PMC:7352545 / 69110-70654 JSONTXT

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    LitCovid-PD-FMA-UBERON

    {"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T658","span":{"begin":175,"end":178},"obj":"Body_part"},{"id":"T659","span":{"begin":452,"end":465},"obj":"Body_part"},{"id":"T660","span":{"begin":452,"end":456},"obj":"Body_part"},{"id":"T661","span":{"begin":489,"end":496},"obj":"Body_part"},{"id":"T662","span":{"begin":594,"end":606},"obj":"Body_part"},{"id":"T663","span":{"begin":673,"end":678},"obj":"Body_part"},{"id":"T664","span":{"begin":722,"end":734},"obj":"Body_part"},{"id":"T665","span":{"begin":858,"end":863},"obj":"Body_part"},{"id":"T666","span":{"begin":899,"end":904},"obj":"Body_part"},{"id":"T667","span":{"begin":937,"end":941},"obj":"Body_part"},{"id":"T668","span":{"begin":942,"end":945},"obj":"Body_part"},{"id":"T669","span":{"begin":1051,"end":1056},"obj":"Body_part"},{"id":"T670","span":{"begin":1072,"end":1077},"obj":"Body_part"},{"id":"T671","span":{"begin":1090,"end":1098},"obj":"Body_part"},{"id":"T672","span":{"begin":1141,"end":1146},"obj":"Body_part"},{"id":"T673","span":{"begin":1152,"end":1160},"obj":"Body_part"},{"id":"T674","span":{"begin":1212,"end":1223},"obj":"Body_part"},{"id":"T675","span":{"begin":1232,"end":1241},"obj":"Body_part"},{"id":"T676","span":{"begin":1251,"end":1259},"obj":"Body_part"},{"id":"T677","span":{"begin":1284,"end":1300},"obj":"Body_part"},{"id":"T678","span":{"begin":1295,"end":1300},"obj":"Body_part"},{"id":"T679","span":{"begin":1307,"end":1311},"obj":"Body_part"},{"id":"T680","span":{"begin":1379,"end":1383},"obj":"Body_part"},{"id":"T681","span":{"begin":1384,"end":1389},"obj":"Body_part"},{"id":"T682","span":{"begin":1502,"end":1507},"obj":"Body_part"},{"id":"T683","span":{"begin":1535,"end":1543},"obj":"Body_part"}],"attributes":[{"id":"A658","pred":"fma_id","subj":"T658","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A659","pred":"fma_id","subj":"T659","obj":"http://purl.org/sig/ont/fma/fma67653"},{"id":"A660","pred":"fma_id","subj":"T660","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A661","pred":"fma_id","subj":"T661","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A662","pred":"fma_id","subj":"T662","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A663","pred":"fma_id","subj":"T663","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A664","pred":"fma_id","subj":"T664","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A665","pred":"fma_id","subj":"T665","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A666","pred":"fma_id","subj":"T666","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A667","pred":"fma_id","subj":"T667","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A668","pred":"fma_id","subj":"T668","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A669","pred":"fma_id","subj":"T669","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A670","pred":"fma_id","subj":"T670","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A671","pred":"fma_id","subj":"T671","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A672","pred":"fma_id","subj":"T672","obj":"http://purl.org/sig/ont/fma/fma68877"},{"id":"A673","pred":"fma_id","subj":"T673","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A674","pred":"fma_id","subj":"T674","obj":"http://purl.org/sig/ont/fma/fma62499"},{"id":"A675","pred":"fma_id","subj":"T675","obj":"http://purl.org/sig/ont/fma/fma7199"},{"id":"A676","pred":"fma_id","subj":"T676","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A677","pred":"fma_id","subj":"T677","obj":"http://purl.org/sig/ont/fma/fma66768"},{"id":"A678","pred":"fma_id","subj":"T678","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A679","pred":"fma_id","subj":"T679","obj":"http://purl.org/sig/ont/fma/fma74402"},{"id":"A680","pred":"fma_id","subj":"T680","obj":"http://purl.org/sig/ont/fma/fma7195"},{"id":"A681","pred":"fma_id","subj":"T681","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A682","pred":"fma_id","subj":"T682","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A683","pred":"fma_id","subj":"T683","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"The emerging CoV-pandemic requires therapeutic agents to block the recognition, binding, replication, amplification and propagation of the CoV in humans. Protease inhibitors, RNA synthase inhibitors and S2 inhibitors are potential targets, and several agents are currently being evaluated. Efficient therapeutic drugs are the most reliable option for patients. The first attachment step of the viral amplification cycle is initiated on the respiratory cell surfaces, driven by the viral S protein. This is a potential therapeutic target. Soon after the SARS-CoV-2 outbreak initiated, the CoV S glycoprotein was demonstrated to recognize ACE2 as a binding receptor on human cells. Human TMPRSS2 enzyme influences the CoV S glycoprotein activation, to facilitate virus infection. ACE2 binding and TMPRSS2 activation facilitate the CoVs to attach to human host cells. Mouse, nonhuman primate and human cells have been analyzed using single-cell RNA new generation sequencing (NGS). For example, for human infection, CoVs can enter nasal goblet secretory cells, because these cells express the proteins required for SARS-CoV-2 infection. In the lungs, the proteins are stored in the alveoli like air sacs of type II pneumocytes. In the intestine, the two proteins are expressed in entero-epithelial cells. ACE2 gene expression correlates with the IFN-related genes [137]. ACE2 helps lung cells to tolerate cellular damage. Therefore, CoVs may evolutionally take advantage of the defense mechanisms of host cells, hijacking such host-borne proteins."}

    LitCovid-PD-UBERON

    {"project":"LitCovid-PD-UBERON","denotations":[{"id":"T36","span":{"begin":1232,"end":1241},"obj":"Body_part"},{"id":"T37","span":{"begin":1379,"end":1383},"obj":"Body_part"}],"attributes":[{"id":"A36","pred":"uberon_id","subj":"T36","obj":"http://purl.obolibrary.org/obo/UBERON_0000160"},{"id":"A37","pred":"uberon_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"}],"text":"The emerging CoV-pandemic requires therapeutic agents to block the recognition, binding, replication, amplification and propagation of the CoV in humans. Protease inhibitors, RNA synthase inhibitors and S2 inhibitors are potential targets, and several agents are currently being evaluated. Efficient therapeutic drugs are the most reliable option for patients. The first attachment step of the viral amplification cycle is initiated on the respiratory cell surfaces, driven by the viral S protein. This is a potential therapeutic target. Soon after the SARS-CoV-2 outbreak initiated, the CoV S glycoprotein was demonstrated to recognize ACE2 as a binding receptor on human cells. Human TMPRSS2 enzyme influences the CoV S glycoprotein activation, to facilitate virus infection. ACE2 binding and TMPRSS2 activation facilitate the CoVs to attach to human host cells. Mouse, nonhuman primate and human cells have been analyzed using single-cell RNA new generation sequencing (NGS). For example, for human infection, CoVs can enter nasal goblet secretory cells, because these cells express the proteins required for SARS-CoV-2 infection. In the lungs, the proteins are stored in the alveoli like air sacs of type II pneumocytes. In the intestine, the two proteins are expressed in entero-epithelial cells. ACE2 gene expression correlates with the IFN-related genes [137]. ACE2 helps lung cells to tolerate cellular damage. Therefore, CoVs may evolutionally take advantage of the defense mechanisms of host cells, hijacking such host-borne proteins."}

    LitCovid-PD-MONDO

    {"project":"LitCovid-PD-MONDO","denotations":[{"id":"T264","span":{"begin":553,"end":561},"obj":"Disease"},{"id":"T265","span":{"begin":761,"end":776},"obj":"Disease"},{"id":"T266","span":{"begin":767,"end":776},"obj":"Disease"},{"id":"T267","span":{"begin":1002,"end":1011},"obj":"Disease"},{"id":"T268","span":{"begin":1112,"end":1120},"obj":"Disease"},{"id":"T269","span":{"begin":1123,"end":1132},"obj":"Disease"},{"id":"T270","span":{"begin":1196,"end":1200},"obj":"Disease"}],"attributes":[{"id":"A264","pred":"mondo_id","subj":"T264","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A265","pred":"mondo_id","subj":"T265","obj":"http://purl.obolibrary.org/obo/MONDO_0005108"},{"id":"A266","pred":"mondo_id","subj":"T266","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A267","pred":"mondo_id","subj":"T267","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A268","pred":"mondo_id","subj":"T268","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A269","pred":"mondo_id","subj":"T269","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A270","pred":"mondo_id","subj":"T270","obj":"http://purl.obolibrary.org/obo/MONDO_0010041"}],"text":"The emerging CoV-pandemic requires therapeutic agents to block the recognition, binding, replication, amplification and propagation of the CoV in humans. Protease inhibitors, RNA synthase inhibitors and S2 inhibitors are potential targets, and several agents are currently being evaluated. Efficient therapeutic drugs are the most reliable option for patients. The first attachment step of the viral amplification cycle is initiated on the respiratory cell surfaces, driven by the viral S protein. This is a potential therapeutic target. Soon after the SARS-CoV-2 outbreak initiated, the CoV S glycoprotein was demonstrated to recognize ACE2 as a binding receptor on human cells. Human TMPRSS2 enzyme influences the CoV S glycoprotein activation, to facilitate virus infection. ACE2 binding and TMPRSS2 activation facilitate the CoVs to attach to human host cells. Mouse, nonhuman primate and human cells have been analyzed using single-cell RNA new generation sequencing (NGS). For example, for human infection, CoVs can enter nasal goblet secretory cells, because these cells express the proteins required for SARS-CoV-2 infection. In the lungs, the proteins are stored in the alveoli like air sacs of type II pneumocytes. In the intestine, the two proteins are expressed in entero-epithelial cells. ACE2 gene expression correlates with the IFN-related genes [137]. ACE2 helps lung cells to tolerate cellular damage. Therefore, CoVs may evolutionally take advantage of the defense mechanisms of host cells, hijacking such host-borne proteins."}

    LitCovid-PD-CLO

    {"project":"LitCovid-PD-CLO","denotations":[{"id":"T985","span":{"begin":146,"end":152},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T986","span":{"begin":203,"end":205},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T987","span":{"begin":203,"end":205},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"},{"id":"T988","span":{"begin":452,"end":456},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T989","span":{"begin":506,"end":507},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T990","span":{"begin":645,"end":646},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T991","span":{"begin":667,"end":678},"obj":"http://purl.obolibrary.org/obo/CLO_0053065"},{"id":"T992","span":{"begin":680,"end":685},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T993","span":{"begin":735,"end":745},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T994","span":{"begin":761,"end":766},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T995","span":{"begin":803,"end":813},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T996","span":{"begin":847,"end":852},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T997","span":{"begin":858,"end":863},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T998","span":{"begin":865,"end":870},"obj":"http://purl.obolibrary.org/obo/CLO_0007836"},{"id":"T999","span":{"begin":881,"end":888},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9443"},{"id":"T1000","span":{"begin":893,"end":904},"obj":"http://purl.obolibrary.org/obo/CLO_0053065"},{"id":"T1001","span":{"begin":937,"end":941},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T1002","span":{"begin":996,"end":1001},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T1003","span":{"begin":1051,"end":1056},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T1004","span":{"begin":1072,"end":1077},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T1005","span":{"begin":1141,"end":1146},"obj":"http://www.ebi.ac.uk/efo/EFO_0000934"},{"id":"T1006","span":{"begin":1196,"end":1200},"obj":"http://purl.obolibrary.org/obo/UBERON_0009856"},{"id":"T1007","span":{"begin":1232,"end":1241},"obj":"http://purl.obolibrary.org/obo/UBERON_0000160"},{"id":"T1008","span":{"begin":1232,"end":1241},"obj":"http://www.ebi.ac.uk/efo/EFO_0000834"},{"id":"T1009","span":{"begin":1284,"end":1294},"obj":"http://purl.obolibrary.org/obo/CL_0000066"},{"id":"T1010","span":{"begin":1295,"end":1300},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T1011","span":{"begin":1307,"end":1311},"obj":"http://purl.obolibrary.org/obo/OGG_0000000002"},{"id":"T1012","span":{"begin":1355,"end":1360},"obj":"http://purl.obolibrary.org/obo/OGG_0000000002"},{"id":"T1013","span":{"begin":1379,"end":1383},"obj":"http://purl.obolibrary.org/obo/UBERON_0002048"},{"id":"T1014","span":{"begin":1379,"end":1383},"obj":"http://www.ebi.ac.uk/efo/EFO_0000934"},{"id":"T1015","span":{"begin":1384,"end":1389},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T1016","span":{"begin":1502,"end":1507},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"The emerging CoV-pandemic requires therapeutic agents to block the recognition, binding, replication, amplification and propagation of the CoV in humans. Protease inhibitors, RNA synthase inhibitors and S2 inhibitors are potential targets, and several agents are currently being evaluated. Efficient therapeutic drugs are the most reliable option for patients. The first attachment step of the viral amplification cycle is initiated on the respiratory cell surfaces, driven by the viral S protein. This is a potential therapeutic target. Soon after the SARS-CoV-2 outbreak initiated, the CoV S glycoprotein was demonstrated to recognize ACE2 as a binding receptor on human cells. Human TMPRSS2 enzyme influences the CoV S glycoprotein activation, to facilitate virus infection. ACE2 binding and TMPRSS2 activation facilitate the CoVs to attach to human host cells. Mouse, nonhuman primate and human cells have been analyzed using single-cell RNA new generation sequencing (NGS). For example, for human infection, CoVs can enter nasal goblet secretory cells, because these cells express the proteins required for SARS-CoV-2 infection. In the lungs, the proteins are stored in the alveoli like air sacs of type II pneumocytes. In the intestine, the two proteins are expressed in entero-epithelial cells. ACE2 gene expression correlates with the IFN-related genes [137]. ACE2 helps lung cells to tolerate cellular damage. Therefore, CoVs may evolutionally take advantage of the defense mechanisms of host cells, hijacking such host-borne proteins."}

    LitCovid-PD-CHEBI

    {"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T389","span":{"begin":163,"end":173},"obj":"Chemical"},{"id":"T390","span":{"begin":188,"end":198},"obj":"Chemical"},{"id":"T64374","span":{"begin":203,"end":205},"obj":"Chemical"},{"id":"T392","span":{"begin":206,"end":216},"obj":"Chemical"},{"id":"T393","span":{"begin":312,"end":317},"obj":"Chemical"},{"id":"T394","span":{"begin":489,"end":496},"obj":"Chemical"},{"id":"T395","span":{"begin":594,"end":606},"obj":"Chemical"},{"id":"T77170","span":{"begin":722,"end":734},"obj":"Chemical"},{"id":"T397","span":{"begin":1090,"end":1098},"obj":"Chemical"},{"id":"T398","span":{"begin":1152,"end":1160},"obj":"Chemical"},{"id":"T399","span":{"begin":1209,"end":1211},"obj":"Chemical"},{"id":"T400","span":{"begin":1251,"end":1259},"obj":"Chemical"},{"id":"T13740","span":{"begin":1535,"end":1543},"obj":"Chemical"}],"attributes":[{"id":"A66289","pred":"chebi_id","subj":"T389","obj":"http://purl.obolibrary.org/obo/CHEBI_35222"},{"id":"A73762","pred":"chebi_id","subj":"T390","obj":"http://purl.obolibrary.org/obo/CHEBI_35222"},{"id":"A70113","pred":"chebi_id","subj":"T64374","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A61346","pred":"chebi_id","subj":"T392","obj":"http://purl.obolibrary.org/obo/CHEBI_35222"},{"id":"A54177","pred":"chebi_id","subj":"T393","obj":"http://purl.obolibrary.org/obo/CHEBI_23888"},{"id":"A19564","pred":"chebi_id","subj":"T394","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A59355","pred":"chebi_id","subj":"T395","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A93827","pred":"chebi_id","subj":"T77170","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A63139","pred":"chebi_id","subj":"T397","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A46849","pred":"chebi_id","subj":"T398","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A36161","pred":"chebi_id","subj":"T399","obj":"http://purl.obolibrary.org/obo/CHEBI_74067"},{"id":"A34095","pred":"chebi_id","subj":"T400","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A64408","pred":"chebi_id","subj":"T13740","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"The emerging CoV-pandemic requires therapeutic agents to block the recognition, binding, replication, amplification and propagation of the CoV in humans. Protease inhibitors, RNA synthase inhibitors and S2 inhibitors are potential targets, and several agents are currently being evaluated. Efficient therapeutic drugs are the most reliable option for patients. The first attachment step of the viral amplification cycle is initiated on the respiratory cell surfaces, driven by the viral S protein. This is a potential therapeutic target. Soon after the SARS-CoV-2 outbreak initiated, the CoV S glycoprotein was demonstrated to recognize ACE2 as a binding receptor on human cells. Human TMPRSS2 enzyme influences the CoV S glycoprotein activation, to facilitate virus infection. ACE2 binding and TMPRSS2 activation facilitate the CoVs to attach to human host cells. Mouse, nonhuman primate and human cells have been analyzed using single-cell RNA new generation sequencing (NGS). For example, for human infection, CoVs can enter nasal goblet secretory cells, because these cells express the proteins required for SARS-CoV-2 infection. In the lungs, the proteins are stored in the alveoli like air sacs of type II pneumocytes. In the intestine, the two proteins are expressed in entero-epithelial cells. ACE2 gene expression correlates with the IFN-related genes [137]. ACE2 helps lung cells to tolerate cellular damage. Therefore, CoVs may evolutionally take advantage of the defense mechanisms of host cells, hijacking such host-borne proteins."}

    LitCovid-PD-GO-BP

    {"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T128","span":{"begin":1307,"end":1322},"obj":"http://purl.obolibrary.org/obo/GO_0010467"}],"text":"The emerging CoV-pandemic requires therapeutic agents to block the recognition, binding, replication, amplification and propagation of the CoV in humans. Protease inhibitors, RNA synthase inhibitors and S2 inhibitors are potential targets, and several agents are currently being evaluated. Efficient therapeutic drugs are the most reliable option for patients. The first attachment step of the viral amplification cycle is initiated on the respiratory cell surfaces, driven by the viral S protein. This is a potential therapeutic target. Soon after the SARS-CoV-2 outbreak initiated, the CoV S glycoprotein was demonstrated to recognize ACE2 as a binding receptor on human cells. Human TMPRSS2 enzyme influences the CoV S glycoprotein activation, to facilitate virus infection. ACE2 binding and TMPRSS2 activation facilitate the CoVs to attach to human host cells. Mouse, nonhuman primate and human cells have been analyzed using single-cell RNA new generation sequencing (NGS). For example, for human infection, CoVs can enter nasal goblet secretory cells, because these cells express the proteins required for SARS-CoV-2 infection. In the lungs, the proteins are stored in the alveoli like air sacs of type II pneumocytes. In the intestine, the two proteins are expressed in entero-epithelial cells. ACE2 gene expression correlates with the IFN-related genes [137]. ACE2 helps lung cells to tolerate cellular damage. Therefore, CoVs may evolutionally take advantage of the defense mechanisms of host cells, hijacking such host-borne proteins."}

    LitCovid-sentences

    {"project":"LitCovid-sentences","denotations":[{"id":"T669","span":{"begin":0,"end":153},"obj":"Sentence"},{"id":"T670","span":{"begin":154,"end":289},"obj":"Sentence"},{"id":"T671","span":{"begin":290,"end":360},"obj":"Sentence"},{"id":"T672","span":{"begin":361,"end":497},"obj":"Sentence"},{"id":"T673","span":{"begin":498,"end":537},"obj":"Sentence"},{"id":"T674","span":{"begin":538,"end":679},"obj":"Sentence"},{"id":"T675","span":{"begin":680,"end":777},"obj":"Sentence"},{"id":"T676","span":{"begin":778,"end":864},"obj":"Sentence"},{"id":"T677","span":{"begin":865,"end":978},"obj":"Sentence"},{"id":"T678","span":{"begin":979,"end":1133},"obj":"Sentence"},{"id":"T679","span":{"begin":1134,"end":1224},"obj":"Sentence"},{"id":"T680","span":{"begin":1225,"end":1301},"obj":"Sentence"},{"id":"T681","span":{"begin":1302,"end":1367},"obj":"Sentence"},{"id":"T682","span":{"begin":1368,"end":1418},"obj":"Sentence"},{"id":"T683","span":{"begin":1419,"end":1544},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The emerging CoV-pandemic requires therapeutic agents to block the recognition, binding, replication, amplification and propagation of the CoV in humans. Protease inhibitors, RNA synthase inhibitors and S2 inhibitors are potential targets, and several agents are currently being evaluated. Efficient therapeutic drugs are the most reliable option for patients. The first attachment step of the viral amplification cycle is initiated on the respiratory cell surfaces, driven by the viral S protein. This is a potential therapeutic target. Soon after the SARS-CoV-2 outbreak initiated, the CoV S glycoprotein was demonstrated to recognize ACE2 as a binding receptor on human cells. Human TMPRSS2 enzyme influences the CoV S glycoprotein activation, to facilitate virus infection. ACE2 binding and TMPRSS2 activation facilitate the CoVs to attach to human host cells. Mouse, nonhuman primate and human cells have been analyzed using single-cell RNA new generation sequencing (NGS). For example, for human infection, CoVs can enter nasal goblet secretory cells, because these cells express the proteins required for SARS-CoV-2 infection. In the lungs, the proteins are stored in the alveoli like air sacs of type II pneumocytes. In the intestine, the two proteins are expressed in entero-epithelial cells. ACE2 gene expression correlates with the IFN-related genes [137]. ACE2 helps lung cells to tolerate cellular damage. Therefore, CoVs may evolutionally take advantage of the defense mechanisms of host cells, hijacking such host-borne proteins."}

    2_test

    {"project":"2_test","denotations":[{"id":"32604730-32413319-51944103","span":{"begin":1362,"end":1365},"obj":"32413319"},{"id":"T60531","span":{"begin":1362,"end":1365},"obj":"32413319"}],"text":"The emerging CoV-pandemic requires therapeutic agents to block the recognition, binding, replication, amplification and propagation of the CoV in humans. Protease inhibitors, RNA synthase inhibitors and S2 inhibitors are potential targets, and several agents are currently being evaluated. Efficient therapeutic drugs are the most reliable option for patients. The first attachment step of the viral amplification cycle is initiated on the respiratory cell surfaces, driven by the viral S protein. This is a potential therapeutic target. Soon after the SARS-CoV-2 outbreak initiated, the CoV S glycoprotein was demonstrated to recognize ACE2 as a binding receptor on human cells. Human TMPRSS2 enzyme influences the CoV S glycoprotein activation, to facilitate virus infection. ACE2 binding and TMPRSS2 activation facilitate the CoVs to attach to human host cells. Mouse, nonhuman primate and human cells have been analyzed using single-cell RNA new generation sequencing (NGS). For example, for human infection, CoVs can enter nasal goblet secretory cells, because these cells express the proteins required for SARS-CoV-2 infection. In the lungs, the proteins are stored in the alveoli like air sacs of type II pneumocytes. In the intestine, the two proteins are expressed in entero-epithelial cells. ACE2 gene expression correlates with the IFN-related genes [137]. ACE2 helps lung cells to tolerate cellular damage. Therefore, CoVs may evolutionally take advantage of the defense mechanisms of host cells, hijacking such host-borne proteins."}