Pub. Date : 2009 Aug 1
PMID : 19515556
10 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Hypoxia-inducible factor (HIF)-1alpha undergoes degradation under normoxia, which involves its proline hydroxylation and subsequent binding of proline-hydroxylated HIF-1alpha to the von Hippel-Lindau protein-Elongin B-Elongin C (VBC) complex. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
2 | Hypoxia-inducible factor (HIF)-1alpha undergoes degradation under normoxia, which involves its proline hydroxylation and subsequent binding of proline-hydroxylated HIF-1alpha to the von Hippel-Lindau protein-Elongin B-Elongin C (VBC) complex. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
3 | Hypoxia-inducible factor (HIF)-1alpha undergoes degradation under normoxia, which involves its proline hydroxylation and subsequent binding of proline-hydroxylated HIF-1alpha to the von Hippel-Lindau protein-Elongin B-Elongin C (VBC) complex. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
4 | In this study, we designed and synthesized a series of peptides containing 556-575 residues of HIF-1alpha with modifications at the Pro-564 residue to inhibit the interaction between proline-hydroxylated HIF-1alpha and VBC. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
5 | In this study, we designed and synthesized a series of peptides containing 556-575 residues of HIF-1alpha with modifications at the Pro-564 residue to inhibit the interaction between proline-hydroxylated HIF-1alpha and VBC. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
6 | In this study, we designed and synthesized a series of peptides containing 556-575 residues of HIF-1alpha with modifications at the Pro-564 residue to inhibit the interaction between proline-hydroxylated HIF-1alpha and VBC. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
7 | In this study, we designed and synthesized a series of peptides containing 556-575 residues of HIF-1alpha with modifications at the Pro-564 residue to inhibit the interaction between proline-hydroxylated HIF-1alpha and VBC. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
8 | Considering that proline hydroxylation of HIF-1alpha is routinely targeted for modulating the HIF pathway, our approach of using inhibitors against the interactions between HIF-1alpha and VBC would provide an alternative way of upregulating HIF-1 activity. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
9 | Considering that proline hydroxylation of HIF-1alpha is routinely targeted for modulating the HIF pathway, our approach of using inhibitors against the interactions between HIF-1alpha and VBC would provide an alternative way of upregulating HIF-1 activity. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
10 | Considering that proline hydroxylation of HIF-1alpha is routinely targeted for modulating the HIF pathway, our approach of using inhibitors against the interactions between HIF-1alpha and VBC would provide an alternative way of upregulating HIF-1 activity. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |