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• W2030872095 abstract "We have identified human and mouse peroxiredoxin V (Prx-V) by virtue of the sequence homologies to yeast peroxisomal antioxidant enzyme PMP20. Prx-V represents the fifth of the six currently known subfamilies of mammalian peroxiredoxins. It is a novel organellar enzyme that has orthologs in bacteria. Biochemically, Prx-V is a thioredoxin peroxidase. One important aspect of p53 function in mammalian cells involves induction of apoptosis likely mediated by redox. We show that overexpression of Prx-V prevented the p53-dependent generation of reactive oxygen species. Likewise, Prx-V inhibited p53-induced apoptosis. Thus, Prx-V is critically involved in intracellular redox signaling." @default.
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• W2030872095 date "2000-02-01" @default.
• W2030872095 modified "2023-10-02" @default.
• W2030872095 title "Mouse Peroxiredoxin V Is a Thioredoxin Peroxidase That Inhibits p53-Induced Apoptosis" @default.
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• W2030872095 doi "https://doi.org/10.1006/bbrc.2000.2231" @default.
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