SUBCELLULAR LOCALIZATION
| extracellular
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| intracellular
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| intracellular,cytoplasm,organelle,mitochondria
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| intracellular,cytoplasm,organelle,endoplasmic reticulum
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| intracellular,cytoplasm,cytosolic
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| intracellular,nucleus
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text
| localized mainly in the nucleus of neural cells |
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only endoplasmic reticulum localized peroxiredoxin |
basic FUNCTION
| playing a regulatory role in the activation of the transcription factor NF-kappaB |
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involved in protection against oxidative stress through the detoxification of cellular peroxides |
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endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells |
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important for spermatogenesis, but not an absolute requisite |
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essential for preventing respiratory syncytial virus-induced oxidative damage in a subset of nuclear intermediate filament and actin binding proteins in epithelial cells |
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ER-localized and implicated in a previously unanticipated, parallel, ERO1-independent pathway that couples hydroperoxide production to oxidative protein folding in mammalian cells |
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PRDX3 and PRDX4, may act as new placental immune targets, and are involved in recurrent pregnancy loss |
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different binding properties of ERO1A and PRDX4 increase the robustness of ER redox homeostasis |
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may have a close relationship with follicular development |
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PRDX4-recycling in the endoplasmic reticulum is much less efficient than in the cytosol or mitochondria, leading to the protection of PRDX4 from hyperoxidation |
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ER-specific antioxidative peroxidase that can utilize luminal H2O2 as driving force for reoxidizing protein disulfide isomerase family members, thus efficiently contributing to disulfide bond formation |
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important role of PRDX4 in maintaining insulin levels and improving the ER folding capacity also under conditions of a high insulin requirement |
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functions not only to eliminate peroxide but also to promote oxidative protein folding via oxidizing protein disulfide isomerase (PDI) |
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novel function of secreted PRDX4 in mediating osteoclast activation by cancer cells |
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PRDX4 oxidative activity acts as a sensor to directly couple neuronal differentiation with redox environments in the ER |
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PRDX2 and PRDX4 are negative regulators of hypoxia-inducible factors under conditions of prolonged hypoxia |
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