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Human peroxiredoxin 5 is a peroxynitrite reductase.

Bibliographic reference Dubuisson, Marlène ; Vander Stricht, Delphine ; Clippe, André ; Etienne, Florence ; Nauser, Thomas ; et. al. Human peroxiredoxin 5 is a peroxynitrite reductase.. In: FEBS letters, Vol. 571, no. 1-3, p. 161-5 (2004)
Permanent URL http://hdl.handle.net/2078.1/9904
  1. Nauser T., Koppenol W. H., The Rate Constant of the Reaction of Superoxide with Nitrogen Monoxide:  Approaching the Diffusion Limit, 10.1021/jp025518z
  2. Radi Rafael, Cassina Adriana, Hodara Roberto, Quijano Celia, Castro Laura, Peroxynitrite reactions and formation in mitochondria, 10.1016/s0891-5849(02)01111-5
  3. Wiseman, Biochem. J., 313, 17 (1996)
  4. Heales Simon J.R., Bolaños Juan P., Stewart Victoria C., Brookes Paul S., Land John M., Clark John B., Nitric oxide, mitochondria and neurological disease, 10.1016/s0005-2728(98)00168-6
  5. Beal M.Flint, Oxidatively modified proteins in aging and disease1,2 1Guest Editor: Earl Stadtman 2This article is part of a series of reviews on “Oxidatively Modified Proteins in Aging and Disease.” The full list of papers may be found on the homepage of the journal., 10.1016/s0891-5849(02)00780-3
  6. Chae H. Z., Robison K., Poole L. B., Church G., Storz G., Rhee S. G., Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes., 10.1073/pnas.91.15.7017
  7. Rhee Sue Goo, Kang Sang Won, Chang Tong-Shin, Jeong Woojin, Kim Kanghwa, Peroxiredoxin, a Novel Family of Peroxidases, 10.1080/15216540252774748
  8. Fujii Junichi, Ikeda Yoshitaka, Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein, 10.1179/135100002125000352
  9. Hofmann, Biol. Chem., 383, 347 (2002)
  10. Wood Zachary A, Schröder Ewald, Robin Harris J, Poole Leslie B, Structure, mechanism and regulation of peroxiredoxins, 10.1016/s0968-0004(02)00003-8
  11. Henkle-Dührsen K, Antioxidant enzyme families in parasitic nematodes, 10.1016/s0166-6851(01)00252-3
  12. Leyens Gregory, Donnay Isabelle, Knoops Bernard, Cloning of bovine peroxiredoxins—gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins, 10.1016/s1096-4959(03)00290-2
  13. Knoops Bernard, Clippe André, Bogard Cédric, Arsalane Karim, Wattiez Ruddy, Hermans Cédric, Duconseille Elee, Falmagne Paul, Bernard Alfred, Cloning and Characterization of AOEB166, a Novel Mammalian Antioxidant Enzyme of the Peroxiredoxin Family, 10.1074/jbc.274.43.30451
  14. Seo Min Seok, Kang Sang Won, Kim Kanghwa, Baines Ivan C., Lee Tae Hoon, Rhee Sue Goo, Identification of a New Type of Mammalian Peroxiredoxin That Forms an Intramolecular Disulfide as a Reaction Intermediate, 10.1074/jbc.m001943200
  15. Declercq Jean-Paul, Evrard Christine, Clippe André, Stricht Delphine Vander, Bernard Alfred, Knoops Bernard, Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution, 10.1006/jmbi.2001.4853
  16. Banmeyer Ingrid, Marchand Cécile, Verhaeghe Catherine, Vucic Bénédicte, Rees Jean-François, Knoops Bernard, Overexpression of human peroxiredoxin 5 in subcellular compartments of chinese hamster ovary cells: effects on cytotoxicity and DNA damage caused by peroxides, 10.1016/j.freeradbiomed.2003.10.019
  17. Nathan Carl, Bryk Ruslana, Griffin Patrick, 10.1038/35025109
  18. Damdimopoulos A. E., Human Mitochondrial Thioredoxin. INVOLVEMENT IN MITOCHONDRIAL MEMBRANE POTENTIAL AND CELL DEATH, 10.1074/jbc.m203036200
  19. Glebska Jolanta, Koppenol Willem H, Peroxynitrite-mediated oxidation of dichlorodihydrofluorescein and dihydrorhodamine, 10.1016/s0891-5849(03)00389-7
  20. Koppenol Willem H., Kissner R., Beckman Joseph S., [27] Syntheses of peroxynitrite: To go with the flow or on solid grounds?, Methods in Enzymology (1996) ISBN:9780121821708 p.296-302, 10.1016/s0076-6879(96)69030-2
  21. Chae Ho Zoon, Kang Sang Won, Rhee Sue Goo, Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin, Methods in Enzymology (1999) ISBN:9780121822019 p.219-226, 10.1016/s0076-6879(99)00128-7
  22. Kissner Reinhard, Koppenol Willem H., Product Distribution of Peroxynitrite Decay as a Function of pH, Temperature, and Concentration, 10.1021/ja010497s
  23. Goldstein Sara, Czapski Gidon, The reaction of NO· with O2·− and HO2·−: A pulse radiolysis study, 10.1016/0891-5849(95)00034-u
  24. Peshenko Igor V, Shichi Hitoshi, Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin to the cysteine sulfenic acid form by peroxide and peroxynitrite, 10.1016/s0891-5849(01)00579-2
  25. Ferrer-Sueta Gerardo, Batinić-Haberle Ines, Spasojević Ivan, Fridovich Irwin, Radi Rafael, Catalytic Scavenging of Peroxynitrite by Isomeric Mn(III)N-Methylpyridylporphyrins in the Presence of Reductants, 10.1021/tx980245d
  26. Hiroshi Masumoto, Kissner Reinhard, Koppenol Willem H., Sies Helmut, Kinetic study of the reaction of ebselen with peroxynitrite, 10.1016/s0014-5793(96)01237-9
  27. Briviba Karlis, Kissner Reinhard, Koppenol Willem H., Sies Helmut, Kinetic Study of the Reaction of Glutathione Peroxidase with Peroxynitrite, 10.1021/tx980086y
  28. Lymar Sergei V., Hurst James K., Carbon Dioxide:  Physiological Catalyst for Peroxynitrite-Mediated Cellular Damage or Cellular Protectant?, 10.1021/tx960046z
  29. Peng Ying, Yang Pai-Hao, Guo Yan, Ng Samuel S. M., Liu Jie, Fung P. C. W., Tay David, Ge Jian, He Ming-Liang, Kung Hsiang-fu, Lin Marie C., Catalase and Peroxiredoxin 5 Protect Xenopus Embryos against Alcohol-Induced Ocular Anomalies, 10.1167/iovs.03-0550
  30. Hattori Fumiyuki, Murayama Norihito, Noshita Takafumi, Oikawa Shinzo, Mitochondrial peroxiredoxin-3 protects hippocampal neurons from excitotoxic injury in vivo : Neuroprotective role of Prx-3, 10.1046/j.1471-4159.2003.01918.x
  31. Yamakura Fumiyuki, Taka Hikari, Fujimura Tsutomu, Murayama Kimie, Inactivation of Human Manganese-superoxide Dismutase by Peroxynitrite Is Caused by Exclusive Nitration of Tyrosine 34 to 3-Nitrotyrosine, 10.1074/jbc.273.23.14085
  32. Asahi Michio, Fujii Junichi, Suzuki Keiichiro, Seo Han Geuk, Kuzuya Tsunehiko, Hori Masatsugu, Tada Michihiko, Fujii Shigeru, Taniguchi Naoyuki, Inactivation of Glutathione Peroxidase by Nitric Oxide : IMPLICATION FOR CYTOTOXICITY, 10.1074/jbc.270.36.21035
  33. Padmaja Sarojini, Squadrito Giuseppe L., Pryor William A., Inactivation of Glutathione Peroxidase by Peroxynitrite, 10.1006/abbi.1997.0407
  34. Sies Helmut, Arteel Gavin E, Interaction of peroxynitrite with selenoproteins and glutathione peroxidase mimics, 10.1016/s0891-5849(00)00253-7
  35. Wong Chi-Ming, Zhou Yuan, Ng Raymond W. M., Kung Hsiang-fu, Jin Dong-Yan, Cooperation of Yeast Peroxiredoxins Tsa1p and Tsa2p in the Cellular Defense against Oxidative and Nitrosative Stress, 10.1074/jbc.m106846200
  36. Chen Lei, Xie Qiao-wen, Nathan Carl, Alkyl Hydroperoxide Reductase Subunit C (AhpC) Protects Bacterial and Human Cells against Reactive Nitrogen Intermediates, 10.1016/s1097-2765(00)80079-9
  37. Comtois S. L., Role of the thioredoxin system and the thiol-peroxidases Tpx and Bcp in mediating resistance to oxidative and nitrosative stress in Helicobacter pylori, 10.1099/mic.0.25896-0
  38. Oberley Terry D, Verwiebe Eric, Zhong Weixiong, Kang Sang Won, Rhee Sue Goo, Localization of the thioredoxin system in normal rat kidney, 10.1016/s0891-5849(00)00486-x
  39. Thompson Julie D., Higgins Desmond G., Gibson Toby J., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, 10.1093/nar/22.22.4673
  40. Emanuelsson Olof, Nielsen Henrik, Brunak Søren, von Heijne Gunnar, Predicting Subcellular Localization of Proteins Based on their N-terminal Amino Acid Sequence, 10.1006/jmbi.2000.3903