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 …

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 …

The physiological identity of every cell is maintained by highly specific transcriptional
networks that establish a coherent molecular program that is in tune with nutritional …

Intermediate filaments (IFs) are cytoskeletal and nucleoskeletal structures that provide
mechanical and stress-coping resilience to cells, contribute to subcellular and tissue-specific …

The hexosamine biosynthetic pathway (HBP) is highly dependent on multiple metabolic
nutrients including glucose, glutamine, and acetyl-CoA. Increased flux through HBP leads to …

In this study, we demonstrated an essential function of the hexosamine biosynthesis
pathway (HBP)–associated O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in …

Post-translational modification with O-linked β-N-acetylglucosamine (O-GlcNAc), a process
referred to as O-GlcNAcylation, occurs on a vast variety of proteins. Mounting evidence in …

Post-translational modifications (PTMs) on proteins often function to regulate signaling
cascades, with the activation of T cells during an adaptive immune response being a classic …