O-GlcNAcylation—the attachment of O-linked N-acetylglucosamine (O-GlcNAc) moieties to
cytoplasmic, nuclear and mitochondrial proteins—is a post-translational modification that …

More and more in-depth studies have revealed that the occurrence and development of
tumors depend on gene mutation and tumor heterogeneity. The most important …

The clinical correlations linking diabetes mellitus with accelerated atherosclerosis,
cardiomyopathy, and increased post-myocardial infarction fatality rates are increasingly …

Altered metabolism and deregulated cellular energetics are now considered a hallmark of
all cancers. Glucose, glutamine, fatty acids, and amino acids are the primary drivers of tumor …

While acute myeloid leukemia (AML) comprises many disparate genetic subtypes, one
shared hallmark is the arrest of leukemic myeloblasts at an immature and self-renewing …

In the mid-1980s, the identification of serine and threonine residues on nuclear and
cytoplasmic proteins modified by a N-acetylglucosamine moiety (O-GlcNAc) via an O …

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

O-GlcNAcylation is a posttranslational modification that adds O-linked β-N-
acetylglucosamine (O-GlcNAc) to serine or threonine residues of many proteins. This protein …

Immune cell differentiation and function are crucially dependent on specific metabolic
programs dictated by mitochondria, including the generation of ATP from the oxidation of …

Simple and complex carbohydrates (glycans) have long been known to play major
metabolic, structural and physical roles in biological systems. Targeted microbial binding to …