PMC:7253482 / 13873-14324 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"522","span":{"begin":228,"end":231},"obj":"Gene"},{"id":"523","span":{"begin":222,"end":227},"obj":"Species"},{"id":"524","span":{"begin":250,"end":259},"obj":"Species"},{"id":"525","span":{"begin":240,"end":243},"obj":"Gene"},{"id":"526","span":{"begin":39,"end":43},"obj":"Gene"},{"id":"527","span":{"begin":96,"end":103},"obj":"Chemical"},{"id":"528","span":{"begin":427,"end":443},"obj":"Chemical"},{"id":"529","span":{"begin":69,"end":73},"obj":"Disease"},{"id":"530","span":{"begin":204,"end":208},"obj":"Disease"},{"id":"531","span":{"begin":366,"end":370},"obj":"Disease"}],"attributes":[{"id":"A522","pred":"tao:has_database_id","subj":"522","obj":"Gene:64006"},{"id":"A523","pred":"tao:has_database_id","subj":"523","obj":"Tax:11676"},{"id":"A524","pred":"tao:has_database_id","subj":"524","obj":"Tax:11320"},{"id":"A525","pred":"tao:has_database_id","subj":"525","obj":"Gene:2995"},{"id":"A526","pred":"tao:has_database_id","subj":"526","obj":"Gene:1803"},{"id":"A527","pred":"tao:has_database_id","subj":"527","obj":"MESH:D011134"},{"id":"A529","pred":"tao:has_database_id","subj":"529","obj":"MESH:D018352"},{"id":"A530","pred":"tao:has_database_id","subj":"530","obj":"MESH:D045169"},{"id":"A531","pred":"tao:has_database_id","subj":"531","obj":"MESH:D018352"}],"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":"antibodies8, it is surprising that the DPP4 receptor-binding site of MERS S was not occluded by glycans (Fig. 3a), as observed for other receptor-binding sites of class I viral fusion proteins, including SARS S (Fig. 3b), HIV-1 Env49, LASV GPC24 and influenza HA50. We suggest that this is likely due to the intrinsic functionality of the receptor-binding domain of MERS S, that would be sterically hindered by the presence of N-linked glycans, wherea"}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T85","span":{"begin":184,"end":192},"obj":"Body_part"},{"id":"T86","span":{"begin":222,"end":225},"obj":"Body_part"}],"attributes":[{"id":"A85","pred":"fma_id","subj":"T85","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A86","pred":"fma_id","subj":"T86","obj":"http://purl.org/sig/ont/fma/fma278683"}],"text":"antibodies8, it is surprising that the DPP4 receptor-binding site of MERS S was not occluded by glycans (Fig. 3a), as observed for other receptor-binding sites of class I viral fusion proteins, including SARS S (Fig. 3b), HIV-1 Env49, LASV GPC24 and influenza HA50. We suggest that this is likely due to the intrinsic functionality of the receptor-binding domain of MERS S, that would be sterically hindered by the presence of N-linked glycans, wherea"}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T52","span":{"begin":204,"end":208},"obj":"Disease"},{"id":"T53","span":{"begin":250,"end":259},"obj":"Disease"}],"attributes":[{"id":"A52","pred":"mondo_id","subj":"T52","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A53","pred":"mondo_id","subj":"T53","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"}],"text":"antibodies8, it is surprising that the DPP4 receptor-binding site of MERS S was not occluded by glycans (Fig. 3a), as observed for other receptor-binding sites of class I viral fusion proteins, including SARS S (Fig. 3b), HIV-1 Env49, LASV GPC24 and influenza HA50. We suggest that this is likely due to the intrinsic functionality of the receptor-binding domain of MERS S, that would be sterically hindered by the presence of N-linked glycans, wherea"}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T161","span":{"begin":96,"end":103},"obj":"Chemical"},{"id":"T162","span":{"begin":184,"end":192},"obj":"Chemical"},{"id":"T163","span":{"begin":436,"end":443},"obj":"Chemical"}],"attributes":[{"id":"A161","pred":"chebi_id","subj":"T161","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A162","pred":"chebi_id","subj":"T162","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A163","pred":"chebi_id","subj":"T163","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"}],"text":"antibodies8, it is surprising that the DPP4 receptor-binding site of MERS S was not occluded by glycans (Fig. 3a), as observed for other receptor-binding sites of class I viral fusion proteins, including SARS S (Fig. 3b), HIV-1 Env49, LASV GPC24 and influenza HA50. We suggest that this is likely due to the intrinsic functionality of the receptor-binding domain of MERS S, that would be sterically hindered by the presence of N-linked glycans, wherea"}

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it is surprising that the DPP4 receptor-binding site of MERS S was not occluded by glycans (Fig. 3a), as observed for other receptor-binding sites of class I viral fusion proteins, including SARS S (Fig. 3b), HIV-1 Env49, LASV GPC24 and influenza HA50. We suggest that this is likely due to the intrinsic functionality of the receptor-binding domain of MERS S, that would be sterically hindered by the presence of N-linked glycans, wherea"}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T84","span":{"begin":184,"end":192},"obj":"Body_part"},{"id":"T85","span":{"begin":222,"end":225},"obj":"Body_part"}],"attributes":[{"id":"A84","pred":"fma_id","subj":"T84","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A85","pred":"fma_id","subj":"T85","obj":"http://purl.org/sig/ont/fma/fma278683"}],"text":"antibodies8, it is surprising that the DPP4 receptor-binding site of MERS S was not occluded by glycans (Fig. 3a), as observed for other receptor-binding sites of class I viral fusion proteins, including SARS S (Fig. 3b), HIV-1 Env49, LASV GPC24 and influenza HA50. We suggest that this is likely due to the intrinsic functionality of the receptor-binding domain of MERS S, that would be sterically hindered by the presence of N-linked glycans, wherea"}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T119","span":{"begin":96,"end":103},"obj":"Chemical"},{"id":"T120","span":{"begin":184,"end":192},"obj":"Chemical"},{"id":"T121","span":{"begin":436,"end":443},"obj":"Chemical"}],"attributes":[{"id":"A119","pred":"chebi_id","subj":"T119","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"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_18154"}],"text":"antibodies8, it is surprising that the DPP4 receptor-binding site of MERS S was not occluded by glycans (Fig. 3a), as observed for other receptor-binding sites of class I viral fusion proteins, including SARS S (Fig. 3b), HIV-1 Env49, LASV GPC24 and influenza HA50. We suggest that this is likely due to the intrinsic functionality of the receptor-binding domain of MERS S, that would be sterically hindered by the presence of N-linked glycans, wherea"}

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T96","span":{"begin":69,"end":73},"obj":"Species"},{"id":"T97","span":{"begin":204,"end":208},"obj":"Species"},{"id":"T98","span":{"begin":222,"end":227},"obj":"Species"},{"id":"T99","span":{"begin":235,"end":239},"obj":"Species"},{"id":"T100","span":{"begin":366,"end":370},"obj":"Species"}],"attributes":[{"id":"A96","pred":"ncbi_taxonomy_id","subj":"T96","obj":"NCBItxid:1335626"},{"id":"A97","pred":"ncbi_taxonomy_id","subj":"T97","obj":"NCBItxid:694009"},{"id":"A98","pred":"ncbi_taxonomy_id","subj":"T98","obj":"NCBItxid:11676"},{"id":"A99","pred":"ncbi_taxonomy_id","subj":"T99","obj":"NCBItxid:11620"},{"id":"A100","pred":"ncbi_taxonomy_id","subj":"T100","obj":"NCBItxid:1335626"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"antibodies8, it is surprising that the DPP4 receptor-binding site of MERS S was not occluded by glycans (Fig. 3a), as observed for other receptor-binding sites of class I viral fusion proteins, including SARS S (Fig. 3b), HIV-1 Env49, LASV GPC24 and influenza HA50. We suggest that this is likely due to the intrinsic functionality of the receptor-binding domain of MERS S, that would be sterically hindered by the presence of N-linked glycans, wherea"}

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T47","span":{"begin":204,"end":208},"obj":"Disease"},{"id":"T48","span":{"begin":250,"end":259},"obj":"Disease"}],"attributes":[{"id":"A47","pred":"mondo_id","subj":"T47","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A48","pred":"mondo_id","subj":"T48","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"}],"text":"antibodies8, it is surprising that the DPP4 receptor-binding site of MERS S was not occluded by glycans (Fig. 3a), as observed for other receptor-binding sites of class I viral fusion proteins, including SARS S (Fig. 3b), HIV-1 Env49, LASV GPC24 and influenza HA50. We suggest that this is likely due to the intrinsic functionality of the receptor-binding domain of MERS S, that would be sterically hindered by the presence of N-linked glycans, wherea"}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"526","span":{"begin":39,"end":43},"obj":"Gene"},{"id":"529","span":{"begin":69,"end":73},"obj":"Disease"},{"id":"527","span":{"begin":96,"end":103},"obj":"Chemical"},{"id":"530","span":{"begin":204,"end":208},"obj":"Disease"},{"id":"523","span":{"begin":222,"end":227},"obj":"Species"},{"id":"522","span":{"begin":228,"end":231},"obj":"Gene"},{"id":"525","span":{"begin":240,"end":243},"obj":"Gene"},{"id":"524","span":{"begin":250,"end":259},"obj":"Species"},{"id":"531","span":{"begin":366,"end":370},"obj":"Disease"},{"id":"528","span":{"begin":427,"end":443},"obj":"Chemical"}],"attributes":[{"id":"A527","pred":"pubann:denotes","subj":"527","obj":"MESH:D011134"},{"id":"A529","pred":"pubann:denotes","subj":"529","obj":"MESH:D018352"},{"id":"A531","pred":"pubann:denotes","subj":"531","obj":"MESH:D018352"},{"id":"A524","pred":"pubann:denotes","subj":"524","obj":"Tax:11320"},{"id":"A525","pred":"pubann:denotes","subj":"525","obj":"Gene:2995"},{"id":"A523","pred":"pubann:denotes","subj":"523","obj":"Tax:11676"},{"id":"A526","pred":"pubann:denotes","subj":"526","obj":"Gene:1803"},{"id":"A530","pred":"pubann:denotes","subj":"530","obj":"MESH:D045169"},{"id":"A522","pred":"pubann:denotes","subj":"522","obj":"Gene:64006"}],"text":"antibodies8, it is surprising that the DPP4 receptor-binding site of MERS S was not occluded by glycans (Fig. 3a), as observed for other receptor-binding sites of class I viral fusion proteins, including SARS S (Fig. 3b), HIV-1 Env49, LASV GPC24 and influenza HA50. We suggest that this is likely due to the intrinsic functionality of the receptor-binding domain of MERS S, that would be sterically hindered by the presence of N-linked glycans, wherea"}

{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T3669","span":{"begin":39,"end":43},"obj":"Protein"}],"attributes":[{"id":"A3669","pred":"uniprot_id","subj":"T3669","obj":"https://www.uniprot.org/uniprot/Q9N2I7"}],"text":"antibodies8, it is surprising that the DPP4 receptor-binding site of MERS S was not occluded by glycans (Fig. 3a), as observed for other receptor-binding sites of class I viral fusion proteins, including SARS S (Fig. 3b), HIV-1 Env49, LASV GPC24 and influenza HA50. We suggest that this is likely due to the intrinsic functionality of the receptor-binding domain of MERS S, that would be sterically hindered by the presence of N-linked glycans, wherea"}