PMC:7029759 / 20538-22069
Annnotations
LitCovid-PubTator
{"project":"LitCovid-PubTator","denotations":[{"id":"468","span":{"begin":81,"end":85},"obj":"Gene"},{"id":"469","span":{"begin":247,"end":251},"obj":"Gene"},{"id":"470","span":{"begin":470,"end":474},"obj":"Gene"},{"id":"471","span":{"begin":649,"end":653},"obj":"Gene"},{"id":"472","span":{"begin":819,"end":823},"obj":"Gene"},{"id":"473","span":{"begin":1238,"end":1242},"obj":"Gene"},{"id":"474","span":{"begin":1258,"end":1262},"obj":"Gene"},{"id":"475","span":{"begin":996,"end":1005},"obj":"Species"},{"id":"476","span":{"begin":1128,"end":1136},"obj":"Species"},{"id":"477","span":{"begin":114,"end":133},"obj":"Disease"},{"id":"478","span":{"begin":192,"end":196},"obj":"Disease"},{"id":"479","span":{"begin":754,"end":766},"obj":"Disease"}],"attributes":[{"id":"A468","pred":"tao:has_database_id","subj":"468","obj":"Gene:59272"},{"id":"A469","pred":"tao:has_database_id","subj":"469","obj":"Gene:59272"},{"id":"A470","pred":"tao:has_database_id","subj":"470","obj":"Gene:59272"},{"id":"A471","pred":"tao:has_database_id","subj":"471","obj":"Gene:59272"},{"id":"A472","pred":"tao:has_database_id","subj":"472","obj":"Gene:59272"},{"id":"A473","pred":"tao:has_database_id","subj":"473","obj":"Gene:652070"},{"id":"A474","pred":"tao:has_database_id","subj":"474","obj":"Gene:59272"},{"id":"A475","pred":"tao:has_database_id","subj":"475","obj":"Tax:9606"},{"id":"A476","pred":"tao:has_database_id","subj":"476","obj":"Tax:9606"},{"id":"A477","pred":"tao:has_database_id","subj":"477","obj":"MESH:C000657245"},{"id":"A478","pred":"tao:has_database_id","subj":"478","obj":"MESH:D045169"},{"id":"A479","pred":"tao:has_database_id","subj":"479","obj":"MESH:D007249"}],"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":"A second, similar strategy would be to administer an antibody that would bind to ACE2 protein, thereby preventing 2019-nCoV infection ( Figure 1). This strategy was shown to effectively block SARS entry and replication in experiments 42. While no ACE2 antibody sequences are published in literature indexes, monoclonal antibodies do exist and the associated hybridoma sequences could be cloned in a matter of days. There would be no concern for any viral escape from an ACE2 binding antibody, which is an advantage over neutralizing approaches against the S protein. There are a couple of design considerations when thinking about how to employ the ACE2 antibody strategy. Any effector functions would need to be removed from the Fc domain 49, such that inflammation would not be caused in different tissues expressing ACE2. This would retain the long-half life endowed by the Fc domain without any of the side effects. The downside of including the Fc domain is the need to use a more expensive mammalian cell production system to preserve proper glycosylation, which would decrease the turnaround time for getting the drug to patients in the outbreak scenario. Alternatively, one could just administer a single chain variable fragment (scFv) that binds to ACE2. A nanobody or VHH domains from camelids are another option as well 50, 51. These could be produced in bacteria, and its small size would allow for rapid permeation into different tissues. The downside is the shorter half-life of these molecules without the Fc domain."}
LitCovid-PMC-OGER-BB
{"project":"LitCovid-PMC-OGER-BB","denotations":[{"id":"T357","span":{"begin":53,"end":61},"obj":"GO:0042571"},{"id":"T356","span":{"begin":81,"end":85},"obj":"G_3;PG_10;PR:000003622"},{"id":"T355","span":{"begin":114,"end":123},"obj":"SP_7"},{"id":"T354","span":{"begin":192,"end":196},"obj":"SP_10"},{"id":"T353","span":{"begin":207,"end":218},"obj":"GO:0006260"},{"id":"T352","span":{"begin":247,"end":251},"obj":"G_3;PG_10;PR:000003622"},{"id":"T351","span":{"begin":252,"end":260},"obj":"GO:0042571"},{"id":"T350","span":{"begin":319,"end":329},"obj":"GO:0042571"},{"id":"T349","span":{"begin":449,"end":454},"obj":"NCBITaxon:10239"},{"id":"T348","span":{"begin":470,"end":474},"obj":"G_3;PG_10;PR:000003622"},{"id":"T347","span":{"begin":483,"end":491},"obj":"GO:0042571"},{"id":"T346","span":{"begin":556,"end":565},"obj":"PG_1"},{"id":"T345","span":{"begin":649,"end":653},"obj":"G_3;PG_10;PR:000003622"},{"id":"T344","span":{"begin":654,"end":662},"obj":"GO:0042571"},{"id":"T343","span":{"begin":677,"end":685},"obj":"CHEBI:35224;CHEBI:35224"},{"id":"T342","span":{"begin":733,"end":739},"obj":"SO:0000417"},{"id":"T341","span":{"begin":800,"end":807},"obj":"UBERON:0000479"},{"id":"T340","span":{"begin":808,"end":818},"obj":"GO:0010467"},{"id":"T339","span":{"begin":819,"end":823},"obj":"G_3;PG_10;PR:000003622"},{"id":"T338","span":{"begin":880,"end":886},"obj":"SO:0000417"},{"id":"T337","span":{"begin":953,"end":959},"obj":"SO:0000417"},{"id":"T336","span":{"begin":996,"end":1005},"obj":"NCBITaxon:40674"},{"id":"T335","span":{"begin":1006,"end":1021},"obj":"GO:0006412"},{"id":"T334","span":{"begin":1120,"end":1124},"obj":"CHEBI:23888;CHEBI:23888"},{"id":"T333","span":{"begin":1258,"end":1262},"obj":"G_3;PG_10;PR:000003622"},{"id":"T332","span":{"begin":1282,"end":1289},"obj":"SO:0000417"},{"id":"T331","span":{"begin":1366,"end":1374},"obj":"NCBITaxon:2"},{"id":"T330","span":{"begin":1443,"end":1450},"obj":"UBERON:0000479"},{"id":"T329","span":{"begin":1499,"end":1508},"obj":"CHEBI:36357;CHEBI:36357"},{"id":"T328","span":{"begin":1524,"end":1530},"obj":"SO:0000417"}],"text":"A second, similar strategy would be to administer an antibody that would bind to ACE2 protein, thereby preventing 2019-nCoV infection ( Figure 1). This strategy was shown to effectively block SARS entry and replication in experiments 42. While no ACE2 antibody sequences are published in literature indexes, monoclonal antibodies do exist and the associated hybridoma sequences could be cloned in a matter of days. There would be no concern for any viral escape from an ACE2 binding antibody, which is an advantage over neutralizing approaches against the S protein. There are a couple of design considerations when thinking about how to employ the ACE2 antibody strategy. Any effector functions would need to be removed from the Fc domain 49, such that inflammation would not be caused in different tissues expressing ACE2. This would retain the long-half life endowed by the Fc domain without any of the side effects. The downside of including the Fc domain is the need to use a more expensive mammalian cell production system to preserve proper glycosylation, which would decrease the turnaround time for getting the drug to patients in the outbreak scenario. Alternatively, one could just administer a single chain variable fragment (scFv) that binds to ACE2. A nanobody or VHH domains from camelids are another option as well 50, 51. These could be produced in bacteria, and its small size would allow for rapid permeation into different tissues. The downside is the shorter half-life of these molecules without the Fc domain."}
LitCovid-PD-FMA-UBERON
{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T117","span":{"begin":53,"end":61},"obj":"Body_part"},{"id":"T118","span":{"begin":86,"end":93},"obj":"Body_part"},{"id":"T119","span":{"begin":252,"end":260},"obj":"Body_part"},{"id":"T120","span":{"begin":483,"end":491},"obj":"Body_part"},{"id":"T121","span":{"begin":558,"end":565},"obj":"Body_part"},{"id":"T122","span":{"begin":654,"end":662},"obj":"Body_part"},{"id":"T123","span":{"begin":800,"end":807},"obj":"Body_part"},{"id":"T124","span":{"begin":1006,"end":1010},"obj":"Body_part"},{"id":"T125","span":{"begin":1443,"end":1450},"obj":"Body_part"}],"attributes":[{"id":"A117","pred":"fma_id","subj":"T117","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A118","pred":"fma_id","subj":"T118","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A119","pred":"fma_id","subj":"T119","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A120","pred":"fma_id","subj":"T120","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A121","pred":"fma_id","subj":"T121","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A122","pred":"fma_id","subj":"T122","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A123","pred":"fma_id","subj":"T123","obj":"http://purl.org/sig/ont/fma/fma9637"},{"id":"A124","pred":"fma_id","subj":"T124","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A125","pred":"fma_id","subj":"T125","obj":"http://purl.org/sig/ont/fma/fma9637"}],"text":"A second, similar strategy would be to administer an antibody that would bind to ACE2 protein, thereby preventing 2019-nCoV infection ( Figure 1). This strategy was shown to effectively block SARS entry and replication in experiments 42. While no ACE2 antibody sequences are published in literature indexes, monoclonal antibodies do exist and the associated hybridoma sequences could be cloned in a matter of days. There would be no concern for any viral escape from an ACE2 binding antibody, which is an advantage over neutralizing approaches against the S protein. There are a couple of design considerations when thinking about how to employ the ACE2 antibody strategy. Any effector functions would need to be removed from the Fc domain 49, such that inflammation would not be caused in different tissues expressing ACE2. This would retain the long-half life endowed by the Fc domain without any of the side effects. The downside of including the Fc domain is the need to use a more expensive mammalian cell production system to preserve proper glycosylation, which would decrease the turnaround time for getting the drug to patients in the outbreak scenario. Alternatively, one could just administer a single chain variable fragment (scFv) that binds to ACE2. A nanobody or VHH domains from camelids are another option as well 50, 51. These could be produced in bacteria, and its small size would allow for rapid permeation into different tissues. The downside is the shorter half-life of these molecules without the Fc domain."}
LitCovid-PD-MONDO
{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T60","span":{"begin":114,"end":133},"obj":"Disease"},{"id":"T61","span":{"begin":124,"end":133},"obj":"Disease"},{"id":"T62","span":{"begin":192,"end":196},"obj":"Disease"},{"id":"T63","span":{"begin":754,"end":766},"obj":"Disease"}],"attributes":[{"id":"A60","pred":"mondo_id","subj":"T60","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A61","pred":"mondo_id","subj":"T61","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A62","pred":"mondo_id","subj":"T62","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A63","pred":"mondo_id","subj":"T63","obj":"http://purl.obolibrary.org/obo/MONDO_0021166"}],"text":"A second, similar strategy would be to administer an antibody that would bind to ACE2 protein, thereby preventing 2019-nCoV infection ( Figure 1). This strategy was shown to effectively block SARS entry and replication in experiments 42. While no ACE2 antibody sequences are published in literature indexes, monoclonal antibodies do exist and the associated hybridoma sequences could be cloned in a matter of days. There would be no concern for any viral escape from an ACE2 binding antibody, which is an advantage over neutralizing approaches against the S protein. There are a couple of design considerations when thinking about how to employ the ACE2 antibody strategy. Any effector functions would need to be removed from the Fc domain 49, such that inflammation would not be caused in different tissues expressing ACE2. This would retain the long-half life endowed by the Fc domain without any of the side effects. The downside of including the Fc domain is the need to use a more expensive mammalian cell production system to preserve proper glycosylation, which would decrease the turnaround time for getting the drug to patients in the outbreak scenario. Alternatively, one could just administer a single chain variable fragment (scFv) that binds to ACE2. A nanobody or VHH domains from camelids are another option as well 50, 51. These could be produced in bacteria, and its small size would allow for rapid permeation into different tissues. The downside is the shorter half-life of these molecules without the Fc domain."}
LitCovid-PD-CLO
{"project":"LitCovid-PD-CLO","denotations":[{"id":"T178","span":{"begin":0,"end":1},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T179","span":{"begin":358,"end":367},"obj":"http://purl.obolibrary.org/obo/CLO_0036932"},{"id":"T180","span":{"begin":397,"end":398},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T181","span":{"begin":577,"end":578},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T182","span":{"begin":730,"end":732},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T183","span":{"begin":877,"end":879},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T184","span":{"begin":950,"end":952},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T185","span":{"begin":979,"end":980},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T186","span":{"begin":1006,"end":1010},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T187","span":{"begin":1204,"end":1205},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T188","span":{"begin":1264,"end":1265},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T189","span":{"begin":1366,"end":1374},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_2"},{"id":"T190","span":{"begin":1521,"end":1523},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"}],"text":"A second, similar strategy would be to administer an antibody that would bind to ACE2 protein, thereby preventing 2019-nCoV infection ( Figure 1). This strategy was shown to effectively block SARS entry and replication in experiments 42. While no ACE2 antibody sequences are published in literature indexes, monoclonal antibodies do exist and the associated hybridoma sequences could be cloned in a matter of days. There would be no concern for any viral escape from an ACE2 binding antibody, which is an advantage over neutralizing approaches against the S protein. There are a couple of design considerations when thinking about how to employ the ACE2 antibody strategy. Any effector functions would need to be removed from the Fc domain 49, such that inflammation would not be caused in different tissues expressing ACE2. This would retain the long-half life endowed by the Fc domain without any of the side effects. The downside of including the Fc domain is the need to use a more expensive mammalian cell production system to preserve proper glycosylation, which would decrease the turnaround time for getting the drug to patients in the outbreak scenario. Alternatively, one could just administer a single chain variable fragment (scFv) that binds to ACE2. A nanobody or VHH domains from camelids are another option as well 50, 51. These could be produced in bacteria, and its small size would allow for rapid permeation into different tissues. The downside is the shorter half-life of these molecules without the Fc domain."}
LitCovid-PD-CHEBI
{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T78","span":{"begin":86,"end":93},"obj":"Chemical"},{"id":"T79","span":{"begin":558,"end":565},"obj":"Chemical"},{"id":"T80","span":{"begin":677,"end":685},"obj":"Chemical"},{"id":"T81","span":{"begin":1120,"end":1124},"obj":"Chemical"},{"id":"T82","span":{"begin":1499,"end":1508},"obj":"Chemical"}],"attributes":[{"id":"A78","pred":"chebi_id","subj":"T78","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A79","pred":"chebi_id","subj":"T79","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A80","pred":"chebi_id","subj":"T80","obj":"http://purl.obolibrary.org/obo/CHEBI_35224"},{"id":"A81","pred":"chebi_id","subj":"T81","obj":"http://purl.obolibrary.org/obo/CHEBI_23888"},{"id":"A82","pred":"chebi_id","subj":"T82","obj":"http://purl.obolibrary.org/obo/CHEBI_25367"}],"text":"A second, similar strategy would be to administer an antibody that would bind to ACE2 protein, thereby preventing 2019-nCoV infection ( Figure 1). This strategy was shown to effectively block SARS entry and replication in experiments 42. While no ACE2 antibody sequences are published in literature indexes, monoclonal antibodies do exist and the associated hybridoma sequences could be cloned in a matter of days. There would be no concern for any viral escape from an ACE2 binding antibody, which is an advantage over neutralizing approaches against the S protein. There are a couple of design considerations when thinking about how to employ the ACE2 antibody strategy. Any effector functions would need to be removed from the Fc domain 49, such that inflammation would not be caused in different tissues expressing ACE2. This would retain the long-half life endowed by the Fc domain without any of the side effects. The downside of including the Fc domain is the need to use a more expensive mammalian cell production system to preserve proper glycosylation, which would decrease the turnaround time for getting the drug to patients in the outbreak scenario. Alternatively, one could just administer a single chain variable fragment (scFv) that binds to ACE2. A nanobody or VHH domains from camelids are another option as well 50, 51. These could be produced in bacteria, and its small size would allow for rapid permeation into different tissues. The downside is the shorter half-life of these molecules without the Fc domain."}
LitCovid-PD-GO-BP
{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T12","span":{"begin":754,"end":766},"obj":"http://purl.obolibrary.org/obo/GO_0006954"},{"id":"T13","span":{"begin":1048,"end":1061},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"A second, similar strategy would be to administer an antibody that would bind to ACE2 protein, thereby preventing 2019-nCoV infection ( Figure 1). This strategy was shown to effectively block SARS entry and replication in experiments 42. While no ACE2 antibody sequences are published in literature indexes, monoclonal antibodies do exist and the associated hybridoma sequences could be cloned in a matter of days. There would be no concern for any viral escape from an ACE2 binding antibody, which is an advantage over neutralizing approaches against the S protein. There are a couple of design considerations when thinking about how to employ the ACE2 antibody strategy. Any effector functions would need to be removed from the Fc domain 49, such that inflammation would not be caused in different tissues expressing ACE2. This would retain the long-half life endowed by the Fc domain without any of the side effects. The downside of including the Fc domain is the need to use a more expensive mammalian cell production system to preserve proper glycosylation, which would decrease the turnaround time for getting the drug to patients in the outbreak scenario. Alternatively, one could just administer a single chain variable fragment (scFv) that binds to ACE2. A nanobody or VHH domains from camelids are another option as well 50, 51. These could be produced in bacteria, and its small size would allow for rapid permeation into different tissues. The downside is the shorter half-life of these molecules without the Fc domain."}
LitCovid-sentences
{"project":"LitCovid-sentences","denotations":[{"id":"T131","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"T132","span":{"begin":147,"end":237},"obj":"Sentence"},{"id":"T133","span":{"begin":238,"end":414},"obj":"Sentence"},{"id":"T134","span":{"begin":415,"end":566},"obj":"Sentence"},{"id":"T135","span":{"begin":567,"end":672},"obj":"Sentence"},{"id":"T136","span":{"begin":673,"end":824},"obj":"Sentence"},{"id":"T137","span":{"begin":825,"end":919},"obj":"Sentence"},{"id":"T138","span":{"begin":920,"end":1162},"obj":"Sentence"},{"id":"T139","span":{"begin":1163,"end":1263},"obj":"Sentence"},{"id":"T140","span":{"begin":1264,"end":1338},"obj":"Sentence"},{"id":"T141","span":{"begin":1339,"end":1451},"obj":"Sentence"},{"id":"T142","span":{"begin":1452,"end":1531},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"A second, similar strategy would be to administer an antibody that would bind to ACE2 protein, thereby preventing 2019-nCoV infection ( Figure 1). This strategy was shown to effectively block SARS entry and replication in experiments 42. While no ACE2 antibody sequences are published in literature indexes, monoclonal antibodies do exist and the associated hybridoma sequences could be cloned in a matter of days. There would be no concern for any viral escape from an ACE2 binding antibody, which is an advantage over neutralizing approaches against the S protein. There are a couple of design considerations when thinking about how to employ the ACE2 antibody strategy. Any effector functions would need to be removed from the Fc domain 49, such that inflammation would not be caused in different tissues expressing ACE2. This would retain the long-half life endowed by the Fc domain without any of the side effects. The downside of including the Fc domain is the need to use a more expensive mammalian cell production system to preserve proper glycosylation, which would decrease the turnaround time for getting the drug to patients in the outbreak scenario. Alternatively, one could just administer a single chain variable fragment (scFv) that binds to ACE2. A nanobody or VHH domains from camelids are another option as well 50, 51. These could be produced in bacteria, and its small size would allow for rapid permeation into different tissues. The downside is the shorter half-life of these molecules without the Fc domain."}