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

Pub. Date : 2003 Oct 3

PMID : 12876291






5 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 hypoxia inducible factor 1 subunit alpha 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). Proline hypoxia inducible factor 1 subunit alpha Rattus norvegicus
3 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 hypoxia inducible factor 1 subunit alpha Rattus norvegicus
4 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 hypoxia inducible factor 1 subunit alpha Rattus norvegicus
5 We also developed hydroxyproline-specific antibodies that recognized hydroxylated forms of a fusion protein (ODD-green fluorescent protein) that combined the ODD domain of HIF-1alpha and the green fluorescent protein. Hydroxyproline hypoxia inducible factor 1 subunit alpha Rattus norvegicus