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 …

Protein post-translational modifications (PTMs) profoundly influence protein functions and
play crucial roles in essentially all cell biological processes. The diverse realm of PTMs and …

Mass spectrometry is unmatched in its versatility for studying practically any aspect of the
proteome. Because the foundations of mass spectrometry-based proteomics are complex …

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

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

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

In the past decade, relative proteomic quantification using isobaric labeling technology has
developed into a key tool for comparing the expression of proteins in biological samples …

Abstract We report O-Pair Search, an approach to identify O-glycopeptides and localize O-
glycosites. Using paired collision-and electron-based dissociation spectra, O-Pair Search …

Post-translational modifications (PTMs) create vast structural and functional diversity of
proteins, ultimately modulating protein function and degradation, influencing cellular …

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 …