Protein O-linked β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) is a
unique monosaccharide modification discovered in the early 1980s. With the technological …

The addition of O-linked-β-DN-acetylglucosamine (O-GlcNAc) onto serine and threonine
residues of nuclear and cytoplasmic proteins is an abundant, unique post-translational …

Protein glycosylation fundamentally impacts biological processes. Nontemplated
biosynthesis introduces unparalleled complexity into glycans that needs tools to understand …

O-Linked α-N-acetylgalactosamine (O-GalNAc) glycans constitute a major part of the human
glycome. They are difficult to study because of the complex interplay of 20 distinct …

N-glycans are displayed on cell-surface proteins and can engage in direct binding
interactions with membrane-bound and secreted glycan-binding proteins (GBPs) …

Intermediate filaments (IF) are a major component of the metazoan cytoskeleton and are
essential for normal cell morphology, motility, and signal transduction. Dysregulation of IFs …

O-Linked β-N-acetylglucosamine (O-GlcNAc) is an essential, dynamic monosaccharide post-
translational modification (PTM) found on serine and threonine residues of thousands of …

O-GlcNAcylation is an atypical, reversible, and dynamic glycosylation that plays a critical
role in maintaining the normal physiological functions of cells by regulating various …

N-acetylglucosaminyltransferase-V (GnT-V or MGAT5) catalyzes the formation of an N-
glycan β1, 6-GlcNAc branch on selective target proteins in the Golgi apparatus and is …

Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a reversible
posttranslational modification that regulates the activity of intracellular proteins according to …