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 …

Carbohydrates possess a variety of distinct features with stereochemistry playing a
particularly important role in distinguishing their structure and function. Monosaccharide …

Post-translational modifications are an area of great interest in mass spectrometry-based
proteomics, with a surge in methods to detect them in recent years. However, post …

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

Mucin domains are densely O-glycosylated modular protein domains that are found in a
wide variety of cell surface and secreted proteins. Mucin-domain glycoproteins are known to …

Protein glycosylation is a highly important, yet poorly understood protein post-translational
modification. Thousands of possible glycan structures and compositions create potential for …

Protein glycosylation, a complex and heterogeneous post-translational modification that is
frequently dysregulated in disease, has been difficult to analyse at scale. Here we report a …

Cell surface glycosylation has a variety of functions, and its dysregulation in cancer
contributes to impaired signaling, metastasis and the evasion of the immune responses …

Glycosylation, and especially O-linked glycosylation, remains a critical blind spot in the
understanding of post-translational modifications. Due to their nature as proteins defined by …

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 …