Title : HIF-1alpha peptide derivatives with modifications at the hydroxyproline residue as activators of HIF-1alpha.

Pub. Date : 2009 Aug 1

PMID : 19515556






10 Functional Relationships(s)
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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