Dephosphorylation of translation initiation factor 2alpha enhances glucose tolerance and attenuates hepatosteatosis in mice - Wikidata - awgldk - TriplyDB

Dephosphorylation of translation initiation factor 2alpha enhances glucose tolerance and attenuates hepatosteatosis in mice

Dephosphorylation of translation initiation factor 2alpha enhances glucose tolerance and attenuates hepatosteatosis in mice

http://www.wikidata.org/entity/Q39975807

about

Endoplasmic reticulum stress and the inflammatory basis of metabolic disease Atf4 regulates obesity, glucose homeostasis, and energy expenditure Hepatitis C virus hijacks host lipid metabolism Pharmacological Modulators of Endoplasmic Reticulum Stress in Metabolic Diseases The Role of Organelle Stresses in Diabetes Mellitus and Obesity: Implication for Treatment Role of endoplasmic reticulum stress in the pathogenesis of nonalcoholic fatty liver disease Energy metabolism in the liver Xenobiotic perturbation of ER stress and the unfolded protein response Stress management: How the unfolded protein response impacts fatty liver disease Lipid biology of breast cancer Divergent effects of PERK and IRE1 signaling on cell viability The membrane stress response buffers lethal effects of lipid disequilibrium by reprogramming the protein homeostasis network.Hepatoprotective role of Sestrin2 against chronic ER stress Inflammation and cellular stress: a mechanistic link between immune-mediated and metabolically driven pathologies Endoplasmic reticulum stress and atherosclerosis HCV causes chronic endoplasmic reticulum stress leading to adaptation and interference with the unfolded protein response PERK-dependent regulation of lipogenesis during mouse mammary gland development and adipocyte differentiation The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 and increase its nuclear translocation Eukaryotic initiation factor 2α--a downstream effector of mammalian target of rapamycin--modulates DNA repair and cancer response to treatment Identification of modulators of the nuclear receptor peroxisome proliferator-activated receptor α (PPARα) in a mouse liver gene expression compendium Rapamycin inhibits postprandial-mediated X-box-binding protein-1 splicing in rat liver Experimental reconstitution of chronic ER stress in the liver reveals feedback suppression of BiP mRNA expression Mechanisms for insulin resistance: common threads and missing links Temporal and spatial regulation of translation in the mammalian oocyte via the mTOR-eIF4F pathway Obesity-induced hepatic steatosis is mediated by endoplasmic reticulum stress in the subfornical organ of the brain Inhibition of hypoxia-inducible factor-1alpha (HIF-1alpha) protein synthesis by DNA damage inducing agents A point mutation in Sec61alpha1 leads to diabetes and hepatosteatosis in mice.Homocysteine Induces Hepatic Steatosis Involving ER Stress Response in High Methionine Diet-Fed Mice ER stress and hepatic lipid metabolism.Hepatic Bax inhibitor-1 inhibits IRE1alpha and protects from obesity-associated insulin resistance and glucose intolerance.Modulation of glucose metabolism by a natural compound from Chloranthus japonicus via activation of AMP-activated protein kinase Differences in betaine-homocysteine methyltransferase expression, endoplasmic reticulum stress response, and liver injury between alcohol-fed mice and rats Overexpression of apolipoprotein A-I alleviates endoplasmic reticulum stress in hepatocytes.Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease.Regulation of basal cellular physiology by the homeostatic unfolded protein response Hsp90 modulates PPARγ activity in a mouse model of nonalcoholic fatty liver disease.Aberrant lipid metabolism disrupts calcium homeostasis causing liver endoplasmic reticulum stress in obesity.Endoplasmic reticulum stress-induced transcription factor, CHOP, is crucial for dendritic cell IL-23 expression Upregulation of the coagulation factor VII gene during glucose deprivation is mediated by activating transcription factor 4.Polysome profiling in liver identifies dynamic regulation of endoplasmic reticulum translatome by obesity and fasting.

P2860

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P2860

Dephosphorylation of translation initiation factor 2alpha enhances glucose tolerance and attenuates hepatosteatosis in mice

http://www.wikidata.org/entity/Q39975807

description

2008 nî lūn-bûn

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2008年の論文

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年學術文章

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2008年學術文章

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2008年學術文章

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name

Dephosphorylation of translati ...... nuates hepatosteatosis in mice

@en

Dephosphorylation of translati ...... uates hepatosteatosis in mice.

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type

label

Dephosphorylation of translati ...... nuates hepatosteatosis in mice

@en

Dephosphorylation of translati ...... uates hepatosteatosis in mice.

@nl

prefLabel

Dephosphorylation of translati ...... nuates hepatosteatosis in mice

@en

Dephosphorylation of translati ...... uates hepatosteatosis in mice.

@nl

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J.CMET.2008.04.011

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Cell Metabolism

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Dephosphorylation of translati ...... nuates hepatosteatosis in mice

@en

P2093

Miho Oyadomari

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Seiichi Oyadomari

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Yuhong Zhang

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P2860

Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development

Gcn4p and novel upstream activating sequences regulate targets of the unfolded protein response

EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome

Translational control is required for the unfolded protein response and in vivo glucose homeostasis

Intracellular signaling by the unfolded protein response

Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis

CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription

The PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas

Cotranslocational degradation protects the stressed endoplasmic reticulum from protein overload

Regulated translation initiation controls stress-induced gene expression in mammalian cells

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520-532

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6

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Heather P Harding

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