PMC:7128678 / 19820-20600 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"539","span":{"begin":75,"end":80},"obj":"Gene"},{"id":"540","span":{"begin":266,"end":267},"obj":"Gene"},{"id":"541","span":{"begin":64,"end":74},"obj":"Species"},{"id":"542","span":{"begin":104,"end":107},"obj":"Chemical"},{"id":"543","span":{"begin":289,"end":300},"obj":"Chemical"},{"id":"544","span":{"begin":379,"end":382},"obj":"Chemical"},{"id":"545","span":{"begin":406,"end":418},"obj":"Chemical"},{"id":"546","span":{"begin":524,"end":536},"obj":"Chemical"},{"id":"547","span":{"begin":565,"end":576},"obj":"Chemical"},{"id":"548","span":{"begin":601,"end":611},"obj":"Chemical"},{"id":"549","span":{"begin":620,"end":623},"obj":"Chemical"}],"attributes":[{"id":"A539","pred":"tao:has_database_id","subj":"539","obj":"Gene:43740568"},{"id":"A540","pred":"tao:has_database_id","subj":"540","obj":"Gene:43740568"},{"id":"A541","pred":"tao:has_database_id","subj":"541","obj":"Tax:2697049"},{"id":"A542","pred":"tao:has_database_id","subj":"542","obj":"MESH:D005677"},{"id":"A543","pred":"tao:has_database_id","subj":"543","obj":"MESH:D005732"},{"id":"A544","pred":"tao:has_database_id","subj":"544","obj":"MESH:D005677"},{"id":"A545","pred":"tao:has_database_id","subj":"545","obj":"MESH:D005732"},{"id":"A546","pred":"tao:has_database_id","subj":"546","obj":"MESH:D005732"},{"id":"A547","pred":"tao:has_database_id","subj":"547","obj":"MESH:D002738"},{"id":"A548","pred":"tao:has_database_id","subj":"548","obj":"MESH:D002241"},{"id":"A549","pred":"tao:has_database_id","subj":"549","obj":"MESH:D005677"}],"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":"Fig. 7 Molecular complex between the N-terminal domain (NTD) of SARS-CoV-2 spike protein and a dimer of GM1. In (a), (c) and (d), the NTD is represented as in Fig. 4. In (b), the surface of the NTD is shown without any transparency. The amino acid residues Q-134 to S-162 belonging to the ganglioside-binding domain (GBD) are represented as green spheres. Compared with a single GM1 molecule, the dimer of gangliosides forms a larger attractive surface for the NTD. In the above view of (d), the anchorage of the NTD to the gangliosides is particularly obvious. As chloroquine also interacts with the saccharide part of GM1, its presence would clearly mask most of the landing surface available for the NTD, preventing attachment of the virus to the plasma membrane of host cells."}

{"project":"LitCovid-PMC-OGER-BB","denotations":[{"id":"T425","span":{"begin":7,"end":24},"obj":"GO:0043234"},{"id":"T426","span":{"begin":48,"end":54},"obj":"SO:0000417"},{"id":"T427","span":{"begin":64,"end":74},"obj":"SP_7"},{"id":"T428","span":{"begin":289,"end":300},"obj":"CHEBI:28892;CHEBI:28892"},{"id":"T429","span":{"begin":309,"end":315},"obj":"SO:0000417"},{"id":"T430","span":{"begin":383,"end":391},"obj":"CHEBI:36357;CHEBI:36357"},{"id":"T431","span":{"begin":406,"end":418},"obj":"CHEBI:5386;CHEBI:5386"},{"id":"T432","span":{"begin":524,"end":536},"obj":"CHEBI:5386;CHEBI:5386"},{"id":"T433","span":{"begin":565,"end":576},"obj":"CHEBI:3638;DG_10;CHEBI:3638"},{"id":"T434","span":{"begin":601,"end":611},"obj":"CHEBI:32111;CHEBI:32111"},{"id":"T435","span":{"begin":737,"end":742},"obj":"NCBITaxon:10239"},{"id":"T436","span":{"begin":750,"end":765},"obj":"GO:0005886"}],"text":"Fig. 7 Molecular complex between the N-terminal domain (NTD) of SARS-CoV-2 spike protein and a dimer of GM1. In (a), (c) and (d), the NTD is represented as in Fig. 4. In (b), the surface of the NTD is shown without any transparency. The amino acid residues Q-134 to S-162 belonging to the ganglioside-binding domain (GBD) are represented as green spheres. Compared with a single GM1 molecule, the dimer of gangliosides forms a larger attractive surface for the NTD. In the above view of (d), the anchorage of the NTD to the gangliosides is particularly obvious. As chloroquine also interacts with the saccharide part of GM1, its presence would clearly mask most of the landing surface available for the NTD, preventing attachment of the virus to the plasma membrane of host cells."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T114","span":{"begin":81,"end":88},"obj":"Body_part"},{"id":"T115","span":{"begin":237,"end":247},"obj":"Body_part"},{"id":"T116","span":{"begin":289,"end":300},"obj":"Body_part"},{"id":"T117","span":{"begin":406,"end":418},"obj":"Body_part"},{"id":"T118","span":{"begin":524,"end":536},"obj":"Body_part"},{"id":"T119","span":{"begin":750,"end":765},"obj":"Body_part"},{"id":"T120","span":{"begin":774,"end":779},"obj":"Body_part"}],"attributes":[{"id":"A114","pred":"fma_id","subj":"T114","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A115","pred":"fma_id","subj":"T115","obj":"http://purl.org/sig/ont/fma/fma82739"},{"id":"A116","pred":"fma_id","subj":"T116","obj":"http://purl.org/sig/ont/fma/fma82816"},{"id":"A117","pred":"fma_id","subj":"T117","obj":"http://purl.org/sig/ont/fma/fma82816"},{"id":"A118","pred":"fma_id","subj":"T118","obj":"http://purl.org/sig/ont/fma/fma82816"},{"id":"A119","pred":"fma_id","subj":"T119","obj":"http://purl.org/sig/ont/fma/fma63841"},{"id":"A120","pred":"fma_id","subj":"T120","obj":"http://purl.org/sig/ont/fma/fma68646"}],"text":"Fig. 7 Molecular complex between the N-terminal domain (NTD) of SARS-CoV-2 spike protein and a dimer of GM1. In (a), (c) and (d), the NTD is represented as in Fig. 4. In (b), the surface of the NTD is shown without any transparency. The amino acid residues Q-134 to S-162 belonging to the ganglioside-binding domain (GBD) are represented as green spheres. Compared with a single GM1 molecule, the dimer of gangliosides forms a larger attractive surface for the NTD. In the above view of (d), the anchorage of the NTD to the gangliosides is particularly obvious. As chloroquine also interacts with the saccharide part of GM1, its presence would clearly mask most of the landing surface available for the NTD, preventing attachment of the virus to the plasma membrane of host cells."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T74","span":{"begin":56,"end":59},"obj":"Disease"},{"id":"T76","span":{"begin":64,"end":72},"obj":"Disease"},{"id":"T77","span":{"begin":134,"end":137},"obj":"Disease"},{"id":"T79","span":{"begin":194,"end":197},"obj":"Disease"},{"id":"T81","span":{"begin":461,"end":464},"obj":"Disease"},{"id":"T83","span":{"begin":513,"end":516},"obj":"Disease"},{"id":"T85","span":{"begin":703,"end":706},"obj":"Disease"}],"attributes":[{"id":"A74","pred":"mondo_id","subj":"T74","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A75","pred":"mondo_id","subj":"T74","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"},{"id":"A76","pred":"mondo_id","subj":"T76","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A77","pred":"mondo_id","subj":"T77","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A78","pred":"mondo_id","subj":"T77","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"},{"id":"A79","pred":"mondo_id","subj":"T79","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A80","pred":"mondo_id","subj":"T79","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"},{"id":"A81","pred":"mondo_id","subj":"T81","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A82","pred":"mondo_id","subj":"T81","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"},{"id":"A83","pred":"mondo_id","subj":"T83","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A84","pred":"mondo_id","subj":"T83","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"},{"id":"A85","pred":"mondo_id","subj":"T85","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A86","pred":"mondo_id","subj":"T85","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"}],"text":"Fig. 7 Molecular complex between the N-terminal domain (NTD) of SARS-CoV-2 spike protein and a dimer of GM1. In (a), (c) and (d), the NTD is represented as in Fig. 4. In (b), the surface of the NTD is shown without any transparency. The amino acid residues Q-134 to S-162 belonging to the ganglioside-binding domain (GBD) are represented as green spheres. Compared with a single GM1 molecule, the dimer of gangliosides forms a larger attractive surface for the NTD. In the above view of (d), the anchorage of the NTD to the gangliosides is particularly obvious. As chloroquine also interacts with the saccharide part of GM1, its presence would clearly mask most of the landing surface available for the NTD, preventing attachment of the virus to the plasma membrane of host cells."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T146","span":{"begin":93,"end":94},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T147","span":{"begin":113,"end":114},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T148","span":{"begin":171,"end":172},"obj":"http://purl.obolibrary.org/obo/CLO_0001021"},{"id":"T149","span":{"begin":237,"end":256},"obj":"http://purl.obolibrary.org/obo/CHEBI_33708"},{"id":"T150","span":{"begin":237,"end":256},"obj":"http://purl.obolibrary.org/obo/PR_000036907"},{"id":"T151","span":{"begin":268,"end":271},"obj":"http://purl.obolibrary.org/obo/CLO_0001002"},{"id":"T152","span":{"begin":370,"end":371},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T153","span":{"begin":425,"end":426},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T154","span":{"begin":737,"end":742},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T155","span":{"begin":750,"end":756},"obj":"http://purl.obolibrary.org/obo/UBERON_0001969"},{"id":"T156","span":{"begin":757,"end":765},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T157","span":{"begin":774,"end":779},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Fig. 7 Molecular complex between the N-terminal domain (NTD) of SARS-CoV-2 spike protein and a dimer of GM1. In (a), (c) and (d), the NTD is represented as in Fig. 4. In (b), the surface of the NTD is shown without any transparency. The amino acid residues Q-134 to S-162 belonging to the ganglioside-binding domain (GBD) are represented as green spheres. Compared with a single GM1 molecule, the dimer of gangliosides forms a larger attractive surface for the NTD. In the above view of (d), the anchorage of the NTD to the gangliosides is particularly obvious. As chloroquine also interacts with the saccharide part of GM1, its presence would clearly mask most of the landing surface available for the NTD, preventing attachment of the virus to the plasma membrane of host cells."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T471","span":{"begin":81,"end":88},"obj":"Chemical"},{"id":"T472","span":{"begin":104,"end":107},"obj":"Chemical"},{"id":"T475","span":{"begin":237,"end":247},"obj":"Chemical"},{"id":"T476","span":{"begin":237,"end":242},"obj":"Chemical"},{"id":"T477","span":{"begin":243,"end":247},"obj":"Chemical"},{"id":"T478","span":{"begin":289,"end":300},"obj":"Chemical"},{"id":"T479","span":{"begin":379,"end":382},"obj":"Chemical"},{"id":"T482","span":{"begin":383,"end":391},"obj":"Chemical"},{"id":"T483","span":{"begin":406,"end":418},"obj":"Chemical"},{"id":"T484","span":{"begin":524,"end":536},"obj":"Chemical"},{"id":"T485","span":{"begin":565,"end":576},"obj":"Chemical"},{"id":"T486","span":{"begin":601,"end":611},"obj":"Chemical"},{"id":"T487","span":{"begin":620,"end":623},"obj":"Chemical"}],"attributes":[{"id":"A471","pred":"chebi_id","subj":"T471","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A472","pred":"chebi_id","subj":"T472","obj":"http://purl.obolibrary.org/obo/CHEBI_18216"},{"id":"A473","pred":"chebi_id","subj":"T472","obj":"http://purl.obolibrary.org/obo/CHEBI_61048"},{"id":"A474","pred":"chebi_id","subj":"T472","obj":"http://purl.obolibrary.org/obo/CHEBI_73110"},{"id":"A475","pred":"chebi_id","subj":"T475","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"},{"id":"A476","pred":"chebi_id","subj":"T476","obj":"http://purl.obolibrary.org/obo/CHEBI_46882"},{"id":"A477","pred":"chebi_id","subj":"T477","obj":"http://purl.obolibrary.org/obo/CHEBI_37527"},{"id":"A478","pred":"chebi_id","subj":"T478","obj":"http://purl.obolibrary.org/obo/CHEBI_28892"},{"id":"A479","pred":"chebi_id","subj":"T479","obj":"http://purl.obolibrary.org/obo/CHEBI_18216"},{"id":"A480","pred":"chebi_id","subj":"T479","obj":"http://purl.obolibrary.org/obo/CHEBI_61048"},{"id":"A481","pred":"chebi_id","subj":"T479","obj":"http://purl.obolibrary.org/obo/CHEBI_73110"},{"id":"A482","pred":"chebi_id","subj":"T482","obj":"http://purl.obolibrary.org/obo/CHEBI_25367"},{"id":"A483","pred":"chebi_id","subj":"T483","obj":"http://purl.obolibrary.org/obo/CHEBI_28892"},{"id":"A484","pred":"chebi_id","subj":"T484","obj":"http://purl.obolibrary.org/obo/CHEBI_28892"},{"id":"A485","pred":"chebi_id","subj":"T485","obj":"http://purl.obolibrary.org/obo/CHEBI_3638"},{"id":"A486","pred":"chebi_id","subj":"T486","obj":"http://purl.obolibrary.org/obo/CHEBI_16646"},{"id":"A487","pred":"chebi_id","subj":"T487","obj":"http://purl.obolibrary.org/obo/CHEBI_18216"},{"id":"A488","pred":"chebi_id","subj":"T487","obj":"http://purl.obolibrary.org/obo/CHEBI_61048"},{"id":"A489","pred":"chebi_id","subj":"T487","obj":"http://purl.obolibrary.org/obo/CHEBI_73110"}],"text":"Fig. 7 Molecular complex between the N-terminal domain (NTD) of SARS-CoV-2 spike protein and a dimer of GM1. In (a), (c) and (d), the NTD is represented as in Fig. 4. In (b), the surface of the NTD is shown without any transparency. The amino acid residues Q-134 to S-162 belonging to the ganglioside-binding domain (GBD) are represented as green spheres. Compared with a single GM1 molecule, the dimer of gangliosides forms a larger attractive surface for the NTD. In the above view of (d), the anchorage of the NTD to the gangliosides is particularly obvious. As chloroquine also interacts with the saccharide part of GM1, its presence would clearly mask most of the landing surface available for the NTD, preventing attachment of the virus to the plasma membrane of host cells."}

{"project":"LitCovid-PD-GlycoEpitope","denotations":[{"id":"T24","span":{"begin":104,"end":107},"obj":"GlycoEpitope"},{"id":"T25","span":{"begin":379,"end":382},"obj":"GlycoEpitope"},{"id":"T26","span":{"begin":620,"end":623},"obj":"GlycoEpitope"}],"attributes":[{"id":"A24","pred":"glyco_epitope_db_id","subj":"T24","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A25","pred":"glyco_epitope_db_id","subj":"T25","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A26","pred":"glyco_epitope_db_id","subj":"T26","obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"Fig. 7 Molecular complex between the N-terminal domain (NTD) of SARS-CoV-2 spike protein and a dimer of GM1. In (a), (c) and (d), the NTD is represented as in Fig. 4. In (b), the surface of the NTD is shown without any transparency. The amino acid residues Q-134 to S-162 belonging to the ganglioside-binding domain (GBD) are represented as green spheres. Compared with a single GM1 molecule, the dimer of gangliosides forms a larger attractive surface for the NTD. In the above view of (d), the anchorage of the NTD to the gangliosides is particularly obvious. As chloroquine also interacts with the saccharide part of GM1, its presence would clearly mask most of the landing surface available for the NTD, preventing attachment of the virus to the plasma membrane of host cells."}

{"project":"LitCovid-sentences","denotations":[{"id":"T168","span":{"begin":0,"end":108},"obj":"Sentence"},{"id":"T169","span":{"begin":109,"end":166},"obj":"Sentence"},{"id":"T170","span":{"begin":167,"end":232},"obj":"Sentence"},{"id":"T171","span":{"begin":233,"end":355},"obj":"Sentence"},{"id":"T172","span":{"begin":356,"end":465},"obj":"Sentence"},{"id":"T173","span":{"begin":466,"end":561},"obj":"Sentence"},{"id":"T174","span":{"begin":562,"end":780},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Fig. 7 Molecular complex between the N-terminal domain (NTD) of SARS-CoV-2 spike protein and a dimer of GM1. In (a), (c) and (d), the NTD is represented as in Fig. 4. In (b), the surface of the NTD is shown without any transparency. The amino acid residues Q-134 to S-162 belonging to the ganglioside-binding domain (GBD) are represented as green spheres. Compared with a single GM1 molecule, the dimer of gangliosides forms a larger attractive surface for the NTD. In the above view of (d), the anchorage of the NTD to the gangliosides is particularly obvious. As chloroquine also interacts with the saccharide part of GM1, its presence would clearly mask most of the landing surface available for the NTD, preventing attachment of the virus to the plasma membrane of host cells."}