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LitCovid-PubTator

LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T59","span":{"begin":103,"end":111},"obj":"Body_part"},{"id":"T60","span":{"begin":555,"end":562},"obj":"Body_part"},{"id":"T61","span":{"begin":974,"end":984},"obj":"Body_part"},{"id":"T62","span":{"begin":1126,"end":1133},"obj":"Body_part"},{"id":"T63","span":{"begin":1189,"end":1199},"obj":"Body_part"},{"id":"T64","span":{"begin":1215,"end":1222},"obj":"Body_part"},{"id":"T65","span":{"begin":1528,"end":1538},"obj":"Body_part"},{"id":"T66","span":{"begin":1578,"end":1588},"obj":"Body_part"}],"attributes":[{"id":"A59","pred":"fma_id","subj":"T59","obj":"http://purl.org/sig/ont/fma/fma67257"},{"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/fma82739"},{"id":"A62","pred":"fma_id","subj":"T62","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A63","pred":"fma_id","subj":"T63","obj":"http://purl.org/sig/ont/fma/fma82739"},{"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/fma82739"},{"id":"A66","pred":"fma_id","subj":"T66","obj":"http://purl.org/sig/ont/fma/fma82739"}],"text":"Most CoVs share a similar viral structure, similar infection pathway, and a similar structure of the S proteins [41], suggesting that similar research strategies should also be applicable for the 2019-nCoV. For example, the study of MERS-CoV vaccines was accelerated by virtue of strategies that had been established for SARS-CoV [42]. It has been reported that the 2019-nCoV is also genetically close to SARS-CoV [43,44]. Therefore, to predict whether vaccines developed for SARS-CoV will also be effective against 2019-nCoV infection, the full length S protein sequences from the 2019-nCoV, a SARS-CoV, and two genetically similar bat CoV strains were selected for alignment (Fig. 1 ). The results indicated more than 50% homology of the viruses. However, the most variable residues are located in S1, a critical vaccine target, implying that neutralizing antibodies that were so effective against SARS-CoV infection may fail to recognize the 2019-nCoV, and that multiple amino acid differences at the receptor binding motif may modify virus tropism, a possible reason for cross-species transmission.\nFig. 1 Comparison of S protein sequences of coronaviruses. Multiple alignment of full amino acid sequences of S protein from 2019-nCoV (GISAID accession no. EPI_ISL_402124), SARS-CoV (GenBank accession no. AY278489), bat-SL-CoVZC45 (GenBank accession no. MG772933.1), and bat-SL-CoVZXC21 (GenBank accession no. MG772934.1) was performed and displayed with clustalx1.83 and MEGA4 respectively. ‘‘-” represents the unconfirmed amino acid residues, “.” represents the identical amino acid residues. The functional domains were labeled based on the research on SARS-CoV [41]; light blue box was for RBD region; dark blue box for receptor binding motif (RBM); light purple box for HR1; and dark purple box for HR2, respectively. Double underlined regions in HR1 and HR2 are fusion cores, which are critical regions responsible for the formation of stable six-helical bundles between HR1 and HR2."}

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T31","span":{"begin":51,"end":60},"obj":"Disease"},{"id":"T32","span":{"begin":321,"end":329},"obj":"Disease"},{"id":"T33","span":{"begin":405,"end":413},"obj":"Disease"},{"id":"T34","span":{"begin":476,"end":484},"obj":"Disease"},{"id":"T35","span":{"begin":516,"end":535},"obj":"Disease"},{"id":"T36","span":{"begin":526,"end":535},"obj":"Disease"},{"id":"T37","span":{"begin":595,"end":603},"obj":"Disease"},{"id":"T38","span":{"begin":900,"end":918},"obj":"Disease"},{"id":"T39","span":{"begin":909,"end":918},"obj":"Disease"},{"id":"T40","span":{"begin":1277,"end":1285},"obj":"Disease"},{"id":"T41","span":{"begin":1660,"end":1668},"obj":"Disease"}],"attributes":[{"id":"A31","pred":"mondo_id","subj":"T31","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A32","pred":"mondo_id","subj":"T32","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A33","pred":"mondo_id","subj":"T33","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A34","pred":"mondo_id","subj":"T34","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A35","pred":"mondo_id","subj":"T35","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A36","pred":"mondo_id","subj":"T36","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A37","pred":"mondo_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A38","pred":"mondo_id","subj":"T38","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A39","pred":"mondo_id","subj":"T39","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A40","pred":"mondo_id","subj":"T40","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A41","pred":"mondo_id","subj":"T41","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Most CoVs share a similar viral structure, similar infection pathway, and a similar structure of the S proteins [41], suggesting that similar research strategies should also be applicable for the 2019-nCoV. For example, the study of MERS-CoV vaccines was accelerated by virtue of strategies that had been established for SARS-CoV [42]. It has been reported that the 2019-nCoV is also genetically close to SARS-CoV [43,44]. Therefore, to predict whether vaccines developed for SARS-CoV will also be effective against 2019-nCoV infection, the full length S protein sequences from the 2019-nCoV, a SARS-CoV, and two genetically similar bat CoV strains were selected for alignment (Fig. 1 ). The results indicated more than 50% homology of the viruses. However, the most variable residues are located in S1, a critical vaccine target, implying that neutralizing antibodies that were so effective against SARS-CoV infection may fail to recognize the 2019-nCoV, and that multiple amino acid differences at the receptor binding motif may modify virus tropism, a possible reason for cross-species transmission.\nFig. 1 Comparison of S protein sequences of coronaviruses. Multiple alignment of full amino acid sequences of S protein from 2019-nCoV (GISAID accession no. EPI_ISL_402124), SARS-CoV (GenBank accession no. AY278489), bat-SL-CoVZC45 (GenBank accession no. MG772933.1), and bat-SL-CoVZXC21 (GenBank accession no. MG772934.1) was performed and displayed with clustalx1.83 and MEGA4 respectively. ‘‘-” represents the unconfirmed amino acid residues, “.” represents the identical amino acid residues. The functional domains were labeled based on the research on SARS-CoV [41]; light blue box was for RBD region; dark blue box for receptor binding motif (RBM); light purple box for HR1; and dark purple box for HR2, respectively. Double underlined regions in HR1 and HR2 are fusion cores, which are critical regions responsible for the formation of stable six-helical bundles between HR1 and HR2."}

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T112","span":{"begin":16,"end":17},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T113","span":{"begin":74,"end":75},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T114","span":{"begin":113,"end":115},"obj":"http://purl.obolibrary.org/obo/CLO_0053794"},{"id":"T115","span":{"begin":339,"end":342},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T116","span":{"begin":593,"end":594},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T117","span":{"begin":633,"end":636},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9397"},{"id":"T118","span":{"begin":740,"end":747},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T119","span":{"begin":800,"end":802},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T120","span":{"begin":804,"end":805},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T121","span":{"begin":1038,"end":1043},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T122","span":{"begin":1053,"end":1054},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T123","span":{"begin":1320,"end":1323},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9397"},{"id":"T124","span":{"begin":1375,"end":1378},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9397"},{"id":"T125","span":{"begin":1528,"end":1547},"obj":"http://purl.obolibrary.org/obo/CHEBI_33708"},{"id":"T126","span":{"begin":1528,"end":1547},"obj":"http://purl.obolibrary.org/obo/PR_000036907"},{"id":"T127","span":{"begin":1578,"end":1597},"obj":"http://purl.obolibrary.org/obo/CHEBI_33708"},{"id":"T128","span":{"begin":1578,"end":1597},"obj":"http://purl.obolibrary.org/obo/PR_000036907"},{"id":"T129","span":{"begin":1627,"end":1634},"obj":"http://purl.obolibrary.org/obo/CLO_0007225"},{"id":"T130","span":{"begin":1670,"end":1672},"obj":"http://purl.obolibrary.org/obo/CLO_0053794"}],"text":"Most CoVs share a similar viral structure, similar infection pathway, and a similar structure of the S proteins [41], suggesting that similar research strategies should also be applicable for the 2019-nCoV. For example, the study of MERS-CoV vaccines was accelerated by virtue of strategies that had been established for SARS-CoV [42]. It has been reported that the 2019-nCoV is also genetically close to SARS-CoV [43,44]. Therefore, to predict whether vaccines developed for SARS-CoV will also be effective against 2019-nCoV infection, the full length S protein sequences from the 2019-nCoV, a SARS-CoV, and two genetically similar bat CoV strains were selected for alignment (Fig. 1 ). The results indicated more than 50% homology of the viruses. However, the most variable residues are located in S1, a critical vaccine target, implying that neutralizing antibodies that were so effective against SARS-CoV infection may fail to recognize the 2019-nCoV, and that multiple amino acid differences at the receptor binding motif may modify virus tropism, a possible reason for cross-species transmission.\nFig. 1 Comparison of S protein sequences of coronaviruses. Multiple alignment of full amino acid sequences of S protein from 2019-nCoV (GISAID accession no. EPI_ISL_402124), SARS-CoV (GenBank accession no. AY278489), bat-SL-CoVZC45 (GenBank accession no. MG772933.1), and bat-SL-CoVZXC21 (GenBank accession no. MG772934.1) was performed and displayed with clustalx1.83 and MEGA4 respectively. ‘‘-” represents the unconfirmed amino acid residues, “.” represents the identical amino acid residues. The functional domains were labeled based on the research on SARS-CoV [41]; light blue box was for RBD region; dark blue box for receptor binding motif (RBM); light purple box for HR1; and dark purple box for HR2, respectively. Double underlined regions in HR1 and HR2 are fusion cores, which are critical regions responsible for the formation of stable six-helical bundles between HR1 and HR2."}

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T36","span":{"begin":1044,"end":1051},"obj":"http://purl.obolibrary.org/obo/GO_0009606"},{"id":"T37","span":{"begin":1933,"end":1942},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"Most CoVs share a similar viral structure, similar infection pathway, and a similar structure of the S proteins [41], suggesting that similar research strategies should also be applicable for the 2019-nCoV. For example, the study of MERS-CoV vaccines was accelerated by virtue of strategies that had been established for SARS-CoV [42]. It has been reported that the 2019-nCoV is also genetically close to SARS-CoV [43,44]. Therefore, to predict whether vaccines developed for SARS-CoV will also be effective against 2019-nCoV infection, the full length S protein sequences from the 2019-nCoV, a SARS-CoV, and two genetically similar bat CoV strains were selected for alignment (Fig. 1 ). The results indicated more than 50% homology of the viruses. However, the most variable residues are located in S1, a critical vaccine target, implying that neutralizing antibodies that were so effective against SARS-CoV infection may fail to recognize the 2019-nCoV, and that multiple amino acid differences at the receptor binding motif may modify virus tropism, a possible reason for cross-species transmission.\nFig. 1 Comparison of S protein sequences of coronaviruses. Multiple alignment of full amino acid sequences of S protein from 2019-nCoV (GISAID accession no. EPI_ISL_402124), SARS-CoV (GenBank accession no. AY278489), bat-SL-CoVZC45 (GenBank accession no. MG772933.1), and bat-SL-CoVZXC21 (GenBank accession no. MG772934.1) was performed and displayed with clustalx1.83 and MEGA4 respectively. ‘‘-” represents the unconfirmed amino acid residues, “.” represents the identical amino acid residues. The functional domains were labeled based on the research on SARS-CoV [41]; light blue box was for RBD region; dark blue box for receptor binding motif (RBM); light purple box for HR1; and dark purple box for HR2, respectively. Double underlined regions in HR1 and HR2 are fusion cores, which are critical regions responsible for the formation of stable six-helical bundles between HR1 and HR2."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T61","span":{"begin":0,"end":206},"obj":"Sentence"},{"id":"T62","span":{"begin":207,"end":335},"obj":"Sentence"},{"id":"T63","span":{"begin":336,"end":422},"obj":"Sentence"},{"id":"T64","span":{"begin":423,"end":687},"obj":"Sentence"},{"id":"T65","span":{"begin":688,"end":748},"obj":"Sentence"},{"id":"T66","span":{"begin":749,"end":1102},"obj":"Sentence"},{"id":"T67","span":{"begin":1103,"end":1161},"obj":"Sentence"},{"id":"T68","span":{"begin":1162,"end":1259},"obj":"Sentence"},{"id":"T69","span":{"begin":1260,"end":1308},"obj":"Sentence"},{"id":"T70","span":{"begin":1309,"end":1357},"obj":"Sentence"},{"id":"T71","span":{"begin":1358,"end":1413},"obj":"Sentence"},{"id":"T72","span":{"begin":1414,"end":1598},"obj":"Sentence"},{"id":"T73","span":{"begin":1599,"end":1826},"obj":"Sentence"},{"id":"T74","span":{"begin":1827,"end":1993},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Most CoVs share a similar viral structure, similar infection pathway, and a similar structure of the S proteins [41], suggesting that similar research strategies should also be applicable for the 2019-nCoV. For example, the study of MERS-CoV vaccines was accelerated by virtue of strategies that had been established for SARS-CoV [42]. It has been reported that the 2019-nCoV is also genetically close to SARS-CoV [43,44]. Therefore, to predict whether vaccines developed for SARS-CoV will also be effective against 2019-nCoV infection, the full length S protein sequences from the 2019-nCoV, a SARS-CoV, and two genetically similar bat CoV strains were selected for alignment (Fig. 1 ). The results indicated more than 50% homology of the viruses. However, the most variable residues are located in S1, a critical vaccine target, implying that neutralizing antibodies that were so effective against SARS-CoV infection may fail to recognize the 2019-nCoV, and that multiple amino acid differences at the receptor binding motif may modify virus tropism, a possible reason for cross-species transmission.\nFig. 1 Comparison of S protein sequences of coronaviruses. Multiple alignment of full amino acid sequences of S protein from 2019-nCoV (GISAID accession no. EPI_ISL_402124), SARS-CoV (GenBank accession no. AY278489), bat-SL-CoVZC45 (GenBank accession no. MG772933.1), and bat-SL-CoVZXC21 (GenBank accession no. MG772934.1) was performed and displayed with clustalx1.83 and MEGA4 respectively. ‘‘-” represents the unconfirmed amino acid residues, “.” represents the identical amino acid residues. The functional domains were labeled based on the research on SARS-CoV [41]; light blue box was for RBD region; dark blue box for receptor binding motif (RBM); light purple box for HR1; and dark purple box for HR2, respectively. Double underlined regions in HR1 and HR2 are fusion cores, which are critical regions responsible for the formation of stable six-helical bundles between HR1 and HR2."}

2_test

{"project":"2_test","denotations":[{"id":"32017984-28393837-69697753","span":{"begin":113,"end":115},"obj":"28393837"},{"id":"32017984-28393837-69697754","span":{"begin":1670,"end":1672},"obj":"28393837"}],"text":"Most CoVs share a similar viral structure, similar infection pathway, and a similar structure of the S proteins [41], suggesting that similar research strategies should also be applicable for the 2019-nCoV. For example, the study of MERS-CoV vaccines was accelerated by virtue of strategies that had been established for SARS-CoV [42]. It has been reported that the 2019-nCoV is also genetically close to SARS-CoV [43,44]. Therefore, to predict whether vaccines developed for SARS-CoV will also be effective against 2019-nCoV infection, the full length S protein sequences from the 2019-nCoV, a SARS-CoV, and two genetically similar bat CoV strains were selected for alignment (Fig. 1 ). The results indicated more than 50% homology of the viruses. However, the most variable residues are located in S1, a critical vaccine target, implying that neutralizing antibodies that were so effective against SARS-CoV infection may fail to recognize the 2019-nCoV, and that multiple amino acid differences at the receptor binding motif may modify virus tropism, a possible reason for cross-species transmission.\nFig. 1 Comparison of S protein sequences of coronaviruses. Multiple alignment of full amino acid sequences of S protein from 2019-nCoV (GISAID accession no. EPI_ISL_402124), SARS-CoV (GenBank accession no. AY278489), bat-SL-CoVZC45 (GenBank accession no. MG772933.1), and bat-SL-CoVZXC21 (GenBank accession no. MG772934.1) was performed and displayed with clustalx1.83 and MEGA4 respectively. ‘‘-” represents the unconfirmed amino acid residues, “.” represents the identical amino acid residues. The functional domains were labeled based on the research on SARS-CoV [41]; light blue box was for RBD region; dark blue box for receptor binding motif (RBM); light purple box for HR1; and dark purple box for HR2, respectively. Double underlined regions in HR1 and HR2 are fusion cores, which are critical regions responsible for the formation of stable six-helical bundles between HR1 and HR2."}

PMC:7102556 / 9880-11873 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:7102556 / 9880-11873 JSON TXT