PMC:7556165 / 5406-5695 JSONTXT

{"project":"LitCovid-sample-MedDRA","denotations":[{"id":"T27","span":{"begin":12,"end":15},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T28","span":{"begin":141,"end":154},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T29","span":{"begin":205,"end":208},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"}],"attributes":[{"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":"A29","pred":"meddra_id","subj":"T29","obj":"http://purl.bioontology.org/ontology/MEDDRA/10050289"}],"text":" 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-term"}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T20","span":{"begin":124,"end":132},"obj":"Chemical"},{"id":"T21","span":{"begin":141,"end":154},"obj":"Chemical"},{"id":"T23","span":{"begin":159,"end":169},"obj":"Chemical"},{"id":"T24","span":{"begin":241,"end":252},"obj":"Chemical"}],"attributes":[{"id":"A20","pred":"chebi_id","subj":"T20","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":"A23","pred":"chebi_id","subj":"T23","obj":"http://purl.obolibrary.org/obo/CHEBI_3165"},{"id":"A24","pred":"chebi_id","subj":"T24","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"}],"text":" 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-term"}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"192","span":{"begin":12,"end":15},"obj":"Gene"},{"id":"193","span":{"begin":141,"end":154},"obj":"Gene"},{"id":"194","span":{"begin":159,"end":169},"obj":"Gene"},{"id":"195","span":{"begin":205,"end":208},"obj":"Gene"}],"attributes":[{"id":"A192","pred":"pubann:denotes","subj":"192","obj":"Gene:1636"},{"id":"A193","pred":"pubann:denotes","subj":"193","obj":"Gene:183"},{"id":"A194","pred":"pubann:denotes","subj":"194","obj":"Gene:3827"},{"id":"A195","pred":"pubann:denotes","subj":"195","obj":"Gene:1636"}],"text":" 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-term"}

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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-term"}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T21","span":{"begin":241,"end":252},"obj":"Body_part"}],"attributes":[{"id":"A21","pred":"fma_id","subj":"T21","obj":"http://purl.org/sig/ont/fma/fma82739"}],"text":" 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-term"}

{"project":"LitCovid-PubTator","denotations":[{"id":"192","span":{"begin":12,"end":15},"obj":"Gene"},{"id":"193","span":{"begin":141,"end":154},"obj":"Gene"},{"id":"194","span":{"begin":159,"end":169},"obj":"Gene"},{"id":"195","span":{"begin":205,"end":208},"obj":"Gene"}],"attributes":[{"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"}],"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":" 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-term"}