Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling.

By S. Rhee, H. Chae, Kanghwa Kim. Free Radical Biology & Medicine, 2005

1,432 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/edd69f7d4f966f8e2bcc910216e0fa33d14f3633

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Citations in the corpus

Cadmium stress: an oxidative challenge (2010, neutral): “Peroxiredoxins function as thiol peroxidases that catalyze the reduction of hydrogen peroxide, organic hydroperoxides as well as peroxynitrite (Rhee et al. 2005).”
Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production (2008, background): “Mammalian cells express six isoforms of PRX (PRX I–VI) that are distributed differentially within the cell: PRX I, II, and VI are found in the cytosol; PRX III is located in the mitochondrion; PRX IV is located in the extracellular space; and PRX V is located in both mitochondria and peroxisomes (32”
Oxidative stress and neurodegeneration: where are we now? (2006, background): “This is probably because H2O2 is involved in many intercellular and intracellular signaling processes (reviewed by Rhee et al. 2005; Halliwell and Gutteridge 2006).”
Redox-based regulation of signal transduction: principles, pitfalls, and promises. (2008, background): “Recent studies have shown that the sulfinic acid form of 2-cys peroxiredoxins can be reduced back to the sulfhydryl in an ATP-dependent enzyme-(sulfiredoxin, Srx) catalyzed reaction [39], and a reversible thioesterifcation has been reported to alter transcriptional activity [40], raising the possibi”
REACTIVE OXYGEN SPECIES, CELLULAR REDOX SYSTEMS AND APOPTOSIS (2010, positive): “Matrix H2O2 is removed by catalase [13] while urate oxidase-catalyzed H2O2 generation within the core is directly released into the cytosol via cristaloid core tubules [13].”
Mechanisms of cell protection by heme oxygenase-1. (2010, background): “Prx1 is a member of a larger family of peroxiredoxins (191, 192) that acts as a cytoplasmic heme scavenger that neutralizes the pro-oxidant activity of free heme (Figure 5).”
Oxidative stress and reactive oxygen species in endothelial dysfunction associated with cardiovascular and metabolic diseases. (2018, background): “Prx1-5 isoforms require 2 cysteine residues whereas Prx6 requires one cysteine residue for the catalytic activity [105].”
Hydrogen Peroxide: A Signaling Messenger (2006, neutral): “Likewise the use of a peroxiredoxin, a thiolate-dependent thioredoxin peroxidase, also does not allow for definitive identification of H2O2 as the specific reactive species involved, as peroxiredoxins react quite well with distinct reactive species such as peroxynitrite and lipid peroxides (178, 231”
Glutathione Peroxidase-1 in Health and Disease: From Molecular Mechanisms to Therapeutic Opportunities (2011, neutral): “Theoretically, hydrogen peroxide may modulate signal transduction through the (reversible) oxidation of proteins at redox-active Cyss, including free thiols in tyrosine kinase phosphatases (307).”
Reactive Species and Antioxidants. Redox Biology Is a Fundamental Theme of Aerobic Life (2006, background): “It has now been realized that peroxiredoxins may be the most important H2O2-removal systems in animals, bacteria, and possibly plants (Rhee et al., 2005).”
Peroxynitrite: biochemistry, pathophysiology and development of therapeutics (2007, background): “Peroxiredoxin V reduced peroxynitrite with a rate constant of 7 × 10 7 M −1 s −1 — a high value not only for peroxynitrite but also for peroxide-thiol reactions in genera”