and is the receptor for bradykinin (BDK). BDK is produced from an inactive pre-protein kininogen through activation by the serine protease kallikrein; in addition, it is considered a potent regulator of blood pressure [22], because it induces vasodilation, natriuresis, and hypotension upon activation of the BDKRB2 receptor. BDK is strongly integrated with the RAS, and the BDK receptor signaling is increased by angiotensin’s action [23]."}

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Following the SARS-CoV-2 infection, in the incubation stage and in the non-serious form of COVID-19, the immune system activates the specific adaptive immune response to eliminate the virus, which should be sufficient to block viral propagation and disease progression. The antiviral system functions well in the presence of general good health and an adequate genetic background. However, the presence of concomitant pathologies (obesity, cardiovascular diseases, diabetes, neurodegenerative diseases and cancer), malnutrition, and impaired immune response determine the spread of the virus and a massive destruction of the affected tissues, especially in organs that have high ACE2 expression [21]. As noted earlier, SARS-CoV-2 enters the cell via ACE2; that inactivates des-Arg bradykinin, which is a potent ligand of the bradykinin receptor type 1 (BDKRB1).This receptor, localized on endothelial cells, is up-regulated by inflammatory cytokines, which is unlike the B2 receptor, that is constituently expressed and is the receptor for bradykinin (BDK). BDK is produced from an inactive pre-protein kininogen through activation by the serine protease kallikrein; in addition, it is considered a potent regulator of blood pressure [22], because it induces vasodilation, natriuresis, and hypotension upon activation of the BDKRB2 receptor. BDK is strongly integrated with the RAS, and the BDK receptor signaling is increased by angiotensin’s action [23]."}

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SARS-CoV peak S protein trimers bind ACE2, expressed in endothelial cells of the vasculature and in the epithelia of the lungs, intestine, heart, brain and kidney. SARS-CoV-2 enters the cell for endocytosis and membrane fusion. Once the virus has infected the cell, it follows a downregulation of ACE2 with a consequent local increase in the levels of Ang II, and the development of acute respiratory distress syndrome (ARDS) [19]. The role of ACE2 in the gut, for expression of neutral amino acid transporters, could explain diarrhoea and intestinal inflammation observed in COVID-19. Moreover, SARS-CoV2 protein E activates the NFκB inflammatory pathway with the consequent activation of MAPK p38, resulting in exacerbation of inflammation and immunopathology [20]. Following the SARS-CoV-2 infection, in the incubation stage and in the non-serious form of COVID-19, the immune system activates the specific adaptive immune response to eliminate the virus, which should be sufficient to block viral propagation and disease progression. The antiviral system functions well in the presence of general good health and an adequate genetic background. However, the presence of concomitant pathologies (obesity, cardiovascular diseases, diabetes, neurodegenerative diseases and cancer), malnutrition, and impaired immune response determine the spread of the virus and a massive destruction of the affected tissues, especially in organs that have high ACE2 expression [21]. As noted earlier, SARS-CoV-2 enters the cell via ACE2; that inactivates des-Arg bradykinin, which is a potent ligand of the bradykinin receptor type 1 (BDKRB1).This receptor, localized on endothelial cells, is up-regulated by inflammatory cytokines, which is unlike the B2 receptor, that is constituently expressed and is the receptor for bradykinin (BDK). BDK is produced from an inactive pre-protein kininogen through activation by the serine protease kallikrein; in addition, it is considered a potent regulator of blood pressure [22], because it induces vasodilation, natriuresis, and hypotension upon activation of the BDKRB2 receptor. BDK is strongly integrated with the RAS, and the BDK receptor signaling is increased by angiotensin’s action [23]."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T132","span":{"begin":111,"end":122},"obj":"Chemical"},{"id":"T133","span":{"begin":172,"end":179},"obj":"Chemical"},{"id":"T134","span":{"begin":512,"end":514},"obj":"Chemical"},{"id":"T135","span":{"begin":643,"end":653},"obj":"Chemical"},{"id":"T136","span":{"begin":643,"end":648},"obj":"Chemical"},{"id":"T137","span":{"begin":649,"end":653},"obj":"Chemical"},{"id":"T138","span":{"begin":762,"end":769},"obj":"Chemical"},{"id":"T139","span":{"begin":786,"end":788},"obj":"Chemical"},{"id":"T142","span":{"begin":1198,"end":1207},"obj":"Chemical"},{"id":"T143","span":{"begin":1701,"end":1704},"obj":"Chemical"},{"id":"T145","span":{"begin":1705,"end":1715},"obj":"Chemical"},{"id":"T146","span":{"begin":1735,"end":1741},"obj":"Chemical"},{"id":"T147","span":{"begin":1749,"end":1759},"obj":"Chemical"},{"id":"T148","span":{"begin":1895,"end":1897},"obj":"Chemical"},{"id":"T149","span":{"begin":1964,"end":1974},"obj":"Chemical"},{"id":"T150","span":{"begin":2019,"end":2026},"obj":"Chemical"},{"id":"T151","span":{"begin":2063,"end":2069},"obj":"Chemical"},{"id":"T152","span":{"begin":2302,"end":2305},"obj":"Chemical"}],"attributes":[{"id":"A132","pred":"chebi_id","subj":"T132","obj":"http://purl.obolibrary.org/obo/CHEBI_2719"},{"id":"A133","pred":"chebi_id","subj":"T133","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A134","pred":"chebi_id","subj":"T134","obj":"http://purl.obolibrary.org/obo/CHEBI_74067"},{"id":"A135","pred":"chebi_id","subj":"T135","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"},{"id":"A136","pred":"chebi_id","subj":"T136","obj":"http://purl.obolibrary.org/obo/CHEBI_46882"},{"id":"A137","pred":"chebi_id","subj":"T137","obj":"http://purl.obolibrary.org/obo/CHEBI_37527"},{"id":"A138","pred":"chebi_id","subj":"T138","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A139","pred":"chebi_id","subj":"T139","obj":"http://purl.obolibrary.org/obo/CHEBI_141424"},{"id":"A140","pred":"chebi_id","subj":"T139","obj":"http://purl.obolibrary.org/obo/CHEBI_25573"},{"id":"A141","pred":"chebi_id","subj":"T139","obj":"http://purl.obolibrary.org/obo/CHEBI_1224"},{"id":"A142","pred":"chebi_id","subj":"T142","obj":"http://purl.obolibrary.org/obo/CHEBI_22587"},{"id":"A143","pred":"chebi_id","subj":"T143","obj":"http://purl.obolibrary.org/obo/CHEBI_16467"},{"id":"A144","pred":"chebi_id","subj":"T143","obj":"http://purl.obolibrary.org/obo/CHEBI_29952"},{"id":"A145","pred":"chebi_id","subj":"T145","obj":"http://purl.obolibrary.org/obo/CHEBI_3165"},{"id":"A146","pred":"chebi_id","subj":"T146","obj":"http://purl.obolibrary.org/obo/CHEBI_52214"},{"id":"A147","pred":"chebi_id","subj":"T147","obj":"http://purl.obolibrary.org/obo/CHEBI_3165"},{"id":"A148","pred":"chebi_id","subj":"T148","obj":"http://purl.obolibrary.org/obo/CHEBI_51707"},{"id":"A149","pred":"chebi_id","subj":"T149","obj":"http://purl.obolibrary.org/obo/CHEBI_3165"},{"id":"A150","pred":"chebi_id","subj":"T150","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A151","pred":"chebi_id","subj":"T151","obj":"http://purl.obolibrary.org/obo/CHEBI_17822"},{"id":"A152","pred":"chebi_id","subj":"T152","obj":"http://purl.obolibrary.org/obo/CHEBI_63620"}],"text":"The access route of SARS-CoV-2 is represented by a hydrophobic pocket of the extracellular catalytic domain of Angiotensin-converting enzyme 2 (ACE2) [18]. SARS-CoV peak S protein trimers bind ACE2, expressed in endothelial cells of the vasculature and in the epithelia of the lungs, intestine, heart, brain and kidney. SARS-CoV-2 enters the cell for endocytosis and membrane fusion. Once the virus has infected the cell, it follows a downregulation of ACE2 with a consequent local increase in the levels of Ang II, and the development of acute respiratory distress syndrome (ARDS) [19]. The role of ACE2 in the gut, for expression of neutral amino acid transporters, could explain diarrhoea and intestinal inflammation observed in COVID-19. Moreover, SARS-CoV2 protein E activates the NFκB inflammatory pathway with the consequent activation of MAPK p38, resulting in exacerbation of inflammation and immunopathology [20]. Following the SARS-CoV-2 infection, in the incubation stage and in the non-serious form of COVID-19, the immune system activates the specific adaptive immune response to eliminate the virus, which should be sufficient to block viral propagation and disease progression. The antiviral system functions well in the presence of general good health and an adequate genetic background. However, the presence of concomitant pathologies (obesity, cardiovascular diseases, diabetes, neurodegenerative diseases and cancer), malnutrition, and impaired immune response determine the spread of the virus and a massive destruction of the affected tissues, especially in organs that have high ACE2 expression [21]. As noted earlier, SARS-CoV-2 enters the cell via ACE2; that inactivates des-Arg bradykinin, which is a potent ligand of the bradykinin receptor type 1 (BDKRB1).This receptor, localized on endothelial cells, is up-regulated by inflammatory cytokines, which is unlike the B2 receptor, that is constituently expressed and is the receptor for bradykinin (BDK). BDK is produced from an inactive pre-protein kininogen through activation by the serine protease kallikrein; in addition, it is considered a potent regulator of blood pressure [22], because it induces vasodilation, natriuresis, and hypotension upon activation of the BDKRB2 receptor. BDK is strongly integrated with the RAS, and the BDK receptor signaling is increased by angiotensin’s action [23]."}

{"project":"LitCovid-PD-HP","denotations":[{"id":"T10","span":{"begin":545,"end":565},"obj":"Phenotype"},{"id":"T11","span":{"begin":682,"end":691},"obj":"Phenotype"},{"id":"T12","span":{"begin":1355,"end":1362},"obj":"Phenotype"},{"id":"T13","span":{"begin":1364,"end":1387},"obj":"Phenotype"},{"id":"T14","span":{"begin":1399,"end":1425},"obj":"Phenotype"},{"id":"T15","span":{"begin":1430,"end":1436},"obj":"Phenotype"},{"id":"T16","span":{"begin":1439,"end":1451},"obj":"Phenotype"},{"id":"T17","span":{"begin":2214,"end":2225},"obj":"Phenotype"}],"attributes":[{"id":"A10","pred":"hp_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/HP_0002098"},{"id":"A11","pred":"hp_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/HP_0002014"},{"id":"A12","pred":"hp_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/HP_0001513"},{"id":"A13","pred":"hp_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/HP_0001626"},{"id":"A14","pred":"hp_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/HP_0002180"},{"id":"A15","pred":"hp_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/HP_0002664"},{"id":"A16","pred":"hp_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/HP_0004395"},{"id":"A17","pred":"hp_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/HP_0002615"}],"text":"The access route of SARS-CoV-2 is represented by a hydrophobic pocket of the extracellular catalytic domain of Angiotensin-converting enzyme 2 (ACE2) [18]. SARS-CoV peak S protein trimers bind ACE2, expressed in endothelial cells of the vasculature and in the epithelia of the lungs, intestine, heart, brain and kidney. SARS-CoV-2 enters the cell for endocytosis and membrane fusion. Once the virus has infected the cell, it follows a downregulation of ACE2 with a consequent local increase in the levels of Ang II, and the development of acute respiratory distress syndrome (ARDS) [19]. The role of ACE2 in the gut, for expression of neutral amino acid transporters, could explain diarrhoea and intestinal inflammation observed in COVID-19. Moreover, SARS-CoV2 protein E activates the NFκB inflammatory pathway with the consequent activation of MAPK p38, resulting in exacerbation of inflammation and immunopathology [20]. Following the SARS-CoV-2 infection, in the incubation stage and in the non-serious form of COVID-19, the immune system activates the specific adaptive immune response to eliminate the virus, which should be sufficient to block viral propagation and disease progression. The antiviral system functions well in the presence of general good health and an adequate genetic background. However, the presence of concomitant pathologies (obesity, cardiovascular diseases, diabetes, neurodegenerative diseases and cancer), malnutrition, and impaired immune response determine the spread of the virus and a massive destruction of the affected tissues, especially in organs that have high ACE2 expression [21]. As noted earlier, SARS-CoV-2 enters the cell via ACE2; that inactivates des-Arg bradykinin, which is a potent ligand of the bradykinin receptor type 1 (BDKRB1).This receptor, localized on endothelial cells, is up-regulated by inflammatory cytokines, which is unlike the B2 receptor, that is constituently expressed and is the receptor for bradykinin (BDK). BDK is produced from an inactive pre-protein kininogen through activation by the serine protease kallikrein; in addition, it is considered a potent regulator of blood pressure [22], because it induces vasodilation, natriuresis, and hypotension upon activation of the BDKRB2 receptor. BDK is strongly integrated with the RAS, and the BDK receptor signaling is increased by angiotensin’s action [23]."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T63","span":{"begin":351,"end":362},"obj":"http://purl.obolibrary.org/obo/GO_0006897"},{"id":"T64","span":{"begin":367,"end":382},"obj":"http://purl.obolibrary.org/obo/GO_0061025"},{"id":"T65","span":{"begin":635,"end":666},"obj":"http://purl.obolibrary.org/obo/GO_0015804"},{"id":"T66","span":{"begin":707,"end":719},"obj":"http://purl.obolibrary.org/obo/GO_0006954"},{"id":"T67","span":{"begin":846,"end":850},"obj":"http://purl.obolibrary.org/obo/GO_0004707"},{"id":"T68","span":{"begin":885,"end":897},"obj":"http://purl.obolibrary.org/obo/GO_0006954"},{"id":"T69","span":{"begin":1066,"end":1090},"obj":"http://purl.obolibrary.org/obo/GO_0002250"},{"id":"T70","span":{"begin":1075,"end":1090},"obj":"http://purl.obolibrary.org/obo/GO_0006955"},{"id":"T71","span":{"begin":1466,"end":1481},"obj":"http://purl.obolibrary.org/obo/GO_0006955"},{"id":"T72","span":{"begin":2130,"end":2157},"obj":"http://purl.obolibrary.org/obo/GO_0008217"},{"id":"T73","span":{"begin":2183,"end":2195},"obj":"http://purl.obolibrary.org/obo/GO_0042311"},{"id":"T74","span":{"begin":2197,"end":2208},"obj":"http://purl.obolibrary.org/obo/GO_0035815"},{"id":"T75","span":{"begin":2328,"end":2337},"obj":"http://purl.obolibrary.org/obo/GO_0023052"}],"text":"The access route of SARS-CoV-2 is represented by a hydrophobic pocket of the extracellular catalytic domain of Angiotensin-converting enzyme 2 (ACE2) [18]. SARS-CoV peak S protein trimers bind ACE2, expressed in endothelial cells of the vasculature and in the epithelia of the lungs, intestine, heart, brain and kidney. SARS-CoV-2 enters the cell for endocytosis and membrane fusion. Once the virus has infected the cell, it follows a downregulation of ACE2 with a consequent local increase in the levels of Ang II, and the development of acute respiratory distress syndrome (ARDS) [19]. The role of ACE2 in the gut, for expression of neutral amino acid transporters, could explain diarrhoea and intestinal inflammation observed in COVID-19. Moreover, SARS-CoV2 protein E activates the NFκB inflammatory pathway with the consequent activation of MAPK p38, resulting in exacerbation of inflammation and immunopathology [20]. Following the SARS-CoV-2 infection, in the incubation stage and in the non-serious form of COVID-19, the immune system activates the specific adaptive immune response to eliminate the virus, which should be sufficient to block viral propagation and disease progression. The antiviral system functions well in the presence of general good health and an adequate genetic background. However, the presence of concomitant pathologies (obesity, cardiovascular diseases, diabetes, neurodegenerative diseases and cancer), malnutrition, and impaired immune response determine the spread of the virus and a massive destruction of the affected tissues, especially in organs that have high ACE2 expression [21]. As noted earlier, SARS-CoV-2 enters the cell via ACE2; that inactivates des-Arg bradykinin, which is a potent ligand of the bradykinin receptor type 1 (BDKRB1).This receptor, localized on endothelial cells, is up-regulated by inflammatory cytokines, which is unlike the B2 receptor, that is constituently expressed and is the receptor for bradykinin (BDK). BDK is produced from an inactive pre-protein kininogen through activation by the serine protease kallikrein; in addition, it is considered a potent regulator of blood pressure [22], because it induces vasodilation, natriuresis, and hypotension upon activation of the BDKRB2 receptor. BDK is strongly integrated with the RAS, and the BDK receptor signaling is increased by angiotensin’s action [23]."}

{"project":"LitCovid-sentences","denotations":[{"id":"T69","span":{"begin":0,"end":155},"obj":"Sentence"},{"id":"T70","span":{"begin":156,"end":319},"obj":"Sentence"},{"id":"T71","span":{"begin":320,"end":383},"obj":"Sentence"},{"id":"T72","span":{"begin":384,"end":587},"obj":"Sentence"},{"id":"T73","span":{"begin":588,"end":741},"obj":"Sentence"},{"id":"T74","span":{"begin":742,"end":923},"obj":"Sentence"},{"id":"T75","span":{"begin":924,"end":1193},"obj":"Sentence"},{"id":"T76","span":{"begin":1194,"end":1304},"obj":"Sentence"},{"id":"T77","span":{"begin":1305,"end":1624},"obj":"Sentence"},{"id":"T78","span":{"begin":1625,"end":1981},"obj":"Sentence"},{"id":"T79","span":{"begin":1982,"end":2265},"obj":"Sentence"},{"id":"T80","span":{"begin":2266,"end":2380},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The access route of SARS-CoV-2 is represented by a hydrophobic pocket of the extracellular catalytic domain of Angiotensin-converting enzyme 2 (ACE2) [18]. SARS-CoV peak S protein trimers bind ACE2, expressed in endothelial cells of the vasculature and in the epithelia of the lungs, intestine, heart, brain and kidney. SARS-CoV-2 enters the cell for endocytosis and membrane fusion. Once the virus has infected the cell, it follows a downregulation of ACE2 with a consequent local increase in the levels of Ang II, and the development of acute respiratory distress syndrome (ARDS) [19]. The role of ACE2 in the gut, for expression of neutral amino acid transporters, could explain diarrhoea and intestinal inflammation observed in COVID-19. Moreover, SARS-CoV2 protein E activates the NFκB inflammatory pathway with the consequent activation of MAPK p38, resulting in exacerbation of inflammation and immunopathology [20]. Following the SARS-CoV-2 infection, in the incubation stage and in the non-serious form of COVID-19, the immune system activates the specific adaptive immune response to eliminate the virus, which should be sufficient to block viral propagation and disease progression. The antiviral system functions well in the presence of general good health and an adequate genetic background. However, the presence of concomitant pathologies (obesity, cardiovascular diseases, diabetes, neurodegenerative diseases and cancer), malnutrition, and impaired immune response determine the spread of the virus and a massive destruction of the affected tissues, especially in organs that have high ACE2 expression [21]. As noted earlier, SARS-CoV-2 enters the cell via ACE2; that inactivates des-Arg bradykinin, which is a potent ligand of the bradykinin receptor type 1 (BDKRB1).This receptor, localized on endothelial cells, is up-regulated by inflammatory cytokines, which is unlike the B2 receptor, that is constituently expressed and is the receptor for bradykinin (BDK). BDK is produced from an inactive pre-protein kininogen through activation by the serine protease kallikrein; in addition, it is considered a potent regulator of blood pressure [22], because it induces vasodilation, natriuresis, and hypotension upon activation of the BDKRB2 receptor. BDK is strongly integrated with the RAS, and the BDK receptor signaling is increased by angiotensin’s action [23]."}

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access route of SARS-CoV-2 is represented by a hydrophobic pocket of the extracellular catalytic domain of Angiotensin-converting enzyme 2 (ACE2) [18]. SARS-CoV peak S protein trimers bind ACE2, expressed in endothelial cells of the vasculature and in the epithelia of the lungs, intestine, heart, brain and kidney. SARS-CoV-2 enters the cell for endocytosis and membrane fusion. Once the virus has infected the cell, it follows a downregulation of ACE2 with a consequent local increase in the levels of Ang II, and the development of acute respiratory distress syndrome (ARDS) [19]. The role of ACE2 in the gut, for expression of neutral amino acid transporters, could explain diarrhoea and intestinal inflammation observed in COVID-19. Moreover, SARS-CoV2 protein E activates the NFκB inflammatory pathway with the consequent activation of MAPK p38, resulting in exacerbation of inflammation and immunopathology [20]. Following the SARS-CoV-2 infection, in the incubation stage and in the non-serious form of COVID-19, the immune system activates the specific adaptive immune response to eliminate the virus, which should be sufficient to block viral propagation and disease progression. The antiviral system functions well in the presence of general good health and an adequate genetic background. However, the presence of concomitant pathologies (obesity, cardiovascular diseases, diabetes, neurodegenerative diseases and cancer), malnutrition, and impaired immune response determine the spread of the virus and a massive destruction of the affected tissues, especially in organs that have high ACE2 expression [21]. As noted earlier, SARS-CoV-2 enters the cell via ACE2; that inactivates des-Arg bradykinin, which is a potent ligand of the bradykinin receptor type 1 (BDKRB1).This receptor, localized on endothelial cells, is up-regulated by inflammatory cytokines, which is unlike the B2 receptor, that is constituently expressed and is the receptor for bradykinin (BDK). BDK is produced from an inactive pre-protein kininogen through activation by the serine protease kallikrein; in addition, it is considered a potent regulator of blood pressure [22], because it induces vasodilation, natriuresis, and hypotension upon activation of the BDKRB2 receptor. BDK is strongly integrated with the RAS, and the BDK receptor signaling is increased by angiotensin’s action [23]."}