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LitCovid_Glycan-Motif-Structure

{"project":"LitCovid_Glycan-Motif-Structure","denotations":[{"id":"T211","span":{"begin":175,"end":177},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T212","span":{"begin":615,"end":617},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T213","span":{"begin":769,"end":771},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T214","span":{"begin":952,"end":954},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Using computer simulation techniques, CLQ and CLQ-OH have been suggested to recognize the enzymatic active site of the UDP-GlcNAc 2-epimerase, known as an essential enzyme in SA biosynthesis [144], blocking the sialylation of host cells. The mechanism underlying the glycosylation inhibition may support the antiviral properties of CLQ and CLQ-OH through interactions of CLQ or CLQ-OH with NDP-saccharide mutases or glycosyltransferases [145]. CLQ was reported to inhibit quinone reductase 2 [146], known as a catalytic mimetic or structural neighbor of UDP-GlcNAc 2-epimerases [147,148]. If CLQ or CLQ-OH inhibits SA synthesis, the inhibitory properties may support the antiviral activity of CLQ or CLQ-OH against SARS-CoVs because the SARS-CoV receptor ACE2 contains SA species. In fact, CLQ exhibits in vitro anti-SARS-CoV-1 activity via defective glycosylation of viral ACE2 in Vero cells [149]. In addition. the interference of CLQ or CLQ-OH with SA synthesis may broadly be applicable as an antiviral because the HcoVs or other orthomyxoviruses also utilize SAs as entry molecules [150]. However, the detailed mechanisms should be further elucidated. The CLQ treatment efficacy in Covid-19 patients has, however, not been conclusively determined."}

LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T707","span":{"begin":231,"end":236},"obj":"Body_part"},{"id":"T708","span":{"begin":887,"end":892},"obj":"Body_part"}],"attributes":[{"id":"A707","pred":"fma_id","subj":"T707","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A708","pred":"fma_id","subj":"T708","obj":"http://purl.org/sig/ont/fma/fma68646"}],"text":"Using computer simulation techniques, CLQ and CLQ-OH have been suggested to recognize the enzymatic active site of the UDP-GlcNAc 2-epimerase, known as an essential enzyme in SA biosynthesis [144], blocking the sialylation of host cells. The mechanism underlying the glycosylation inhibition may support the antiviral properties of CLQ and CLQ-OH through interactions of CLQ or CLQ-OH with NDP-saccharide mutases or glycosyltransferases [145]. CLQ was reported to inhibit quinone reductase 2 [146], known as a catalytic mimetic or structural neighbor of UDP-GlcNAc 2-epimerases [147,148]. If CLQ or CLQ-OH inhibits SA synthesis, the inhibitory properties may support the antiviral activity of CLQ or CLQ-OH against SARS-CoVs because the SARS-CoV receptor ACE2 contains SA species. In fact, CLQ exhibits in vitro anti-SARS-CoV-1 activity via defective glycosylation of viral ACE2 in Vero cells [149]. In addition. the interference of CLQ or CLQ-OH with SA synthesis may broadly be applicable as an antiviral because the HcoVs or other orthomyxoviruses also utilize SAs as entry molecules [150]. However, the detailed mechanisms should be further elucidated. The CLQ treatment efficacy in Covid-19 patients has, however, not been conclusively determined."}

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T286","span":{"begin":390,"end":393},"obj":"Disease"},{"id":"T287","span":{"begin":715,"end":719},"obj":"Disease"},{"id":"T288","span":{"begin":737,"end":745},"obj":"Disease"},{"id":"T289","span":{"begin":817,"end":825},"obj":"Disease"}],"attributes":[{"id":"A286","pred":"mondo_id","subj":"T286","obj":"http://purl.obolibrary.org/obo/MONDO_0010691"},{"id":"A287","pred":"mondo_id","subj":"T287","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A288","pred":"mondo_id","subj":"T288","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A289","pred":"mondo_id","subj":"T289","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Using computer simulation techniques, CLQ and CLQ-OH have been suggested to recognize the enzymatic active site of the UDP-GlcNAc 2-epimerase, known as an essential enzyme in SA biosynthesis [144], blocking the sialylation of host cells. The mechanism underlying the glycosylation inhibition may support the antiviral properties of CLQ and CLQ-OH through interactions of CLQ or CLQ-OH with NDP-saccharide mutases or glycosyltransferases [145]. CLQ was reported to inhibit quinone reductase 2 [146], known as a catalytic mimetic or structural neighbor of UDP-GlcNAc 2-epimerases [147,148]. If CLQ or CLQ-OH inhibits SA synthesis, the inhibitory properties may support the antiviral activity of CLQ or CLQ-OH against SARS-CoVs because the SARS-CoV receptor ACE2 contains SA species. In fact, CLQ exhibits in vitro anti-SARS-CoV-1 activity via defective glycosylation of viral ACE2 in Vero cells [149]. In addition. the interference of CLQ or CLQ-OH with SA synthesis may broadly be applicable as an antiviral because the HcoVs or other orthomyxoviruses also utilize SAs as entry molecules [150]. However, the detailed mechanisms should be further elucidated. The CLQ treatment efficacy in Covid-19 patients has, however, not been conclusively determined."}

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T1049","span":{"begin":100,"end":106},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T1050","span":{"begin":231,"end":236},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T1051","span":{"begin":508,"end":509},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T1052","span":{"begin":681,"end":689},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T1053","span":{"begin":828,"end":836},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T1054","span":{"begin":882,"end":886},"obj":"http://purl.obolibrary.org/obo/CLO_0009524"},{"id":"T1055","span":{"begin":882,"end":886},"obj":"http://purl.obolibrary.org/obo/CLO_0050515"},{"id":"T1056","span":{"begin":887,"end":892},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T1057","span":{"begin":1064,"end":1067},"obj":"http://purl.obolibrary.org/obo/CLO_0051568"},{"id":"T1058","span":{"begin":1205,"end":1208},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"}],"text":"Using computer simulation techniques, CLQ and CLQ-OH have been suggested to recognize the enzymatic active site of the UDP-GlcNAc 2-epimerase, known as an essential enzyme in SA biosynthesis [144], blocking the sialylation of host cells. The mechanism underlying the glycosylation inhibition may support the antiviral properties of CLQ and CLQ-OH through interactions of CLQ or CLQ-OH with NDP-saccharide mutases or glycosyltransferases [145]. CLQ was reported to inhibit quinone reductase 2 [146], known as a catalytic mimetic or structural neighbor of UDP-GlcNAc 2-epimerases [147,148]. If CLQ or CLQ-OH inhibits SA synthesis, the inhibitory properties may support the antiviral activity of CLQ or CLQ-OH against SARS-CoVs because the SARS-CoV receptor ACE2 contains SA species. In fact, CLQ exhibits in vitro anti-SARS-CoV-1 activity via defective glycosylation of viral ACE2 in Vero cells [149]. In addition. the interference of CLQ or CLQ-OH with SA synthesis may broadly be applicable as an antiviral because the HcoVs or other orthomyxoviruses also utilize SAs as entry molecules [150]. However, the detailed mechanisms should be further elucidated. The CLQ treatment efficacy in Covid-19 patients has, however, not been conclusively determined."}

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T139","span":{"begin":178,"end":190},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T140","span":{"begin":211,"end":222},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T141","span":{"begin":267,"end":280},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T142","span":{"begin":618,"end":627},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T143","span":{"begin":851,"end":864},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T144","span":{"begin":955,"end":964},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"Using computer simulation techniques, CLQ and CLQ-OH have been suggested to recognize the enzymatic active site of the UDP-GlcNAc 2-epimerase, known as an essential enzyme in SA biosynthesis [144], blocking the sialylation of host cells. The mechanism underlying the glycosylation inhibition may support the antiviral properties of CLQ and CLQ-OH through interactions of CLQ or CLQ-OH with NDP-saccharide mutases or glycosyltransferases [145]. CLQ was reported to inhibit quinone reductase 2 [146], known as a catalytic mimetic or structural neighbor of UDP-GlcNAc 2-epimerases [147,148]. If CLQ or CLQ-OH inhibits SA synthesis, the inhibitory properties may support the antiviral activity of CLQ or CLQ-OH against SARS-CoVs because the SARS-CoV receptor ACE2 contains SA species. In fact, CLQ exhibits in vitro anti-SARS-CoV-1 activity via defective glycosylation of viral ACE2 in Vero cells [149]. In addition. the interference of CLQ or CLQ-OH with SA synthesis may broadly be applicable as an antiviral because the HcoVs or other orthomyxoviruses also utilize SAs as entry molecules [150]. However, the detailed mechanisms should be further elucidated. The CLQ treatment efficacy in Covid-19 patients has, however, not been conclusively determined."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T720","span":{"begin":0,"end":237},"obj":"Sentence"},{"id":"T721","span":{"begin":238,"end":443},"obj":"Sentence"},{"id":"T722","span":{"begin":444,"end":588},"obj":"Sentence"},{"id":"T723","span":{"begin":589,"end":780},"obj":"Sentence"},{"id":"T724","span":{"begin":781,"end":899},"obj":"Sentence"},{"id":"T725","span":{"begin":900,"end":1093},"obj":"Sentence"},{"id":"T726","span":{"begin":1094,"end":1156},"obj":"Sentence"},{"id":"T727","span":{"begin":1157,"end":1252},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Using computer simulation techniques, CLQ and CLQ-OH have been suggested to recognize the enzymatic active site of the UDP-GlcNAc 2-epimerase, known as an essential enzyme in SA biosynthesis [144], blocking the sialylation of host cells. The mechanism underlying the glycosylation inhibition may support the antiviral properties of CLQ and CLQ-OH through interactions of CLQ or CLQ-OH with NDP-saccharide mutases or glycosyltransferases [145]. CLQ was reported to inhibit quinone reductase 2 [146], known as a catalytic mimetic or structural neighbor of UDP-GlcNAc 2-epimerases [147,148]. If CLQ or CLQ-OH inhibits SA synthesis, the inhibitory properties may support the antiviral activity of CLQ or CLQ-OH against SARS-CoVs because the SARS-CoV receptor ACE2 contains SA species. In fact, CLQ exhibits in vitro anti-SARS-CoV-1 activity via defective glycosylation of viral ACE2 in Vero cells [149]. In addition. the interference of CLQ or CLQ-OH with SA synthesis may broadly be applicable as an antiviral because the HcoVs or other orthomyxoviruses also utilize SAs as entry molecules [150]. However, the detailed mechanisms should be further elucidated. The CLQ treatment efficacy in Covid-19 patients has, however, not been conclusively determined."}

2_test

{"project":"2_test","denotations":[{"id":"32604730-16439323-51944110","span":{"begin":192,"end":195},"obj":"16439323"},{"id":"32604730-32171740-51944111","span":{"begin":438,"end":441},"obj":"32171740"},{"id":"32604730-15078100-51944112","span":{"begin":493,"end":496},"obj":"15078100"},{"id":"32604730-9068613-51944113","span":{"begin":583,"end":586},"obj":"9068613"},{"id":"32604730-16115318-51944114","span":{"begin":894,"end":897},"obj":"16115318"},{"id":"32604730-15766653-51944115","span":{"begin":1088,"end":1091},"obj":"15766653"},{"id":"T27482","span":{"begin":192,"end":195},"obj":"16439323"},{"id":"T60108","span":{"begin":438,"end":441},"obj":"32171740"},{"id":"T75339","span":{"begin":493,"end":496},"obj":"15078100"},{"id":"T38963","span":{"begin":583,"end":586},"obj":"9068613"},{"id":"T54788","span":{"begin":894,"end":897},"obj":"16115318"},{"id":"T38477","span":{"begin":1088,"end":1091},"obj":"15766653"}],"text":"Using computer simulation techniques, CLQ and CLQ-OH have been suggested to recognize the enzymatic active site of the UDP-GlcNAc 2-epimerase, known as an essential enzyme in SA biosynthesis [144], blocking the sialylation of host cells. The mechanism underlying the glycosylation inhibition may support the antiviral properties of CLQ and CLQ-OH through interactions of CLQ or CLQ-OH with NDP-saccharide mutases or glycosyltransferases [145]. CLQ was reported to inhibit quinone reductase 2 [146], known as a catalytic mimetic or structural neighbor of UDP-GlcNAc 2-epimerases [147,148]. If CLQ or CLQ-OH inhibits SA synthesis, the inhibitory properties may support the antiviral activity of CLQ or CLQ-OH against SARS-CoVs because the SARS-CoV receptor ACE2 contains SA species. In fact, CLQ exhibits in vitro anti-SARS-CoV-1 activity via defective glycosylation of viral ACE2 in Vero cells [149]. In addition. the interference of CLQ or CLQ-OH with SA synthesis may broadly be applicable as an antiviral because the HcoVs or other orthomyxoviruses also utilize SAs as entry molecules [150]. However, the detailed mechanisms should be further elucidated. The CLQ treatment efficacy in Covid-19 patients has, however, not been conclusively determined."}

PMC:7352545 / 74229-75481 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:7352545 / 74229-75481 JSON TXT