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 …

Abstract Coronavirus disease 2019 (COVID-19), a highly infectious disease caused by
severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has infected more than …

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 …

Cells encode information in the sequence of biopolymers, such as nucleic acids, proteins,
and glycans. Although glycans are essential to all living organisms, surprisingly little is …

Upregulation of sialyltransferases—the enzymes responsible for the addition of sialic acid to
growing glycoconjugate chains—and the resultant hypersialylation of up to 40–60% of …

Recent advances in methods for enrichment and mass spectrometric analysis of intact
glycopeptides have produced large-scale glycoproteomics datasets, but interpreting these …

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 …

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

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 …