PMC:7228307 / 21853-22817
Annnotations
LitCovid-PubTator
{"project":"LitCovid-PubTator","denotations":[{"id":"411","span":{"begin":655,"end":659},"obj":"Gene"},{"id":"412","span":{"begin":222,"end":226},"obj":"Gene"},{"id":"413","span":{"begin":92,"end":96},"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":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-PD-FMA-UBERON
{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T235","span":{"begin":48,"end":51},"obj":"Body_part"},{"id":"T236","span":{"begin":731,"end":736},"obj":"Body_part"},{"id":"T237","span":{"begin":765,"end":783},"obj":"Body_part"},{"id":"T238","span":{"begin":806,"end":823},"obj":"Body_part"},{"id":"T239","span":{"begin":824,"end":834},"obj":"Body_part"},{"id":"T240","span":{"begin":879,"end":892},"obj":"Body_part"}],"attributes":[{"id":"A235","pred":"fma_id","subj":"T235","obj":"http://purl.org/sig/ont/fma/fma62872"},{"id":"A236","pred":"fma_id","subj":"T236","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A237","pred":"fma_id","subj":"T237","obj":"http://purl.org/sig/ont/fma/fma84684"},{"id":"A238","pred":"fma_id","subj":"T238","obj":"http://purl.org/sig/ont/fma/fma63011"},{"id":"A239","pred":"fma_id","subj":"T239","obj":"http://purl.org/sig/ont/fma/fma66838"},{"id":"A240","pred":"fma_id","subj":"T240","obj":"http://purl.org/sig/ont/fma/fma62925"}],"text":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-PD-MONDO
{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T31","span":{"begin":561,"end":565},"obj":"Disease"}],"attributes":[{"id":"A31","pred":"mondo_id","subj":"T31","obj":"http://purl.obolibrary.org/obo/MONDO_0008734"}],"text":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-PD-CLO
{"project":"LitCovid-PD-CLO","denotations":[{"id":"T434","span":{"begin":52,"end":54},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T435","span":{"begin":92,"end":94},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T436","span":{"begin":107,"end":108},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T437","span":{"begin":222,"end":224},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T438","span":{"begin":300,"end":302},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T439","span":{"begin":312,"end":314},"obj":"http://purl.obolibrary.org/obo/CLO_0001000"},{"id":"T440","span":{"begin":355,"end":357},"obj":"http://purl.obolibrary.org/obo/CLO_0001313"},{"id":"T441","span":{"begin":415,"end":417},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T442","span":{"begin":431,"end":432},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T443","span":{"begin":646,"end":648},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T444","span":{"begin":655,"end":657},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T445","span":{"begin":731,"end":736},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T446","span":{"begin":902,"end":906},"obj":"http://purl.obolibrary.org/obo/PR_000001307"}],"text":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-PD-CHEBI
{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T106","span":{"begin":10,"end":18},"obj":"Chemical"},{"id":"T107","span":{"begin":162,"end":169},"obj":"Chemical"},{"id":"T108","span":{"begin":227,"end":235},"obj":"Chemical"},{"id":"T109","span":{"begin":461,"end":468},"obj":"Chemical"},{"id":"T110","span":{"begin":511,"end":518},"obj":"Chemical"},{"id":"T111","span":{"begin":534,"end":542},"obj":"Chemical"},{"id":"T112","span":{"begin":722,"end":730},"obj":"Chemical"},{"id":"T113","span":{"begin":806,"end":823},"obj":"Chemical"},{"id":"T114","span":{"begin":879,"end":892},"obj":"Chemical"}],"attributes":[{"id":"A106","pred":"chebi_id","subj":"T106","obj":"http://purl.obolibrary.org/obo/CHEBI_35224"},{"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"},{"id":"A112","pred":"chebi_id","subj":"T112","obj":"http://purl.obolibrary.org/obo/CHEBI_35224"},{"id":"A113","pred":"chebi_id","subj":"T113","obj":"http://purl.obolibrary.org/obo/CHEBI_18085"},{"id":"A114","pred":"chebi_id","subj":"T114","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"}],"text":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-sample-PD-IDO
{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T134","span":{"begin":731,"end":736},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T135","span":{"begin":844,"end":852},"obj":"http://purl.obolibrary.org/obo/BFO_0000034"}],"text":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-sample-CHEBI
{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T23","span":{"begin":806,"end":823},"obj":"Chemical"},{"id":"T24","span":{"begin":879,"end":892},"obj":"Chemical"}],"attributes":[{"id":"A23","pred":"chebi_id","subj":"T23","obj":"http://purl.obolibrary.org/obo/CHEBI_18085"},{"id":"A24","pred":"chebi_id","subj":"T24","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"}],"text":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-sample-Pubtator
{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"411","span":{"begin":655,"end":659},"obj":"Gene"},{"id":"412","span":{"begin":222,"end":226},"obj":"Gene"},{"id":"413","span":{"begin":92,"end":96},"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":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-sample-sentences
{"project":"LitCovid-sample-sentences","denotations":[{"id":"T134","span":{"begin":29,"end":703},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-sample-UniProt
{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T97","span":{"begin":765,"end":770},"obj":"Protein"},{"id":"T110","span":{"begin":879,"end":892},"obj":"Protein"},{"id":"T195","span":{"begin":902,"end":906},"obj":"Protein"}],"attributes":[{"id":"A97","pred":"uniprot_id","subj":"T97","obj":"https://www.uniprot.org/uniprot/Q92193"},{"id":"A98","pred":"uniprot_id","subj":"T97","obj":"https://www.uniprot.org/uniprot/Q92192"},{"id":"A99","pred":"uniprot_id","subj":"T97","obj":"https://www.uniprot.org/uniprot/Q24733"},{"id":"A100","pred":"uniprot_id","subj":"T97","obj":"https://www.uniprot.org/uniprot/Q11212"},{"id":"A101","pred":"uniprot_id","subj":"T97","obj":"https://www.uniprot.org/uniprot/P91754"},{"id":"A102","pred":"uniprot_id","subj":"T97","obj":"https://www.uniprot.org/uniprot/P90689"},{"id":"A103","pred":"uniprot_id","subj":"T97","obj":"https://www.uniprot.org/uniprot/P80709"},{"id":"A104","pred":"uniprot_id","subj":"T97","obj":"https://www.uniprot.org/uniprot/P68555"},{"id":"A105","pred":"uniprot_id","subj":"T97","obj":"https://www.uniprot.org/uniprot/P45521"},{"id":"A106","pred":"uniprot_id","subj":"T97","obj":"https://www.uniprot.org/uniprot/P38136"},{"id":"A107","pred":"uniprot_id","subj":"T97","obj":"https://www.uniprot.org/uniprot/P14227"},{"id":"A108","pred":"uniprot_id","subj":"T97","obj":"https://www.uniprot.org/uniprot/O17320"},{"id":"A109","pred":"uniprot_id","subj":"T97","obj":"https://www.uniprot.org/uniprot/O16808"},{"id":"A110","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q9QSP1"},{"id":"A111","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q9QJT6"},{"id":"A112","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q9JGT4"},{"id":"A113","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q9IPJ6"},{"id":"A114","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q9DIC6"},{"id":"A115","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q91DS0"},{"id":"A116","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q91C28"},{"id":"A117","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q8QQA2"},{"id":"A118","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q8QPE5"},{"id":"A119","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q8QPE4"},{"id":"A120","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q8QPE3"},{"id":"A121","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q8JTH0"},{"id":"A122","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q8BDV6"},{"id":"A123","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q8B6J6"},{"id":"A124","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q8B0I1"},{"id":"A125","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q8B0H6"},{"id":"A126","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q8B0H1"},{"id":"A127","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q89669"},{"id":"A128","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q85213"},{"id":"A129","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q82706"},{"id":"A130","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q82683"},{"id":"A131","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q82020"},{"id":"A132","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q787B5"},{"id":"A133","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q77SK0"},{"id":"A134","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q77N36"},{"id":"A135","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q76G52"},{"id":"A136","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q75T09"},{"id":"A137","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q6X1D5"},{"id":"A138","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q6X1D1"},{"id":"A139","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q6TYA0"},{"id":"A140","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q6E0W7"},{"id":"A141","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q66T62"},{"id":"A142","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q5VKP3"},{"id":"A143","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q5VKN9"},{"id":"A144","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q5K2K4"},{"id":"A145","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q5IX93"},{"id":"A146","pred":"uniprot_id","subj":"T110","obj":"https://www.uniprot.org/uniprot/Q5IX92"},{"id":"A147","pre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an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-sample-PD-FMA
{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T234","span":{"begin":48,"end":51},"obj":"Body_part"},{"id":"T235","span":{"begin":731,"end":736},"obj":"Body_part"},{"id":"T236","span":{"begin":765,"end":783},"obj":"Body_part"},{"id":"T237","span":{"begin":806,"end":823},"obj":"Body_part"},{"id":"T238","span":{"begin":824,"end":834},"obj":"Body_part"},{"id":"T239","span":{"begin":879,"end":892},"obj":"Body_part"}],"attributes":[{"id":"A234","pred":"fma_id","subj":"T234","obj":"http://purl.org/sig/ont/fma/fma62872"},{"id":"A235","pred":"fma_id","subj":"T235","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A236","pred":"fma_id","subj":"T236","obj":"http://purl.org/sig/ont/fma/fma84684"},{"id":"A237","pred":"fma_id","subj":"T237","obj":"http://purl.org/sig/ont/fma/fma63011"},{"id":"A238","pred":"fma_id","subj":"T238","obj":"http://purl.org/sig/ont/fma/fma66838"},{"id":"A239","pred":"fma_id","subj":"T239","obj":"http://purl.org/sig/ont/fma/fma62925"}],"text":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-sample-PD-GO-BP-0
{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T54","span":{"begin":561,"end":565},"obj":"http://purl.obolibrary.org/obo/GO_0001788"}],"text":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-sample-GO-BP
{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T54","span":{"begin":561,"end":565},"obj":"http://purl.obolibrary.org/obo/GO_0001788"}],"text":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-PD-GO-BP
{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T54","span":{"begin":561,"end":565},"obj":"http://purl.obolibrary.org/obo/GO_0001788"}],"text":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}
LitCovid-sentences
{"project":"LitCovid-sentences","denotations":[{"id":"T134","span":{"begin":29,"end":703},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"tiates an effector response. 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\nSecond, in innate effector cells at rest, the largely linear actin cytoskeleton and the extracellular glycosaminoglycan glycocalyx regulate function by interacting with large glycoproteins, such as CD44, arranging these into ordered “picket” fences.39, 40 Thes"}