PMC:7228307 / 46049-47030 JSONTXT

{"project":"LitCovid_Glycan-Motif-Structure","denotations":[{"id":"T2","span":{"begin":88,"end":94},"obj":"https://glytoucan.org/Structures/Glycans/G82576YO"},{"id":"T3","span":{"begin":124,"end":130},"obj":"https://glytoucan.org/Structures/Glycans/G82576YO"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-PubTator","denotations":[{"id":"879","span":{"begin":178,"end":186},"obj":"Gene"},{"id":"880","span":{"begin":191,"end":199},"obj":"Gene"},{"id":"881","span":{"begin":272,"end":279},"obj":"Gene"},{"id":"882","span":{"begin":377,"end":385},"obj":"Gene"},{"id":"883","span":{"begin":482,"end":486},"obj":"Gene"},{"id":"884","span":{"begin":493,"end":497},"obj":"Gene"},{"id":"885","span":{"begin":639,"end":646},"obj":"Gene"},{"id":"886","span":{"begin":750,"end":757},"obj":"Gene"},{"id":"887","span":{"begin":894,"end":902},"obj":"Gene"},{"id":"888","span":{"begin":948,"end":955},"obj":"Gene"},{"id":"889","span":{"begin":878,"end":886},"obj":"Gene"},{"id":"890","span":{"begin":20,"end":35},"obj":"Chemical"},{"id":"891","span":{"begin":88,"end":94},"obj":"Chemical"},{"id":"892","span":{"begin":124,"end":130},"obj":"Chemical"},{"id":"893","span":{"begin":448,"end":453},"obj":"Disease"}],"attributes":[{"id":"A879","pred":"tao:has_database_id","subj":"879","obj":"Gene:2214"},{"id":"A880","pred":"tao:has_database_id","subj":"880","obj":"Gene:2215"},{"id":"A881","pred":"tao:has_database_id","subj":"881","obj":"Gene:2213"},{"id":"A882","pred":"tao:has_database_id","subj":"882","obj":"Gene:2214"},{"id":"A883","pred":"tao:has_database_id","subj":"883","obj":"Gene:2064"},{"id":"A884","pred":"tao:has_database_id","subj":"884","obj":"Gene:1956"},{"id":"A885","pred":"tao:has_database_id","subj":"885","obj":"Gene:2214"},{"id":"A886","pred":"tao:has_database_id","subj":"886","obj":"Gene:2214"},{"id":"A887","pred":"tao:has_database_id","subj":"887","obj":"Gene:2214"},{"id":"A888","pred":"tao:has_database_id","subj":"888","obj":"Gene:2212"},{"id":"A889","pred":"tao:has_database_id","subj":"889","obj":"Gene:2215"},{"id":"A891","pred":"tao:has_database_id","subj":"891","obj":"MESH:D005643"},{"id":"A892","pred":"tao:has_database_id","subj":"892","obj":"MESH:D005643"},{"id":"A893","pred":"tao:has_database_id","subj":"893","obj":"MESH:D009369"}],"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":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T376","span":{"begin":88,"end":94},"obj":"Body_part"},{"id":"T377","span":{"begin":98,"end":108},"obj":"Body_part"},{"id":"T378","span":{"begin":124,"end":130},"obj":"Body_part"},{"id":"T379","span":{"begin":802,"end":809},"obj":"Body_part"},{"id":"T380","span":{"begin":805,"end":809},"obj":"Body_part"},{"id":"T381","span":{"begin":837,"end":847},"obj":"Body_part"},{"id":"T382","span":{"begin":923,"end":933},"obj":"Body_part"}],"attributes":[{"id":"A376","pred":"fma_id","subj":"T376","obj":"http://purl.org/sig/ont/fma/fma82790"},{"id":"A377","pred":"fma_id","subj":"T377","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A378","pred":"fma_id","subj":"T378","obj":"http://purl.org/sig/ont/fma/fma82790"},{"id":"A379","pred":"fma_id","subj":"T379","obj":"http://purl.org/sig/ont/fma/fma63147"},{"id":"A380","pred":"fma_id","subj":"T380","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A381","pred":"fma_id","subj":"T381","obj":"http://purl.org/sig/ont/fma/fma62860"},{"id":"A382","pred":"fma_id","subj":"T382","obj":"http://purl.org/sig/ont/fma/fma62860"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T79","span":{"begin":448,"end":453},"obj":"Disease"},{"id":"T80","span":{"begin":819,"end":823},"obj":"Disease"}],"attributes":[{"id":"A79","pred":"mondo_id","subj":"T79","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"},{"id":"A80","pred":"mondo_id","subj":"T80","obj":"http://purl.obolibrary.org/obo/MONDO_0008734"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T803","span":{"begin":81,"end":82},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T804","span":{"begin":178,"end":180},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T805","span":{"begin":191,"end":193},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T806","span":{"begin":272,"end":274},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T807","span":{"begin":377,"end":379},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T808","span":{"begin":585,"end":586},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T809","span":{"begin":639,"end":641},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T810","span":{"begin":750,"end":752},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T811","span":{"begin":802,"end":809},"obj":"http://purl.obolibrary.org/obo/CL_0000623"},{"id":"T812","span":{"begin":878,"end":880},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T813","span":{"begin":894,"end":896},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"},{"id":"T814","span":{"begin":948,"end":950},"obj":"http://purl.obolibrary.org/obo/CLO_0052676"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T235","span":{"begin":88,"end":94},"obj":"Chemical"},{"id":"T236","span":{"begin":124,"end":130},"obj":"Chemical"},{"id":"T237","span":{"begin":766,"end":774},"obj":"Chemical"}],"attributes":[{"id":"A235","pred":"chebi_id","subj":"T235","obj":"http://purl.obolibrary.org/obo/CHEBI_33984"},{"id":"A236","pred":"chebi_id","subj":"T236","obj":"http://purl.obolibrary.org/obo/CHEBI_33984"},{"id":"A237","pred":"chebi_id","subj":"T237","obj":"http://purl.obolibrary.org/obo/CHEBI_35224"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T221","span":{"begin":805,"end":809},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T222","span":{"begin":934,"end":943},"obj":"http://purl.obolibrary.org/obo/BFO_0000034"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T48","span":{"begin":88,"end":94},"obj":"Chemical"},{"id":"T49","span":{"begin":124,"end":130},"obj":"Chemical"}],"attributes":[{"id":"A48","pred":"chebi_id","subj":"T48","obj":"http://purl.obolibrary.org/obo/CHEBI_33984"},{"id":"A49","pred":"chebi_id","subj":"T49","obj":"http://purl.obolibrary.org/obo/CHEBI_33984"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"879","span":{"begin":178,"end":186},"obj":"Gene"},{"id":"880","span":{"begin":191,"end":199},"obj":"Gene"},{"id":"881","span":{"begin":272,"end":279},"obj":"Gene"},{"id":"882","span":{"begin":377,"end":385},"obj":"Gene"},{"id":"883","span":{"begin":482,"end":486},"obj":"Gene"},{"id":"884","span":{"begin":493,"end":497},"obj":"Gene"},{"id":"885","span":{"begin":639,"end":646},"obj":"Gene"},{"id":"886","span":{"begin":750,"end":757},"obj":"Gene"},{"id":"887","span":{"begin":894,"end":902},"obj":"Gene"},{"id":"888","span":{"begin":948,"end":955},"obj":"Gene"},{"id":"889","span":{"begin":878,"end":886},"obj":"Gene"},{"id":"890","span":{"begin":20,"end":35},"obj":"Chemical"},{"id":"891","span":{"begin":88,"end":94},"obj":"Chemical"},{"id":"892","span":{"begin":124,"end":130},"obj":"Chemical"},{"id":"893","span":{"begin":448,"end":453},"obj":"Disease"}],"attributes":[{"id":"A879","pred":"pubann:denotes","subj":"879","obj":"Gene:2214"},{"id":"A880","pred":"pubann:denotes","subj":"880","obj":"Gene:2215"},{"id":"A892","pred":"pubann:denotes","subj":"892","obj":"MESH:D005643"},{"id":"A889","pred":"pubann:denotes","subj":"889","obj":"Gene:2215"},{"id":"A893","pred":"pubann:denotes","subj":"893","obj":"MESH:D009369"},{"id":"A886","pred":"pubann:denotes","subj":"886","obj":"Gene:2214"},{"id":"A884","pred":"pubann:denotes","subj":"884","obj":"Gene:1956"},{"id":"A881","pred":"pubann:denotes","subj":"881","obj":"Gene:2213"},{"id":"A887","pred":"pubann:denotes","subj":"887","obj":"Gene:2214"},{"id":"A885","pred":"pubann:denotes","subj":"885","obj":"Gene:2214"},{"id":"A888","pred":"pubann:denotes","subj":"888","obj":"Gene:2212"},{"id":"A883","pred":"pubann:denotes","subj":"883","obj":"Gene:2064"},{"id":"A891","pred":"pubann:denotes","subj":"891","obj":"MESH:D005643"},{"id":"A882","pred":"pubann:denotes","subj":"882","obj":"Gene:2214"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T269","span":{"begin":0,"end":280},"obj":"Sentence"},{"id":"T270","span":{"begin":281,"end":655},"obj":"Sentence"},{"id":"T271","span":{"begin":656,"end":981},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T582","span":{"begin":507,"end":511},"obj":"Protein"}],"attributes":[{"id":"A582","pred":"uniprot_id","subj":"T582","obj":"https://www.uniprot.org/uniprot/Q3C2E2"},{"id":"A583","pred":"uniprot_id","subj":"T582","obj":"https://www.uniprot.org/uniprot/Q13963"},{"id":"A584","pred":"uniprot_id","subj":"T582","obj":"https://www.uniprot.org/uniprot/P19437"},{"id":"A585","pred":"uniprot_id","subj":"T582","obj":"https://www.uniprot.org/uniprot/P11836"},{"id":"A586","pred":"uniprot_id","subj":"T582","obj":"https://www.uniprot.org/uniprot/P08984"},{"id":"A587","pred":"uniprot_id","subj":"T582","obj":"https://www.uniprot.org/uniprot/B4DT24"},{"id":"A588","pred":"uniprot_id","subj":"T582","obj":"https://www.uniprot.org/uniprot/A6NMS4"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T375","span":{"begin":88,"end":94},"obj":"Body_part"},{"id":"T376","span":{"begin":98,"end":108},"obj":"Body_part"},{"id":"T377","span":{"begin":124,"end":130},"obj":"Body_part"},{"id":"T378","span":{"begin":802,"end":809},"obj":"Body_part"},{"id":"T379","span":{"begin":805,"end":809},"obj":"Body_part"},{"id":"T380","span":{"begin":837,"end":847},"obj":"Body_part"},{"id":"T381","span":{"begin":923,"end":933},"obj":"Body_part"}],"attributes":[{"id":"A375","pred":"fma_id","subj":"T375","obj":"http://purl.org/sig/ont/fma/fma82790"},{"id":"A376","pred":"fma_id","subj":"T376","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A377","pred":"fma_id","subj":"T377","obj":"http://purl.org/sig/ont/fma/fma82790"},{"id":"A378","pred":"fma_id","subj":"T378","obj":"http://purl.org/sig/ont/fma/fma63147"},{"id":"A379","pred":"fma_id","subj":"T379","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A380","pred":"fma_id","subj":"T380","obj":"http://purl.org/sig/ont/fma/fma62860"},{"id":"A381","pred":"fma_id","subj":"T381","obj":"http://purl.org/sig/ont/fma/fma62860"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T107","span":{"begin":493,"end":497},"obj":"http://purl.obolibrary.org/obo/GO_0005006"},{"id":"T108","span":{"begin":819,"end":823},"obj":"http://purl.obolibrary.org/obo/GO_0001788"},{"id":"T109","span":{"begin":857,"end":869},"obj":"http://purl.obolibrary.org/obo/GO_0006909"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T35","span":{"begin":448,"end":453},"obj":"Disease"}],"attributes":[{"id":"A35","pred":"mondo_id","subj":"T35","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-sample-PD-HP","denotations":[{"id":"T31","span":{"begin":448,"end":453},"obj":"Phenotype"}],"attributes":[{"id":"A31","pred":"hp_id","subj":"T31","obj":"http://purl.obolibrary.org/obo/HP_0002664"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T107","span":{"begin":493,"end":497},"obj":"http://purl.obolibrary.org/obo/GO_0005006"},{"id":"T108","span":{"begin":819,"end":823},"obj":"http://purl.obolibrary.org/obo/GO_0001788"},{"id":"T109","span":{"begin":857,"end":869},"obj":"http://purl.obolibrary.org/obo/GO_0006909"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T107","span":{"begin":493,"end":497},"obj":"http://purl.obolibrary.org/obo/GO_0005006"},{"id":"T108","span":{"begin":819,"end":823},"obj":"http://purl.obolibrary.org/obo/GO_0001788"},{"id":"T109","span":{"begin":857,"end":869},"obj":"http://purl.obolibrary.org/obo/GO_0006909"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-sentences","denotations":[{"id":"T269","span":{"begin":0,"end":280},"obj":"Sentence"},{"id":"T270","span":{"begin":281,"end":655},"obj":"Sentence"},{"id":"T271","span":{"begin":656,"end":981},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}

{"project":"LitCovid-PD-HP","denotations":[{"id":"T31","span":{"begin":448,"end":453},"obj":"Phenotype"}],"attributes":[{"id":"A31","pred":"hp_id","subj":"T31","obj":"http://purl.obolibrary.org/obo/HP_0002664"}],"text":"The typical complex N‐linked glycan attached to N297 of the heavy chain includes a core fucose.85 Antibodies that lack this fucose have approximately 50‐fold improved binding to FcγRIIIa and FcγRIIIb and importantly retain the weak, low‐affinity binding to the inhibitory FcγRIIb. Furthermore, this glycoengineering increased binding affinity of the modified IgG1 mAb for both FcγRIIIa V158 and F158 allelotypes.86, 87, 88 Afucosyl versions of the tumor targeting mAbs such as anti‐HER2, anti‐EGFR and anti‐CD20 had greater antitumor effects and increased survival,68, 88, 89 which is a reflection of the greatly increased, and selective, FcγRIII binding. Compared with their unmodified counterparts, the afucosyl mAbs showed dramatic improvement of FcγRIII‐related effector responses such as stronger NK cell‐mediated ADCC, or enhanced neutrophil‐mediated phagocytosis through FcγRIIIb and/or FcγRIIIa.23 However, certain neutrophil functions via FcγRIIa may be compromised.90, 91"}