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Scholar Results 1 - 10 of about 101 related to Wang: Site-Specific GlcNAcylation of Human Erythrocyte Proteins. (0.18 sec) 

Site-Specific GlcNAcylation of Human Erythrocyte Proteins


Z Wang, K Park, F Comer, LC Hsieh-Wilson, … - Diabetes, 2009 - Am Diabetes Assoc
RESEARCH DESIGN AND METHODS—GlcNAcylated erythrocyte proteins or GlcNAcylated
peptides were tagged and selectively enriched by a chemoenzymatic approach and
identified by mass spectrometry. The enrichment approach was combined with ...
Related articles - All 4 versions

Insulin Acutely Regulates Munc 18-c Subcellular Trafficking. ALTERED RESPONSE IN …


BA Nelson, KA Robinson, MG Buse - Journal of Biological Chemistry, 2002 - ASBMB
Preincubation of 3T3-L1 adipocytes in high glucose or glucosamine decreases
acute insulin (100 nM)-stimulated glucose transport provided that insulin (0.6
nM) is included during preincubation. GLUT4 expression is unchanged ...
Cited by 10 - Related articles - BL Direct - All 4 versions

Reduction of O-GlcNAc protein modification does not prevent insulin resistance in 3T3-L1 …

- physiology.org
KA Robinson, LE Ball, MG Buse - American Journal of Physiology- Endocrinology And …, 2007 - Am Physiological Soc
3T3-L1 adipocytes develop insulin-resistant glucose transport upon preincubation
with high (25 mM) glucose, provided that insulin (0.6 nM) is included, Akt
activation is impaired, and high glucose and insulin act synergistically. ...
Cited by 10 - Related articles - BL Direct - All 6 versions

Glycomic approaches to study GlcNAcylation: protein identification, site-mapping, and site- …


Z Wang, GW Hart - Clinical Proteomics, 2008 - Springer
Abstract Background O-Linked β-N-acetylglucosamine (O-GlcNAc) is an
enzyme-catalyzed posttranslational modification of serine or threonine side
chains of nuclear and cytoplasmic proteins. O-GlcNAc is present in all ...
Cited by 3 - Related articles

[CITATION] Continuous glucose excursions in everyday living: normal, pre-diabetes, and mild type 2 …


C Chia, BC Astor, CD Saudek - Diabetes, 2004
Cited by 3 - Related articles

Impaired fasting glucose with or without impaired glucose tolerance: progressive or parallel …

- physiology.org
L Perreault, BC Bergman, MC Playdon, C … - American Journal of Physiology- Endocrinology And …, 2008 - Am Physiological Soc
Our objective was to determine whether defects underlying impaired fasting
glucose (IFG) are maintained and additive when combined with impaired glucose
tolerance (IGT) (representing a progressive form of prediabetes) or are ...
Cited by 2 - Related articles - All 5 versions

Cross-talk between GlcNAcylation and phosphorylation: Site-specific phosphorylation …

- Free from Publisher
Z Wang, M Gucek, GW Hart - Proceedings of the National Academy of Sciences, 2008 - nihongo.j-talk.com
Protein GlcNAcylation serves as a nutrient/stress sensor to modulate the
functions of many nuclear and cytoplasmic proteins. O-GlcNAc cycles on serine or
threonine residues like phosphorylation, is nearly as abundant, and ...
Cited by 12 - Related articles - All 8 versions

Cross-talk between GlcNAcylation and phosphorylation: roles in insulin resistance and …

- physiology.org
RJ Copeland, JW Bullen, GW Hart - American Journal of Physiology- Endocrinology And …, 2008 - Am Physiological Soc
O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic posttranslational
modification that, analogous to phosphorylation, cycles on and off serine and/or
threonine hydroxyl groups. Cycling of O-GlcNAc is regulated by the ...
Cited by 16 - Related articles - All 3 versions

Molecular convergence of hexosamine biosynthetic pathway and ER stress leading to insulin …


V Srinivasan, U Tatu, V Mohan, M … - Molecular and Cellular Biochemistry, 2009 - Springer
Abstract Augmentation of hexosamine biosynthetic pathway (HBP) and endoplasmic
reticulum (ER) stress were independently related to be the underlying causes of
insulin resistance. We hypothesized that there might be a molecular ...
Related articles

Structure of an O-GlcNAc transferase homolog provides insight into intracellular …


C Martinez-Fleites, MS Macauley, Y He, DL … - Nature structural & molecular biology, 2008 - ncbi.nlm.nih.gov
1: Nat Struct Mol Biol. 2008 Jul;15(7):764-5. Epub 2008 Jun 8. Structure of an
O-GlcNAc transferase homolog provides insight into intracellular glycosylation. ...
Cited by 12 - Related articles - All 3 versions


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