Monoclonal therapeutic antibodies have revolutionized the treatment of cancer and other
diseases. Fc engineering aims to enhance the effector functions or half-life of therapeutic …

Rationale: Fc engineering has become the focus of antibody drug development. The current
mutagenesis and in silico protein design methods are confined by the limited throughput …

Since the establishment of monoclonal antibody production using hybridoma technology in
the mid-1970s, there has been expanding progress and continuous technological …

The Fc (crystallizable fragment) region of therapeutic antibodies can have an important role
in their safety and efficacy. Although much is known about the structure–activity relationship …

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

The human fragment crystallizable (Fc) γ receptor (R) interacts with antigen‐complexed
immunoglobulin (Ig) G ligands to both activate and modulate a powerful network of …

Abstract The Fc variant of IgG2, designated as IgG2σ, was engineered with
V234A/G237A/P238S/H268A/V309L/A330S/P331S substitutions to eliminate affinity for Fcγ …

Antibody fragments are emerging as promising biopharmaceuticals because of their
relatively small size and other unique properties. However, compared with full-size …

Several novel technologies have evolved over the last decade for the modification of
antibodies to enhance their inherent effector functions. All focus on the constant Fc domain …

Fc fusion proteins are molecules in which the immunoglobulin Fc is fused genetically to a
protein of interest, such as an extracellular domain of a receptor, ligand, enzyme, or peptide …