Regulation of the HIF pathway: enzymatic hydroxylation of a conserved prolyl residue in hypoxia-inducible factor alpha subunits governs capture by the pVHL E3 ubiquitin ligase complex

Adv Enzyme Regul. 2002:42:333-47. doi: 10.1016/s0065-2571(01)00037-1.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Basic Helix-Loop-Helix Transcription Factors
  • Cobalt / metabolism
  • Dose-Response Relationship, Drug
  • Humans
  • Hypoxia
  • Hypoxia-Inducible Factor 1, alpha Subunit
  • Iron / metabolism
  • Ketoglutaric Acids / metabolism
  • Ligases / metabolism
  • Oxygen / metabolism
  • Plasmids / metabolism
  • Proline / chemistry*
  • Protein Biosynthesis
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / metabolism
  • Reticulocytes / metabolism
  • Time Factors
  • Trans-Activators / chemistry
  • Trans-Activators / metabolism*
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism*
  • Tumor Cells, Cultured
  • Tumor Suppressor Proteins*
  • Ubiquitin / metabolism
  • Ubiquitin-Protein Ligases
  • Von Hippel-Lindau Tumor Suppressor Protein

Substances

  • Basic Helix-Loop-Helix Transcription Factors
  • HIF1A protein, human
  • Hypoxia-Inducible Factor 1, alpha Subunit
  • Ketoglutaric Acids
  • Recombinant Fusion Proteins
  • Trans-Activators
  • Transcription Factors
  • Tumor Suppressor Proteins
  • Ubiquitin
  • endothelial PAS domain-containing protein 1
  • Cobalt
  • Proline
  • Iron
  • Ubiquitin-Protein Ligases
  • Von Hippel-Lindau Tumor Suppressor Protein
  • Ligases
  • VHL protein, human
  • Oxygen