PMC:7253482 / 378-703 JSONTXT

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{"project":"LitCovid-PD-CLO","denotations":[{"id":"T2","span":{"begin":153,"end":154},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T3","span":{"begin":322,"end":323},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"lycoprotein. Coronavirus S proteins are extensively glycosylated, encoding around 66–87 N-linked glycosylation sites per trimeric spike. Here, we reveal a specific area of high glycan density on MERS S that results in the formation of oligomannose-type glycan clusters, which were absent on SARS and HKU1 CoVs. We provide a c"}

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Coronavirus S proteins are extensively glycosylated, encoding around 66–87 N-linked glycosylation sites per trimeric spike. Here, we reveal a specific area of high glycan density on MERS S that results in the formation of oligomannose-type glycan clusters, which were absent on SARS and HKU1 CoVs. We provide a c"}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T2","span":{"begin":27,"end":35},"obj":"Body_part"}],"attributes":[{"id":"A2","pred":"fma_id","subj":"T2","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"lycoprotein. Coronavirus S proteins are extensively glycosylated, encoding around 66–87 N-linked glycosylation sites per trimeric spike. Here, we reveal a specific area of high glycan density on MERS S that results in the formation of oligomannose-type glycan clusters, which were absent on SARS and HKU1 CoVs. We provide a c"}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T2","span":{"begin":27,"end":35},"obj":"Chemical"}],"attributes":[{"id":"A2","pred":"chebi_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"lycoprotein. Coronavirus S proteins are extensively glycosylated, encoding around 66–87 N-linked glycosylation sites per trimeric spike. Here, we reveal a specific area of high glycan density on MERS S that results in the formation of oligomannose-type glycan clusters, which were absent on SARS and HKU1 CoVs. We provide a c"}

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T4","span":{"begin":195,"end":199},"obj":"Species"},{"id":"T5","span":{"begin":291,"end":295},"obj":"Species"},{"id":"T6","span":{"begin":300,"end":309},"obj":"Species"}],"attributes":[{"id":"A4","pred":"ncbi_taxonomy_id","subj":"T4","obj":"NCBItxid:1335626"},{"id":"A5","pred":"ncbi_taxonomy_id","subj":"T5","obj":"NCBItxid:694009"},{"id":"A6","pred":"ncbi_taxonomy_id","subj":"T6","obj":"NCBItxid:290028"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"lycoprotein. Coronavirus S proteins are extensively glycosylated, encoding around 66–87 N-linked glycosylation sites per trimeric spike. Here, we reveal a specific area of high glycan density on MERS S that results in the formation of oligomannose-type glycan clusters, which were absent on SARS and HKU1 CoVs. We provide a c"}

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{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T3","span":{"begin":291,"end":295},"obj":"Disease"}],"attributes":[{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"lycoprotein. Coronavirus S proteins are extensively glycosylated, encoding around 66–87 N-linked glycosylation sites per trimeric spike. Here, we reveal a specific area of high glycan density on MERS S that results in the formation of oligomannose-type glycan clusters, which were absent on SARS and HKU1 CoVs. We provide a c"}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"27","span":{"begin":13,"end":24},"obj":"Species"},{"id":"24","span":{"begin":130,"end":135},"obj":"Gene"},{"id":"34","span":{"begin":177,"end":183},"obj":"Chemical"},{"id":"42","span":{"begin":195,"end":199},"obj":"Disease"},{"id":"35","span":{"begin":235,"end":247},"obj":"Chemical"},{"id":"36","span":{"begin":253,"end":259},"obj":"Chemical"},{"id":"43","span":{"begin":291,"end":295},"obj":"Disease"},{"id":"28","span":{"begin":305,"end":309},"obj":"Species"}],"attributes":[{"id":"A43","pred":"pubann:denotes","subj":"43","obj":"MESH:D045169"},{"id":"A34","pred":"pubann:denotes","subj":"34","obj":"MESH:D011134"},{"id":"A36","pred":"pubann:denotes","subj":"36","obj":"MESH:D011134"},{"id":"A24","pred":"pubann:denotes","subj":"24","obj":"Gene:43740568"},{"id":"A28","pred":"pubann:denotes","subj":"28","obj":"Tax:11118"},{"id":"A27","pred":"pubann:denotes","subj":"27","obj":"Tax:11118"},{"id":"A42","pred":"pubann:denotes","subj":"42","obj":"MESH:D018352"}],"text":"lycoprotein. Coronavirus S proteins are extensively glycosylated, encoding around 66–87 N-linked glycosylation sites per trimeric spike. Here, we reveal a specific area of high glycan density on MERS S that results in the formation of oligomannose-type glycan clusters, which were absent on SARS and HKU1 CoVs. We provide a c"}

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{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T4","span":{"begin":97,"end":110},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T5","span":{"begin":222,"end":231},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"lycoprotein. Coronavirus S proteins are extensively glycosylated, encoding around 66–87 N-linked glycosylation sites per trimeric spike. Here, we reveal a specific area of high glycan density on MERS S that results in the formation of oligomannose-type glycan clusters, which were absent on SARS and HKU1 CoVs. We provide a c"}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T4","span":{"begin":97,"end":110},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T5","span":{"begin":222,"end":231},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"lycoprotein. Coronavirus S proteins are extensively glycosylated, encoding around 66–87 N-linked glycosylation sites per trimeric spike. Here, we reveal a specific area of high glycan density on MERS S that results in the formation of oligomannose-type glycan clusters, which were absent on SARS and HKU1 CoVs. We provide a c"}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T4","span":{"begin":88,"end":110},"obj":"http://purl.obolibrary.org/obo/GO_0006487"},{"id":"T5","span":{"begin":97,"end":110},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T6","span":{"begin":222,"end":231},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"lycoprotein. Coronavirus S proteins are extensively glycosylated, encoding around 66–87 N-linked glycosylation sites per trimeric spike. Here, we reveal a specific area of high glycan density on MERS S that results in the formation of oligomannose-type glycan clusters, which were absent on SARS and HKU1 CoVs. We provide a c"}

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