IgG-Fc-mediated effector functions: molecular definition of interaction sites for effector ligands and the role of glycosylation.
about
Role of oligosaccharide residues of IgG1-Fc in Fc gamma RIIb bindingStructure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alphaThe 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complexThe structure of a human type III Fcgamma receptor in complex with FcConformational Flexibility in Immunoglobulin E-Fc3–4 Revealed in Multiple Crystal FormsStructural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycansCrystal Structure of an Anti-Ang2 CrossFab Demonstrates Complete Structural and Functional Integrity of the Variable DomainPotent anti-tumor response by targeting B cell maturation antigen (BCMA) in a mouse model of multiple myelomaAdvances in Therapeutic Fc Engineering - Modulation of IgG-Associated Effector Functions and Serum Half-lifeHuman IgG/Fc gamma R interactions are modulated by streptococcal IgG glycan hydrolysisStabilisation of the Fc fragment of human IgG1 by engineered intradomain disulfide bondsBiochemical Characterization of Human Anti-Hepatitis B Monoclonal Antibody Produced in the Microalgae Phaeodactylum tricornutumN-linked glycosylation is essential for the stability but not the signaling function of the interleukin-6 signal transducer glycoprotein 130.Post-translational modifications differentially affect IgG1 conformation and receptor binding.Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity.Pairing of oligosaccharides in the Fc region of immunoglobulin G.Exchanging murine and human immunoglobulin constant chains affects the kinetics and thermodynamics of antigen binding and chimeric antibody autoreactivity.Evolutional selection of a combinatorial phage library displaying randomly-rearranged various single domains of immunoglobulin (Ig)-binding proteins (IBPs) with four kinds of Ig molecules.A monoclonal antibody with anti-D-like activity in murine immune thrombocytopenia requires Fc domain function for immune thrombocytopenia ameliorative effects.Aglycosylated IgG variants expressed in bacteria that selectively bind FcgammaRI potentiate tumor cell killing by monocyte-dendritic cells.Optimized expression of full-length IgG1 antibody in a common E. coli strain.IgG subclass antibodies to human and bacterial HSP60 are not associated with disease activity and progression over time in axial spondyloarthritis.Molecular cloning, characterization, genomic organization and promoter analysis of the α1,6-fucosyltransferase gene (fut8) expressed in the rat hybridoma cell line YB2/0The principle of delivery of T cell epitopes to antigen-presenting cells applied to peptides from influenza virus, ovalbumin, and hen egg lysozyme: implications for peptide vaccination.Overview on the use of therapeutic antibodies in drug discovery.Cleavage of IgG1 and IgG3 by gingipain K from Porphyromonas gingivalis may compromise host defense in progressive periodontitis.Aleuria Aurantia Lectin (AAL)-reactive immunoglobulin G rapidly appears in sera of animals following antigen exposureChemically modified antibodies as diagnostic imaging agentsFc Engineering for Developing Therapeutic Bispecific Antibodies and Novel Scaffolds.Non-fucosylated therapeutic antibodies as next-generation therapeutic antibodies.Change in IgG1 Fc N-linked glycosylation in human lung cancer: age- and sex-related diagnostic potential.Enhancement of antitumor immunity using a DNA-based replicon vaccine derived from Semliki Forest virus.Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity.L-ficolin and capsular polysaccharide-specific IgG in cord serum contribute synergistically to opsonophagocytic killing of serotype III and V group B streptococci.The Structural Role of Antibody N-Glycosylation in Receptor InteractionsEfficient expression of full-length antibodies in the cytoplasm of engineered bacteria.Processing of complex N-glycans in IgG Fc-region is affected by core fucosylationRevisiting the role of glycosylation in the structure of human IgG Fc.CCR4 as a novel molecular target for immunotherapy of cancer.Cleavage of IgG1 in gingival crevicular fluid is associated with the presence of Porphyromonas gingivalis
P2860
Q24291716-300B6AEC-DF4A-41CF-9075-5285E19926EDQ27625567-0A4052AC-9C1A-4DC3-92E5-96CC44003A18Q27625570-55278B22-BD82-4DF1-983E-523308673646Q27631148-F6562395-778E-4CD9-B344-F06B155F9BE6Q27657021-5EBDE71E-4DAB-4F25-9E21-EE5EC1A1AE02Q27675205-7FBE6989-2350-43F3-A1E8-E40C75134F4CQ27677540-76BAC036-01D4-4E39-8F41-9D48047FB1ADQ27700745-C4AE10D6-A1CB-412B-87AE-EBC33D00F876Q28079016-21C0C8A2-485E-4A9E-9D9C-32E46032CEEAQ28471918-7A924C93-3BAA-4FC3-AEA9-6622E6B10423Q28478914-96B402F6-B16E-4AF3-9F45-45208033162DQ28550050-BC496A5E-CA80-4E4C-895D-763A5270C0F8Q30382563-75CEA785-DAF7-490E-B8E8-302FBD937560Q30384877-116B08AF-6F05-4272-8A2A-F22AD9F81063Q30835165-9B50FA34-4064-42EA-A62A-F7167BDB284CQ30872201-B6B37DF2-F6DD-4ED4-92C6-D92A8C3A0859Q33309958-87FEE90A-BF92-4F73-BE98-2D6F625E2842Q33359795-3FACCC72-4830-4157-907C-CA0ACAB07CAFQ33420988-71DF704E-881B-4B67-92C5-0F95C4062C3FQ33524710-969585B8-01B6-4C4F-801E-8FC0D5073274Q33565621-3568384D-2181-4020-8A4F-2EDC05B72012Q33765701-76874BED-0516-44CE-9A9A-7C965269BB2AQ33786180-5B45F096-1E0C-48A3-9BD6-78EBBDC068F4Q33943143-B22B871A-A5A3-41D8-B6B5-ACA2521D4183Q34147273-2F793A2A-04FB-41A7-83EB-141A065048EEQ34201574-2CA4A87B-8FB0-49E3-B112-2FB656FC3574Q34424997-852D4290-6161-40EB-9C72-E4A8B9B8034FQ34441433-F374BBC0-E203-43B6-A9C8-D8CA5245A92DQ34550963-A7137993-126A-4816-9CA8-62E267C499C1Q34574834-2CBF32BD-3884-4AE0-81B5-41E62C4DB751Q34772586-07766C2B-B62F-41AB-9B47-A218A5CFC64FQ35114611-881AB374-9C4B-4F12-912C-1E4E727E56EBQ35850207-8F92D711-50AE-43B7-A517-B16A771DA93DQ36018153-A7D3C540-3CF3-4D88-9CB9-15C30568F571Q36021825-D648C04A-6542-484D-87A2-886D4261AC48Q36030124-39865A72-1843-479B-8BDC-7D5837098062Q36211489-A6E33D6F-B43A-4DB3-8A77-810A204ABE27Q36252642-43544E33-9EB5-4B1B-B3C1-4525F34A9740Q36585299-28DA3F32-5A93-45AE-92BA-2F6C033A9F54Q36592516-6854803F-F750-4EB3-959B-F5BC202544AB
P2860
IgG-Fc-mediated effector functions: molecular definition of interaction sites for effector ligands and the role of glycosylation.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
IgG-Fc-mediated effector funct ...... and the role of glycosylation.
@ast
IgG-Fc-mediated effector funct ...... and the role of glycosylation.
@en
type
label
IgG-Fc-mediated effector funct ...... and the role of glycosylation.
@ast
IgG-Fc-mediated effector funct ...... and the role of glycosylation.
@en
prefLabel
IgG-Fc-mediated effector funct ...... and the role of glycosylation.
@ast
IgG-Fc-mediated effector funct ...... and the role of glycosylation.
@en
P2093
P1476
IgG-Fc-mediated effector funct ...... and the role of glycosylation.
@en
P2093
P356
10.1111/J.1600-065X.1998.TB01188.X
P577
1998-06-01T00:00:00Z