GW Hart, MP Housley, C Slawson - Nature, 2007 - nature.com All animals and plants dynamically attach and remove O-linked
-N-acetylglucosamine (O-GlcNAc) at serine and threonine residues on myriad
nuclear and cytoplasmic proteins. O-GlcNAc cycling, which is tightly ... Cited by 130 - Related articles - BL Direct - All 6 versions
- ►physiology.org MG Buse - American Journal of Physiology- Endocrinology And …, 2006 - Am Physiological Soc The hexosamine biosynthesis pathway (HBP) is a relatively minor branch of
glycolysis. Fructose 6-phosphate is converted to glucosamine 6-phosphate,
catalyzed by the first and rate-limiting enzyme ... Cited by 79 - Related articles - BL Direct - All 6 versions
- ►sciencesignaling.org DC Love, JA Hanover - Science's STKE, 2005 - stke.sciencemag.org Note to users. If you're seeing this message, it means that your browser cannot
find this page's style/presentation instructions -- or possibly that you are
using a browser that does not support current Web standards. Find out more ... Cited by 69 - Related articles - All 12 versions
C Slawson, MP Housley, GW Hart - Journal of cellular biochemistry, 2006 - interscience.wiley.com O-GlcNAc is an ubiquitous post-translational protein modification consisting of
a single N-acetlyglucosamine moiety linked to serine or threonine residues on
nuclear and cytoplasmic proteins. Recent work has begun to uncover the ... Cited by 65 - Related articles - BL Direct - All 5 versions
X Yang, PP Ongusaha, PD Miles, JC Havstad, … - NATURE-LONDON-, 2008 - sethfield.ucsd.edu Glucose flux through the hexosamine biosynthetic pathway leads to the
post-translational modification of cytoplasmic and nuclear proteins by O-linked
bN-acetylglucosamine (O-GlcNAc). This tandem system serves as a nutrient ... Cited by 50 - Related articles - View as HTML - BL Direct - All 8 versions
- ►shouxi.net DM Lehman, KJ Hunt, RJ Leach, J Hamlington, … - Diabetes, 2007 - Am Diabetes Assoc TCF7L2 acts as both a repressor and transactivator of genes, as directed by the
Wnt signaling pathway. Recently, several highly correlated sequence variants
located within a haplotype block of the TCF7L2 gene were observed to ... Cited by 49 - Related articles - BL Direct - All 4 versions
- ►cardiovascres.org N Fulop, RB Marchase, JC Chatham - Cardiovascular research, 2007 - cardiovascres.org There is growing recognition that the O-linked attachment of
N-acetyl-glucosamine (O-GlcNAc) on serine and threonine residues of nuclear and
cytoplasmic proteins is a highly dynamic post-translational modification ... Cited by 36 - Related articles - All 7 versions
RJ Dennis, EJ Taylor, MS Macauley, KA … - Nat Struct Mol Biol, 2006 - northumbria.openrepository.com O-GlcNAc is an abundant post-translational modification of serine and threonine
residues of nucleocytoplasmic proteins. This modification, found only within
higher eukaryotes, is a dynamic modification that is often reciprocal to ... Cited by 33 - Related articles - All 7 versions
JE Kudlow - Journal of cellular biochemistry, 2006 - interscience.wiley.com Modification of intracellular proteins by the -linkage of the monosaccharide,
N-acetylglucosamine to serine or threonine hydroxyls (O-GlcNAc) is abundant and
reversible. Although many proteins bear this post-translational covalent ... Cited by 25 - Related articles - BL Direct - All 5 versions
WB Dias, GW Hart - Molecular BioSystems, 2007 - rsc.org Similar to phosphorylation, O-GlcNAcylation (or simply GlcNAcylation) is an
abundant, dynamic, and inducible post-translational modification. In some cases,
GlcNAcylation and phosphorylation occur at the same or adjacent sites, ... Cited by 23 - Related articles - Cached - BL Direct - All 4 versions
