PMC:7228307 / 33148-33795 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"572","span":{"begin":115,"end":122},"obj":"Gene"},{"id":"573","span":{"begin":163,"end":168},"obj":"Gene"},{"id":"574","span":{"begin":300,"end":307},"obj":"Gene"},{"id":"575","span":{"begin":35,"end":39},"obj":"Gene"},{"id":"576","span":{"begin":386,"end":395},"obj":"Chemical"},{"id":"577","span":{"begin":616,"end":624},"obj":"Chemical"}],"attributes":[{"id":"A572","pred":"tao:has_database_id","subj":"572","obj":"Gene:2213"},{"id":"A573","pred":"tao:has_database_id","subj":"573","obj":"Gene:2214"},{"id":"A574","pred":"tao:has_database_id","subj":"574","obj":"Gene:2212"},{"id":"A575","pred":"tao:has_database_id","subj":"575","obj":"Gene:2213"},{"id":"A576","pred":"tao:has_database_id","subj":"576","obj":"MESH:D006639"},{"id":"A577","pred":"tao:has_database_id","subj":"577","obj":"MESH:D001120"}],"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":"IgG4 and IgG2 have more restricted FcγR specificity. IgG4 has low affinity (KA = ~2 × 105 m –1) for the inhibitory FcγRIIb, but is also a high‐affinity ligand for FcγRI (KA = ~4 × 108 m –1). IgG2 exhibits a highly restricted specificity, showing functional activity with only one polymorphic form of FcγRIIa (binding affinity KA = ~4.5 × 105 m –1) which is permitted by the presence of histidine at position 131 of its IgG‐binding site. This FcγRIIa–H131 form is expressed in approximately 70% of the population, whereas IgG2 has no functional activity on the other common allelic form, FcγRIIa‐R131, which contains arginine at position 131.11, 61"}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T324","span":{"begin":386,"end":395},"obj":"Body_part"},{"id":"T325","span":{"begin":419,"end":422},"obj":"Body_part"},{"id":"T326","span":{"begin":616,"end":624},"obj":"Body_part"}],"attributes":[{"id":"A324","pred":"fma_id","subj":"T324","obj":"http://purl.org/sig/ont/fma/fma82755"},{"id":"A325","pred":"fma_id","subj":"T325","obj":"http://purl.org/sig/ont/fma/fma62872"},{"id":"A326","pred":"fma_id","subj":"T326","obj":"http://purl.org/sig/ont/fma/fma82763"}],"text":"IgG4 and IgG2 have more restricted FcγR specificity. IgG4 has low affinity (KA = ~2 × 105 m –1) for the inhibitory FcγRIIb, but is also a high‐affinity ligand for FcγRI (KA = ~4 × 108 m –1). IgG2 exhibits a highly restricted specificity, showing functional activity with only one polymorphic form of FcγRIIa (binding affinity KA = ~4.5 × 105 m –1) which is permitted by the presence of histidine at position 131 of its IgG‐binding site. This FcγRIIa–H131 form is expressed in approximately 70% of the population, whereas IgG2 has no functional activity on the other common allelic form, FcγRIIa‐R131, which contains arginine at position 131.11, 61"}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T626","span":{"begin":35,"end":37},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T627","span":{"begin":58,"end":61},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T628","span":{"begin":90,"end":94},"obj":"http://purl.obolibrary.org/obo/CLO_0007437"},{"id":"T629","span":{"begin":90,"end":94},"obj":"http://purl.obolibrary.org/obo/CLO_0007448"},{"id":"T630","span":{"begin":90,"end":94},"obj":"http://purl.obolibrary.org/obo/CLO_0007449"},{"id":"T631","span":{"begin":90,"end":94},"obj":"http://purl.obolibrary.org/obo/CLO_0050175"},{"id":"T632","span":{"begin":90,"end":94},"obj":"http://purl.obolibrary.org/obo/CLO_0052399"},{"id":"T633","span":{"begin":115,"end":117},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T634","span":{"begin":136,"end":137},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T635","span":{"begin":163,"end":165},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T636","span":{"begin":184,"end":188},"obj":"http://purl.obolibrary.org/obo/CLO_0007437"},{"id":"T637","span":{"begin":184,"end":188},"obj":"http://purl.obolibrary.org/obo/CLO_0007448"},{"id":"T638","span":{"begin":184,"end":188},"obj":"http://purl.obolibrary.org/obo/CLO_0007449"},{"id":"T639","span":{"begin":184,"end":188},"obj":"http://purl.obolibrary.org/obo/CLO_0050175"},{"id":"T640","span":{"begin":184,"end":188},"obj":"http://purl.obolibrary.org/obo/CLO_0052399"},{"id":"T641","span":{"begin":205,"end":206},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T642","span":{"begin":257,"end":265},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T643","span":{"begin":300,"end":302},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T644","span":{"begin":342,"end":346},"obj":"http://purl.obolibrary.org/obo/CLO_0007437"},{"id":"T645","span":{"begin":342,"end":346},"obj":"http://purl.obolibrary.org/obo/CLO_0007448"},{"id":"T646","span":{"begin":342,"end":346},"obj":"http://purl.obolibrary.org/obo/CLO_0007449"},{"id":"T647","span":{"begin":342,"end":346},"obj":"http://purl.obolibrary.org/obo/CLO_0050175"},{"id":"T648","span":{"begin":342,"end":346},"obj":"http://purl.obolibrary.org/obo/CLO_0052399"},{"id":"T649","span":{"begin":442,"end":444},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T650","span":{"begin":526,"end":529},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T651","span":{"begin":544,"end":552},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T652","span":{"begin":587,"end":589},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"}],"text":"IgG4 and IgG2 have more restricted FcγR specificity. IgG4 has low affinity (KA = ~2 × 105 m –1) for the inhibitory FcγRIIb, but is also a high‐affinity ligand for FcγRI (KA = ~4 × 108 m –1). IgG2 exhibits a highly restricted specificity, showing functional activity with only one polymorphic form of FcγRIIa (binding affinity KA = ~4.5 × 105 m –1) which is permitted by the presence of histidine at position 131 of its IgG‐binding site. This FcγRIIa–H131 form is expressed in approximately 70% of the population, whereas IgG2 has no functional activity on the other common allelic form, FcγRIIa‐R131, which contains arginine at position 131.11, 61"}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T177","span":{"begin":152,"end":158},"obj":"Chemical"},{"id":"T178","span":{"begin":166,"end":168},"obj":"Chemical"},{"id":"T180","span":{"begin":386,"end":395},"obj":"Chemical"},{"id":"T181","span":{"begin":616,"end":624},"obj":"Chemical"}],"attributes":[{"id":"A177","pred":"chebi_id","subj":"T177","obj":"http://purl.obolibrary.org/obo/CHEBI_52214"},{"id":"A178","pred":"chebi_id","subj":"T178","obj":"http://purl.obolibrary.org/obo/CHEBI_73814"},{"id":"A179","pred":"chebi_id","subj":"T178","obj":"http://purl.obolibrary.org/obo/CHEBI_8753"},{"id":"A180","pred":"chebi_id","subj":"T180","obj":"http://purl.obolibrary.org/obo/CHEBI_27570"},{"id":"A181","pred":"chebi_id","subj":"T181","obj":"http://purl.obolibrary.org/obo/CHEBI_16467"},{"id":"A182","pred":"chebi_id","subj":"T181","obj":"http://purl.obolibrary.org/obo/CHEBI_29016"},{"id":"A183","pred":"chebi_id","subj":"T181","obj":"http://purl.obolibrary.org/obo/CHEBI_32696"}],"text":"IgG4 and IgG2 have more restricted FcγR specificity. IgG4 has low affinity (KA = ~2 × 105 m –1) for the inhibitory FcγRIIb, but is also a high‐affinity ligand for FcγRI (KA = ~4 × 108 m –1). IgG2 exhibits a highly restricted specificity, showing functional activity with only one polymorphic form of FcγRIIa (binding affinity KA = ~4.5 × 105 m –1) which is permitted by the presence of histidine at position 131 of its IgG‐binding site. This FcγRIIa–H131 form is expressed in approximately 70% of the population, whereas IgG2 has no functional activity on the other common allelic form, FcγRIIa‐R131, which contains arginine at position 131.11, 61"}

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T193","span":{"begin":246,"end":256},"obj":"http://purl.obolibrary.org/obo/BFO_0000034"},{"id":"T194","span":{"begin":431,"end":435},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T195","span":{"begin":533,"end":543},"obj":"http://purl.obolibrary.org/obo/BFO_0000034"}],"text":"IgG4 and IgG2 have more restricted FcγR specificity. IgG4 has low affinity (KA = ~2 × 105 m –1) for the inhibitory FcγRIIb, but is also a high‐affinity ligand for FcγRI (KA = ~4 × 108 m –1). IgG2 exhibits a highly restricted specificity, showing functional activity with only one polymorphic form of FcγRIIa (binding affinity KA = ~4.5 × 105 m –1) which is permitted by the presence of histidine at position 131 of its IgG‐binding site. This FcγRIIa–H131 form is expressed in approximately 70% of the population, whereas IgG2 has no functional activity on the other common allelic form, FcγRIIa‐R131, which contains arginine at position 131.11, 61"}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T33","span":{"begin":386,"end":395},"obj":"Chemical"},{"id":"T34","span":{"begin":616,"end":624},"obj":"Chemical"}],"attributes":[{"id":"A33","pred":"chebi_id","subj":"T33","obj":"http://purl.obolibrary.org/obo/CHEBI_27570"},{"id":"A34","pred":"chebi_id","subj":"T34","obj":"http://purl.obolibrary.org/obo/CHEBI_32696"},{"id":"A35","pred":"chebi_id","subj":"T34","obj":"http://purl.obolibrary.org/obo/CHEBI_16467"},{"id":"A36","pred":"chebi_id","subj":"T34","obj":"http://purl.obolibrary.org/obo/CHEBI_29016"}],"text":"IgG4 and IgG2 have more restricted FcγR specificity. IgG4 has low affinity (KA = ~2 × 105 m –1) for the inhibitory FcγRIIb, but is also a high‐affinity ligand for FcγRI (KA = ~4 × 108 m –1). IgG2 exhibits a highly restricted specificity, showing functional activity with only one polymorphic form of FcγRIIa (binding affinity KA = ~4.5 × 105 m –1) which is permitted by the presence of histidine at position 131 of its IgG‐binding site. This FcγRIIa–H131 form is expressed in approximately 70% of the population, whereas IgG2 has no functional activity on the other common allelic form, FcγRIIa‐R131, which contains arginine at position 131.11, 61"}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"572","span":{"begin":115,"end":122},"obj":"Gene"},{"id":"573","span":{"begin":163,"end":168},"obj":"Gene"},{"id":"574","span":{"begin":300,"end":307},"obj":"Gene"},{"id":"575","span":{"begin":35,"end":39},"obj":"Gene"},{"id":"576","span":{"begin":386,"end":395},"obj":"Chemical"},{"id":"577","span":{"begin":616,"end":624},"obj":"Chemical"}],"attributes":[{"id":"A572","pred":"pubann:denotes","subj":"572","obj":"Gene:2213"},{"id":"A573","pred":"pubann:denotes","subj":"573","obj":"Gene:2214"},{"id":"A574","pred":"pubann:denotes","subj":"574","obj":"Gene:2212"},{"id":"A575","pred":"pubann:denotes","subj":"575","obj":"Gene:2213"},{"id":"A576","pred":"pubann:denotes","subj":"576","obj":"MESH:D006639"},{"id":"A577","pred":"pubann:denotes","subj":"577","obj":"MESH:D001120"}],"text":"IgG4 and IgG2 have more restricted FcγR specificity. IgG4 has low affinity (KA = ~2 × 105 m –1) for the inhibitory FcγRIIb, but is also a high‐affinity ligand for FcγRI (KA = ~4 × 108 m –1). IgG2 exhibits a highly restricted specificity, showing functional activity with only one polymorphic form of FcγRIIa (binding affinity KA = ~4.5 × 105 m –1) which is permitted by the presence of histidine at position 131 of its IgG‐binding site. This FcγRIIa–H131 form is expressed in approximately 70% of the population, whereas IgG2 has no functional activity on the other common allelic form, FcγRIIa‐R131, which contains arginine at position 131.11, 61"}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T187","span":{"begin":0,"end":52},"obj":"Sentence"},{"id":"T188","span":{"begin":53,"end":190},"obj":"Sentence"},{"id":"T189","span":{"begin":191,"end":436},"obj":"Sentence"},{"id":"T190","span":{"begin":437,"end":647},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"IgG4 and IgG2 have more restricted FcγR specificity. IgG4 has low affinity (KA = ~2 × 105 m –1) for the inhibitory FcγRIIb, but is also a high‐affinity ligand for FcγRI (KA = ~4 × 108 m –1). IgG2 exhibits a highly restricted specificity, showing functional activity with only one polymorphic form of FcγRIIa (binding affinity KA = ~4.5 × 105 m –1) which is permitted by the presence of histidine at position 131 of its IgG‐binding site. This FcγRIIa–H131 form is expressed in approximately 70% of the population, whereas IgG2 has no functional activity on the other common allelic form, FcγRIIa‐R131, which contains arginine at position 131.11, 61"}

{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T366","span":{"begin":76,"end":83},"obj":"Protein"}],"attributes":[{"id":"A366","pred":"uniprot_id","subj":"T366","obj":"https://www.uniprot.org/uniprot/Q8WWG8"},{"id":"A367","pred":"uniprot_id","subj":"T366","obj":"https://www.uniprot.org/uniprot/Q63273"},{"id":"A368","pred":"uniprot_id","subj":"T366","obj":"https://www.uniprot.org/uniprot/Q62643"},{"id":"A369","pred":"uniprot_id","subj":"T366","obj":"https://www.uniprot.org/uniprot/Q61626"},{"id":"A370","pred":"uniprot_id","subj":"T366","obj":"https://www.uniprot.org/uniprot/Q16478"},{"id":"A371","pred":"uniprot_id","subj":"T366","obj":"https://www.uniprot.org/uniprot/G5E822"}],"text":"IgG4 and IgG2 have more restricted FcγR specificity. IgG4 has low affinity (KA = ~2 × 105 m –1) for the inhibitory FcγRIIb, but is also a high‐affinity ligand for FcγRI (KA = ~4 × 108 m –1). IgG2 exhibits a highly restricted specificity, showing functional activity with only one polymorphic form of FcγRIIa (binding affinity KA = ~4.5 × 105 m –1) which is permitted by the presence of histidine at position 131 of its IgG‐binding site. This FcγRIIa–H131 form is expressed in approximately 70% of the population, whereas IgG2 has no functional activity on the other common allelic form, FcγRIIa‐R131, which contains arginine at position 131.11, 61"}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T323","span":{"begin":386,"end":395},"obj":"Body_part"},{"id":"T324","span":{"begin":419,"end":422},"obj":"Body_part"},{"id":"T325","span":{"begin":616,"end":624},"obj":"Body_part"}],"attributes":[{"id":"A323","pred":"fma_id","subj":"T323","obj":"http://purl.org/sig/ont/fma/fma82755"},{"id":"A324","pred":"fma_id","subj":"T324","obj":"http://purl.org/sig/ont/fma/fma62872"},{"id":"A325","pred":"fma_id","subj":"T325","obj":"http://purl.org/sig/ont/fma/fma82763"}],"text":"IgG4 and IgG2 have more restricted FcγR specificity. IgG4 has low affinity (KA = ~2 × 105 m –1) for the inhibitory FcγRIIb, but is also a high‐affinity ligand for FcγRI (KA = ~4 × 108 m –1). IgG2 exhibits a highly restricted specificity, showing functional activity with only one polymorphic form of FcγRIIa (binding affinity KA = ~4.5 × 105 m –1) which is permitted by the presence of histidine at position 131 of its IgG‐binding site. This FcγRIIa–H131 form is expressed in approximately 70% of the population, whereas IgG2 has no functional activity on the other common allelic form, FcγRIIa‐R131, which contains arginine at position 131.11, 61"}

{"project":"LitCovid-sentences","denotations":[{"id":"T187","span":{"begin":0,"end":52},"obj":"Sentence"},{"id":"T188","span":{"begin":53,"end":190},"obj":"Sentence"},{"id":"T189","span":{"begin":191,"end":436},"obj":"Sentence"},{"id":"T190","span":{"begin":437,"end":647},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"IgG4 and IgG2 have more restricted FcγR specificity. IgG4 has low affinity (KA = ~2 × 105 m –1) for the inhibitory FcγRIIb, but is also a high‐affinity ligand for FcγRI (KA = ~4 × 108 m –1). IgG2 exhibits a highly restricted specificity, showing functional activity with only one polymorphic form of FcγRIIa (binding affinity KA = ~4.5 × 105 m –1) which is permitted by the presence of histidine at position 131 of its IgG‐binding site. This FcγRIIa–H131 form is expressed in approximately 70% of the population, whereas IgG2 has no functional activity on the other common allelic form, FcγRIIa‐R131, which contains arginine at position 131.11, 61"}