PMC:7199903 / 11211-11910 JSON TXT

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LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T58","span":{"begin":287,"end":300},"obj":"Body_part"},{"id":"T59","span":{"begin":340,"end":343},"obj":"Body_part"},{"id":"T60","span":{"begin":676,"end":689},"obj":"Body_part"}],"attributes":[{"id":"A58","pred":"fma_id","subj":"T58","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A59","pred":"fma_id","subj":"T59","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A60","pred":"fma_id","subj":"T60","obj":"http://purl.org/sig/ont/fma/fma62925"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T44","span":{"begin":47,"end":55},"obj":"Disease"},{"id":"T45","span":{"begin":317,"end":325},"obj":"Disease"},{"id":"T46","span":{"begin":356,"end":365},"obj":"Disease"}],"attributes":[{"id":"A44","pred":"mondo_id","subj":"T44","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A45","pred":"mondo_id","subj":"T45","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A46","pred":"mondo_id","subj":"T46","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T68","span":{"begin":261,"end":262},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T69","span":{"begin":351,"end":353},"obj":"http://purl.obolibrary.org/obo/CLO_0050509"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-PD-CHEBI

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T113","span":{"begin":250,"end":257},"obj":"Chemical"},{"id":"T114","span":{"begin":287,"end":300},"obj":"Chemical"},{"id":"T115","span":{"begin":575,"end":582},"obj":"Chemical"},{"id":"T116","span":{"begin":676,"end":689},"obj":"Chemical"}],"attributes":[{"id":"A113","pred":"chebi_id","subj":"T113","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A114","pred":"chebi_id","subj":"T114","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A115","pred":"chebi_id","subj":"T115","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A116","pred":"chebi_id","subj":"T116","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-sample-PD-IDO

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T56","span":{"begin":34,"end":39},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T57","span":{"begin":90,"end":95},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T58","span":{"begin":241,"end":246},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T59","span":{"begin":419,"end":429},"obj":"http://purl.obolibrary.org/obo/BFO_0000034"},{"id":"T60","span":{"begin":462,"end":467},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-sample-Enju

LitCovid-sample-PD-FMA

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T57","span":{"begin":287,"end":300},"obj":"Body_part"},{"id":"T58","span":{"begin":340,"end":343},"obj":"Body_part"},{"id":"T59","span":{"begin":676,"end":689},"obj":"Body_part"}],"attributes":[{"id":"A58","pred":"fma_id","subj":"T58","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A59","pred":"fma_id","subj":"T59","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A57","pred":"fma_id","subj":"T57","obj":"http://purl.org/sig/ont/fma/fma62925"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-sample-CHEBI

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T85","span":{"begin":250,"end":257},"obj":"Chemical"},{"id":"T86","span":{"begin":287,"end":300},"obj":"Chemical"},{"id":"T87","span":{"begin":575,"end":582},"obj":"Chemical"},{"id":"T88","span":{"begin":676,"end":689},"obj":"Chemical"}],"attributes":[{"id":"A86","pred":"chebi_id","subj":"T86","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A88","pred":"chebi_id","subj":"T88","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A87","pred":"chebi_id","subj":"T87","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A85","pred":"chebi_id","subj":"T85","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-sample-PD-NCBITaxon

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T43","span":{"begin":47,"end":57},"obj":"Species"},{"id":"T44","span":{"begin":317,"end":325},"obj":"Species"},{"id":"T45","span":{"begin":340,"end":345},"obj":"Species"},{"id":"T46","span":{"begin":394,"end":398},"obj":"Species"}],"attributes":[{"id":"A43","pred":"ncbi_taxonomy_id","subj":"T43","obj":"NCBItxid:2697049"},{"id":"A44","pred":"ncbi_taxonomy_id","subj":"T44","obj":"NCBItxid:694009"},{"id":"A45","pred":"ncbi_taxonomy_id","subj":"T45","obj":"NCBItxid:11676"},{"id":"A46","pred":"ncbi_taxonomy_id","subj":"T46","obj":"NCBItxid:11620"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-sample-sentences

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T77","span":{"begin":0,"end":206},"obj":"Sentence"},{"id":"T78","span":{"begin":207,"end":408},"obj":"Sentence"},{"id":"T79","span":{"begin":409,"end":699},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-sample-PD-MONDO

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T38","span":{"begin":47,"end":57},"obj":"Disease"},{"id":"T39","span":{"begin":317,"end":325},"obj":"Disease"},{"id":"T40","span":{"begin":356,"end":365},"obj":"Disease"}],"attributes":[{"id":"A38","pred":"mondo_id","subj":"T38","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A39","pred":"mondo_id","subj":"T39","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A40","pred":"mondo_id","subj":"T40","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-sample-Pubtator

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"376","span":{"begin":58,"end":63},"obj":"Gene"},{"id":"377","span":{"begin":47,"end":57},"obj":"Species"},{"id":"378","span":{"begin":317,"end":325},"obj":"Species"},{"id":"380","span":{"begin":356,"end":365},"obj":"Species"},{"id":"382","span":{"begin":250,"end":257},"obj":"Chemical"},{"id":"383","span":{"begin":566,"end":582},"obj":"Chemical"}],"attributes":[{"id":"A377","pred":"pubann:denotes","subj":"377","obj":"Tax:2697049"},{"id":"A380","pred":"pubann:denotes","subj":"380","obj":"Tax:11309"},{"id":"A376","pred":"pubann:denotes","subj":"376","obj":"Gene:43740568"},{"id":"A382","pred":"pubann:denotes","subj":"382","obj":"MESH:D011134"},{"id":"A378","pred":"pubann:denotes","subj":"378","obj":"Tax:694009"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-sample-UniProt

LitCovid-sample-PD-MAT

{"project":"LitCovid-sample-PD-MAT","denotations":[{"id":"T3","span":{"begin":67,"end":75},"obj":"http://purl.obolibrary.org/obo/MAT_0000491"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-sample-PD-GO-BP-0

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T34","span":{"begin":76,"end":89},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-sample-GO-BP

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T32","span":{"begin":76,"end":89},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T37","span":{"begin":76,"end":89},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T77","span":{"begin":0,"end":206},"obj":"Sentence"},{"id":"T78","span":{"begin":207,"end":408},"obj":"Sentence"},{"id":"T79","span":{"begin":409,"end":699},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

LitCovid-PubTator

{"project":"LitCovid-PubTator","denotations":[{"id":"374","span":{"begin":346,"end":349},"obj":"Gene"},{"id":"375","span":{"begin":399,"end":402},"obj":"Gene"},{"id":"376","span":{"begin":58,"end":63},"obj":"Gene"},{"id":"377","span":{"begin":47,"end":57},"obj":"Species"},{"id":"378","span":{"begin":317,"end":325},"obj":"Species"},{"id":"379","span":{"begin":340,"end":345},"obj":"Species"},{"id":"380","span":{"begin":356,"end":365},"obj":"Species"},{"id":"381","span":{"begin":394,"end":398},"obj":"Species"},{"id":"382","span":{"begin":250,"end":257},"obj":"Chemical"},{"id":"383","span":{"begin":566,"end":582},"obj":"Chemical"}],"attributes":[{"id":"A374","pred":"tao:has_database_id","subj":"374","obj":"Gene:100616444"},{"id":"A375","pred":"tao:has_database_id","subj":"375","obj":"Gene:2995"},{"id":"A376","pred":"tao:has_database_id","subj":"376","obj":"Gene:43740568"},{"id":"A377","pred":"tao:has_database_id","subj":"377","obj":"Tax:2697049"},{"id":"A378","pred":"tao:has_database_id","subj":"378","obj":"Tax:694009"},{"id":"A379","pred":"tao:has_database_id","subj":"379","obj":"Tax:11676"},{"id":"A380","pred":"tao:has_database_id","subj":"380","obj":"Tax:11309"},{"id":"A381","pred":"tao:has_database_id","subj":"381","obj":"Tax:11620"},{"id":"A382","pred":"tao:has_database_id","subj":"382","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":"Shielding of the receptor binding sites on the SARS-CoV-2 spike by proximal glycosylation sites (N165, N234, N343) can be observed, especially when the receptor binding domain is in the “down” conformation. The shielding of receptor binding sites by glycans is a common feature of viral glycoproteins, as observed on SARS-CoV-1 S (10, 13), HIV-1 Env (27), influenza hemagglutinin (28, 29), and LASV GPC (24). Given the functional constraints of receptor binding sites and the resulting low mutation rates of these residues, there is likely selective pressure to use N-linked glycans to camouflage one of the most conserved and potentially vulnerable areas of their respective glycoproteins (30, 31)."}

PMC:7199903 / 11211-11910 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:7199903 / 11211-11910 JSON TXT