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Volumn 59, Issue 7, 2005, Pages 374-379

Sulfiredoxin: A potential therapeutic agent?

Author keywords

Glutathione; Glutathionylation; GST; Oxidative stress; Reactive oxygen nitrogen species; Sulfiredoxin

Indexed keywords

ANTIOXIDANT; CYSTEINE; GLUTATHIONE TRANSFERASE; PEROXIREDOXIN; REACTIVE NITROGEN SPECIES; SULFENIC ACID DERIVATIVE; SULFINIC ACID DERIVATIVE; SULFIREDOXIN; SUPEROXIDE DISMUTASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 24044465140     PISSN: 07533322     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biopha.2005.07.003     Document Type: Article
Times cited : (61)

References (34)
  • 1
    • 0033105414 scopus 로고    scopus 로고
    • Regulation of JNK signaling by GSTp
    • V. Adler, and Z. Yin Regulation of JNK signaling by GSTp EMBO J. 18 5 1999 1321 1334
    • (1999) EMBO J. , vol.18 , Issue.5 , pp. 1321-1334
    • Adler, V.1    Yin, Z.2
  • 2
    • 0035917819 scopus 로고    scopus 로고
    • Changes in thiol content and expression of glutathione redox system genes in the hippocampus and cerebellum in Alzheimer's disease
    • M.Y. Aksenov, and W.R. Markesbery Changes in thiol content and expression of glutathione redox system genes in the hippocampus and cerebellum in Alzheimer's disease Neurosci. Lett. 302 2-3 2001 141 145
    • (2001) Neurosci. Lett. , vol.302 , Issue.2-3 , pp. 141-145
    • Aksenov, M.Y.1    Markesbery, W.R.2
  • 3
    • 0033580609 scopus 로고    scopus 로고
    • Regulation of PTP1B via glutathionylation of the active site cysteine 215
    • W.C. Barrett, and J.P. DeGnore Regulation of PTP1B via glutathionylation of the active site cysteine 215 Biochemistry 38 20 1999 6699 6705
    • (1999) Biochemistry , vol.38 , Issue.20 , pp. 6699-6705
    • Barrett, W.C.1    Degnore, J.P.2
  • 4
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
    • B. Biteau, and J. Labarre ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin Nature 425 6961 2003 980 984
    • (2003) Nature , vol.425 , Issue.6961 , pp. 980-984
    • Biteau, B.1    Labarre, J.2
  • 5
    • 20744438779 scopus 로고    scopus 로고
    • Oxidation of a eukaryotic 2-cys peroxiredoxin is a molecular switch controlling the transcriptional response to increasing levels of hydrogen peroxide
    • S.M. Bozonet, and V.J. Findlay Oxidation of a eukaryotic 2-cys peroxiredoxin is a molecular switch controlling the transcriptional response to increasing levels of hydrogen peroxide J. Biol. Chem. 280 24 2005 23319 23327
    • (2005) J. Biol. Chem. , vol.280 , Issue.24 , pp. 23319-23327
    • Bozonet, S.M.1    Findlay, V.J.2
  • 6
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • H.Z. Chae, and S.J. Chung Thioredoxin-dependent peroxide reductase from yeast J. Biol. Chem. 269 44 1994 27670 27678
    • (1994) J. Biol. Chem. , vol.269 , Issue.44 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2
  • 7
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • B. Chance, and H. Sies Hydroperoxide metabolism in mammalian organs Physiol. Rev. 59 3 1979 527 605
    • (1979) Physiol. Rev. , vol.59 , Issue.3 , pp. 527-605
    • Chance, B.1    Sies, H.2
  • 8
    • 10944237769 scopus 로고    scopus 로고
    • Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine
    • T.S. Chang, and W. Jeong Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine J. Biol. Chem. 279 49 2004 50994 51001
    • (2004) J. Biol. Chem. , vol.279 , Issue.49 , pp. 50994-51001
    • Chang, T.S.1    Jeong, W.2
  • 9
    • 0035918227 scopus 로고    scopus 로고
    • Glutathione S-transferase mu modulates the stress-activated signals by suppressing apoptosis signal-regulating kinase 1
    • S.G. Cho, and Y.H. Lee Glutathione S-transferase mu modulates the stress-activated signals by suppressing apoptosis signal-regulating kinase 1 J. Biol. Chem. 276 16 2001 12749 12755
    • (2001) J. Biol. Chem. , vol.276 , Issue.16 , pp. 12749-12755
    • Cho, S.G.1    Lee, Y.H.2
  • 10
    • 0031010596 scopus 로고    scopus 로고
    • Parkinson disease: A new link between monoamine oxidase and mitochondrial electron flow
    • G. Cohen, and R. Farooqui Parkinson disease: a new link between monoamine oxidase and mitochondrial electron flow Proc. Natl. Acad. Sci. USA 94 10 1997 4890 4894
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.10 , pp. 4890-4894
    • Cohen, G.1    Farooqui, R.2
  • 11
    • 0029004898 scopus 로고
    • Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis
    • J.F. Collard, and F. Cote Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis Nature 375 6526 1995 61 64
    • (1995) Nature , vol.375 , Issue.6526 , pp. 61-64
    • Collard, J.F.1    Cote, F.2
  • 12
    • 4344686072 scopus 로고    scopus 로고
    • Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain
    • J.V. Cross, and D.J. Templeton Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain Biochem. J. 381 Pt 3 2004 675 683
    • (2004) Biochem. J. , vol.381 , Issue.3 PART , pp. 675-683
    • Cross, J.V.1    Templeton, D.J.2
  • 13
    • 0030586798 scopus 로고    scopus 로고
    • Protein S-thiolation and regulation of microsomal glutathione transferase activity by the glutathione redox couple
    • A.L. Dafre, and H. Sies Protein S-thiolation and regulation of microsomal glutathione transferase activity by the glutathione redox couple Arch. Biochem. Biophys. 332 2 1996 288 294
    • (1996) Arch. Biochem. Biophys. , vol.332 , Issue.2 , pp. 288-294
    • Dafre, A.L.1    Sies, H.2
  • 14
    • 12444296480 scopus 로고    scopus 로고
    • Proteins as biomarkers of oxidative/nitrosative stress in diseases: The contribution of redox proteomics
    • I. Dalle-Donne, and A. Scaloni Proteins as biomarkers of oxidative/nitrosative stress in diseases: the contribution of redox proteomics Mass Spectrom. Rev. 24 1 2005 55 99
    • (2005) Mass Spectrom. Rev. , vol.24 , Issue.1 , pp. 55-99
    • Dalle-Donne, I.1    Scaloni, A.2
  • 15
    • 0036545912 scopus 로고    scopus 로고
    • The plasma redox state and ageing
    • W. Droge The plasma redox state and ageing Ageing Res. Rev. 1 2 2002 257 278
    • (2002) Ageing Res. Rev. , vol.1 , Issue.2 , pp. 257-278
    • Droge, W.1
  • 16
    • 18344390036 scopus 로고    scopus 로고
    • Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes
    • M. Fratelli, and H. Demol Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes Proc. Natl. Acad. Sci. USA 99 6 2002 3505 3510
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.6 , pp. 3505-3510
    • Fratelli, M.1    Demol, H.2
  • 17
    • 0029065402 scopus 로고
    • Thiol/disulfide exchange equilibria and disulfide bond stability
    • H.F. Gilbert Thiol/disulfide exchange equilibria and disulfide bond stability Methods Enzymol. 251 1995 8 28
    • (1995) Methods Enzymol. , vol.251 , pp. 8-28
    • Gilbert, H.F.1
  • 18
    • 14044272119 scopus 로고    scopus 로고
    • S-glutathionylation: From redox regulation of protein functions to human diseases
    • D. Giustarini, and R. Rossi S-glutathionylation: from redox regulation of protein functions to human diseases J. Cell. Mol. Med. 8 2 2004 201 212
    • (2004) J. Cell. Mol. Med. , vol.8 , Issue.2 , pp. 201-212
    • Giustarini, D.1    Rossi, R.2
  • 19
    • 0027238801 scopus 로고
    • Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase
    • S.A. Gravina, and J.J. Mieyal Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase Biochemistry 32 13 1993 3368 3376
    • (1993) Biochemistry , vol.32 , Issue.13 , pp. 3368-3376
    • Gravina, S.A.1    Mieyal, J.J.2
  • 20
    • 0033080394 scopus 로고    scopus 로고
    • S-nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitroso glutathione
    • Y. Ji, and T.P. Akerboom S-nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitroso glutathione Arch. Biochem. Biophys. 362 1 1999 67 78
    • (1999) Arch. Biochem. Biophys. , vol.362 , Issue.1 , pp. 67-78
    • Ji, Y.1    Akerboom, T.P.2
  • 21
    • 15444367716 scopus 로고    scopus 로고
    • Regulation of mitochondrial NADP+-dependent isocitrate dehydrogenase activity by glutathionylation
    • I.S. Kil, and J.W. Park Regulation of mitochondrial NADP+-dependent isocitrate dehydrogenase activity by glutathionylation J. Biol. Chem. 280 11 2005 10846 10854
    • (2005) J. Biol. Chem. , vol.280 , Issue.11 , pp. 10846-10854
    • Kil, I.S.1    Park, J.W.2
  • 22
    • 0032826055 scopus 로고    scopus 로고
    • Redox regulation of c-Jun DNA binding by reversible S-glutathiolation
    • P. Klatt, and E.P. Molina Redox regulation of c-Jun DNA binding by reversible S-glutathiolation FASEB J. 13 12 1999 1481 1490
    • (1999) FASEB J. , vol.13 , Issue.12 , pp. 1481-1490
    • Klatt, P.1    Molina, E.P.2
  • 23
    • 0034662178 scopus 로고    scopus 로고
    • Novel application of S-nitrosoglutathione-sepharose to identify proteins that are potential targets for S-nitrosoglutathione-induced mixed-disulphide formation
    • P. Klatt, and E. Pineda Molina Novel application of S-nitrosoglutathione- sepharose to identify proteins that are potential targets for S-nitrosoglutathione-induced mixed-disulphide formation Biochem. J. 349 Pt 2 2000 567 578
    • (2000) Biochem. J. , vol.349 , Issue.2 PART , pp. 567-578
    • Klatt, P.1    Pineda Molina, E.2
  • 24
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • J.M. McCord, and I. Fridovich Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein) J. Biol. Chem. 244 22 1969 6049 6055
    • (1969) J. Biol. Chem. , vol.244 , Issue.22 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 25
    • 0032863136 scopus 로고    scopus 로고
    • Molecular pathogenesis of Friedreich ataxia
    • M. Pandolfo Molecular pathogenesis of Friedreich ataxia Arch. Neurol. 56 10 1999 1201 1208
    • (1999) Arch. Neurol. , vol.56 , Issue.10 , pp. 1201-1208
    • Pandolfo, M.1
  • 26
    • 0035780208 scopus 로고    scopus 로고
    • Glutathione in blood of patients with Friedreich's ataxia
    • F. Piemonte, and A. Pastore Glutathione in blood of patients with Friedreich's ataxia Eur. J. Clin. Invest. 31 11 2001 1007 1011
    • (2001) Eur. J. Clin. Invest. , vol.31 , Issue.11 , pp. 1007-1011
    • Piemonte, F.1    Pastore, A.2
  • 27
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • M. Saitoh, and H. Nishitoh Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1 EMBO J. 17 9 1998 2596 2606
    • (1998) EMBO J. , vol.17 , Issue.9 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2
  • 28
    • 0026644192 scopus 로고
    • Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease
    • E. Sofic, and K.W. Lange Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease Neurosci. Lett. 142 2 1992 128 130
    • (1992) Neurosci. Lett. , vol.142 , Issue.2 , pp. 128-130
    • Sofic, E.1    Lange, K.W.2
  • 30
    • 0027504297 scopus 로고
    • Advances in our understanding of the mechanisms of the neurotoxicity of MPTP and related compounds
    • K.F. Tipton, and T.P. Singer Advances in our understanding of the mechanisms of the neurotoxicity of MPTP and related compounds J. Neurochem. 61 4 1993 1191 1206
    • (1993) J. Neurochem. , vol.61 , Issue.4 , pp. 1191-1206
    • Tipton, K.F.1    Singer, T.P.2
  • 32
    • 0024026479 scopus 로고
    • Co-ordinate control of synthesis of mitochondrial and non-mitochondrial hemoproteins: A binding site for the HAP1 (CYP1) protein in the UAS region of the yeast catalase T gene (CTT1)
    • H. Winkler, and G. Adam Co-ordinate control of synthesis of mitochondrial and non-mitochondrial hemoproteins: a binding site for the HAP1 (CYP1) protein in the UAS region of the yeast catalase T gene (CTT1) EMBO J. 7 6 1988 1799 1804
    • (1988) EMBO J. , vol.7 , Issue.6 , pp. 1799-1804
    • Winkler, H.1    Adam, G.2
  • 33
    • 13544272571 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins
    • H.A. Woo, and W. Jeong Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins J. Biol. Chem. 280 5 2005 3125 3128
    • (2005) J. Biol. Chem. , vol.280 , Issue.5 , pp. 3125-3128
    • Woo, H.A.1    Jeong, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.