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10.1126/science.1059817

http://scihub22266oqcxt.onion/10.1126/science.1059817
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11292862!?!11292862

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suck abstract from ncbi

pmid11292862      Science 2001 ; 292 (5516): 464-8
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  • HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing #MMPMID11292862
  • Ivan M; Kondo K; Yang H; Kim W; Valiando J; Ohh M; Salic A; Asara JM; Lane WS; Kaelin WG Jr
  • Science 2001[Apr]; 292 (5516): 464-8 PMID11292862show ga
  • HIF (hypoxia-inducible factor) is a transcription factor that plays a pivotal role in cellular adaptation to changes in oxygen availability. In the presence of oxygen, HIF is targeted for destruction by an E3 ubiquitin ligase containing the von Hippel-Lindau tumor suppressor protein (pVHL). We found that human pVHL binds to a short HIF-derived peptide when a conserved proline residue at the core of this peptide is hydroxylated. Because proline hydroxylation requires molecular oxygen and Fe(2+), this protein modification may play a key role in mammalian oxygen sensing.
  • |*Ligases[MESH]
  • |*Tumor Suppressor Proteins[MESH]
  • |*Ubiquitin-Protein Ligases[MESH]
  • |Amino Acid Sequence[MESH]
  • |Animals[MESH]
  • |Basic Helix-Loop-Helix Transcription Factors[MESH]
  • |Cell Hypoxia[MESH]
  • |Cell Line[MESH]
  • |Cobalt/pharmacology[MESH]
  • |Deferoxamine/pharmacology[MESH]
  • |Humans[MESH]
  • |Hydroxylation[MESH]
  • |Hydroxyproline/*metabolism[MESH]
  • |Mass Spectrometry[MESH]
  • |Mice[MESH]
  • |Molecular Sequence Data[MESH]
  • |Oxygen/*physiology[MESH]
  • |Protein Structure, Tertiary[MESH]
  • |Proteins/*metabolism[MESH]
  • |Recombinant Fusion Proteins/metabolism[MESH]
  • |Trans-Activators/chemistry/genetics/*metabolism[MESH]
  • |Transcription Factors/*metabolism[MESH]
  • |Tumor Cells, Cultured[MESH]
  • |Ubiquitins/metabolism[MESH]


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