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    LitCovid-PD-FMA-UBERON

    {"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T453","span":{"begin":271,"end":277},"obj":"Body_part"},{"id":"T454","span":{"begin":332,"end":336},"obj":"Body_part"},{"id":"T455","span":{"begin":392,"end":397},"obj":"Body_part"},{"id":"T456","span":{"begin":566,"end":572},"obj":"Body_part"},{"id":"T457","span":{"begin":588,"end":593},"obj":"Body_part"},{"id":"T458","span":{"begin":611,"end":614},"obj":"Body_part"},{"id":"T459","span":{"begin":635,"end":640},"obj":"Body_part"},{"id":"T460","span":{"begin":701,"end":711},"obj":"Body_part"},{"id":"T461","span":{"begin":751,"end":756},"obj":"Body_part"},{"id":"T462","span":{"begin":766,"end":772},"obj":"Body_part"}],"attributes":[{"id":"A453","pred":"fma_id","subj":"T453","obj":"http://purl.org/sig/ont/fma/fma82764"},{"id":"A454","pred":"fma_id","subj":"T454","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A455","pred":"fma_id","subj":"T455","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A456","pred":"fma_id","subj":"T456","obj":"http://purl.org/sig/ont/fma/fma7203"},{"id":"A457","pred":"fma_id","subj":"T457","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A458","pred":"fma_id","subj":"T458","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A459","pred":"fma_id","subj":"T459","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A460","pred":"fma_id","subj":"T460","obj":"http://purl.org/sig/ont/fma/fma82739"},{"id":"A461","pred":"fma_id","subj":"T461","obj":"http://purl.org/sig/ont/fma/fma68877"},{"id":"A462","pred":"fma_id","subj":"T462","obj":"http://purl.org/sig/ont/fma/fma82764"}],"text":"The fact that SARS- and MERS-CoV infections are potentiated by TMPRSS2 indicates that TMPRSS2 is a promising target for therapeutic agents. For example, several Ser protease inhibitors such as camostat mesylate inhibit TMPRSS2–ACE2-involved SARS-CoV-2 entry. camostat, a serine protease inhibitor, reduces influenza virus titers in cell culture. camostat-treated TMPRSS2 inhibition in Calu-3 cells greatly reduces SARS-CoV viral titers and improves survival rate in SARS-CoV infected mice. A treatment of 10-μM camostat blocks MERS-CoV entry to African green monkey kidney (Vero)-TMPRSS2 cells and blocks viral RNA synthesis in Calu-3 cells upon MERS-CoV infection. Aprotinin is a polypeptide with 58 amino acid residues that was isolated from bovine lungs. Another serine protease inhibitor, nafamostat, inhibits MERS-CoV entry and infection by TMPRSS2 inhibition [93]. nafamostat mesylate blocks the TMPRSS2–ACE2-involved SARS-CoV-2 envelope–PM fusion and prevents SARS-CoV-2 entry [95]. nafamostat mesylate inhibits viral entry and thrombosis in COVID-19 patients. Similarly, an FDA-approved mucolytic cough suppressant, Bromhexine hydrochloride (BHH), inhibits TMPRSS2 (IC50 0.75 μM) and hence blocks infection of CoV and influenza virus. MPRSS2 as a host factor plays a pivotal role in SARS-CoV and MERS-CoV infections. FDA-approved TMPRSS2 inhibitors are yet under development. Because TMPRSS2 mediates efficient viral entry and replication, it should be a promising target for new therapeutics against CoV infection."}

    LitCovid-PD-UBERON

    {"project":"LitCovid-PD-UBERON","denotations":[{"id":"T25","span":{"begin":566,"end":572},"obj":"Body_part"}],"attributes":[{"id":"A25","pred":"uberon_id","subj":"T25","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"}],"text":"The fact that SARS- and MERS-CoV infections are potentiated by TMPRSS2 indicates that TMPRSS2 is a promising target for therapeutic agents. For example, several Ser protease inhibitors such as camostat mesylate inhibit TMPRSS2–ACE2-involved SARS-CoV-2 entry. camostat, a serine protease inhibitor, reduces influenza virus titers in cell culture. camostat-treated TMPRSS2 inhibition in Calu-3 cells greatly reduces SARS-CoV viral titers and improves survival rate in SARS-CoV infected mice. A treatment of 10-μM camostat blocks MERS-CoV entry to African green monkey kidney (Vero)-TMPRSS2 cells and blocks viral RNA synthesis in Calu-3 cells upon MERS-CoV infection. Aprotinin is a polypeptide with 58 amino acid residues that was isolated from bovine lungs. Another serine protease inhibitor, nafamostat, inhibits MERS-CoV entry and infection by TMPRSS2 inhibition [93]. nafamostat mesylate blocks the TMPRSS2–ACE2-involved SARS-CoV-2 envelope–PM fusion and prevents SARS-CoV-2 entry [95]. nafamostat mesylate inhibits viral entry and thrombosis in COVID-19 patients. Similarly, an FDA-approved mucolytic cough suppressant, Bromhexine hydrochloride (BHH), inhibits TMPRSS2 (IC50 0.75 μM) and hence blocks infection of CoV and influenza virus. MPRSS2 as a host factor plays a pivotal role in SARS-CoV and MERS-CoV infections. FDA-approved TMPRSS2 inhibitors are yet under development. Because TMPRSS2 mediates efficient viral entry and replication, it should be a promising target for new therapeutics against CoV infection."}

    LitCovid-PD-MONDO

    {"project":"LitCovid-PD-MONDO","denotations":[{"id":"T204","span":{"begin":14,"end":18},"obj":"Disease"},{"id":"T205","span":{"begin":33,"end":43},"obj":"Disease"},{"id":"T206","span":{"begin":241,"end":249},"obj":"Disease"},{"id":"T207","span":{"begin":306,"end":315},"obj":"Disease"},{"id":"T208","span":{"begin":414,"end":422},"obj":"Disease"},{"id":"T209","span":{"begin":466,"end":474},"obj":"Disease"},{"id":"T210","span":{"begin":655,"end":664},"obj":"Disease"},{"id":"T211","span":{"begin":833,"end":842},"obj":"Disease"},{"id":"T212","span":{"begin":924,"end":932},"obj":"Disease"},{"id":"T213","span":{"begin":967,"end":975},"obj":"Disease"},{"id":"T214","span":{"begin":1035,"end":1045},"obj":"Disease"},{"id":"T215","span":{"begin":1049,"end":1057},"obj":"Disease"},{"id":"T216","span":{"begin":1205,"end":1214},"obj":"Disease"},{"id":"T217","span":{"begin":1226,"end":1235},"obj":"Disease"},{"id":"T218","span":{"begin":1291,"end":1299},"obj":"Disease"},{"id":"T219","span":{"begin":1313,"end":1323},"obj":"Disease"},{"id":"T220","span":{"begin":1513,"end":1522},"obj":"Disease"}],"attributes":[{"id":"A204","pred":"mondo_id","subj":"T204","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A205","pred":"mondo_id","subj":"T205","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A206","pred":"mondo_id","subj":"T206","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A207","pred":"mondo_id","subj":"T207","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A208","pred":"mondo_id","subj":"T208","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A209","pred":"mondo_id","subj":"T209","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A210","pred":"mondo_id","subj":"T210","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A211","pred":"mondo_id","subj":"T211","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A212","pred":"mondo_id","subj":"T212","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A213","pred":"mondo_id","subj":"T213","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A214","pred":"mondo_id","subj":"T214","obj":"http://purl.obolibrary.org/obo/MONDO_0000831"},{"id":"A215","pred":"mondo_id","subj":"T215","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A216","pred":"mondo_id","subj":"T216","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A217","pred":"mondo_id","subj":"T217","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A218","pred":"mondo_id","subj":"T218","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A219","pred":"mondo_id","subj":"T219","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A220","pred":"mondo_id","subj":"T220","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"}],"text":"The fact that SARS- and MERS-CoV infections are potentiated by TMPRSS2 indicates that TMPRSS2 is a promising target for therapeutic agents. For example, several Ser protease inhibitors such as camostat mesylate inhibit TMPRSS2–ACE2-involved SARS-CoV-2 entry. camostat, a serine protease inhibitor, reduces influenza virus titers in cell culture. camostat-treated TMPRSS2 inhibition in Calu-3 cells greatly reduces SARS-CoV viral titers and improves survival rate in SARS-CoV infected mice. A treatment of 10-μM camostat blocks MERS-CoV entry to African green monkey kidney (Vero)-TMPRSS2 cells and blocks viral RNA synthesis in Calu-3 cells upon MERS-CoV infection. Aprotinin is a polypeptide with 58 amino acid residues that was isolated from bovine lungs. Another serine protease inhibitor, nafamostat, inhibits MERS-CoV entry and infection by TMPRSS2 inhibition [93]. nafamostat mesylate blocks the TMPRSS2–ACE2-involved SARS-CoV-2 envelope–PM fusion and prevents SARS-CoV-2 entry [95]. nafamostat mesylate inhibits viral entry and thrombosis in COVID-19 patients. Similarly, an FDA-approved mucolytic cough suppressant, Bromhexine hydrochloride (BHH), inhibits TMPRSS2 (IC50 0.75 μM) and hence blocks infection of CoV and influenza virus. MPRSS2 as a host factor plays a pivotal role in SARS-CoV and MERS-CoV infections. FDA-approved TMPRSS2 inhibitors are yet under development. Because TMPRSS2 mediates efficient viral entry and replication, it should be a promising target for new therapeutics against CoV infection."}

    LitCovid-PD-CLO

    {"project":"LitCovid-PD-CLO","denotations":[{"id":"T717","span":{"begin":97,"end":98},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T718","span":{"begin":269,"end":270},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T719","span":{"begin":316,"end":321},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T720","span":{"begin":332,"end":336},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T721","span":{"begin":385,"end":397},"obj":"http://purl.obolibrary.org/obo/CLO_0051840"},{"id":"T722","span":{"begin":385,"end":397},"obj":"http://purl.obolibrary.org/obo/CLO_0051841"},{"id":"T723","span":{"begin":385,"end":397},"obj":"http://purl.obolibrary.org/obo/CLO_0051842"},{"id":"T724","span":{"begin":385,"end":397},"obj":"http://purl.obolibrary.org/obo/CLO_0051843"},{"id":"T725","span":{"begin":385,"end":397},"obj":"http://purl.obolibrary.org/obo/CLO_0051844"},{"id":"T726","span":{"begin":385,"end":391},"obj":"http://purl.obolibrary.org/obo/CLO_0002192"},{"id":"T727","span":{"begin":490,"end":491},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T728","span":{"begin":559,"end":565},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9479"},{"id":"T729","span":{"begin":566,"end":572},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"T730","span":{"begin":566,"end":572},"obj":"http://www.ebi.ac.uk/efo/EFO_0000927"},{"id":"T731","span":{"begin":566,"end":572},"obj":"http://www.ebi.ac.uk/efo/EFO_0000929"},{"id":"T732","span":{"begin":574,"end":578},"obj":"http://purl.obolibrary.org/obo/CLO_0009524"},{"id":"T733","span":{"begin":574,"end":578},"obj":"http://purl.obolibrary.org/obo/CLO_0050515"},{"id":"T734","span":{"begin":588,"end":593},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T735","span":{"begin":628,"end":640},"obj":"http://purl.obolibrary.org/obo/CLO_0051840"},{"id":"T736","span":{"begin":628,"end":640},"obj":"http://purl.obolibrary.org/obo/CLO_0051841"},{"id":"T737","span":{"begin":628,"end":640},"obj":"http://purl.obolibrary.org/obo/CLO_0051842"},{"id":"T738","span":{"begin":628,"end":640},"obj":"http://purl.obolibrary.org/obo/CLO_0051843"},{"id":"T739","span":{"begin":628,"end":640},"obj":"http://purl.obolibrary.org/obo/CLO_0051844"},{"id":"T740","span":{"begin":628,"end":634},"obj":"http://purl.obolibrary.org/obo/CLO_0002192"},{"id":"T741","span":{"begin":679,"end":680},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T742","span":{"begin":701,"end":720},"obj":"http://purl.obolibrary.org/obo/CHEBI_33708"},{"id":"T743","span":{"begin":701,"end":720},"obj":"http://purl.obolibrary.org/obo/PR_000036907"},{"id":"T744","span":{"begin":751,"end":756},"obj":"http://www.ebi.ac.uk/efo/EFO_0000934"},{"id":"T745","span":{"begin":1236,"end":1241},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T746","span":{"begin":1253,"end":1254},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T747","span":{"begin":1273,"end":1274},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T748","span":{"begin":1461,"end":1462},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"The fact that SARS- and MERS-CoV infections are potentiated by TMPRSS2 indicates that TMPRSS2 is a promising target for therapeutic agents. For example, several Ser protease inhibitors such as camostat mesylate inhibit TMPRSS2–ACE2-involved SARS-CoV-2 entry. camostat, a serine protease inhibitor, reduces influenza virus titers in cell culture. camostat-treated TMPRSS2 inhibition in Calu-3 cells greatly reduces SARS-CoV viral titers and improves survival rate in SARS-CoV infected mice. A treatment of 10-μM camostat blocks MERS-CoV entry to African green monkey kidney (Vero)-TMPRSS2 cells and blocks viral RNA synthesis in Calu-3 cells upon MERS-CoV infection. Aprotinin is a polypeptide with 58 amino acid residues that was isolated from bovine lungs. Another serine protease inhibitor, nafamostat, inhibits MERS-CoV entry and infection by TMPRSS2 inhibition [93]. nafamostat mesylate blocks the TMPRSS2–ACE2-involved SARS-CoV-2 envelope–PM fusion and prevents SARS-CoV-2 entry [95]. nafamostat mesylate inhibits viral entry and thrombosis in COVID-19 patients. Similarly, an FDA-approved mucolytic cough suppressant, Bromhexine hydrochloride (BHH), inhibits TMPRSS2 (IC50 0.75 μM) and hence blocks infection of CoV and influenza virus. MPRSS2 as a host factor plays a pivotal role in SARS-CoV and MERS-CoV infections. FDA-approved TMPRSS2 inhibitors are yet under development. Because TMPRSS2 mediates efficient viral entry and replication, it should be a promising target for new therapeutics against CoV infection."}

    LitCovid-PD-CHEBI

    {"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T46","span":{"begin":161,"end":164},"obj":"Chemical"},{"id":"T48","span":{"begin":165,"end":184},"obj":"Chemical"},{"id":"T50","span":{"begin":174,"end":184},"obj":"Chemical"},{"id":"T51","span":{"begin":193,"end":210},"obj":"Chemical"},{"id":"T76162","span":{"begin":259,"end":267},"obj":"Chemical"},{"id":"T53","span":{"begin":271,"end":296},"obj":"Chemical"},{"id":"T54","span":{"begin":271,"end":277},"obj":"Chemical"},{"id":"T55","span":{"begin":278,"end":296},"obj":"Chemical"},{"id":"T23789","span":{"begin":287,"end":296},"obj":"Chemical"},{"id":"T43182","span":{"begin":346,"end":354},"obj":"Chemical"},{"id":"T59","span":{"begin":511,"end":519},"obj":"Chemical"},{"id":"T60","span":{"begin":681,"end":692},"obj":"Chemical"},{"id":"T61","span":{"begin":701,"end":711},"obj":"Chemical"},{"id":"T62","span":{"begin":701,"end":706},"obj":"Chemical"},{"id":"T62698","span":{"begin":707,"end":711},"obj":"Chemical"},{"id":"T64","span":{"begin":766,"end":791},"obj":"Chemical"},{"id":"T65","span":{"begin":766,"end":772},"obj":"Chemical"},{"id":"T66","span":{"begin":773,"end":791},"obj":"Chemical"},{"id":"T57087","span":{"begin":782,"end":791},"obj":"Chemical"},{"id":"T93241","span":{"begin":793,"end":803},"obj":"Chemical"},{"id":"T70","span":{"begin":871,"end":890},"obj":"Chemical"},{"id":"T84586","span":{"begin":944,"end":946},"obj":"Chemical"},{"id":"T74","span":{"begin":990,"end":1009},"obj":"Chemical"},{"id":"T75","span":{"begin":1095,"end":1104},"obj":"Chemical"},{"id":"T76","span":{"begin":1105,"end":1122},"obj":"Chemical"},{"id":"T77","span":{"begin":1124,"end":1148},"obj":"Chemical"},{"id":"T78217","span":{"begin":1135,"end":1148},"obj":"Chemical"},{"id":"T79","span":{"begin":1346,"end":1356},"obj":"Chemical"}],"attributes":[{"id":"A39907","pred":"chebi_id","subj":"T46","obj":"http://purl.obolibrary.org/obo/CHEBI_17115"},{"id":"A14257","pred":"chebi_id","subj":"T46","obj":"http://purl.obolibrary.org/obo/CHEBI_29999"},{"id":"A8646","pred":"chebi_id","subj":"T48","obj":"http://purl.obolibrary.org/obo/CHEBI_37670"},{"id":"A1536","pred":"chebi_id","subj":"T48","obj":"http://purl.obolibrary.org/obo/CHEBI_60258"},{"id":"A4854","pred":"chebi_id","subj":"T50","obj":"http://purl.obolibrary.org/obo/CHEBI_35222"},{"id":"A87440","pred":"chebi_id","subj":"T51","obj":"http://purl.obolibrary.org/obo/CHEBI_135632"},{"id":"A76156","pred":"chebi_id","subj":"T76162","obj":"http://purl.obolibrary.org/obo/CHEBI_135632"},{"id":"A47951","pred":"chebi_id","subj":"T53","obj":"http://purl.obolibrary.org/obo/CHEBI_64926"},{"id":"A60898","pred":"chebi_id","subj":"T54","obj":"http://purl.obolibrary.org/obo/CHEBI_17822"},{"id":"A41232","pred":"chebi_id","subj":"T55","obj":"http://purl.obolibrary.org/obo/CHEBI_37670"},{"id":"A82607","pred":"chebi_id","subj":"T55","obj":"http://purl.obolibrary.org/obo/CHEBI_60258"},{"id":"A37247","pred":"chebi_id","subj":"T23789","obj":"http://purl.obolibrary.org/obo/CHEBI_35222"},{"id":"A87380","pred":"chebi_id","subj":"T43182","obj":"http://purl.obolibrary.org/obo/CHEBI_135632"},{"id":"A85423","pred":"chebi_id","subj":"T59","obj":"http://purl.obolibrary.org/obo/CHEBI_135632"},{"id":"A9751","pred":"chebi_id","subj":"T60","obj":"http://purl.obolibrary.org/obo/CHEBI_15841"},{"id":"A31701","pred":"chebi_id","subj":"T61","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"},{"id":"A42352","pred":"chebi_id","subj":"T62","obj":"http://purl.obolibrary.org/obo/CHEBI_46882"},{"id":"A18534","pred":"chebi_id","subj":"T62698","obj":"http://purl.obolibrary.org/obo/CHEBI_37527"},{"id":"A59415","pred":"chebi_id","subj":"T64","obj":"http://purl.obolibrary.org/obo/CHEBI_64926"},{"id":"A89222","pred":"chebi_id","subj":"T65","obj":"http://purl.obolibrary.org/obo/CHEBI_17822"},{"id":"A80953","pred":"chebi_id","subj":"T66","obj":"http://purl.obolibrary.org/obo/CHEBI_37670"},{"id":"A47692","pred":"chebi_id","subj":"T66","obj":"http://purl.obolibrary.org/obo/CHEBI_60258"},{"id":"A98308","pred":"chebi_id","subj":"T57087","obj":"http://purl.obolibrary.org/obo/CHEBI_35222"},{"id":"A23595","pred":"chebi_id","subj":"T93241","obj":"http://purl.obolibrary.org/obo/CHEBI_135466"},{"id":"A58541","pred":"chebi_id","subj":"T70","obj":"http://purl.obolibrary.org/obo/CHEBI_135466"},{"id":"A64016","pred":"chebi_id","subj":"T84586","obj":"http://purl.obolibrary.org/obo/CHEBI_141444"},{"id":"A90486","pred":"chebi_id","subj":"T84586","obj":"http://purl.obolibrary.org/obo/CHEBI_16410"},{"id":"A70766","pred":"chebi_id","subj":"T84586","obj":"http://purl.obolibrary.org/obo/CHEBI_53551"},{"id":"A41557","pred":"chebi_id","subj":"T74","obj":"http://purl.obolibrary.org/obo/CHEBI_135466"},{"id":"A14291","pred":"chebi_id","subj":"T75","obj":"http://purl.obolibrary.org/obo/CHEBI_77034"},{"id":"A52094","pred":"chebi_id","subj":"T76","obj":"http://purl.obolibrary.org/obo/CHEBI_51177"},{"id":"A67133","pred":"chebi_id","subj":"T77","obj":"http://purl.obolibrary.org/obo/CHEBI_31303"},{"id":"A28470","pred":"chebi_id","subj":"T78217","obj":"http://purl.obolibrary.org/obo/CHEBI_36807"},{"id":"A32264","pred":"chebi_id","subj":"T79","obj":"http://purl.obolibrary.org/obo/CHEBI_35222"}],"text":"The fact that SARS- and MERS-CoV infections are potentiated by TMPRSS2 indicates that TMPRSS2 is a promising target for therapeutic agents. For example, several Ser protease inhibitors such as camostat mesylate inhibit TMPRSS2–ACE2-involved SARS-CoV-2 entry. camostat, a serine protease inhibitor, reduces influenza virus titers in cell culture. camostat-treated TMPRSS2 inhibition in Calu-3 cells greatly reduces SARS-CoV viral titers and improves survival rate in SARS-CoV infected mice. A treatment of 10-μM camostat blocks MERS-CoV entry to African green monkey kidney (Vero)-TMPRSS2 cells and blocks viral RNA synthesis in Calu-3 cells upon MERS-CoV infection. Aprotinin is a polypeptide with 58 amino acid residues that was isolated from bovine lungs. Another serine protease inhibitor, nafamostat, inhibits MERS-CoV entry and infection by TMPRSS2 inhibition [93]. nafamostat mesylate blocks the TMPRSS2–ACE2-involved SARS-CoV-2 envelope–PM fusion and prevents SARS-CoV-2 entry [95]. nafamostat mesylate inhibits viral entry and thrombosis in COVID-19 patients. Similarly, an FDA-approved mucolytic cough suppressant, Bromhexine hydrochloride (BHH), inhibits TMPRSS2 (IC50 0.75 μM) and hence blocks infection of CoV and influenza virus. MPRSS2 as a host factor plays a pivotal role in SARS-CoV and MERS-CoV infections. FDA-approved TMPRSS2 inhibitors are yet under development. Because TMPRSS2 mediates efficient viral entry and replication, it should be a promising target for new therapeutics against CoV infection."}

    LitCovid-PD-GO-BP

    {"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T85","span":{"begin":611,"end":624},"obj":"http://purl.obolibrary.org/obo/GO_0032774"},{"id":"T86","span":{"begin":615,"end":624},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"The fact that SARS- and MERS-CoV infections are potentiated by TMPRSS2 indicates that TMPRSS2 is a promising target for therapeutic agents. For example, several Ser protease inhibitors such as camostat mesylate inhibit TMPRSS2–ACE2-involved SARS-CoV-2 entry. camostat, a serine protease inhibitor, reduces influenza virus titers in cell culture. camostat-treated TMPRSS2 inhibition in Calu-3 cells greatly reduces SARS-CoV viral titers and improves survival rate in SARS-CoV infected mice. A treatment of 10-μM camostat blocks MERS-CoV entry to African green monkey kidney (Vero)-TMPRSS2 cells and blocks viral RNA synthesis in Calu-3 cells upon MERS-CoV infection. Aprotinin is a polypeptide with 58 amino acid residues that was isolated from bovine lungs. Another serine protease inhibitor, nafamostat, inhibits MERS-CoV entry and infection by TMPRSS2 inhibition [93]. nafamostat mesylate blocks the TMPRSS2–ACE2-involved SARS-CoV-2 envelope–PM fusion and prevents SARS-CoV-2 entry [95]. nafamostat mesylate inhibits viral entry and thrombosis in COVID-19 patients. Similarly, an FDA-approved mucolytic cough suppressant, Bromhexine hydrochloride (BHH), inhibits TMPRSS2 (IC50 0.75 μM) and hence blocks infection of CoV and influenza virus. MPRSS2 as a host factor plays a pivotal role in SARS-CoV and MERS-CoV infections. FDA-approved TMPRSS2 inhibitors are yet under development. Because TMPRSS2 mediates efficient viral entry and replication, it should be a promising target for new therapeutics against CoV infection."}

    LitCovid-sentences

    {"project":"LitCovid-sentences","denotations":[{"id":"T509","span":{"begin":0,"end":139},"obj":"Sentence"},{"id":"T510","span":{"begin":140,"end":489},"obj":"Sentence"},{"id":"T511","span":{"begin":490,"end":665},"obj":"Sentence"},{"id":"T512","span":{"begin":666,"end":757},"obj":"Sentence"},{"id":"T513","span":{"begin":758,"end":1067},"obj":"Sentence"},{"id":"T514","span":{"begin":1068,"end":1242},"obj":"Sentence"},{"id":"T515","span":{"begin":1243,"end":1324},"obj":"Sentence"},{"id":"T516","span":{"begin":1325,"end":1383},"obj":"Sentence"},{"id":"T517","span":{"begin":1384,"end":1523},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The fact that SARS- and MERS-CoV infections are potentiated by TMPRSS2 indicates that TMPRSS2 is a promising target for therapeutic agents. For example, several Ser protease inhibitors such as camostat mesylate inhibit TMPRSS2–ACE2-involved SARS-CoV-2 entry. camostat, a serine protease inhibitor, reduces influenza virus titers in cell culture. camostat-treated TMPRSS2 inhibition in Calu-3 cells greatly reduces SARS-CoV viral titers and improves survival rate in SARS-CoV infected mice. A treatment of 10-μM camostat blocks MERS-CoV entry to African green monkey kidney (Vero)-TMPRSS2 cells and blocks viral RNA synthesis in Calu-3 cells upon MERS-CoV infection. Aprotinin is a polypeptide with 58 amino acid residues that was isolated from bovine lungs. Another serine protease inhibitor, nafamostat, inhibits MERS-CoV entry and infection by TMPRSS2 inhibition [93]. nafamostat mesylate blocks the TMPRSS2–ACE2-involved SARS-CoV-2 envelope–PM fusion and prevents SARS-CoV-2 entry [95]. nafamostat mesylate inhibits viral entry and thrombosis in COVID-19 patients. Similarly, an FDA-approved mucolytic cough suppressant, Bromhexine hydrochloride (BHH), inhibits TMPRSS2 (IC50 0.75 μM) and hence blocks infection of CoV and influenza virus. MPRSS2 as a host factor plays a pivotal role in SARS-CoV and MERS-CoV infections. FDA-approved TMPRSS2 inhibitors are yet under development. Because TMPRSS2 mediates efficient viral entry and replication, it should be a promising target for new therapeutics against CoV infection."}

    2_test

    {"project":"2_test","denotations":[{"id":"32604730-10485450-51944057","span":{"begin":866,"end":868},"obj":"10485450"},{"id":"32604730-32139904-51944058","span":{"begin":985,"end":987},"obj":"32139904"},{"id":"T88382","span":{"begin":866,"end":868},"obj":"10485450"},{"id":"T92226","span":{"begin":985,"end":987},"obj":"32139904"}],"text":"The fact that SARS- and MERS-CoV infections are potentiated by TMPRSS2 indicates that TMPRSS2 is a promising target for therapeutic agents. For example, several Ser protease inhibitors such as camostat mesylate inhibit TMPRSS2–ACE2-involved SARS-CoV-2 entry. camostat, a serine protease inhibitor, reduces influenza virus titers in cell culture. camostat-treated TMPRSS2 inhibition in Calu-3 cells greatly reduces SARS-CoV viral titers and improves survival rate in SARS-CoV infected mice. A treatment of 10-μM camostat blocks MERS-CoV entry to African green monkey kidney (Vero)-TMPRSS2 cells and blocks viral RNA synthesis in Calu-3 cells upon MERS-CoV infection. Aprotinin is a polypeptide with 58 amino acid residues that was isolated from bovine lungs. Another serine protease inhibitor, nafamostat, inhibits MERS-CoV entry and infection by TMPRSS2 inhibition [93]. nafamostat mesylate blocks the TMPRSS2–ACE2-involved SARS-CoV-2 envelope–PM fusion and prevents SARS-CoV-2 entry [95]. nafamostat mesylate inhibits viral entry and thrombosis in COVID-19 patients. Similarly, an FDA-approved mucolytic cough suppressant, Bromhexine hydrochloride (BHH), inhibits TMPRSS2 (IC50 0.75 μM) and hence blocks infection of CoV and influenza virus. MPRSS2 as a host factor plays a pivotal role in SARS-CoV and MERS-CoV infections. FDA-approved TMPRSS2 inhibitors are yet under development. Because TMPRSS2 mediates efficient viral entry and replication, it should be a promising target for new therapeutics against CoV infection."}

    LitCovid-PD-HP

    {"project":"LitCovid-PD-HP","denotations":[{"id":"T14","span":{"begin":1105,"end":1110},"obj":"Phenotype"}],"attributes":[{"id":"A14","pred":"hp_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/HP_0012735"}],"text":"The fact that SARS- and MERS-CoV infections are potentiated by TMPRSS2 indicates that TMPRSS2 is a promising target for therapeutic agents. For example, several Ser protease inhibitors such as camostat mesylate inhibit TMPRSS2–ACE2-involved SARS-CoV-2 entry. camostat, a serine protease inhibitor, reduces influenza virus titers in cell culture. camostat-treated TMPRSS2 inhibition in Calu-3 cells greatly reduces SARS-CoV viral titers and improves survival rate in SARS-CoV infected mice. A treatment of 10-μM camostat blocks MERS-CoV entry to African green monkey kidney (Vero)-TMPRSS2 cells and blocks viral RNA synthesis in Calu-3 cells upon MERS-CoV infection. Aprotinin is a polypeptide with 58 amino acid residues that was isolated from bovine lungs. Another serine protease inhibitor, nafamostat, inhibits MERS-CoV entry and infection by TMPRSS2 inhibition [93]. nafamostat mesylate blocks the TMPRSS2–ACE2-involved SARS-CoV-2 envelope–PM fusion and prevents SARS-CoV-2 entry [95]. nafamostat mesylate inhibits viral entry and thrombosis in COVID-19 patients. Similarly, an FDA-approved mucolytic cough suppressant, Bromhexine hydrochloride (BHH), inhibits TMPRSS2 (IC50 0.75 μM) and hence blocks infection of CoV and influenza virus. MPRSS2 as a host factor plays a pivotal role in SARS-CoV and MERS-CoV infections. FDA-approved TMPRSS2 inhibitors are yet under development. Because TMPRSS2 mediates efficient viral entry and replication, it should be a promising target for new therapeutics against CoV infection."}