Protein glycosylation involves the co-translational or post-translational addition of glycans to
proteins and is a crucial protein modification in health and disease. The aim of …

Glycomic and glycoproteomic analyses involve the characterization of oligosaccharides
(glycans) conjugated to proteins. Glycans are produced through a complicated nontemplate …

Site-specific characterization of glycosylation requires intact glycopeptide analysis, and
recent efforts have focused on how to best interrogate glycopeptides using tandem mass …

Glycopeptides with unusual glycans or poor peptide backbone fragmentation in tandem
mass spectrometry are unaccounted for in typical site-specific glycoproteomics analysis and …

Chemical tools have accelerated progress in glycoscience, reducing experimental barriers
to studying protein glycosylation, the most widespread and complex form of posttranslational …

Glycosylation is one of the most significant and abundant posttranslational modifications in
mammalian cells. It mediates a wide range of biofunctions, including cell adhesion, cell …

Intact glycopeptide identification has long been known as a key and challenging barrier to
the comprehensive and accurate understanding the role of glycosylation in an organism …

Glycosylation is an important and variable protein modification that can have a profound
effect on the physiological characteristics of the substrate, warranting careful examination in …

Protein glycosylation, an important PTM, plays an essential role in a wide range of biological
processes such as immune response, intercellular signaling, inflammation, and host …

Advances in software-driven glycopeptide identification have facilitated N-glycoproteomics
studies reporting thousands of intact N-glycopeptides, ie, N-glycan-conjugated peptides, but …