The asparaginyl hydroxylase factor inhibiting HIF-1alpha is an essential regulator of metabolism - Test2 - elhamkhani - TriplyDB

The asparaginyl hydroxylase factor inhibiting HIF-1alpha is an essential regulator of metabolism

The asparaginyl hydroxylase factor inhibiting HIF-1alpha is an essential regulator of metabolism

http://www.wikidata.org/entity/Q33945163

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Hypoxia-inducible factors and the response to hypoxic stress Oncometabolite 2-hydroxyglutarate is a competitive inhibitor of α-ketoglutarate-dependent dioxygenases Epigenetic regulation by histone demethylases in hypoxia HIF1α and HIF2α: sibling rivalry in hypoxic tumour growth and progression FIH Regulates Cellular Metabolism through Hydroxylation of the Deubiquitinase OTUB1 HIF prolyl hydroxylase inhibitors for anemia Consequences of IkappaB alpha hydroxylation by the factor inhibiting HIF (FIH)Genome-wide association study identifies novel loci associated with concentrations of four plasma phospholipid fatty acids in the de novo lipogenesis pathway: results from the Cohorts for Heart and Aging Research in Genomic Epidemiology (CHARGE) con Global microRNA depletion suppresses tumor angiogenesis.FIH-1-Mint3 axis does not control HIF-1 transcriptional activity in nucleus pulposus cells.Notch inhibitors for cancer treatment.FIH-1, a novel interactor of mindbomb, functions as an essential anti-angiogenic factor during zebrafish vascular development.A GWA study reveals genetic loci for body conformation traits in Chinese Laiwu pigs and its implications for human BMI.Intermediary metabolite precursor dimethyl-2-ketoglutarate stabilizes hypoxia-inducible factor-1α by inhibiting prolyl-4-hydroxylase PHD2.FIH-1/c-kit signaling: a novel contributor to corneal epithelial glycogen metabolism.FIH-1 disrupts an LRRK1/EGFR complex to positively regulate keratinocyte migration.Hypoxia-inducible factor directs POMC gene to mediate hypothalamic glucose sensing and energy balance regulation Nothing Iffy about HIF in the Hypothalamus.Quantitative mass spectrometry reveals dynamics of factor-inhibiting hypoxia-inducible factor-catalyzed hydroxylation.The chromatin remodeler ISWI regulates the cellular response to hypoxia: role of FIH.Factor inhibiting HIF (FIH) recognizes distinct molecular features within hypoxia-inducible factor-α (HIF-α) versus ankyrin repeat substrates The FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity.Activation of the HIF prolyl hydroxylase by the iron chaperones PCBP1 and PCBP2.MicroRNA-31 targets FIH-1 to positively regulate corneal epithelial glycogen metabolism.Ankyrin Repeat Proteins of Orf Virus Influence the Cellular Hypoxia Response Pathway microRNA-31/factor-inhibiting hypoxia-inducible factor 1 nexus regulates keratinocyte differentiation Transcriptional and Post-Transcriptional Regulation of Thrombospondin-1 Expression: A Computational Model.Modulation of TRP Channel Activity by Hydroxylation and Its Therapeutic Potential.Orexin: pathways to obesity resistance?The "Sharp" blade against HIF-mediated metastasis.Complex role of HIF in cancer: the known, the unknown, and the unexpected.Hypoxia: from basic mechanisms to therapeutics - a meeting report on the Keystone and HypoxiaNet Symposium.Adaptive and maladaptive cardiorespiratory responses to continuous and intermittent hypoxia mediated by hypoxia-inducible factors 1 and 2.NUMB inhibition of NOTCH signalling as a therapeutic target in prostate cancer.Molecular responses to hypoxia-inducible factor 1α and beyond.The Siah2-HIF-FoxA2 axis in prostate cancer – new markers and therapeutic opportunities.Chromatin as an oxygen sensor and active player in the hypoxia response.HIF expression and the role of hypoxic microenvironments within primary tumours as protective sites driving cancer stem cell renewal and metastatic progression.Hypoxia-inducible factor (HIF) network: insights from mathematical models.The roles of Jumonji-type oxygenases in human disease.

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The asparaginyl hydroxylase factor inhibiting HIF-1alpha is an essential regulator of metabolism

http://www.wikidata.org/entity/Q33945163

description

2010 nî lūn-bûn

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2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

The asparaginyl hydroxylase fa ...... ential regulator of metabolism

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The asparaginyl hydroxylase fa ...... ential regulator of metabolism

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The asparaginyl hydroxylase fa ...... ential regulator of metabolism

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The asparaginyl hydroxylase fa ...... ential regulator of metabolism

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J.CMET.2010.03.001

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Cell Metabolism

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The asparaginyl hydroxylase fa ...... ential regulator of metabolism

@en

P2093

Frank Powell

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

Gabriel G Haddad

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

Jeffrey J Gorman

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

Johana Chicher

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

Lorenz Poellinger

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

Na Zhang

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

Sarah Linke

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

Zhenxing Fu

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

P2860

FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity

FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor

Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)

Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor

MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)

Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways

ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism

Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases

Hydroxylation of HIF-1: oxygen sensing at the molecular level

Placental but not heart defects are associated with elevated hypoxia-inducible factor alpha levels in mice lacking prolyl hydroxylase domain protein 2

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364-378

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scholarly article

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10.1016/J.CMET.2010.03.001

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5

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11

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Randall S. Johnson

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2010-04-15T00:00:00Z

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238300771

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20399150

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2893150

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