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 …

Glycosylation is a prevalent, yet heterogeneous modification with a broad range of
implications in molecular biology. This heterogeneity precludes enrichment strategies that …

Great advances have been made in mass spectrometric data interpretation for intact
glycopeptide analysis. However, accurate identification of intact glycopeptides and modified …

Glycoproteomics is a powerful yet analytically challenging research tool. Software packages
aiding the interpretation of complex glycopeptide tandem mass spectra have appeared, but …

Glycoproteomics, or characterizing glycosylation events at a proteome scale, has seen rapid
advances in methods for analyzing glycopeptides by tandem mass spectrometry in recent …

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 …

Mucin-domain glycoproteins are densely O-glycosylated and play critical roles in a host of
biological functions. In particular, the T cell immunoglobulin and mucin-domain containing …

Epithelial surfaces throughout the body are coated by mucins, a class of proteins carrying
domains characterized by a high density of O-glycosylated serine and threonine residues …

The proteome, or collection of proteoforms expressed in a biological system, is dynamic and
heterogeneous. As our appreciation for the complexity of the proteome has evolved, so have …

Altered protein glycosylation is typically associated with cognitive defects and other
phenotypes, but there is a lack of knowledge about the brain glycoproteome. Here, we used …