Title : Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.

Pub. Date : 2001 Aug 10

PMID : 11390385






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 hCyP-A supported antioxidant activity of Prx II and Prx VI both against thiol (dithiothreitol)-containing metal-catalyzed oxidation (MCO) systems and ascorbate-containing MCO systems. Sulfhydryl Compounds peptidylprolyl isomerase A Homo sapiens
2 hCyP-A supported antioxidant activity of Prx II and Prx VI both against thiol (dithiothreitol)-containing metal-catalyzed oxidation (MCO) systems and ascorbate-containing MCO systems. Dithiothreitol peptidylprolyl isomerase A Homo sapiens
3 hCyP-A supported antioxidant activity of Prx II and Prx VI both against thiol (dithiothreitol)-containing metal-catalyzed oxidation (MCO) systems and ascorbate-containing MCO systems. Metals peptidylprolyl isomerase A Homo sapiens
4 hCyP-A supported antioxidant activity of Prx II and Prx VI both against thiol (dithiothreitol)-containing metal-catalyzed oxidation (MCO) systems and ascorbate-containing MCO systems. Ascorbic Acid peptidylprolyl isomerase A Homo sapiens
5 In addition, Cys(115) and Cys(161) of hCyP-A were found to be involved in the activation and the reduction of Prx. Cysteine peptidylprolyl isomerase A Homo sapiens
6 In addition, Cys(115) and Cys(161) of hCyP-A were found to be involved in the activation and the reduction of Prx. Cysteine peptidylprolyl isomerase A Homo sapiens