Factor-inhibiting HIF-1 (FIH-1) is required for human vascular endothelial cell survival

Factor-inhibiting HIF-1 (FIH-1) is required for human vascular endothelial cell survival

<p style="text-align:justify;"> Factor-inhibiting hypoxia-inducible factor (HIF)-1 (FIH-1) is an asparaginyl β-hydroxylase enzyme that was initially found to hydroxylate the HIF-α, preventing its transcriptional activity and leading to adaptive responses to hypoxia. More recently, o...

Disgrifiad llawn

Manylion Llyfryddiaeth
Prif Awduron:	Kiriakidis, S, Henze, A, Kruszynska-Ziaja, I, Skobridis, K, Theodorou, V, Paleolog, E, Mazzone, M
Fformat:	Journal article
Iaith:	English
Cyhoeddwyd:	Federation of American Society of Experimental Biology 2015

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The role of factor inhibiting HIF (FIH-1) in inhibiting HIF-1 transcriptional activity in glioblastoma multiforme.
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Factor inhibiting HIF (FIH1) modulates cardiac function and metabolism
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Investigating the role of factor inhibiting HIF (FIH) in tumourigenesis
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Factor-inhibiting HIF (FIH) promotes lung cancer progression
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Nuclear entry and export of FIH are mediated by HIF1α and exportin1 respectively
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Vascular endothelial growth factor signalling in endothelial cell survival: a role for NFkappaB.
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Signalling cross talk of the HIF system: involvement of the FIH protein.
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Cyhoeddwyd: (2009)

Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family.
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Overexpression of the HIF hydroxylases PHD1, PHD2, PHD3 and FIH are individually and collectively unfavorable prognosticators for NSCLC survival.
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FIH permits NAA10 to catalyze the oxygen-dependent lysyl-acetylation of HIF-1α
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Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH).
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The FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity.
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The FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity
gan: Masson, N, et al.
Cyhoeddwyd: (2012)

Evidence that two enzyme-derived histidine ligands are sufficient for iron binding and catalysis by factor inhibiting HIF (FIH).
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Fih attenuates the hypoxic tolerance of Megalobrama amblycephala by inhibiting the activity of hypoxia-inducible factor alpha (hif-α)
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HIF-isoforms have divergent roles in the angiogenesis of colorectal cancer
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Vascular endothelium--role in chronic inflammatory disease.
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Hypoxia. The role of hypoxia and HIF-dependent signalling events in rheumatoid arthritis.
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Studies on FIH interactions
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HIF1 and ID1 Interplay Confers Adaptive Survival to HIF1α-Inhibition
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Activation of hypoxia-inducible factor (HIF) pathway in varicose veins
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The inhibition of factor inhibiting hypoxia-inducible factor (FIH) by beta-oxocarboxylic acids.
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The relationship between factor inhibiting HIF-1-alpha (HIF1AN( expression and vascular invasion in colon cancer
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Expression of prolyl-hydroxylases PHD-1, 2 and 3 and of the asparagine hydroxylase FIH in non-small cell lung cancer relates to an activated HIF pathway.
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Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.
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FIH Regulates Cellular Metabolism through Hydroxylation of the Deubiquitinase OTUB1.
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Caenorhabditis elegans HIF-1 Is Broadly Required for Survival in Hydrogen Sulfide
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FIH-1, a novel interactor of mindbomb, functions as an essential anti-angiogenic factor during zebrafish vascular development.
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Genetic analysis of the role of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH) in regulating hypoxia-inducible factor (HIF) transcriptional target genes [corrected].
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Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity.
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CircCDR1as Suppresses Bone Microvascular Endothelial Cell Activity and Angiogenesis Through Targeting miR‐135b/ FIH‐1 Axis
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La verità, vi prego, sul criterio del creditore privato: Commissione c. FIH Holding e FIH Erhvervsbank
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Advanced glycation end products (AGEs) augment production of vascular endothelial growth factor (VEGF) and tumor necrosis factor alpha (TNF alpha) in human monocyte-derived macrophages.
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Oxygen-dependent bond formation with FIH regulates the activity of the client protein OTUB1
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STEAP4 Inhibits HIF-1α/PKM2 Signaling and Reduces High Glucose-Induced Apoptosis of Retinal Vascular Endothelial Cells
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HIF-1 reduces ischaemia-reperfusion injury in the heart by targeting the mitochondrial permeability transition pore.
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Rapamycin inhibits proliferation of hemangioma endothelial cells by reducing HIF-1-dependent expression of VEGF.
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