"Peroxiredoxins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A family of ubiquitously-expressed peroxidases that play a role in the reduction of a broad spectrum of PEROXIDES like HYDROGEN PEROXIDE; LIPID PEROXIDES and peroxinitrite. They are found in a wide range of organisms, such as BACTERIA; PLANTS; and MAMMALS. The enzyme requires the presence of a thiol-containing intermediate such as THIOREDOXIN as a reducing cofactor.
| Descriptor ID |
D054464
|
| MeSH Number(s) |
D08.811.682.732.850
|
| Concept/Terms |
Peroxiredoxins- Peroxiredoxins
- Alkylhydroperoxide Reductase
- Peroxidoxin
- Thioredoxin Peroxidase
- Protector Protein (Mixed-Function Oxidase Systems)
- Thiol-Specific Antioxidant Protein
- Thiol Specific Antioxidant Protein
- Alkyl Hydroperoxide Reductase
- Hydroperoxide Reductase, Alkyl
- Peroxiredoxin
Peroxiredoxin II- Peroxiredoxin II
- Thioredoxin Peroxidase 1
- Thioredoxin-Dependent Peroxide Reductase 1
- Thioredoxin Dependent Peroxide Reductase 1
- Peroxiredoxin 2
Peroxiredoxin I- Peroxiredoxin I
- Thioredoxin Peroxidase 2
- Thioredoxin-Dependent Peroxide Reductase 2
- Thioredoxin Dependent Peroxide Reductase 2
- Peroxiredoxin 1
|
Below are MeSH descriptors whose meaning is more general than "Peroxiredoxins".
Below are MeSH descriptors whose meaning is more specific than "Peroxiredoxins".
This graph shows the total number of publications written about "Peroxiredoxins" by people in this website by year, and whether "Peroxiredoxins" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1996 | 0 | 1 | 1 |
| 2004 | 0 | 1 | 1 |
| 2006 | 0 | 1 | 1 |
| 2007 | 0 | 1 | 1 |
| 2008 | 1 | 0 | 1 |
| 2013 | 1 | 0 | 1 |
| 2016 | 1 | 1 | 2 |
| 2019 | 1 | 0 | 1 |
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Below are the most recent publications written about "Peroxiredoxins" by people in Profiles.
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ABHD10 is an S-depalmitoylase affecting redox homeostasis through peroxiredoxin-5. Nat Chem Biol. 2019 12; 15(12):1232-1240.
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Epigenetic regulation of redox state mediates persistent cardiorespiratory abnormalities after long-term intermittent hypoxia. J Physiol. 2017 01 01; 595(1):63-77.
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Increasing extracellular H2O2 produces a bi-phasic response in intracellular H2O2, with peroxiredoxin hyperoxidation only triggered once the cellular H2O2-buffering capacity is overwhelmed. Free Radic Biol Med. 2016 06; 95:333-48.
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Peroxiredoxin-5 targeted to the mitochondrial intermembrane space attenuates hypoxia-induced reactive oxygen species signalling. Biochem J. 2013 Dec 15; 456(3):337-46.
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Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1. Nature. 2010 Dec 02; 468(7324):696-700.
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Decreased expression of peroxiredoxins in Fuchs' endothelial dystrophy. Invest Ophthalmol Vis Sci. 2008 Jul; 49(7):2956-63.
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Characterization of the complex of glutathione S-transferase pi and 1-cysteine peroxiredoxin. Arch Biochem Biophys. 2008 Jun 01; 474(1):109-18.
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Paraquat induces dopaminergic dysfunction and proteasome impairment in DJ-1-deficient mice. Hum Mol Genet. 2007 Dec 01; 16(23):2900-10.
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Cytogenetic and molecular study of the PRDX4 gene in a t(X;18)(p22;q23): a cautionary tale. Cancer Genet Cytogenet. 2007 Jul 15; 176(2):131-6.
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Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes. Biochemistry. 2006 Jan 17; 45(2):360-72.