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Volumn 527, Issue , 2013, Pages 41-63

Peroxiredoxins as preferential targets in H2O 2-induced signaling

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN PEROXIDE; PEROXIDASE; PEROXIREDOXIN; PROTEIN TYROSINE KINASE; THIOL;

EID: 84879867517     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-405882-8.00003-9     Document Type: Chapter
Times cited : (79)

References (93)
  • 3
    • 77954737814 scopus 로고    scopus 로고
    • Discovery of fragment molecules that bind the human peroxiredoxin 5 active site
    • S. Barelier, D. Linard, J. Pons, A. Clippe, B. Knoops, and J.M. Lancelin Discovery of fragment molecules that bind the human peroxiredoxin 5 active site PLoS One 5 3 2010 e9744
    • (2010) PLoS One , vol.5 , Issue.3 , pp. 9744
    • Barelier, S.1    Linard, D.2    Pons, J.3    Clippe, A.4    Knoops, B.5    Lancelin, J.M.6
  • 4
    • 0033521019 scopus 로고    scopus 로고
    • Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B
    • W.C. Barrett, J.P. DeGnore, Y.F. Keng, Z.Y. Zhang, M.B. Yim, and P.B. Chock Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B Journal of Biological Chemistry 274 49 1999 34543 34546
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.49 , pp. 34543-34546
    • Barrett, W.C.1    Degnore, J.P.2    Keng, Y.F.3    Zhang, Z.Y.4    Yim, M.B.5    Chock, P.B.6
  • 6
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
    • B. Biteau, J. Labarre, and M.B. Toledano 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    Toledano, M.B.3
  • 8
    • 79954504166 scopus 로고    scopus 로고
    • Basic principles and emerging concepts in the redox control of transcription factors
    • R. Brigelius-Flohe, and L. Flohe Basic principles and emerging concepts in the redox control of transcription factors Antioxidants & Redox Signaling 15 8 2011 2335 2381
    • (2011) Antioxidants & Redox Signaling , vol.15 , Issue.8 , pp. 2335-2381
    • Brigelius-Flohe, R.1    Flohe, L.2
  • 10
    • 0001445231 scopus 로고    scopus 로고
    • Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin
    • H.Z. Chae, H.J. Kim, S.W. Kang, and S.G. Rhee Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin Diabetes Research and Clinical Practice 45 2-3 1999 101 112
    • (1999) Diabetes Research and Clinical Practice , vol.45 , Issue.23 , pp. 101-112
    • Chae, H.Z.1    Kim, H.J.2    Kang, S.W.3    Rhee, S.G.4
  • 12
    • 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, W. Jeong, H.A. Woo, S.M. Lee, S. Park, and S.G. Rhee Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine Journal of Biological Chemistry 279 49 2004 50994 51001
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 50994-51001
    • Chang, T.S.1    Jeong, W.2    Woo, H.A.3    Lee, S.M.4    Park, S.5    Rhee, S.G.6
  • 14
    • 0035897653 scopus 로고    scopus 로고
    • Homologs of gp91phox: Cloning and tissue expression of Nox3, Nox4, and Nox5
    • G. Cheng, Z. Cao, X. Xu, E.G. van Meir, and J.D. Lambeth Homologs of gp91phox: Cloning and tissue expression of Nox3, Nox4, and Nox5 Gene 269 1-2 2001 131 140
    • (2001) Gene , vol.269 , Issue.12 , pp. 131-140
    • Cheng, G.1    Cao, Z.2    Xu, X.3    Van Meir, E.G.4    Lambeth, J.D.5
  • 15
    • 77953004335 scopus 로고    scopus 로고
    • Hydroxyurea-induced expression of glutathione peroxidase 1 in red blood cells of individuals with sickle cell anemia
    • C.S. Cho, G.J. Kato, S.H. Yang, S.W. Bae, J.S. Lee, and M.T. Gladwin Hydroxyurea-induced expression of glutathione peroxidase 1 in red blood cells of individuals with sickle cell anemia Antioxidants & Redox Signaling 13 1 2010 1 11
    • (2010) Antioxidants & Redox Signaling , vol.13 , Issue.1 , pp. 1-11
    • Cho, C.S.1    Kato, G.J.2    Yang, S.H.3    Bae, S.W.4    Lee, J.S.5    Gladwin, M.T.6
  • 16
    • 1342308079 scopus 로고    scopus 로고
    • Redox regulation of PTEN and protein tyrosine phosphatases in H(2)O(2) mediated cell signaling
    • S.H. Cho, C.H. Lee, Y. Ahn, H. Kim, H. Kim, and C.Y. Ahn Redox regulation of PTEN and protein tyrosine phosphatases in H(2)O(2) mediated cell signaling FEBS Letters 560 1-3 2004 7 13
    • (2004) FEBS Letters , vol.560 , Issue.13 , pp. 7-13
    • Cho, S.H.1    Lee, C.H.2    Ahn, Y.3    Kim, H.4    Kim, H.5    Ahn, C.Y.6
  • 19
    • 73849144014 scopus 로고    scopus 로고
    • Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling
    • A.G. Cox, C.C. Winterbourn, and M.B. Hampton Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling The Biochemical Journal 425 2 2010 313 325
    • (2010) The Biochemical Journal , vol.425 , Issue.2 , pp. 313-325
    • Cox, A.G.1    Winterbourn, C.C.2    Hampton, M.B.3
  • 20
    • 84862777700 scopus 로고    scopus 로고
    • Inactivation of a peroxiredoxin by hydrogen peroxide is critical for thioredoxin-mediated repair of oxidized proteins and cell survival
    • A.M. Day, J.D. Brown, S.R. Taylor, J.D. Rand, B.A. Morgan, and E.A. Veal Inactivation of a peroxiredoxin by hydrogen peroxide is critical for thioredoxin-mediated repair of oxidized proteins and cell survival Molecular Cell 45 3 2012 398 408
    • (2012) Molecular Cell , vol.45 , Issue.3 , pp. 398-408
    • Day, A.M.1    Brown, J.D.2    Taylor, S.R.3    Rand, J.D.4    Morgan, B.A.5    Veal, E.A.6
  • 22
    • 79960478547 scopus 로고    scopus 로고
    • Chemistry and biology of reactive oxygen species in signaling or stress responses
    • B.C. Dickinson, and C.J. Chang Chemistry and biology of reactive oxygen species in signaling or stress responses Nature Chemical Biology 7 8 2011 504 511
    • (2011) Nature Chemical Biology , vol.7 , Issue.8 , pp. 504-511
    • Dickinson, B.C.1    Chang, C.J.2
  • 27
    • 70049083635 scopus 로고    scopus 로고
    • Protein S-nitrosylation in health and disease: A current perspective
    • M.W. Foster, D.T. Hess, and J.S. Stamler Protein S-nitrosylation in health and disease: A current perspective Trends in Molecular Medicine 15 9 2009 391 404
    • (2009) Trends in Molecular Medicine , vol.15 , Issue.9 , pp. 391-404
    • Foster, M.W.1    Hess, D.T.2    Stamler, J.S.3
  • 29
    • 80055008140 scopus 로고    scopus 로고
    • Hydrogen peroxide: A Jekyll and Hyde signalling molecule
    • D.R. Gough, and T.G. Cotter Hydrogen peroxide: A Jekyll and Hyde signalling molecule Cell Death & Disease 2 2011 e213
    • (2011) Cell Death & Disease , vol.2 , pp. 213
    • Gough, D.R.1    Cotter, T.G.2
  • 31
    • 77956171017 scopus 로고    scopus 로고
    • Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization
    • A. Hall, D. Parsonage, L.B. Poole, and P.A. Karplus Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization Journal of Molecular Biology 402 1 2010 194 209
    • (2010) Journal of Molecular Biology , vol.402 , Issue.1 , pp. 194-209
    • Hall, A.1    Parsonage, D.2    Poole, L.B.3    Karplus, P.A.4
  • 32
    • 77954754565 scopus 로고    scopus 로고
    • Targeted quantitation of site-specific cysteine oxidation in endogenous proteins using a differential alkylation and multiple reaction monitoring mass spectrometry approach
    • J.M. Held, S.R. Danielson, J.B. Behring, C. Atsriku, D.J. Britton, and R.L. Puckett Targeted quantitation of site-specific cysteine oxidation in endogenous proteins using a differential alkylation and multiple reaction monitoring mass spectrometry approach Molecular & Cellular Proteomics 9 7 2010 1400 1410
    • (2010) Molecular & Cellular Proteomics , vol.9 , Issue.7 , pp. 1400-1410
    • Held, J.M.1    Danielson, S.R.2    Behring, J.B.3    Atsriku, C.4    Britton, D.J.5    Puckett, R.L.6
  • 33
    • 84859822386 scopus 로고    scopus 로고
    • Regulatory control or oxidative damage? Proteomic approaches to interrogate the role of cysteine oxidation status in biological processes
    • R111.013037
    • J.M. Held, and B.W. Gibson Regulatory control or oxidative damage? Proteomic approaches to interrogate the role of cysteine oxidation status in biological processes Molecular & Cellular Proteomics 11 4 2012 R111.013037
    • (2012) Molecular & Cellular Proteomics , vol.11 , Issue.4
    • Held, J.M.1    Gibson, B.W.2
  • 34
    • 78650881150 scopus 로고    scopus 로고
    • Peroxiredoxin-2 protects against 6-hydroxydopamine-induced dopaminergic neurodegeneration via attenuation of the apoptosis signal-regulating kinase (ASK1) signaling cascade
    • X. Hu, Z. Weng, C.T. Chu, L. Zhang, G. Cao, and Y. Gao Peroxiredoxin-2 protects against 6-hydroxydopamine-induced dopaminergic neurodegeneration via attenuation of the apoptosis signal-regulating kinase (ASK1) signaling cascade The Journal of Neuroscience 31 1 2011 247 261
    • (2011) The Journal of Neuroscience , vol.31 , Issue.1 , pp. 247-261
    • Hu, X.1    Weng, Z.2    Chu, C.T.3    Zhang, L.4    Cao, G.5    Gao, Y.6
  • 35
    • 70350050576 scopus 로고    scopus 로고
    • Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: Kinetics, acidity constants, and conformational dynamics
    • M. Hugo, L. Turell, B. Manta, H. Botti, G. Monteiro, and L.E. Netto Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: Kinetics, acidity constants, and conformational dynamics Biochemistry 48 40 2009 9416 9426
    • (2009) Biochemistry , vol.48 , Issue.40 , pp. 9416-9426
    • Hugo, M.1    Turell, L.2    Manta, B.3    Botti, H.4    Monteiro, G.5    Netto, L.E.6
  • 37
    • 29344451931 scopus 로고    scopus 로고
    • Phosphorylation and concomitant structural changes in human 2-Cys peroxiredoxin isotype i differentially regulate its peroxidase and molecular chaperone functions
    • H.H. Jang, S.Y. Kim, S.K. Park, H.S. Jeon, Y.M. Lee, and J.H. Jung Phosphorylation and concomitant structural changes in human 2-Cys peroxiredoxin isotype I differentially regulate its peroxidase and molecular chaperone functions FEBS Letters 580 1 2006 351 355
    • (2006) FEBS Letters , vol.580 , Issue.1 , pp. 351-355
    • Jang, H.H.1    Kim, S.Y.2    Park, S.K.3    Jeon, H.S.4    Lee, Y.M.5    Jung, J.H.6
  • 38
    • 2542464938 scopus 로고    scopus 로고
    • Two enzymes in one; Two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function
    • H.H. Jang, K.O. Lee, Y.H. Chi, B.G. Jung, S.K. Park, and J.H. Park Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function Cell 117 5 2004 625 635
    • (2004) Cell , vol.117 , Issue.5 , pp. 625-635
    • Jang, H.H.1    Lee, K.O.2    Chi, Y.H.3    Jung, B.G.4    Park, S.K.5    Park, J.H.6
  • 39
    • 84866357593 scopus 로고    scopus 로고
    • Peroxiredoxin 1 functions as a signal peroxidase to receive, transduce, and transmit peroxide signals in mammalian cells
    • R.M. Jarvis, S.M. Hughes, and E.C. Ledgerwood Peroxiredoxin 1 functions as a signal peroxidase to receive, transduce, and transmit peroxide signals in mammalian cells Free Radical Biology & Medicine 53 7 2012 1522 1530
    • (2012) Free Radical Biology & Medicine , vol.53 , Issue.7 , pp. 1522-1530
    • Jarvis, R.M.1    Hughes, S.M.2    Ledgerwood, E.C.3
  • 40
    • 53049083629 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid in peroxiredoxin by sulfiredoxin proceeds directly through a sulfinic phosphoryl ester intermediate
    • T.J. Jonsson, M.S. Murray, L.C. Johnson, and W.T. Lowther Reduction of cysteine sulfinic acid in peroxiredoxin by sulfiredoxin proceeds directly through a sulfinic phosphoryl ester intermediate Journal of Biological Chemistry 283 35 2008 23846 23851
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.35 , pp. 23846-23851
    • Jonsson, T.J.1    Murray, M.S.2    Johnson, L.C.3    Lowther, W.T.4
  • 41
    • 80052290597 scopus 로고    scopus 로고
    • Global proteomic assessment of the classical protein-tyrosine phosphatome and "redoxome"
    • R. Karisch, M. Fernandez, P. Taylor, C. Virtanen, J.R. St-Germain, and L.L. Jin Global proteomic assessment of the classical protein-tyrosine phosphatome and "Redoxome" Cell 146 5 2011 826 840
    • (2011) Cell , vol.146 , Issue.5 , pp. 826-840
    • Karisch, R.1    Fernandez, M.2    Taylor, P.3    Virtanen, C.4    St-Germain, J.R.5    Jin, L.L.6
  • 42
    • 77956198422 scopus 로고    scopus 로고
    • Use of dimedone-based chemical probes for sulfenic acid detection evaluation of conditions affecting probe incorporation into redox-sensitive proteins
    • C. Klomsiri, K.J. Nelson, E. Bechtold, L. Soito, L.C. Johnson, and W.T. Lowther Use of dimedone-based chemical probes for sulfenic acid detection evaluation of conditions affecting probe incorporation into redox-sensitive proteins Methods in Enzymology 473 2010 77 94
    • (2010) Methods in Enzymology , vol.473 , pp. 77-94
    • Klomsiri, C.1    Nelson, K.J.2    Bechtold, E.3    Soito, L.4    Johnson, L.C.5    Lowther, W.T.6
  • 43
    • 77954142511 scopus 로고    scopus 로고
    • Electrode potentials of partially reduced oxygen species, from dioxygen to water
    • W.H. Koppenol, D.M. Stanbury, and P.L. Bounds Electrode potentials of partially reduced oxygen species, from dioxygen to water Free Radical Biology & Medicine 49 3 2010 317 322
    • (2010) Free Radical Biology & Medicine , vol.49 , Issue.3 , pp. 317-322
    • Koppenol, W.H.1    Stanbury, D.M.2    Bounds, P.L.3
  • 47
    • 0017089701 scopus 로고
    • Potentiometric determination of ionizations at the active site of papain
    • S.D. Lewis, F.A. Johnson, and J.A. Shafer Potentiometric determination of ionizations at the active site of papain Biochemistry 15 23 1976 5009 5017
    • (1976) Biochemistry , vol.15 , Issue.23 , pp. 5009-5017
    • Lewis, S.D.1    Johnson, F.A.2    Shafer, J.A.3
  • 48
    • 57649213405 scopus 로고    scopus 로고
    • Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity
    • J.C. Lim, H.I. Choi, Y.S. Park, H.W. Nam, H.A. Woo, and K.S. Kwon Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity Journal of Biological Chemistry 283 43 2008 28873 28880
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.43 , pp. 28873-28880
    • Lim, J.C.1    Choi, H.I.2    Park, Y.S.3    Nam, H.W.4    Woo, H.A.5    Kwon, K.S.6
  • 50
    • 84867711090 scopus 로고    scopus 로고
    • Thioredoxin system in cell death progression
    • J. Lu, and A. Holmgren Thioredoxin system in cell death progression Antioxidants & Redox Signaling 17 12 2012 1738 1747
    • (2012) Antioxidants & Redox Signaling , vol.17 , Issue.12 , pp. 1738-1747
    • Lu, J.1    Holmgren, A.2
  • 52
    • 80052206812 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase A contributes to the Trojan horse mechanism of immune defense evasion with its intrinsic resistance to Cys184 oxidation
    • J.A. Melvin, C.F. Murphy, L.G. Dubois, J.W. Thompson, M.A. Moseley, and D.G. McCafferty Staphylococcus aureus sortase A contributes to the Trojan horse mechanism of immune defense evasion with its intrinsic resistance to Cys184 oxidation Biochemistry 50 35 2011 7591 7599
    • (2011) Biochemistry , vol.50 , Issue.35 , pp. 7591-7599
    • Melvin, J.A.1    Murphy, C.F.2    Dubois, L.G.3    Thompson, J.W.4    Moseley, M.A.5    McCafferty, D.G.6
  • 54
    • 0025996014 scopus 로고
    • Reconstitution of Ca(2 +)-dependent K + transport in erythrocyte membrane vesicles requires a cytoplasmic protein
    • R.B. Moore, M.V. Mankad, S.K. Shriver, V.N. Mankad, and G.A. Plishker Reconstitution of Ca(2 +)-dependent K + transport in erythrocyte membrane vesicles requires a cytoplasmic protein Journal of Biological Chemistry 266 28 1991 18964 18968
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.28 , pp. 18964-18968
    • Moore, R.B.1    Mankad, M.V.2    Shriver, S.K.3    Mankad, V.N.4    Plishker, G.A.5
  • 55
    • 80053614220 scopus 로고    scopus 로고
    • Oligomeric peroxiredoxin-I is an essential intermediate for p53 to activate MST1 kinase and apoptosis
    • A. Morinaka, Y. Funato, K. Uesugi, and H. Miki Oligomeric peroxiredoxin-I is an essential intermediate for p53 to activate MST1 kinase and apoptosis Oncogene 30 40 2011 4208 4218
    • (2011) Oncogene , vol.30 , Issue.40 , pp. 4208-4218
    • Morinaka, A.1    Funato, Y.2    Uesugi, K.3    Miki, H.4
  • 56
    • 34948845017 scopus 로고    scopus 로고
    • Disulfide bond-mediated multimerization of Ask1 and its reduction by thioredoxin-1 regulate H(2)O(2)-induced c-Jun NH(2)-terminal kinase activation and apoptosis
    • P.J. Nadeau, S.J. Charette, M.B. Toledano, and J. Landry Disulfide bond-mediated multimerization of Ask1 and its reduction by thioredoxin-1 regulate H(2)O(2)-induced c-Jun NH(2)-terminal kinase activation and apoptosis Molecular Biology of the Cell 18 10 2007 3903 3913
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.10 , pp. 3903-3913
    • Nadeau, P.J.1    Charette, S.J.2    Toledano, M.B.3    Landry, J.4
  • 57
    • 72449180503 scopus 로고    scopus 로고
    • Protein cysteine modifications: (2) reactivity specificity and topics of medicinal chemistry and protein engineering
    • N. Nagahara, T. Matsumura, R. Okamoto, and Y. Kajihara Protein cysteine modifications: (2) reactivity specificity and topics of medicinal chemistry and protein engineering Current Medicinal Chemistry 16 34 2009 4490 4501
    • (2009) Current Medicinal Chemistry , vol.16 , Issue.34 , pp. 4490-4501
    • Nagahara, N.1    Matsumura, T.2    Okamoto, R.3    Kajihara, Y.4
  • 58
    • 57049161455 scopus 로고    scopus 로고
    • Cysteine pK(a) values for the bacterial peroxiredoxin AhpC
    • K.J. Nelson, D. Parsonage, A. Hall, P.A. Karplus, and L.B. Poole Cysteine pK(a) values for the bacterial peroxiredoxin AhpC Biochemistry 47 48 2008 12860 12868
    • (2008) Biochemistry , vol.47 , Issue.48 , pp. 12860-12868
    • Nelson, K.J.1    Parsonage, D.2    Hall, A.3    Karplus, P.A.4    Poole, L.B.5
  • 59
    • 69949115433 scopus 로고    scopus 로고
    • Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin
    • J.W. Park, J.J. Mieyal, S.G. Rhee, and P.B. Chock Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin Journal of Biological Chemistry 284 35 2009 23364 23374
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.35 , pp. 23364-23374
    • Park, J.W.1    Mieyal, J.J.2    Rhee, S.G.3    Chock, P.B.4
  • 60
    • 79953871561 scopus 로고    scopus 로고
    • Glutathionylation of peroxiredoxin i induces decamer to dimers dissociation with concomitant loss of chaperone activity
    • J.W. Park, G. Piszczek, S.G. Rhee, and P.B. Chock Glutathionylation of peroxiredoxin I induces decamer to dimers dissociation with concomitant loss of chaperone activity Biochemistry 50 15 2011 3204 3210
    • (2011) Biochemistry , vol.50 , Issue.15 , pp. 3204-3210
    • Park, J.W.1    Piszczek, G.2    Rhee, S.G.3    Chock, P.B.4
  • 63
    • 34249703509 scopus 로고    scopus 로고
    • The high reactivity of peroxiredoxin 2 with H(2)O(2) is not reflected in its reaction with other oxidants and thiol reagents
    • A.V. Peskin, F.M. Low, L.N. Paton, G.J. Maghzal, M.B. Hampton, and C.C. Winterbourn The high reactivity of peroxiredoxin 2 with H(2)O(2) is not reflected in its reaction with other oxidants and thiol reagents Journal of Biological Chemistry 282 16 2007 11885 11892
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.16 , pp. 11885-11892
    • Peskin, A.V.1    Low, F.M.2    Paton, L.N.3    Maghzal, G.J.4    Hampton, M.B.5    Winterbourn, C.C.6
  • 64
    • 84857116578 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
    • P.D. Ray, B.W. Huang, and Y. Tsuji Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling Cellular Signalling 24 5 2012 981 990
    • (2012) Cellular Signalling , vol.24 , Issue.5 , pp. 981-990
    • Ray, P.D.1    Huang, B.W.2    Tsuji, Y.3
  • 65
    • 79959341904 scopus 로고    scopus 로고
    • Oxidizing substrate specificity of Mycobacterium tuberculosis alkyl hydroperoxide reductase E: Kinetics and mechanisms of oxidation and overoxidation
    • A.M. Reyes, M. Hugo, A. Trostchansky, L. Capece, R. Radi, and M. Trujillo Oxidizing substrate specificity of Mycobacterium tuberculosis alkyl hydroperoxide reductase E: kinetics and mechanisms of oxidation and overoxidation Free Radical Biology and Medicine 51 2 2011 464 473
    • (2011) Free Radical Biology and Medicine , vol.51 , Issue.2 , pp. 464-473
    • Reyes, A.M.1    Hugo, M.2    Trostchansky, A.3    Capece, L.4    Radi, R.5    Trujillo, M.6
  • 66
    • 84856940017 scopus 로고    scopus 로고
    • Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
    • S.G. Rhee, H.A. Woo, I.S. Kil, and S.H. Bae Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides Journal of Biological Chemistry 287 7 2012 4403 4410
    • (2012) Journal of Biological Chemistry , vol.287 , Issue.7 , pp. 4403-4410
    • Rhee, S.G.1    Woo, H.A.2    Kil, I.S.3    Bae, S.H.4
  • 67
    • 12144287638 scopus 로고    scopus 로고
    • Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense
    • N. Rouhier, E. Gelhaye, J.M. Gualberto, M.N. Jordy, E. De Fay, and M. Hirasawa Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense Plant Physiology 134 3 2004 1027 1038
    • (2004) Plant Physiology , vol.134 , Issue.3 , pp. 1027-1038
    • Rouhier, N.1    Gelhaye, E.2    Gualberto, J.M.3    Jordy, M.N.4    De Fay, E.5    Hirasawa, M.6
  • 68
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • M. Saitoh, H. Nishitoh, M. Fujii, K. Takeda, K. Tobiume, and Y. Sawada Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1 The EMBO Journal 17 9 1998 2596 2606
    • (1998) The EMBO Journal , vol.17 , Issue.9 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2    Fujii, M.3    Takeda, K.4    Tobiume, K.5    Sawada, Y.6
  • 69
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • A. Salmeen, J.N. Andersen, M.P. Myers, T.C. Meng, J.A. Hinks, and N.K. Tonks Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate Nature 423 6941 2003 769 773
    • (2003) Nature , vol.423 , Issue.6941 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6
  • 71
    • 67649391256 scopus 로고    scopus 로고
    • Novel protective mechanism against irreversible hyperoxidation of peroxiredoxin: Nalpha-terminal acetylation of human peroxiredoxin II
    • J.H. Seo, J.C. Lim, D.Y. Lee, K.S. Kim, G. Piszczek, and H.W. Nam Novel protective mechanism against irreversible hyperoxidation of peroxiredoxin: Nalpha-terminal acetylation of human peroxiredoxin II Journal of Biological Chemistry 284 20 2009 13455 13465
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.20 , pp. 13455-13465
    • Seo, J.H.1    Lim, J.C.2    Lee, D.Y.3    Kim, K.S.4    Piszczek, G.5    Nam, H.W.6
  • 72
    • 0041323072 scopus 로고    scopus 로고
    • Catalytic and chemical competence of regulation of cdc25 phosphatase by oxidation/reduction
    • J. Sohn, and J. Rudolph Catalytic and chemical competence of regulation of cdc25 phosphatase by oxidation/reduction Biochemistry 42 34 2003 10060 10070
    • (2003) Biochemistry , vol.42 , Issue.34 , pp. 10060-10070
    • Sohn, J.1    Rudolph, J.2
  • 73
    • 0842348252 scopus 로고    scopus 로고
    • An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems
    • J.R. Stone An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems Archives of Biochemistry and Biophysics 422 2 2004 119 124
    • (2004) Archives of Biochemistry and Biophysics , vol.422 , Issue.2 , pp. 119-124
    • Stone, J.R.1
  • 74
    • 70349650326 scopus 로고    scopus 로고
    • 2 + diffusion using a particle-based simulation model
    • 2 + diffusion using a particle-based simulation model Chaos 19 3 2009 037110
    • (2009) Chaos , vol.19 , Issue.3 , pp. 037110
    • Straube, R.1    Ridgway, D.2
  • 75
    • 0033517275 scopus 로고    scopus 로고
    • Cell transformation by the superoxide-generating oxidase Mox1
    • Y.A. Suh, R.S. Arnold, B. Lassegue, J. Shi, X. Xu, and D. Sorescu Cell transformation by the superoxide-generating oxidase Mox1 Nature 401 6748 1999 79 82
    • (1999) Nature , vol.401 , Issue.6748 , pp. 79-82
    • Suh, Y.A.1    Arnold, R.S.2    Lassegue, B.3    Shi, J.4    Xu, X.5    Sorescu, D.6
  • 78
    • 79953242071 scopus 로고    scopus 로고
    • Horseradish peroxidase compound i as a tool to investigate reactive protein-cysteine residues: From quantification to kinetics
    • J.C. Toledo Jr., R. Audi, R. Ogusucu, G. Monteiro, L.E. Netto, and O. Augusto Horseradish peroxidase compound I as a tool to investigate reactive protein-cysteine residues: From quantification to kinetics Free Radical Biology & Medicine 50 9 2011 1032 1038
    • (2011) Free Radical Biology & Medicine , vol.50 , Issue.9 , pp. 1032-1038
    • Toledo, Jr.J.C.1    Audi, R.2    Ogusucu, R.3    Monteiro, G.4    Netto, L.E.5    Augusto, O.6
  • 79
    • 35448954324 scopus 로고    scopus 로고
    • Pre-steady state kinetic characterization of human peroxiredoxin 5: Taking advantage of Trp84 fluorescence increase upon oxidation
    • M. Trujillo, A. Clippe, B. Manta, G. Ferrer-Sueta, A. Smeets, and J.P. Declercq Pre-steady state kinetic characterization of human peroxiredoxin 5: Taking advantage of Trp84 fluorescence increase upon oxidation Archives of Biochemistry and Biophysics 467 1 2007 95 106
    • (2007) Archives of Biochemistry and Biophysics , vol.467 , Issue.1 , pp. 95-106
    • Trujillo, M.1    Clippe, A.2    Manta, B.3    Ferrer-Sueta, G.4    Smeets, A.5    Declercq, J.P.6
  • 83
    • 34147210988 scopus 로고    scopus 로고
    • Hydrogen peroxide sensing and signaling
    • E.A. Veal, A.M. Day, and B.A. Morgan Hydrogen peroxide sensing and signaling Molecular Cell 26 1 2007 1 14
    • (2007) Molecular Cell , vol.26 , Issue.1 , pp. 1-14
    • Veal, E.A.1    Day, A.M.2    Morgan, B.A.3
  • 85
    • 0032865515 scopus 로고    scopus 로고
    • Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
    • C.C. Winterbourn, and D. Metodiewa Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide Free Radical Biology & Medicine 27 3-4 1999 322 328
    • (1999) Free Radical Biology & Medicine , vol.27 , Issue.34 , pp. 322-328
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 86
    • 0242668688 scopus 로고    scopus 로고
    • Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
    • H.A. Woo, H.Z. Chae, S.C. Hwang, K.S. Yang, S.W. Kang, and K. Kim Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation Science 300 5619 2003 653 656
    • (2003) Science , vol.300 , Issue.5619 , 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
  • 87
  • 88
    • 76749102420 scopus 로고    scopus 로고
    • Inactivation of peroxiredoxin i by phosphorylation allows localized H(2)O(2) accumulation for cell signaling
    • H.A. Woo, S.H. Yim, D.H. Shin, D. Kang, D.Y. Yu, and S.G. Rhee Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling Cell 140 4 2010 517 528
    • (2010) Cell , vol.140 , Issue.4 , pp. 517-528
    • Woo, H.A.1    Yim, S.H.2    Shin, D.H.3    Kang, D.4    Yu, D.Y.5    Rhee, S.G.6
  • 89
    • 0037197672 scopus 로고    scopus 로고
    • Dimers to doughnuts: Redox-sensitive oligomerization of 2-cysteine peroxiredoxins
    • Z.A. Wood, L.B. Poole, R.R. Hantgan, and P.A. Karplus Dimers to doughnuts: Redox-sensitive oligomerization of 2-cysteine peroxiredoxins Biochemistry 41 17 2002 5493 5504
    • (2002) Biochemistry , vol.41 , Issue.17 , pp. 5493-5504
    • Wood, Z.A.1    Poole, L.B.2    Hantgan, R.R.3    Karplus, P.A.4
  • 90
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Z.A. Wood, L.B. Poole, and P.A. Karplus Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling Science 300 5619 2003 650 653
    • (2003) Science , vol.300 , Issue.5619 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 92
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
    • M. Wunderlich, and R. Glockshuber Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli Protein Science 2 5 1993 717 726
    • (1993) Protein Science , vol.2 , Issue.5 , pp. 717-726
    • Wunderlich, M.1    Glockshuber, R.2
  • 93
    • 77956541126 scopus 로고    scopus 로고
    • T-LAK cell-originated protein kinase (TOPK) phosphorylation of Prx1 at Ser-32 prevents UVB-induced apoptosis in RPMI7951 melanoma cells through the regulation of Prx1 peroxidase activity
    • T.A. Zykova, F. Zhu, T.I. Vakorina, J. Zhang, L.A. Higgins, and D.V. Urusova T-LAK cell-originated protein kinase (TOPK) phosphorylation of Prx1 at Ser-32 prevents UVB-induced apoptosis in RPMI7951 melanoma cells through the regulation of Prx1 peroxidase activity Journal of Biological Chemistry 285 38 2010 29138 29146
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.38 , pp. 29138-29146
    • Zykova, T.A.1    Zhu, F.2    Vakorina, T.I.3    Zhang, J.4    Higgins, L.A.5    Urusova, D.V.6


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