Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity. - Wikidata - wikimedia - TriplyDB

Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity.

Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity.

http://www.wikidata.org/entity/Q35063067

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Genealogy of an ancient protein family: the Sirtuins, a family of disordered members A high-confidence interaction map identifies SIRT1 as a mediator of acetylation of USP22 and the SAGA coactivator complex JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships Mechanisms of intrahepatic triglyceride accumulation Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications Redox regulation of SIRT1 in inflammation and cellular senescence New Insights for Oxidative Stress and Diabetes Mellitus Emerging Roles of SIRT1 in Cancer Drug Resistance ANG II promotes IGF-IIR expression and cardiomyocyte apoptosis by inhibiting HSF1 via JNK activation and SIRT1 degradation Mutations that Allow SIR2 Orthologs to Function in a NAD+-Depleted Environment.SIRT1 phosphorylation by AMP-activated protein kinase regulates p53 acetylation The ways and means that fine tune Sirt1 activity.mIGF-1/JNK1/SirT1 signaling confers protection against oxidative stress in the heart.Phosphoproteomics combined with quantitative 14-3-3-affinity capture identifies SIRT1 and RAI as novel regulators of cytosolic double-stranded RNA recognition pathway.WISP1: Clinical insights for a proliferative and restorative member of the CCN family Upregulation of Unc-51-like kinase 1 by nitric oxide stabilizes SIRT1, independent of autophagy.Sorting out functions of sirtuins in cancer Nutrigenomics of high fat diet induced obesity in mice suggests relationships between susceptibility to fatty liver disease and the proteasome.Ginsenoside Rb1 prevents H2O2-induced HUVEC senescence by stimulating sirtuin-1 pathway.Ubiquitinated sirtuin 1 (SIRT1) function is modulated during DNA damage-induced cell death and survival.Palmitate Inhibits SIRT1-Dependent BMAL1/CLOCK Interaction and Disrupts Circadian Gene Oscillations in Hepatocytes.Combined influence of insulin resistance, overweight/obesity, and fatty liver as risk factors for type 2 diabetes.Nicotinamide N-methyltransferase regulates hepatic nutrient metabolism through Sirt1 protein stabilization.Role of deleted in breast cancer 1 (DBC1) protein in SIRT1 deacetylase activation induced by protein kinase A and AMP-activated protein kinase.A novel inverse relationship between metformin-triggered AMPK-SIRT1 signaling and p53 protein abundance in high glucose-exposed HepG2 cells.Regeneration in the nervous system with erythropoietin Salmonella Typhimurium disrupts Sirt1/AMPK checkpoint control of mTOR to impair autophagy.Acetylation of HDAC1 and degradation of SIRT1 form a positive feedback loop to regulate p53 acetylation during heat-shock stress.Repositioning antipsychotic chlorpromazine for treating colorectal cancer by inhibiting sirtuin 1 High-fat diet triggers inflammation-induced cleavage of SIRT1 in adipose tissue to promote metabolic dysfunction.Change in fatty liver status and 5-year risk of incident metabolic syndrome: a retrospective cohort study WISP1 neuroprotection requires FoxO3a post-translational modulation with autoregulatory control of SIRT1 Developmental programming of pediatric nonalcoholic fatty liver disease: redefining the"first hit".The REGγ proteasome regulates hepatic lipid metabolism through inhibition of autophagy.Calorie restriction and sirtuins revisited CHFR negatively regulates SIRT1 activity upon oxidative stress.Non-alcoholic steatohepatitis and hepatocellular carcinoma: implications for lycopene intervention.Amphetamines promote mitochondrial dysfunction and DNA damage in pulmonary hypertension A redox-resistant sirtuin-1 mutant protects against hepatic metabolic and oxidant stress.c-Jun N-terminal kinase 1/c-Jun activation of the p53/microRNA 34a/sirtuin 1 pathway contributes to apoptosis induced by deoxycholic acid in rat liver.

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P2860

Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity.

http://www.wikidata.org/entity/Q35063067

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2011 nî lūn-bûn

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2011 թվականի մայիսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Sirtuin 1 (SIRT1) protein degr ...... hepatic steatosis in obesity.

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Sirtuin 1 (SIRT1) protein degr ...... hepatic steatosis in obesity.

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type

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Sirtuin 1 (SIRT1) protein degr ...... hepatic steatosis in obesity.

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Sirtuin 1 (SIRT1) protein degr ...... hepatic steatosis in obesity.

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Sirtuin 1 (SIRT1) protein degr ...... hepatic steatosis in obesity.

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Sirtuin 1 (SIRT1) protein degr ...... hepatic steatosis in obesity.

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Sirtuin 1 (SIRT1) protein degr ...... hepatic steatosis in obesity.

@en

P2093

Indu Kheterpal

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Jianping Ye

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

Jin Zhang

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Norm Kennedy

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Roger J Davis

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Zhanguo Gao

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P2860

JNK1 phosphorylates SIRT1 and promotes its enzymatic activity

Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma

Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase

JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain

Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase

Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes

A fasting inducible switch modulates gluconeogenesis via activator/coactivator exchange

Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase

Resveratrol improves health and survival of mice on a high-calorie diet

Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae.

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