Title : Hypoxia up-regulates prolyl hydroxylase activity: a feedback mechanism that limits HIF-1 responses during reoxygenation.

Pub. Date : 2003 Oct 3

PMID : 12876291






4 Functional Relationships(s)
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1 Hypoxia reduces activity of prolyl hydroxylases (PHD) that hydroxylate specific proline residues in the oxygen-dependent degradation domain (ODD) of hypoxia-inducible factor-1alpha (HIF-1alpha). Proline egl-9 family hypoxia-inducible factor 1 Rattus norvegicus
2 Hypoxia reduces activity of prolyl hydroxylases (PHD) that hydroxylate specific proline residues in the oxygen-dependent degradation domain (ODD) of hypoxia-inducible factor-1alpha (HIF-1alpha). Oxygen egl-9 family hypoxia-inducible factor 1 Rattus norvegicus
3 We developed assays for PHD activity that used (i) the peptide-specific conversion of labeled 2-oxoglutarate into succinate and (ii) the binding of the von Hippel-Lindau protein to a glutathione S-transferase-ODD fusion protein. Ketoglutaric Acids egl-9 family hypoxia-inducible factor 1 Rattus norvegicus
4 We developed assays for PHD activity that used (i) the peptide-specific conversion of labeled 2-oxoglutarate into succinate and (ii) the binding of the von Hippel-Lindau protein to a glutathione S-transferase-ODD fusion protein. Succinic Acid egl-9 family hypoxia-inducible factor 1 Rattus norvegicus