PMC:7094172 / 13814-15212 JSONTXT

{"project":"LitCovid-PMC-OGER-BB","denotations":[{"id":"T715","span":{"begin":51,"end":59},"obj":"SP_9"},{"id":"T714","span":{"begin":60,"end":69},"obj":"PG_4"},{"id":"T713","span":{"begin":110,"end":118},"obj":"SP_9"},{"id":"T712","span":{"begin":119,"end":128},"obj":"PG_4"},{"id":"T711","span":{"begin":284,"end":293},"obj":"PG_4"},{"id":"T710","span":{"begin":307,"end":314},"obj":"GO:0032991"},{"id":"T709","span":{"begin":399,"end":408},"obj":"PG_4"},{"id":"T708","span":{"begin":426,"end":433},"obj":"GO:0032991"},{"id":"T707","span":{"begin":526,"end":535},"obj":"PG_4"},{"id":"T706","span":{"begin":553,"end":560},"obj":"GO:0032991"},{"id":"T705","span":{"begin":774,"end":782},"obj":"SP_9"},{"id":"T704","span":{"begin":783,"end":792},"obj":"PG_4"},{"id":"T703","span":{"begin":866,"end":870},"obj":"CHEBI:9754;CHEBI:9754"},{"id":"T702","span":{"begin":871,"end":874},"obj":"CHEBI:17883;CHEBI:17883"},{"id":"T701","span":{"begin":883,"end":887},"obj":"CHEBI:26710;CHEBI:26710"},{"id":"T700","span":{"begin":1048,"end":1060},"obj":"GO:0046983"},{"id":"T699","span":{"begin":1092,"end":1104},"obj":"GO:0046983"},{"id":"T698","span":{"begin":1207,"end":1216},"obj":"PG_4"},{"id":"T697","span":{"begin":1320,"end":1327},"obj":"SO:0000409"},{"id":"T696","span":{"begin":1380,"end":1397},"obj":"GO:0005840"}],"text":"P3-induced abnormal aggregation on the full-length MERS-CoV N protein. (A–E) SAXS analysis of the full-length MERS-CoV N protein. (A) Normalized results from GNOM showing pairwise distance distribution P(r) and maximum distance. The radius of gyration fitted to 207 and 230 Å for the N protein and the N-P3 complex, respectively. “r” represents pairwise distances. (B, C) Scattering profiles of the N protein (B) and the N-P3 complex (C) and normalization fitting with GNOM (dashed lines). (D, E) Representative models of the N protein (D) and the N-P3 complex (E) generated by CRYSOL simulations of the SAXS data. Only α carbons are shown. NTD (yellow), CTD (green), and disorder region (cyan). (F, G) Conformation (F) and stability (G) analyses based on FL spectra of the MERS-CoV N protein (1 μM) incubated with P3 (10 μM) for 1 h in a buffer consisting of 50 mM Tris-HCl, 150 mM NaCl (pH 8.3). (H) Schematic of the P3 inhibition mechanism. Left panel: in the absence of RNA, N proteins organize as a dimeric building block contributed by N-CTD dimerization. Middle panel: P3 promoted the dimerization of N-NTDs from different building blocks, by which the distance between CTD cuboids was shortened and N protein aggregation occurred. Right panel: octameric conformation of building blocks buried in the RNA-binding surface of N-CTDs. It hindered the formation of filamentous ribonucleocapsids."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T60","span":{"begin":62,"end":69},"obj":"Body_part"},{"id":"T61","span":{"begin":121,"end":128},"obj":"Body_part"},{"id":"T62","span":{"begin":233,"end":239},"obj":"Body_part"},{"id":"T63","span":{"begin":286,"end":293},"obj":"Body_part"},{"id":"T64","span":{"begin":401,"end":408},"obj":"Body_part"},{"id":"T65","span":{"begin":528,"end":535},"obj":"Body_part"},{"id":"T66","span":{"begin":785,"end":792},"obj":"Body_part"},{"id":"T67","span":{"begin":974,"end":977},"obj":"Body_part"},{"id":"T68","span":{"begin":981,"end":989},"obj":"Body_part"},{"id":"T69","span":{"begin":1181,"end":1188},"obj":"Body_part"},{"id":"T70","span":{"begin":1209,"end":1216},"obj":"Body_part"},{"id":"T71","span":{"begin":1308,"end":1311},"obj":"Body_part"}],"attributes":[{"id":"A60","pred":"fma_id","subj":"T60","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A61","pred":"fma_id","subj":"T61","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A62","pred":"fma_id","subj":"T62","obj":"http://purl.org/sig/ont/fma/fma23463"},{"id":"A63","pred":"fma_id","subj":"T63","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A64","pred":"fma_id","subj":"T64","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A65","pred":"fma_id","subj":"T65","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A66","pred":"fma_id","subj":"T66","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A67","pred":"fma_id","subj":"T67","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A68","pred":"fma_id","subj":"T68","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A69","pred":"fma_id","subj":"T69","obj":"http://purl.org/sig/ont/fma/fma24527"},{"id":"A70","pred":"fma_id","subj":"T70","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A71","pred":"fma_id","subj":"T71","obj":"http://purl.org/sig/ont/fma/fma67095"}],"text":"P3-induced abnormal aggregation on the full-length MERS-CoV N protein. (A–E) SAXS analysis of the full-length MERS-CoV N protein. (A) Normalized results from GNOM showing pairwise distance distribution P(r) and maximum distance. The radius of gyration fitted to 207 and 230 Å for the N protein and the N-P3 complex, respectively. “r” represents pairwise distances. (B, C) Scattering profiles of the N protein (B) and the N-P3 complex (C) and normalization fitting with GNOM (dashed lines). (D, E) Representative models of the N protein (D) and the N-P3 complex (E) generated by CRYSOL simulations of the SAXS data. Only α carbons are shown. NTD (yellow), CTD (green), and disorder region (cyan). (F, G) Conformation (F) and stability (G) analyses based on FL spectra of the MERS-CoV N protein (1 μM) incubated with P3 (10 μM) for 1 h in a buffer consisting of 50 mM Tris-HCl, 150 mM NaCl (pH 8.3). (H) Schematic of the P3 inhibition mechanism. Left panel: in the absence of RNA, N proteins organize as a dimeric building block contributed by N-CTD dimerization. Middle panel: P3 promoted the dimerization of N-NTDs from different building blocks, by which the distance between CTD cuboids was shortened and N protein aggregation occurred. Right panel: octameric conformation of building blocks buried in the RNA-binding surface of N-CTDs. It hindered the formation of filamentous ribonucleocapsids."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T57","span":{"begin":641,"end":644},"obj":"Disease"}],"attributes":[{"id":"A57","pred":"mondo_id","subj":"T57","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A58","pred":"mondo_id","subj":"T57","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"}],"text":"P3-induced abnormal aggregation on the full-length MERS-CoV N protein. (A–E) SAXS analysis of the full-length MERS-CoV N protein. (A) Normalized results from GNOM showing pairwise distance distribution P(r) and maximum distance. The radius of gyration fitted to 207 and 230 Å for the N protein and the N-P3 complex, respectively. “r” represents pairwise distances. (B, C) Scattering profiles of the N protein (B) and the N-P3 complex (C) and normalization fitting with GNOM (dashed lines). (D, E) Representative models of the N protein (D) and the N-P3 complex (E) generated by CRYSOL simulations of the SAXS data. Only α carbons are shown. NTD (yellow), CTD (green), and disorder region (cyan). (F, G) Conformation (F) and stability (G) analyses based on FL spectra of the MERS-CoV N protein (1 μM) incubated with P3 (10 μM) for 1 h in a buffer consisting of 50 mM Tris-HCl, 150 mM NaCl (pH 8.3). (H) Schematic of the P3 inhibition mechanism. Left panel: in the absence of RNA, N proteins organize as a dimeric building block contributed by N-CTD dimerization. Middle panel: P3 promoted the dimerization of N-NTDs from different building blocks, by which the distance between CTD cuboids was shortened and N protein aggregation occurred. Right panel: octameric conformation of building blocks buried in the RNA-binding surface of N-CTDs. It hindered the formation of filamentous ribonucleocapsids."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T96","span":{"begin":72,"end":75},"obj":"http://purl.obolibrary.org/obo/CLO_0051456"},{"id":"T97","span":{"begin":131,"end":132},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T98","span":{"begin":274,"end":275},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T99","span":{"begin":366,"end":367},"obj":"http://purl.obolibrary.org/obo/CLO_0001021"},{"id":"T100","span":{"begin":410,"end":411},"obj":"http://purl.obolibrary.org/obo/CLO_0001021"},{"id":"T101","span":{"begin":756,"end":758},"obj":"http://purl.obolibrary.org/obo/CLO_0003358"},{"id":"T102","span":{"begin":837,"end":838},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T103","span":{"begin":990,"end":998},"obj":"http://purl.obolibrary.org/obo/OBI_0000245"},{"id":"T104","span":{"begin":990,"end":998},"obj":"http://purl.obolibrary.org/obo/OBI_0100026"},{"id":"T105","span":{"begin":990,"end":998},"obj":"http://purl.obolibrary.org/obo/UBERON_0000468"},{"id":"T106","span":{"begin":1002,"end":1003},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"P3-induced abnormal aggregation on the full-length MERS-CoV N protein. (A–E) SAXS analysis of the full-length MERS-CoV N protein. (A) Normalized results from GNOM showing pairwise distance distribution P(r) and maximum distance. The radius of gyration fitted to 207 and 230 Å for the N protein and the N-P3 complex, respectively. “r” represents pairwise distances. (B, C) Scattering profiles of the N protein (B) and the N-P3 complex (C) and normalization fitting with GNOM (dashed lines). (D, E) Representative models of the N protein (D) and the N-P3 complex (E) generated by CRYSOL simulations of the SAXS data. Only α carbons are shown. NTD (yellow), CTD (green), and disorder region (cyan). (F, G) Conformation (F) and stability (G) analyses based on FL spectra of the MERS-CoV N protein (1 μM) incubated with P3 (10 μM) for 1 h in a buffer consisting of 50 mM Tris-HCl, 150 mM NaCl (pH 8.3). (H) Schematic of the P3 inhibition mechanism. Left panel: in the absence of RNA, N proteins organize as a dimeric building block contributed by N-CTD dimerization. Middle panel: P3 promoted the dimerization of N-NTDs from different building blocks, by which the distance between CTD cuboids was shortened and N protein aggregation occurred. Right panel: octameric conformation of building blocks buried in the RNA-binding surface of N-CTDs. It hindered the formation of filamentous ribonucleocapsids."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T118","span":{"begin":62,"end":69},"obj":"Chemical"},{"id":"T119","span":{"begin":121,"end":128},"obj":"Chemical"},{"id":"T120","span":{"begin":286,"end":293},"obj":"Chemical"},{"id":"T121","span":{"begin":401,"end":408},"obj":"Chemical"},{"id":"T122","span":{"begin":528,"end":535},"obj":"Chemical"},{"id":"T123","span":{"begin":756,"end":758},"obj":"Chemical"},{"id":"T124","span":{"begin":785,"end":792},"obj":"Chemical"},{"id":"T125","span":{"begin":839,"end":845},"obj":"Chemical"},{"id":"T126","span":{"begin":866,"end":870},"obj":"Chemical"},{"id":"T127","span":{"begin":871,"end":874},"obj":"Chemical"},{"id":"T128","span":{"begin":883,"end":887},"obj":"Chemical"},{"id":"T129","span":{"begin":981,"end":989},"obj":"Chemical"},{"id":"T130","span":{"begin":1209,"end":1216},"obj":"Chemical"}],"attributes":[{"id":"A118","pred":"chebi_id","subj":"T118","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A119","pred":"chebi_id","subj":"T119","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A120","pred":"chebi_id","subj":"T120","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A121","pred":"chebi_id","subj":"T121","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A122","pred":"chebi_id","subj":"T122","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A123","pred":"chebi_id","subj":"T123","obj":"http://purl.obolibrary.org/obo/CHEBI_91150"},{"id":"A124","pred":"chebi_id","subj":"T124","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A125","pred":"chebi_id","subj":"T125","obj":"http://purl.obolibrary.org/obo/CHEBI_35225"},{"id":"A126","pred":"chebi_id","subj":"T126","obj":"http://purl.obolibrary.org/obo/CHEBI_9754"},{"id":"A127","pred":"chebi_id","subj":"T127","obj":"http://purl.obolibrary.org/obo/CHEBI_17883"},{"id":"A128","pred":"chebi_id","subj":"T128","obj":"http://purl.obolibrary.org/obo/CHEBI_26710"},{"id":"A129","pred":"chebi_id","subj":"T129","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A130","pred":"chebi_id","subj":"T130","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"P3-induced abnormal aggregation on the full-length MERS-CoV N protein. (A–E) SAXS analysis of the full-length MERS-CoV N protein. (A) Normalized results from GNOM showing pairwise distance distribution P(r) and maximum distance. The radius of gyration fitted to 207 and 230 Å for the N protein and the N-P3 complex, respectively. “r” represents pairwise distances. (B, C) Scattering profiles of the N protein (B) and the N-P3 complex (C) and normalization fitting with GNOM (dashed lines). (D, E) Representative models of the N protein (D) and the N-P3 complex (E) generated by CRYSOL simulations of the SAXS data. Only α carbons are shown. NTD (yellow), CTD (green), and disorder region (cyan). (F, G) Conformation (F) and stability (G) analyses based on FL spectra of the MERS-CoV N protein (1 μM) incubated with P3 (10 μM) for 1 h in a buffer consisting of 50 mM Tris-HCl, 150 mM NaCl (pH 8.3). (H) Schematic of the P3 inhibition mechanism. Left panel: in the absence of RNA, N proteins organize as a dimeric building block contributed by N-CTD dimerization. Middle panel: P3 promoted the dimerization of N-NTDs from different building blocks, by which the distance between CTD cuboids was shortened and N protein aggregation occurred. Right panel: octameric conformation of building blocks buried in the RNA-binding surface of N-CTDs. It hindered the formation of filamentous ribonucleocapsids."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T13","span":{"begin":1355,"end":1364},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"P3-induced abnormal aggregation on the full-length MERS-CoV N protein. (A–E) SAXS analysis of the full-length MERS-CoV N protein. (A) Normalized results from GNOM showing pairwise distance distribution P(r) and maximum distance. The radius of gyration fitted to 207 and 230 Å for the N protein and the N-P3 complex, respectively. “r” represents pairwise distances. (B, C) Scattering profiles of the N protein (B) and the N-P3 complex (C) and normalization fitting with GNOM (dashed lines). (D, E) Representative models of the N protein (D) and the N-P3 complex (E) generated by CRYSOL simulations of the SAXS data. Only α carbons are shown. NTD (yellow), CTD (green), and disorder region (cyan). (F, G) Conformation (F) and stability (G) analyses based on FL spectra of the MERS-CoV N protein (1 μM) incubated with P3 (10 μM) for 1 h in a buffer consisting of 50 mM Tris-HCl, 150 mM NaCl (pH 8.3). (H) Schematic of the P3 inhibition mechanism. Left panel: in the absence of RNA, N proteins organize as a dimeric building block contributed by N-CTD dimerization. Middle panel: P3 promoted the dimerization of N-NTDs from different building blocks, by which the distance between CTD cuboids was shortened and N protein aggregation occurred. Right panel: octameric conformation of building blocks buried in the RNA-binding surface of N-CTDs. It hindered the formation of filamentous ribonucleocapsids."}

{"project":"LitCovid-sentences","denotations":[{"id":"T113","span":{"begin":229,"end":614},"obj":"Sentence"},{"id":"T114","span":{"begin":615,"end":640},"obj":"Sentence"},{"id":"T115","span":{"begin":641,"end":943},"obj":"Sentence"},{"id":"T116","span":{"begin":944,"end":1061},"obj":"Sentence"},{"id":"T117","span":{"begin":1062,"end":1238},"obj":"Sentence"},{"id":"T118","span":{"begin":1239,"end":1338},"obj":"Sentence"},{"id":"T119","span":{"begin":1339,"end":1398},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"P3-induced abnormal aggregation on the full-length MERS-CoV N protein. (A–E) SAXS analysis of the full-length MERS-CoV N protein. (A) Normalized results from GNOM showing pairwise distance distribution P(r) and maximum distance. The radius of gyration fitted to 207 and 230 Å for the N protein and the N-P3 complex, respectively. “r” represents pairwise distances. (B, C) Scattering profiles of the N protein (B) and the N-P3 complex (C) and normalization fitting with GNOM (dashed lines). (D, E) Representative models of the N protein (D) and the N-P3 complex (E) generated by CRYSOL simulations of the SAXS data. Only α carbons are shown. NTD (yellow), CTD (green), and disorder region (cyan). (F, G) Conformation (F) and stability (G) analyses based on FL spectra of the MERS-CoV N protein (1 μM) incubated with P3 (10 μM) for 1 h in a buffer consisting of 50 mM Tris-HCl, 150 mM NaCl (pH 8.3). (H) Schematic of the P3 inhibition mechanism. Left panel: in the absence of RNA, N proteins organize as a dimeric building block contributed by N-CTD dimerization. Middle panel: P3 promoted the dimerization of N-NTDs from different building blocks, by which the distance between CTD cuboids was shortened and N protein aggregation occurred. Right panel: octameric conformation of building blocks buried in the RNA-binding surface of N-CTDs. It hindered the formation of filamentous ribonucleocapsids."}

{"project":"LitCovid-PubTator","denotations":[{"id":"233","span":{"begin":51,"end":59},"obj":"Species"},{"id":"234","span":{"begin":110,"end":118},"obj":"Species"},{"id":"235","span":{"begin":774,"end":782},"obj":"Species"},{"id":"236","span":{"begin":0,"end":2},"obj":"Chemical"},{"id":"237","span":{"begin":302,"end":306},"obj":"Chemical"},{"id":"238","span":{"begin":421,"end":425},"obj":"Chemical"},{"id":"239","span":{"begin":548,"end":552},"obj":"Chemical"},{"id":"240","span":{"begin":622,"end":629},"obj":"Chemical"},{"id":"241","span":{"begin":815,"end":817},"obj":"Chemical"},{"id":"242","span":{"begin":866,"end":874},"obj":"Chemical"},{"id":"243","span":{"begin":883,"end":887},"obj":"Chemical"},{"id":"244","span":{"begin":1076,"end":1078},"obj":"Chemical"},{"id":"245","span":{"begin":1108,"end":1114},"obj":"Chemical"},{"id":"246","span":{"begin":1331,"end":1337},"obj":"Chemical"},{"id":"247","span":{"begin":11,"end":31},"obj":"Disease"}],"attributes":[{"id":"A233","pred":"tao:has_database_id","subj":"233","obj":"Tax:1335626"},{"id":"A234","pred":"tao:has_database_id","subj":"234","obj":"Tax:1335626"},{"id":"A235","pred":"tao:has_database_id","subj":"235","obj":"Tax:1335626"},{"id":"A240","pred":"tao:has_database_id","subj":"240","obj":"MESH:D002244"},{"id":"A243","pred":"tao:has_database_id","subj":"243","obj":"MESH:D012965"},{"id":"A247","pred":"tao:has_database_id","subj":"247","obj":"MESH:D001791"}],"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":"P3-induced abnormal aggregation on the full-length MERS-CoV N protein. (A–E) SAXS analysis of the full-length MERS-CoV N protein. (A) Normalized results from GNOM showing pairwise distance distribution P(r) and maximum distance. The radius of gyration fitted to 207 and 230 Å for the N protein and the N-P3 complex, respectively. “r” represents pairwise distances. (B, C) Scattering profiles of the N protein (B) and the N-P3 complex (C) and normalization fitting with GNOM (dashed lines). (D, E) Representative models of the N protein (D) and the N-P3 complex (E) generated by CRYSOL simulations of the SAXS data. Only α carbons are shown. NTD (yellow), CTD (green), and disorder region (cyan). (F, G) Conformation (F) and stability (G) analyses based on FL spectra of the MERS-CoV N protein (1 μM) incubated with P3 (10 μM) for 1 h in a buffer consisting of 50 mM Tris-HCl, 150 mM NaCl (pH 8.3). (H) Schematic of the P3 inhibition mechanism. Left panel: in the absence of RNA, N proteins organize as a dimeric building block contributed by N-CTD dimerization. Middle panel: P3 promoted the dimerization of N-NTDs from different building blocks, by which the distance between CTD cuboids was shortened and N protein aggregation occurred. Right panel: octameric conformation of building blocks buried in the RNA-binding surface of N-CTDs. It hindered the formation of filamentous ribonucleocapsids."}