A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis (Q24536498)

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Quan Zhao

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Adrian Flores

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Claire Harrison

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Terence R J Lappin

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Patrick H Maxwell

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Mary Frances McMullin

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Frank S Lee

original language of film or TV show

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English

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publication date

17 January 2006

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published in

Proceedings of the National Academy of Sciences of the United States of America

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volume

103

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issue

3

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page(s)

654-9

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cites work

VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1alpha

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A common polymorphism in the oxygen-dependent degradation (ODD) domain of hypoxia inducible factor-1alpha (HIF-1alpha) does not impair Pro-564 hydroxylation

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HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia

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The VHL protein recruits a novel KRAB-A domain protein to repress HIF-1alpha transcriptional activity

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Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha

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Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor

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A conserved family of prolyl-4-hydroxylases that modify HIF

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C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

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HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation

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HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing

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Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex

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Mechanism of regulation of the hypoxia-inducible factor-1 alpha by the von Hippel-Lindau tumor suppressor protein

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The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis

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Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway

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Targeting HIF-1 for cancer therapy

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Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation

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Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

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Induction of human endometrial cancer cell senescence through modulation of HIF-1alpha activity by EGLN1

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Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor

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Tat-binding protein-1, a component of the 26S proteasome, contributes to the E3 ubiquitin ligase function of the von Hippel-Lindau protein

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