Sulfiredoxin, the cysteine sulfinic acid reductase specific to 2-Cys peroxiredoxin: its discovery, mechanism of action, and biological significance.

[1]  C. Winterbourn,et al.  The High Reactivity of Peroxiredoxin 2 with H2O2 Is Not Reflected in Its Reaction with Other Oxidants and Thiol Reagents* , 2007, Journal of Biological Chemistry.

[2]  Ho Jin Sung,et al.  Mutagenesis and modeling of the peroxiredoxin (Prx) complex with the NMR structure of ATP-bound human sulfiredoxin implicate aspartate 187 of Prx I as the catalytic residue in ATP hydrolysis. , 2006, Biochemistry.

[3]  S. Rhee,et al.  Molecular Mechanism of the Reduction of Cysteine Sulfinic Acid of Peroxiredoxin to Cysteine by Mammalian Sulfiredoxin* , 2006, Journal of Biological Chemistry.

[4]  P. Karplus,et al.  Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. , 2005, Biochemistry.

[5]  M. Cho,et al.  Oxidative Stress-dependent Structural and Functional Switching of a Human 2-Cys Peroxiredoxin Isotype II That Enhances HeLa Cell Resistance to H2O2-induced Cell Death* , 2005, Journal of Biological Chemistry.

[6]  A. Vivancos,et al.  A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[7]  W. Lowther,et al.  Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxin. , 2005, Biochemistry.

[8]  B. Morgan,et al.  Oxidation of a Eukaryotic 2-Cys Peroxiredoxin Is a Molecular Switch Controlling the Transcriptional Response to Increasing Levels of Hydrogen Peroxide* , 2005, Journal of Biological Chemistry.

[9]  S. Rhee,et al.  Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. , 2005, Free radical biology & medicine.

[10]  N. Tonks Redox Redux: Revisiting PTPs and the Control of Cell Signaling , 2005, Cell.

[11]  E. Koonin,et al.  Evolution of Eukaryotic Cysteine Sulfinic Acid Reductase, Sulfiredoxin (Srx), from Bacterial Chromosome Partitioning Protein ParB , 2005, Cell cycle.

[12]  Kap-Seok Yang,et al.  Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. , 2005, Current opinion in cell biology.

[13]  Michael Karin,et al.  Reactive Oxygen Species Promote TNFα-Induced Death and Sustained JNK Activation by Inhibiting MAP Kinase Phosphatases , 2005, Cell.

[14]  S. Rhee,et al.  Reduction of Cysteine Sulfinic Acid by Sulfiredoxin Is Specific to 2-Cys Peroxiredoxins* , 2005, Journal of Biological Chemistry.

[15]  S. Rhee,et al.  Characterization of Mammalian Sulfiredoxin and Its Reactivation of Hyperoxidized Peroxiredoxin through Reduction of Cysteine Sulfinic Acid in the Active Site to Cysteine* , 2004, Journal of Biological Chemistry.

[16]  Kap-Seok Yang,et al.  Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[17]  B. Morgan,et al.  A 2-Cys peroxiredoxin regulates peroxide-induced oxidation and activation of a stress-activated MAP kinase. , 2004, Molecular cell.

[18]  N. Jones,et al.  Activation of the redox sensor Pap1 by hydrogen peroxide requires modulation of the intracellular oxidant concentration , 2004, Molecular microbiology.

[19]  Sang Yeol Lee,et al.  Two Enzymes in One Two Yeast Peroxiredoxins Display Oxidative Stress-Dependent Switching from a Peroxidase to a Molecular Chaperone Function , 2004, Cell.

[20]  Kap-Seok Yang,et al.  Reversible Oxidation of the Active Site Cysteine of Peroxiredoxins to Cysteine Sulfinic Acid , 2003, Journal of Biological Chemistry.

[21]  M. Toledano,et al.  ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin , 2003, Nature.

[22]  S. Orkin,et al.  Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression , 2003, Nature.

[23]  Kap-Seok Yang,et al.  Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation , 2003, Science.

[24]  P. Karplus,et al.  Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling , 2003, Science.

[25]  Z. A. Wood,et al.  Structure, mechanism and regulation of peroxiredoxins. , 2003, Trends in biochemical sciences.

[26]  Sue Goo Rhee,et al.  Inactivation of Human Peroxiredoxin I during Catalysis as the Result of the Oxidation of the Catalytic Site Cysteine to Cysteine-sulfinic Acid* , 2002, The Journal of Biological Chemistry.

[27]  N. Jones,et al.  Diethylmaleate activates the transcription factor Pap1 by covalent modification of critical cysteine residues , 2002, Molecular microbiology.

[28]  P. Karplus,et al.  Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins. , 2002, Biochemistry.

[29]  M. Won,et al.  Aggregation of alpha-synuclein induced by the Cu,Zn-superoxide dismutase and hydrogen peroxide system. , 2002, Free radical biology & medicine.

[30]  W. Toone,et al.  Distinct regulatory proteins control the graded transcriptional response to increasing H(2)O(2) levels in fission yeast Schizosaccharomyces pombe. , 2002, Molecular biology of the cell.

[31]  Eui Tae Kim,et al.  Regulation of thioredoxin peroxidase activity by C-terminal truncation. , 2002, Archives of biochemistry and biophysics.

[32]  S. Rhee,et al.  Peroxiredoxin, a Novel Family of Peroxidases , 2001, IUBMB life.

[33]  Sue Goo Rhee,et al.  Hydrogen Peroxide: A Key Messenger That Modulates Protein Phosphorylation Through Cysteine Oxidation , 2000, Science's STKE.

[34]  S. Rhee,et al.  Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH. , 2000, Analytical biochemistry.

[35]  A. Fairlamb,et al.  The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins. , 2000, Journal of molecular biology.

[36]  A. Vagin,et al.  Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution. , 2000, Structure.

[37]  T. Hakoshima,et al.  Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[38]  H. J. Kim,et al.  Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin. , 1999, Diabetes research and clinical practice.

[39]  S. Rhee Redox signaling: hydrogen peroxide as intracellular messenger , 1999, Experimental & Molecular Medicine.

[40]  S. Ryu,et al.  Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution , 1998, Nature Structural Biology.

[41]  T. Finkel Oxygen radicals and signaling. , 1998, Current opinion in cell biology.

[42]  S. Rhee,et al.  Mammalian Peroxiredoxin Isoforms Can Reduce Hydrogen Peroxide Generated in Response to Growth Factors and Tumor Necrosis Factor-α* , 1998, The Journal of Biological Chemistry.

[43]  K. Jeang,et al.  Regulatory Role for a Novel Human Thioredoxin Peroxidase in NF-κB Activation* , 1997, The Journal of Biological Chemistry.

[44]  L. Obeid,et al.  Thioredoxin Peroxidase Is a Novel Inhibitor of Apoptosis with a Mechanism Distinct from That of Bcl-2* , 1997, The Journal of Biological Chemistry.

[45]  S. Rhee,et al.  Thioredoxin-dependent peroxide reductase from yeast. , 1994, The Journal of biological chemistry.

[46]  S. Rhee,et al.  Dimerization of thiol-specific antioxidant and the essential role of cysteine 47. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[47]  G. Church,et al.  Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[48]  J. Dixon,et al.  Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate. , 1991, The Journal of biological chemistry.