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Volumn 7, Issue 5-6, 2005, Pages 768-777

Peroxiredoxins, oxidative stress, and cell proliferation

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; MYC PROTEIN; PEROXIREDOXIN; REACTIVE OXYGEN METABOLITE; STRESS ACTIVATED PROTEIN KINASE; THIOREDOXIN PEROXIDASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 17644423479     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2005.7.768     Document Type: Review
Times cited : (266)

References (84)
  • 2
    • 0346056899 scopus 로고    scopus 로고
    • Overexpression of human peroxiredoxin 5 in subcellular compartments of Chinese hamster ovary cells: Effects on cytotoxicity and DNA damage caused by peroxides
    • Banmeyer I, Marchand C, Verhaeghe C, Vucic B, Rees JF, and Knoops B. Overexpression of human peroxiredoxin 5 in subcellular compartments of Chinese hamster ovary cells: effects on cytotoxicity and DNA damage caused by peroxides. Free Radic Biol Med 36: 65-77, 2004.
    • (2004) Free Radic Biol Med , vol.36 , pp. 65-77
    • Banmeyer, I.1    Marchand, C.2    Verhaeghe, C.3    Vucic, B.4    Rees, J.F.5    Knoops, B.6
  • 3
    • 0036595970 scopus 로고    scopus 로고
    • Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells
    • Bast A, Wolf G, Oberbaumer I, and Walther R. Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells. Diabetologia 45: 867-876, 2002.
    • (2002) Diabetologia , vol.45 , pp. 867-876
    • Bast, A.1    Wolf, G.2    Oberbaumer, I.3    Walther, R.4
  • 4
    • 0027938689 scopus 로고
    • Oxy-radicals and cancer
    • Cerutti PA. Oxy-radicals and cancer. Lancet 344: 862-863, 1994.
    • (1994) Lancet , vol.344 , pp. 862-863
    • Cerutti, P.A.1
  • 5
    • 0027323871 scopus 로고
    • Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae
    • Chae HZ, Kim IH, Kim K, and Rhee SG. Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae. J Biol Chem 268: 16815-16821, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 16815-16821
    • Chae, H.Z.1    Kim, I.H.2    Kim, K.3    Rhee, S.G.4
  • 6
    • 0028226006 scopus 로고
    • 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 HZ, Robison K, Poole LB, Church G, Storz G, and Rhee SG. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc Natl Acad Sci USA 91: 7017-7021, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 7
    • 0028229670 scopus 로고
    • Dimerization of thiol-specific antioxidant and the essential role of cysteine 47
    • Chae HZ, Uhm TB, and Rhee SG. Dimerization of thiol-specific antioxidant and the essential role of cysteine 47. Proc Natl Acad Sci USA 91: 7022-7026, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7022-7026
    • Chae, H.Z.1    Uhm, T.B.2    Rhee, S.G.3
  • 8
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B, Sies H, and Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 59: 527-605, 1979.
    • (1979) Physiol Rev , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 10
    • 0037067763 scopus 로고    scopus 로고
    • Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation
    • Chang TS, Jeong W, Choi SY, Yu S, Kang SW, and Rhee SG. Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation. J Biol Chem 277: 25370-25376, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 25370-25376
    • Chang, T.S.1    Jeong, W.2    Choi, S.Y.3    Yu, S.4    Kang, S.W.5    Rhee, S.G.6
  • 11
    • 0037204948 scopus 로고    scopus 로고
    • TNF-R1 signaling: A beautiful pathway
    • Chen G and Goeddel DV. TNF-R1 signaling: a beautiful pathway. Science 296: 1634-1635, 2002.
    • (2002) Science , vol.296 , pp. 1634-1635
    • Chen, G.1    Goeddel, D.V.2
  • 12
    • 0043175418 scopus 로고    scopus 로고
    • Roles of reactive oxygen species, NF-kappaB, and peroxiredoxins in glycochenodeoxycholic acid-induced rat hepatocytes death
    • Chu SH, Lee-Kang J, Lee KH, and Lee K. Roles of reactive oxygen species, NF-kappaB, and peroxiredoxins in glycochenodeoxycholic acid-induced rat hepatocytes death. Pharmacology 69: 12-19, 2003.
    • (2003) Pharmacology , vol.69 , pp. 12-19
    • Chu, S.H.1    Lee-Kang, J.2    Lee, K.H.3    Lee, K.4
  • 13
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • Finkel T. Oxygen radicals and signaling. Curr Opin Cell Biol 10: 248-253, 1998.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 248-253
    • Finkel, T.1
  • 14
    • 0034817898 scopus 로고    scopus 로고
    • Augmented expression of peroxiredoxin VI in rat lung and kidney after birth implies an antioxidative role
    • Fujii T, Fujii J, and Taniguchi N. Augmented expression of peroxiredoxin VI in rat lung and kidney after birth implies an antioxidative role. Eur J Biochem 268: 218-225, 2001.
    • (2001) Eur J Biochem , vol.268 , pp. 218-225
    • Fujii, T.1    Fujii, J.2    Taniguchi, N.3
  • 15
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • Gopalakrishna R and Jaken S. Protein kinase C signaling and oxidative stress. Free Radic Biol Med 28: 1349-1361, 2000.
    • (2000) Free Radic Biol Med , vol.28 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 18
    • 0242580940 scopus 로고    scopus 로고
    • Phorbol ester-dependent activation of peroxiredoxin I gene expression via a protein kinase C, Ras, p38 mitogen-activated protein kinase signaling pathway
    • Hess A, Wijayanti N, Neuschäfer-Rube AP, Katz N, Kietzmann T, and Immenschuh S. Phorbol ester-dependent activation of peroxiredoxin I gene expression via a protein kinase C, Ras, p38 mitogen-activated protein kinase signaling pathway. J Biol Chem 278: 45419-45434, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 45419-45434
    • Hess, A.1    Wijayanti, N.2    Neuschäfer-Rube, A.P.3    Katz, N.4    Kietzmann, T.5    Immenschuh, S.6
  • 19
    • 0033607229 scopus 로고    scopus 로고
    • Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product
    • Hirotsu S, Abe Y, Okada K, Nagahara N, Hori H, Nishino T, and Hakoshima T. Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product. Proc Natl Acad Sci USA 96: 12333-12338, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12333-12338
    • Hirotsu, S.1    Abe, Y.2    Okada, K.3    Nagahara, N.4    Hori, H.5    Nishino, T.6    Hakoshima, T.7
  • 21
    • 0023886170 scopus 로고
    • DNA damage and oxygen radical toxicity
    • Imlay JA and Linn S. DNA damage and oxygen radical toxicity. Science 240: 1302-1309, 1988.
    • (1988) Science , vol.240 , pp. 1302-1309
    • Imlay, J.A.1    Linn, S.2
  • 22
    • 0028818098 scopus 로고
    • Expression of the mRNA of heme-binding protein 23 is coordinated with that of heme oxygenase-1 by heme and heavy metals in primary rat hepatocytes and hepatoma cells
    • Immenschuh S, Iwahara S-I, Satoh H, Nell C, Katz N, and Muller-Eberhard U. Expression of the mRNA of heme-binding protein 23 is coordinated with that of heme oxygenase-1 by heme and heavy metals in primary rat hepatocytes and hepatoma cells. Biochemistry 34: 13407-13411, 1995.
    • (1995) Biochemistry , vol.34 , pp. 13407-13411
    • Immenschuh, S.1    Iwahara, S.-I.2    Satoh, H.3    Nell, C.4    Katz, N.5    Muller-Eberhard, U.6
  • 23
    • 0032999307 scopus 로고    scopus 로고
    • Up-regulation of heme-binding protein 23 (HBP23) gene expression by lipopolysaccharide is mediated via a nitric oxide-dependent signaling pathway in rat Kupffer cells
    • Immenschuh S, Stritzke J, Iwahara S-I, and Ramadori G. Up-regulation of heme-binding protein 23 (HBP23) gene expression by lipopolysaccharide is mediated via a nitric oxide-dependent signaling pathway in rat Kupffer cells. Hepatology 30: 118-127, 1999.
    • (1999) Hepatology , vol.30 , pp. 118-127
    • Immenschuh, S.1    Stritzke, J.2    Iwahara, S.-I.3    Ramadori, G.4
  • 24
    • 0344862115 scopus 로고    scopus 로고
    • Differential cellular and subcellular localization of heme-binding protein 23/peroxiredoxin I and heme oxygenase-1 in rat liver
    • Immenschuh S, Baumgart-Vogt E, Tan M, Iwahara S, Ramadori G, and Fahimi HD. Differential cellular and subcellular localization of heme-binding protein 23/peroxiredoxin I and heme oxygenase-1 in rat liver. J Histochem Cytochem 51: 1621-1631, 2003.
    • (2003) J Histochem Cytochem , vol.51 , pp. 1621-1631
    • Immenschuh, S.1    Baumgart-Vogt, E.2    Tan, M.3    Iwahara, S.4    Ramadori, G.5    Fahimi, H.D.6
  • 27
    • 0028809758 scopus 로고
    • Inhibition of the thiol-specific antioxidant activity of rat liver MSP23 protein by hemin
    • Ishii T, Kawane T, Taketani S, and Bannai S. Inhibition of the thiol-specific antioxidant activity of rat liver MSP23 protein by hemin. Biochem Biophys Res Commun 216: 970-975, 1995.
    • (1995) Biochem Biophys Res Commun , vol.216 , pp. 970-975
    • Ishii, T.1    Kawane, T.2    Taketani, S.3    Bannai, S.4
  • 29
    • 0034717329 scopus 로고    scopus 로고
    • Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages
    • Ishii T, Itoh K, Takahashi S, Sato H, Yanagawa T, Katoh Y, Bannai S, and Yamamoto M. Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages. J Biol Chem 275: 16023-16029, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 16023-16029
    • Ishii, T.1    Itoh, K.2    Takahashi, S.3    Sato, H.4    Yanagawa, T.5    Katoh, Y.6    Bannai, S.7    Yamamoto, M.8
  • 30
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant response elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K, Wakabayashi N, Katoh Y, Ishii T, Igarashi K, Engel JD, and Yamamoto M. Keap1 represses nuclear activation of antioxidant response elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev 13: 76-86, 1999.
    • (1999) Genes Dev , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 32
    • 1842295744 scopus 로고    scopus 로고
    • Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
    • Jin DY, Chae HZ, Rhee SG, and Jeang KT. Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation. J Biol Chem 272: 30952-30961, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 30952-30961
    • Jin, D.Y.1    Chae, H.Z.2    Rhee, S.G.3    Jeang, K.T.4
  • 33
    • 0141746553 scopus 로고    scopus 로고
    • Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha
    • Kang SW, Chae HZ, Seo MS, Kim K, Baines IC, and Rhee SG. Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha. J Biol Chem 273: 6297-6302, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 6297-6302
    • Kang, S.W.1    Chae, H.Z.2    Seo, M.S.3    Kim, K.4    Baines, I.C.5    Rhee, S.G.6
  • 34
    • 1642576090 scopus 로고    scopus 로고
    • Cytosolic peroxiredoxin attenuates the activation of JNK and p38 but potentiates that of ERK in HeLa cells stimulated with tumor necrosis factor-α
    • Kang SW, Chang TS, Lee TH, Kim ES, Yu DY, and Rhee SG. Cytosolic peroxiredoxin attenuates the activation of JNK and p38 but potentiates that of ERK in HeLa cells stimulated with tumor necrosis factor-α. J Biol Chem 279: 2535-2543, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 2535-2543
    • Kang, S.W.1    Chang, T.S.2    Lee, T.H.3    Kim, E.S.4    Yu, D.Y.5    Rhee, S.G.6
  • 35
    • 0034674703 scopus 로고    scopus 로고
    • Role of peroxiredoxins in regulating intracellular hydrogen peroxide and hydrogen peroxide-induced apoptosis in thyroid cells
    • Kim H, Lee TH, Park ES, Suh JM, Park SJ, Chung HK, Kwon OY, Kim YK, Ro HK, and Shong M. Role of peroxiredoxins in regulating intracellular hydrogen peroxide and hydrogen peroxide-induced apoptosis in thyroid cells. J Biol Chem 275: 18266-18270, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 18266-18270
    • Kim, H.1    Lee, T.H.2    Park, E.S.3    Suh, J.M.4    Park, S.J.5    Chung, H.K.6    Kwon, O.Y.7    Kim, Y.K.8    Ro, H.K.9    Shong, M.10
  • 40
    • 0034518248 scopus 로고    scopus 로고
    • Peroxiredoxin is ubiquitously expressed in rat skin: Isotype-specific expression in the epidermis and hair follicle
    • Lee SC, Chae HZ, Lee JE, Kwon BD, Lee JB, Won YH, Ahn KY, and Kim YP. Peroxiredoxin is ubiquitously expressed in rat skin: isotype-specific expression in the epidermis and hair follicle. J Invest Dermatol 115: 1108-1114, 2000.
    • (2000) J Invest Dermatol , vol.115 , pp. 1108-1114
    • Lee, S.C.1    Chae, H.Z.2    Lee, J.E.3    Kwon, B.D.4    Lee, J.B.5    Won, Y.H.6    Ahn, K.Y.7    Kim, Y.P.8
  • 41
    • 0035839494 scopus 로고    scopus 로고
    • Cyclophilin A binds to peroxiredoxins and activates its peroxidase activity
    • Lee SP, Hwang YS, Kim YJ, Kwon KS, Kim HJ, Kim K, and Chae HZ. Cyclophilin A binds to peroxiredoxins and activates its peroxidase activity. J Biol Chem 276: 29826-29832, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 29826-29832
    • Lee, S.P.1    Hwang, Y.S.2    Kim, Y.J.3    Kwon, K.S.4    Kim, H.J.5    Kim, K.6    Chae, H.Z.7
  • 42
    • 0032739625 scopus 로고    scopus 로고
    • Characterization of mouse peroxiredoxin I genomic DNA and its expression
    • Lee TH, Yu SL, Kim SU, Lee KK, Rhee SG, and Yu DY. Characterization of mouse peroxiredoxin I genomic DNA and its expression. Gene 239: 243-250, 1999.
    • (1999) Gene , vol.239 , pp. 243-250
    • Lee, T.H.1    Yu, S.L.2    Kim, S.U.3    Lee, K.K.4    Rhee, S.G.5    Yu, D.Y.6
  • 44
    • 0037023713 scopus 로고    scopus 로고
    • Pathways of induction of peroxiredoxin I expression in osteoblasts: Roles of p38 mitogen-activated protein kinase and protein kinase C
    • Li B, Ishii T, Tan CP, Soh JW, and Goff SP. Pathways of induction of peroxiredoxin I expression in osteoblasts: roles of p38 mitogen-activated protein kinase and protein kinase C. J Biol Chem 277: 12418-12422, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 12418-12422
    • Li, B.1    Ishii, T.2    Tan, C.P.3    Soh, J.W.4    Goff, S.P.5
  • 45
    • 0031709365 scopus 로고    scopus 로고
    • Modulation of antioxidant enzymes, reactive oxygen species, and glutathione levels in manganese superoxide dismutase-overexpressing NIH/3T3 fibroblasts during the cell cycle
    • Li N and Oberley TD. Modulation of antioxidant enzymes, reactive oxygen species, and glutathione levels in manganese superoxide dismutase-overexpressing NIH/3T3 fibroblasts during the cell cycle. J Cell Physiol 177: 148-160, 1998.
    • (1998) J Cell Physiol , vol.177 , pp. 148-160
    • Li, N.1    Oberley, T.D.2
  • 46
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • Maines MD. The heme oxygenase system: a regulator of second messenger gases. Annu Rev Pharmacol Toxicol 37: 517-554, 1997.
    • (1997) Annu Rev Pharmacol Toxicol , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 47
    • 0034737541 scopus 로고    scopus 로고
    • Peroxiredoxin I (macrophage 23 kDa stress protein) is highly and widely expressed in the rat nervous system
    • Mizusawa H, Ishii T, and Bannai S. Peroxiredoxin I (macrophage 23 kDa stress protein) is highly and widely expressed in the rat nervous system. Neurosci Lett 283: 57-60, 2000.
    • (2000) Neurosci Lett , vol.283 , pp. 57-60
    • Mizusawa, H.1    Ishii, T.2    Bannai, S.3
  • 49
    • 0037044804 scopus 로고    scopus 로고
    • Pag, a putative tumor suppressor, interacts with the Myc box II domain of c-Myc and selectively alters its biological function and target gene expression
    • Mu ZM, Yin XY, and Prochownik EV. Pag, a putative tumor suppressor, interacts with the Myc box II domain of c-Myc and selectively alters its biological function and target gene expression. J Biol Chem 277: 43175-43184, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 43175-43184
    • Mu, Z.M.1    Yin, X.Y.2    Prochownik, E.V.3
  • 50
    • 0034693445 scopus 로고    scopus 로고
    • Co-induction of heme oxygenase-1 and peroxiredoxin I in astrocytes and microglia around hemorrhagic region in the rat brain
    • Nakaso K, Kitayama M, Mizuta E, Fukuda H, Ishii T, Nakashima K, and Yamada K. Co-induction of heme oxygenase-1 and peroxiredoxin I in astrocytes and microglia around hemorrhagic region in the rat brain. Neurosci Lett 293: 49-52, 2000.
    • (2000) Neurosci Lett , vol.293 , pp. 49-52
    • Nakaso, K.1    Kitayama, M.2    Mizuta, E.3    Fukuda, H.4    Ishii, T.5    Nakashima, K.6    Yamada, K.7
  • 52
    • 0037763721 scopus 로고    scopus 로고
    • Regulatory mechanisms controlling gene expression mediated by the antioxidant response element
    • Nguyen T, Sherratt PJ, and Pickett CB. Regulatory mechanisms controlling gene expression mediated by the antioxidant response element. Annu Rev Pharmacol Toxicol 43: 233-260, 2003.
    • (2003) Annu Rev Pharmacol Toxicol , vol.43 , pp. 233-260
    • Nguyen, T.1    Sherratt, P.J.2    Pickett, C.B.3
  • 53
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 258: 607-614, 1992.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 55
    • 0036174453 scopus 로고    scopus 로고
    • Oxidative damage and cancer
    • Oberley TD. Oxidative damage and cancer. Am J Pathol 160: 403-408, 2002.
    • (2002) Am J Pathol , vol.160 , pp. 403-408
    • Oberley, T.D.1
  • 58
    • 0027247446 scopus 로고
    • A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins
    • Prosperi MT, Ferbus D, Karczinski I, and Goubin G. A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins. J Biol Chem 268: 11050-11056, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 11050-11056
    • Prosperi, M.T.1    Ferbus, D.2    Karczinski, I.3    Goubin, G.4
  • 59
    • 0345647078 scopus 로고    scopus 로고
    • The pag gene product, a physiological inhibitor of c-abl tyrosine kinase, is overexpressed in cells entering S phase and by contact with agents inducing oxidative stress
    • Prosperi MT, Ferbus D, Rouillard D, and Goubin G. The pag gene product, a physiological inhibitor of c-abl tyrosine kinase, is overexpressed in cells entering S phase and by contact with agents inducing oxidative stress. FEBS Lett 423: 39-44, 1998.
    • (1998) FEBS Lett , vol.423 , pp. 39-44
    • Prosperi, M.T.1    Ferbus, D.2    Rouillard, D.3    Goubin, G.4
  • 60
    • 0037065722 scopus 로고    scopus 로고
    • An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum
    • Reynolds CM, Meyer J, and Poole LB. An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum. Biochemistry 41: 1990-2001, 2002.
    • (2002) Biochemistry , vol.41 , pp. 1990-2001
    • Reynolds, C.M.1    Meyer, J.2    Poole, L.B.3
  • 63
    • 0034873185 scopus 로고    scopus 로고
    • Reactive oxygen species as intracellular messengers during cell growth and differentiation
    • Sauer H, Wartenberg M, and Hescheler J. Reactive oxygen species as intracellular messengers during cell growth and differentiation. Cell Physiol Biochem 11: 173-186, 2001.
    • (2001) Cell Physiol Biochem , vol.11 , pp. 173-186
    • Sauer, H.1    Wartenberg, M.2    Hescheler, J.3
  • 65
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappaB transcription factor and HIV-1
    • Schreck R, Rieber P, and Baeuerle PA. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappaB transcription factor and HIV-1. EMBO J 10: 2247-2258, 1991.
    • (1991) EMBO J , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 66
    • 0001015125 scopus 로고    scopus 로고
    • Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
    • Seo MS, Kang SW, Kim K, Baines IC, Lee TH, and Rhee SG. Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. J Biol Chem 275: 20346-20354, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 20346-20354
    • Seo, M.S.1    Kang, S.W.2    Kim, K.3    Baines, I.C.4    Lee, T.H.5    Rhee, S.G.6
  • 68
    • 0027530060 scopus 로고
    • Identification of a natural killer enhancing factor (NKEF) from human erythroid cells
    • Shau H, Gupta RK, and Golub SH. Identification of a natural killer enhancing factor (NKEF) from human erythroid cells. Cell Immunol 147: 1-11, 1993.
    • (1993) Cell Immunol , vol.147 , pp. 1-11
    • Shau, H.1    Gupta, R.K.2    Golub, S.H.3
  • 69
    • 0028283906 scopus 로고
    • Cloning and sequence of candidate human natural killer-enhancing factor genes
    • Shau H, Butterfield LH, Chiu R, and Kim A. Cloning and sequence of candidate human natural killer-enhancing factor genes. Immunogenetics 40: 129-134, 1994.
    • (1994) Immunogenetics , vol.40 , pp. 129-134
    • Shau, H.1    Butterfield, L.H.2    Chiu, R.3    Kim, A.4
  • 70
    • 0032575488 scopus 로고    scopus 로고
    • Thioredoxin peroxidase (natural killer enhancing factor) regulation of activator protein-1 function in endothelial cells
    • Shau H, Huang AC, Faris M, Nazarian R, de Vellis J, and Chen W. Thioredoxin peroxidase (natural killer enhancing factor) regulation of activator protein-1 function in endothelial cells. Biochem Biophys Res Commun 249: 683-686, 1998.
    • (1998) Biochem Biophys Res Commun , vol.249 , pp. 683-686
    • Shau, H.1    Huang, A.C.2    Faris, M.3    Nazarian, R.4    De Vellis, J.5    Chen, W.6
  • 71
    • 0034916788 scopus 로고    scopus 로고
    • Organization of the NKEF gene and its expression in the common carp (Cyprinus carpio)
    • Shin DH, Fujiki K, Nakao M, and Yano T. Organization of the NKEF gene and its expression in the common carp (Cyprinus carpio). Dev Camp Immunol 25: 597-606, 2001.
    • (2001) Dev Camp Immunol , vol.25 , pp. 597-606
    • Shin, D.H.1    Fujiki, K.2    Nakao, M.3    Yano, T.4
  • 72
    • 0030477745 scopus 로고    scopus 로고
    • Mammalian peroxisomes: Metabolism of oxygen and reactive oxygen species
    • Singh I. Mammalian peroxisomes: metabolism of oxygen and reactive oxygen species. Ann N Y Acad Sci 804: 612-627, 1996.
    • (1996) Ann N Y Acad Sci , vol.804 , pp. 612-627
    • Singh, I.1
  • 73
    • 0029016985 scopus 로고
    • Induction of the antioxidant stress proteins heme oxygenase-1 and MSP23 by stress agents and oxidised LDL in cultured vascular smooth muscle cells
    • Siow RCM, Ishii T, Sato H, Taketani S, Leake DS, Sweiry JH, Pearson JD, Bannai S, and Mann GE. Induction of the antioxidant stress proteins heme oxygenase-1 and MSP23 by stress agents and oxidised LDL in cultured vascular smooth muscle cells. FEBS Lett 368: 239-242, 1995.
    • (1995) FEBS Lett , vol.368 , pp. 239-242
    • Siow, R.C.M.1    Ishii, T.2    Sato, H.3    Taketani, S.4    Leake, D.S.5    Sweiry, J.H.6    Pearson, J.D.7    Bannai, S.8    Mann, G.E.9
  • 74
    • 0037273615 scopus 로고    scopus 로고
    • Identification of multiple transcripts for antioxidant protein 2 (Aop2): Differential regulation by oxidative stress and growth factors
    • Sparling NE and Phelan SA. Identification of multiple transcripts for antioxidant protein 2 (Aop2): differential regulation by oxidative stress and growth factors. Redox Rep 8: 87-94, 2003.
    • (2003) Redox Rep , vol.8 , pp. 87-94
    • Sparling, N.E.1    Phelan, S.A.2
  • 75
    • 0344844531 scopus 로고    scopus 로고
    • Androgenic regulation of oxidative stress in the rat prostate. Involvement of NAD(P)H oxidases and antioxidant defense machinery during prostatic involution and regrowth
    • Tam NNC, Gao Y, Leung Y-K, and Ho S-M. Androgenic regulation of oxidative stress in the rat prostate. Involvement of NAD(P)H oxidases and antioxidant defense machinery during prostatic involution and regrowth. Am J Pathol 163: 2513-2522, 2003.
    • (2003) Am J Pathol , vol.163 , pp. 2513-2522
    • Tam, N.N.C.1    Gao, Y.2    Leung, Y.-K.3    Ho, S.-M.4
  • 78
    • 0025083101 scopus 로고
    • Inflammation and cancer: Role of phagocyte-generated oxidants in carcinogenesis
    • Weitzman SA and Gordon LI. Inflammation and cancer: role of phagocyte-generated oxidants in carcinogenesis. Blood 76: 655-663, 1990.
    • (1990) Blood , vol.76 , pp. 655-663
    • Weitzman, S.A.1    Gordon, L.I.2
  • 79
    • 0030803669 scopus 로고    scopus 로고
    • The pag gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity
    • Wen S-T and Van Etten RA. The pag gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity. Genes Dev 11: 2456-2467, 1997.
    • (1997) Genes Dev , vol.11 , pp. 2456-2467
    • Wen, S.-T.1    Van Etten, R.A.2
  • 80
    • 0242668688 scopus 로고    scopus 로고
    • Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
    • Woo HA, Chae HZ, Hwang SC, Yang KS, Kang SW, Kim K, and Rhee SG. Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. Science 300: 653-656, 2003.
    • (2003) Science , vol.300 , pp. 653-656
    • Woo, H.A.1    Chae, H.Z.2    Hwang, S.C.3    Yang, K.S.4    Kang, S.W.5    Kim, K.6    Rhee, S.G.7
  • 81
    • 0037197672 scopus 로고    scopus 로고
    • Dimers to doughnuts: Redox-sensitive oligomerization of 2-cysteine peroxiredoxins
    • Wood ZA, Poole LB, Hantgan RR, and Karplus PA. Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins. Biochemistry 41: 5493-5504, 2002.
    • (2002) Biochemistry , vol.41 , pp. 5493-5504
    • Wood, Z.A.1    Poole, L.B.2    Hantgan, R.R.3    Karplus, P.A.4
  • 82
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Wood ZA, Poole LB, and Karplus PA. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300: 650-653, 2003.
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 84
    • 0030692005 scopus 로고    scopus 로고
    • Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2
    • Zhang P, Liu B, Kang SW, Seo MS, Rhee SG, and Obeid LM. Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2. J Biol Chem 272: 30615-30618, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 30615-30618
    • Zhang, P.1    Liu, B.2    Kang, S.W.3    Seo, M.S.4    Rhee, S.G.5    Obeid, L.M.6


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