The pH-selective interaction between the immunoglobulin G (IgG) fragment crystallizable
region (Fc region) and the neonatal Fc receptor (FcRn) is critical for prolonging the …

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

Interactions between the crystallizable fragment (Fc) domain of antibodies and a plethora of
cellular Fc receptors (FcRs) or soluble proteins form a critical link between humoral and …

The in vivo biological activities of IgG antibodies result from their bifunctional nature, in
which antigen recognition by the Fab is coupled to the effector and immunomodulatory …

Autoantibody immune complex (IC) activation of Fcγ receptors (FcγRs) is a common
pathogenic hallmark of multiple autoimmune diseases. Given that the IC structural features …

Antibody‐based immunotherapies are becoming powerful means of modern medicine for
treating cancers and autoimmune diseases. The increasing popularity of antibody‐based …

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

Antibody interactions with Fcγ receptors (FcγRs), like FcγRIIIA, play a critical role in
mediating antibody effector functions and thereby contribute significantly to the biologic and …

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 …

Yeast surface display libraries of human IgG1 Fc regions were prepared in which loop
sequences at the C-terminal tip of the CH3 domain were randomized. A high percentage of …