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 …

Inhibition of O-GlcNAcase (OGA) has emerged as a promising therapeutic approach to treat
tau pathology in neurodegenerative diseases such as Alzheimer's disease and progressive …

In the past few decades, our understanding of glycan information‐encoding power has
notably increased, thus leading to a significant growth also in the design and synthesis of …

The lytic transglycosylases (LTs) are bacterial enzymes that catalyze the non-hydrolytic
cleavage of the peptidoglycan structures of the bacterial cell wall. They are not catalysts of …

Glycosyltransferases are a superfamily of enzymes that are notoriously difficult to inhibit.
Here we apply an mRNA display technology integrated with genetic code reprogramming …

O-GlcNAc is a common modification found on nuclear and cytoplasmic proteins.
Determining the catalytic mechanism of the enzyme O-GlcNAcase (OGA), which removes O …

O-GlcNAc hydrolase (OGA) removes O-linked N-acetylglucosamine (O-GlcNAc) from a
myriad of nucleocytoplasmic proteins. Through co-expression and assembly of OGA …

Introduction: O-GlcNAcylation is a highly abundant post-translational modification of multiple
proteins, including the microtubule-binding protein tau, governed by just two enzymes' …

Highlights•Good cell active competitive inhibitors of O-GlcNAc processing enzymes are
available.•In vitro assays for O-GlcNAc processing enzymes are established.•OGA inhibitors …