Catalytic degradation of vitamin D up-regulated protein 1 mRNA enhances cardiomyocyte survival and prevents left ventricular remodeling after myocardial ischemia - Wikidata - awgldk - TriplyDB

Catalytic degradation of vitamin D up-regulated protein 1 mRNA enhances cardiomyocyte survival and prevents left ventricular remodeling after myocardial ischemia

Catalytic degradation of vitamin D up-regulated protein 1 mRNA enhances cardiomyocyte survival and prevents left ventricular remodeling after myocardial ischemia

http://www.wikidata.org/entity/Q28566874

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Structure of the N-terminal domain of human thioredoxin-interacting protein The Emerging Role of Thioredoxin-Interacting Protein in Myocardial Ischemia/Reperfusion Injury Adenosine-containing molecules amplify glucose signaling and enhance txnip expression.Minireview: Thioredoxin-interacting protein: regulation and function in the pancreatic β-cell.Crystallization and preliminary X-ray analysis of the N-terminal domain of human thioredoxin-interacting protein.The emerging role of the thioredoxin system in angiogenesis Deoxyribozymes: new therapeutics to treat central nervous system disorders A novel role of myosin VI in human prostate cancer Thioredoxin binding protein (TBP)-2/Txnip and α-arrestin proteins in cancer and diabetes mellitus.Deletion of thioredoxin-interacting protein in mice impairs mitochondrial function but protects the myocardium from ischemia-reperfusion injury Pathogenesis of aortic stenosis: not just a matter of wear and tear Early-outgrowth bone marrow cells attenuate renal injury and dysfunction via an antioxidant effect in a mouse model of type 2 diabetes.Calcium channel blockers act through nuclear factor Y to control transcription of key cardiac genes.Serum NT-proBNP Levels Are Not Related to Vitamin D Status in Young Patients with Congenital Heart Defects Thioredoxin and thioredoxin target proteins: from molecular mechanisms to functional significance.A bimodal association of vitamin D levels and vascular disease in children on dialysis HECT-Type Ubiquitin E3 Ligase ITCH Interacts With Thioredoxin-Interacting Protein and Ameliorates Reactive Oxygen Species-Induced Cardiotoxicity.Brothers in arms: DNA enzymes, short interfering RNA, and the emerging wave of small-molecule nucleic acid-based gene-silencing strategies.Expression, localization, and function of the thioredoxin system in diabetic nephropathy.DNAzymes and cardiovascular disease.Diabetes induces and calcium channel blockers prevent cardiac expression of proapoptotic thioredoxin-interacting protein Selective inhibition of the master regulator transcription factor Egr-1 with catalytic oligonucleotides reduces myocardial injury and improves left ventricular systolic function in a preclinical model of myocardial infarction Transcription factors Krüppel-like factor 6 and peroxisome proliferator-activated receptor-{gamma} mediate high glucose-induced thioredoxin-interacting protein.Thioredoxin interacting protein: redox dependent and independent regulatory mechanisms.Thioredoxin-interacting protein and myocardial mitochondrial function in ischemia-reperfusion injury.Thioredoxin-interacting protein: pathophysiology and emerging pharmacotherapeutics in cardiovascular disease and diabetes.DNA enzymes as potential therapeutics: towards clinical application of 10-23 DNAzymes.Identification of Novel Non-secosteroidal Vitamin D Receptor Agonists with Potent Cardioprotective Effects and devoid of Hypercalcemia.The vitamin D analogue paricalcitol attenuates hepatic ischemia/reperfusion injury through down-regulation of Toll-like receptor 4 signaling in rats.Impaired cardiac anti-oxidant activity in diabetes: human and correlative experimental studies.Melatonin rescues cardiac thioredoxin system during ischemia-reperfusion injury in acute hyperglycemic state by restoring Notch1/Hes1/Akt signaling in a membrane receptor-dependent manner.Diabetes pathogenic mechanisms and potential new therapies based upon a novel target called TXNIP.Inhibition of RIP1-dependent necrosis prevents adverse cardiac remodeling after myocardial ischemia-reperfusion in vivo.The Role of Parathyroid Hormone and Vitamin D Serum Concentrations in Patients with Cardiovascular Diseases.

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P2860

Catalytic degradation of vitamin D up-regulated protein 1 mRNA enhances cardiomyocyte survival and prevents left ventricular remodeling after myocardial ischemia

http://www.wikidata.org/entity/Q28566874

description

2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

artículu científicu espublizáu en 2005

@ast

im November 2005 veröffentlichter wissenschaftlicher Artikel

@de

scientific journal article

@en

vedecký článok (publikovaný 2005/11/25)

@sk

vědecký článek publikovaný v roce 2005

@cs

wetenschappelijk artikel (gepubliceerd op 2005/11/25)

@nl

наукова стаття, опублікована в листопаді 2005

@uk

name

Catalytic degradation of vitam ...... ling after myocardial ischemia

@ast

Catalytic degradation of vitam ...... ling after myocardial ischemia

@en

Catalytic degradation of vitam ...... ling after myocardial ischemia

@nl

type

label

Catalytic degradation of vitam ...... ling after myocardial ischemia

@ast

Catalytic degradation of vitam ...... ling after myocardial ischemia

@en

Catalytic degradation of vitam ...... ling after myocardial ischemia

@nl

prefLabel

Catalytic degradation of vitam ...... ling after myocardial ischemia

@ast

Catalytic degradation of vitam ...... ling after myocardial ischemia

@en

Catalytic degradation of vitam ...... ling after myocardial ischemia

@nl

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P1433

Journal of Biological Chemistry

P1476

Catalytic degradation of vitam ...... ling after myocardial ischemia

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P2093

Alfred Kocher

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

Andrew J. Boyle

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

Fiona See

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

Guosheng Xiang

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

Hugo Sondermeijer

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

Michael D. Schuster

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

Piotr Witkowski

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

Silviu Itescu

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

Tetsunori Seki

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

Timothy P. Martens

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

P2860

Activation of apoptosis signal-regulating kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer

The expression of vitamin D-upregulated protein 1 in skin and its interaction with sciellin in cultured keratinocytes

Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1.

Negative feedback regulation of ASK1 by protein phosphatase 5 (PP5) in response to oxidative stress

Apoptosis signal-regulating kinase 1 (ASK1) induces neuronal differentiation and survival of PC12 cells

ASK1 associates with troponin T and induces troponin T phosphorylation and contractile dysfunction in cardiomyocytes

VDUP1 upregulated by TGF-beta1 and 1,25-dihydorxyvitamin D3 inhibits tumor cell growth by blocking cell-cycle progression

Vitamin D3-upregulated protein-1 (VDUP-1) regulates redox-dependent vascular smooth muscle cell proliferation through interaction with thioredoxin

Isolation and characterization of a novel cDNA from HL-60 cells treated with 1,25-dihydroxyvitamin D-3

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

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39394–39402

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scholarly article

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4764662

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10.1074/JBC.M502966200

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47

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280

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2005-11-25T00:00:00Z

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16172122

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