Inactivation of Human Peroxiredoxin I during Catalysis as the Result of the Oxidation of the Catalytic Site Cysteine to Cysteine-sulfinic Acid

Thioredoxin-dependent peroxide reductase from yeast.

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Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes.

Chae, H. Z., Robison, K. E., Poole, L. B., Church, G. M., Storz, G., & Rhee, S. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.7017 · Cited by 749 · see citing works

Mammalian Peroxiredoxin Isoforms Can Reduce Hydrogen Peroxide Generated in Response to Growth Factors and Tumor Necrosis Factor-α

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Peroxiredoxin, a Novel Family of Peroxidases

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Protein-Sulfenic Acids: Diverse Roles for an Unlikely Player in Enzyme Catalysis and Redox Regulation

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The isolation and purification of a specific “protector” protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system.

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Identification of a New Type of Mammalian Peroxiredoxin That Forms an Intramolecular Disulfide as a Reaction Intermediate

Seo, M. S., Kang, S. W., Kim, K., Baines, I., Lee, T., & Rhee, S. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001943200 · Cited by 473 · see citing works

Characterization of a Mammalian Peroxiredoxin That Contains One Conserved Cysteine

Kang, S. W., Baines, I., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.11.6303 · Cited by 448 · see citing works

Regulatory Role for a Novel Human Thioredoxin Peroxidase in NF-κB Activation

Jin, D., Chae, H. Z., Rhee, S. G., & Jeang, K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.30952 · Cited by 412 · see citing works

Proteomics Analysis of Cellular Response to Oxidative Stress

Rabilloud, T., Heller, M., Gasnier, F., Luche, S., Rey, C., Aebersold, R., Benahmed, M., Louisot, P., & Lunardi, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106585200 · Cited by 393 · see citing works

Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin

Chae, H. Z., Kim, H. J., Kang, S. W., & Rhee, S. G. (1999) · Diabetes Research and Clinical Practice · doi:10.1016/s0168-8227(99)00037-6 · Cited by 390 · see citing works

Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution

Choi, H., Kang, S. W., Yang, C., Rhee, S. G., & Ryu, S.-E. (1998) · Nature Structural Biology · doi:10.1038/nsb0598-400 · Cited by 380 · see citing works

Thioredoxin Peroxidase Is a Novel Inhibitor of Apoptosis with a Mechanism Distinct from That of Bcl-2

Zhang, P., Liu, B., Kang, S. W., Seo, M. S., Rhee, S. G., & Obeid, L. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.30615 · Cited by 368 · see citing works

An Alkyl Hydroperoxide Reductase from Salmonella typhimurium Involved in the Defense of DNA against Oxidative Damage

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Dimers to Doughnuts: Redox-Sensitive Oligomerization of 2-Cysteine Peroxiredoxins,

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Dimerization of thiol-specific antioxidant and the essential role of cysteine 47.

Chae, H. Z., Uhm, T.-B., & Rhee, S. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.7022 · Cited by 309 · see citing works

Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7Å resolution

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Phospholipid Hydroperoxides Are Substrates for Non-selenium Glutathione Peroxidase

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Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae

Chae, H. Z., Kim, I. H., Kim, K., & Rhee, S. G. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85489-3 · Cited by 294 · see citing works

Identification of Proteins Containing Cysteine Residues That Are Sensitive to Oxidation by Hydrogen Peroxide at Neutral pH

Kim, J.-R., Yoon, H. W., Kwon, K., Lee, S.-R., & Rhee, S. G. (2000) · Analytical Biochemistry · doi:10.1006/abio.2000.4623 · Cited by 273 · see citing works

An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp

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Formation and reactions of sulfenic acids in proteins

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Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product

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Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin

Chae, H. Z., Kang, S. W., & Rhee, S. G. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)00128-7 · Cited by 238 · see citing works

Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaptation to oxidative stress

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Roles for the Two Cysteine Residues of AhpC in Catalysis of Peroxide Reduction by Alkyl Hydroperoxide Reductase from Salmonella typhimurium

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Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases.

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Perchloric Acid Enhances Sensitivity and Reproducibility of the Ferric–Xylenol Orange Peroxide Assay

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The Structure of Reduced Tryparedoxin Peroxidase Reveals a Decamer and Insight into Reactivity of 2Cys-peroxiredoxins

Alphey, M. S., Bond, C. S., Tétaud, E., Fairlamb, A. H., & Hunter, W. N. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3881 · Cited by 155 · see citing works

Induction of an antioxidant protein of Saccharomyces cerevisiae by O2, Fe3+, or 2-mercaptoethanol.

Kim, I. H., Kim, K., & Rhee, S. G. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.16.6018 · Cited by 137 · see citing works

Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member

Matsumoto, A., Okado‐Matsumoto, A., Fujii, T., Fujii, J., Egashira, M., Niikawa, N., & Taniguchi, N. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01736-0 · Cited by 133 · see citing works

Tryparedoxin Peroxidase of Leishmania donovani: Molecular Cloning, Heterologous Expression, Specificity, and Catalytic Mechanism

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Variants of peroxiredoxins expression in response to hydroperoxide stress

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Chemistry of sulfenic acids. 7. Reason for the high reactivity of sulfenic acids. Stabilization by intramolecular hydrogen bonding and electronegativity effects

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The Non-flavin Redox Center of the Streptococcal NADH Peroxidase

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Structure of the Native Cysteine-Sulfenic Acid Redox Center of Enterococcal NADH Peroxidase Refined at 2.8 Å Resolution,

Yeh, J. I., Claiborne, A., & Hol, W. G. J. (1996) · Biochemistry · doi:10.1021/bi961037s · Cited by 87 · see citing works

Augmented expression of peroxiredoxin VI in rat lung and kidney after birth implies an antioxidative role

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A Novel Glutathione Peroxidase in Bovine Eye

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Activation of active‐site cysteine residues in the peroxiredoxin‐type tryparedoxin peroxidase of Crithidia fasciculata

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A thiol-specific antioxidant and sequence homology to various proteins of unknown function.

Chae, H. Z., & Rhee, S. (1994) · PubMed · Cited by 73 · see citing works

Identification of a 28 kDa secretory protein from rat olfactory epithelium as a thiol-specific antioxidant

Peshenko, I. V., Novoselov, V. I., Va, E., Nikolaev, Y. V., Kamzalov, S., Shuvaeva, T. M., Липкин, В. М., & Fesenko, E. E. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00111-7 · Cited by 53 · see citing works

Nonredundant Antioxidant Defense by Multiple Two-Cysteine Peroxiredoxins in Human Prostate Cancer Cells

Shen, C., & Nathan, C. (2002) · Molecular Medicine · doi:10.1007/bf03402079 · Cited by 44 · see citing works

A QSPR-Approach to the Estimation of the p K HB of Six-Membered Nitrogen-Heterocycles using Quantum Mechanically Derived Descriptors

Hennemann, M., & Clark, T. (2002) · Journal of Molecular Modeling · doi:10.1007/s00894-002-0075-z · Cited by 39 · see citing works

Monitoring Antisense Oligodeoxynucleotide Activity in Hematopoietic Cells

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Analysis of the Kinetic and Redox Properties of the NADH Peroxidase R303M Mutant: Correlation with the Crystal Structure,

Crane, E. J., Yeh, J. I., Luba, J. P., & Claiborne, A. (2000) · Biochemistry · doi:10.1021/bi000553m · Cited by 18 · see citing works

ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis

D'Autréaux, B., & Toledano, M. B. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2256 · Cited by 3,642 · see citing works

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

Rhee, S. G., Chae, H. Z., & Kim, K. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.026 · Cited by 1,409 · see citing works

Thiol chemistry and specificity in redox signaling

Winterbourn, C. C., & Hampton, M. B. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.004 · Cited by 1,226 · see citing works

Mitochondrial Dysfunction and Oxidative Damage in parkin-deficient Mice

Palacino, J. J., Sagi, D., Goldberg, M. S., Krauss, S., Motz, C., Wacker, M., Klose, J., & Shen, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401135200 · Cited by 995 · see citing works

Redox-based regulation of signal transduction: principles, pitfalls, and promises

Janssen-Heininger, Y. M. W., Mossman, B. T., Heintz, N. H., Forman, H. J., Kalyanaraman, B., Finkel, T., Stamler, J. S., Rhee, S. G., & van der Vliet, A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.011 · Cited by 784 · see citing works

Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD

Budanov, A. V., Sablina, A. A., Feinstein, E., Koonin, E. V., & Chumakov, P. M. (2004) · Science · doi:10.1126/science.1095569 · Cited by 731 · see citing works

Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors

Kwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., & Rhee, S. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407396101 · Cited by 631 · see citing works

Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides

Rhee, S. G., Woo, H. A., Kil, I. S., & Bae, S. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.283432 · Cited by 603 · see citing works

Redox regulation of mitochondrial function

Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works

Multiple Functions of Peroxiredoxins: Peroxidases, Sensors and Regulators of the Intracellular Messenger H ₂ O ₂ , and Protein Chaperones

Rhee, S. G., & Woo, H. A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3393 · Cited by 463 · see citing works

Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II

Choi, M. H., Lee, I. K., Kim, G. W., Kim, B. U., Han, Y.-H., Yu, D.-Y., Park, H. S., Kim, K. Y., Lee, J. S., Choi, C., et al. (2005) · Nature · doi:10.1038/nature03587 · Cited by 403 · see citing works

Characterization of Mammalian Sulfiredoxin and Its Reactivation of Hyperoxidized Peroxiredoxin through Reduction of Cysteine Sulfinic Acid in the Active Site to Cysteine

Chang, T.-S., Jeong, W., Woo, H. A., Lee, S. M., Park, S., & Rhee, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409482200 · Cited by 388 · see citing works

Controlled Elimination of Intracellular H ₂ O2: Regulation of Peroxiredoxin, Catalase, and Glutathione Peroxidase via Post-translational Modification

Rhee, S. G., Yang, K.-S., Kang, S. W., Woo, H. A., & Chang, T.-S. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.619 · Cited by 376 · see citing works

Metformin promotes lifespan through mitohormesis via the peroxiredoxin PRDX-2

De Haes, W., Frooninckx, L., Van Assche, R., Smolders, A., Depuydt, G., Billen, J., Braeckman, B. P., Schoofs, L., & Temmerman, L. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321776111 · Cited by 355 · see citing works

A Model of Redox Kinetics Implicates the Thiol Proteome in Cellular Hydrogen Peroxide Responses

Adimora, N. J., Jones, D. P., & Kemp, M. L. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2968 · Cited by 175 · see citing works

Inhibition of Mitochondrial Aconitase by Succination in Fumarate Hydratase Deficiency

Ternette, N., Yang, M., Laroyia, M., Kitagawa, M., O’Flaherty, L., Wolhulter, K., Igarashi, K., Saito, K., Kato, K., Fischer, R., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.02.013 · Cited by 158 · see citing works

Concerted Action of Sulfiredoxin and Peroxiredoxin I Protects Against Alcohol-Induced Oxidative Injury in Mouse Liver σ

Bae, S. H., Sung, S. H., Cho, E. J., Lee, S. K., Lee, H. E., Woo, H. A., Yu, D.-Y., Kil, I. S., & Rhee, S. G. (2011) · Hepatology · doi:10.1002/hep.24104 · Cited by 93 · see citing works

Proteomics Analysis of Cellular Response to Oxidative Stress

Rabilloud, T., Heller, M., Gasnier, F., Luche, S., Rey, C., Aebersold, R., Benahmed, M., Louisot, P., & Lunardi, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106585200 · Cited by 393 · see citing works

Mechanistic characterization of the thioredoxin system in the removal of hydrogen peroxide

Pannala, V. R., & Dash, R. K. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.10.508 · Cited by 72 · see citing works

Mechanistic Characterization of the Thioredoxin System in the Removal of Hydrogen Peroxide

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Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica

Arias, D. G., Carranza, P. G., Luján, H. D., et al. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.008 · Cited by 33 · see citing works

Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin

Chae, H. Z., Kang, S. W., & Rhee, S. G. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)00128-7 · Cited by 238 · see citing works