A single amino acid substitution abolishes the heterogeneity of chimeric mouse/human (IgG4) antibody

This publication has 24 references indexed in Scilit:

• The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region.
  The Journal of Experimental Medicine, 1991
• Expression of antibody genes in nonlymphoid mammalian cells
  Methods, 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 concentration
  European Journal of Immunology, 1991
• Chimeric B72.3 mouse/human (IgG1) antibody directs the lysis of tumor cells by lymphokine-activated killer cells
  Cancer Immunology, Immunotherapy, 1990
• Site-specific attachment to recombinant antibodies via introduced surface cysteine residues
  Protein Engineering, Design and Selection, 1990
• Human monoclonal IgG isotypes differ in complement activating function at the level of C4 as well as C1q.
  The Journal of Experimental Medicine, 1988
• Comparison of the effector functions of human immunoglobulins using a matched set of chimeric antibodies.
  The Journal of Experimental Medicine, 1987
• Nucleotide Sequence of a Human Immunoglobulin Cγ4 Gene
  DNA, 1981
• Disulphide Bridges of a Human Immunoglobulin G Protein
  Nature, 1967
• Disulphide Bridges of Immunoglobin G1 Heavy Chains
  Nature, 1967