Glycosylated human IgG contains fucosylated biantennary N-glycans with different
modifications including N-acetylglucosamine, which bisects the mannose core. Although …

All immunoglobulin G molecules carry N-glycans, which modulate their biological activity.
Changes in N-glycosylation of IgG associate with various diseases and affect the activity of …

Sialylation and sialic acid linkage in N-glycans are markers of disease but are analytically
challenging to quantify. A capillary electrophoresis method is reported that integrates a …

To characterize the structures of N-glycans derived from human serum, we report a strategy
that combines microchip electrophoresis, standard addition, enzymatic digestion, and matrix …

The IgG N-glycome provides sufficient complexity and information content to serve as an
excellent source for biomarker discovery in mammalian health. Since oligosaccharides play …

With mice being the top model organism in immunology and with Fc glycosylation being
increasingly recognized as important modulator of antibody function, the time has come to …

Capillary gel electrophoresis is a widely used method for rapid separation of fluorophore
labeled carbohydrates. Even though, many publications conferred about this popular …

Structural isomers of sialylated N‐glycans contribute to the diversity of the N‐glycome and to
a range of biological functions. Sialyl linkage isomers can be readily distinguished by mass …

All four subclasses of human serum IgG contain a single N‐glycosylation site in the constant
region of their heavy chain, which is occupied by biantennary, largely core‐fucosylated and …

Glycosylation, one of the most common post-translational modifications in mammalian cells,
impacts many biological processes such as cell adhesion, proliferation and differentiation …