The Fab Conformations in the Solution Structure of Human Immunoglobulin G4 (IgG4) Restrict Access to Its Fc Region
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Title
The Fab Conformations in the Solution Structure of Human Immunoglobulin G4 (IgG4) Restrict Access to Its Fc Region
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 289, Issue 30, Pages 20740-20756
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2014-05-30
DOI
10.1074/jbc.m114.572404
References
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Note: Only part of the references are listed.- Structural Determinants of Unique Properties of Human IgG4-Fc
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- Crystal Structure of Fcγ Receptor I and Its Implication in High Affinity γ-Immunoglobulin Binding
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- Species-Specific Determinants in the IgG CH3 Domain Enable Fab-Arm Exchange by Affecting the Noncovalent CH3-CH3 Interaction Strength
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- Mechanism of Immunoglobulin G4 Fab-arm Exchange
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- (2010) Xiaoling Wang et al. mAbs
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- Constrained solution scattering modelling of human antibodies and complement proteins reveals novel biological insights
- (2009) S. J. Perkins et al. Journal of the Royal Society Interface
- Therapeutic IgG4 antibodies engage in Fab-arm exchange with endogenous human IgG4 in vivo
- (2009) Aran F Labrijn et al. NATURE BIOTECHNOLOGY
- Structure determinations of human and chimaeric antibodies by solution scattering and constrained molecular modelling
- (2008) Stephen J. Perkins et al. BIOCHEMICAL SOCIETY TRANSACTIONS
- Specificity and affinity of human Fc receptors and their polymorphic variants for human IgG subclasses
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- The Effect of a Point Mutation on the Stability of IgG4 as Monitored by Analytical Ultracentrifugation
- (2007) Yanling Lu et al. JOURNAL OF PHARMACEUTICAL SCIENCES
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