Frontiers in Immunology, 2016 The monospecific and bivalent characteristics of naturally occurring immunoglobulin G (IgG) antibodies depend on homodimerization of the fragment crystallizable (Fc) regions of two identical heavy chains (HCs) and the subsequent assembly of two identical
Ji-Hee Ha, Jung-Eun Kim, Yong-Sung Kim
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13C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G [PDF]
FEBS Letters, 1923 The mode of interaction of the B domain (FB) of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G (IgG) has been investigated by 13C NMR spectroscopy.
Langone +22 more
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The Fab region of IgG impairs the internalization pathway of FcRn upon Fc engagement
Nature Communications, 2022 Disrupting the association between the Immunoglobulin G constant fragment (Fc) and the neonatal Fc receptor (FcRn) by engineered antibodies is a promising strategy to reduce autoantibody levels in autoimmune diseases.
Maximilian Brinkhaus +13 more
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Frontiers in Immunology, 2017 Binding of the complement component C1q to the CH2 domain of antigen-bound immunoglobulin gamma (IgG) activates the classical complement pathway and depends on its close proximity to Fc fragments of neighboring antibodies. IgG subclasses contain a highly
Benjamin Peschke +6 more
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The herpes virus Fc receptor gE-gI mediates antibody bipolar bridging to clear viral antigens from the cell surface. [PDF]
PLoS Pathogens, 2014 The Herpes Simplex Virus 1 (HSV-1) glycoprotein gE-gI is a transmembrane Fc receptor found on the surface of infected cells and virions that binds human immunoglobulin G (hIgG).
Blaise Ndjamen +4 more
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Altered IgG N-Glycosylation at Onset of Type 1 Diabetes in Children Is Predominantly Driven by Changes in the Fab N-Glycans [PDF]
BiomedicinesBackground: N-glycosylation is a post-translational modification involving the attachment of oligosaccharides to proteins and is known to influence immunoglobulin G (IgG) effector functions and even antigen binding.
Branimir Plavša +3 more
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Role of Fc fragments in inhibition of xenogenic hyperacute rejection by intravenous immunoglobulin.
Transplantation, 1996 It has been shown that a high dose administration of human intravenous immunoglobulin G (IVIG) prolonged the survival time of xenografted guinea pig heart in the rat. In this study, we compared the effectiveness of intact IVIG (I-IVIG), Fc fragments of IVIG (Fc-IVIG), and F(ab') fragments of IVIG (Fab-IVIG) in preventing xenogenic hyperacute rejection ...
T. Kojima +3 more
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Customized extracellular vesicles targeting lysosomal biogenesis deliver therapeutic cargo for intervertebral disc degeneration treatment [PDF]
Journal of NanobiotechnologyExtracellular vesicles (EVs) have gained prominence as advanced drug delivery systems due to their inherent merits. Recent advancements highlight their utility in transporting therapeutic proteins with significant progress in targeted therapies.
Zhiwei Liao +4 more
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Fc Engineering for Developing Therapeutic Bispecific Antibodies and Novel Scaffolds [PDF]
Frontiers in Immunology, 2017 Therapeutic monoclonal antibodies have become molecules of choice to treat autoimmune disorders, inflammatory diseases, and cancer. Moreover, bispecific/multispecific antibodies that target more than one antigen or epitope on a target cell or recruit ...
Abhishek Saxena +3 more
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Effect of IgG fragments in IVIG(pH4)on phagocytosis of sensitized erythrocytes by macrophage
Zhongguo shuxue zazhi, 2022 Objective To research the effect of the Fc, Fab and F(ab′)2 fragments of immunoglobulin G, the main components of Human Immunoglobulin(pH4) for Intravenous Injection(IVIG), on the phagocytic function of macrophages derived from THP-1 cells. Methods First
Liyuan ZHU +6 more
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