PMC:7253482 / 20507-21362 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"704","span":{"begin":213,"end":216},"obj":"Gene"},{"id":"705","span":{"begin":221,"end":232},"obj":"Species"},{"id":"706","span":{"begin":362,"end":373},"obj":"Species"},{"id":"707","span":{"begin":778,"end":791},"obj":"Species"},{"id":"708","span":{"begin":507,"end":510},"obj":"Gene"},{"id":"709","span":{"begin":147,"end":153},"obj":"Chemical"},{"id":"710","span":{"begin":259,"end":265},"obj":"Chemical"},{"id":"711","span":{"begin":402,"end":408},"obj":"Chemical"},{"id":"712","span":{"begin":586,"end":593},"obj":"Chemical"},{"id":"713","span":{"begin":811,"end":817},"obj":"Chemical"}],"attributes":[{"id":"A704","pred":"tao:has_database_id","subj":"704","obj":"Gene:2995"},{"id":"A705","pred":"tao:has_database_id","subj":"705","obj":"Tax:11118"},{"id":"A706","pred":"tao:has_database_id","subj":"706","obj":"Tax:11118"},{"id":"A707","pred":"tao:has_database_id","subj":"707","obj":"Tax:11118"},{"id":"A708","pred":"tao:has_database_id","subj":"708","obj":"Gene:2995"},{"id":"A709","pred":"tao:has_database_id","subj":"709","obj":"MESH:D011134"},{"id":"A710","pred":"tao:has_database_id","subj":"710","obj":"MESH:D011134"},{"id":"A711","pred":"tao:has_database_id","subj":"711","obj":"MESH:D011134"},{"id":"A712","pred":"tao:has_database_id","subj":"712","obj":"MESH:D011134"},{"id":"A713","pred":"tao:has_database_id","subj":"713","obj":"MESH:D011134"}],"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":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T116","span":{"begin":15,"end":23},"obj":"Body_part"},{"id":"T117","span":{"begin":235,"end":243},"obj":"Body_part"},{"id":"T118","span":{"begin":327,"end":334},"obj":"Body_part"},{"id":"T119","span":{"begin":376,"end":384},"obj":"Body_part"},{"id":"T120","span":{"begin":559,"end":566},"obj":"Body_part"},{"id":"T121","span":{"begin":706,"end":719},"obj":"Body_part"}],"attributes":[{"id":"A116","pred":"fma_id","subj":"T116","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A117","pred":"fma_id","subj":"T117","obj":"http://purl.org/sig/ont/fma/fma67257"},{"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/fma67257"},{"id":"A120","pred":"fma_id","subj":"T120","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A121","pred":"fma_id","subj":"T121","obj":"http://purl.org/sig/ont/fma/fma62925"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T118","span":{"begin":527,"end":528},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T119","span":{"begin":651,"end":652},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T120","span":{"begin":834,"end":835},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T208","span":{"begin":15,"end":23},"obj":"Chemical"},{"id":"T209","span":{"begin":235,"end":243},"obj":"Chemical"},{"id":"T210","span":{"begin":327,"end":334},"obj":"Chemical"},{"id":"T211","span":{"begin":376,"end":384},"obj":"Chemical"},{"id":"T212","span":{"begin":559,"end":566},"obj":"Chemical"},{"id":"T213","span":{"begin":586,"end":593},"obj":"Chemical"},{"id":"T214","span":{"begin":706,"end":719},"obj":"Chemical"}],"attributes":[{"id":"A208","pred":"chebi_id","subj":"T208","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A209","pred":"chebi_id","subj":"T209","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A210","pred":"chebi_id","subj":"T210","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A211","pred":"chebi_id","subj":"T211","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A212","pred":"chebi_id","subj":"T212","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A213","pred":"chebi_id","subj":"T213","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A214","pred":"chebi_id","subj":"T214","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

{"project":"LitCovid-sample-MedDRA","denotations":[{"id":"T7","span":{"begin":279,"end":285},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"}],"attributes":[{"id":"A7","pred":"meddra_id","subj":"T7","obj":"http://purl.bioontology.org/ontology/MEDDRA/10047890"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T55","span":{"begin":671,"end":686},"obj":"http://purl.obolibrary.org/obo/GO_0006955"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

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{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T115","span":{"begin":15,"end":23},"obj":"Body_part"},{"id":"T116","span":{"begin":235,"end":243},"obj":"Body_part"},{"id":"T117","span":{"begin":327,"end":334},"obj":"Body_part"},{"id":"T118","span":{"begin":376,"end":384},"obj":"Body_part"},{"id":"T119","span":{"begin":559,"end":566},"obj":"Body_part"},{"id":"T120","span":{"begin":706,"end":719},"obj":"Body_part"}],"attributes":[{"id":"A115","pred":"fma_id","subj":"T115","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A116","pred":"fma_id","subj":"T116","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A117","pred":"fma_id","subj":"T117","obj":"http://purl.org/sig/ont/fma/fma67257"},{"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/fma67257"},{"id":"A120","pred":"fma_id","subj":"T120","obj":"http://purl.org/sig/ont/fma/fma62925"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T142","span":{"begin":15,"end":23},"obj":"Chemical"},{"id":"T143","span":{"begin":235,"end":243},"obj":"Chemical"},{"id":"T144","span":{"begin":327,"end":334},"obj":"Chemical"},{"id":"T145","span":{"begin":376,"end":384},"obj":"Chemical"},{"id":"T146","span":{"begin":559,"end":566},"obj":"Chemical"},{"id":"T147","span":{"begin":586,"end":593},"obj":"Chemical"},{"id":"T148","span":{"begin":706,"end":719},"obj":"Chemical"}],"attributes":[{"id":"A142","pred":"chebi_id","subj":"T142","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A143","pred":"chebi_id","subj":"T143","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A144","pred":"chebi_id","subj":"T144","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A145","pred":"chebi_id","subj":"T145","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A146","pred":"chebi_id","subj":"T146","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A147","pred":"chebi_id","subj":"T147","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A148","pred":"chebi_id","subj":"T148","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T150","span":{"begin":208,"end":212},"obj":"Species"},{"id":"T151","span":{"begin":502,"end":506},"obj":"Species"}],"attributes":[{"id":"A150","pred":"ncbi_taxonomy_id","subj":"T150","obj":"NCBItxid:11620"},{"id":"A151","pred":"ncbi_taxonomy_id","subj":"T151","obj":"NCBItxid:11620"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T120","span":{"begin":0,"end":189},"obj":"Sentence"},{"id":"T121","span":{"begin":190,"end":286},"obj":"Sentence"},{"id":"T122","span":{"begin":287,"end":594},"obj":"Sentence"},{"id":"T123","span":{"begin":595,"end":855},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"709","span":{"begin":147,"end":153},"obj":"Chemical"},{"id":"704","span":{"begin":213,"end":216},"obj":"Gene"},{"id":"705","span":{"begin":221,"end":232},"obj":"Species"},{"id":"710","span":{"begin":259,"end":265},"obj":"Chemical"},{"id":"706","span":{"begin":362,"end":373},"obj":"Species"},{"id":"711","span":{"begin":402,"end":408},"obj":"Chemical"},{"id":"708","span":{"begin":507,"end":510},"obj":"Gene"},{"id":"712","span":{"begin":586,"end":593},"obj":"Chemical"},{"id":"707","span":{"begin":778,"end":791},"obj":"Species"},{"id":"713","span":{"begin":811,"end":817},"obj":"Chemical"}],"attributes":[{"id":"A711","pred":"pubann:denotes","subj":"711","obj":"MESH:D011134"},{"id":"A706","pred":"pubann:denotes","subj":"706","obj":"Tax:11118"},{"id":"A712","pred":"pubann:denotes","subj":"712","obj":"MESH:D011134"},{"id":"A705","pred":"pubann:denotes","subj":"705","obj":"Tax:11118"},{"id":"A710","pred":"pubann:denotes","subj":"710","obj":"MESH:D011134"},{"id":"A704","pred":"pubann:denotes","subj":"704","obj":"Gene:2995"},{"id":"A707","pred":"pubann:denotes","subj":"707","obj":"Tax:11118"},{"id":"A713","pred":"pubann:denotes","subj":"713","obj":"MESH:D011134"},{"id":"A709","pred":"pubann:denotes","subj":"709","obj":"MESH:D011134"},{"id":"A708","pred":"pubann:denotes","subj":"708","obj":"Gene:2995"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

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"pred":"uniprot_id","subj":"T4125","obj":"https://www.uniprot.org/uniprot/A3RM22"},{"id":"A4204","pred":"uniprot_id","subj":"T4125","obj":"https://www.uniprot.org/uniprot/A3F5R8"},{"id":"A4205","pred":"uniprot_id","subj":"T4125","obj":"https://www.uniprot.org/uniprot/A3F5R3"},{"id":"A4206","pred":"uniprot_id","subj":"T4125","obj":"https://www.uniprot.org/uniprot/A3F5Q8"},{"id":"A4207","pred":"uniprot_id","subj":"T4125","obj":"https://www.uniprot.org/uniprot/A3F5N3"},{"id":"A4208","pred":"uniprot_id","subj":"T4125","obj":"https://www.uniprot.org/uniprot/A3F5M3"},{"id":"A4209","pred":"uniprot_id","subj":"T4125","obj":"https://www.uniprot.org/uniprot/A3F5L8"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T40","span":{"begin":631,"end":644},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T41","span":{"begin":671,"end":686},"obj":"http://purl.obolibrary.org/obo/GO_0006955"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T37","span":{"begin":631,"end":644},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T38","span":{"begin":671,"end":686},"obj":"http://purl.obolibrary.org/obo/GO_0006955"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T41","span":{"begin":631,"end":644},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T42","span":{"begin":671,"end":686},"obj":"http://purl.obolibrary.org/obo/GO_0006955"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}

{"project":"LitCovid-sentences","denotations":[{"id":"T120","span":{"begin":0,"end":189},"obj":"Sentence"},{"id":"T121","span":{"begin":190,"end":286},"obj":"Sentence"},{"id":"T122","span":{"begin":287,"end":594},"obj":"Sentence"},{"id":"T123","span":{"begin":595,"end":855},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Viral envelope proteins are glycosylated to varying degrees, but depending on their overall mass, surface area, and volume, the overall density of glycan shielding may differ significantly. For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan “shield” over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context."}