Cardiomyocyte-specific prolyl-4-hydroxylase domain 2 knock out protects from acute myocardial ischemic injury - Wikidata - wikimedia - TriplyDB

Cardiomyocyte-specific prolyl-4-hydroxylase domain 2 knock out protects from acute myocardial ischemic injury

Cardiomyocyte-specific prolyl-4-hydroxylase domain 2 knock out protects from acute myocardial ischemic injury

http://www.wikidata.org/entity/Q34719547

about

HIF hydroxylase pathways in cardiovascular physiology and medicine PHD2: from hypoxia regulation to disease progression Molecular mechanisms of ischemic preconditioning in the kidney Human high-altitude adaptation: forward genetics meets the HIF pathway.Remote ischaemic preconditioning: closer to the mechanism?Epidermal or dermal specific knockout of PHD-2 enhances wound healing and minimizes ischemic injury.Depletion of PHD3 protects heart from ischemia/reperfusion injury by inhibiting cardiomyocyte apoptosis.Preischemic targeting of HIF prolyl hydroxylation inhibits fibrosis associated with acute kidney injury PHD2/3-dependent hydroxylation tunes cardiac response to β-adrenergic stress via phospholamban.Hypoxia-inducible factor prolyl hydroxylase inhibition: robust new target or another big bust for stroke therapeutics?Metabolic stress in the myocardium: adaptations of gene expression.EGLN1 Inhibition and Rerouting of α-Ketoglutarate Suffice for Remote Ischemic Protection.Prolyl hydroxylase domain protein 2 silencing enhances the survival and paracrine function of transplanted adipose-derived stem cells in infarcted myocardium Activation of hypoxia response in endothelial cells contributes to ischemic cardioprotection.Hematological, hepatic, and retinal phenotypes in mice deficient for prolyl hydroxylase domain proteins in the liver Prolyl 4-hydroxylases, master regulators of the hypoxia response.Prolyl 4 hydroxylase: a critical target in the pathophysiology of diseases.Novel perspectives on the PHD-HIF oxygen sensing pathway in cardioprotection mediated by IPC and RIPC PHD2 Is a Regulator for Glycolytic Reprogramming in Macrophages.Prolyl hydroxylase domain enzymes: important regulators of cancer metabolism.The VHL Tumor Suppressor Gene: Insights into Oxygen Sensing and Cancer.Prolyl-4-hydroxylase domain 3 (PHD3) is a critical terminator for cell survival of macrophages under stress conditions.A role for prolyl hydroxylase domain proteins in hippocampal synaptic plasticity.HIF-1α and HIF-2α induce angiogenesis and improve muscle energy recovery.Unfavourable consequences of chronic cardiac HIF-1α stabilization.Pre- and post-conditional inhibition of prolyl-4-hydroxylase domain enzymes protects the heart from an ischemic insult.Hypoxia-inducible factor 2-alpha-dependent induction of amphiregulin dampens myocardial ischemia-reperfusion injury.HIF-P4H-2 deficiency protects against skeletal muscle ischemia-reperfusion injury.Ischemic preconditioning attenuates ischemia/reperfusion-induced kidney injury by activating autophagy via the SGK1 signaling pathway.

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Cardiomyocyte-specific prolyl-4-hydroxylase domain 2 knock out protects from acute myocardial ischemic injury

http://www.wikidata.org/entity/Q34719547

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունվարին 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年論文

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2011年論文

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2011年论文

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name

Cardiomyocyte-specific prolyl- ...... ute myocardial ischemic injury

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Cardiomyocyte-specific prolyl- ...... ute myocardial ischemic injury

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Cardiomyocyte-specific prolyl- ...... ute myocardial ischemic injury

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Cardiomyocyte-specific prolyl- ...... ute myocardial ischemic injury

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Cardiomyocyte-specific prolyl- ...... ute myocardial ischemic injury

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Cardiomyocyte-specific prolyl- ...... ute myocardial ischemic injury

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Cardiomyocyte-specific prolyl- ...... ute myocardial ischemic injury

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Cardiomyocyte-specific prolyl- ...... ute myocardial ischemic injury

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Cardiomyocyte-specific prolyl- ...... ute myocardial ischemic injury

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JBC.M110.186809

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Journal of Biological Chemistry

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Cardiomyocyte-specific prolyl- ...... ute myocardial ischemic injury

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Amke Hesse

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

Anke Zieseniss

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

Dörthe M Katschinski

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Marion Hölscher

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

Melanie von Ahlen

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

Monique Silter

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

Peter Schwartz

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Sabine Krull

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P2860

The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis

HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing

C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

A conserved family of prolyl-4-hydroxylases that modify HIF

Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling

Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL

HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia

A novel erythrocytosis-associated PHD2 mutation suggests the location of a HIF binding groove

Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation

Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor

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11185-11194

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286

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2011-01-26T00:00:00Z

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21270129

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3064173

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