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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 1

The protein encoded by this gene catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. HIF is a transcriptional complex that plays a central role in mammalian oxygen homeostasis. This protein functions as a cellular oxygen sensor, and under normal oxygen concentration, modification by prolyl hydroxylation is a key regulatory event that targets HIF subunits for proteasomal destruction via the von Hippel-Lindau ubiquitylation complex. Mutations in this gene are associated with erythrocytosis familial type 3 (ECYT3). [provided by RefSeq, Nov 2009] (from NCBI)
Top mentioned proteins: HIF-1alpha, PHD1, CAN, V1a, VHL
Papers using PHD2 antibodies
Resolution of glycoproteins by a lectin gel-shift assay.
Bielinsky Anja-Katrin, In PLoS ONE, 1999
... Polyclonal antibodies against OS-9 (NB100-520) and PHD2 (NB100-137) were from Novus Biologicals (Littleton, USA) ...
Papers on PHD2
HMOX2 Functions as a Modifier Gene for High-Altitude Adaptation in Tibetans.
Su et al., Kunming, China. In Hum Mutat, Feb 2016
Previously, EPAS1 and EGLN1, the major upstream regulators in the hypoxic pathway, were reportedly involved in the hemoglobin regulation in Tibetans.
Class I and IIa HDACs Mediate HIF-1α Stability through PHD2-Dependent Mechanism while HDAC6, a Class IIb Member, Promotes HIF-1α Transcriptional Activity in Nucleus Pulposus Cells of the Intervertebral Disc.
Risbud et al., Philadelphia, United States. In J Bone Miner Res, Feb 2016
TSA-mediated HIF-1α degradation was rescued by concomitant inhibition of not only the 26S proteasome but also PHD2 function.
Roles of renal erythropoietin-producing (REP) cells in the maintenance of systemic oxygen homeostasis.
Yamamoto et al., Sendai, Japan. In Pflugers Arch, Jan 2016
In fact, the loss of Epo production in REP cells causes chronic severe anemia in genetically modified mice, and REP cell-specific inactivation of PHD2 (prolyl-hydroxylase domain enzyme 2) results in erythrocytosis via overexpression of the Epo gene due to the constitutive activation of HIF2α (hypoxia-inducible transcription factor 2α). REP cells are located in the interstitial spaces between renal tubules and capillaries, where the oxygen supply is low but oxygen consumption is high, for the highly sensitive detection of decreased oxygen supplies to the body.
Oxidative Dimerization of PHD2 is Responsible for its Inactivation and Contributes to Metabolic Reprogramming via HIF-1α Activation.
Lim et al., Ch'ŏngju, South Korea. In Sci Rep, Dec 2015
Prolyl hydroxylase domain protein 2 (PHD2) belongs to an evolutionarily conserved superfamily of 2-oxoglutarate and Fe(II)-dependent dioxygenases that mediates homeostatic responses to oxygen deprivation by mediating hypoxia-inducible factor-1α (HIF-1α) hydroxylation and degradation.
Computational analysis of prolyl hydroxylase domain-containing protein 2 (PHD2) mutations promoting polycythemia insurgence in humans.
Tosatto et al., Padova, Italy. In Sci Rep, Dec 2015
Idiopathic erythrocytosis is a rare disease characterized by an increase in red blood cell mass due to mutations in proteins of the oxygen-sensing pathway, such as prolyl hydroxylase 2 (PHD2).
Adaptive genetic changes related to haemoglobin concentration in native high-altitude Tibetans.
Jorde et al., San Diego, United States. In Exp Physiol, Dec 2015
Many highland Tibetans exhibit a haemoglobin concentration within the range expected at sea level, and this trait is associated with putatively adaptive regions harbouring the hypoxia-inducible factor pathway genes EGLN1, EPAS1 and PPARA.
[Expression of plateau adaptation gene of rat tissues after plain acute exposure to high altitude].
Rong et al., Lanzhou, China. In Zhejiang Da Xue Xue Bao Yi Xue Ban, Jun 2015
OBJECTIVE: To detect the expression of the plateau adaptablity gene(EPAS1, EGLN1 and PPARα) and proteins(HIF-2, PHD2 and PPARα) in rats blood, heart, liver, lung and kidney tissue after the rats exposed to high altitude.
A lactate-induced response to hypoxia.
Yeom et al., Taejŏn, South Korea. In Cell, May 2015
We find that the NDRG3 protein is degraded in a PHD2/VHL-dependent manner in normoxia but is protected from destruction by binding to lactate that accumulates under hypoxia.
[Hereditary pheochromocytoma-associated syndromes. Part 1].
Beltsevich et al., In Ter Arkh, 2014
New EGLN1/PHD2, KIF1B, SDH5/SDHAF2, IDH1, TMEM127, SDHA, MAX, and HIF2A gene mutations have been recently discovered.
Pheochromocytomas and Paragangliomas: Clinical and Genetic Approaches.
Vaisman et al., Rio de Janeiro, Brazil. In Front Endocrinol (lausanne), 2014
The description of new genes linked to familial forms of PCC/PGLs, such as succinate dehydrogenase (SDH) complex subunits, KIF1Bβ, EGLN1, TMEM127, and MAX, added to the well-known PCC familial syndrome (MEN2, VHL, and neurofibromatosis type 1) presents new challenges for diagnosis.
Recent Advances in Developing Inhibitors for Hypoxia-Inducible Factor Prolyl Hydroxylases and Their Therapeutic Implications.
Yang et al., Seoul, South Korea. In Molecules, 2014
In this review, we first describe the structure of PHD2 as a molecular basis for structure-based drug design (SBDD) and various experimental methods developed for measuring PHD activity.
A genetic mechanism for Tibetan high-altitude adaptation.
Prchal et al., Salt Lake City, United States. In Nat Genet, 2014
We describe a high-frequency missense mutation in the EGLN1 gene, which encodes prolyl hydroxylase 2 (PHD2), that contributes to this adaptive response.
GNAS1 and PHD2 short-interfering RNA support bone regeneration in vitro and in an in vivo sheep model.
Mathur et al., Pittsburgh, United States. In Clin Orthop Relat Res, 2012
PHD2 short interfering RNA supports bone regeneration in vivo.
Inverse solvent isotope effects demonstrate slow aquo release from hypoxia inducible factor-prolyl hydroxylase (PHD2).
Knapp et al., Amherst Center, United States. In Biochemistry, 2012
The unusual kinetic pK(a) further suggested that PHD2 might function physiologically to sense both intracellular pO(2) as well as pH, which could provide for feedback between anaerobic metabolism and hypoxia sensing.
Gene-targeting of Phd2 improves tumor response to chemotherapy and prevents side-toxicity.
Mazzone et al., Leuven, Belgium. In Cancer Cell, 2012
Prolyl hydroxylase domain protein 2 (PHD2) is an oxygen/redox-sensitive enzyme that induces cellular adaptations to stress conditions.
Effect of prolyl hydroxylase domain-2 haplodeficiency on the hepatocarcinogenesis in mice.
Van Vlierberghe et al., Gent, Belgium. In J Hepatol, 2012
This study shows that inhibiting prolyl hydroxylase domain 2 increases the hepatocarcinogenesis and stimulates the development of cholangiocarcinoma.
Low expression of prolyl hydroxylase 2 is associated with tumor grade and poor prognosis in patients with colorectal cancer.
Liang et al., Chongqing, China. In Exp Biol Med (maywood), 2012
present study indicated that low expression of PHD2 in CRC predicts poor survival independent of HIF-1alpha, specifically for patients who have early stage tumors
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.
Macrophage skewing by Phd2 haplodeficiency prevents ischaemia by inducing arteriogenesis.
Mazzone et al., Leuven, Belgium. In Nature, 2011
results unravel how PHD2 regulates arteriogenesis and artery homeostasis by controlling a specific differentiation state in macrophages and suggest new treatment options for ischaemic disorders
Activation of the HIF prolyl hydroxylase by the iron chaperones PCBP1 and PCBP2.
Philpott et al., Bethesda, United States. In Cell Metab, 2011
PHD activity was restored in vitro by addition of excess Fe(II), or purified Fe-PCBP1, and PCBP1 bound to PHD2 and FIH1 in vivo.
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