Results 221 to 230 of about 37,468 (260)
Cracking the O-GlcNAc code in metabolism [PDF]
Nuclear, cytoplasmic, and mitochondrial proteins are extensively modified by O-linked β-N-acetylglucosamine (O-GlcNAc) moieties. This sugar modification regulates fundamental cellular processes in response to diverse nutritional and hormonal cues. The enzymes O-GlcNAc transferase (OGT) and O-linked β-N-acetylglucosaminase (O-GlcNAcase) mediate the ...
Hai-Bin Ruan +2 more
exaly +3 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Amino Acids, 2013
O-linked β-N-actylglucosamine (O-GlcNAc) is a carbohydrate post-translational modification on hydroxyl groups of serine and/or threonine residues of cytosolic and nuclear proteins. Analogous to phosphorylation, O-GlcNAcylation plays crucial regulatory roles in a variety of cellular processes.
Zhiyuan, Ma, Keith, Vosseller
openaire +2 more sources
O-linked β-N-actylglucosamine (O-GlcNAc) is a carbohydrate post-translational modification on hydroxyl groups of serine and/or threonine residues of cytosolic and nuclear proteins. Analogous to phosphorylation, O-GlcNAcylation plays crucial regulatory roles in a variety of cellular processes.
Zhiyuan, Ma, Keith, Vosseller
openaire +2 more sources
Localization of the O-GlcNAc transferase and O-GlcNAc-modified proteins in rat cerebellar cortex
Brain Research, 2003O-linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous nucleocytoplasmic protein modification that has a complex interplay with phosphorylation on cytoskeletal proteins, signaling proteins and transcription factors. O-GlcNAc is essential for life at the single cell level, and much indirect evidence suggests it plays an important role in nerve cell ...
Yoshihiro, Akimoto +6 more
openaire +2 more sources
O-GlcNAc site-mapping of liver X receptor-α and O-GlcNAc transferase
Biochemical and Biophysical Research Communications, 2018The Liver X Receptor α (LXRα) belongs to the nuclear receptor superfamily and plays an essential role in regulating cholesterol, lipid and glucose metabolism and inflammatory responses. We have previously shown that LXRα is post-translationally modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) with increased transcriptional activity.
Qiong Fan +6 more
openaire +2 more sources
Targeted protein O-GlcNAc reveals transcriptional functions for O-GlcNAc
Cell Chemical BiologyO-Linked β-N-acetylglucosamine (O-GlcNAc) is an essential nucleocytoplasmic post-translational modification (PTM) installed on many substrates by a single O-GlcNAc transferase (OGT), although functional outcomes for most of these modifications are unknown.
Alison C. Mody +2 more
openaire +2 more sources
2002
Glycosylation of nuclear and cytoplasmic proteins by the addition of a single N- acetylglucosamine monosaccharide (O-GlcNAc) is a major posttranslational modification in higher eukaryotes (Hart 1997). O-GlcNAcylation is characterized by the addition of single GlcNAc residues from a UDP-GlcNAc sugar donor to the hydroxyl groups of serine/threonine ...
Sai Prasad N. Iyer, Gerald W. Hart
openaire +1 more source
Glycosylation of nuclear and cytoplasmic proteins by the addition of a single N- acetylglucosamine monosaccharide (O-GlcNAc) is a major posttranslational modification in higher eukaryotes (Hart 1997). O-GlcNAcylation is characterized by the addition of single GlcNAc residues from a UDP-GlcNAc sugar donor to the hydroxyl groups of serine/threonine ...
Sai Prasad N. Iyer, Gerald W. Hart
openaire +1 more source
Identification of O‐GlcNAc Sites on Proteins
2006O-linked N-acetylglucosamine (O-GlcNAc) is a monosaccharide posttranslational modification that modifies serine/threonine residues of nucleocytoplasmic proteins in metazoans. O-GlcNAc, like phosphorylation, is dynamic and responsive to numerous stimuli in diverse regulatory pathways.
Stephen A, Whelan, Gerald W, Hart
openaire +2 more sources
Structure and function of extracellular O-GlcNAc
Current Opinion in Structural Biology, 2019Extracellular O-GlcNAc is a unique modification restricted to the epidermal growth factor (EGF) domain-containing glycoproteins. This O-GlcNAcylation is catalyzed by the EGF-domain specific O-GlcNAc transferase (EOGT), which is localized in the lumen of endoplasmic reticulum.
Mitsutaka, Ogawa, Tetsuya, Okajima
openaire +2 more sources
Opportunities for Therapeutic Modulation of O-GlcNAc
Chemical ReviewsO-Linked β-N-acetylglucosamine (O-GlcNAc) is an essential, dynamic monosaccharide post-translational modification (PTM) found on serine and threonine residues of thousands of nucleocytoplasmic proteins. The installation and removal of O-GlcNAc is controlled by a single pair of enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), respectively ...
Steven S. Cheng +2 more
openaire +2 more sources
O-GlcNAc informatics: advances and trends
Analytical and Bioanalytical ChemistryAs a post-translational modification, protein glycosylation is critical in health and disease. O-Linked β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation), as an intracellular monosaccharide modification on proteins, was discovered 40 years ago.
Chunyan Hou +3 more
openaire +2 more sources

