Pub. Date : 2014 Mar 13
PMID : 23542169
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | In addition, RUNX3 directly interacted with the C-terminal activation domain of HIF-1alpha and prolyl hydroxylase (PHD) 2 and enhanced the interaction between HIF-1alpha and PHD2, which potentiated proline hydroxylation and promoted the degradation of HIF-1alpha. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
| 2 | In addition, RUNX3 directly interacted with the C-terminal activation domain of HIF-1alpha and prolyl hydroxylase (PHD) 2 and enhanced the interaction between HIF-1alpha and PHD2, which potentiated proline hydroxylation and promoted the degradation of HIF-1alpha. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
| 3 | In addition, RUNX3 directly interacted with the C-terminal activation domain of HIF-1alpha and prolyl hydroxylase (PHD) 2 and enhanced the interaction between HIF-1alpha and PHD2, which potentiated proline hydroxylation and promoted the degradation of HIF-1alpha. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
| 4 | Taken together, these results suggest that RUNX3 destabilizes HIF-1alpha protein by promoting the proline hydroxylation of HIF-1alpha through binding to HIF-1alpha/PHD2. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
| 5 | Taken together, these results suggest that RUNX3 destabilizes HIF-1alpha protein by promoting the proline hydroxylation of HIF-1alpha through binding to HIF-1alpha/PHD2. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
| 6 | Taken together, these results suggest that RUNX3 destabilizes HIF-1alpha protein by promoting the proline hydroxylation of HIF-1alpha through binding to HIF-1alpha/PHD2. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |