Protein O-GlcNAcylation is a non-canonical glycosylation of nuclear, mitochondrial, and cytoplasmic proteins with the attachment of a single O-linked β-N-acetyl-glucosamine (O-GlcNAc) moiety. Advances in labeling and identifying O-GlcNAcylated proteins have helped improve the understanding of O-GlcNAcylation at levels that range from basic molecular biology to cell signaling and gene regulation to physiology and disease. This review describes these advances in chemistry involving chemical reporters and their bioorthogonal reactions utilized for detection and construction of O-GlcNAc proteomes in a molecular mechanistic view. This detailed view will help better understand the principles of the chemistries utilized for biology discovery ...
O-GlcNAcylation is dynamic and a ubiquitous post-translational modification. O-GlcNAcylated proteins...
The addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to serine/threonine residues of proteins i...
Protein O-GlcNAcylation is an abundant post-translational modification of intracellular proteins wit...
Protein O-GlcNAcylation is a non-canonical glycosylation of nuclear, mitochondrial, and cytoplasmic ...
The concepts of both protein glycosylation and cellular signaling have been influenced by O-linked-β...
The modification on proteins with O-linked N-acetyl-β-D-glucosamine (O-GlcNAcylation) is essential f...
The attachment of N-acetylglucosamine to serine or thre-onine residues (O-GlcNAc) is a post-translat...
The dynamic posttranslational modification of proteins by O-linked-b-N-acetylglucosamine (O-GlcNAcyl...
The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in t...
The modification of proteins with O-linked N-acetylglucosamine residues (O-GlcNAc) is found on many ...
Abstract Background Protein O-GlcNAcylation (or O-GlcNAc-ylation) is an O-linked glycosylation invol...
Protein glycosylation is one of the most abundant posttransla-tional modifications and plays a funda...
The development of tools, techniques and methods has been important to the evolution of glycobiology...
O-linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous post-translational modification of proteins ...
International audienceMetabolic chemical reporters (MCRs) of glycosylation are analogues of monosacc...
O-GlcNAcylation is dynamic and a ubiquitous post-translational modification. O-GlcNAcylated proteins...
The addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to serine/threonine residues of proteins i...
Protein O-GlcNAcylation is an abundant post-translational modification of intracellular proteins wit...
Protein O-GlcNAcylation is a non-canonical glycosylation of nuclear, mitochondrial, and cytoplasmic ...
The concepts of both protein glycosylation and cellular signaling have been influenced by O-linked-β...
The modification on proteins with O-linked N-acetyl-β-D-glucosamine (O-GlcNAcylation) is essential f...
The attachment of N-acetylglucosamine to serine or thre-onine residues (O-GlcNAc) is a post-translat...
The dynamic posttranslational modification of proteins by O-linked-b-N-acetylglucosamine (O-GlcNAcyl...
The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in t...
The modification of proteins with O-linked N-acetylglucosamine residues (O-GlcNAc) is found on many ...
Abstract Background Protein O-GlcNAcylation (or O-GlcNAc-ylation) is an O-linked glycosylation invol...
Protein glycosylation is one of the most abundant posttransla-tional modifications and plays a funda...
The development of tools, techniques and methods has been important to the evolution of glycobiology...
O-linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous post-translational modification of proteins ...
International audienceMetabolic chemical reporters (MCRs) of glycosylation are analogues of monosacc...
O-GlcNAcylation is dynamic and a ubiquitous post-translational modification. O-GlcNAcylated proteins...
The addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to serine/threonine residues of proteins i...
Protein O-GlcNAcylation is an abundant post-translational modification of intracellular proteins wit...