[HTML][HTML] Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation

P Hu, S Shimoji, GW Hart - FEBS letters, 2010 - Elsevier
Ser (Thr)-O-linked β-N-acetylglucosamine (O-GlcNAc) is a ubiquitous modification of
nucleocytoplasmic proteins. Extensive crosstalk exists between O-GlcNAcylation and …

Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease

GW Hart, C Slawson, G Ramirez-Correa… - Annual review of …, 2011 - annualreviews.org
O-GlcNAcylation is the addition of β-DN-acetylglucosamine to serine or threonine residues
of nuclear and cytoplasmic proteins. O-linked N-acetylglucosamine (O-GlcNAc) was not …

O-linked β-N-acetylglucosamine (O-GlcNAc): extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress

C Butkinaree, K Park, GW Hart - … et Biophysica Acta (BBA)-General Subjects, 2010 - Elsevier
BACKGROUND: Since its discovery in the early 1980s, O-linked-β-N-acetylglucosamine (O-
GlcNAc), a single sugar modification on the hydroxyl group of serine or threonine residues …

Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation

Z Wang, A Pandey, GW Hart - Molecular & Cellular Proteomics, 2007 - ASBMB
O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is
dynamically regulated in response to various environmental and biological stimuli. O …

Metabolic cross-talk allows labeling of O-linked β-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway

M Boyce, IS Carrico, AS Ganguli… - Proceedings of the …, 2011 - National Acad Sciences
Hundreds of mammalian nuclear and cytoplasmic proteins are reversibly glycosylated by O-
linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and …

Nutrient regulation of signaling, transcription, and cell physiology by O-GlcNAcylation

S Hardivillé, GW Hart - Cell metabolism, 2014 - cell.com
The nutrient sensor, O-linked N-acetylglucosamine (O-GlcNAc), cycles on and off nuclear
and cytosolic proteins to regulate many cellular processes, including transcription and …

The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways

Q Zeidan, GW Hart - Journal of cell science, 2010 - journals.biologists.com
A paradigm-changing discovery in biology came about when it was found that nuclear and
cytosolic proteins could be dynamically glycosylated with a single O-linked β-N …

[HTML][HTML] O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar

L Wells, GW Hart - FEBS letters, 2003 - Elsevier
O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic nucleocytoplasmic post-
translational modification more analogous to phosphorylation than to classical complex O …

Nucleocytoplasmic O-glycosylation: O-GlcNAc and functional proteomics

K Vosseller, L Wells, GW Hart - Biochimie, 2001 - Elsevier
The molecular complexity that defines different cell types and their biological responses
occurs at the level of the cell's proteome. The recent increase in availability of genomic …

Protein O-GlcNAcylation: emerging mechanisms and functions

X Yang, K Qian - Nature reviews Molecular cell biology, 2017 - nature.com
O-GlcNAcylation—the attachment of O-linked N-acetylglucosamine (O-GlcNAc) moieties to
cytoplasmic, nuclear and mitochondrial proteins—is a post-translational modification that …