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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Hypoxia inducible factor 1, alpha subunit inhibitor

FIH-1, factor inhibiting HIF, factor inhibiting HIF-1
Top mentioned proteins: HIF-1alpha, p300, CAN, PHD2, V1a
Papers on FIH-1
Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH.
Knapp et al., Amherst Center, United States. In Biochemistry, Feb 2016
Factor inhibiting HIF (FIH) is a Fe(2+)/αKG-dependent oxygenase that forms part of the O2 sensing machinery in human cells by hydroxylating the C-terminal transactivation domain (CTAD) found within the HIF-1α protein.
Investigation of FIH-1 and SOCS3 expression in KRAS mutant and wild-type patients with colorectal cancer.
Javadi et al., Qazvīn, Iran. In Tumour Biol, Feb 2016
Next, we investigated the expression of two tumor suppressor genes, factor-inhibiting hypoxia-inducible factor 1 (FIH-1) and suppressor of cytokine signaling (SOCS3), in both KRAS mutant and wild-type groups and looked for any correlation between their expression and clinicopathological parameters.
FIH Regulates Cellular Metabolism through Hydroxylation of the Deubiquitinase OTUB1.
Taylor et al., Dublin, Ireland. In Plos Biol, Jan 2016
The asparagine hydroxylase, factor inhibiting HIF (FIH), confers oxygen-dependence upon the hypoxia-inducible factor (HIF), a master regulator of the cellular adaptive response to hypoxia.
Hydroxytyrosol decreases the oxidative and nitrosative stress levels and promotes angiogenesis through HIF-1 independent mechanisms in renal hypoxic cells.
Siles et al., Jaén, Spain. In Food Funct, Dec 2015
However, HT does not affect mTOR activation or the factor inhibiting HIF level but promotes the expression of angiogenic proteins, suggesting that HT activates an adaptive response to hypoxia in a HIF-1α-independent pathway.
Metabolic Modulation of Clear-cell Renal Cell Carcinoma with Dichloroacetate, an Inhibitor of Pyruvate Dehydrogenase Kinase.
Michelakis et al., Edmonton, Canada. In Eur Urol, Oct 2015
DCA reactivated mitochondrial function (increased respiration, Krebs cycle metabolites such as α-ketoglutarate [cofactor of factor inhibiting HIF], and mitochondrial reactive oxygen species), increased p53 activity and apoptosis, and decreased proliferation in 786-O cells.
Influence of allelic Variations of hypoxia-related and DNA repair genes on patient outcome and toxicity in head and neck cancer treated with radiotherapy plus cetuximab.
Grau et al., Barcelona, Spain. In Eur Arch Otorhinolaryngol, Sep 2015
We analyzed 61 consecutive patients with HNSCC for the presence of specific SNPs (HIF-1α, HIF-2α, HIF-1β, VHL, FIH-1, XRCC1, and XRCC5).
Nuclear-cytoplasmatic shuttling of proteins in control of cellular oxygen sensing.
Kosyna et al., Lübeck, Germany. In J Mol Med (berl), Jun 2015
In the presence of O2, the α subunits are hydroxylated by specific prolyl-4-hydroxylase domain proteins (PHD1, PHD2, and PHD3) and an asparaginyl hydroxylase (factor inhibiting HIF-1, FIH-1).
Role of copper in regression of cardiac hypertrophy.
Kang et al., Chengdu, China. In Pharmacol Ther, Apr 2015
Copper is also required for hypoxia-inducible factor-1 (HIF-1) transcriptional activity, acting on the interaction between HIF-1 and the hypoxia responsible element and the formation of HIF-1 transcriptional complex by inhibiting the factor inhibiting HIF-1.
Hypoxia-inducible miR-182 enhances HIF1α signaling via targeting PHD2 and FIH1 in prostate cancer.
Ying et al., Shanghai, China. In Sci Rep, 2014
Prolyl hydroxylase domain enzymes (PHD) and factor inhibiting HIF-1 (FIH1), negative regulators of HIF1 signaling, are direct targets of miR-182.
Comparative microRNA profiling of sporadic and BRCA1 associated basal-like breast cancers.
Fox et al., Australia. In Bmc Cancer, 2014
The expression of Cyclin D1, FOXP1, FIH-1, pan-ERβ, NRP1 and CD99, predicted to be regulated by BRCA1 specific miRNAs by computer prediction algorithms, was assessed via immunohistochemistry in a cohort of 35 BRCA1 and 52 sporadic basal-like cancers.
Deciphering the emerging role of SUMO conjugation in the hypoxia-signaling cascade.
Berra et al., Spain. In Biol Chem, 2013
HIF is formed by the interaction of a constitutive HIF-1β subunit with a HIF-α subunit tightly regulated through the concerted action of the prolyl hydroxylase domain containing proteins (PHDs) and factor inhibiting HIF.
First phase insulin secretion and type 2 diabetes.
Gunton et al., Sydney, Australia. In Curr Mol Med, 2013
These include, among others, hypoxia inducible factor 1α, von Hippel-Lindau, factor inhibiting HIF, nicotinamide phospho-ribosyl-transferase, and the sirtuin family.
MicroRNA-31 targets FIH-1 to positively regulate corneal epithelial glycogen metabolism.
Lavker et al., Chicago, United States. In Faseb J, 2012
Glycogen regulation in a HIF-1alpha-independent manner is a novel function for FIH-1 and provides new insight into how the corneal epithelium regulates its energy requirements.
The asparaginyl hydroxylase factor-inhibiting HIF is essential for tumor growth through suppression of the p53-p21 axis.
Mazure et al., Nice, France. In Oncogene, 2012
FIH activity is essential for tumor growth through the suppression of the p53-p21 axis, the major barrier that prevents cancer progression.
Subcellular FIH-1 expression patterns in invasive breast cancer in relation to HIF-1α expression.
van Diest et al., Utrecht, Netherlands. In Cell Oncol (dordr), 2011
FIH1 is expressed in the majority of invasive breast carcinomas and shows distinct subcellular localization patterns.
Quantitative mass spectrometry reveals dynamics of factor-inhibiting hypoxia-inducible factor-catalyzed hydroxylation.
Cockman et al., Oxford, United Kingdom. In J Biol Chem, 2011
Quantitative mass spectrometry reveals dynamics of factor-inhibiting hypoxia-inducible factor-catalyzed hydroxylation.
Uncoupled O2-activation in the human HIF-asparaginyl hydroxylase, FIH, does not produce reactive oxygen species.
Knapp et al., Amherst Center, United States. In J Inorg Biochem, 2011
FIH does not uncouple O2 during turnover conditions, nor does it release reactive oxygen species under any tested conditions.
Regulation of erythropoietin production.
Jelkmann, Lübeck, Germany. In J Physiol, 2011
Three HIF-α prolyl hydroxylases (PHD-1, -2 and -3) initiate proteasomal degradation of HIF-α, while an asparaginyl hydroxylase ('factor inhibiting HIF-1', FIH-1) inhibits the transactivation potential.
The asparaginyl hydroxylase factor inhibiting HIF-1alpha is an essential regulator of metabolism.
Johnson et al., San Diego, United States. In Cell Metab, 2010
Factor inhibiting HIF-1alpha (FIH) is an asparaginyl hydroxylase.
Proline hydroxylation and gene expression.
Kaelin, Boston, United States. In Annu Rev Biochem, 2004
In addition, the HIFalpha transcriptional activation function is modulated further by asparagine hydroxylation by FIH (factor-inhibiting HIF), which affects recruitment of the coactivators p300 and CBP.
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