Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function. - Wikidata - wikimedia - TriplyDB

Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function.

Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function.

http://www.wikidata.org/entity/Q33652111

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Hyperglycemia-associated alterations in cellular signaling and dysregulated mitochondrial bioenergetics in human metabolic disorders O-GlcNAcylation: The Sweet Side of the Cancer.The regulatory roles of O-GlcNAcylation in mitochondrial homeostasis and metabolic syndrome.O-GlcNAcase Expression is Sensitive to Changes in O-GlcNAc Homeostasis.A little sugar goes a long way: the cell biology of O-GlcNAc.High glucose induces mitochondrial dysfunction independently of protein O-GlcNAcylation.Diabetes-associated dysregulation of O-GlcNAcylation in rat cardiac mitochondria Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).Quantitative phosphoproteomics reveals crosstalk between phosphorylation and O-GlcNAc in the DNA damage response pathway.O-linked N-acetylglucosamine glycosylation of p65 aggravated the inflammation in both fibroblast-like synoviocytes stimulated by tumor necrosis factor-α and mice with collagen induced arthritis O-GlcNAc transferase and O-GlcNAcase: achieving target substrate specificity.O-GlcNAcomic Profiling Identifies Widespread O-Linked β-N-Acetylglucosamine Modification (O-GlcNAcylation) in Oxidative Phosphorylation System Regulating Cardiac Mitochondrial Function Mitochondrial dysfunction and cell death in neurodegenerative diseases through nitroxidative stress Reduced O-GlcNAcase expression promotes mitotic errors and spindle defects.Nucleocytoplasmic human O-GlcNAc transferase is sufficient for O-GlcNAcylation of mitochondrial proteins O-Linked N-Acetylglucosamine (O-GlcNAc) Transferase and O-GlcNAcase Interact with Mi2β Protein at the Aγ-Globin Promoter.Abnormal Glycosylation Profile and High Alpha-Fetoprotein in a Patient with Twinkle Variants.System-based proteomic and metabonomic analysis of the Df(16)A+/- mouse identifies potential miR-185 targets and molecular pathway alterations New insights: A role for O-GlcNAcylation in diabetic complications.Post-translational modifications in mitochondria: protein signaling in the powerhouse.Hyperglycemia induced damage to mitochondrial respiration in renal mesangial and tubular cells: Implications for diabetic nephropathy.Sustained O-GlcNAcylation reprograms mitochondrial function to regulate energy metabolism.Mitochondrial O-GlcNAc Transferase (mOGT) Regulates Mitochondrial Structure, Function, and Survival in HeLa Cells.Skeletal muscle O-GlcNAc transferase is important for muscle energy homeostasis and whole-body insulin sensitivity.Gold Nanoparticles Impinge on Nucleoli and the Stress Response in MCF7 Breast Cancer Cells.O-GlcNAc cycling in the developing, adult and geriatric brain.The Nutrient-Sensing Hexosamine Biosynthetic Pathway as the Hub of Cancer Metabolic Rewiring.Real Talk: The Inter-play Between the mTOR, AMPK, and Hexosamine Biosynthetic Pathways in Cell Signaling

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P2860

Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function.

http://www.wikidata.org/entity/Q33652111

description

2014 nî lūn-bûn

@nan

2014 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի ապրիլին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function.

@ast

Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function.

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type

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Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function.

@ast

Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function.

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prefLabel

Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function.

@ast

Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function.

@en

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JBC.M113.525790

P1433

Journal of Biological Chemistry

P1476

Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function.

@en

P2093

Antonio Artigues

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

Chad Slawson

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

Ee Phie Tan

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

J Eva Selfridge

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

Jianghua Lu

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

Lezi E

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

Maria T Villar

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

Russell H Swerdlow

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

P2860

Elevated O-GlcNAc-dependent signaling through inducible mOGT expression selectively triggers apoptosis

Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance

Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytes

Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose

O-GlcNAc regulates FoxO activation in response to glucose.

Mitochondria in cybrids containing mtDNA from persons with mitochondriopathies.

O-GlcNAc cycling enzymes associate with the translational machinery and modify core ribosomal proteins

O-GlcNAc signaling: a metabolic link between diabetes and cancer?

O-GlcNAc signalling: implications for cancer cell biology.

Chronic ingestion of a Western diet increases O-linked-β-N-acetylglucosamine (O-GlcNAc) protein modification in the rat heart.

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14719-14730

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scholarly article

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10.1074/JBC.M113.525790

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21

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289

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2014-04-08T00:00:00Z

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24713701

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4031527

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