Antibodies and Fc-fusion antibody-like proteins have become successful biologics
developed for cancer treatment, passive immunity against infection, addiction, and …

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 …

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 …

Introduction The Fc region of monoclonal antibodies (mAbs) interacts with the CD16a
receptor on natural killer (NK) cells with “low affinity” and “low selectivity”. This low …

The pharmacokinetic properties of antibodies are largely dictated by the pH-dependent
binding of the IgG fragment crystallizable (Fc) domain to the human neonatal Fc receptor …

Background Rituximab is widely used to treat autoimmunity but clinical response varies.
Efficacy is determined by the efficiency of B-cell depletion, which may depend on various Fc …

Although several antibody fragments and antibody fragment-fusion proteins produced in
Escherichia coli (E. coli) are approved as therapeutics for various human diseases, a full …

Fc gamma receptors (FcγRs) are critical effector receptors for immunoglobulin G (IgG)
antibodies. On macrophages, FcγRs mediate multiple effector functions, including …

Despite the exquisite specificity and high affinity of antibody-based cancer therapies,
treatment side effects can occur since the tumor-associated antigens targeted are also …

The loss of CD47 on aging cells serves as a signal to macrophages to eliminate the target.
Therefore, CD47 is a “do-not-eat-me” sign preventing macrophagal phagocytosis via …