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LitCovid_Glycan-Motif-Structure

{"project":"LitCovid_Glycan-Motif-Structure","denotations":[{"id":"T236","span":{"begin":26,"end":29},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T237","span":{"begin":26,"end":29},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T238","span":{"begin":213,"end":216},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T239","span":{"begin":213,"end":216},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T240","span":{"begin":250,"end":253},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T241","span":{"begin":250,"end":253},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T242","span":{"begin":370,"end":373},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T243","span":{"begin":370,"end":373},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T244","span":{"begin":487,"end":490},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T245","span":{"begin":487,"end":490},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"}],"text":"As CLQ interacts with the GM1 sugar part, the N-terminal domain of the S protein loses viral attachment capacity to the cell receptors [166]. The S protein NTD and the CLQ/CLQ-OH maintain the same position during GM1 binding, consequently preventing GM1 binding to the S protein and the drug at the same time, because the NTD and the CLQ/CLQ-OH simultaneously recognize GM1. Asn-167 forms a hydrogen bond with the GalNAc residue, whereas an aromatic Phe-135 stacks to the Glc residue of GM1. Therefore, the antiviral activities of CLQ and CLQ-OH is to block the interaction between the SARS-CoV-2 S glycoprotein and gangliosides on host cell surfaces. The lipid composition of host cell PM can also be a potential target for preventive and therapeutic drugs against such viruses."}

LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T768","span":{"begin":30,"end":35},"obj":"Body_part"},{"id":"T769","span":{"begin":73,"end":80},"obj":"Body_part"},{"id":"T770","span":{"begin":120,"end":124},"obj":"Body_part"},{"id":"T771","span":{"begin":148,"end":155},"obj":"Body_part"},{"id":"T772","span":{"begin":271,"end":278},"obj":"Body_part"},{"id":"T773","span":{"begin":599,"end":611},"obj":"Body_part"},{"id":"T774","span":{"begin":616,"end":628},"obj":"Body_part"},{"id":"T775","span":{"begin":637,"end":650},"obj":"Body_part"},{"id":"T776","span":{"begin":637,"end":641},"obj":"Body_part"},{"id":"T777","span":{"begin":656,"end":661},"obj":"Body_part"},{"id":"T778","span":{"begin":682,"end":686},"obj":"Body_part"}],"attributes":[{"id":"A768","pred":"fma_id","subj":"T768","obj":"http://purl.org/sig/ont/fma/fma82737"},{"id":"A769","pred":"fma_id","subj":"T769","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A770","pred":"fma_id","subj":"T770","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A771","pred":"fma_id","subj":"T771","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A772","pred":"fma_id","subj":"T772","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A773","pred":"fma_id","subj":"T773","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A774","pred":"fma_id","subj":"T774","obj":"http://purl.org/sig/ont/fma/fma82816"},{"id":"A775","pred":"fma_id","subj":"T775","obj":"http://purl.org/sig/ont/fma/fma67653"},{"id":"A776","pred":"fma_id","subj":"T776","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A777","pred":"fma_id","subj":"T777","obj":"http://purl.org/sig/ont/fma/fma67264"},{"id":"A778","pred":"fma_id","subj":"T778","obj":"http://purl.org/sig/ont/fma/fma68646"}],"text":"As CLQ interacts with the GM1 sugar part, the N-terminal domain of the S protein loses viral attachment capacity to the cell receptors [166]. The S protein NTD and the CLQ/CLQ-OH maintain the same position during GM1 binding, consequently preventing GM1 binding to the S protein and the drug at the same time, because the NTD and the CLQ/CLQ-OH simultaneously recognize GM1. Asn-167 forms a hydrogen bond with the GalNAc residue, whereas an aromatic Phe-135 stacks to the Glc residue of GM1. Therefore, the antiviral activities of CLQ and CLQ-OH is to block the interaction between the SARS-CoV-2 S glycoprotein and gangliosides on host cell surfaces. The lipid composition of host cell PM can also be a potential target for preventive and therapeutic drugs against such viruses."}

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T326","span":{"begin":156,"end":159},"obj":"Disease"},{"id":"T328","span":{"begin":322,"end":325},"obj":"Disease"},{"id":"T330","span":{"begin":586,"end":594},"obj":"Disease"}],"attributes":[{"id":"A326","pred":"mondo_id","subj":"T326","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A327","pred":"mondo_id","subj":"T326","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"},{"id":"A328","pred":"mondo_id","subj":"T328","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A329","pred":"mondo_id","subj":"T328","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"},{"id":"A330","pred":"mondo_id","subj":"T330","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"As CLQ interacts with the GM1 sugar part, the N-terminal domain of the S protein loses viral attachment capacity to the cell receptors [166]. The S protein NTD and the CLQ/CLQ-OH maintain the same position during GM1 binding, consequently preventing GM1 binding to the S protein and the drug at the same time, because the NTD and the CLQ/CLQ-OH simultaneously recognize GM1. Asn-167 forms a hydrogen bond with the GalNAc residue, whereas an aromatic Phe-135 stacks to the Glc residue of GM1. Therefore, the antiviral activities of CLQ and CLQ-OH is to block the interaction between the SARS-CoV-2 S glycoprotein and gangliosides on host cell surfaces. The lipid composition of host cell PM can also be a potential target for preventive and therapeutic drugs against such viruses."}

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T1110","span":{"begin":120,"end":124},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T1111","span":{"begin":389,"end":390},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T1112","span":{"begin":517,"end":527},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T1113","span":{"begin":637,"end":641},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T1114","span":{"begin":682,"end":686},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T1115","span":{"begin":702,"end":703},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T1116","span":{"begin":771,"end":778},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"}],"text":"As CLQ interacts with the GM1 sugar part, the N-terminal domain of the S protein loses viral attachment capacity to the cell receptors [166]. The S protein NTD and the CLQ/CLQ-OH maintain the same position during GM1 binding, consequently preventing GM1 binding to the S protein and the drug at the same time, because the NTD and the CLQ/CLQ-OH simultaneously recognize GM1. Asn-167 forms a hydrogen bond with the GalNAc residue, whereas an aromatic Phe-135 stacks to the Glc residue of GM1. Therefore, the antiviral activities of CLQ and CLQ-OH is to block the interaction between the SARS-CoV-2 S glycoprotein and gangliosides on host cell surfaces. The lipid composition of host cell PM can also be a potential target for preventive and therapeutic drugs against such viruses."}

LitCovid-PD-CHEBI

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T770","span":{"begin":0,"end":141},"obj":"Sentence"},{"id":"T771","span":{"begin":142,"end":374},"obj":"Sentence"},{"id":"T772","span":{"begin":375,"end":491},"obj":"Sentence"},{"id":"T773","span":{"begin":492,"end":651},"obj":"Sentence"},{"id":"T774","span":{"begin":652,"end":779},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"As CLQ interacts with the GM1 sugar part, the N-terminal domain of the S protein loses viral attachment capacity to the cell receptors [166]. The S protein NTD and the CLQ/CLQ-OH maintain the same position during GM1 binding, consequently preventing GM1 binding to the S protein and the drug at the same time, because the NTD and the CLQ/CLQ-OH simultaneously recognize GM1. Asn-167 forms a hydrogen bond with the GalNAc residue, whereas an aromatic Phe-135 stacks to the Glc residue of GM1. Therefore, the antiviral activities of CLQ and CLQ-OH is to block the interaction between the SARS-CoV-2 S glycoprotein and gangliosides on host cell surfaces. The lipid composition of host cell PM can also be a potential target for preventive and therapeutic drugs against such viruses."}

LitCovid-PD-GlycoEpitope

{"project":"LitCovid-PD-GlycoEpitope","denotations":[{"id":"T22","span":{"begin":26,"end":29},"obj":"GlycoEpitope"},{"id":"T23","span":{"begin":213,"end":216},"obj":"GlycoEpitope"},{"id":"T24","span":{"begin":250,"end":253},"obj":"GlycoEpitope"},{"id":"T25","span":{"begin":370,"end":373},"obj":"GlycoEpitope"},{"id":"T26","span":{"begin":487,"end":490},"obj":"GlycoEpitope"}],"attributes":[{"id":"A22","pred":"glyco_epitope_db_id","subj":"T22","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A23","pred":"glyco_epitope_db_id","subj":"T23","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A24","pred":"glyco_epitope_db_id","subj":"T24","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A25","pred":"glyco_epitope_db_id","subj":"T25","obj":"http://www.glycoepitope.jp/epitopes/EP0050"},{"id":"A26","pred":"glyco_epitope_db_id","subj":"T26","obj":"http://www.glycoepitope.jp/epitopes/EP0050"}],"text":"As CLQ interacts with the GM1 sugar part, the N-terminal domain of the S protein loses viral attachment capacity to the cell receptors [166]. The S protein NTD and the CLQ/CLQ-OH maintain the same position during GM1 binding, consequently preventing GM1 binding to the S protein and the drug at the same time, because the NTD and the CLQ/CLQ-OH simultaneously recognize GM1. Asn-167 forms a hydrogen bond with the GalNAc residue, whereas an aromatic Phe-135 stacks to the Glc residue of GM1. Therefore, the antiviral activities of CLQ and CLQ-OH is to block the interaction between the SARS-CoV-2 S glycoprotein and gangliosides on host cell surfaces. The lipid composition of host cell PM can also be a potential target for preventive and therapeutic drugs against such viruses."}

2_test

{"project":"2_test","denotations":[{"id":"32604730-32293710-51944131","span":{"begin":136,"end":139},"obj":"32293710"},{"id":"T9412","span":{"begin":136,"end":139},"obj":"32293710"}],"text":"As CLQ interacts with the GM1 sugar part, the N-terminal domain of the S protein loses viral attachment capacity to the cell receptors [166]. The S protein NTD and the CLQ/CLQ-OH maintain the same position during GM1 binding, consequently preventing GM1 binding to the S protein and the drug at the same time, because the NTD and the CLQ/CLQ-OH simultaneously recognize GM1. Asn-167 forms a hydrogen bond with the GalNAc residue, whereas an aromatic Phe-135 stacks to the Glc residue of GM1. Therefore, the antiviral activities of CLQ and CLQ-OH is to block the interaction between the SARS-CoV-2 S glycoprotein and gangliosides on host cell surfaces. The lipid composition of host cell PM can also be a potential target for preventive and therapeutic drugs against such viruses."}

PMC:7352545 / 80056-80835 JSONTXT

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PMC:7352545 / 80056-80835 JSON TXT