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DALDLEMLAPYISMDDDFQL + 2-oxoglutarate + O2
?
a HIF-3alpha peptide. Vmax is 120% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DALDLEMLAPYISMDDDFQL + 2-oxoglutarate + O2
DALDLEMLA-((4R)-4-hydroxy-L-proline)-YISMDDDFQL + succinate + CO2
DALTLLAPAAGDTIISLDF + 2-oxoglutarate + O2
DALTLLA-((4R)-4-hydroxy-L-proline)-AAGDTIISLDF + succinate + CO2
hybrid substrate derived from C-terminal and N-terminal oxygen-dependent degradation domain
-
-
?
DALTLLAPAAGDTIISLDF + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-AAGDTIISLDF + succinate + CO2
substrate derived from N-terminal oxygen-dependent degradation domain
-
-
?
DALTLLAPAAGDTIISLFG + 2-oxoglutarate + O2
DALTLLA-((4R)-4-hydroxy-L-proline)-AAGDTIISLFG + succinate + CO2
DLDLEALAPYIPADDDFQL + 2-oxoglutarate + O2
DLDLEALA-((4R)-4-hydroxy-L-proline)-YIPADDDFQL + succinate + CO2
-
-
-
?
DLDLEMLAPAIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-AIPMDDDFQL + succinate + CO2
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLDLEMLAPGIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-GIPMDDDFQL + succinate + CO2
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLDLEMLAPYIPMD + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMD + succinate + CO2
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLDLEMLAPYIPMDD + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDD + succinate + CO2
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLDLEMLAPYIPMDDDF + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDF + succinate + CO2
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLDLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2
?
-
-
-
?
DLDLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
DLDLEMLAPYIPMDDDFQLRSFDQ + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQLRSFDQ + succinate + CO2
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLDLEMLAPYIPTIISLDF + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPTIISLDF + succinate + CO2
hybrid substrate derived from C-terminal and N-terminal oxygen-dependent degradation domain
-
-
?
DLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2
DLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
EEPDLSCLAPFVDTYDMMQM + 2-oxoglutarate + O2
?
ELDLETLAPYIPMDGEDFQ + 2-oxoglutarate + O2
?
ELDLETLAPYIPMDGEDFQ + 2-oxoglutarate + O2
ELDLETLA-((4R)-4-hydroxy-L-proline)-YIPMDGEDFQ + succinate + CO2
C-terminal hydroxylation site of HIF-2alpha. Vmax is 80% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
EMLAPYIPMDD + 2-oxoglutarate + O2
EMLA-((4R)-4-hydroxy-L-proline)-YIPMDD + succinate + CO2
Vmax is 30% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
EMLAPYIPMDDDFQL + 2-oxoglutarate + O2
EMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
EPEELAQLAPTPGDAIISLD + 2-oxoglutarate + O2
?
hypoxia-inducible factor 1alpha-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor 1alpha-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
hypoxia-inducible factor HIF1alpha-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor HIF1alpha-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor HIF2alpha-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor HIF2alpha-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor HIF3alpha-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor HIF3alpha-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor-alpha-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-alpha-trans-4-hydroxy-L-proline + succinate + CO2
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
hypoxia-inducible factor-L-proline peptide + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline peptide + succinate + CO2
-
peptide substrate is a peptide derived from the natural sequence of HIF-1alpha residues 556-574
hydroxylation at Pro564
-
?
hypoxia-inducible factor-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(3S)-3-hydroxy-proline + succinate + CO2
-
HIF-1alpha
-
-
?
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
hypoxia-inducible factor2alpha C-terminal oxygen dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor2alpha C-terminal oxygen dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor2alpha N-terminal oxygen dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor2alpha N-terminal oxygen dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
L-ascorbate + 2-oxoglutarate + O2
? + succinate + CO2
L-ascorbate is a co-substrate of HIF prolyl hydroxylase PHD that may compete for the binding site of 2-oxoglutarate in the enzyme active center
-
-
?
LAPYIPMDDDFQL + 2-oxoglutarate + O2
LA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
Vmax is 90% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
additional information
?
-
DALDLEMLAPYISMDDDFQL + 2-oxoglutarate + O2
DALDLEMLA-((4R)-4-hydroxy-L-proline)-YISMDDDFQL + succinate + CO2
a HIF-3alpha peptide. Vmax is 120% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DALDLEMLAPYISMDDDFQL + 2-oxoglutarate + O2
DALDLEMLA-((4R)-4-hydroxy-L-proline)-YISMDDDFQL + succinate + CO2
a HIF-3alpha peptide. Vmax is 150% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DALTLLAPAAGDTIISLFG + 2-oxoglutarate + O2
DALTLLA-((4R)-4-hydroxy-L-proline)-AAGDTIISLFG + succinate + CO2
N-terminal hydroxylation site of HIF-1alpha, Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DALTLLAPAAGDTIISLFG + 2-oxoglutarate + O2
DALTLLA-((4R)-4-hydroxy-L-proline)-AAGDTIISLFG + succinate + CO2
N-terminal hydroxylation site of HIF-1alpha, Vmax is 60% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
DLDLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
-
-
-
?
DLDLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
peptide derived from HIF-1alpha
-
-
?
DLDLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
substrate derived from C-terminal oxygen-dependent degradation domain
-
-
?
EEPDLSCLAPFVDTYDMMQM + 2-oxoglutarate + O2
?
hydroxylation site of Caenorhabditis elegans HIF-alpha. Vmax is 60% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
EEPDLSCLAPFVDTYDMMQM + 2-oxoglutarate + O2
?
hydroxylation site of Caenorhabditis elegans HIF-alpha. Vmax is 80% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
ELDLETLAPYIPMDGEDFQ + 2-oxoglutarate + O2
?
C-terminal hydroxylation site of HIF-2alpha. Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
ELDLETLAPYIPMDGEDFQ + 2-oxoglutarate + O2
?
C-terminal hydroxylation site of HIF-2alpha. Vmax is 70% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
EMLAPYIPMDDDFQL + 2-oxoglutarate + O2
EMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
EMLAPYIPMDDDFQL + 2-oxoglutarate + O2
EMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
Vmax is 80% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
EPEELAQLAPTPGDAIISLD + 2-oxoglutarate + O2
?
N-terminal hydroxylation site of HIF-2alpha. Vmax is 30% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
EPEELAQLAPTPGDAIISLD + 2-oxoglutarate + O2
?
N-terminal hydroxylation site of HIF-2alpha. Vmax is 70% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
EPEELAQLAPTPGDAIISLD + 2-oxoglutarate + O2
?
N-terminal hydroxylation site of HIF-2alpha. Vmax is 80% of the activity with DLDLEMLAPYIPMDDDFQL
-
-
?
hypoxia-inducible factor-alpha-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-alpha-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor-alpha-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-alpha-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
hypoxia-inducible factor-alpha-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-alpha-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2
-
HIF (hypoxia-inducible factor) is a transcription factor that plays a pivotal role in cellular adaptation to changes in oxygen availability. In the presence of oxygen, HIF is targeted for destruction by an E3 ubiquitin ligase containing the von Hippel-Lindau tumor suppressor protein (pVHL). Human pVHL binds to a short HIF-derived peptide when a conserved proline residue at the core of this peptide is hydroxylated. This protein modifiation may play a key role in mammalian oxygen sensing
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2
-
hypoxia-inducible factor (HIF) is a transcriptional complex that plays a central role in the regulation of gene expression by oxygen. In oxygenated and iron replete cells, HIF-alpha subunits are rapidly destroyed by a mechanism that involves ubiquitylation by the von Hippel-Lindau tumor suppressor (pVHL) E3 ligase complex. This process is suppressed by hypoxia and iron chelation, allowing transcriptional activation. The interaction between human pVHL and a specific domain of the HIF-1alpha subunit is regulated through hydroxylation of a proline residue (HIF-1alpha P564) by HIF-alpha prolyl-hydroxylase (HIF-PH). HIF-PH functions directly as a cellular oxygen sensor
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2
mammalian cells respond to changes in oxygen availability through a conserved pathway that is regulated by the hypoxia-inducible factor (HIF). The alpha subunit of the hypoxia-inducible factor is targeted for degradation under normoxic conditions by a ubiquitin-ligase complex that recognizes a hydroxylated proline residue in hypoxia-inducible factor. HIF prolyl hydroxylase is responsible for this posttranslational modification
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2
mammalian cells respond to changes in oxygen availability through a conserved pathway that is regulated by the hypoxia-inducible factor (HIF). The alpha subunit of the hypoxia-inducible factor is targeted for degradation under normoxic conditions by a ubiquitin-ligase complex that recognizes a hydroxylated proline residue in hypoxia-inducible factor. HIF prolyl is responsible for this posttranslational modification
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2
target proline residue: Pro564 in human HIF-alpha. A control peptide in which the target proline residue is replaced by alanine is not modified
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2
target proline residue: Pro564 in human HIF-alpha. A control peptide in which the target proline residue is replaced by alanine is not modified. The endogenous HIF prolyl hydroxylase, HPH-1 generates by in vitro transcription/translation does not modify peptides containing the L562A, A563G, or Y565A mutations. However, a peptide containing the Pro567 to Gly mutation is an equal, if not better, substrate for the human HPH enzymes
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2
target proline residue: Pro564 in human HIF-alpha. A control peptide in which the target proline residue is replaced by alanine is not modified. The recombinant HPH-2 purified from Escherichia coli does not modify peptides containing the L562A, A563G, or Y565A mutations. However, a peptide containing the Pro567 to Gly mutation is an equal, if not better, substrate for the human HPH enzymes
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
HIF1alpha is a better substrate than HIF2alpha for PHD2
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
PHD enzymes hydroxylates HIF-alpha at prolyl residues present in the transcriptional activation domain N-TAD
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
PHD2 hydroxylates Pro402 and/or Pro564 of HIF-1alpha
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
differential regulation of HIF1alpha and HIF2alpha at the N-terminal oxygen-dependent degradation domain site by PHD2
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
hydroxylation at P402 and P564
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
hydroxylation of the proline residue in the HIF-1alpha (556-574) peptide substrate, sequence of residues 556-574: DLDLEMLAPYIPMDDDFQL
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
the HIF1alpha C-terminal oxygen-dependent degradation domain is highly preferred for hydroxylation, no N-terminal oxygen-dependent degradation domain hydroxylation for both HIF2alpha and HIF1alpha
-
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
the PHD1 reaction at the N-terminal oxygen-dependent degradation domain site shows low level hydroxylation
-
-
?
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
low activity
-
-
?
hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2
low activity
-
-
?
additional information
?
-
-
the enzyme requires long peptide substrates. No hydroxylation of: Leu-Ala-Pro, Leu-Ala-Pro-Tyr, Leu-Glu-Met-Leu-Ala-Pro, and Leu-Glu-Met-Leu-Ala-Pro-Tyr
-
-
?
additional information
?
-
the enzyme requires long peptide substrates. No hydroxylation of: Leu-Ala-Pro, Leu-Ala-Pro-Tyr, Leu-Glu-Met-Leu-Ala-Pro, and Leu-Glu-Met-Leu-Ala-Pro-Tyr
-
-
?
additional information
?
-
the enzyme requires long peptide substrates. No hydroxylation of: Leu-Ala-Pro, Leu-Ala-Pro-Tyr, Leu-Glu-Met-Leu-Ala-Pro, and Leu-Glu-Met-Leu-Ala-Pro-Tyr
-
-
?
additional information
?
-
-
HIF prolyl-4-hydroxylase 2 substrate binding analysis using isolated sequences of the C-terminal oxygen degradation domain DLDLEALAP564YIPADDDFQL mutant M561A/M568A, and the N-terminal oxygen degradation domain DALTLLAP402AAGDTIISLDYG mutant F413Y, overview
-
-
?
additional information
?
-
-
substrate selectivity of PHD2 by kinetic competition assays, varied ionic strength, and global protein flexibility using amide H/D exchange, overview
-
-
?
additional information
?
-
the substrate contains a C-terminal and a N-terminal oxygen-dependent degradation domain, as well as a C-terminal transactivation domain
-
-
?
additional information
?
-
the substrate contains a C-terminal and a N-terminal oxygen-dependent degradation domain, as well as a C-terminal transactivation domain
-
-
?
additional information
?
-
the substrate contains a C-terminal and a N-terminal oxygen-dependent degradation domain, as well as a C-terminal transactivation domain
-
-
?
additional information
?
-
the subtrate contains a C-terminal and a N-terminal oxygen-dependent degradation domain, as well as a C-terminal transactivation domain
-
-
?
additional information
?
-
the subtrate contains a C-terminal and a N-terminal oxygen-dependent degradation domain, as well as a C-terminal transactivation domain
-
-
?
additional information
?
-
the subtrate contains a C-terminal and a N-terminal oxygen-dependent degradation domain, as well as a C-terminal transactivation domain
-
-
?
additional information
?
-
-
isozyme PHD2 is more active on hypoxia-inducible factor-1alpha than on hypoxia-inducible factor-2alpha, whereas PHD1 and PHD3 hydroxylate hypoxia-inducible factor-2alpha more efficiently
-
-
?
additional information
?
-
prolyl hydroxylation is not assigned on any of the teste non-HIF substrate sites. Recombinant PHD enzymes provide no support for the wide range of non-HIF PHD substrates reported
-
-
-
additional information
?
-
prolyl hydroxylation is not assigned on any of the teste non-HIF substrate sites. Recombinant PHD enzymes provide no support for the wide range of non-HIF PHD substrates reported
-
-
-
additional information
?
-
prolyl hydroxylation is not assigned on any of the teste non-HIF substrate sites. Recombinant PHD enzymes provide no support for the wide range of non-HIF PHD substrates reported
-
-
-
additional information
?
-
-
prolyl hydroxylation is not assigned on any of the teste non-HIF substrate sites. Recombinant PHD enzymes provide no support for the wide range of non-HIF PHD substrates reported
-
-
-
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(2R)-[2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetamido](phenyl)acetic acid
-
-
(2S)-[2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetamido](phenyl)acetic acid
-
-
1,1',1'',1'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetrapropan-2-ol
1-(5-chloro-6-(trifluoromethoxy)-1H-benzoimidazol-2-yl)-1H-pyrazole-4-carboxylic acid
-
i.e. JNJ-42041935, 2-oxoglutarate analogue
-
2,2',2'',2'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetraacetamide
-
chelates Fe2+ in a hexacoordinative mode through four nitrogens of the macrocycle and two oxygens in side arms
2,3-dihydroxypyridine
-
-
2-(2-(5-cyano-3-hydroxy-4-methylpyridin-2-yl)-5-methylthiazol-4-yl)-N-(2-(diethylamino)ethyl)acetamide
-
-
2-(2-(5-cyano-3-hydroxy-4-methylpyridin-2-yl)-5-phenylthiazol-4-yl)-N-(2-(pyridin-2-yl)ethyl)acetamide
-
-
2-(2-(5-cyano-3-hydroxypyridin-2-yl)-5-phenylthiazol-4-yl)-N-(2-(pyridin-2-yl)ethyl)acetamide
-
-
2-hydroxypyridine 1-oxide
-
-
2-[2-(5-cyano-3-hydroxy-4-methylpyridin-2-yl)-1,3-thiazol-4-yl]-N-[2-(diethylamino)ethyl]acetamide
-
-
2-[2-(5-cyano-3-hydroxy-4-methylpyridin-2-yl)-1,3-thiazol-4-yl]-N-[2-(pyridin-2-yl)ethyl]acetamide
-
-
2-[2-(5-cyano-3-hydroxy-4-methylpyridin-2-yl)-5-methyl-1,3-thiazol-4-yl]-N-propylacetamide
-
-
2-[2-(5-cyano-3-hydroxy-4-methylpyridin-2-yl)-5-methyl-1,3-thiazol-4-yl]-N-[2-(pyridin-2-yl)ethyl]acetamide
-
-
2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]-N-(2-phenylethyl)acetamide
-
-
2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]-N-[(1R)-2-hydroxy-1-phenylethyl]acetamide
-
-
2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]-N-[(1S)-2-hydroxy-1-phenylethyl]acetamide
-
-
2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]-N-[2-(pyridin-2-yl)ethyl]acetamide
-
-
2-[2-(5-cyano-3-hydroxypyridin-2-yl)-5-methyl-1,3-thiazol-4-yl]-N-[2-(pyridin-2-yl)ethyl]acetamide
-
-
2-[2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetamido]-2-methylpropanoic acid
-
-
3,3'-[(pyridin-2-ylmethyl)imino]dipropanenitrile
-
noncompetitive inhibition
3,3'-[(pyridin-4-ylimino)bis(propane-3,1-diyliminomethanediyl)]diphenol
-
noncompetitive inhibition
3,3'-[(pyridin-4-ylimino)bis[propane-3,1-diylnitrilo(Z)methylylidene]]diphenol
-
noncompetitive inhibition
3,4-dihydroxybenzoate
-
-
3,6,9-tris(naphthalen-1-ylmethyl)-3,6,9,15-tetraazabicyclo[9.3.1]pentadeca-1(15),11,13-triene
-
coordinates Fe2+ via triad or tetrad from nitrogen atoms of the parent ring, which leaves vacant position for other ligands binding
3-([1,1'-biphenyl]-4-yl)-8-[(3-methylpyridin-2-yl)methyl]-1-(pyrimidin-2-yl)-1,3,8-triazaspiro[4.5]decane-2,4-dione
compound stabilizes HIF-1alpha levels and is also active against lysine-specific demethylase KDM4A
-
3-carboxy-4-oxo-3,4-dihydro-1,10-phenanthroline
-
3-cyano-6-methyl-2(H)-pyridinone
-
-
3-hydroxy-1,2-dimethyl-4(1H)-pyridinone
-
-
3-hydroxy-2-methyl-4-pyrone
-
-
3-hydroxypyridine-2-carbonyl-glycine
-
3-[(1,3-benzoxazol-2-yl)carbamoyl]propanoic acid
-
-
3-[(5-chloro-1,3-benzoxazol-2-yl)carbamoyl]propanoic acid
-
-
4-hydroxy-2-(1H-pyrazol-1-yl)-N-[[4-(trifluoromethyl)phenyl]methyl]pyrimidine-5-carboxamide
-
-
4-hydroxy-N-[(1R)-2-hydroxy-1-phenylethyl]-2-(1H-pyrazol-1-yl)pyrimidine-5-carboxamide
-
-
4-hydroxy-N-[(4-phenoxyphenyl)methyl]-2-(1H-pyrazol-1-yl)pyrimidine-5-carboxamide
-
-
5-hydroxy-2-hydroxymethyl-4-pyrone
-
-
5-hydroxy-4-oxo-4H-pyran-2-carboxylic acid
-
-
5-hydroxy-6-[4-[2-oxo-2-(pyrrolidin-1-yl)ethyl]-1,3-thiazol-2-yl]pyridine-3-carbonitrile
-
-
6-[5-oxo-4-(1H-1,2,3-triazol-1-yl)-2,5-dihydro-1H-pyrazol-1-yl]pyridine-3-carboxylic acid
-
7-[(4-chlorophenyl)[(3-hydroxypyridin-2-yl)amino]methyl]quinolin-8-ol
-
CO releasing molecule-2
i.e.CORM-2, [RuCl2(CO)3]2, in situ CO donor, reduces the hydroxylation of C-terminal and N-terminal oxygen-dependent degradation domains of HIF-1alpha
-
desferrioxamine
-
iron chelator
dimethyloxalyl glycine
mimicks 2-oxoglutarate binding mode
-
DLDLEALA-L-3,4-dehydroproline-YIPADDDFQLR
-
-
DLDLEALA-L-4-thioproline-YIPADDDFQLR
-
-
DLDLEALA-L-piperidine-2-carboxylic acid-YIPADDDFQLR
-
-
DLDLEALA-L-trans-4-fluoroproline-YIPADDDFQLR
-
-
DLDLEALA-L-trans-4-hydroxyproline-YIPADDDFQLR
-
-
ethyl 3,4-dihydroxybenzoate
iron chelator that can fit inside the active center
H2O2
-
poor inhibition. Prolyl hydroxylase is less sensitive to peroxide, preferential inhibition of N803-hydroxylation by FIH, EC 1.14.11.30, compared with inhibition of P402/P564 hydroxylation by PHDs
IOX2
mimicks 2-oxoglutarate binding mode
-
JNJ1935
-
a prolyl-hydroxylase selective inhibitor. Low concentrations of JNJ1935 selectively inhibit PHDs, whereas higher concentrations inhibit all hydroxylases, including FIH, EC 1.14.11.30, in vitro and in vivo inhibition
N,N-dimethyl-5-[3,6,9,15-tetraazabicyclo[9.3.1]pentadeca-1(15),11,13-trien-6-ylsulfonyl]naphthalen-1-amine
-
coordinates Fe2+ via triad or tetrad from nitrogen atoms of the parent ring, which leaves vacant position for other ligands binding
N-((3,4-dimethoxyphenyl)(8-hydroxyquinolin-7-yl)methyl)-2-phenylacetamide
-
N-((3-hydroxy-6-chloroquinolin-2-yl)carbonyl)glycine
-
N-(1-[[6-(4-chlorophenoxy)pyridin-3-yl]methyl]-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridine-3-carbonyl)glycine
clinical candidate as PHD2 inhibitor, promotes the production of erythropoietin following oral administration in mice and rats. The predicted half-life in humans is 1.3-5.6 h
-
N-(4-hydroxy-1-[[4-(4-methylphenoxy)phenyl]methyl]-2-oxo-1,2,5,6-tetrahydropyridine-3-carbonyl)glycine
-
-
N-(4-hydroxy-1-[[5-(4-methylphenoxy)pyridin-2-yl]methyl]-2-oxo-1,2,5,6-tetrahydropyridine-3-carbonyl)glycine
-
-
N-(4-hydroxy-1-[[6-(4-methylphenoxy)pyridin-3-yl]methyl]-2-oxo-1,2,5,6-tetrahydropyridine-3-carbonyl)glycine
-
-
N-(methoxyoxoacetyl)-glycine methyl ester
-
a pan-hydroxylase inhibitor, in vitro and in vivo inhibition
N-([1,1'-biphenyl]-4-yl)-4-hydroxy-2-(1H-pyrazol-1-yl)pyrimidine-5-carboxamide
compound stabilizes HIF-1alpha levels
-
N-benzyl-2-[2-(3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetamide
-
-
N-benzyl-2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetamide
-
-
N-oxalyl-(2S)-alanine
-
competed by 2-oxoglutarate, no inhibition by the enantiomer N-oxalyl-(2R)-alanine
N-[(1,3-dihydro-2-benzofuran-5-yl)methyl]-4-hydroxy-2-(1H-pyrazol-1-yl)pyrimidine-5-carboxamide
-
-
N-[(3,4-dimethoxyphenyl)(8-hydroxyquinolin-7-yl)methyl]-2-phenylacetamide
-
optimized adaptaquin analog, shows no toxicity up to a 100fold increased range over EC50. The drug is ismetabolized by CYP3A4 and CYP2B6
-
N-[([1,1'-biphenyl]-4-yl)methyl]-4-hydroxy-2-(1H-pyrazol-1-yl)pyrimidine-5-carboxamide
-
-
N-[1-[([1,1'-biphenyl]-4-yl)methyl]-4-hydroxy-2-oxo-1-azaspiro[5.5]undec-3-ene-3-carbonyl]glycine
lead compound for synthesis of orally administered agents for the treatment of renal anemia
-
oxygen
the transiently overexpressed HPH-1 enzyme is inhibited by a low-oxygen environment
Pyridine-2,4-dicarboxylate
-
RuCl3
inhibitor of PHD2 under the standard assay conditions in presence of 10 microM Fe(II). This effect can be alleviated by supplementing the enzymatic reaction mixture with excess Fe(II)
tert-butyl 6-(5-oxo-4-(1H-1,2,3-triazol-1-yl)-2,5-dihydro-1H-pyrazol-1-yl)nicotinate
potent and selective inhibitor of isoform PHD2
[(1-benzyl-4-hydroxy-2-oxo-1,2-dihydroquinoline-3-carbonyl)amino]acetic acid
-
[(1-chloro-4-hydroxyisoquinoline-3-carbonyl)amino]acetic acid
-
[(2E)-3-hydroxy-2-({[(naphthalen-2-yl)methanesulfonyl]acetyl}imino)-2,3-dihydro-1,3-thiazol-4-yl]acetic acid
-
[(4-hydroxy-1-methyl-2-oxo-1,2-dihydroquinoline-3-carbonyl)amino]acetic acid
-
[2-(3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetic acid
-
-
[2-(3-hydroxypyridin-2-yl)-6-oxo-1,6-dihydropyrimidin-5-yl]acetic acid
-
-
[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetic acid
-
-
[2-(5-cyano-3-hydroxypyridin-2-yl)-6-oxo-1,6-dihydropyrimidin-5-yl]acetic acid
-
-
[2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetamido]acetic acid
-
-
1,1',1'',1'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetrapropan-2-ol
-
noncompetitive inhibition
1,1',1'',1'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetrapropan-2-ol
-
chelates Fe2+ in a hexacoordinative mode through four nitrogens of the macrocycle and two oxygens in side arms
adaptaquin
-
-
adaptaquin
-
EC50 of ca 2 mM in HIF1 ODD-luc fusion reporter assay
-
ciclopirox
-
Cu2+
-
binding analysis
dimethyloxalylglycine
-
-
dimethyloxalylglycine
-
2-oxoglutarate analogue
FG-4592
-
FG-4592
mimicks 2-oxoglutarate binding mode
FG-4592
-
i.e. roxadustat, 2-oxoglutarate analogue
N-oxalylglycine
-
competed by 2-oxoglutarate
additional information
-
the peptide inhibitors consist of amino acids identical to those in the CODD556-575 except the 564 proline residue, and target the C-terminal oxygen-dependent degradation domain binding site in the PHD2 active pocket. Specific inhibition of PHD2, no inhibition of FIH, EC 1.14.11.30
-
additional information
-
temporal dynamics of hydroxylase inhibition, overview
-
additional information
-
polynitrogen compound as HIF-1alpha PHD3 inhibitors, the metal complexes of these polynitrogen compounds cannot inhibit the catalytical activity of PHD3, overview. The inhibitory mechanism of PHD3 activity by polynitrogen compounds is due to their binding to iron to form stable coordination complexes
-
additional information
-
screening of iron chelators pyridines, hydroxypyrones/hydroxypyridinones, and catechols as inhibitors for PHD2, analysis of selectivity of the inhibitors for PHD2 compared to FIH, EC 1.14.11.30. Ligand binding kinetics and structural analysis, overview. Representative inhibitors bind to the metal center in PHD2 as an 2-oxoglutarate mimic
-
additional information
-
inhibition of the recombinant human PHD3 activity by tetraazamacrocycles, overview
-
additional information
compounds with a 3-carbamoylpropanoic acids-containing benzoxazole moiety are inhibitors of PHD-2. However, neither the acids nor their respective ethyl esters upregulate HIF-1alpha levels in cells
-
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Acute Kidney Injury
Pre-ischemic Targeting of HIF Prolyl Hydroxylation Inhibits Fibrosis associated with Acute Kidney Injury.
Adenocarcinoma
Induction of apoptosis in human pancreatic carcinoma cells by a synthetic bleomycin-like ligand.
Adenocarcinoma of Lung
An integrative functional genomics approach reveals EGLN1 as a novel therapeutic target in KRAS mutated lung adenocarcinoma.
Adenocarcinoma of Lung
Elevated PHD2 expression might serve as a valuable biomarker of poor prognosis in lung adenocarcinoma, but no lung squamous cell carcinoma.
Adenoma, Oxyphilic
Somatic pairing of chromosome 19 in renal oncocytoma is associated with deregulated ELGN2-mediated oxygen-sensing response.
Altitude Sickness
EPAS1 and EGLN1 associations with high altitude sickness in Han and Tibetan Chinese at the Qinghai-Tibetan Plateau.
Altitude Sickness
Population History and Altitude-Related Adaptation in the Sherpa.
Altitude Sickness
Variants of the low oxygen sensors EGLN1 and HIF-1AN associated with acute mountain sickness.
Anemia
A mechanistic link between renal ischemia and fibrosis.
Anemia
A small-molecule inhibitor of hypoxia-inducible factor prolyl hydroxylase improves obesity, nephropathy and cardiomyopathy in obese ZSF1 rats.
Anemia
American chemical society - 239th national meeting - investigating new therapeutic candidates: part 2.
Anemia
Anemia in conventional hemodialysis: Finding the optimal treatment balance.
Anemia
Discovery of Molidustat (BAY 85-3934): A Small-Molecule Oral HIF-Prolyl Hydroxylase (HIF-PH) Inhibitor for the Treatment of Renal Anemia.
Anemia
Effects of oral iron and calcium supplement on the pharmacokinetics and pharmacodynamics of molidustat: an oral HIF-PH inhibitor for the treatment of renal anaemia.
Anemia
ESA, Iron Therapy and New Drugs: Are There New Perspectives in the Treatment of Anaemia?
Anemia
First-in-man / proof of concept study with molidustat - a novel selective oral HIF-prolyl hydroxylase inhibitor for the treatment of renal anaemia.
Anemia
Hearts of hypoxia-inducible factor prolyl 4-hydroxylase-2 hypomorphic mice show protection against acute ischemia-reperfusion injury.
Anemia
HIF hydroxylase inhibitors decrease cellular oxygen consumption depending on their selectivity.
Anemia
HIF prolyl hydroxylase inhibitors for anemia.
Anemia
Hypoxia-Inducible Factor Activators in Renal Anemia: Current Clinical Experience.
Anemia
Hypoxia-inducible factor prolyl hydroxylase domain inhibitor may maintain hemoglobin synthesis at lower serum ferritin and transferrin saturation levels than darbepoetin alfa.
Anemia
Hypoxia-inducible factor prolyl hydroxylase inhibitors: a paradigm shift for treatment of anemia in chronic kidney disease?
Anemia
Hypoxia-Inducible Factor Prolyl Hydroxylase Inhibitors: A Potential New Treatment for Anemia in Patients With CKD.
Anemia
Hypoxia-inducible factor stabilizers for treating anemia of chronic kidney disease.
Anemia
Hypoxia-Inducible Factor-Prolyl Hydroxylase Domain Inhibitors to Treat Anemia in Chronic Kidney Disease.
Anemia
Inhibition of prolyl hydroxylase domain (PHD) by JTZ-951 reduces obesity-related diseases in the liver, white adipose tissue, and kidney in mice with a high-fat diet.
Anemia
Managing Anemia across the Stages of Kidney Disease in Those Hyporesponsive to Erythropoiesis-Stimulating Agents.
Anemia
New cancer targets emerging from studies of the Von Hippel-Lindau tumor suppressor protein.
Anemia
Nonclinical Characterization of the Hypoxia-Inducible Factor Prolyl Hydroxylase Inhibitor Roxadustat, a Novel Treatment of Anemia of Chronic Kidney Disease.
Anemia
Novel Iron Parameters in Patients with Type 2 Diabetes Mellitus in Relation to Kidney Function.
Anemia
Pre-ischemic Targeting of HIF Prolyl Hydroxylation Inhibits Fibrosis associated with Acute Kidney Injury.
Anemia
Profile of Daprodustat in the Treatment of Renal Anemia Due to Chronic Kidney Disease.
Anemia
Prolyl Hydroxylase Domain Inhibitor Protects against Metabolic Disorders and Associated Kidney Disease in Obese Type 2 Diabetic Mice.
Anemia
Prolyl hydroxylase domain inhibitors as a novel therapeutic approach against anemia in chronic kidney disease.
Anemia
Prolyl hydroxylase domain inhibitors: a new era in the management of renal anemia.
Anemia
Pyrazolo[4,3-d]pyrimidine Derivatives as a Novel Hypoxia-Inducible Factor Prolyl Hydroxylase Domain Inhibitor for the Treatment of Anemia.
Anemia
Recommendations by the Asian Pacific society of nephrology (APSN) on the appropriate use of HIF-PH inhibitors.
Anemia
Suppression of thyrotropin secretion during roxadustat treatment for renal anemia in a patient undergoing hemodialysis.
Anemia
Therapeutic targeting of the HIF oxygen-sensing pathway: Lessons learned from clinical studies.
Anemia
Treatment of anemia in difficult-to-manage patients with chronic kidney disease.
Anemia
Treatment of Renal Anemia with Roxadustat: Advantages and Achievement.
Anemia
[Future perspectives of treatment for anemia in chronic kidney disease (CKD) using hypoxia-inducible factor prolyl hydroxylase inhibitors].
Aneurysm
Circulating tetrahydrobiopterin as a novel biomarker for abdominal aortic aneurysm.
Aortic Aneurysm, Abdominal
Recoupling of eNOS with folic acid prevents abdominal aortic aneurysm formation in angiotensin II-infused apolipoprotein E null mice.
Aortic Aneurysm, Abdominal
Role of uncoupled endothelial nitric oxide synthase in abdominal aortic aneurysm formation: treatment with folic acid.
Aortic Aneurysm, Abdominal
Suppression of abdominal aortic aneurysm formation by inhibition of prolyl hydroxylase domain protein through attenuation of inflammation and extracellular matrix disruption.
Atherosclerosis
Deficiency of the oxygen sensor prolyl hydroxylase 1 attenuates hypercholesterolaemia, atherosclerosis, and hyperglycaemia.
Autoimmune Diseases
American chemical society - 239th national meeting - investigating new therapeutic candidates: part 2.
Bone Resorption
Hypoxia-inducible factor 1-alpha does not regulate osteoclastogenesis but enhances bone resorption activity via prolyl-4-hydroxylase 2.
Brain Injuries
Neuron-Specific Prolyl-4-Hydroxylase Domain 2 Knockout Reduces Brain Injury After Transient Cerebral Ischemia.
Breast Neoplasms
Control of cyclin D1 and breast tumorigenesis by the EglN2 prolyl hydroxylase.
Breast Neoplasms
Detection of a 4-bp Insertion/deletion Polymorphism within the Promoter of EGLN2 Using Mismatch PCR-RFLP and Its Association with Susceptibility to Breast Cancer
Breast Neoplasms
DNA methylation analysis of the HIF-1? prolyl hydroxylase domain genes PHD1, PHD2, PHD3 and the factor inhibiting HIF gene FIH in invasive breast carcinomas.
Breast Neoplasms
EglN2 associates with the NRF1-PGC1? complex and controls mitochondrial function in breast cancer.
Breast Neoplasms
EglN2 contributes to triple negative breast tumorigenesis by functioning as a substrate for the FBW7 tumor suppressor.
Breast Neoplasms
EglN2 positively regulates mitochondrial function in breast cancer.
Breast Neoplasms
Hypoxia represses microRNA biogenesis proteins in breast cancer cells.
Breast Neoplasms
Hypoxia-inducible factor prolyl hydroxylase 2 (PHD2) is a direct regulator of epidermal growth factor receptor (EGFR) signaling in breast cancer.
Breast Neoplasms
Knockdown of prolyl-4-hydroxylase domain 2 inhibits tumor growth of human breast cancer MDA-MB-231 cells by affecting TGF-?1 processing.
Breast Neoplasms
Long non-coding RNA LINC00662 promotes proliferation and migration of breast cancer cells via regulating the miR-497-5p/EglN2 axis.
Breast Neoplasms
Paracrine Induction of HIF by Glutamate in Breast Cancer: EglN1 Senses Cysteine.
Breast Neoplasms
Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer.
Breast Neoplasms
Targeting MCM2 function as a novel strategy for the treatment of highly malignant breast tumors.
Carcinogenesis
Association of chromosome 19 to lung cancer genotypes and phenotypes.
Carcinogenesis
Control of cyclin D1 and breast tumorigenesis by the EglN2 prolyl hydroxylase.
Carcinogenesis
Edging toward new therapeutics with cyclin D1 Egl'ng on cancer.
Carcinogenesis
EglN2 associates with the NRF1-PGC1? complex and controls mitochondrial function in breast cancer.
Carcinogenesis
EglN2 contributes to triple negative breast tumorigenesis by functioning as a substrate for the FBW7 tumor suppressor.
Carcinogenesis
EglN2 positively regulates mitochondrial function in breast cancer.
Carcinogenesis
Prolyl hydroxylase domain 2 protein is a strong prognostic marker in human gastric cancer.
Carcinogenesis
Renal cyst formation in Fh1-deficient mice is independent of the Hif/Phd pathway: roles for fumarate in KEAP1 succination and Nrf2 signaling.
Carcinogenesis
Waves of gene regulation suppress and then restore oxidative phosphorylation in cancer cells.
Carcinoma
Activation of prolyl hydroxylase-2 for stabilization of mitochondrial stress along with simultaneous downregulation of HIF-1?/FASN in ER + breast cancer subtype.
Carcinoma
An insertion/deletion polymorphism within RERT-lncRNA modulates hepatocellular carcinoma risk.
Carcinoma
Decreased prolyl hydroxylase 3 mRNA expression in oncocytomas compared with clear cell renal cell carcinoma.
Carcinoma
Effect of Voacamine upon inhibition of hypoxia induced fatty acid synthesis in a rat model of methyln-nitrosourea induced mammary gland carcinoma.
Carcinoma
Elevated PHD2 expression might serve as a valuable biomarker of poor prognosis in lung adenocarcinoma, but no lung squamous cell carcinoma.
Carcinoma
Hypoxia-inducible factor (HIF)-independent expression mechanism and novel function of HIF prolyl hydroxylase-3 in renal cell carcinoma.
Carcinoma
Induction of apoptosis in human pancreatic carcinoma cells by a synthetic bleomycin-like ligand.
Carcinoma, Hepatocellular
Effect of stable transfection with PHD3 on growth and proliferation of HepG2 cells in vitro and in vivo.
Carcinoma, Hepatocellular
Prolyl hydroxylase domain protein 3 and asparaginyl hydroxylase factor inhibiting HIF-1 levels are predictive of tumoral behavior and prognosis in hepatocellular carcinoma.
Carcinoma, Non-Small-Cell Lung
The expression of prolyl hydroxylase domain enzymes are up-regulated and negatively correlated with Bcl-2 in non-small cell lung cancer.
Carcinoma, Renal Cell
Decreased prolyl hydroxylase 3 mRNA expression in oncocytomas compared with clear cell renal cell carcinoma.
Carcinoma, Renal Cell
Hypoxia-inducible factor (HIF)-independent expression mechanism and novel function of HIF prolyl hydroxylase-3 in renal cell carcinoma.
Carcinoma, Renal Cell
iTRAQ proteomic identification of pVHL-dependent and -independent targets of Egln1 prolyl hydroxylase knockdown in renal carcinoma cells.
Carcinoma, Squamous Cell
Elevated PHD2 expression might serve as a valuable biomarker of poor prognosis in lung adenocarcinoma, but no lung squamous cell carcinoma.
Choroidal Neovascularization
Gene Transfer of Prolyl Hydroxylase Domain 2 Inhibits Hypoxia-inducible Angiogenesis in a Model of Choroidal Neovascularization.
Chronic Limb-Threatening Ischemia
HIF-prolyl hydroxylase 2 inhibition enhances the efficiency of mesenchymal stem cells-based therapies for the treatment of critical limb ischemia.
Colitis
Hypoxia and gastrointestinal disease.
Colitis
Loss of Prolyl Hydroxylase-1 Protects Against Colitis Through Reduced Epithelial Cell Apoptosis and Increased Barrier Function.
Colitis
N-(2-Mercaptopropionyl)-glycine, a diffusible antioxidant, activates HIF-1 by inhibiting HIF prolyl hydroxylase-2: implication in amelioration of rat colitis by the antioxidant.
Colitis
Therapeutic treatment with a novel hypoxia-inducible factor hydroxylase inhibitor (TRC160334) ameliorates murine colitis.
Colorectal Neoplasms
An insertion/deletion polymorphism within the promoter of EGLN2 is associated with susceptibility to colorectal cancer.
Dystonia
Alterations in expression of dopamine receptors and neuropeptides in the striatum of GTP cyclohydrolase-deficient mice.
Dystonia
Congenic mapping and genotyping of the tetrahydrobiopterin-deficient hph-1 mouse.
Dystonia
GCH1 variants, tetrahydrobiopterin and their effects on pain sensitivity.
Dystonia
Tetrahydrobiopterin and biogenic amine metabolism in the hph-1 mouse.
Endometrial Neoplasms
Induction of human endometrial cancer cell senescence through modulation of HIF-1alpha activity by EGLN1.
Escherichia coli Infections
Acidosis induces antimicrobial peptide expression and resistance to uropathogenic E. coli infection in kidney collecting duct cells via HIF-1?.
Gastroparesis
In vivo ultrasound assessment of gastric emptying in newborn mice.
Glioblastoma
Prolyl-4-hydroxylase 2 enhances hypoxia-induced glioblastoma cell death by regulating the gene expression of hypoxia-inducible factor-?.
Glioma
Enhanced delivery efficiency of recombinant adenovirus into tumor and mesenchymal stem cells by a novel PTD.
Glucose Intolerance
Tetrahydrobiopterin activates brown adipose tissue and regulates systemic energy metabolism.
gtp cyclohydrolase i deficiency
GTP cyclohydrolase I expression, protein, and activity determine intracellular tetrahydrobiopterin levels, independent of GTP cyclohydrolase feedback regulatory protein expression.
gtp cyclohydrolase i deficiency
Tetrahydrobiopterin deficiency and brain nitric oxide synthase in the hph1 mouse.
Heart Defects, Congenital
An EGLN1 mutation may regulate hypoxic response in cyanotic congenital heart disease through the PHD2/HIF-1A pathway.
Herpes Simplex
Antiviral activities against herpes simplex virus type 1 by HPH derivatives and their structure-activity relationships.
Hyperemia
GTP-cyclohydrolase deficiency induced peripheral and deep microcirculation dysfunction with age.
Hyperglycemia
Elevating VEGF-A and PDGF-BB secretion by salidroside enhances neoangiogenesis in diabetic hind-limb ischemia.
Hyperglycemia
ROS- and HIF1?-dependent IGFBP3 upregulation blocks IGF1 survival signaling and thereby mediates high-glucose-induced cardiomyocyte apoptosis.
Hypersensitivity
Erythrocytosis: genes and pathways involved in disease development.
Hypertension
GTP cyclohydrolase I/BH4 pathway protects EPCs via suppressing oxidative stress and thrombospondin-1 in salt-sensitive hypertension.
Hypertension
Pulmonary hypertension in a GTP-cyclohydrolase 1-deficient mouse.
Hypertension
Role of uncoupled endothelial nitric oxide synthase in abdominal aortic aneurysm formation: treatment with folic acid.
Hypertension
[Correlation between EGLN1 gene, protein express in lung tissue of rats and pulmonary artery pressure at different altitude].
Hypertension, Pulmonary
Pivotal role for endothelial tetrahydrobiopterin in pulmonary hypertension.
Hypertension, Pulmonary
Prolyl Hydroxylase Domain-2 Protein Regulates Lipopolysaccharide-Induced Vascular Inflammation.
Hypertension, Pulmonary
Pulmonary hypertension in the newborn GTP cyclohydrolase I-deficient mouse.
hypoxia-inducible factor-proline dioxygenase deficiency
Neuronal prolyl-4-hydroxylase 2 deficiency improves cognitive abilities in a murine model of cerebral hypoperfusion.
hypoxia-inducible factor-proline dioxygenase deficiency
Tetrahydrobiopterin (BH
Infections
Acidosis induces antimicrobial peptide expression and resistance to uropathogenic E. coli infection in kidney collecting duct cells via HIF-1?.
Infections
Hypoxic gene expression in chronic hepatitis B virus infected patients is not observed in state-of-the-art in vitro and mouse infection models.
Insulin Resistance
Tetrahydrobiopterin activates brown adipose tissue and regulates systemic energy metabolism.
Intellectual Disability
Transmembrane Prolyl 4-Hydroxylase is a Novel Regulator of Calcium Signaling in Astrocytes.
Ischemic Attack, Transient
Neuron-Specific Prolyl-4-Hydroxylase Domain 2 Knockout Reduces Brain Injury After Transient Cerebral Ischemia.
Ischemic Stroke
HIF-prolyl hydroxylase 2 silencing using siRNA delivered by MRI-visible nanoparticles improves therapy efficacy of transplanted EPCs for ischemic stroke.
Ischemic Stroke
Neuronal deficiency of HIF prolyl 4-hydroxylase 2 in mice improves ischemic stroke recovery in an HIF dependent manner.
Kidney Diseases
?-Ketoglutarate-related inhibitors of HIF prolyl hydroxylases are substrates of renal organic anion transporters 1 (OAT1) and 4 (OAT4).
Kidney Diseases
A small-molecule inhibitor of hypoxia-inducible factor prolyl hydroxylase improves obesity, nephropathy and cardiomyopathy in obese ZSF1 rats.
Kidney Diseases
Inhibitors of oxygen sensing prolyl hydroxylases regulate nuclear localization of the transcription factors Smad2 and YAP/TAZ involved in CTGF synthesis.
Kidney Diseases
Prolyl Hydroxylase Domain Inhibitor Protects against Metabolic Disorders and Associated Kidney Disease in Obese Type 2 Diabetic Mice.
Liver Diseases
Regulatory Role of Endothelial PHD2 in the Hepatic Steatosis.
Liver Neoplasms
Effect of prolyl hydroxylase domain-2 haplodeficiency on the hepatocarcinogenesis in mice.
Lung Neoplasms
Correlations of an Insertion/Deletion Polymorphism (rs10680577) in the RERT-lncRNA with the Susceptibility, Clinicopathological Features, and Prognosis of Lung Cancer.
Lung Neoplasms
Gene Expression Levels of the Prolyl Hydroxylase Domain Proteins PHD1 and PHD2 but Not PHD3 Are Decreased in Primary Tumours and Correlate with Poor Prognosis of Patients with Surgically Resected Non-Small-Cell Lung Cancer.
Lung Neoplasms
The expression of prolyl hydroxylase domain enzymes are up-regulated and negatively correlated with Bcl-2 in non-small cell lung cancer.
Lung Neoplasms
The predictive prognostic values of CBFA2T3, STX3, DENR, EGLN1, FUT4, and PCDH7 in lung cancer.
Lung Neoplasms
Variants in two adjacent genes, EGLN2 and CYP2A6, influence smoking behavior related to disease risk via different mechanisms.
Melanoma
Endothelin-1 inhibits prolyl hydroxylase domain 2 to activate hypoxia-inducible factor-1alpha in melanoma cells.
Melanoma
Melanoma antigen-11 inhibits the hypoxia-inducible factor prolyl hydroxylase 2 and activates hypoxic response.
Mitochondrial Diseases
Biallelic P4HTM variants associated with HIDEA syndrome and mitochondrial respiratory chain complex I deficiency.
Monoclonal Gammopathy of Undetermined Significance
The prolyl-hydroxylase EGLN3 and not EGLN1 is inactivated by methylation in plasma cell neoplasia.
Mouth Neoplasms
Hypoxia responsiveness linked variant in EGLN1 gene is enriched in oral cancer patients.
Multiple Myeloma
The prolyl-hydroxylase EGLN3 and not EGLN1 is inactivated by methylation in plasma cell neoplasia.
Myocardial Infarction
Targeted Gene deletion of Prolyl Hydroxylase Domain Protein 3 Triggers Angiogenesis And Preserves Cardiac Function by stabilizing Hypoxia inducible Factor 1 Alpha Following Myocardial Infarction.
Nasopharyngeal Neoplasms
Identification and characterization of the hypoxia-responsive element in human stanniocalcin-1 gene.
Neoplasm Metastasis
Extracellular matrix signatures of human mammary carcinoma identify novel metastasis promoters.
Neoplasm Metastasis
Hypoxia-inducible factors as key regulators of tumor inflammation.
Neoplasm Metastasis
Loss of prolyl hydroxylase-2 in myeloid cells and T-lymphocytes impairs tumor development.
Neoplasm Metastasis
Overexpression of hydroxyproline via EGLN/HIF1A is associated with distant metastasis in pancreatic cancer.
Neoplasm Metastasis
Thermal unfolding pathway of PHD2 catalytic domain in three different PHD2 species: computational approaches.
Neoplasms
A New Role for PHD in Chemotherapy.
Neoplasms
Activation of prolyl hydroxylase-2 for stabilization of mitochondrial stress along with simultaneous downregulation of HIF-1?/FASN in ER + breast cancer subtype.
Neoplasms
An insertion/deletion polymorphism within RERT-lncRNA modulates hepatocellular carcinoma risk.
Neoplasms
Analysis of the oxygen sensing pathway genes in familial chronic myeloproliferative neoplasms and identification of a novel EGLN1 germ-line mutation.
Neoplasms
Association between an indel polymorphism within the distal promoter of EGLN2 and cancer risk: An updated meta-analysis.
Neoplasms
Association of EGLN2 rs10680577 Polymorphism with the Risk and Clinicopathological Features of Patients with Prostate Cancer.
Neoplasms
Clockophagy is a novel selective autophagy process favoring ferroptosis.
Neoplasms
Control of cyclin D1 and breast tumorigenesis by the EglN2 prolyl hydroxylase.
Neoplasms
Correlations of an Insertion/Deletion Polymorphism (rs10680577) in the RERT-lncRNA with the Susceptibility, Clinicopathological Features, and Prognosis of Lung Cancer.
Neoplasms
Decreased prolyl hydroxylase 3 mRNA expression in oncocytomas compared with clear cell renal cell carcinoma.
Neoplasms
Distinct deregulation of the hypoxia inducible factor by PHD2 mutants identified in germline DNA of patients with polycythemia.
Neoplasms
Edging toward new therapeutics with cyclin D1 Egl'ng on cancer.
Neoplasms
Effect of prolyl hydroxylase domain-2 haplodeficiency on the hepatocarcinogenesis in mice.
Neoplasms
Effect of stable transfection with PHD3 on growth and proliferation of HepG2 cells in vitro and in vivo.
Neoplasms
EglN2 contributes to triple negative breast tumorigenesis by functioning as a substrate for the FBW7 tumor suppressor.
Neoplasms
EGLN2 DNA methylation and expression interact with HIF1A to affect survival of early-stage NSCLC.
Neoplasms
Elevated PHD2 expression might serve as a valuable biomarker of poor prognosis in lung adenocarcinoma, but no lung squamous cell carcinoma.
Neoplasms
Estrogen receptor ? sustains epithelial differentiation by regulating prolyl hydroxylase 2 transcription.
Neoplasms
Exposure to cigarette smoke induces overexpression of von Hippel-Lindau tumor suppressor in mouse skeletal muscle.
Neoplasms
Extracellular matrix signatures of human mammary carcinoma identify novel metastasis promoters.
Neoplasms
Gene Expression Levels of the Prolyl Hydroxylase Domain Proteins PHD1 and PHD2 but Not PHD3 Are Decreased in Primary Tumours and Correlate with Poor Prognosis of Patients with Surgically Resected Non-Small-Cell Lung Cancer.
Neoplasms
Genome-wide Analysis of Common Copy Number Variation and Epithelial Ovarian Cancer Risk.
Neoplasms
Genome-Wide Interrogation of Human Cancers Identifies EGLN1 Dependency in Clear Cell Ovarian Cancers.
Neoplasms
HIF prolyl hydroxylase-2 inhibition diminishes tumor growth through matrix metalloproteinase-induced TGF? activation.
Neoplasms
HIF prolyl hydroxylase-3 mediates alpha-ketoglutarate-induced apoptosis and tumor suppression.
Neoplasms
Hypoxia Exacerbates Inflammatory Acute Lung Injury via the Toll-Like Receptor 4 Signaling Pathway.
Neoplasms
Hypoxia Pathway Mutations in Pheochromocytomas and Paragangliomas.
Neoplasms
Hypoxia-inducible factors as key regulators of tumor inflammation.
Neoplasms
Identification of a novel recurrent 1q42.2-1qter deletion in high risk MYCN single copy 11q deleted neuroblastomas.
Neoplasms
Identification of hub genes and key pathways associated with the progression of gynecological cancer.
Neoplasms
Induction of human endometrial cancer cell senescence through modulation of HIF-1alpha activity by EGLN1.
Neoplasms
Induction of plasminogen activator inhibitor I gene expression by intracellular calcium via hypoxia-inducible factor-1.
Neoplasms
Inhibition of HIF Prolyl Hydroxylase-2 Blocks Tumor Growth in Mice through the Anti-Proliferative Activity of Transforming Growth Factor{beta}
Neoplasms
Inhibition of poly adenosine diphosphate-ribose polymerase decreases hepatocellular carcinoma growth by modulation of tumor-related gene expression.
Neoplasms
Knockdown of prolyl-4-hydroxylase domain 2 inhibits tumor growth of human breast cancer MDA-MB-231 cells by affecting TGF-?1 processing.
Neoplasms
Loss of prolyl hydroxylase-2 in myeloid cells and T-lymphocytes impairs tumor development.
Neoplasms
New cancer targets emerging from studies of the Von Hippel-Lindau tumor suppressor protein.
Neoplasms
Overexpression of the Oxygen Sensors PHD-1, PHD-2, PHD-3, and FIH Is Associated with Tumor Aggressiveness in Pancreatic Endocrine Tumors.
Neoplasms
Paragangliomas/Pheochromocytomas: clinically oriented genetic testing.
Neoplasms
PHD2 mutation and congenital erythrocytosis with paraganglioma.
Neoplasms
Prolyl hydroxylase domain 2 protein is a strong prognostic marker in human gastric cancer.
Neoplasms
Prolyl hydroxylase domain enzymes and their role in cell signaling and cancer metabolism.
Neoplasms
Prolyl hydroxylase domain enzymes: important regulators of cancer metabolism.
Neoplasms
Prolyl hydroxylase-2 inhibits liver tumor cell proliferation and cyclin D1 expression in a hydroxylase-dependent manner.
Neoplasms
Rare germline mutations identified by targeted next-generation sequencing of susceptibility genes in pheochromocytoma and paraganglioma.
Neoplasms
Regulation of HIF by prolyl hydroxylases: recruitment of the candidate tumor suppressor protein ING4.
Neoplasms
Regulation of IL-1?-induced NF-?B by hydroxylases links key hypoxic and inflammatory signaling pathways.
Neoplasms
Targeting MCM2 function as a novel strategy for the treatment of highly malignant breast tumors.
Neoplasms
The non-canonical functions of HIF prolyl hydroxylases and their dual roles in cancer.
Neoplasms
The prolyl-hydroxylase EGLN3 and not EGLN1 is inactivated by methylation in plasma cell neoplasia.
Neoplasms
The role of HIF prolyl hydroxylases in tumor growth.
Neoplasms
The roles and signaling pathways of prolyl-4-hydroxylase 2 in the tumor microenvironment.
Neoplasms
The VHL gene is epigenetically inactivated in pheochromocytomas and abdominal paragangliomas.
Neoplasms
The VHL Tumor Suppressor Gene: Insights into Oxygen Sensing and Cancer.
Neoplasms
Tumor hypoxia does not drive differentiation of tumor-associated macrophages but rather fine-tunes the M2-like macrophage population.
Neoplasms
Tumor suppressor SPOP ubiquitinates and degrades EglN2 to compromise growth of prostate cancer cells.
Neuroblastoma
An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is induced by hypoxia and acts on hypoxia-inducible factor alpha.
Neurofibromatoses
Pheochromocytomas and Paragangliomas: Clinical and Genetic Approaches.
Non-alcoholic Fatty Liver Disease
Regulatory Role of Endothelial PHD2 in the Hepatic Steatosis.
Obesity
HIF Prolyl 4-Hydroxylase-2 Inhibition Improves Glucose and Lipid Metabolism and Protects Against Obesity and Metabolic Dysfunction.
Obesity
Tetrahydrobiopterin activates brown adipose tissue and regulates systemic energy metabolism.
Ovarian Neoplasms
Genome-Wide Interrogation of Human Cancers Identifies EGLN1 Dependency in Clear Cell Ovarian Cancers.
Pancreatic Neoplasms
Overexpression of hydroxyproline via EGLN/HIF1A is associated with distant metastasis in pancreatic cancer.
Pancreatic Neoplasms
Prolyl hydroxylase domain 3 influences the radiotherapy efficacy of pancreatic cancer cells by targeting hypoxia-inducible factor-1?.
Pancreatic Neoplasms
Prolyl hydroxylase-2 (PHD2) exerts tumor-suppressive activity in pancreatic cancer.
Paraganglioma
Modeling dioxygenase enzyme kinetics in familial paraganglioma.
Paraganglioma, Extra-Adrenal
Distinct deregulation of the hypoxia inducible factor by PHD2 mutants identified in germline DNA of patients with polycythemia.
Paraproteinemias
The prolyl-hydroxylase EGLN3 and not EGLN1 is inactivated by methylation in plasma cell neoplasia.
Parkinson Disease
A protective role for N-acylphosphatidylethanolamine phospholipase D in 6-OHDA-induced neurodegeneration.
Parkinson Disease
Genetic Analysis of EGLN1 C127S Variant in Taiwanese Parkinson's Disease.
Parkinson Disease
Pharmacological Prolyl Hydroxylase Domain Inhibition as a Therapeutic Target for Parkinson's Disease.
Parkinson Disease
Regulation of ATP13A2 via PHD2-HIF1? Signaling Is Critical for Cellular Iron Homeostasis: Implications for Parkinson's Disease.
Peripheral Arterial Disease
Short-term treatment with a novel HIF-prolyl hydroxylase inhibitor (GSK1278863) failed to improve measures of performance in subjects with claudication-limited peripheral artery disease.
Phenylketonurias
A histological study of the hph-1 mouse mutant: an animal model of phenylketonuria and infantile hypertrophic pyloric stenosis.
Phenylketonurias
Anxiety- and depression-like phenotype of hph-1 mice deficient in tetrahydrobiopterin.
Phenylketonurias
Congenic mapping and genotyping of the tetrahydrobiopterin-deficient hph-1 mouse.
Phenylketonurias
Impairment of the nitric oxide/cyclic GMP pathway in cerebellar slices prepared from the hph-1 mouse.
Phenylketonurias
Molecular characterization of HPH-1: a mouse mutant deficient in GTP cyclohydrolase I activity.
Phenylketonurias
Neurochemical effects following peripheral administration of tetrahydropterin derivatives to the hph-1 mouse.
Phenylketonurias
Pivotal role for endothelial tetrahydrobiopterin in pulmonary hypertension.
Phenylketonurias
Regulation of ?-adrenergic control of heart rate by GTP-cyclohydrolase 1 (GCH1) and tetrahydrobiopterin.
Phenylketonurias
Synthesis and recycling of tetrahydrobiopterin in endothelial function and vascular disease.
Phenylketonurias
Tetrahydrobiopterin (BH4) deficiency is associated with augmented inflammation and microvascular degeneration in the retina.
Phenylketonurias
Tetrahydrobiopterin activates brown adipose tissue and regulates systemic energy metabolism.
Phenylketonurias
Tetrahydrobiopterin and biogenic amine metabolism in the hph-1 mouse.
Phenylketonurias
Tetrahydrobiopterin availability, nitric oxide metabolism and glutathione status in the hph-1 mouse; implications for the pathogenesis and treatment of tetrahydrobiopterin deficiency states.
Phenylketonurias
Tetrahydrobiopterin deficiency and brain nitric oxide synthase in the hph1 mouse.
Pneumonia
Manganese (II) induces chemical hypoxia by inhibiting HIF-prolyl hydroxylase: implication in manganese-induced pulmonary inflammation.
Pneumonia
Manganese (II) induces chemical hypoxia by inhibiting HIF-prolyl hydroxylase: Implication in manganese-induced pulmonary inflammation.
Polycythemia
An Erythrocytosis-Associated Mutation in the Zinc Finger of PHD2 Provides Insights into Its Binding of p23.
Polycythemia
Congenital erythrocytosis - discover of a new mutation in the EGLN1 gene.
Polycythemia
Distinct deregulation of the hypoxia inducible factor by PHD2 mutants identified in germline DNA of patients with polycythemia.
Polycythemia
EPAS1 p.M535T mutation in a Bulgarian family with congenital erythrocytosis.
Polycythemia
Erythrocytosis: genes and pathways involved in disease development.
Polycythemia
Genotype-Phenotype Correlation of Hereditary Erythrocytosis Mutations, a single center experience.
Polycythemia
Hereditary gene mutations in Korean patients with isolated erythrocytosis.
Polycythemia
Hypoxia Pathway Mutations in Pheochromocytomas and Paragangliomas.
Polycythemia
Identification of Variants Associated With Rare Hematological Disorder Erythrocytosis Using Targeted Next-Generation Sequencing Analysis.
Polycythemia
Isolated Erythrocytosis Associated With 3 Novel Missense Mutations in the EGLN1 Gene.
Polycythemia
Loss-of-function zinc finger mutation in the EGLN1 gene associated with erythrocytosis.
Polycythemia
Molecular study of congenital erythrocytosis in 70 unrelated patients revealed a potential causal mutation in less than half of the cases (Where is/are the missing gene(s)?).
Polycythemia
Notch Downregulation and Extramedullary Erythrocytosis in Hypoxia-Inducible Factor Prolyl 4-Hydroxylase 2-Deficient Mice.
Polycythemia
PHD2 mutation and congenital erythrocytosis with paraganglioma.
Polycythemia
Prolyl-4-Hydroxylase 2 Potentially Contributes to Hepatocellular Carcinoma-Associated Erythrocytosis by Maintaining Hepatocyte Nuclear Factor-4? Expression.
Polycythemia
The VHL Tumor Suppressor Gene: Insights into Oxygen Sensing and Cancer.
Polycythemia
The Zinc Finger of Prolyl Hydroxylase Domain Protein 2 Is Essential for Efficient Hydroxylation of Hypoxia-Inducible Factor ?.
Polycythemia
[A new case of rare erythrocytosis due to EGLN1 mutation with review of the literature].
Pre-Eclampsia
High altitude and pre-eclampsia: Adaptation or protection.
Pre-Eclampsia
Novel association of SNP rs479200 in EGLN1 gene with predisposition to preeclampsia.
Prostatic Neoplasms
Association of EGLN2 rs10680577 Polymorphism with the Risk and Clinicopathological Features of Patients with Prostate Cancer.
Prostatic Neoplasms
Tumor suppressor SPOP ubiquitinates and degrades EglN2 to compromise growth of prostate cancer cells.
Pulmonary Arterial Hypertension
[Correlation between EGLN1 gene, protein express in lung tissue of rats and pulmonary artery pressure at different altitude].
Pulmonary Disease, Chronic Obstructive
EGLN2 and RNF150 genetic variants are associated with chronic obstructive pulmonary disease risk in the Chinese population.
Pulmonary Disease, Chronic Obstructive
Refining susceptibility loci of chronic obstructive pulmonary disease with lung eqtls.
Pulmonary Disease, Chronic Obstructive
Smoking dysregulates the human airway basal cell transcriptome at COPD risk locus 19q13.2.
Pulmonary Disease, Chronic Obstructive
Variants in two adjacent genes, EGLN2 and CYP2A6, influence smoking behavior related to disease risk via different mechanisms.
Pulmonary Edema
EGLN1 involvement in high-altitude adaptation revealed through genetic analysis of extreme constitution types defined in Ayurveda.
Pulmonary Edema
Raised HIF1? during normoxia in high altitude pulmonary edema susceptible non-mountaineers.
Pyloric Stenosis, Hypertrophic
A histological study of the hph-1 mouse mutant: an animal model of phenylketonuria and infantile hypertrophic pyloric stenosis.
Pyloric Stenosis, Hypertrophic
Infantile hypertrophic pyloric stenosis (IHPS): a study of its pathophysiology utilizing the newborn hph-1 mouse model of the disease.
Renal Insufficiency
HIF prolyl hydroxylase inhibitors for anemia.
Renal Insufficiency, Chronic
HIF hydroxylase inhibitors decrease cellular oxygen consumption depending on their selectivity.
Renal Insufficiency, Chronic
Hypoxia-inducible factor prolyl hydroxylase inhibitors: a paradigm shift for treatment of anemia in chronic kidney disease?
Renal Insufficiency, Chronic
Inhibition of prolyl hydroxylase domain (PHD) by JTZ-951 reduces obesity-related diseases in the liver, white adipose tissue, and kidney in mice with a high-fat diet.
Renal Insufficiency, Chronic
Prolyl hydroxylase domain inhibitors as a novel therapeutic approach against anemia in chronic kidney disease.
Renal Insufficiency, Chronic
Therapeutic targeting of the HIF oxygen-sensing pathway: Lessons learned from clinical studies.
Renal Insufficiency, Chronic
[Future perspectives of treatment for anemia in chronic kidney disease (CKD) using hypoxia-inducible factor prolyl hydroxylase inhibitors].
Reperfusion Injury
HIF hydroxylase inhibitors decrease cellular oxygen consumption depending on their selectivity.
Sarcoma
Induction of human endometrial cancer cell senescence through modulation of HIF-1alpha activity by EGLN1.
Spinal Cord Injuries
Hypoxia-inducible factor prolyl hydroxylase domain (PHD) inhibition after contusive spinal cord injury does not improve locomotor recovery.
Stomach Neoplasms
An Insertion/Deletion Polymorphism Within the Proximal Promoter of EGLN2 Is Associated With Susceptibility for Gastric Cancer in the Chinese Population.
Stomach Neoplasms
Overexpression of the HIF hydroxylase PHD3 is a favorable prognosticator for gastric cancer.
Stomach Neoplasms
Prolyl hydroxylase domain 2 protein is a strong prognostic marker in human gastric cancer.
Stroke
HIF prolyl hydroxylase inhibitors for anemia.
Stroke
Hypoxia-inducible factor prolyl 4-hydroxylase inhibition. A target for neuroprotection in the central nervous system.
Thrombosis
Hypoxia and Upregulation of Hypoxia-Inducible Factor 1{alpha} Stimulate Venous Thrombus Recanalization.
Thrombosis
Inhibition of prolyl hydroxylase domain proteins selectively enhances venous thrombus neovascularisation.
Triple Negative Breast Neoplasms
EglN2 contributes to triple negative breast tumorigenesis by functioning as a substrate for the FBW7 tumor suppressor.
Triple Negative Breast Neoplasms
Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer.
Uterine Neoplasms
Induction of human endometrial cancer cell senescence through modulation of HIF-1alpha activity by EGLN1.
Vascular System Injuries
Tetrahydrobiopterin deficiency exaggerates intimal hyperplasia after vascular injury.
Ventricular Dysfunction
Chronic Inhibition of Hypoxia-Inducible Factor (HIF) Prolyl 4-Hydroxylase Improves Ventricular Performance, Remodeling and Vascularity Following Myocardial Infarction in the Rat.
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0.0026
(2R)-[2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetamido](phenyl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0028
(2S)-[2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetamido](phenyl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0295 - 0.0397
1,1',1'',1'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetrapropan-2-ol
0.0309
2,2',2'',2'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetraacetamide
Homo sapiens
-
recombinant enzyme, pH 7.0, 37°C
0.005
2,3-dihydroxypyridine
Homo sapiens
-
pH 7.0, 37°C
0.0004
2-(2-(5-cyano-3-hydroxy-4-methylpyridin-2-yl)-5-methylthiazol-4-yl)-N-(2-(diethylamino)ethyl)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0057
2-(2-(5-cyano-3-hydroxy-4-methylpyridin-2-yl)-5-phenylthiazol-4-yl)-N-(2-(pyridin-2-yl)ethyl)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.024
2-(2-(5-cyano-3-hydroxypyridin-2-yl)-5-phenylthiazol-4-yl)-N-(2-(pyridin-2-yl)ethyl)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.003
2-hydroxypyridine 1-oxide
Homo sapiens
-
pH 7.0, 37°C
0.0038
2-[2-(5-cyano-3-hydroxy-4-methylpyridin-2-yl)-1,3-thiazol-4-yl]-N-[2-(diethylamino)ethyl]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0007
2-[2-(5-cyano-3-hydroxy-4-methylpyridin-2-yl)-1,3-thiazol-4-yl]-N-[2-(pyridin-2-yl)ethyl]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
2-[2-(5-cyano-3-hydroxy-4-methylpyridin-2-yl)-5-methyl-1,3-thiazol-4-yl]-N-propylacetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
2-[2-(5-cyano-3-hydroxy-4-methylpyridin-2-yl)-5-methyl-1,3-thiazol-4-yl]-N-[2-(pyridin-2-yl)ethyl]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0034
2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]-N-(2-phenylethyl)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0021
2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]-N-[(1R)-2-hydroxy-1-phenylethyl]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0024
2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]-N-[(1S)-2-hydroxy-1-phenylethyl]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.003
2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]-N-[2-(pyridin-2-yl)ethyl]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
2-[2-(5-cyano-3-hydroxypyridin-2-yl)-5-methyl-1,3-thiazol-4-yl]-N-[2-(pyridin-2-yl)ethyl]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0073
2-[2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetamido]-2-methylpropanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0604
3,3'-[(pyridin-2-ylmethyl)imino]dipropanenitrile
Homo sapiens
-
recombinant enzyme, pH 7.0, 37°C
0.0128
3,3'-[(pyridin-4-ylimino)bis(propane-3,1-diyliminomethanediyl)]diphenol
Homo sapiens
-
recombinant enzyme, pH 7.0, 37°C
0.016
3,3'-[(pyridin-4-ylimino)bis[propane-3,1-diylnitrilo(Z)methylylidene]]diphenol
Homo sapiens
-
recombinant enzyme, pH 7.0, 37°C
0.0103
3,6,9-tris(naphthalen-1-ylmethyl)-3,6,9,15-tetraazabicyclo[9.3.1]pentadeca-1(15),11,13-triene
Homo sapiens
-
recombinant enzyme, pH 7.0, 37°C
0.000253
3-([1,1'-biphenyl]-4-yl)-8-[(3-methylpyridin-2-yl)methyl]-1-(pyrimidin-2-yl)-1,3,8-triazaspiro[4.5]decane-2,4-dione
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
1
3-cyano-6-methyl-2(H)-pyridinone
Homo sapiens
-
above, pH 7.0, 37°C
0.04
3-hydroxy-1,2-dimethyl-4(1H)-pyridinone
Homo sapiens
-
pH 7.0, 37°C
1
3-hydroxy-2-methyl-4-pyrone
Homo sapiens
-
above, pH 7.0, 37°C
0.00224
3-[(1,3-benzoxazol-2-yl)carbamoyl]propanoic acid
Homo sapiens
pH 7.8, temperature not specified in the publication
-
0.00132
3-[(5-chloro-1,3-benzoxazol-2-yl)carbamoyl]propanoic acid
Homo sapiens
pH 7.8, temperature not specified in the publication
-
0.000153
4-hydroxy-2-(1H-pyrazol-1-yl)-N-[[4-(trifluoromethyl)phenyl]methyl]pyrimidine-5-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.000093
4-hydroxy-N-[(1R)-2-hydroxy-1-phenylethyl]-2-(1H-pyrazol-1-yl)pyrimidine-5-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.000256
4-hydroxy-N-[(4-phenoxyphenyl)methyl]-2-(1H-pyrazol-1-yl)pyrimidine-5-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.004
4-methylcatechol
Homo sapiens
-
pH 7.0, 37°C
0.006
4-nitrocatechol
Homo sapiens
-
pH 7.0, 37°C
0.03
4-tert-butylcatechol
Homo sapiens
-
pH 7.0, 37°C
0.4
5-hydroxy-2-hydroxymethyl-4-pyrone
Homo sapiens
-
pH 7.0, 37°C
0.03
5-hydroxy-4-oxo-4H-pyran-2-carboxylic acid
Homo sapiens
-
pH 7.0, 37°C
0.002
5-hydroxy-6-[4-[2-oxo-2-(pyrrolidin-1-yl)ethyl]-1,3-thiazol-2-yl]pyridine-3-carbonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.0000048
6-[5-oxo-4-(1H-1,2,3-triazol-1-yl)-2,5-dihydro-1H-pyrazol-1-yl]pyridine-3-carboxylic acid
Homo sapiens
isoform PHD2, pH and temperature not specified in the publication
0.0244 - 0.1425
CO releasing molecule-2
-
0.0039
FG-2216
Homo sapiens
-
pH and temperature not specified in the publication
0.00221
FG-4592
Homo sapiens
pH 7.8, temperature not specified in the publication
0.0207
N,N-dimethyl-5-[3,6,9,15-tetraazabicyclo[9.3.1]pentadeca-1(15),11,13-trien-6-ylsulfonyl]naphthalen-1-amine
Homo sapiens
-
recombinant enzyme, pH 7.0, 37°C
0.000013
N-(1-[[6-(4-chlorophenoxy)pyridin-3-yl]methyl]-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridine-3-carbonyl)glycine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.000049
N-(4-hydroxy-1-[[4-(4-methylphenoxy)phenyl]methyl]-2-oxo-1,2,5,6-tetrahydropyridine-3-carbonyl)glycine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.000069
N-(4-hydroxy-1-[[5-(4-methylphenoxy)pyridin-2-yl]methyl]-2-oxo-1,2,5,6-tetrahydropyridine-3-carbonyl)glycine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.000039
N-(4-hydroxy-1-[[6-(4-methylphenoxy)pyridin-3-yl]methyl]-2-oxo-1,2,5,6-tetrahydropyridine-3-carbonyl)glycine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.000213
N-([1,1'-biphenyl]-4-yl)-4-hydroxy-2-(1H-pyrazol-1-yl)pyrimidine-5-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.081
N-benzyl-2-[2-(3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0054
N-benzyl-2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000022
N-oxalylglycine
Homo sapiens
isoform PHD2, pH and temperature not specified in the publication
0.000261
N-[(1,3-dihydro-2-benzofuran-5-yl)methyl]-4-hydroxy-2-(1H-pyrazol-1-yl)pyrimidine-5-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.00021
N-[([1,1'-biphenyl]-4-yl)methyl]-4-hydroxy-2-(1H-pyrazol-1-yl)pyrimidine-5-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.0000016
tert-butyl 6-(5-oxo-4-(1H-1,2,3-triazol-1-yl)-2,5-dihydro-1H-pyrazol-1-yl)nicotinate
Homo sapiens
isoform PHD2, pH and temperature not specified in the publication
0.000022
[(1-benzyl-4-hydroxy-2-oxo-1,2-dihydroquinoline-3-carbonyl)amino]acetic acid
Homo sapiens
isoform PHD2, pH and temperature not specified in the publication
0.195
[2-(3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0275
[2-(3-hydroxypyridin-2-yl)-6-oxo-1,6-dihydropyrimidin-5-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.006
[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0135
[2-(5-cyano-3-hydroxypyridin-2-yl)-6-oxo-1,6-dihydropyrimidin-5-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0022
[2-[2-(5-cyano-3-hydroxypyridin-2-yl)-1,3-thiazol-4-yl]acetamido]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0295
1,1',1'',1'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetrapropan-2-ol
Homo sapiens
-
recombinant enzyme, pH 7.0, 37°C
0.0397
1,1',1'',1'''-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrayl)tetrapropan-2-ol
Homo sapiens
-
recombinant enzyme, pH 7.0, 37°C
0.0244
CO releasing molecule-2
Homo sapiens
substrate DLDLEMLAPYIPTIISLDF, pH 7.5, 37°C
-
0.0342
CO releasing molecule-2
Homo sapiens
substrate DALTLLAPAAGDTIISLDF, pH 7.5, 37°C
-
0.0468
CO releasing molecule-2
Homo sapiens
substrate DALTLLAPAAGDTIISLDF, pH 7.5, 37°C
-
0.1425
CO releasing molecule-2
Homo sapiens
substrate DLDLEMLAPYIPMDDDFQL, pH 7.5, 37°C
-
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Hirsila, M.; Koivunen, P.; Gunzler, V.; Kivirikko, K.I.; Myllyharju, J.
Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
J. Biol. Chem.
278
30772-30780
2003
Homo sapiens, Homo sapiens (Q9GZT9), Homo sapiens (Q9H6Z9)
brenda
Ivan, M.; Kondo, K.; Yang, H.F.; Kim, W.; Valiando, J.; Ohh, M.; Salic, A.; Asara, J.M.; Lane, W.S.; Kaelin, W.G.
HIF alpha targeted for VHL-mediated destruction by proline hydroxylation: Implications for O2 sensing
Science
292
464-468
2001
Homo sapiens
brenda
Jaakkola, P.; Mole, D.R.; Tian, Y.M.; Wilson, M.I.; Gielbert, J.; Gaskell, S.J.; von Kriegsheim, A.; Hebestreit, H.F.; Mukherji, M.; Schofield, C.J.; Maxwell, P.H.; Pugh, C.W.; Ratcliffe, P.J.
Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
Science
292
468-472
2001
Homo sapiens
brenda
Bruick, R.K.; McKnight, S.L.
A conserved family of prolyl-4-hydroxylases that modify HIF
Science
294
1337-1340
2001
Drosophila melanogaster, Homo sapiens, Homo sapiens (Q96KS0), Homo sapiens (Q9GZT9)
brenda
Pappalardi, M.B.; McNulty, D.E.; Martin, J.D.; Fisher, K.E.; Jiang, Y.; Burns, M.C.; Zhao, H.; Ho, T.; Sweitzer, S.; Schwartz, B.; Annan, R.S.; Copeland, R.A.; Tummino, P.J.; Luo, L.
Biochemical characterization of human HIF hydroxylases using HIF protein substrates that contain all three hydroxylation sites
Biochem. J.
436
363-369
2011
Homo sapiens (Q96KS0), Homo sapiens (Q9GZT9), Homo sapiens (Q9H6Z9)
brenda
Kwon, H.S.; Choi, Y.K.; Kim, J.W.; Park, Y.K.; Yang, E.G.; Ahn, D.R.
Inhibition of a prolyl hydroxylase domain (PHD) by substrate analog peptides
Bioorg. Med. Chem. Lett.
21
4325-4328
2011
Homo sapiens
brenda
Cavadas, M.A.; Nguyen, L.K.; Cheong, A.
Hypoxia-inducible factor (HIF) network: insights from mathematical models
Cell Commun. Signal.
11
42
2013
Homo sapiens
brenda
Masson, N.; Singleton, R.S.; Sekirnik, R.; Trudgian, D.C.; Ambrose, L.J.; Miranda, M.X.; Tian, Y.M.; Kessler, B.M.; Schofield, C.J.; Ratcliffe, P.J.
The FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity
EMBO Rep.
13
251-257
2012
Homo sapiens
brenda
Nguyen, L.K.; Cavadas, M.A.; Scholz, C.C.; Fitzpatrick, S.F.; Bruning, U.; Cummins, E.P.; Tambuwala, M.M.; Manresa, M.C.; Kholodenko, B.N.; Taylor, C.T.; Cheong, A.
A dynamic model of the hypoxia-inducible factor 1alpha (HIF-1alpha) network
J. Cell Sci.
126
1454-1463
2013
Homo sapiens
brenda
Geng, Z.; Zhu, J.; Cao, J.; Geng, J.; Song, X.; Zhang, Z.; Bian, N.; Wang, Z.
Effects of polynitrogen compounds on the activity of recombinant human HIF-1alpha prolyl hydroxylase 3 in E. coli
J. Inorg. Biochem.
105
391-399
2011
Homo sapiens
brenda
Flagg, S.C.; Martin, C.B.; Taabazuing, C.Y.; Holmes, B.E.; Knapp, M.J.
Screening chelating inhibitors of HIF-prolyl hydroxylase domain 2 (PHD2) and factor inhibiting HIF (FIH)
J. Inorg. Biochem.
113
25-30
2012
Homo sapiens
brenda
Pektas, S.; Knapp, M.J.
Substrate preference of the HIF-prolyl hydroxylase-2 (PHD2) and substrate-induced conformational change
J. Inorg. Biochem.
126
55-60
2013
Homo sapiens
brenda
Cao, J.; Geng, Z.; Ma, X.; Wen, J.; Yin, Y.; Wang, Z.
Evidence for inhibition of HIF-1alpha prolyl hydroxylase 3 activity by four biologically active tetraazamacrocycles
Org. Biomol. Chem.
10
3913-3923
2012
Homo sapiens
brenda
Tarhonskaya, H.; Chowdhury, R.; Leung, I.K.; Loik, N.D.; McCullagh, J.S.; Claridge, T.D.; Schofield, C.J.; Flashman, E.
Investigating the contribution of the active site environment to the slow reaction of hypoxia-inducible factor prolyl hydroxylase domain 2 with oxygen
Biochem. J.
463
363-372
2014
Homo sapiens (Q9GZT9), Homo sapiens
brenda
Pektas, S.; Taabazuing, C.Y.; Knapp, M.J.
Increased turnover at limiting O2 concentrations by the Thr387 -> Ala variant of HIF-prolyl hydroxylase PHD2
Biochemistry
54
2851-2857
2015
Homo sapiens (Q9GZT9), Homo sapiens
brenda
Osipyants, A.; Smirnova, N.; Khristichenko, A.; Hushpulian, D.; Nikulin, S.; Chubar, T.; Zakhariants, A.; Tishkov, V.; Gazaryan, I.; Poloznikov, A.
Enzymesubstrate reporters for evaluation of substrate specificity of HIF prolyl hydroxylase isoforms
Biochemistry
82
1207-1214
2017
Homo sapiens (Q96KS0), Homo sapiens (Q9GZT9), Homo sapiens (Q9H6Z9)
brenda
Fan, L.; Li, J.; Yu, Z.; Dang, X.; Wang, K.
The hypoxia-inducible factor pathway, prolyl hydroxylase domain protein inhibitors, and their roles in bone repair and regeneration
BioMed Res. Int.
2014
239356
2014
Homo sapiens
brenda
Hong, Y.R.; Kim, H.T.; Ro, S.; Cho, J.M.; Lee, S.H.; Kim, I.S.; Jung, Y.H.
Discovery of novel 2-[2-(3-hydroxy-pyridin-2-yl)-thiazol-4-yl]-acetamide derivatives as HIF prolyl 4-hydroxylase inhibitors; SAR, synthesis and modeling evaluation
Bioorg. Med. Chem. Lett.
24
3142-3145
2014
Homo sapiens
brenda
Miikkulainen, P.; Hoegel, H.; Rantanen, K.; Suomi, T.; Kouvonen, P.; Elo, L.L.; Jaakkola, P.M.
HIF prolyl hydroxylase PHD3 regulates translational machinery and glucose metabolism in clear cell renal cell carcinoma
Cancer Metab.
5
5-5
2017
Homo sapiens (Q9H6Z9)
brenda
Bishop, T.; Ratcliffe, P.J.
HIF hydroxylase pathways in cardiovascular physiology and medicine
Circ. Res.
117
65-79
2015
Homo sapiens
brenda
Badawi, Y.; Shi, H.
Relative contribution of prolyl hydroxylase-dependent and -independent degradation of HIF-1alpha by proteasomal pathways in cerebral ischemia
Front. Neurosci.
11
239
2017
Homo sapiens
brenda
Kozlova, N.; Wottawa, M.; Katschinski, D.M.; Kristiansen, G.; Kietzmann, T.
Hypoxia-inducible factor prolyl hydroxylase 2 (PHD2) is a direct regulator of epidermal growth factor receptor (EGFR) signaling in breast cancer
Oncotarget
8
9885-9898
2017
Homo sapiens
brenda
Chan, M.C.; Atasoylu, O.; Hodson, E.; Tumber, A.; Leung, I.K.; Chowdhury, R.; Gomez-Perez, V.; Demetriades, M.; Rydzik, A.M.; Holt-Martyn, J.; Tian, Y.M.; Bishop, T.; Claridge, T.D.; Kawamura, A.; Pugh, C.W.; Ratcliffe, P.J.; Schofield, C.J.
Potent and selective triazole-based inhibitors of the hypoxia-inducible factor prolyl-hydroxylases with activity in the murine brain
PLoS ONE
10
e0132004
2015
Mus musculus (Q91UZ4), Mus musculus (Q91YE2), Mus musculus (Q91YE3), Homo sapiens (Q96KS0), Homo sapiens (Q9GZT9), Homo sapiens (Q9H6Z9)
brenda
Sun, W.; Jelkmann, W.; Depping, R.
Prolyl-4-hydroxylase 2 enhances hypoxia-induced glioblastoma cell death by regulating the gene expression of hypoxia-inducible factor-alpha
Cell Death Dis.
5
e1322
2014
Homo sapiens (Q9GZT9)
brenda
Sun, W.; Kosyna, F.K.; Jelkmann, W.; Depping, R.
Prolyl-4-hydroxylase 2 potentially contributes to hepatocellular carcinoma-associated erythrocytosis by maintaining hepatocyte nuclear factor-4alpha expression
Cell. Physiol. Biochem.
37
2257-2264
2015
Homo sapiens (Q9GZT9), Homo sapiens
brenda
Li, J.; Yuan, W.; Jiang, S.; Ye, W.; Yang, H.; Shapiro, I.M.; Risbud, M.V.
Prolyl-4-hydroxylase domain protein 2 controls NF-kappaB/p65 transactivation and enhances the catabolic effects of inflammatory cytokines on cells of the nucleus pulposus
J. Biol. Chem.
290
7195-7207
2015
Rattus norvegicus (P59722), Homo sapiens (Q9GZT9)
brenda
Osipyants, A.I.; Poloznikov, A.A.; Smirnova, N.A.; Hushpulian, D.M.; Khristichenko, A.Y.; Chubar, T.A.; Zakhariants, A.A.; Ahuja, M.; Gaisina, I.N.; Thomas, B.; Brown, A.M.; Gazaryan, I.G.; Tishkov, V.I.
L-ascorbic acid A true substrate for HIF prolyl hydroxylase?
Biochimie
147
46-54
2018
Homo sapiens (Q9GZT9)
brenda
Hamada, M.; Takayama, T.; Shibata, T.; Hiratate, A.; Takahashi, M.; Yashiro, M.; Takayama, N.; Okumura-Kitajima, L.; Koretsune, H.; Kajiyama, H.; Naruse, T.; Kato, S.; Takano, H.; Kakinuma, H.
Discovery of novel 2-[(4-hydroxy-6-oxo-2,3-dihydro-1H-pyridine-5-carbonyl)amino]acetic acid derivatives as HIF prolyl hydroxylase inhibitors for treatment of renal anemia
Bioorg. Med. Chem. Lett.
28
1725-1730
2018
Homo sapiens (Q9GZT9)
brenda
Mbenza, N.M.; Nasarudin, N.; Vadakkedath, P.G.; Patel, K.; Ismail, A.Z.; Hanif, M.; Wright, L.J.; Sarojini, V.; Hartinger, C.G.; Leung, I.K.H.
Carbon monoxide is an inhibitor of HIF prolyl hydroxylase domain 2
ChemBioChem
22
2521-2525
2021
Homo sapiens (Q9GZT9)
brenda
Holt-Martyn, J.P.; Chowdhury, R.; Tumber, A.; Yeh, T.L.; Abboud, M.I.; Lippl, K.; Lohans, C.T.; Langley, G.W.; Figg, W.; McDonough, M.A.; Pugh, C.W.; Ratcliffe, P.J.; Schofield, C.J.
Structure-activity relationship and crystallographic studies on 4-hydroxypyrimidine HIF prolyl hydroxylase domain inhibitors
ChemMedChem
15
270-273
2020
Homo sapiens (Q9GZT9)
brenda
Poloznikov, A.A.; Nikulin, S.V.; Zakhariants, A.A.; Khristichenko, A.Y.; Hushpulian, D.M.; Gazizov, I.N.; Tishkov, V.I.; Gazaryan, I.G.
''Branched Tail'' oxyquinoline inhibitors of HIF prolyl hydroxylase early evaluation of toxicity and metabolism using liver-on-a-chip
Drug Metab. Lett.
13
45-52
2019
Homo sapiens
brenda
Cockman, M.E.; Lippl, K.; Tian, Y.M.; Pegg, H.B.; Figg, W.D.; Abboud, M.I.; Heilig, R.; Fischer, R.; Myllyharju, J.; Schofield, C.J.; Ratcliffe, P.J.
Lack of activity of recombinant HIF prolyl hydroxylases (PHDs) on reported non-HIF substrates
eLife
8
e46490
2019
Homo sapiens (Q96KS0), Homo sapiens (Q9GZT9), Homo sapiens (Q9H6Z9), Homo sapiens
brenda
Myllykoski, M.; Sutinen, A.; Koski, M.; Kallio, J.; Raasakka, A.; Myllyharju, J.; Wierenga, R.; Koivunen, P.
Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains
J. Biol. Chem.
296
100197
2021
Homo sapiens (Q9NXG6), Homo sapiens
brenda
Chong, M.; Toh, L.; Tumber, A.; Chan, Y.; Chan, M.; Abboud, M.; Schofield, C.; Yeoh, K.
Evaluation of 3-carbamoylpropanoic acid analogs as inhibitors of human hypoxia-inducible factor (HIF) prolyl hydroxylase domain enzymes
Med. Chem. Res.
30
977-986
2021
Homo sapiens (Q9GZT9)
-
brenda
Pickel, C.; Taylor, C.; Scholz, C.
Genetic knockdown and pharmacologic inhibition of hypoxia-inducible factor (HIF) hydroxylases
Methods Mol. Biol.
1742
1-14
2018
Homo sapiens
brenda
Koivunen, P.; Myllyharju, J.
Kinetic analysis of HIF prolyl hydroxylases
Methods Mol. Biol.
1742
15-25
2018
Homo sapiens (Q9GZT9)
brenda