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oxygen via Phd2 has a decisive influence on the formation of the vascular network during vertebrate embryogenesis.
comparative analysis of phd1 (Montrer EGLN2 Protéines), 2, and 3 expression in Xenopus laevis
brain tissue protection and increased angiogenesis upon sub-acute ischemic stroke was completely absent in Phd2 knockout mice that were additionally deficient for both Hif1a (Montrer HIF1A Protéines) and Hif2a (Montrer EPAS1 Protéines)
expression of PHD2 in endothelial cells plays a critical role in preventing pulmonary arterial remodeling in mice
PHD-2 knockdown mesenchymal stromal cells overexpressed HIF-1alpha (Montrer HIF1A Protéines) and multiple angiogenic factors compared to control. Wounds treated with PHD-2 knockdown mesenchymal stromal cells healed at a significantly accelerated rate compared with wounds treated with shScramble mesenchymal stromal cells.
data identify the PHD2:HIF-2alpha:EPO axis as a so far unknown regulator of osteohematology by controlling bone homeostasis.
miR-21 contributes to the protection of delayed ischemic preconditioning against renal ischemia reperfusion injury in mice, which is at least in part mediated by targeting of PHD2 and subsequently up-regulating HIF-1alpha/VEGF pathway.
Phd2 is the dominant HIF-hydroxylase in neutrophils under normoxic conditions; intrinsic regulation of glycolysis and glycogen (Montrer GYS1 Protéines) stores is linked to the resolution of neutrophil-mediated inflammatory responses
Epo (Montrer EPO Protéines) transcription in brain pericytes was HIF-2 dependent and cocontrolled by PHD2 and PHD3 (Montrer EGLN3 Protéines), oxygen- and 2-oxoglutarate-dependent prolyl-4-hydroxylases that regulate HIF activity.
Notch ligand (Montrer JAG2 Protéines) genes Jag1 (Montrer JAG1 Protéines), Jag2 (Montrer JAG2 Protéines), and Dll1 (Montrer DLL1 Protéines) and target Hes1 became downregulated upon aging HIF-2alpha (Montrer EPAS1 Protéines) dependently.
Results identified a critical role of PHD2 for a reversible glycolytic reprogramming in macrophages with a direct impact on their function.
Results found that loss of endothelial PHD2 induced pulmonary arterial hypertension and vascular remodeling in a HIF-2-dependent fashion.
PHD2 is a direct binding partner of EGFR (Montrer EGFR Protéines) and show that PHD2 regulates EGFR (Montrer EGFR Protéines) stability as well as its subsequent signaling in breast carcinoma cells.
A mechanism of PHD2 regulation that involves the mTOR (Montrer FRAP1 Protéines) and PP2A (Montrer PPP2R4 Protéines) pathways.
These data unravel B55alpha (Montrer PPP2R2A Protéines) as a PHD2 substrate and highlight a role for PHD2-B55alpha (Montrer PPP2R2A Protéines) in the response to nutrient deprivation.
Genetic variants in HIF-1alpha (Montrer HIF1A Protéines) and PHD2 genes exist in Caucasians but do not appear to alter 30-day mortality in sepsis
The role of PHD-2 in breast cancer [review]
Sulfur mustard negatively affects hypoxia-stimulated HIF-1alpha (Montrer HIF1A Protéines) signaling in keratinocytes and fibroblasts and thus possibly contributes to delayed wound healing in SM-injured patients, which could be treated with PHD-2 inhibitors.
The HIFalpha subunit is usually prolyl-hydroxylated by EglN family members under normoxic conditions, causing its rapid degradation. Study confirmed that triple-negative breast cancer cells secrete glutamate (Montrer GRIN1 Protéines), which is both necessary and sufficient for the paracrine induction of HIF1alpha (Montrer HIF1A Protéines) in such cells under normoxic conditions.
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).
egl nine homolog 1 (C. elegans)
, egl nine homolog 1
, egl nine homolog 1-like
, egl nine homolog 2
, HIF-prolyl hydroxylase 2
, hypoxia-inducible factor prolyl hydroxylase 2
, prolyl hydroxylase domain-containing protein 2
, HIF prolyl hydroxylase 2
, egl nine-like protein 1
, zinc finger MYND domain-containing protein 6