The structural requirements for complement activation by IgG: does it hinge on the hinge?
- 31 December 1995
- journal article
- review article
- Published by Elsevier BV in Immunology Today
- Vol. 16 (2), 85-90
- https://doi.org/10.1016/0167-5699(95)80094-8
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Dynamical Structure of the Hinge Region of Immunoglobulin G as Studied by 13C Nuclear Magnetic Resonance SpectroscopyJournal of Molecular Biology, 1994
- Structural features of human immunoglobulin G that determine isotype-specific differences in complement activation.The Journal of Experimental Medicine, 1993
- The extended hinge region of IgG3 is not required for high phagocytic capacity mediated by Fcγ receptors, but the heavy chains must be disulfide bondedEuropean Journal of Immunology, 1993
- Structural motifs involved in human IgG antibody effector functionsEuropean Journal of Immunology, 1993
- A genetically engineered human IgG with limited flexibility fully initiates cytolysis via complementMolecular Immunology, 1993
- Chimeric mouse human IgG3 antibodies with an IgG4-like hinge region induce complement-mediated lysis more efficiently than IgG3 with normal hingEuropean Journal of Immunology, 1991
- Human IgG subclass pattern of inducing complement‐mediated cytolysis depends on antigen concentration and to a lesser extent on epitope patchiness, antibody affinity and complement concentrationEuropean Journal of Immunology, 1991
- Preparation and biologic characterization of fragments containing dimeric and monomeric Cγ2 domain of rabbit IgGMolecular Immunology, 1985
- Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolutionJournal of Molecular Biology, 1980
- Indications That the Cγ2 Homology Region Is Not a Regular DomainScandinavian Journal of Immunology, 1976