PMC:7228307 / 52503-53104 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"1063","span":{"begin":267,"end":272},"obj":"Gene"},{"id":"1064","span":{"begin":584,"end":587},"obj":"Gene"},{"id":"1065","span":{"begin":531,"end":535},"obj":"Gene"},{"id":"1066","span":{"begin":135,"end":139},"obj":"Gene"},{"id":"1067","span":{"begin":494,"end":498},"obj":"Gene"},{"id":"1068","span":{"begin":74,"end":78},"obj":"Gene"},{"id":"1069","span":{"begin":250,"end":260},"obj":"Chemical"},{"id":"1070","span":{"begin":278,"end":289},"obj":"Chemical"},{"id":"1071","span":{"begin":376,"end":381},"obj":"Mutation"},{"id":"1072","span":{"begin":415,"end":420},"obj":"Mutation"},{"id":"1073","span":{"begin":444,"end":449},"obj":"Mutation"}],"attributes":[{"id":"A1063","pred":"tao:has_database_id","subj":"1063","obj":"Gene:29126"},{"id":"A1064","pred":"tao:has_database_id","subj":"1064","obj":"Gene:712"},{"id":"A1065","pred":"tao:has_database_id","subj":"1065","obj":"Gene:2213"},{"id":"A1066","pred":"tao:has_database_id","subj":"1066","obj":"Gene:2213"},{"id":"A1067","pred":"tao:has_database_id","subj":"1067","obj":"Gene:2213"},{"id":"A1068","pred":"tao:has_database_id","subj":"1068","obj":"Gene:2213"},{"id":"A1069","pred":"tao:has_database_id","subj":"1069","obj":"MESH:C000613593"},{"id":"A1070","pred":"tao:has_database_id","subj":"1070","obj":"MESH:C582345"},{"id":"A1071","pred":"tao:has_standard_notation","subj":"1071","obj":"p.L234F"},{"id":"A1072","pred":"tao:has_standard_notation","subj":"1072","obj":"p.L235E"},{"id":"A1073","pred":"tao:has_standard_notation","subj":"1073","obj":"p.P331S"}],"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":"A separate strategy has used combinations of amino acid residues from the FcγR‐binding regions of IgG2 and IgG4, which have restricted FcγR specificity, together with other binding‐inactivating mutations. The lower hinge amino acids of the IgG1 mAbs durvalumab (anti‐PD‐L1) and anifrolumab (anti‐interferon‐α receptor; Table 4) were modified to mimic the lower hinge of IgG4 (L234F). They additionally incorporated L235E in the lower hinge and P331S in the F/G loop of the CH2 domain to ablate FcγR binding by disrupting two major FcγR contact sites7 and also coincidently decreasing C1q activation.16"}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T407","span":{"begin":45,"end":55},"obj":"Body_part"},{"id":"T408","span":{"begin":221,"end":232},"obj":"Body_part"}],"attributes":[{"id":"A407","pred":"fma_id","subj":"T407","obj":"http://purl.org/sig/ont/fma/fma82739"},{"id":"A408","pred":"fma_id","subj":"T408","obj":"http://purl.org/sig/ont/fma/fma82739"}],"text":"A separate strategy has used combinations of amino acid residues from the FcγR‐binding regions of IgG2 and IgG4, which have restricted FcγR specificity, together with other binding‐inactivating mutations. The lower hinge amino acids of the IgG1 mAbs durvalumab (anti‐PD‐L1) and anifrolumab (anti‐interferon‐α receptor; Table 4) were modified to mimic the lower hinge of IgG4 (L234F). They additionally incorporated L235E in the lower hinge and P331S in the F/G loop of the CH2 domain to ablate FcγR binding by disrupting two major FcγR contact sites7 and also coincidently decreasing C1q activation.16"}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T886","span":{"begin":0,"end":1},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T887","span":{"begin":20,"end":23},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T888","span":{"begin":45,"end":64},"obj":"http://purl.obolibrary.org/obo/CHEBI_33708"},{"id":"T889","span":{"begin":45,"end":64},"obj":"http://purl.obolibrary.org/obo/PR_000036907"},{"id":"T890","span":{"begin":74,"end":76},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T891","span":{"begin":135,"end":137},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T892","span":{"begin":267,"end":272},"obj":"http://purl.obolibrary.org/obo/CLO_0008407"},{"id":"T893","span":{"begin":494,"end":496},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T894","span":{"begin":531,"end":533},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T895","span":{"begin":588,"end":598},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"}],"text":"A separate strategy has used combinations of amino acid residues from the FcγR‐binding regions of IgG2 and IgG4, which have restricted FcγR specificity, together with other binding‐inactivating mutations. The lower hinge amino acids of the IgG1 mAbs durvalumab (anti‐PD‐L1) and anifrolumab (anti‐interferon‐α receptor; Table 4) were modified to mimic the lower hinge of IgG4 (L234F). They additionally incorporated L235E in the lower hinge and P331S in the F/G loop of the CH2 domain to ablate FcγR binding by disrupting two major FcγR contact sites7 and also coincidently decreasing C1q activation.16"}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T5000","span":{"begin":45,"end":55},"obj":"Chemical"},{"id":"T20266","span":{"begin":45,"end":50},"obj":"Chemical"},{"id":"T44260","span":{"begin":51,"end":55},"obj":"Chemical"},{"id":"T10443","span":{"begin":221,"end":232},"obj":"Chemical"},{"id":"T57589","span":{"begin":221,"end":226},"obj":"Chemical"},{"id":"T8912","span":{"begin":227,"end":232},"obj":"Chemical"},{"id":"T75315","span":{"begin":267,"end":269},"obj":"Chemical"},{"id":"T36188","span":{"begin":296,"end":306},"obj":"Chemical"}],"attributes":[{"id":"A35475","pred":"chebi_id","subj":"T5000","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"},{"id":"A44131","pred":"chebi_id","subj":"T20266","obj":"http://purl.obolibrary.org/obo/CHEBI_46882"},{"id":"A68370","pred":"chebi_id","subj":"T44260","obj":"http://purl.obolibrary.org/obo/CHEBI_37527"},{"id":"A72620","pred":"chebi_id","subj":"T10443","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"},{"id":"A36706","pred":"chebi_id","subj":"T57589","obj":"http://purl.obolibrary.org/obo/CHEBI_46882"},{"id":"A23112","pred":"chebi_id","subj":"T8912","obj":"http://purl.obolibrary.org/obo/CHEBI_37527"},{"id":"A81916","pred":"chebi_id","subj":"T75315","obj":"http://purl.obolibrary.org/obo/CHEBI_74756"},{"id":"A4305","pred":"chebi_id","subj":"T36188","obj":"http://purl.obolibrary.org/obo/CHEBI_52999"}],"text":"A separate strategy has used combinations of amino acid residues from the FcγR‐binding regions of IgG2 and IgG4, which have restricted FcγR specificity, together with other binding‐inactivating mutations. The lower hinge amino acids of the IgG1 mAbs durvalumab (anti‐PD‐L1) and anifrolumab (anti‐interferon‐α receptor; Table 4) were modified to mimic the lower hinge of IgG4 (L234F). They additionally incorporated L235E in the lower hinge and P331S in the F/G loop of the CH2 domain to ablate FcγR binding by disrupting two major FcγR contact sites7 and also coincidently decreasing C1q activation.16"}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T57","span":{"begin":45,"end":55},"obj":"Chemical"},{"id":"T58","span":{"begin":221,"end":232},"obj":"Chemical"}],"attributes":[{"id":"A57","pred":"chebi_id","subj":"T57","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"},{"id":"A58","pred":"chebi_id","subj":"T58","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"}],"text":"A separate strategy has used combinations of amino acid residues from the FcγR‐binding regions of IgG2 and IgG4, which have restricted FcγR specificity, together with other binding‐inactivating mutations. The lower hinge amino acids of the IgG1 mAbs durvalumab (anti‐PD‐L1) and anifrolumab (anti‐interferon‐α receptor; Table 4) were modified to mimic the lower hinge of IgG4 (L234F). They additionally incorporated L235E in the lower hinge and P331S in the F/G loop of the CH2 domain to ablate FcγR binding by disrupting two major FcγR contact sites7 and also coincidently decreasing C1q activation.16"}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"1063","span":{"begin":267,"end":272},"obj":"Gene"},{"id":"1064","span":{"begin":584,"end":587},"obj":"Gene"},{"id":"1065","span":{"begin":531,"end":535},"obj":"Gene"},{"id":"1066","span":{"begin":135,"end":139},"obj":"Gene"},{"id":"1067","span":{"begin":494,"end":498},"obj":"Gene"},{"id":"1068","span":{"begin":74,"end":78},"obj":"Gene"},{"id":"1069","span":{"begin":250,"end":260},"obj":"Chemical"},{"id":"1070","span":{"begin":278,"end":289},"obj":"Chemical"},{"id":"1071","span":{"begin":376,"end":381},"obj":"Mutation"},{"id":"1072","span":{"begin":415,"end":420},"obj":"Mutation"},{"id":"1073","span":{"begin":444,"end":449},"obj":"Mutation"}],"attributes":[{"id":"A1072","pred":"pubann:has_HGVS_notation","subj":"1072","obj":"p.L235E"},{"id":"A1070","pred":"pubann:denotes","subj":"1070","obj":"MESH:C582345"},{"id":"A1068","pred":"pubann:denotes","subj":"1068","obj":"Gene:2213"},{"id":"A1064","pred":"pubann:denotes","subj":"1064","obj":"Gene:712"},{"id":"A1066","pred":"pubann:denotes","subj":"1066","obj":"Gene:2213"},{"id":"A1073","pred":"pubann:has_HGVS_notation","subj":"1073","obj":"p.P331S"},{"id":"A1071","pred":"pubann:has_HGVS_notation","subj":"1071","obj":"p.L234F"},{"id":"A1063","pred":"pubann:denotes","subj":"1063","obj":"Gene:29126"},{"id":"A1065","pred":"pubann:denotes","subj":"1065","obj":"Gene:2213"},{"id":"A1069","pred":"pubann:denotes","subj":"1069","obj":"MESH:C000613593"},{"id":"A1067","pred":"pubann:denotes","subj":"1067","obj":"Gene:2213"}],"text":"A separate strategy has used combinations of amino acid residues from the FcγR‐binding regions of IgG2 and IgG4, which have restricted FcγR specificity, together with other binding‐inactivating mutations. The lower hinge amino acids of the IgG1 mAbs durvalumab (anti‐PD‐L1) and anifrolumab (anti‐interferon‐α receptor; Table 4) were modified to mimic the lower hinge of IgG4 (L234F). They additionally incorporated L235E in the lower hinge and P331S in the F/G loop of the CH2 domain to ablate FcγR binding by disrupting two major FcγR contact sites7 and also coincidently decreasing C1q activation.16"}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T299","span":{"begin":0,"end":204},"obj":"Sentence"},{"id":"T300","span":{"begin":205,"end":383},"obj":"Sentence"},{"id":"T301","span":{"begin":384,"end":601},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"A separate strategy has used combinations of amino acid residues from the FcγR‐binding regions of IgG2 and IgG4, which have restricted FcγR specificity, together with other binding‐inactivating mutations. The lower hinge amino acids of the IgG1 mAbs durvalumab (anti‐PD‐L1) and anifrolumab (anti‐interferon‐α receptor; Table 4) were modified to mimic the lower hinge of IgG4 (L234F). They additionally incorporated L235E in the lower hinge and P331S in the F/G loop of the CH2 domain to ablate FcγR binding by disrupting two major FcγR contact sites7 and also coincidently decreasing C1q activation.16"}

{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T704","span":{"begin":267,"end":272},"obj":"Protein"},{"id":"T713","span":{"begin":296,"end":306},"obj":"Protein"}],"attributes":[{"id":"A704","pred":"uniprot_id","subj":"T704","obj":"https://www.uniprot.org/uniprot/Q9NZQ7"},{"id":"A705","pred":"uniprot_id","subj":"T704","obj":"https://www.uniprot.org/uniprot/Q9NUZ5"},{"id":"A706","pred":"uniprot_id","subj":"T704","obj":"https://www.uniprot.org/uniprot/Q9EP73"},{"id":"A707","pred":"uniprot_id","subj":"T704","obj":"https://www.uniprot.org/uniprot/Q6WEX4"},{"id":"A708","pred":"uniprot_id","subj":"T704","obj":"https://www.uniprot.org/uniprot/Q66RK1"},{"id":"A709","pred":"uniprot_id","subj":"T704","obj":"https://www.uniprot.org/uniprot/Q2V8D5"},{"id":"A710","pred":"uniprot_id","subj":"T704","obj":"https://www.uniprot.org/uniprot/Q14CJ2"},{"id":"A711","pred":"uniprot_id","subj":"T704","obj":"https://www.uniprot.org/uniprot/B4DU27"},{"id":"A712","pred":"uniprot_id","subj":"T704","obj":"https://www.uniprot.org/uniprot/B2RBA2"},{"id":"A713","pred":"uniprot_id","subj":"T713","obj":"https://www.uniprot.org/uniprot/P51527"},{"id":"A714","pred":"uniprot_id","subj":"T713","obj":"https://www.uniprot.org/uniprot/P51526"}],"text":"A separate strategy has used combinations of amino acid residues from the FcγR‐binding regions of IgG2 and IgG4, which have restricted FcγR specificity, together with other binding‐inactivating mutations. The lower hinge amino acids of the IgG1 mAbs durvalumab (anti‐PD‐L1) and anifrolumab (anti‐interferon‐α receptor; Table 4) were modified to mimic the lower hinge of IgG4 (L234F). They additionally incorporated L235E in the lower hinge and P331S in the F/G loop of the CH2 domain to ablate FcγR binding by disrupting two major FcγR contact sites7 and also coincidently decreasing C1q activation.16"}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T406","span":{"begin":45,"end":55},"obj":"Body_part"},{"id":"T407","span":{"begin":221,"end":232},"obj":"Body_part"}],"attributes":[{"id":"A407","pred":"fma_id","subj":"T407","obj":"http://purl.org/sig/ont/fma/fma82739"},{"id":"A406","pred":"fma_id","subj":"T406","obj":"http://purl.org/sig/ont/fma/fma82739"}],"text":"A separate strategy has used combinations of amino acid residues from the FcγR‐binding regions of IgG2 and IgG4, which have restricted FcγR specificity, together with other binding‐inactivating mutations. The lower hinge amino acids of the IgG1 mAbs durvalumab (anti‐PD‐L1) and anifrolumab (anti‐interferon‐α receptor; Table 4) were modified to mimic the lower hinge of IgG4 (L234F). They additionally incorporated L235E in the lower hinge and P331S in the F/G loop of the CH2 domain to ablate FcγR binding by disrupting two major FcγR contact sites7 and also coincidently decreasing C1q activation.16"}

{"project":"LitCovid-sentences","denotations":[{"id":"T299","span":{"begin":0,"end":204},"obj":"Sentence"},{"id":"T300","span":{"begin":205,"end":383},"obj":"Sentence"},{"id":"T301","span":{"begin":384,"end":601},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"A separate strategy has used combinations of amino acid residues from the FcγR‐binding regions of IgG2 and IgG4, which have restricted FcγR specificity, together with other binding‐inactivating mutations. The lower hinge amino acids of the IgG1 mAbs durvalumab (anti‐PD‐L1) and anifrolumab (anti‐interferon‐α receptor; Table 4) were modified to mimic the lower hinge of IgG4 (L234F). They additionally incorporated L235E in the lower hinge and P331S in the F/G loop of the CH2 domain to ablate FcγR binding by disrupting two major FcγR contact sites7 and also coincidently decreasing C1q activation.16"}