Mucosal protection by hypoxia-inducible factor prolyl hydroxylase inhibition. - Wikidata - awgldk - TriplyDB

Mucosal protection by hypoxia-inducible factor prolyl hydroxylase inhibition.

Mucosal protection by hypoxia-inducible factor prolyl hydroxylase inhibition.

http://www.wikidata.org/entity/Q36372667

about

Adenosine and hypoxia-inducible factor signaling in intestinal injury and recovery The impact of hypoxia on intestinal epithelial cell functions: consequences for invasion by bacterial pathogens Exploring the HIFs, buts and maybes of hypoxia signalling in disease: lessons from zebrafish models Neutrophils and inflammatory resolution in the mucosa Hypoxia and Integrin-Mediated Epithelial Restitution during Mucosal Inflammation EGL-9 controls C. elegans host defense specificity through prolyl hydroxylation-dependent and -independent HIF-1 pathways Actions of adenosine on cullin neddylation: implications for inflammatory responses Hypoxia: an alarm signal during intestinal inflammation Molecular mechanisms of action and therapeutic uses of pharmacological inhibitors of HIF-prolyl 4-hydroxylases for treatment of ischemic diseases Potent and selective chemical probe of hypoxic signalling downstream of HIF-α hydroxylation via VHL inhibition Inflammatory bowel disease Up-regulation of hypoxia-inducible factor 1 alpha and hemodynamic responses following massive small bowel resection.Adenosine: an old drug newly discovered.Cucurbitacin I induces protective autophagy in glioblastoma in vitro and in vivo Impaired Ca(2+)-handling in HIF-1alpha(+/-) mice as a consequence of pressure overload.IFN-γ attenuates hypoxia-inducible factor (HIF) activity in intestinal epithelial cells through transcriptional repression of HIF-1β Contributions of neutrophils to resolution of mucosal inflammation.Pharmacological intervention studies using mouse models of the inflammatory bowel diseases: translating preclinical data into new drug therapies.Metabolic shifts in immunity and inflammation.Targeting the A2B adenosine receptor during gastrointestinal ischemia and inflammation Boosting the hypoxia-induced adaptive response in inflammatory bowel disease: a novel concept of treatment.Purinergic signaling during inflammation.Hypoxia-inducible factor/MAZ-dependent induction of caveolin-1 regulates colon permeability through suppression of occludin, leading to hypoxia-induced inflammation.Adora2b adenosine receptor engagement enhances regulatory T cell abundance during endotoxin-induced pulmonary inflammation HIF-1 mediates pathogenic inflammatory responses to intestinal ischemia-reperfusion injury.Relationship between inflammation and tissue hypoxia in a mouse model of chronic colitis.Hypoxia-inducible factor activation protects the kidney from gentamicin-induced acute injury.Targeting hypoxia signalling for the treatment of ischaemic and inflammatory diseases Biological functions of ecto-enzymes in regulating extracellular adenosine levels in neoplastic and inflammatory disease states.Hypoxia-inducible factor signaling provides protection in Clostridium difficile-induced intestinal injury.Hypoxia and metabolic factors that influence inflammatory bowel disease pathogenesis.Hypoxia-inducible factor plays a gut-injurious role in intestinal ischemia reperfusion injury.Anti-inflammatory actions of adrenomedullin through fine tuning of HIF stabilization.Hypoxia integration in the serological proteome analysis unmasks tumor antigens and fosters the identification of anti-phospho-eEF2 antibodies as potential cancer biomarkers.HIF transcription factors, inflammation, and immunity.Bacterial protein AvrA stabilizes intestinal epithelial tight junctions via blockage of the C-Jun N-terminal kinase pathway.Activation of hypoxia-inducible factor-1 protects airway epithelium against oxidant-induced barrier dysfunction.Crosstalk between Microbiota-Derived Short-Chain Fatty Acids and Intestinal Epithelial HIF Augments Tissue Barrier Function.Pathogenesis of Crohn's disease The hypoxia-inflammation link and potential drug targets.

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Mucosal protection by hypoxia-inducible factor prolyl hydroxylase inhibition.

http://www.wikidata.org/entity/Q36372667

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

Mucosal protection by hypoxia-inducible factor prolyl hydroxylase inhibition.

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Mucosal protection by hypoxia-inducible factor prolyl hydroxylase inhibition.

@en

type

label

Mucosal protection by hypoxia-inducible factor prolyl hydroxylase inhibition.

@ast

Mucosal protection by hypoxia-inducible factor prolyl hydroxylase inhibition.

@en

prefLabel

Mucosal protection by hypoxia-inducible factor prolyl hydroxylase inhibition.

@ast

Mucosal protection by hypoxia-inducible factor prolyl hydroxylase inhibition.

@en

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J.GASTRO.2007.09.033

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Gastroenterology

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Mucosal protection by hypoxia-inducible factor prolyl hydroxylase inhibition

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Andreas Robinson

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Jörn Karhausen

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

Mark E Gerich

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Sean P Colgan

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P2860

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

Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300.

HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation

Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway

Crucial role for ecto-5'-nucleotidase (CD73) in vascular leakage during hypoxia.

A new mathematical model for relative quantification in real-time RT-PCR

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

HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus

Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes

Molecular mechanism of hypoxia-inducible factor 1alpha -p300 interaction. A leucine-rich interface regulated by a single cysteine.

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18166352

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