Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.
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PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an Nepsilon-dimethyl lysine demethylaseAsparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factorOGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formationFactor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domainsHydroxylation of the eukaryotic ribosomal decoding center affects translational accuracyNew insights into the role of RNase L in innate immunityThe Roles of RNase-L in Antimicrobial Immunity and the Cytoskeleton-Associated Innate ResponseHIF hydroxylase pathways in cardiovascular physiology and medicineMolecular signaling network motifs provide a mechanistic basis for cellular threshold responsesSubstrate selectivity analyses of factor inhibiting hypoxia-inducible factorSubstrate-Trapped Interactors of PHD3 and FIH Cluster in Distinct Signaling PathwaysFIH Regulates Cellular Metabolism through Hydroxylation of the Deubiquitinase OTUB1HIF prolyl hydroxylase inhibitors for anemiaPrediction and analysis of protein hydroxyproline and hydroxylysinePotent and Selective Triazole-Based Inhibitors of the Hypoxia-Inducible Factor Prolyl-Hydroxylases with Activity in the Murine BrainConsequences of IkappaB alpha hydroxylation by the factor inhibiting HIF (FIH)Ultrasensitive response motifs: basic amplifiers in molecular signalling networks.Hypoxia-dependent sequestration of an oxygen sensor by a widespread structural motif can shape the hypoxic response--a predictive kinetic model.iHyd-PseAAC: predicting hydroxyproline and hydroxylysine in proteins by incorporating dipeptide position-specific propensity into pseudo amino acid compositionThe asparaginyl hydroxylase factor inhibiting HIF-1alpha is an essential regulator of metabolismQuantification of proteins using data-independent analysis (MSE) in simple andcomplex samples: a systematic evaluation.Applications of proteomic technologies for understanding the premature proteolysis of CFTR.Small-molecule-based inhibition of histone demethylation in cells assessed by quantitative mass spectrometry.Differential sensitivity of hypoxia inducible factor hydroxylation sites to hypoxia and hydroxylase inhibitorsSILAC-based quantitative proteomic analysis of human lung cell response to copper oxide nanoparticles.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.New classes of mind bomb-interacting proteins identified from yeast two-hybrid screens.Quantitative mass spectrometry reveals dynamics of factor-inhibiting hypoxia-inducible factor-catalyzed hydroxylation.Factor inhibiting HIF (FIH) recognizes distinct molecular features within hypoxia-inducible factor-α (HIF-α) versus ankyrin repeat substratesThe FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity.Ankyrin Repeat Proteins of Orf Virus Influence the Cellular Hypoxia Response PathwayIdentification and proteomic analysis of distinct UBE3A/E6AP protein complexes.microRNA-31/factor-inhibiting hypoxia-inducible factor 1 nexus regulates keratinocyte differentiationProlyl hydroxylation regulates protein degradation, synthesis, and splicing in human induced pluripotent stem cell-derived cardiomyocytes.Hypoxia: from basic mechanisms to therapeutics - a meeting report on the Keystone and HypoxiaNet Symposium.Protein oxidation: role in signalling and detection by mass spectrometry.Tankyrases as drug targets.Cell cycle progression in response to oxygen levels.Tankyrases: structure, function and therapeutic implications in cancer.
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Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 20 October 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Proteomics-based identificatio ...... at domain-containing proteins.
@en
Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor
@nl
type
label
Proteomics-based identificatio ...... at domain-containing proteins.
@en
Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor
@nl
prefLabel
Proteomics-based identificatio ...... at domain-containing proteins.
@en
Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor
@nl
P2860
P50
P1476
Proteomics-based identificatio ...... eat domain-containing proteins
@en
P2093
James D Webb
P2860
P304
P356
10.1074/MCP.M800340-MCP200
P577
2008-10-20T00:00:00Z