The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms.
about
Glycans in the immune system and The Altered Glycan Theory of Autoimmunity: a critical reviewA perspective on the structure and receptor binding properties of immunoglobulin G FcTranslating basic mechanisms of IgG effector activity into next generation cancer therapiesTargeting the Fc receptor in autoimmune diseaseUnique carbohydrate-carbohydrate interactions are required for high affinity binding between Fc RIII and antibodies lacking core fucoseStructural Basis for Fc RIIa Recognition of Human IgG and Formation of Inflammatory Signaling ComplexesStructural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycansEngineering Hydrophobic Protein–Carbohydrate Interactions to Fine-Tune Monoclonal AntibodiesFcγ Receptors in Solid Organ TransplantationFc gamma receptors: glycobiology and therapeutic prospectsIn vitro glycoengineering of IgG1 and its effect on Fc receptor binding and ADCC activityGlycoengineering of therapeutic antibodies enhances monocyte/macrophage-mediated phagocytosis and cytotoxicityAssessing Analytical Similarity of Proposed Amgen Biosimilar ABP 501 to AdalimumabIntravital imaging reveals improved Kupffer cell-mediated phagocytosis as a mode of action of glycoengineered anti-CD20 antibodiesFcγRIIB and autoimmunity.Selective clearance of glycoforms of a complex glycoprotein pharmaceutical caused by terminal N-acetylglucosamine is similar in humans and cynomolgus monkeys.A monoclonal antibody with anti-D-like activity in murine immune thrombocytopenia requires Fc domain function for immune thrombocytopenia ameliorative effects.Contribution of Human FcγRs to Disease with Evidence from Human Polymorphisms and Transgenic Animal StudiesIncreasing the efficacy of CD20 antibody therapy through the engineering of a new type II anti-CD20 antibody with enhanced direct and immune effector cell-mediated B-cell cytotoxicityClearance of human IgG1-sensitised red blood cells in vivo in humans relates to the in vitro properties of antibodies from alternative cell lines.Loci associated with N-glycosylation of human immunoglobulin G show pleiotropy with autoimmune diseases and haematological cancers.Galactosyltransferase 4 is a major control point for glycan branching in N-linked glycosylation.Low anti-RhD IgG-Fc-fucosylation in pregnancy: a new variable predicting severity in haemolytic disease of the fetus and newbornSialic acid methylation refines capillary electrophoresis laser-induced fluorescence analyses of immunoglobulin G N-glycans of ovarian cancer patients.EB66 cell line, a duck embryonic stem cell-derived substrate for the industrial production of therapeutic monoclonal antibodies with enhanced ADCC activity.Prophylactic anti-D preparations display variable decreases in Fc-fucosylation of anti-D.High throughput isolation and glycosylation analysis of IgG-variability and heritability of the IgG glycome in three isolated human populations.Chemoenzymatic synthesis and Fcγ receptor binding of homogeneous glycoforms of antibody Fc domain. Presence of a bisecting sugar moiety enhances the affinity of Fc to FcγIIIa receptor.Multi-Angle Effector Function Analysis of Human Monoclonal IgG Glycovariants.7th annual European Antibody Congress 2011: November 29-December 1, 2011, Geneva, Switzerland.Association of systemic lupus erythematosus with decreased immunosuppressive potential of the IgG glycomeStructural characterization of GASDALIE Fc bound to the activating Fc receptor FcγRIIIa.Glycosylation Profile of IgG in Moderate Kidney Dysfunction.In vivo enzymatic modulation of IgG glycosylation inhibits autoimmune disease in an IgG subclass-dependent manner.The N-linked oligosaccharide at Fc gamma RIIIa Asn-45: an inhibitory element for high Fc gamma RIIIa binding affinity to IgG glycoforms lacking core fucosylationHumanised IgG1 antibody variants targeting membrane-bound carcinoembryonic antigen by antibody-dependent cellular cytotoxicity and phagocytosis.Knobs-into-holes antibody production in mammalian cell lines reveals that asymmetric afucosylation is sufficient for full antibody-dependent cellular cytotoxicity.Low-affinity Fcgamma receptors, autoimmunity and infection.Changes in IgG and total plasma protein glycomes in acute systemic inflammation.Glyco-engineered anti-EGFR mAb elicits ADCC by NK cells from colorectal cancer patients irrespective of chemotherapy.
P2860
Q26782025-A8255DF2-AE7B-4022-829C-8F92C361CE05Q26827579-4661FAF5-6CB0-4CB7-9E5D-BEA4190750B2Q26991899-3668C8E4-3C2C-4BC0-9DC2-49DBD858B810Q27002843-648B9FEF-0EB8-47FF-B929-93335860E499Q27670877-4DA9F620-D6B2-4420-968D-F14C028A3EEEQ27671845-22778813-150B-47C2-B1AD-D2D6E3402BD6Q27675205-143D043D-DCA8-4D10-A89B-CCDDF9692574Q27678524-52E1780F-9A35-42AA-B769-E3011F805E38Q28076012-A5A3714C-2E7E-451A-97A4-982B5C985B8AQ28076303-908D80D7-B08C-4D5B-9544-7A79F70C2DD7Q28547176-DCB943DF-7A8A-4B5B-B647-31DCEF9B0F3DQ28658712-09AF9F38-096D-4EAD-B778-5DF714FE16BDQ28831404-17820976-B87F-46A5-8D18-503548C60F51Q30818421-13C44671-4192-47E6-A2F9-28B125D26A2EQ30981881-CB92303C-6A72-45E9-AF68-5CB8AD29D42CQ33276349-6B3DE2E1-B8C0-4528-9447-97B522DCF539Q33420988-F22C6C6E-2332-49CB-B9F7-A7DA3E719E74Q33686907-D77A4844-9C59-4172-AF89-14120933724BQ33896738-C7771487-8DA2-477D-87E1-22DCA9B1E75AQ34323394-81B88F29-D404-4FD7-A125-978AD035CCD2Q34574913-45424AAD-51A0-4649-87DB-A43E7470FC0FQ34589283-3200E74A-F7FC-4763-9A17-868DA8E4B690Q34803358-334B37C7-EA11-4745-8284-C684BF0D0E23Q35165824-D64326C7-B4CD-4725-A5CD-C770D5851DC8Q35232342-2BFC03D5-6293-49EE-A5DE-03F03A1B8A04Q35262648-008F33B7-E9F6-4580-99D8-99D2024362EDQ35497686-1775EE90-E24C-4441-96C2-F94D47480E57Q35555990-6CD5FE3E-EBAF-4314-93B7-4ECEFA51911DQ35866472-D35DB6E5-B2F6-4DC8-B8F1-301B3FDF6BBBQ35992488-3829930D-23C5-43A4-AD20-4CEA43E33A41Q36225198-52C96AB6-3F9B-431A-A7EA-F78570F25CB0Q36624176-58EC66A0-3B84-4B6E-81AF-CB0299ED933CQ36624721-3D1DD52A-5F46-4E05-A048-444913E8814FQ36937137-A3100B3F-7577-4DD8-B5B7-26DE9109945AQ37090829-8F61ACDB-8884-4CC1-A127-C5CD83605B9EQ37424092-9D512A3C-2212-4976-A69F-25FDE5D4C3B7Q37496563-C2B7C79C-DB8B-4B3C-8DF1-52D1F70FD116Q37578785-7130228B-71CD-48D0-AB88-BBFE1BEE3CE1Q37629724-EC0C5D35-CFF9-4B2D-92B0-647FF9AFD63DQ37632159-9A1DA021-B18A-415B-81F4-3ADFEEA74A50
P2860
The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
The carbohydrate at FcgammaRII ...... on-fucosylated IgG glycoforms.
@en
type
label
The carbohydrate at FcgammaRII ...... on-fucosylated IgG glycoforms.
@en
prefLabel
The carbohydrate at FcgammaRII ...... on-fucosylated IgG glycoforms.
@en
P2093
P2860
P356
P1476
The carbohydrate at FcgammaRII ...... on-fucosylated IgG glycoforms.
@en
P2093
Claudia Ferrara
Fiona Stuart
Pablo Umaña
Peter Brünker
Peter Sondermann
P2860
P304
P356
10.1074/JBC.M510171200
P407
P577
2005-12-05T00:00:00Z