Abstract Engaging inhibitory FcγRIIb by Fc region has been recently reported to be an
attractive approach for improving the efficacy of antibody therapeutics. However, the …

Immunoglobulin G (IgG) Fc receptors play a critical role in linking IgG antibody-mediated
immune responses with cellular effector functions. A high resolution map of the binding site …

Fc engineering is a promising approach to enhance the antitumor efficacy of monoclonal
antibodies (mAbs) through antibody-dependent cell-mediated cytotoxicity (ADCC). Glyco …

IgG isotypes can differentially bind to Fcγ receptors and complement, making the selection of
which isotype to pursue for development of a particular therapeutic antibody important in …

Antibody-dependent cellular cytotoxicity (ADCC) is mediated through the engagement of the
Fc segment of antibodies with Fcγ receptors (FcγRs) on immune cells upon binding of tumor …

Elimination of the binding of immunoglobulin Fc to Fc gamma receptors (FcγR) is highly
desirable for the avoidance of unwanted inflammatory responses to therapeutic antibodies …

Monoclonal antibodies (mAbs) are one of the most widely used drug platforms for infectious
diseases or cancer therapeutics because they selectively target pathogens, infectious cells …

The Fc region of the IgG antibody recruits immune leukocytes or serum complement
molecules, which in turn triggers the clearance of defective cells such as tumor cells or …

Recombinant human IgG antibodies (hIgGs) completely devoid of binding to Fcγ receptors
(FcγRs) and complement protein C1q, and thus with abolished immune effector functions …

The binding sites on human IgG1 for human Fcγ receptor (FcγR) I, FcγRIIa, FcγRIIb, FcγRIIIa
and neonatal FcR have been mapped. A common set of IgG1 residues is involved in binding …