Insulin resistance of glycogen synthase mediated by o-linked N-acetylglucosamine. - Wikidata - awgldk - TriplyDB

Insulin resistance of glycogen synthase mediated by o-linked N-acetylglucosamine.

Insulin resistance of glycogen synthase mediated by o-linked N-acetylglucosamine.

http://www.wikidata.org/entity/Q42435341

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Hexosamines, insulin resistance, and the complications of diabetes: current status.Regulation of glucose and glycogen metabolism during and after exercise Functional O-GlcNAc modifications: implications in molecular regulation and pathophysiology Structure of a bacterial putative acetyltransferase defines the fold of the human O-GlcNAcase C-terminal domain Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress High glucose-induced O-GlcNAcylated carbohydrate response element-binding protein (ChREBP) mediates mesangial cell lipogenesis and fibrosis: the possible role in the development of diabetic nephropathy Quantitative secretome and glycome of primary human adipocytes during insulin resistance.A Caenorhabditis elegans model of insulin resistance: altered macronutrient storage and dauer formation in an OGT-1 knockout.Analysis of hepatic glycogen-associated proteins.O-GlcNAc signaling in the cardiovascular system.Inhibition of O-GlcNAcase in perfused rat hearts by NAG-thiazolines at the time of reperfusion is cardioprotective in an O-GlcNAc-dependent manner.Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis Global O-GlcNAc Levels Modulate Transcription of the Adipocyte Secretome during Chronic Insulin Resistance.Pleiotropic and age-dependent effects of decreased protein modification by O-linked N-acetylglucosamine on pancreatic β-cell function and vascularization.O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar.Conditional knock-out reveals a requirement for O-linked N-Acetylglucosaminase (O-GlcNAcase) in metabolic homeostasis Expression and purification of functional human glycogen synthase-1:glycogenin-1 complex in insect cells.A chemical approach for identifying O-GlcNAc-modified proteins in cells.The roles of O-linked β-N-acetylglucosamine in cardiovascular physiology and disease.Palmitate action to inhibit glycogen synthase and stimulate protein phosphatase 2A increases with risk factors for type 2 diabetes.Role of protein O-linked N-acetyl-glucosamine in mediating cell function and survival in the cardiovascular system.Regulation of Akt signaling by O-GlcNAc in euglycemia.Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux.Glycogen and its metabolism: some new developments and old themes.Cross-talk between GlcNAcylation and phosphorylation: roles in insulin resistance and glucose toxicity.The chemical neurobiology of carbohydrates Cracking the O-GlcNAc code in metabolism.The O-linked N-acetylglucosamine modification in cellular signalling and the immune system. 'Protein modifications: beyond the usual suspects' review series.Dual regulation of muscle glycogen synthase during exercise by activation and compartmentalization.Protein modification by O-linked GlcNAc reduces angiogenesis by inhibiting Akt activity in endothelial cells TRIB3 mediates glucose-induced insulin resistance via a mechanism that requires the hexosamine biosynthetic pathway.Hexosamine flux, the O-GlcNAc modification, and the development of insulin resistance in adipocytes.Advanced glycation end products: role in pathology of diabetic cardiomyopathy.Protein O-GlcNAcylation in diabetes and diabetic complications.Role of O-GlcNAcylation in nutritional sensing, insulin resistance and in mediating the benefits of exercise.O-GlcNAc: A Bittersweet Switch in Liver

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P2860

Insulin resistance of glycogen synthase mediated by o-linked N-acetylglucosamine.

http://www.wikidata.org/entity/Q42435341

description

2003 nî lūn-bûn

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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2003年论文

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2003年论文

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name

Insulin resistance of glycogen synthase mediated by o-linked N-acetylglucosamine.

@en

Insulin resistance of glycogen synthase mediated by o-linked N-acetylglucosamine.

@nl

type

label

Insulin resistance of glycogen synthase mediated by o-linked N-acetylglucosamine.

@en

Insulin resistance of glycogen synthase mediated by o-linked N-acetylglucosamine.

@nl

prefLabel

Insulin resistance of glycogen synthase mediated by o-linked N-acetylglucosamine.

@en

Insulin resistance of glycogen synthase mediated by o-linked N-acetylglucosamine.

@nl

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Journal of Biological Chemistry

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Insulin resistance of glycogen synthase mediated by o-linked N-acetylglucosamine

@en

P2093

Glendon J Parker

http://www.w3.org/2001/XMLSchema#string

Kelli C Lund

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Rodrick P Taylor

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P2860

Organizing glucose disposal: emerging roles of the glycogen targeting subunits of protein phosphatase-1

Insulin signalling and the regulation of glucose and lipid metabolism

Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats

O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats

Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Biochemistry and molecular cell biology of diabetic complications

Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity

Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats

PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism

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10022-10027

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10.1074/JBC.M207787200

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278

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2003-01-01T00:00:00Z

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12510058

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