PMC:7228307 / 36129-36757 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"624","span":{"begin":143,"end":152},"obj":"Chemical"},{"id":"625","span":{"begin":541,"end":550},"obj":"Chemical"}],"attributes":[{"id":"A624","pred":"tao:has_database_id","subj":"624","obj":"MESH:D004220"},{"id":"A625","pred":"tao:has_database_id","subj":"625","obj":"MESH:D004220"}],"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":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T336","span":{"begin":198,"end":209},"obj":"Body_part"},{"id":"T337","span":{"begin":258,"end":266},"obj":"Body_part"},{"id":"T338","span":{"begin":272,"end":275},"obj":"Body_part"}],"attributes":[{"id":"A336","pred":"fma_id","subj":"T336","obj":"http://purl.org/sig/ont/fma/fma82739"},{"id":"A337","pred":"fma_id","subj":"T337","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A338","pred":"fma_id","subj":"T338","obj":"http://purl.org/sig/ont/fma/fma24890"}],"text":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T19","span":{"begin":272,"end":275},"obj":"Body_part"}],"attributes":[{"id":"A19","pred":"uberon_id","subj":"T19","obj":"http://purl.obolibrary.org/obo/UBERON_0001460"}],"text":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T680","span":{"begin":272,"end":275},"obj":"http://www.ebi.ac.uk/efo/EFO_0001410"}],"text":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T194","span":{"begin":143,"end":152},"obj":"Chemical"},{"id":"T195","span":{"begin":198,"end":209},"obj":"Chemical"},{"id":"T196","span":{"begin":198,"end":203},"obj":"Chemical"},{"id":"T197","span":{"begin":204,"end":209},"obj":"Chemical"},{"id":"T198","span":{"begin":541,"end":550},"obj":"Chemical"},{"id":"T199","span":{"begin":598,"end":606},"obj":"Chemical"}],"attributes":[{"id":"A194","pred":"chebi_id","subj":"T194","obj":"http://purl.obolibrary.org/obo/CHEBI_48343"},{"id":"A195","pred":"chebi_id","subj":"T195","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"},{"id":"A196","pred":"chebi_id","subj":"T196","obj":"http://purl.obolibrary.org/obo/CHEBI_46882"},{"id":"A197","pred":"chebi_id","subj":"T197","obj":"http://purl.obolibrary.org/obo/CHEBI_37527"},{"id":"A198","pred":"chebi_id","subj":"T198","obj":"http://purl.obolibrary.org/obo/CHEBI_48343"},{"id":"A199","pred":"chebi_id","subj":"T199","obj":"http://purl.obolibrary.org/obo/CHEBI_25367"}],"text":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T41","span":{"begin":143,"end":152},"obj":"Chemical"},{"id":"T42","span":{"begin":198,"end":209},"obj":"Chemical"},{"id":"T43","span":{"begin":541,"end":550},"obj":"Chemical"}],"attributes":[{"id":"A41","pred":"chebi_id","subj":"T41","obj":"http://purl.obolibrary.org/obo/CHEBI_48343"},{"id":"A42","pred":"chebi_id","subj":"T42","obj":"http://purl.obolibrary.org/obo/CHEBI_33709"},{"id":"A43","pred":"chebi_id","subj":"T43","obj":"http://purl.obolibrary.org/obo/CHEBI_48343"}],"text":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"624","span":{"begin":143,"end":152},"obj":"Chemical"},{"id":"625","span":{"begin":541,"end":550},"obj":"Chemical"}],"attributes":[{"id":"A624","pred":"pubann:denotes","subj":"624","obj":"MESH:D004220"},{"id":"A625","pred":"pubann:denotes","subj":"625","obj":"MESH:D004220"}],"text":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T208","span":{"begin":0,"end":159},"obj":"Sentence"},{"id":"T209","span":{"begin":160,"end":628},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}

{"project":"LitCovid-sample-PD-UBERON","denotations":[{"id":"T19","span":{"begin":272,"end":275},"obj":"Body_part"}],"attributes":[{"id":"A19","pred":"uberon_id","subj":"T19","obj":"http://purl.obolibrary.org/obo/UBERON_0001460"}],"text":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T335","span":{"begin":198,"end":209},"obj":"Body_part"},{"id":"T336","span":{"begin":258,"end":266},"obj":"Body_part"},{"id":"T337","span":{"begin":272,"end":275},"obj":"Body_part"}],"attributes":[{"id":"A335","pred":"fma_id","subj":"T335","obj":"http://purl.org/sig/ont/fma/fma82739"},{"id":"A336","pred":"fma_id","subj":"T336","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A337","pred":"fma_id","subj":"T337","obj":"http://purl.org/sig/ont/fma/fma24890"}],"text":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T91","span":{"begin":277,"end":285},"obj":"http://purl.obolibrary.org/obo/GO_0015297"},{"id":"T92","span":{"begin":607,"end":615},"obj":"http://purl.obolibrary.org/obo/GO_0015297"}],"text":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T92","span":{"begin":277,"end":285},"obj":"http://purl.obolibrary.org/obo/GO_0015297"},{"id":"T93","span":{"begin":607,"end":615},"obj":"http://purl.obolibrary.org/obo/GO_0015297"}],"text":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T92","span":{"begin":277,"end":285},"obj":"http://purl.obolibrary.org/obo/GO_0015297"},{"id":"T93","span":{"begin":607,"end":615},"obj":"http://purl.obolibrary.org/obo/GO_0015297"}],"text":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}

{"project":"LitCovid-sentences","denotations":[{"id":"T208","span":{"begin":0,"end":159},"obj":"Sentence"},{"id":"T209","span":{"begin":160,"end":628},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Furthermore, the core hinge of IgG4 differs from IgG1 at position 228 (P228 in IgG1 and S228 in IgG4), resulting in unstable inter‐heavy‐chain disulfide bonds. This, together with the destabilizing amino acids in the CH3, confers the unique property of half‐antibody (Fab arm) exchange between different IgG4 antibodies,69 thereby creating monovalent, bispecific IgG4 antibodies in vivo.69, 70 The similarly unstable interactions between the CH3 domains in IgG2 are conferred by the interface residue M397; however, the stable inter‐H‐chain disulfide bonds of the core and upper hinge prevent half‐molecule exchange (Table 3).69"}