PMC:7556165 / 43286-43679 JSONTXT

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    LitCovid-sample-PD-NCBITaxon

    {"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T188","span":{"begin":0,"end":10},"obj":"Species"},{"id":"T189","span":{"begin":0,"end":4},"obj":"Species"}],"attributes":[{"id":"A188","pred":"ncbi_taxonomy_id","subj":"T188","obj":"NCBItxid:2697049"},{"id":"A189","pred":"ncbi_taxonomy_id","subj":"T189","obj":"NCBItxid:694009"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"SARS-COV-2 shows a large flexibility with regard to protease priming, which may independently occur by a) furin and furin-like proteases intracellularly, b) trypsin-like proteases such as TMPRSS2 that are present on the host cell membrane (particularly on airway epithelial cells), and 3) endosomal cathepsins activated by a drop in pH (e.g., cathepsin L) (Figure 7; Hoffmann et al., 2020a,b)."}

    LitCovid-sample-sentences

    {"project":"LitCovid-sample-sentences","denotations":[{"id":"T267","span":{"begin":0,"end":393},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"SARS-COV-2 shows a large flexibility with regard to protease priming, which may independently occur by a) furin and furin-like proteases intracellularly, b) trypsin-like proteases such as TMPRSS2 that are present on the host cell membrane (particularly on airway epithelial cells), and 3) endosomal cathepsins activated by a drop in pH (e.g., cathepsin L) (Figure 7; Hoffmann et al., 2020a,b)."}

    LitCovid-sample-Pubtator

    {"project":"LitCovid-sample-Pubtator","denotations":[{"id":"1164","span":{"begin":106,"end":111},"obj":"Gene"},{"id":"1165","span":{"begin":188,"end":195},"obj":"Gene"},{"id":"1166","span":{"begin":343,"end":354},"obj":"Gene"},{"id":"1173","span":{"begin":230,"end":238},"obj":"Gene"},{"id":"1180","span":{"begin":0,"end":10},"obj":"Species"},{"id":"1182","span":{"begin":116,"end":121},"obj":"Gene"}],"attributes":[{"id":"A1164","pred":"pubann:denotes","subj":"1164","obj":"Gene:5045"},{"id":"A1165","pred":"pubann:denotes","subj":"1165","obj":"Gene:7113"},{"id":"A1166","pred":"pubann:denotes","subj":"1166","obj":"Gene:1514"},{"id":"A1173","pred":"pubann:denotes","subj":"1173","obj":"Gene:43740571"},{"id":"A1180","pred":"pubann:denotes","subj":"1180","obj":"Tax:2697049"},{"id":"A1182","pred":"pubann:denotes","subj":"1182","obj":"Gene:5045"}],"text":"SARS-COV-2 shows a large flexibility with regard to protease priming, which may independently occur by a) furin and furin-like proteases intracellularly, b) trypsin-like proteases such as TMPRSS2 that are present on the host cell membrane (particularly on airway epithelial cells), and 3) endosomal cathepsins activated by a drop in pH (e.g., cathepsin L) (Figure 7; Hoffmann et al., 2020a,b)."}

    LitCovid-sample-UniProt

    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shows a large flexibility with regard to protease priming, which may independently occur by a) furin and furin-like proteases intracellularly, b) trypsin-like proteases such as TMPRSS2 that are present on the host cell membrane (particularly on airway epithelial cells), and 3) endosomal cathepsins activated by a drop in pH (e.g., cathepsin L) (Figure 7; Hoffmann et al., 2020a,b)."}

    LitCovid-sample-PD-IDO

    {"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T165","span":{"begin":220,"end":224},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T166","span":{"begin":225,"end":229},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T167","span":{"begin":274,"end":279},"obj":"http://purl.obolibrary.org/obo/CL_0000000"}],"text":"SARS-COV-2 shows a large flexibility with regard to protease priming, which may independently occur by a) furin and furin-like proteases intracellularly, b) trypsin-like proteases such as TMPRSS2 that are present on the host cell membrane (particularly on airway epithelial cells), and 3) endosomal cathepsins activated by a drop in pH (e.g., cathepsin L) (Figure 7; Hoffmann et al., 2020a,b)."}

    LitCovid-sample-PD-FMA

    {"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T357","span":{"begin":225,"end":238},"obj":"Body_part"},{"id":"T358","span":{"begin":225,"end":229},"obj":"Body_part"},{"id":"T359","span":{"begin":263,"end":279},"obj":"Body_part"},{"id":"T360","span":{"begin":274,"end":279},"obj":"Body_part"},{"id":"T361","span":{"begin":289,"end":298},"obj":"Body_part"}],"attributes":[{"id":"A357","pred":"fma_id","subj":"T357","obj":"http://purl.org/sig/ont/fma/fma63841"},{"id":"A358","pred":"fma_id","subj":"T358","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A359","pred":"fma_id","subj":"T359","obj":"http://purl.org/sig/ont/fma/fma66768"},{"id":"A360","pred":"fma_id","subj":"T360","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A361","pred":"fma_id","subj":"T361","obj":"http://purl.org/sig/ont/fma/fma67180"}],"text":"SARS-COV-2 shows a large flexibility with regard to protease priming, which may independently occur by a) furin and furin-like proteases intracellularly, b) trypsin-like proteases such as TMPRSS2 that are present on the host cell membrane (particularly on airway epithelial cells), and 3) endosomal cathepsins activated by a drop in pH (e.g., cathepsin L) (Figure 7; Hoffmann et al., 2020a,b)."}

    LitCovid-sample-PD-MONDO

    {"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T174","span":{"begin":0,"end":10},"obj":"Disease"},{"id":"T175","span":{"begin":0,"end":4},"obj":"Disease"}],"attributes":[{"id":"A174","pred":"mondo_id","subj":"T174","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A175","pred":"mondo_id","subj":"T175","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"SARS-COV-2 shows a large flexibility with regard to protease priming, which may independently occur by a) furin and furin-like proteases intracellularly, b) trypsin-like proteases such as TMPRSS2 that are present on the host cell membrane (particularly on airway epithelial cells), and 3) endosomal cathepsins activated by a drop in pH (e.g., cathepsin L) (Figure 7; Hoffmann et al., 2020a,b)."}

    LitCovid-PubTator

    {"project":"LitCovid-PubTator","denotations":[{"id":"1164","span":{"begin":106,"end":111},"obj":"Gene"},{"id":"1165","span":{"begin":188,"end":195},"obj":"Gene"},{"id":"1166","span":{"begin":343,"end":354},"obj":"Gene"},{"id":"1173","span":{"begin":230,"end":238},"obj":"Gene"},{"id":"1180","span":{"begin":0,"end":10},"obj":"Species"},{"id":"1182","span":{"begin":116,"end":121},"obj":"Gene"}],"attributes":[{"id":"A1164","pred":"tao:has_database_id","subj":"1164","obj":"Gene:5045"},{"id":"A1165","pred":"tao:has_database_id","subj":"1165","obj":"Gene:7113"},{"id":"A1166","pred":"tao:has_database_id","subj":"1166","obj":"Gene:1514"},{"id":"A1173","pred":"tao:has_database_id","subj":"1173","obj":"Gene:43740571"},{"id":"A1180","pred":"tao:has_database_id","subj":"1180","obj":"Tax:2697049"},{"id":"A1182","pred":"tao:has_database_id","subj":"1182","obj":"Gene:5045"}],"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":"SARS-COV-2 shows a large flexibility with regard to protease priming, which may independently occur by a) furin and furin-like proteases intracellularly, b) trypsin-like proteases such as TMPRSS2 that are present on the host cell membrane (particularly on airway epithelial cells), and 3) endosomal cathepsins activated by a drop in pH (e.g., cathepsin L) (Figure 7; Hoffmann et al., 2020a,b)."}

    LitCovid-sentences

    {"project":"LitCovid-sentences","denotations":[{"id":"T267","span":{"begin":0,"end":393},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"SARS-COV-2 shows a large flexibility with regard to protease priming, which may independently occur by a) furin and furin-like proteases intracellularly, b) trypsin-like proteases such as TMPRSS2 that are present on the host cell membrane (particularly on airway epithelial cells), and 3) endosomal cathepsins activated by a drop in pH (e.g., cathepsin L) (Figure 7; Hoffmann et al., 2020a,b)."}