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this study adds further evidence suggesting that extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, in comparison to glycan shields of certain other viruses, which is reflected by the overall structure, density and oligomannose abundance across the corresponding trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vulnerability on the glycoprotein. Furthermore, comparisons between glycan shields from a number of viruses highlight the importance of a glycan shield in immune evasion and reveal structural principles that govern glycosylation status."}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T144","span":{"begin":121,"end":129},"obj":"Body_part"},{"id":"T145","span":{"begin":341,"end":354},"obj":"Body_part"},{"id":"T146","span":{"begin":381,"end":391},"obj":"Body_part"},{"id":"T147","span":{"begin":425,"end":433},"obj":"Body_part"},{"id":"T148","span":{"begin":562,"end":574},"obj":"Body_part"}],"attributes":[{"id":"A144","pred":"fma_id","subj":"T144","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A147","pred":"fma_id","subj":"T147","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A145","pred":"fma_id","subj":"T145","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A148","pred":"fma_id","subj":"T148","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A146","pred":"fma_id","subj":"T146","obj":"http://purl.org/sig/ont/fma/fma82739"}],"text":"Overall, this study adds further evidence suggesting that extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, in comparison to glycan shields of certain other viruses, which is reflected by the overall structure, density and oligomannose abundance across the corresponding trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vulnerability on the glycoprotein. Furthermore, comparisons between glycan shields from a number of viruses highlight the importance of a glycan shield in immune evasion and reveal structural principles that govern glycosylation status."}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T169","span":{"begin":121,"end":129},"obj":"Chemical"},{"id":"T170","span":{"begin":341,"end":354},"obj":"Chemical"},{"id":"T171","span":{"begin":381,"end":386},"obj":"Chemical"},{"id":"T172","span":{"begin":488,"end":495},"obj":"Chemical"},{"id":"T173","span":{"begin":562,"end":574},"obj":"Chemical"}],"attributes":[{"id":"A170","pred":"chebi_id","subj":"T170","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A173","pred":"chebi_id","subj":"T173","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A171","pred":"chebi_id","subj":"T171","obj":"http://purl.obolibrary.org/obo/CHEBI_46882"},{"id":"A169","pred":"chebi_id","subj":"T169","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A172","pred":"chebi_id","subj":"T172","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"}],"text":"Overall, this study adds further evidence suggesting that extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, in comparison to glycan shields of certain other viruses, which is reflected by the overall structure, density and oligomannose abundance across the corresponding trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vulnerability on the glycoprotein. Furthermore, comparisons between glycan shields from a number of viruses highlight the importance of a glycan shield in immune evasion and reveal structural principles that govern glycosylation status."}

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T192","span":{"begin":101,"end":105},"obj":"Species"},{"id":"T193","span":{"begin":110,"end":118},"obj":"Species"},{"id":"T194","span":{"begin":218,"end":225},"obj":"Species"},{"id":"T195","span":{"begin":641,"end":648},"obj":"Species"}],"attributes":[{"id":"A192","pred":"ncbi_taxonomy_id","subj":"T192","obj":"NCBItxid:694009"},{"id":"A195","pred":"ncbi_taxonomy_id","subj":"T195","obj":"NCBItxid:10239"},{"id":"A194","pred":"ncbi_taxonomy_id","subj":"T194","obj":"NCBItxid:10239"},{"id":"A193","pred":"ncbi_taxonomy_id","subj":"T193","obj":"NCBItxid:1335626"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"Overall, this study adds further evidence suggesting that extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, in comparison to glycan shields of certain other viruses, which is reflected by the overall structure, density and oligomannose abundance across the corresponding trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vulnerability on the glycoprotein. Furthermore, comparisons between glycan shields from a number of viruses highlight the importance of a glycan shield in immune evasion and reveal structural principles that govern glycosylation status."}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T147","span":{"begin":0,"end":355},"obj":"Sentence"},{"id":"T148","span":{"begin":356,"end":575},"obj":"Sentence"},{"id":"T149","span":{"begin":576,"end":777},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Overall, this study adds further evidence suggesting that extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, in comparison to glycan shields of certain other viruses, which is reflected by the overall structure, density and oligomannose abundance across the corresponding trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vulnerability on the glycoprotein. Furthermore, comparisons between glycan shields from a number of viruses highlight the importance of a glycan shield in immune evasion and reveal structural principles that govern glycosylation status."}

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T88","span":{"begin":101,"end":105},"obj":"Disease"}],"attributes":[{"id":"A88","pred":"mondo_id","subj":"T88","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Overall, this study adds further evidence suggesting that extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, in comparison to glycan shields of certain other viruses, which is reflected by the overall structure, density and oligomannose abundance across the corresponding trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vulnerability on the glycoprotein. Furthermore, comparisons between glycan shields from a number of viruses highlight the importance of a glycan shield in immune evasion and reveal structural principles that govern glycosylation status."}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"845","span":{"begin":68,"end":83},"obj":"Chemical"},{"id":"851","span":{"begin":101,"end":105},"obj":"Disease"},{"id":"844","span":{"begin":110,"end":118},"obj":"Species"},{"id":"846","span":{"begin":186,"end":192},"obj":"Chemical"},{"id":"847","span":{"begin":284,"end":296},"obj":"Chemical"},{"id":"848","span":{"begin":488,"end":495},"obj":"Chemical"},{"id":"849","span":{"begin":609,"end":615},"obj":"Chemical"},{"id":"850","span":{"begin":679,"end":685},"obj":"Chemical"}],"attributes":[{"id":"A850","pred":"pubann:denotes","subj":"850","obj":"MESH:D011134"},{"id":"A848","pred":"pubann:denotes","subj":"848","obj":"MESH:D011134"},{"id":"A851","pred":"pubann:denotes","subj":"851","obj":"MESH:D045169"},{"id":"A849","pred":"pubann:denotes","subj":"849","obj":"MESH:D011134"},{"id":"A846","pred":"pubann:denotes","subj":"846","obj":"MESH:D011134"},{"id":"A844","pred":"pubann:denotes","subj":"844","obj":"Tax:1335626"}],"text":"Overall, this study adds further evidence suggesting that extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, in comparison to glycan shields of certain other viruses, which is reflected by the overall structure, density and oligomannose abundance across the corresponding trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vulnerability on the glycoprotein. Furthermore, comparisons between glycan shields from a number of viruses highlight the importance of a glycan shield in immune evasion and reveal structural principles that govern glycosylation status."}

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this study adds further evidence suggesting that extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, in comparison to glycan shields of certain other viruses, which is reflected by the overall structure, density and oligomannose abundance across the corresponding trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vulnerability on the glycoprotein. Furthermore, comparisons between glycan shields from a number of viruses highlight the importance of a glycan shield in immune evasion and reveal structural principles that govern glycosylation status."}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T54","span":{"begin":696,"end":710},"obj":"http://purl.obolibrary.org/obo/GO_0020012"},{"id":"T55","span":{"begin":696,"end":710},"obj":"http://purl.obolibrary.org/obo/GO_0051805"},{"id":"T56","span":{"begin":756,"end":769},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Overall, this study adds further evidence suggesting that extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, in comparison to glycan shields of certain other viruses, which is reflected by the overall structure, density and oligomannose abundance across the corresponding trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vulnerability on the glycoprotein. Furthermore, comparisons between glycan shields from a number of viruses highlight the importance of a glycan shield in immune evasion and reveal structural principles that govern glycosylation status."}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T49","span":{"begin":696,"end":710},"obj":"http://purl.obolibrary.org/obo/GO_0042783"},{"id":"T50","span":{"begin":756,"end":769},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Overall, this study adds further evidence suggesting that extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, in comparison to glycan shields of certain other viruses, which is reflected by the overall structure, density and oligomannose abundance across the corresponding trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vulnerability on the glycoprotein. Furthermore, comparisons between glycan shields from a number of viruses highlight the importance of a glycan shield in immune evasion and reveal structural principles that govern glycosylation status."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T54","span":{"begin":696,"end":710},"obj":"http://purl.obolibrary.org/obo/GO_0042783"},{"id":"T55","span":{"begin":756,"end":769},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Overall, this study adds further evidence suggesting that extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, in comparison to glycan shields of certain other viruses, which is reflected by the overall structure, density and oligomannose abundance across the corresponding trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vulnerability on the glycoprotein. Furthermore, comparisons between glycan shields from a number of viruses highlight the importance of a glycan shield in immune evasion and reveal structural principles that govern glycosylation status."}

{"project":"LitCovid-sentences","denotations":[{"id":"T147","span":{"begin":0,"end":355},"obj":"Sentence"},{"id":"T148","span":{"begin":356,"end":575},"obj":"Sentence"},{"id":"T149","span":{"begin":576,"end":777},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Overall, this study adds further evidence suggesting that extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, in comparison to glycan shields of certain other viruses, which is reflected by the overall structure, density and oligomannose abundance across the corresponding trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vulnerability on the glycoprotein. Furthermore, comparisons between glycan shields from a number of viruses highlight the importance of a glycan shield in immune evasion and reveal structural principles that govern glycosylation status."}