Glycomics aims to identify the structure and function of the glycome, the complete set of
oligosaccharides (glycans), produced in a given cell or organism, as well as to identify …

Glycans expand the structural complexity of proteins by several orders of magnitude,
resulting in a tremendous analytical challenge when including them in biomedical research …

Recent advances in analytical techniques provide the opportunity to quantify even low‐
abundance glycopeptides derived from complex biological mixtures, allowing for the …

Characterization of protein glycosylation by tandem mass spectrometry remains challenging
owing to the vast diversity of oligosaccharides bound to proteins, the variation in …

Mass spectrometry (MS) can unlock crucial insights into the intricate world of glycosylation
analysis. Despite its immense potential, the qualitative and quantitative analysis of isobaric …

Currently, cancer is one of the leading causes of death worldwide, partially owing to the lack
of early diagnosis methods and effective therapies. With the rapid development of various …

Human immunoglobulin G (IgG), which is a major class of globulin antibodies with a typical
immunoglobulin monomer structure, is mainly involved in immune activities such as binding …

Glycoproteomics reveals site-specific O-and N-glycosylation that may influence protein
properties including binding, activity, and half-life. The increasingly mature toolbox with …

Targeted quantification of proteins is a standard methodology with broad utility, but targeted
quantification of glycoproteins has not reached its full potential. The lack of optimized …

LC-MS-based N-glycosylation profiling in four human serum IgG subclasses (IgG1, IgG2,
IgG3, and IgG4) often requires additional affinity-based enrichment of specific IgG …