Glycans are involved in numerous biological recognition events. Being secondary gene
products, their labeling by genetic methods–comparable to GFP labeling of proteins–is not …

The surface of all living cells is decorated with carbohydrate molecules. Hundreds of
functional proteins bind to these glycosylated ligands; such binding events subsequently …

Post-translational modifications (PTMs) immensely expand the diversity of the proteome.
Glycosylation, among the most ubiquitous PTMs, is a dynamic and multifarious modification …

Tools to interrogate glycoconjugate–protein interactions in the context of living cells are
highly attractive for the identification of critically important functional binding partners of …

Glycan recognition by glycan‐binding proteins is central to the biology of all living
organisms. The efficient capture and characterization of relatively weak non‐covalent …

Glycosylation is one of the most common and important protein modifications, and it
regulates the properties and functions of a wide range of proteins. Aberrant glycosylation is …

Human milk oligosaccharides (HMOs) are a family of unconjugated soluble glycans found in
human breast milk that exhibit a myriad of biological activity. While recent studies have …

Exo-enzymatic glyco-engineering of cell-surface glycoconjugates enables the selective
display of well-defined glyco-motifs bearing bioorthogonal functional groups, which can be …

Glycan binding often mediates extracellular macromolecular recognition events. Accurate
characterization of these binding interactions can be difficult because of dissociation and …

Glycosylation is a ubiquitous post-translational modification read by glycan-binding proteins
(GBP) to encode important functions, but a robust understanding of these interactions and …