PMC:7228307 / 21882-22556 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"411","span":{"begin":626,"end":630},"obj":"Gene"},{"id":"412","span":{"begin":193,"end":197},"obj":"Gene"},{"id":"413","span":{"begin":63,"end":67},"obj":"Gene"}],"attributes":[{"id":"A411","pred":"tao:has_database_id","subj":"411","obj":"Gene:2213"},{"id":"A412","pred":"tao:has_database_id","subj":"412","obj":"Gene:2213"},{"id":"A413","pred":"tao:has_database_id","subj":"413","obj":"Gene:2213"}],"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":"Although it is the IgG Fc that interacts with and clusters the FcγR to induce a response, the nature of the Fab interaction with its epitope can strongly influence the likelihood or potency of FcγR effector responses by influencing the density of appropriately presented Fc portions.35 and also the size of the immune complex.36 Furthermore, the display/orientation and geometry of the Fc portions, as a consequence of the fragment antigen‐binding (Fab) interaction with the target epitope, can result in effector responses such as ADCC that differ substantially in potency, presumably because the orientation of the Fc makes FcγR engagement more, or less, accessible.37, 38"}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T235","span":{"begin":19,"end":22},"obj":"Body_part"}],"attributes":[{"id":"A235","pred":"fma_id","subj":"T235","obj":"http://purl.org/sig/ont/fma/fma62872"}],"text":"Although it is the IgG Fc that interacts with and clusters the FcγR to induce a response, the nature of the Fab interaction with its epitope can strongly influence the likelihood or potency of FcγR effector responses by influencing the density of appropriately presented Fc portions.35 and also the size of the immune complex.36 Furthermore, the display/orientation and geometry of the Fc portions, as a consequence of the fragment antigen‐binding (Fab) interaction with the target epitope, can result in effector responses such as ADCC that differ substantially in potency, presumably because the orientation of the Fc makes FcγR engagement more, or less, accessible.37, 38"}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T31","span":{"begin":532,"end":536},"obj":"Disease"}],"attributes":[{"id":"A31","pred":"mondo_id","subj":"T31","obj":"http://purl.obolibrary.org/obo/MONDO_0008734"}],"text":"Although it is the IgG Fc that interacts with and clusters the FcγR to induce a response, the nature of the Fab interaction with its epitope can strongly influence the likelihood or potency of FcγR effector responses by influencing the density of appropriately presented Fc portions.35 and also the size of the immune complex.36 Furthermore, the display/orientation and geometry of the Fc portions, as a consequence of the fragment antigen‐binding (Fab) interaction with the target epitope, can result in effector responses such as ADCC that differ substantially in potency, presumably because the orientation of the Fc makes FcγR engagement more, or less, accessible.37, 38"}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T434","span":{"begin":23,"end":25},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T435","span":{"begin":63,"end":65},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T436","span":{"begin":78,"end":79},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T437","span":{"begin":193,"end":195},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T438","span":{"begin":271,"end":273},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T439","span":{"begin":283,"end":285},"obj":"http://purl.obolibrary.org/obo/CLO_0001000"},{"id":"T440","span":{"begin":326,"end":328},"obj":"http://purl.obolibrary.org/obo/CLO_0001313"},{"id":"T441","span":{"begin":386,"end":388},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T442","span":{"begin":402,"end":403},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T443","span":{"begin":617,"end":619},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T444","span":{"begin":626,"end":628},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"}],"text":"Although it is the IgG Fc that interacts with and clusters the FcγR to induce a response, the nature of the Fab interaction with its epitope can strongly influence the likelihood or potency of FcγR effector responses by influencing the density of appropriately presented Fc portions.35 and also the size of the immune complex.36 Furthermore, the display/orientation and geometry of the Fc portions, as a consequence of the fragment antigen‐binding (Fab) interaction with the target epitope, can result in effector responses such as ADCC that differ substantially in potency, presumably because the orientation of the Fc makes FcγR engagement more, or less, accessible.37, 38"}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T107","span":{"begin":133,"end":140},"obj":"Chemical"},{"id":"T108","span":{"begin":198,"end":206},"obj":"Chemical"},{"id":"T109","span":{"begin":432,"end":439},"obj":"Chemical"},{"id":"T110","span":{"begin":482,"end":489},"obj":"Chemical"},{"id":"T111","span":{"begin":505,"end":513},"obj":"Chemical"}],"attributes":[{"id":"A107","pred":"chebi_id","subj":"T107","obj":"http://purl.obolibrary.org/obo/CHEBI_53000"},{"id":"A108","pred":"chebi_id","subj":"T108","obj":"http://purl.obolibrary.org/obo/CHEBI_35224"},{"id":"A109","pred":"chebi_id","subj":"T109","obj":"http://purl.obolibrary.org/obo/CHEBI_59132"},{"id":"A110","pred":"chebi_id","subj":"T110","obj":"http://purl.obolibrary.org/obo/CHEBI_53000"},{"id":"A111","pred":"chebi_id","subj":"T111","obj":"http://purl.obolibrary.org/obo/CHEBI_35224"}],"text":"Although it is the IgG Fc that interacts with and clusters the FcγR to induce a response, the nature of the Fab interaction with its epitope can strongly influence the likelihood or potency of FcγR effector responses by influencing the density of appropriately presented Fc portions.35 and also the size of the immune complex.36 Furthermore, the display/orientation and geometry of the Fc portions, as a consequence of the fragment antigen‐binding (Fab) interaction with the target epitope, can result in effector responses such as ADCC that differ substantially in potency, presumably because the orientation of the Fc makes FcγR engagement more, or less, accessible.37, 38"}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"411","span":{"begin":626,"end":630},"obj":"Gene"},{"id":"412","span":{"begin":193,"end":197},"obj":"Gene"},{"id":"413","span":{"begin":63,"end":67},"obj":"Gene"}],"attributes":[{"id":"A411","pred":"pubann:denotes","subj":"411","obj":"Gene:2213"},{"id":"A412","pred":"pubann:denotes","subj":"412","obj":"Gene:2213"},{"id":"A413","pred":"pubann:denotes","subj":"413","obj":"Gene:2213"}],"text":"Although it is the IgG Fc that interacts with and clusters the FcγR to induce a response, the nature of the Fab interaction with its epitope can strongly influence the likelihood or potency of FcγR effector responses by influencing the density of appropriately presented Fc portions.35 and also the size of the immune complex.36 Furthermore, the display/orientation and geometry of the Fc portions, as a consequence of the fragment antigen‐binding (Fab) interaction with the target epitope, can result in effector responses such as ADCC that differ substantially in potency, presumably because the orientation of the Fc makes FcγR engagement more, or less, accessible.37, 38"}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T134","span":{"begin":0,"end":674},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Although it is the IgG Fc that interacts with and clusters the FcγR to induce a response, the nature of the Fab interaction with its epitope can strongly influence the likelihood or potency of FcγR effector responses by influencing the density of appropriately presented Fc portions.35 and also the size of the immune complex.36 Furthermore, the display/orientation and geometry of the Fc portions, as a consequence of the fragment antigen‐binding (Fab) interaction with the target epitope, can result in effector responses such as ADCC that differ substantially in potency, presumably because the orientation of the Fc makes FcγR engagement more, or less, accessible.37, 38"}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T234","span":{"begin":19,"end":22},"obj":"Body_part"}],"attributes":[{"id":"A234","pred":"fma_id","subj":"T234","obj":"http://purl.org/sig/ont/fma/fma62872"}],"text":"Although it is the IgG Fc that interacts with and clusters the FcγR to induce a response, the nature of the Fab interaction with its epitope can strongly influence the likelihood or potency of FcγR effector responses by influencing the density of appropriately presented Fc portions.35 and also the size of the immune complex.36 Furthermore, the display/orientation and geometry of the Fc portions, as a consequence of the fragment antigen‐binding (Fab) interaction with the target epitope, can result in effector responses such as ADCC that differ substantially in potency, presumably because the orientation of the Fc makes FcγR engagement more, or less, accessible.37, 38"}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T54","span":{"begin":532,"end":536},"obj":"http://purl.obolibrary.org/obo/GO_0001788"}],"text":"Although it is the IgG Fc that interacts with and clusters the FcγR to induce a response, the nature of the Fab interaction with its epitope can strongly influence the likelihood or potency of FcγR effector responses by influencing the density of appropriately presented Fc portions.35 and also the size of the immune complex.36 Furthermore, the display/orientation and geometry of the Fc portions, as a consequence of the fragment antigen‐binding (Fab) interaction with the target epitope, can result in effector responses such as ADCC that differ substantially in potency, presumably because the orientation of the Fc makes FcγR engagement more, or less, accessible.37, 38"}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T54","span":{"begin":532,"end":536},"obj":"http://purl.obolibrary.org/obo/GO_0001788"}],"text":"Although it is the IgG Fc that interacts with and clusters the FcγR to induce a response, the nature of the Fab interaction with its epitope can strongly influence the likelihood or potency of FcγR effector responses by influencing the density of appropriately presented Fc portions.35 and also the size of the immune complex.36 Furthermore, the display/orientation and geometry of the Fc portions, as a consequence of the fragment antigen‐binding (Fab) interaction with the target epitope, can result in effector responses such as ADCC that differ substantially in potency, presumably because the orientation of the Fc makes FcγR engagement more, or less, accessible.37, 38"}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T54","span":{"begin":532,"end":536},"obj":"http://purl.obolibrary.org/obo/GO_0001788"}],"text":"Although it is the IgG Fc that interacts with and clusters the FcγR to induce a response, the nature of the Fab interaction with its epitope can strongly influence the likelihood or potency of FcγR effector responses by influencing the density of appropriately presented Fc portions.35 and also the size of the immune complex.36 Furthermore, the display/orientation and geometry of the Fc portions, as a consequence of the fragment antigen‐binding (Fab) interaction with the target epitope, can result in effector responses such as ADCC that differ substantially in potency, presumably because the orientation of the Fc makes FcγR engagement more, or less, accessible.37, 38"}

{"project":"LitCovid-sentences","denotations":[{"id":"T134","span":{"begin":0,"end":674},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Although it is the IgG Fc that interacts with and clusters the FcγR to induce a response, the nature of the Fab interaction with its epitope can strongly influence the likelihood or potency of FcγR effector responses by influencing the density of appropriately presented Fc portions.35 and also the size of the immune complex.36 Furthermore, the display/orientation and geometry of the Fc portions, as a consequence of the fragment antigen‐binding (Fab) interaction with the target epitope, can result in effector responses such as ADCC that differ substantially in potency, presumably because the orientation of the Fc makes FcγR engagement more, or less, accessible.37, 38"}