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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Association of chromosome 19 to lung cancer genotypes and phenotypes.
Marko-Varga et al., Shanghai, China. In Cancer Metastasis Rev, Jun 2015
Gene aberrations include translocation t(15, 19) (q13, p13.1) fusion oncogene BRD4-NUT, DNA repair genes (ERCC1, ERCC2, XRCC1), TGFβ1 pathway activation genes (TGFB1, LTBP4), Dyrk1B, and potential oncogenesis protector genes such as NFkB pathway inhibition genes (NFKBIB, PPP1R13L) and EGLN2.
Nuclear-cytoplasmatic shuttling of proteins in control of cellular oxygen sensing.
Kosyna et al., Lübeck, Germany. In J Mol Med (berl), Jun 2015
In the presence of O2, the α subunits are hydroxylated by specific prolyl-4-hydroxylase domain proteins (PHD1, PHD2, and PHD3) and an asparaginyl hydroxylase (factor inhibiting HIF-1, FIH-1).
The role of hypoxia and Morg1 in renal injury.
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).
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).
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.
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.
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.
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.
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.
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.
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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