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

Egl nine homolog 2

PHD1, HIF prolyl hydroxylase, EGLN2
The hypoxia inducible factor (HIF) is a transcriptional complex that is involved in oxygen homeostasis. At normal oxygen levels, the alpha subunit of HIF is targeted for degration by prolyl hydroxylation. This gene encodes an enzyme responsible for this post-translational modification. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the upstream RAB4B (RAB4B, member RAS oncogene family) gene. [provided by RefSeq, Feb 2011] (from NCBI)
Top mentioned proteins: PHD2, HIF-1alpha, CAN, V1a, VHL
Papers on PHD1
Alternative splicing transcription of Megalobrama amblycephala HIF prolyl hydroxylase PHD3 and up-regulation of PHD3 by HIF-1α.
New
Wang et al., Wuhan, China. In Biochem Biophys Res Commun, Feb 2016
PHD3 is a hydroxylase that hydroxylates prolyl residues on hypoxia-inducible factors (HIFs) in mammals.
An ID2-dependent mechanism for VHL inactivation in cancer.
New
Impact
Lasorella et al., New York City, United States. In Nature, Feb 2016
The activity of these kinases is stimulated in normoxia by the oxygen-sensing prolyl hydroxylase PHD1 (also known as EGLN2).
Deletion or Inhibition of the Oxygen Sensor PHD1 Protects against Ischemic Stroke via Reprogramming of Neuronal Metabolism.
New
Impact
Carmeliet et al., Leuven, Belgium. In Cell Metab, Feb 2016
Here we report that PHD1 deficiency provides neuroprotection in a murine model of permanent brain ischemia.
CDK-dependent phosphorylation of PHD1 on serine 130 alters its substrate preference in cells.
New
Rocha et al., Dundee, United Kingdom. In J Cell Sci, Feb 2016
PHD1 (also known as EGLN2) belongs to a family of prolyl hydroxylases (PHDs) that are involved in the control of the cellular response to hypoxia.
HIF prolyl hydroxylase inhibitors for the treatment of renal anaemia and beyond.
Review
New
Eckardt et al., Erlangen, Germany. In Nat Rev Nephrol, Jan 2016
UNASSIGNED: Small-molecule stabilizers of hypoxia inducible factor (HIF) are being developed for the treatment of renal anaemia.
Characterization of a linked Jumonji domain of the KDM5/JARID1 family of histone H3 lysine 4 demethylases.
New
Cheng et al., United States. In J Biol Chem, Jan 2016
Here we demonstrate that internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes.
EglN2 associates with the NRF1-PGC1α complex and controls mitochondrial function in breast cancer.
New
Zhang et al., Chapel Hill, United States. In Embo J, Jan 2016
The EglN2/PHD1 prolyl hydroxylase is an important oxygen sensor contributing to breast tumorigenesis.
2-Oxoglutarate-dependent dioxygenases are sensors of energy metabolism, oxygen availability, and iron homeostasis: potential role in the regulation of aging process.
Review
New
Kaarniranta et al., Kuopio, Finland. In Cell Mol Life Sci, Oct 2015
The functions of hypoxia-inducible factor (HIF) prolyl hydroxylases (PHD1-3) as well as those of collagen hydroxylases are associated with age-related degeneration.
Dominant Mutations in the Autoimmune Regulator AIRE Are Associated with Common Organ-Specific Autoimmune Diseases.
New
Impact
Husebye et al., Bergen, Norway. In Immunity, Jul 2015
We have identified multiple cases and families with mono-allelic mutations in the first plant homeodomain (PHD1) zinc finger of AIRE that followed dominant inheritance, typically characterized by later onset, milder phenotypes, and reduced penetrance compared to classical APS-1.
Nuclear-cytoplasmatic shuttling of proteins in control of cellular oxygen sensing.
Review
New
Kosyna et al., Lübeck, Germany. In J Mol Med (berl), Jun 2015
In the presence of O2, the α subunits are hydroxylated by specific prolyl-4-hydroxylase domain proteins (PHD1, PHD2, and PHD3) and an asparaginyl hydroxylase (factor inhibiting HIF-1, FIH-1).
The role of hypoxia and Morg1 in renal injury.
Review
New
Wolf et al., Jena, Germany. In Eur J Clin Invest, Mar 2015
Under normoxic conditions constitutively expressed HIF-α subunits are hydroxylated by prolyl hydroxylases (PHD1, PHD2, and PHD3) and subsequently degraded by proteasomes.
Involvement of Prolyl Hydroxylase Domain Protein in the Rosiglitazone-Induced Suppression of Osteoblast Differentiation.
Cheon et al., Inch'ŏn, South Korea. In Plos One, 2014
Rosiglitazone inhibited osteoblast differentiation in a concentration-dependent manner, and in parallel induced three PHD isoforms (PHD1, 2, and 3).
Inhibition of hypoxia-inducible factor prolyl hydroxylase domain oxygen sensors: tricking the body into mounting orchestrated survival and repair responses.
Review
Rabinowitz, San Diego, United States. In J Med Chem, 2014
The HIF prolyl hydroxylase domain (PHD) enzymes are non-heme, iron-containing dioxygenases requiring for activity both molecular oxygen and 2-oxoglutarate that, under normoxia, selectively hydroxylate proline residues of HIF, initiating proteosomal degradation of the latter.
Low-level laser therapy alleviates neuropathic pain and promotes function recovery in rats with chronic constriction injury: possible involvements in hypoxia-inducible factor 1α (HIF-1α).
GeneRIF
Hong et al., Taiwan. In J Comp Neurol, 2012
In conclusion, a low-level laser could modulate HIF-1alpha activity in nerve entrapment neuropathy
Molecular oxygen sensing: implications for visceral surgery.
Review
GeneRIF
Schneider et al., Heidelberg, Germany. In Langenbecks Arch Surg, 2012
Here, we outline specific functions of PHD enzymes in surgically relevant pathological conditions, and discuss how these functions might be exploited in order to support the treatment of surgically relevant diseases.
Transformation by the (R)-enantiomer of 2-hydroxyglutarate linked to EGLN activation.
Impact
GeneRIF
Kaelin et al., Oulu, Finland. In Nature, 2012
(R)-2HG, but not (S)-2HG, stimulates EGLN activity, leading to diminished HIF levels, which enhances the proliferation and soft agar growth of human astrocytes
Cdk8 regulates stability of the transcription factor Phd1 to control pseudohyphal differentiation of Saccharomyces cerevisiae.
GeneRIF
Sadowski et al., Vancouver, Canada. In Mol Cell Biol, 2012
It was shown that Phd1 is an unstable protein whose degradation is initiated through phosphorylation by Cdk8 of the RNA polymerase II mediator subcomplex.
The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity.
Impact
Sharp et al., Nottingham, United Kingdom. In Nat Cell Biol, 2012
There are three prolyl hydroxylases (PHD1, 2 and 3) that regulate the hypoxia-inducible factors (HIFs), the master transcriptional regulators that respond to changes in intracellular O(2) tension.
PHD1 interacts with ATF4 and negatively regulates its transcriptional activity without prolyl hydroxylation.
GeneRIF
Yasumoto et al., Sendai, Japan. In Exp Cell Res, 2012
Coexistence of PHD1 stabilized ATF4, as opposed to the destabilization of ATF4 by PHD3.
Activation of the HIF prolyl hydroxylase by the iron chaperones PCBP1 and PCBP2.
Impact
Philpott et al., Bethesda, United States. In Cell Metab, 2011
Mammalian cells express dozens of iron-containing proteins, yet little is known about the mechanism of metal ligand incorporation.
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