Nutrient regulation of signaling and transcription
GW Hart - Journal of Biological Chemistry, 2019 - ASBMB
In the early 1980s, while using purified glycosyltransferases to probe glycan structures on
surfaces of living cells in the murine immune system, we discovered a novel form of …
surfaces of living cells in the murine immune system, we discovered a novel form of …
Analytical and biochemical perspectives of protein O-GlcNAcylation
Protein O-linked β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) is a
unique monosaccharide modification discovered in the early 1980s. With the technological …
unique monosaccharide modification discovered in the early 1980s. With the technological …
Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease
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 …
of nuclear and cytoplasmic proteins. O-linked N-acetylglucosamine (O-GlcNAc) was not …
Protein glycosylation: structural and functional aspects
H Lis, N Sharon - European journal of biochemistry, 1993 - Wiley Online Library
During the last decade, there have been enormous advances in our knowledge of
glycoproteins and the stage has been set for the biotechnological production of many of …
glycoproteins and the stage has been set for the biotechnological production of many of …
Demystifying the O-GlcNAc code: a systems view
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 …
referred to as O-GlcNAcylation, occurs on a vast variety of proteins. Mounting evidence in …
Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic β-N-acetylglucosaminidase from human brain
Dynamic modification of cytoplasmic and nuclear proteins by O-linked N-acetylglucosamine
(O-GlcNAc) on Ser/Thr residues is ubiquitous in higher eukaryotes and is analogous to …
(O-GlcNAc) on Ser/Thr residues is ubiquitous in higher eukaryotes and is analogous to …
O-GlcNAc profiling: from proteins to proteomes
Abstract O-linked β-DN-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) onto
serine and threonine residues of proteins is an important post-translational modification …
serine and threonine residues of proteins is an important post-translational modification …
Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol.
DL Dong, GW Hart - Journal of Biological Chemistry, 1994 - ASBMB
Glycosylation of nuclear and cytoplasmic proteins by O-linked N-acetylglucosamine (O-
GlcNAc) monosaccharides is an abundant, ubiquitous, and transient post-translational …
GlcNAc) monosaccharides is an abundant, ubiquitous, and transient post-translational …
O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress
NE Zachara, GW Hart - Biochimica et Biophysica Acta (BBA)-General …, 2004 - Elsevier
Myriad nuclear and cytoplasmic proteins in metazoans are modified on Ser and Thr residues
by the monosaccharide O-linked β-N-acetylglucosamine (O-GlcNAc). The rapid and …
by the monosaccharide O-linked β-N-acetylglucosamine (O-GlcNAc). The rapid and …
Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
GW Hart - Annual review of biochemistry, 1997 - annualreviews.org
Modification of Ser and Thr residues by attachment of O-linked N-acetylglucosamine [Ser
(Thr)-O-GlcNAcylation] to eukaryotic nuclear and cytosolic proteins is as dynamic and …
(Thr)-O-GlcNAcylation] to eukaryotic nuclear and cytosolic proteins is as dynamic and …