PMC:7352545 / 67655-69051 JSON TXT

Annnotations TAB JSON ListView MergeView

LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T647","span":{"begin":13,"end":17},"obj":"Body_part"},{"id":"T648","span":{"begin":58,"end":70},"obj":"Body_part"},{"id":"T649","span":{"begin":214,"end":227},"obj":"Body_part"},{"id":"T650","span":{"begin":294,"end":307},"obj":"Body_part"},{"id":"T651","span":{"begin":353,"end":365},"obj":"Body_part"},{"id":"T652","span":{"begin":442,"end":454},"obj":"Body_part"},{"id":"T653","span":{"begin":588,"end":599},"obj":"Body_part"},{"id":"T654","span":{"begin":717,"end":722},"obj":"Body_part"},{"id":"T655","span":{"begin":929,"end":941},"obj":"Body_part"},{"id":"T656","span":{"begin":1129,"end":1141},"obj":"Body_part"},{"id":"T657","span":{"begin":1235,"end":1248},"obj":"Body_part"}],"attributes":[{"id":"A647","pred":"fma_id","subj":"T647","obj":"http://purl.org/sig/ont/fma/fma9712"},{"id":"A648","pred":"fma_id","subj":"T648","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A649","pred":"fma_id","subj":"T649","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A650","pred":"fma_id","subj":"T650","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A651","pred":"fma_id","subj":"T651","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A652","pred":"fma_id","subj":"T652","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A653","pred":"fma_id","subj":"T653","obj":"http://purl.org/sig/ont/fma/fma62845"},{"id":"A654","pred":"fma_id","subj":"T654","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A655","pred":"fma_id","subj":"T655","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A656","pred":"fma_id","subj":"T656","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A657","pred":"fma_id","subj":"T657","obj":"http://purl.org/sig/ont/fma/fma62925"}],"text":"On the other hand, from the aspect of virus ligand, the S glycoprotein decorates viral surfaces and is, therefore, the target for vaccination design. Virus internalization requires potential glycosylation of viral glycoproteins. Among the three viral envelope components, S and M are the major glycoproteins and E is nascent and not glycosylated. The M glycoprotein consists of a short glycosylated ectodomain in the N-terminal region. The S glycoprotein expressed in hemagglutinating encephalomyelitis virus is an HA that recognizes N-acetyl-9-O-NeuAc as a binding receptor expressed on erythrocyte surfaces [134]. For example, BCoVs attach to the surface receptor of N-acetyl-9-O-NeuAc (9-O-acetylated SAs) on host cells. TGEV and PEDV are currently known as a similar class of such CoVs. PEDV infects multiple hosts including bat, pig, human and monkey, where bats are considered to be the evolutionary origin for PEDV. The S glycoprotein of SARS-CoV-2 utilizes different glycosylation patterns to recognize its receptors. The glycosylation sites in minimal RBD exhibits similar sites to other CoVs. The trimeric SARS-CoV-2 S glycoprotein is also highly glycosylated with 66 N-glycans, but a few O-glycans [135]. Glycosylation of S glycoproteins leads to immune evasion. In the MERS-CoV and the bat-specific CoV-HKU4, glycosylation is linked to zoonotic infection for fusion-based entry [136]."}

LitCovid-PD-UBERON

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T35","span":{"begin":13,"end":17},"obj":"Body_part"}],"attributes":[{"id":"A35","pred":"uberon_id","subj":"T35","obj":"http://purl.obolibrary.org/obo/UBERON_0002398"}],"text":"On the other hand, from the aspect of virus ligand, the S glycoprotein decorates viral surfaces and is, therefore, the target for vaccination design. Virus internalization requires potential glycosylation of viral glycoproteins. Among the three viral envelope components, S and M are the major glycoproteins and E is nascent and not glycosylated. The M glycoprotein consists of a short glycosylated ectodomain in the N-terminal region. The S glycoprotein expressed in hemagglutinating encephalomyelitis virus is an HA that recognizes N-acetyl-9-O-NeuAc as a binding receptor expressed on erythrocyte surfaces [134]. For example, BCoVs attach to the surface receptor of N-acetyl-9-O-NeuAc (9-O-acetylated SAs) on host cells. TGEV and PEDV are currently known as a similar class of such CoVs. PEDV infects multiple hosts including bat, pig, human and monkey, where bats are considered to be the evolutionary origin for PEDV. The S glycoprotein of SARS-CoV-2 utilizes different glycosylation patterns to recognize its receptors. The glycosylation sites in minimal RBD exhibits similar sites to other CoVs. The trimeric SARS-CoV-2 S glycoprotein is also highly glycosylated with 66 N-glycans, but a few O-glycans [135]. Glycosylation of S glycoproteins leads to immune evasion. In the MERS-CoV and the bat-specific CoV-HKU4, glycosylation is linked to zoonotic infection for fusion-based entry [136]."}

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T258","span":{"begin":485,"end":502},"obj":"Disease"},{"id":"T259","span":{"begin":945,"end":953},"obj":"Disease"},{"id":"T260","span":{"begin":1116,"end":1124},"obj":"Disease"},{"id":"T261","span":{"begin":1348,"end":1366},"obj":"Disease"},{"id":"T262","span":{"begin":1357,"end":1366},"obj":"Disease"}],"attributes":[{"id":"A258","pred":"mondo_id","subj":"T258","obj":"http://purl.obolibrary.org/obo/MONDO_0005156"},{"id":"A259","pred":"mondo_id","subj":"T259","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A260","pred":"mondo_id","subj":"T260","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A261","pred":"mondo_id","subj":"T261","obj":"http://purl.obolibrary.org/obo/MONDO_0025481"},{"id":"A262","pred":"mondo_id","subj":"T262","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"}],"text":"On the other hand, from the aspect of virus ligand, the S glycoprotein decorates viral surfaces and is, therefore, the target for vaccination design. Virus internalization requires potential glycosylation of viral glycoproteins. Among the three viral envelope components, S and M are the major glycoproteins and E is nascent and not glycosylated. The M glycoprotein consists of a short glycosylated ectodomain in the N-terminal region. The S glycoprotein expressed in hemagglutinating encephalomyelitis virus is an HA that recognizes N-acetyl-9-O-NeuAc as a binding receptor expressed on erythrocyte surfaces [134]. For example, BCoVs attach to the surface receptor of N-acetyl-9-O-NeuAc (9-O-acetylated SAs) on host cells. TGEV and PEDV are currently known as a similar class of such CoVs. PEDV infects multiple hosts including bat, pig, human and monkey, where bats are considered to be the evolutionary origin for PEDV. The S glycoprotein of SARS-CoV-2 utilizes different glycosylation patterns to recognize its receptors. The glycosylation sites in minimal RBD exhibits similar sites to other CoVs. The trimeric SARS-CoV-2 S glycoprotein is also highly glycosylated with 66 N-glycans, but a few O-glycans [135]. Glycosylation of S glycoproteins leads to immune evasion. In the MERS-CoV and the bat-specific CoV-HKU4, glycosylation is linked to zoonotic infection for fusion-based entry [136]."}

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T970","span":{"begin":38,"end":43},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T971","span":{"begin":150,"end":155},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T972","span":{"begin":378,"end":379},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T973","span":{"begin":503,"end":508},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T974","span":{"begin":556,"end":557},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T975","span":{"begin":588,"end":599},"obj":"http://purl.obolibrary.org/obo/CL_0000232"},{"id":"T976","span":{"begin":704,"end":707},"obj":"http://purl.obolibrary.org/obo/CLO_0051568"},{"id":"T977","span":{"begin":717,"end":722},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T978","span":{"begin":761,"end":762},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T979","span":{"begin":829,"end":832},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9397"},{"id":"T980","span":{"begin":839,"end":844},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T981","span":{"begin":849,"end":855},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9479"},{"id":"T982","span":{"begin":863,"end":867},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9397"},{"id":"T983","span":{"begin":1193,"end":1194},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T984","span":{"begin":1298,"end":1301},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9397"}],"text":"On the other hand, from the aspect of virus ligand, the S glycoprotein decorates viral surfaces and is, therefore, the target for vaccination design. Virus internalization requires potential glycosylation of viral glycoproteins. Among the three viral envelope components, S and M are the major glycoproteins and E is nascent and not glycosylated. The M glycoprotein consists of a short glycosylated ectodomain in the N-terminal region. The S glycoprotein expressed in hemagglutinating encephalomyelitis virus is an HA that recognizes N-acetyl-9-O-NeuAc as a binding receptor expressed on erythrocyte surfaces [134]. For example, BCoVs attach to the surface receptor of N-acetyl-9-O-NeuAc (9-O-acetylated SAs) on host cells. TGEV and PEDV are currently known as a similar class of such CoVs. PEDV infects multiple hosts including bat, pig, human and monkey, where bats are considered to be the evolutionary origin for PEDV. The S glycoprotein of SARS-CoV-2 utilizes different glycosylation patterns to recognize its receptors. The glycosylation sites in minimal RBD exhibits similar sites to other CoVs. The trimeric SARS-CoV-2 S glycoprotein is also highly glycosylated with 66 N-glycans, but a few O-glycans [135]. Glycosylation of S glycoproteins leads to immune evasion. In the MERS-CoV and the bat-specific CoV-HKU4, glycosylation is linked to zoonotic infection for fusion-based entry [136]."}

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T122","span":{"begin":191,"end":204},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T123","span":{"begin":975,"end":988},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T124","span":{"begin":1030,"end":1043},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T125","span":{"begin":1216,"end":1229},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T126","span":{"begin":1258,"end":1272},"obj":"http://purl.obolibrary.org/obo/GO_0042783"},{"id":"T127","span":{"begin":1321,"end":1334},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"On the other hand, from the aspect of virus ligand, the S glycoprotein decorates viral surfaces and is, therefore, the target for vaccination design. Virus internalization requires potential glycosylation of viral glycoproteins. Among the three viral envelope components, S and M are the major glycoproteins and E is nascent and not glycosylated. The M glycoprotein consists of a short glycosylated ectodomain in the N-terminal region. The S glycoprotein expressed in hemagglutinating encephalomyelitis virus is an HA that recognizes N-acetyl-9-O-NeuAc as a binding receptor expressed on erythrocyte surfaces [134]. For example, BCoVs attach to the surface receptor of N-acetyl-9-O-NeuAc (9-O-acetylated SAs) on host cells. TGEV and PEDV are currently known as a similar class of such CoVs. PEDV infects multiple hosts including bat, pig, human and monkey, where bats are considered to be the evolutionary origin for PEDV. The S glycoprotein of SARS-CoV-2 utilizes different glycosylation patterns to recognize its receptors. The glycosylation sites in minimal RBD exhibits similar sites to other CoVs. The trimeric SARS-CoV-2 S glycoprotein is also highly glycosylated with 66 N-glycans, but a few O-glycans [135]. Glycosylation of S glycoproteins leads to immune evasion. In the MERS-CoV and the bat-specific CoV-HKU4, glycosylation is linked to zoonotic infection for fusion-based entry [136]."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T654","span":{"begin":0,"end":149},"obj":"Sentence"},{"id":"T655","span":{"begin":150,"end":228},"obj":"Sentence"},{"id":"T656","span":{"begin":229,"end":346},"obj":"Sentence"},{"id":"T657","span":{"begin":347,"end":435},"obj":"Sentence"},{"id":"T658","span":{"begin":436,"end":615},"obj":"Sentence"},{"id":"T659","span":{"begin":616,"end":723},"obj":"Sentence"},{"id":"T660","span":{"begin":724,"end":790},"obj":"Sentence"},{"id":"T661","span":{"begin":791,"end":922},"obj":"Sentence"},{"id":"T662","span":{"begin":923,"end":1025},"obj":"Sentence"},{"id":"T663","span":{"begin":1026,"end":1102},"obj":"Sentence"},{"id":"T664","span":{"begin":1103,"end":1215},"obj":"Sentence"},{"id":"T665","span":{"begin":1216,"end":1273},"obj":"Sentence"},{"id":"T666","span":{"begin":1274,"end":1396},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"On the other hand, from the aspect of virus ligand, the S glycoprotein decorates viral surfaces and is, therefore, the target for vaccination design. Virus internalization requires potential glycosylation of viral glycoproteins. Among the three viral envelope components, S and M are the major glycoproteins and E is nascent and not glycosylated. The M glycoprotein consists of a short glycosylated ectodomain in the N-terminal region. The S glycoprotein expressed in hemagglutinating encephalomyelitis virus is an HA that recognizes N-acetyl-9-O-NeuAc as a binding receptor expressed on erythrocyte surfaces [134]. For example, BCoVs attach to the surface receptor of N-acetyl-9-O-NeuAc (9-O-acetylated SAs) on host cells. TGEV and PEDV are currently known as a similar class of such CoVs. PEDV infects multiple hosts including bat, pig, human and monkey, where bats are considered to be the evolutionary origin for PEDV. The S glycoprotein of SARS-CoV-2 utilizes different glycosylation patterns to recognize its receptors. The glycosylation sites in minimal RBD exhibits similar sites to other CoVs. The trimeric SARS-CoV-2 S glycoprotein is also highly glycosylated with 66 N-glycans, but a few O-glycans [135]. Glycosylation of S glycoproteins leads to immune evasion. In the MERS-CoV and the bat-specific CoV-HKU4, glycosylation is linked to zoonotic infection for fusion-based entry [136]."}

2_test

{"project":"2_test","denotations":[{"id":"32604730-32366695-51944101","span":{"begin":1210,"end":1213},"obj":"32366695"},{"id":"32604730-26063432-51944102","span":{"begin":1391,"end":1394},"obj":"26063432"},{"id":"T49065","span":{"begin":1210,"end":1213},"obj":"32366695"},{"id":"T76870","span":{"begin":1391,"end":1394},"obj":"26063432"}],"text":"On the other hand, from the aspect of virus ligand, the S glycoprotein decorates viral surfaces and is, therefore, the target for vaccination design. Virus internalization requires potential glycosylation of viral glycoproteins. Among the three viral envelope components, S and M are the major glycoproteins and E is nascent and not glycosylated. The M glycoprotein consists of a short glycosylated ectodomain in the N-terminal region. The S glycoprotein expressed in hemagglutinating encephalomyelitis virus is an HA that recognizes N-acetyl-9-O-NeuAc as a binding receptor expressed on erythrocyte surfaces [134]. For example, BCoVs attach to the surface receptor of N-acetyl-9-O-NeuAc (9-O-acetylated SAs) on host cells. TGEV and PEDV are currently known as a similar class of such CoVs. PEDV infects multiple hosts including bat, pig, human and monkey, where bats are considered to be the evolutionary origin for PEDV. The S glycoprotein of SARS-CoV-2 utilizes different glycosylation patterns to recognize its receptors. The glycosylation sites in minimal RBD exhibits similar sites to other CoVs. The trimeric SARS-CoV-2 S glycoprotein is also highly glycosylated with 66 N-glycans, but a few O-glycans [135]. Glycosylation of S glycoproteins leads to immune evasion. In the MERS-CoV and the bat-specific CoV-HKU4, glycosylation is linked to zoonotic infection for fusion-based entry [136]."}

PMC:7352545 / 67655-69051 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:7352545 / 67655-69051 JSON TXT