The characterization of glycosylation is critical for obtaining a comprehensive view of the
regulation and functions of glycoproteins of interest. Due to the complex nature of …

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 …

Glycosylation is an important posttranslational modifier of proteins and lipid conjugates
critical for the stability and function of these macromolecules. Particularly important are N …

Alterations of protein glycosylation can serve as sensitive and specific disease biomarkers.
Labeling procedures for improved separation and detectability of oligosaccharides have …

Protein glycosylation is a common post-translational modification that has significant impacts
on protein folding, lifespan, conformation, distribution and function. N-Glycans, which are …

IgG carrying terminal α2, 6-linked sialic acids added to conserved N-glycans within the Fc
domain by the sialyltransferase ST6Gal1 accounts for the anti-inflammatory effects of large …

Abstract Changes in the glycome of human proteins and cells are associated with the
progression of multiple diseases such as Alzheimer's, diabetes mellitus, many types of …

Notes 408 Biographies 408 Acknowledgments 409 References 409 The enormous
structural diversity of glycoconjugates mirrors their myriad biological functions in prokaryotic …

Growing implications of glycosylation in physiological occurrences and human disease have
prompted intensive focus on revealing glycomic perturbations through absolute and relative …

The wide variety of chemical properties and biological functions found in proteins is attained
via post‐translational modifications like glycosylation. Covalently bonded to proteins …