Glycosylation is the most abundant and diverse form of post-translational modification of
proteins that is common to all eukaryotic cells. Enzymatic glycosylation of proteins involves a …

Abstract The Immunoglobulin G (IgG) glycome is well known for its heterogeneity and shows
a significant degree of variation within populations. IgG glycome composition is influenced …

Simple Summary All cells are covered in a thick layer of sugar molecules known as glycans.
Changes to this sugar coat are common in cancer, and in particular cancer cells often …

Immunoglobulin (IgG) glycosylation is a complex enzymatically controlled process, essential
for the structure and function of IgG. IgG glycome is relatively stable in the state of …

Chronic inflammation is the main feature of many long-term inflammatory diseases such as
autoimmune diseases, metabolic disorders, and cancer. There is a growing number of …

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 …

Self-reactive IgGs contribute to the pathology of autoimmune diseases, including systemic
lupus erythematosus and rheumatoid arthritis. Paradoxically, IgGs are used to treat …

Sialylated N-glycans play essential roles in the immune system, pathogen recognition and
cancer. This review approaches the sialylation of N-glycans from three perspectives. The …

Human IgG contains one evolutionarily conserved N-linked glycan in its Fc region at position
297. This glycan is crucial for Fc-mediated functions, including its induction of the classical …

Glycans cover the surfaces of all mammalian cells through a process called glycosylation.
Nearly all proteins and receptors that integrate the intricate series of co-stimulatory/inhibitory …