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    LitCovid-sample-MedDRA

    {"project":"LitCovid-sample-MedDRA","denotations":[{"id":"T25","span":{"begin":38,"end":41},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T26","span":{"begin":123,"end":128},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T27","span":{"begin":286,"end":289},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T28","span":{"begin":415,"end":428},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T29","span":{"begin":479,"end":482},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T30","span":{"begin":576,"end":589},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T31","span":{"begin":602,"end":616},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T32","span":{"begin":702,"end":705},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T33","span":{"begin":824,"end":827},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"}],"attributes":[{"id":"A25","pred":"meddra_id","subj":"T25","obj":"http://purl.bioontology.org/ontology/MEDDRA/10050289"},{"id":"A27","pred":"meddra_id","subj":"T27","obj":"http://purl.bioontology.org/ontology/MEDDRA/10050289"},{"id":"A28","pred":"meddra_id","subj":"T28","obj":"http://purl.bioontology.org/ontology/MEDDRA/10002484"},{"id":"A33","pred":"meddra_id","subj":"T33","obj":"http://purl.bioontology.org/ontology/MEDDRA/10050289"},{"id":"A26","pred":"meddra_id","subj":"T26","obj":"http://purl.bioontology.org/ontology/MEDDRA/10038555"},{"id":"A29","pred":"meddra_id","subj":"T29","obj":"http://purl.bioontology.org/ontology/MEDDRA/10050289"},{"id":"A30","pred":"meddra_id","subj":"T30","obj":"http://purl.bioontology.org/ontology/MEDDRA/10002484"},{"id":"A32","pred":"meddra_id","subj":"T32","obj":"http://purl.bioontology.org/ontology/MEDDRA/10050289"},{"id":"A31","pred":"meddra_id","subj":"T31","obj":"http://purl.bioontology.org/ontology/MEDDRA/10002491"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-sample-CHEBI

    {"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T17","span":{"begin":129,"end":140},"obj":"Chemical"},{"id":"T18","span":{"begin":141,"end":152},"obj":"Chemical"},{"id":"T20","span":{"begin":398,"end":406},"obj":"Chemical"},{"id":"T21","span":{"begin":415,"end":428},"obj":"Chemical"},{"id":"T23","span":{"begin":433,"end":443},"obj":"Chemical"},{"id":"T24","span":{"begin":515,"end":526},"obj":"Chemical"},{"id":"T25","span":{"begin":576,"end":589},"obj":"Chemical"},{"id":"T27","span":{"begin":602,"end":616},"obj":"Chemical"},{"id":"T30","span":{"begin":748,"end":758},"obj":"Chemical"},{"id":"T31","span":{"begin":795,"end":802},"obj":"Chemical"},{"id":"T32","span":{"begin":891,"end":895},"obj":"Chemical"}],"attributes":[{"id":"A27","pred":"chebi_id","subj":"T27","obj":"http://purl.obolibrary.org/obo/CHEBI_2719"},{"id":"A28","pred":"chebi_id","subj":"T27","obj":"http://purl.obolibrary.org/obo/CHEBI_48432"},{"id":"A29","pred":"chebi_id","subj":"T27","obj":"http://purl.obolibrary.org/obo/CHEBI_58506"},{"id":"A25","pred":"chebi_id","subj":"T25","obj":"http://purl.obolibrary.org/obo/CHEBI_147350"},{"id":"A26","pred":"chebi_id","subj":"T25","obj":"http://purl.obolibrary.org/obo/CHEBI_2718"},{"id":"A32","pred":"chebi_id","subj":"T32","obj":"http://purl.obolibrary.org/obo/CHEBI_24866"},{"id":"A33","pred":"chebi_id","subj":"T32","obj":"http://purl.obolibrary.org/obo/CHEBI_26710"},{"id":"A23","pred":"chebi_id","subj":"T23","obj":"http://purl.obolibrary.org/obo/CHEBI_3165"},{"id":"A31","pred":"chebi_id","subj":"T31","obj":"http://purl.obolibrary.org/obo/CHEBI_16670"},{"id":"A21","pred":"chebi_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/CHEBI_147350"},{"id":"A22","pred":"chebi_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/CHEBI_2718"},{"id":"A24","pred":"chebi_id","subj":"T24","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"},{"id":"A18","pred":"chebi_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/CHEBI_27584"},{"id":"A19","pred":"chebi_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/CHEBI_30834"},{"id":"A20","pred":"chebi_id","subj":"T20","obj":"http://purl.obolibrary.org/obo/CHEBI_16670"},{"id":"A30","pred":"chebi_id","subj":"T30","obj":"http://purl.obolibrary.org/obo/CHEBI_3165"},{"id":"A17","pred":"chebi_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-sample-sentences

    {"project":"LitCovid-sample-sentences","denotations":[{"id":"T36","span":{"begin":0,"end":236},"obj":"Sentence"},{"id":"T37","span":{"begin":237,"end":470},"obj":"Sentence"},{"id":"T38","span":{"begin":471,"end":691},"obj":"Sentence"},{"id":"T39","span":{"begin":692,"end":803},"obj":"Sentence"},{"id":"T40","span":{"begin":804,"end":931},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-sample-PD-UBERON

    {"project":"LitCovid-sample-PD-UBERON","denotations":[{"id":"T8","span":{"begin":864,"end":869},"obj":"Body_part"}],"attributes":[{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-sample-Pubtator

    {"project":"LitCovid-sample-Pubtator","denotations":[{"id":"191","span":{"begin":38,"end":41},"obj":"Gene"},{"id":"192","span":{"begin":286,"end":289},"obj":"Gene"},{"id":"193","span":{"begin":415,"end":428},"obj":"Gene"},{"id":"194","span":{"begin":433,"end":443},"obj":"Gene"},{"id":"195","span":{"begin":479,"end":482},"obj":"Gene"},{"id":"196","span":{"begin":576,"end":589},"obj":"Gene"},{"id":"197","span":{"begin":602,"end":616},"obj":"Gene"},{"id":"198","span":{"begin":702,"end":705},"obj":"Gene"},{"id":"199","span":{"begin":748,"end":758},"obj":"Gene"},{"id":"200","span":{"begin":824,"end":827},"obj":"Gene"},{"id":"201","span":{"begin":129,"end":152},"obj":"Chemical"},{"id":"202","span":{"begin":154,"end":158},"obj":"Chemical"},{"id":"203","span":{"begin":891,"end":895},"obj":"Chemical"},{"id":"204","span":{"begin":174,"end":197},"obj":"Disease"},{"id":"205","span":{"begin":783,"end":794},"obj":"Disease"}],"attributes":[{"id":"A193","pred":"pubann:denotes","subj":"193","obj":"Gene:183"},{"id":"A203","pred":"pubann:denotes","subj":"203","obj":"MESH:D012492"},{"id":"A195","pred":"pubann:denotes","subj":"195","obj":"Gene:1636"},{"id":"A198","pred":"pubann:denotes","subj":"198","obj":"Gene:1636"},{"id":"A197","pred":"pubann:denotes","subj":"197","obj":"Gene:183"},{"id":"A199","pred":"pubann:denotes","subj":"199","obj":"Gene:3827"},{"id":"A194","pred":"pubann:denotes","subj":"194","obj":"Gene:3827"},{"id":"A192","pred":"pubann:denotes","subj":"192","obj":"Gene:1636"},{"id":"A196","pred":"pubann:denotes","subj":"196","obj":"Gene:183"},{"id":"A205","pred":"pubann:denotes","subj":"205","obj":"MESH:D007022"},{"id":"A200","pred":"pubann:denotes","subj":"200","obj":"Gene:1636"},{"id":"A204","pred":"pubann:denotes","subj":"204","obj":"MESH:D002318"},{"id":"A191","pred":"pubann:denotes","subj":"191","obj":"Gene:1636"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-sample-UniProt

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12822"},{"id":"A1043","pred":"uniprot_id","subj":"T1026","obj":"https://www.uniprot.org/uniprot/P12821"},{"id":"A1044","pred":"uniprot_id","subj":"T1026","obj":"https://www.uniprot.org/uniprot/P12820"},{"id":"A1045","pred":"uniprot_id","subj":"T1026","obj":"https://www.uniprot.org/uniprot/P09470"},{"id":"A1046","pred":"uniprot_id","subj":"T1026","obj":"https://www.uniprot.org/uniprot/O02852"},{"id":"A1047","pred":"uniprot_id","subj":"T1026","obj":"https://www.uniprot.org/uniprot/E7EU16"},{"id":"A1048","pred":"uniprot_id","subj":"T1026","obj":"https://www.uniprot.org/uniprot/B4DXI3"},{"id":"A1049","pred":"uniprot_id","subj":"T1026","obj":"https://www.uniprot.org/uniprot/B0LPF0"},{"id":"A1050","pred":"uniprot_id","subj":"T1026","obj":"https://www.uniprot.org/uniprot/Q9VJV3"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-sample-PD-IDO

    {"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T18","span":{"begin":189,"end":197},"obj":"http://purl.obolibrary.org/obo/OGMS_0000031"},{"id":"T19","span":{"begin":864,"end":869},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-sample-PD-FMA

    {"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T21","span":{"begin":515,"end":526},"obj":"Body_part"},{"id":"T22","span":{"begin":864,"end":869},"obj":"Body_part"}],"attributes":[{"id":"A22","pred":"fma_id","subj":"T22","obj":"http://purl.org/sig/ont/fma/fma9670"},{"id":"A21","pred":"fma_id","subj":"T21","obj":"http://purl.org/sig/ont/fma/fma82739"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-sample-PD-MONDO

    {"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T37","span":{"begin":174,"end":197},"obj":"Disease"}],"attributes":[{"id":"A37","pred":"mondo_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/MONDO_0004995"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-sample-PD-MAT

    {"project":"LitCovid-sample-PD-MAT","denotations":[{"id":"T8","span":{"begin":864,"end":869},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T9","span":{"begin":864,"end":869},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-sample-PD-GO-BP-0

    {"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T9","span":{"begin":108,"end":119},"obj":"http://purl.obolibrary.org/obo/GO_0042592"},{"id":"T10","span":{"begin":896,"end":907},"obj":"http://purl.obolibrary.org/obo/GO_0042592"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-sample-PD-HP

    {"project":"LitCovid-sample-PD-HP","denotations":[{"id":"T8","span":{"begin":174,"end":197},"obj":"Phenotype"}],"attributes":[{"id":"A8","pred":"hp_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/HP_0001626"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-sample-GO-BP

    {"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T9","span":{"begin":108,"end":119},"obj":"http://purl.obolibrary.org/obo/GO_0042592"},{"id":"T10","span":{"begin":896,"end":907},"obj":"http://purl.obolibrary.org/obo/GO_0042592"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-PD-HP

    {"project":"LitCovid-PD-HP","denotations":[{"id":"T8","span":{"begin":174,"end":197},"obj":"Phenotype"}],"attributes":[{"id":"A8","pred":"hp_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/HP_0001626"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-PubTator

    {"project":"LitCovid-PubTator","denotations":[{"id":"191","span":{"begin":38,"end":41},"obj":"Gene"},{"id":"192","span":{"begin":286,"end":289},"obj":"Gene"},{"id":"193","span":{"begin":415,"end":428},"obj":"Gene"},{"id":"194","span":{"begin":433,"end":443},"obj":"Gene"},{"id":"195","span":{"begin":479,"end":482},"obj":"Gene"},{"id":"196","span":{"begin":576,"end":589},"obj":"Gene"},{"id":"197","span":{"begin":602,"end":616},"obj":"Gene"},{"id":"198","span":{"begin":702,"end":705},"obj":"Gene"},{"id":"199","span":{"begin":748,"end":758},"obj":"Gene"},{"id":"200","span":{"begin":824,"end":827},"obj":"Gene"},{"id":"201","span":{"begin":129,"end":152},"obj":"Chemical"},{"id":"202","span":{"begin":154,"end":158},"obj":"Chemical"},{"id":"203","span":{"begin":891,"end":895},"obj":"Chemical"},{"id":"204","span":{"begin":174,"end":197},"obj":"Disease"},{"id":"205","span":{"begin":783,"end":794},"obj":"Disease"}],"attributes":[{"id":"A191","pred":"tao:has_database_id","subj":"191","obj":"Gene:1636"},{"id":"A192","pred":"tao:has_database_id","subj":"192","obj":"Gene:1636"},{"id":"A193","pred":"tao:has_database_id","subj":"193","obj":"Gene:183"},{"id":"A194","pred":"tao:has_database_id","subj":"194","obj":"Gene:3827"},{"id":"A195","pred":"tao:has_database_id","subj":"195","obj":"Gene:1636"},{"id":"A196","pred":"tao:has_database_id","subj":"196","obj":"Gene:183"},{"id":"A197","pred":"tao:has_database_id","subj":"197","obj":"Gene:183"},{"id":"A198","pred":"tao:has_database_id","subj":"198","obj":"Gene:1636"},{"id":"A199","pred":"tao:has_database_id","subj":"199","obj":"Gene:3827"},{"id":"A200","pred":"tao:has_database_id","subj":"200","obj":"Gene:1636"},{"id":"A203","pred":"tao:has_database_id","subj":"203","obj":"MESH:D012492"},{"id":"A204","pred":"tao:has_database_id","subj":"204","obj":"MESH:D002318"},{"id":"A205","pred":"tao:has_database_id","subj":"205","obj":"MESH:D007022"}],"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":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}

    LitCovid-sentences

    {"project":"LitCovid-sentences","denotations":[{"id":"T36","span":{"begin":0,"end":236},"obj":"Sentence"},{"id":"T37","span":{"begin":237,"end":470},"obj":"Sentence"},{"id":"T38","span":{"begin":471,"end":691},"obj":"Sentence"},{"id":"T39","span":{"begin":692,"end":803},"obj":"Sentence"},{"id":"T40","span":{"begin":804,"end":931},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"sACE, hereafter referred to simply as ACE, has been extensively studied, because of its crucial role in the homeostasis of renin-angiotensin-aldosterone (RAAS) system and in cardiovascular diseases (Takimoto-Ohnishi and Murakami, 2019). The two extracellular domains N and C domains of ACE (Wei et al., 1991; Jaspard et al., 1993; Natesh et al., 2003; Riordan, 2003) can both hydrolase two crucial peptides, namely angiotensin I and bradykinin, with the same efficiency. Indeed, ACE carries out the cleavage of two amino acids (dipeptidase action) from the C-terminal part of angiotensin I to generate angiotensin II, which exerts a potent vasopressor, proliferative, and profibrotic effect. Moreover, ACE mediates the cleavage and inactivation of bradykinin, which is a vasodilator hypotensive peptide. The pivotal role of ACE in the RAAS system allows a refined blood pressure control and salt homeostasis (Sayer and Bhat, 2014)."}