Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins. - Test2 - elhamkhani - TriplyDB

Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins.

Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins.

http://www.wikidata.org/entity/Q37375712

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Redox regulation by Nrf2: gatekeeping for the basal and diabetes-induced expression of thioredoxin interacting protein Mammalian α arrestins link activated seven transmembrane receptors to Nedd4 family e3 ubiquitin ligases and interact with β arrestins The arrestin domain-containing 3 protein regulates body mass and energy expenditure Coordination of nutrient availability and utilization by MAX- and MLX-centered transcription networks Thioredoxin/Txnip: redoxisome, as a redox switch for the pathogenesis of diseases Thioredoxin-interacting protein regulates glucose metabolism and affects cytoplasmic streaming in mouse oocytes Design of a microfluidic device to quantify dynamic intra-nuclear deformation during cell migration through confining environments.Structure of the N-terminal domain of human thioredoxin-interacting protein A calcineurin-dependent switch controls the trafficking function of α-arrestin Aly1/Art6.A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis.Structural basis for a novel interaction between TXNIP and Vav2 Thioredoxin Interacting Protein (TXNIP) and Pathogenesis of Diabetic Retinopathy AMP-activated protein kinase (AMPK) mediates nutrient regulation of thioredoxin-interacting protein (TXNIP) in pancreatic beta-cells MondoA coordinately regulates skeletal myocyte lipid homeostasis and insulin signaling Hepatic gene expression profiling of 5'-AMP-induced hypometabolism in mice The interaction between nesprins and sun proteins at the nuclear envelope is critical for force transmission between the nucleus and cytoskeleton.Endocytic regulation of alkali metal transport proteins in mammals, yeast and plants.Spo0M: structure and function beyond regulation of sporulation.The Emerging Role of Thioredoxin-Interacting Protein in Myocardial Ischemia/Reperfusion Injury Metabolic Remodeling in Diabetic Cardiomyopathy.Deletion of the alpha-arrestin protein Txnip in mice promotes adiposity and adipogenesis while preserving insulin sensitivity.Glucose controls nuclear accumulation, promoter binding, and transcriptional activity of the MondoA-Mlx heterodimer.Minireview: Thioredoxin-interacting protein: regulation and function in the pancreatic β-cell.Prediction of miRNA-mRNA associations in Alzheimer's disease mice using network topology.Thioredoxin-interacting protein (Txnip) gene expression: sensing oxidative phosphorylation status and glycolytic rate.Thioredoxin-interacting protein inhibits hypoxia-inducible factor transcriptional activity.Deficiency of thioredoxin binding protein-2 (TBP-2) enhances TGF-β signaling and promotes epithelial to mesenchymal transition.Myc, mondo, and metabolism Analysis of lead toxicity in human cells Thioredoxin-interacting protein regulates protein disulfide isomerases and endoplasmic reticulum stress.Thioredoxin-interacting protein gene expression via MondoA is rapidly and transiently suppressed during inflammatory responses Disruption of TBP-2 ameliorates insulin sensitivity and secretion without affecting obesity.Prenatal metformin exposure in a maternal high fat diet mouse model alters the transcriptome and modifies the metabolic responses of the offspring.Endocytic adaptors--social networking at the plasma membrane.Crystallization and preliminary X-ray analysis of the N-terminal domain of human thioredoxin-interacting protein.Diminished AMPK signaling response to fasting in thioredoxin-interacting protein knockout mice Transcriptional and Translational Downregulation of Thioredoxin Interacting Protein Is Required for Metabolic Reprogramming during G(1).The emerging role of the thioredoxin system in angiogenesis Thioredoxin regulates adipogenesis through thioredoxin-interacting protein (Txnip) protein stability.MondoA senses non-glucose sugars: regulation of thioredoxin-interacting protein (TXNIP) and the hexose transport curb.

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Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins.

http://www.wikidata.org/entity/Q37375712

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 15 July 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins.

@en

Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins.

@nl

type

label

Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins.

@en

Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins.

@nl

prefLabel

Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins.

@en

Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins.

@nl

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JBC.M109.018093

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Journal of Biological Chemistry

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Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins

@en

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Jan Lammerding

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

Kiersten Cummings

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

Parth Patwari

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Richard T Lee

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Valerie L R M Verstraeten

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

William A Chutkow

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

P2860

Thioredoxin modulates activator protein 1 (AP-1) activity and p27Kip1 degradation through direct interaction with Jab1

The proton-linked monocarboxylate transporter (MCT) family: structure, function and regulation

Positional cloning of the combined hyperlipidemia gene Hyplip1

The structural basis of arrestin-mediated regulation of G-protein-coupled receptors

The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain

PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance.

Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface.

Identification of thioredoxin-binding protein-2/vitamin D(3) up-regulated protein 1 as a negative regulator of thioredoxin function and expression

Hyperglycemia promotes oxidative stress through inhibition of thioredoxin function by thioredoxin-interacting protein

Importin alpha1 (Rch1) mediates nuclear translocation of thioredoxin-binding protein-2/vitamin D(3)-up-regulated protein 1

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24996-25003

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scholarly article

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10.1074/JBC.M109.018093

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37

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284

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Eric R Schreiter

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2009-07-15T00:00:00Z

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19605364

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2757204

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