Immunoglobulin G (IgG)-based drugs are arguably the most successful class of protein
therapeutics due in part to their remarkably long blood circulation. This arises from IgG …

The neonatal Fc receptor (FcRn) is expressed by cells of epithelial, endothelial and myeloid
lineages and performs multiple roles in adaptive immunity. Characterizing the FcRn/IgG …

Binding to the neonatal Fc receptor (FcRn) extends serum half-life of IgG, and antagonizing
this interaction is a promising therapeutic approach in IgG-mediated autoimmune diseases …

The neonatal Fc receptor (FcRn) plays a critical role in regulating IgG homeostasis in vivo.
There are mixed reports on whether modification of the interaction with FcRn can be used as …

The neonatal Fc receptor FcRn provides IgG molecules with their characteristically long half-
lives in vivo by protecting them from intracellular catabolism and then returning them to the …

The maintenance of the homeostasis of immunoglobulin G (IgG) represents a fundamental
aspect of humoral immunity that has direct relevance to the successful delivery of antibody …

The neonatal crystallizable fragment receptor (FcRn) functions as an intracellular protection
receptor for immunoglobulin G (IgG). Recently, several clinical studies have reported the …

It is well established that the neonatal Fc receptor (FcRn) plays a critical role in regulating
IgG homeostasis in vivo. As such, modification of the interaction of IgG with FcRn has been …

Many biological functions, including control of the homeostasis and maternofetal transfer of
serum γ-globulins, are mediated by the MHC class I-related neonatal FcR (FcRn). A …

Summary The neonatal Fc receptor, FcRn, is best known for its role in transporting IgG in
various tissues, providing newborns with humoral immunity, and for prolonging the half‐life …