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Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-74 Sentence denotes Isolation and characterization of IgG1 with asymmetrical Fc glycosylation.
T1 0-74 Sentence denotes Isolation and characterization of IgG1 with asymmetrical Fc glycosylation.
T1 0-74 Sentence denotes Isolation and characterization of IgG1 with asymmetrical Fc glycosylation.
TextSentencer_T2 75-233 Sentence denotes N-glycosylation of immunoglobulin G (IgG) at asparigine residue 297 plays a critical role in antibody stability and immune cell-mediated Fc effector function.
T2 75-233 Sentence denotes N-glycosylation of immunoglobulin G (IgG) at asparigine residue 297 plays a critical role in antibody stability and immune cell-mediated Fc effector function.
T2 75-233 Sentence denotes N-glycosylation of immunoglobulin G (IgG) at asparigine residue 297 plays a critical role in antibody stability and immune cell-mediated Fc effector function.
TextSentencer_T3 234-432 Sentence denotes Current understanding pertaining to Fc glycosylation is based on studies with IgGs that are either fully glycosylated [both heavy chain (HC) glycosylated] or aglycosylated (neither HC glycosylated).
T3 234-432 Sentence denotes Current understanding pertaining to Fc glycosylation is based on studies with IgGs that are either fully glycosylated [both heavy chain (HC) glycosylated] or aglycosylated (neither HC glycosylated).
T3 234-432 Sentence denotes Current understanding pertaining to Fc glycosylation is based on studies with IgGs that are either fully glycosylated [both heavy chain (HC) glycosylated] or aglycosylated (neither HC glycosylated).
TextSentencer_T4 433-629 Sentence denotes No study has been reported on the properties of hemi-glycosylated IgGs, antibodies with asymmetrical glycosylation in the Fc region such that one HC is glycosylated and the other is aglycosylated.
T4 433-629 Sentence denotes No study has been reported on the properties of hemi-glycosylated IgGs, antibodies with asymmetrical glycosylation in the Fc region such that one HC is glycosylated and the other is aglycosylated.
T4 433-629 Sentence denotes No study has been reported on the properties of hemi-glycosylated IgGs, antibodies with asymmetrical glycosylation in the Fc region such that one HC is glycosylated and the other is aglycosylated.
TextSentencer_T5 630-835 Sentence denotes We report here for the first time a detailed study of how hemi-glycosylation affects the stability and functional activities of an IgG1 antibody, mAb-X, in comparison to its fully glycosylated counterpart.
T5 630-835 Sentence denotes We report here for the first time a detailed study of how hemi-glycosylation affects the stability and functional activities of an IgG1 antibody, mAb-X, in comparison to its fully glycosylated counterpart.
T5 630-835 Sentence denotes We report here for the first time a detailed study of how hemi-glycosylation affects the stability and functional activities of an IgG1 antibody, mAb-X, in comparison to its fully glycosylated counterpart.
TextSentencer_T6 836-971 Sentence denotes Our results show that hemi-glycosylation does not impact Fab-mediated antigen binding, nor does it impact neonatal Fc receptor binding.
T6 836-971 Sentence denotes Our results show that hemi-glycosylation does not impact Fab-mediated antigen binding, nor does it impact neonatal Fc receptor binding.
T6 836-971 Sentence denotes Our results show that hemi-glycosylation does not impact Fab-mediated antigen binding, nor does it impact neonatal Fc receptor binding.
TextSentencer_T7 972-1101 Sentence denotes Hemi-glycosylated mAb-X has slightly decreased thermal stability in the CH2 domain and a moderate decrease (∼20%) in C1q binding.
T7 972-1101 Sentence denotes Hemi-glycosylated mAb-X has slightly decreased thermal stability in the CH2 domain and a moderate decrease (∼20%) in C1q binding.
T7 972-1101 Sentence denotes Hemi-glycosylated mAb-X has slightly decreased thermal stability in the CH2 domain and a moderate decrease (∼20%) in C1q binding.
TextSentencer_T8 1102-1330 Sentence denotes More importantly, the hemi-glycosylated form shows significantly decreased binding affinities toward all Fc gamma receptors (FcγRs) including the high-affinity FcγRI, and the low-affinity FcγRIIA, FcγRIIB, FcγRIIIA and FcγRIIIB.
T8 1102-1330 Sentence denotes More importantly, the hemi-glycosylated form shows significantly decreased binding affinities toward all Fc gamma receptors (FcγRs) including the high-affinity FcγRI, and the low-affinity FcγRIIA, FcγRIIB, FcγRIIIA and FcγRIIIB.
T8 1102-1330 Sentence denotes More importantly, the hemi-glycosylated form shows significantly decreased binding affinities toward all Fc gamma receptors (FcγRs) including the high-affinity FcγRI, and the low-affinity FcγRIIA, FcγRIIB, FcγRIIIA and FcγRIIIB.
TextSentencer_T9 1331-1450 Sentence denotes The decreased binding affinities to FcγRs result in a 3.5-fold decrease in antibody-dependent cell cytotoxicity (ADCC).
T9 1331-1450 Sentence denotes The decreased binding affinities to FcγRs result in a 3.5-fold decrease in antibody-dependent cell cytotoxicity (ADCC).
T9 1331-1450 Sentence denotes The decreased binding affinities to FcγRs result in a 3.5-fold decrease in antibody-dependent cell cytotoxicity (ADCC).
TextSentencer_T10 1451-1645 Sentence denotes As ADCC often plays an important role in therapeutic antibody efficacy, glycosylation status will not only affect the antibody quality but also may impact the biological function of the product.
T10 1451-1645 Sentence denotes As ADCC often plays an important role in therapeutic antibody efficacy, glycosylation status will not only affect the antibody quality but also may impact the biological function of the product.
T10 1451-1645 Sentence denotes As ADCC often plays an important role in therapeutic antibody efficacy, glycosylation status will not only affect the antibody quality but also may impact the biological function of the product.