Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family
about
JMJD6 is a histone arginine demethylaseEvidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygenThe peptidyl prolyl cis/trans isomerase FKBP38 determines hypoxia-inducible transcription factor prolyl-4-hydroxylase PHD2 protein stabilityIOP1, a novel hydrogenase-like protein that modulates hypoxia-inducible factor-1alpha activityPosttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an Nepsilon-dimethyl lysine demethylaseMint3 enhances the activity of hypoxia-inducible factor-1 (HIF-1) in macrophages by suppressing the activity of factor inhibiting HIF-1Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathwaysAsparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factorStructure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alphaProlyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymesStructural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediatesFactor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domainsHuman AlkB homologue 5 is a nuclear 2-oxoglutarate dependent oxygenase and a direct target of hypoxia-inducible factor 1α (HIF-1α)Regulation of the prolyl hydroxylase domain protein 2 (phd2/egln-1) gene: identification of a functional hypoxia-responsive elementThe candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF).Suppression of hypoxia-inducible factor 1alpha (HIF-1alpha) transcriptional activity by the HIF prolyl hydroxylase EGLN1Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway.Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)Screening chelating inhibitors of HIF-prolyl hydroxylase domain 2 (PHD2) and factor inhibiting HIF (FIH)The human side of hypoxia-inducible factorStudies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assayHIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxiaAscorbate depletion: a critical step in nickel carcinogenesis?Hypoxia-inducible factor-1alpha polymorphisms and TSC1/2 mutations are complementary in head and neck cancersTargeting Protein-Protein Interactions in the HIF SystemHypoxia-Inducible Factors (HIFs) and Phosphorylation: Impact on Stability, Localization, and TransactivityThe Role of Oxygen Sensors, Hydroxylases, and HIF in Cardiac Function and DiseaseHIF hydroxylase pathways in cardiovascular physiology and medicineNutrient sensing, metabolism, and cell growth controlHIF1α and HIF2α: sibling rivalry in hypoxic tumour growth and progressionCrystal structure of human pirin: an iron-binding nuclear protein and transcription cofactorEvidence That Two Enzyme-derived Histidine Ligands Are Sufficient for Iron Binding and Catalysis by Factor Inhibiting HIF (FIH)Asparagine beta-hydroxylation stabilizes the ankyrin repeat domain foldSelective Inhibitors of the JMJD2 Histone Demethylases: Combined Nondenaturing Mass Spectrometric Screening and Crystallographic ApproachesQuantitative High-Throughput Screening Identifies 8-Hydroxyquinolines as Cell-Active Histone Demethylase InhibitorsHuman UTY(KDM6C) Is a Male-specific N -Methyl Lysyl DemethylaseSubstrate selectivity analyses of factor inhibiting hypoxia-inducible factorSubstrate-Trapped Interactors of PHD3 and FIH Cluster in Distinct Signaling Pathways
P2860
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P2860
Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family
description
2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2002
@ast
im Juli 2002 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2002/07/19)
@sk
vědecký článek publikovaný v roce 2002
@cs
wetenschappelijk artikel (gepubliceerd op 2002/07/19)
@nl
наукова стаття, опублікована в липні 2002
@uk
name
Hypoxia-inducible factor (HIF) ...... to the cupin structural family
@ast
Hypoxia-inducible factor (HIF) ...... to the cupin structural family
@en
Hypoxia-inducible factor (HIF) ...... to the cupin structural family
@nl
type
label
Hypoxia-inducible factor (HIF) ...... to the cupin structural family
@ast
Hypoxia-inducible factor (HIF) ...... to the cupin structural family
@en
Hypoxia-inducible factor (HIF) ...... to the cupin structural family
@nl
prefLabel
Hypoxia-inducible factor (HIF) ...... to the cupin structural family
@ast
Hypoxia-inducible factor (HIF) ...... to the cupin structural family
@en
Hypoxia-inducible factor (HIF) ...... to the cupin structural family
@nl
P2093
P50
P3181
P356
P1476
Hypoxia-inducible factor (HIF) ...... to the cupin structural family
@en
P2093
Alex N Bullock
Christopher W Pugh
Kirsty S Hewitson
Luke A McNeill
Madeline V Riordan
Richard W Welford
Ya-Min Tian
P304
26351-26355
P3181
P356
10.1074/JBC.C200273200
P407
P50
P577
2002-05-31T00:00:00Z