PMC:7443692 / 35556-36194 JSON TXT

Annnotations TAB JSON ListView MergeView

LitCovid-sample-CHEBI

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T200","span":{"begin":422,"end":435},"obj":"Chemical"},{"id":"T201","span":{"begin":624,"end":637},"obj":"Chemical"}],"attributes":[{"id":"A200","pred":"chebi_id","subj":"T200","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A201","pred":"chebi_id","subj":"T201","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"}],"text":"We have defined the glycomics-informed, site-specific microheterogeneity of 22 sites of N-linked glycosylation per monomer on a SARS-CoV-2 trimer and the six sites of N-linked glycosylation on a soluble version of its human ACE2 receptor by using a combination of mass spectrometry approaches coupled with evolutionary and variant sequence analyses to provide a detailed understanding of the glycosylation states of these glycoproteins (Figures 1, 2, 3, 4, 5, and 6). Our results suggest essential roles for glycosylation in mediating receptor binding, antigenic shielding, and potentially the evolution/divergence of these glycoproteins."}

LitCovid-sample-PD-NCBITaxon

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T97","span":{"begin":128,"end":138},"obj":"Species"},{"id":"T98","span":{"begin":218,"end":223},"obj":"Species"}],"attributes":[{"id":"A98","pred":"ncbi_taxonomy_id","subj":"T98","obj":"NCBItxid:9606"},{"id":"A97","pred":"ncbi_taxonomy_id","subj":"T97","obj":"NCBItxid:2697049"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"We have defined the glycomics-informed, site-specific microheterogeneity of 22 sites of N-linked glycosylation per monomer on a SARS-CoV-2 trimer and the six sites of N-linked glycosylation on a soluble version of its human ACE2 receptor by using a combination of mass spectrometry approaches coupled with evolutionary and variant sequence analyses to provide a detailed understanding of the glycosylation states of these glycoproteins (Figures 1, 2, 3, 4, 5, and 6). Our results suggest essential roles for glycosylation in mediating receptor binding, antigenic shielding, and potentially the evolution/divergence of these glycoproteins."}

LitCovid-sample-sentences

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T224","span":{"begin":0,"end":467},"obj":"Sentence"},{"id":"T225","span":{"begin":468,"end":638},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"We have defined the glycomics-informed, site-specific microheterogeneity of 22 sites of N-linked glycosylation per monomer on a SARS-CoV-2 trimer and the six sites of N-linked glycosylation on a soluble version of its human ACE2 receptor by using a combination of mass spectrometry approaches coupled with evolutionary and variant sequence analyses to provide a detailed understanding of the glycosylation states of these glycoproteins (Figures 1, 2, 3, 4, 5, and 6). Our results suggest essential roles for glycosylation in mediating receptor binding, antigenic shielding, and potentially the evolution/divergence of these glycoproteins."}

LitCovid-sample-PD-MONDO

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T64","span":{"begin":128,"end":138},"obj":"Disease"}],"attributes":[{"id":"A64","pred":"mondo_id","subj":"T64","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"We have defined the glycomics-informed, site-specific microheterogeneity of 22 sites of N-linked glycosylation per monomer on a SARS-CoV-2 trimer and the six sites of N-linked glycosylation on a soluble version of its human ACE2 receptor by using a combination of mass spectrometry approaches coupled with evolutionary and variant sequence analyses to provide a detailed understanding of the glycosylation states of these glycoproteins (Figures 1, 2, 3, 4, 5, and 6). Our results suggest essential roles for glycosylation in mediating receptor binding, antigenic shielding, and potentially the evolution/divergence of these glycoproteins."}

LitCovid-sample-UniProt

LitCovid-sample-PD-IDO

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T94","span":{"begin":40,"end":44},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T95","span":{"begin":79,"end":84},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T96","span":{"begin":158,"end":163},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"}],"text":"We have defined the glycomics-informed, site-specific microheterogeneity of 22 sites of N-linked glycosylation per monomer on a SARS-CoV-2 trimer and the six sites of N-linked glycosylation on a soluble version of its human ACE2 receptor by using a combination of mass spectrometry approaches coupled with evolutionary and variant sequence analyses to provide a detailed understanding of the glycosylation states of these glycoproteins (Figures 1, 2, 3, 4, 5, and 6). Our results suggest essential roles for glycosylation in mediating receptor binding, antigenic shielding, and potentially the evolution/divergence of these glycoproteins."}

LitCovid-sample-PD-FMA

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T104","span":{"begin":422,"end":435},"obj":"Body_part"},{"id":"T105","span":{"begin":624,"end":637},"obj":"Body_part"}],"attributes":[{"id":"A105","pred":"fma_id","subj":"T105","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A104","pred":"fma_id","subj":"T104","obj":"http://purl.org/sig/ont/fma/fma62925"}],"text":"We have defined the glycomics-informed, site-specific microheterogeneity of 22 sites of N-linked glycosylation per monomer on a SARS-CoV-2 trimer and the six sites of N-linked glycosylation on a soluble version of its human ACE2 receptor by using a combination of mass spectrometry approaches coupled with evolutionary and variant sequence analyses to provide a detailed understanding of the glycosylation states of these glycoproteins (Figures 1, 2, 3, 4, 5, and 6). Our results suggest essential roles for glycosylation in mediating receptor binding, antigenic shielding, and potentially the evolution/divergence of these glycoproteins."}

LitCovid-sample-PD-GO-BP-0

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T77","span":{"begin":97,"end":110},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T78","span":{"begin":176,"end":189},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T79","span":{"begin":392,"end":405},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T80","span":{"begin":508,"end":521},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"We have defined the glycomics-informed, site-specific microheterogeneity of 22 sites of N-linked glycosylation per monomer on a SARS-CoV-2 trimer and the six sites of N-linked glycosylation on a soluble version of its human ACE2 receptor by using a combination of mass spectrometry approaches coupled with evolutionary and variant sequence analyses to provide a detailed understanding of the glycosylation states of these glycoproteins (Figures 1, 2, 3, 4, 5, and 6). Our results suggest essential roles for glycosylation in mediating receptor binding, antigenic shielding, and potentially the evolution/divergence of these glycoproteins."}

LitCovid-sample-GO-BP

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T73","span":{"begin":97,"end":110},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T74","span":{"begin":176,"end":189},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T75","span":{"begin":392,"end":405},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T76","span":{"begin":508,"end":521},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"We have defined the glycomics-informed, site-specific microheterogeneity of 22 sites of N-linked glycosylation per monomer on a SARS-CoV-2 trimer and the six sites of N-linked glycosylation on a soluble version of its human ACE2 receptor by using a combination of mass spectrometry approaches coupled with evolutionary and variant sequence analyses to provide a detailed understanding of the glycosylation states of these glycoproteins (Figures 1, 2, 3, 4, 5, and 6). Our results suggest essential roles for glycosylation in mediating receptor binding, antigenic shielding, and potentially the evolution/divergence of these glycoproteins."}

PMC:7443692 / 35556-36194 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:7443692 / 35556-36194 JSON TXT