Title : Identification of an alternative mechanism of degradation of the hypoxia-inducible factor-1alpha.

Pub. Date : 2008 Oct 24

PMID : 18694926






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 At normoxia two specific proline residues (Pro(402) and Pro(563)) of mHIF-1alpha are hydroxylated and recognized by the von Hippel-Lindau E3 ubiquitin ligase (pVHL) complex, which upon binding mediates degradation of the protein. Proline von Hippel-Lindau tumor suppressor Homo sapiens
2 At normoxia two specific proline residues (Pro(402) and Pro(563)) of mHIF-1alpha are hydroxylated and recognized by the von Hippel-Lindau E3 ubiquitin ligase (pVHL) complex, which upon binding mediates degradation of the protein. Proline von Hippel-Lindau tumor suppressor Homo sapiens
3 At normoxia two specific proline residues (Pro(402) and Pro(563)) of mHIF-1alpha are hydroxylated and recognized by the von Hippel-Lindau E3 ubiquitin ligase (pVHL) complex, which upon binding mediates degradation of the protein. Proline von Hippel-Lindau tumor suppressor Homo sapiens
4 Previous studies have demonstrated that these two proline residues are critical for high affinity binding to pVHL. Proline von Hippel-Lindau tumor suppressor Homo sapiens