It has been more than three decades since the first monoclonal antibody was approved by
the United States Food and Drug Administration (US FDA) in 1986, and during this time …

Antibody–drug conjugates (ADCs) harness the highly specific targeting capabilities of an
antibody to deliver a cytotoxic payload to specific cell types. They have garnered …

The glycome describes the complete repertoire of glycoconjugates composed of
carbohydrate chains, or glycans, that are covalently linked to lipid or protein molecules …

Glycoconjugates are major constituents of mammalian cells that are formed via covalent
conjugation of carbohydrates to other biomolecules like proteins and lipids and often …

Therapeutic monoclonal antibodies are the fastest growing class of biological therapeutics
for the treatment of various cancers and inflammatory disorders. In cancer immunotherapy …

IgG antibodies contain a conserved N-glycosylation site on the Fc domain to which a
complex, biantennary glycan is attached. The fine structures of this glycan modulate …

Glycosylation is one of the most prevalent posttranslational modifications that profoundly
affects the structure and functions of proteins in a wide variety of biological recognition …

IgG glycosylation is currently at the forefront of both immunology and glycobiology, likely due
in part to the widespread and growing use of antibodies as drugs. For over four decades, it …

IgG3 comprises only a minor fraction of IgG and has remained relatively understudied until
recent years. Key physiochemical characteristics of IgG3 include an elongated hinge region …

Glycosylation of the Fc region of IgG has a profound impact on the safety and clinical efficacy
of therapeutic antibodies. While the biantennary complex-type oligosaccharide attached to …