Structure, mechanism and regulation of peroxiredoxins.

By Z. A. Wood, E. Schröder, J. Robin Harris, Leslie B. Poole. TIBS -Trends in Biochemical Sciences. Regular ed, 2003

2,477 citations recorded by the source corpus.

Subfields: Biochemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/3142366b92b67f1ecf693ef55b8ed52517a0abc7

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Citations in the corpus

Antioxidants and Antioxidant Enzymes in Higher Plants (2018, background): “Specific cyclin-dependent kinases phosphorylate a Thr residue at the a3 helix of the mammalian prx1-type peroxiredoxins, which leads to the attenuation of peroxidase activity probably by destabilization of the decamers (Chang et al. 2002; Wood et al. 2003; Jang et al. 2006).”
Multiple catalytically active thioredoxin folds: a winning strategy for many functions (2010, background): “Prxs can be divided into 2-Cys and 1-Cys type based on the number of cysteine residues involved in the catalysis [157].”
Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. (2005, methodology): “Members of the Prx family of peroxidases catalyze the reduction of H2O2 and alkyl hydroperoxides to water and alcohol, respectively, using reducing equivalents provided by thiol-containing proteins [29–32], and they have been detected in organisms representative of all kingdoms.”
Reactive Oxygen Species and Antioxidant Enzymes Involved in Plant Tolerance to Stress (2016, background): “These enzymes do not possess a prosthetic group and catalyze the reduction of H2O2, perox‐ ynitrite, and a wide variety of organic hydroperoxides to their corresponding alcohols [31].”
Redox Regulation of Cell Survival (2008, neutral): “Peroxiredoxins use the peroxidatic cysteine (reactive center) to reduce hydroperoxides in a two-step reaction [for review, see (332)].”
DJ‐1 has a role in antioxidative stress to prevent cell death (2004, background): “Members of the family of peroxiredoxin proteins, such as thioredoxin peroxidase, eliminate hydrogen peroxide by the use of electrons provided by thioredoxin, and the resultant oxidized thioredoxin peroxidase is then reduced back to the active form (Jacquot et al, 2002; Wood et al, 2003).”
Trends in oxidative aging theories. (2007, background): “Six peroxiredoxins have been identified in the mammalian genome [225].”
Antioxidant responses and cellular adjustments to oxidative stress (2015, background): “Peroxiredoxins are thiol-specific proteins that react with H2O2 at a very high rate [22].”