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Volumn 80, Issue , 2015, Pages 164-170

Are free radicals involved in thiol-based redox signaling?

Author keywords

Cell signalling; Free radicals; Hydrogen peroxide; Superoxide; Thiol protein oxidation

Indexed keywords

FREE RADICAL; HYDROGEN PEROXIDE; SUPEROXIDE; THIOL; DISULFIDE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; HOMEODOMAIN PROTEIN; PROTEIN TYROSINE PHOSPHATASE 1B; PRRX2 PROTEIN, HUMAN; PTPN1 PROTEIN, HUMAN; THIOL DERIVATIVE;

EID: 84924119180     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.08.017     Document Type: Article
Times cited : (159)

References (76)
  • 1
    • 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 1969 6049 6055
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 2
    • 75749136883 scopus 로고    scopus 로고
    • Signaling functions of reactive oxygen species
    • H.J. Forman, M. Maiorino, and F. Ursini Signaling functions of reactive oxygen species Biochemistry 49 2010 835 842
    • (2010) Biochemistry , vol.49 , pp. 835-842
    • Forman, H.J.1    Maiorino, M.2    Ursini, F.3
  • 3
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • C.C. Winterbourn, and M.B. Hampton Thiol chemistry and specificity in redox signaling Free Radic. Biol. Med. 45 2008 549 561
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 4
    • 33646698671 scopus 로고    scopus 로고
    • Hydrogen peroxide: A signaling messenger
    • J.R. Stone, and S. Yang Hydrogen peroxide: a signaling messenger Antioxid. Redox Signal. 8 2006 243 270
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 243-270
    • Stone, J.R.1    Yang, S.2
  • 5
    • 84901741434 scopus 로고    scopus 로고
    • Hydrogen peroxide sensing, signaling and regulation of transcription factors
    • H.S. Marinho, C. Real, L. Cyrne, H. Soares, and F. Antunes Hydrogen peroxide sensing, signaling and regulation of transcription factors Redox Biol 2 2014 535 562
    • (2014) Redox Biol , vol.2 , pp. 535-562
    • Marinho, H.S.1    Real, C.2    Cyrne, L.3    Soares, H.4    Antunes, F.5
  • 6
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • C.C. Winterbourn Reconciling the chemistry and biology of reactive oxygen species Nat. Chem. Biol. 4 2008 278 286
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 278-286
    • Winterbourn, C.C.1
  • 7
    • 84862516895 scopus 로고    scopus 로고
    • Biological chemistry of reactive oxygen species
    • Chatgilialoglu, C., Studer, A., editors. Chichester: Wiley
    • Winterbourn, C. C. Biological chemistry of reactive oxygen species. In: Chatgilialoglu, C., Studer, A., editors. Encyclopedia of radicals in chemistry, biology & materials. Chichester: Wiley; 2012. p. 1259-1282.
    • (2012) Encyclopedia of Radicals in Chemistry, Biology & Materials , pp. 1259-1282
    • Winterbourn, C.C.1
  • 9
    • 84901316606 scopus 로고    scopus 로고
    • Cellular mechanisms and physiological consequences of redox-dependent signalling
    • K.M. Holmstrom, and T. Finkel Cellular mechanisms and physiological consequences of redox-dependent signalling Nat. Rev. Mol. Cell. Biol. 15 2014 411 421
    • (2014) Nat. Rev. Mol. Cell. Biol. , vol.15 , pp. 411-421
    • Holmstrom, K.M.1    Finkel, T.2
  • 10
    • 79958152853 scopus 로고    scopus 로고
    • Superoxide dismutase in redox biology: The roles of superoxide and hydrogen peroxide
    • G.R. Buettner Superoxide dismutase in redox biology: the roles of superoxide and hydrogen peroxide Anticancer Agents Med. Chem 11 2011 341 346
    • (2011) Anticancer Agents Med. Chem , vol.11 , pp. 341-346
    • Buettner, G.R.1
  • 12
    • 33744962865 scopus 로고    scopus 로고
    • Redefining oxidative stress
    • D.P. Jones Redefining oxidative stress Antioxid. Redox Signal. 8 2006 1865 1879
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 1865-1879
    • Jones, D.P.1
  • 13
    • 84871309537 scopus 로고    scopus 로고
    • Redox regulation of epidermal growth factor receptor signaling through cysteine oxidation
    • T.H. Truong, and K.S. Carroll Redox regulation of epidermal growth factor receptor signaling through cysteine oxidation Biochemistry 51 2012 9954 9965
    • (2012) Biochemistry , vol.51 , pp. 9954-9965
    • Truong, T.H.1    Carroll, K.S.2
  • 14
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • B. D'Autreaux, and M.B. Toledano ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis Nat. Rev. Mol. Cell. Biol. 8 2007 813 824
    • (2007) Nat. Rev. Mol. Cell. Biol. , vol.8 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 15
    • 84880277784 scopus 로고    scopus 로고
    • The biological chemistry of hydrogen peroxide
    • C.C. Winterbourn The biological chemistry of hydrogen peroxide Methods Enzymol. 528 2013 3 25
    • (2013) Methods Enzymol. , vol.528 , pp. 3-25
    • Winterbourn, C.C.1
  • 17
    • 80053476859 scopus 로고    scopus 로고
    • Conformation-sensing antibodies stabilize the oxidized form of PTP1B and inhibit its phosphatase activity
    • A. Haque, J.N. Andersen, A. Salmeen, D. Barford, and N.K. Tonks Conformation-sensing antibodies stabilize the oxidized form of PTP1B and inhibit its phosphatase activity Cell 147 2011 185 198
    • (2011) Cell , vol.147 , pp. 185-198
    • Haque, A.1    Andersen, J.N.2    Salmeen, A.3    Barford, D.4    Tonks, N.K.5
  • 18
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: Revisiting PTPs and the control of cell signaling
    • N.K. Tonks Redox redux: revisiting PTPs and the control of cell signaling Cell 121 2005 667 670
    • (2005) Cell , vol.121 , pp. 667-670
    • Tonks, N.K.1
  • 19
    • 64149085448 scopus 로고    scopus 로고
    • Typical 2-Cys peroxiredoxins - Structures, mechanisms and functions
    • A. Hall, P.A. Karplus, and L.B. Poole Typical 2-Cys peroxiredoxins - structures, mechanisms and functions FEBS J. 276 2009 2469 2477
    • (2009) FEBS J. , vol.276 , pp. 2469-2477
    • Hall, A.1    Karplus, P.A.2    Poole, L.B.3
  • 20
    • 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 J. Biol. Chem. 287 2012 4403 4410
    • (2012) J. Biol. Chem. , vol.287 , pp. 4403-4410
    • Rhee, S.G.1    Woo, H.A.2    Kil, I.S.3    Bae, S.H.4
  • 23
    • 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 Radic. Biol. Med. 53 2012 1522 1530
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 1522-1530
    • Jarvis, R.M.1    Hughes, S.M.2    Ledgerwood, E.C.3
  • 24
    • 74849098583 scopus 로고    scopus 로고
    • Peroxiredoxin 1 and its role in cell signaling
    • C.A. Neumann, J. Cao, and Y. Manevich Peroxiredoxin 1 and its role in cell signaling Cell Cycle 8 2009 4072 4078
    • (2009) Cell Cycle , vol.8 , pp. 4072-4078
    • Neumann, C.A.1    Cao, J.2    Manevich, Y.3
  • 26
    • 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 Mol. Cell 26 2007 1 14
    • (2007) Mol. Cell , vol.26 , pp. 1-14
    • Veal, E.A.1    Day, A.M.2    Morgan, B.A.3
  • 27
    • 84924184124 scopus 로고    scopus 로고
    • Genetically encoded fluorescent redox sensors
    • K.A. Lukyanovov, and V. Belousov Genetically encoded fluorescent redox sensors Biochim. Biophys. Acta 1860 2014 1850 1860
    • (2014) Biochim. Biophys. Acta , vol.1860 , pp. 1850-1860
    • Lukyanovov, K.A.1    Belousov, V.2
  • 28
    • 77954356493 scopus 로고    scopus 로고
    • Fluorescent protein-based redox probes
    • A.J. Meyer, and T.P. Dick Fluorescent protein-based redox probes Antioxid. Redox Signal. 13 2010 621 650
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 621-650
    • Meyer, A.J.1    Dick, T.P.2
  • 29
    • 80053049200 scopus 로고    scopus 로고
    • Boronate oxidation as a bioorthogonal reaction approach for studying the chemistry of hydrogen peroxide in living systems
    • A.R. Lippert, G.C. Van de Bittner, and C.J. Chang Boronate oxidation as a bioorthogonal reaction approach for studying the chemistry of hydrogen peroxide in living systems Acc. Chem. Res. 44 2011 793 804
    • (2011) Acc. Chem. Res. , vol.44 , pp. 793-804
    • Lippert, A.R.1    Van De Bittner, G.C.2    Chang, C.J.3
  • 30
    • 84890114880 scopus 로고    scopus 로고
    • The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells
    • C.C. Winterbourn The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells Biochim. Biophys. Acta 1840 2014 730 738
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 730-738
    • Winterbourn, C.C.1
  • 31
    • 46249086250 scopus 로고    scopus 로고
    • Nox4 and nox2 NADPH oxidases mediate distinct cellular redox signaling responses to agonist stimulation
    • N. Anilkumar, R. Weber, M. Zhang, A. Brewer, and A.M. Shah Nox4 and nox2 NADPH oxidases mediate distinct cellular redox signaling responses to agonist stimulation Arterioscler. Thromb. Vasc. Biol. 28 2008 1347 1354
    • (2008) Arterioscler. Thromb. Vasc. Biol. , vol.28 , pp. 1347-1354
    • Anilkumar, N.1    Weber, R.2    Zhang, M.3    Brewer, A.4    Shah, A.M.5
  • 32
    • 34548126843 scopus 로고    scopus 로고
    • Fluorescent and luminescent probes for measurement of oxidative and nitrosative species in cells and tissues: Progress, pitfalls, and prospects
    • P. Wardman Fluorescent and luminescent probes for measurement of oxidative and nitrosative species in cells and tissues: progress, pitfalls, and prospects Free Radic. Biol. Med. 43 2007 995 1022
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 995-1022
    • Wardman, P.1
  • 33
    • 33644872102 scopus 로고    scopus 로고
    • The oxidation of 2′,7′-dichlorofluorescin to reactive oxygen species: A self-fulfilling prophesy?
    • M.G. Bonini, C. Rota, A. Tomasi, and R.P. Mason The oxidation of 2′,7′-dichlorofluorescin to reactive oxygen species: a self-fulfilling prophesy? Free Radic. Biol. Med. 40 2006 968 975
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 968-975
    • Bonini, M.G.1    Rota, C.2    Tomasi, A.3    Mason, R.P.4
  • 34
    • 77949593677 scopus 로고    scopus 로고
    • Targeting and regulation of reactive oxygen species generation by Nox family NADPH oxidases
    • T.L. Leto, S. Morand, D. Hurt, and T. Ueyama Targeting and regulation of reactive oxygen species generation by Nox family NADPH oxidases Antioxid. Redox Signal. 11 2009 2607 2619
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2607-2619
    • Leto, T.L.1    Morand, S.2    Hurt, D.3    Ueyama, T.4
  • 35
    • 70449715463 scopus 로고    scopus 로고
    • Reactive oxygen species and peroxisomes: Struggling for balance
    • N.A. Bonekamp, A. Volkl, H.D. Fahimi, and M. Schrader Reactive oxygen species and peroxisomes: struggling for balance Biofactors 35 2009 346 355
    • (2009) Biofactors , vol.35 , pp. 346-355
    • Bonekamp, N.A.1    Volkl, A.2    Fahimi, H.D.3    Schrader, M.4
  • 36
    • 31044452359 scopus 로고    scopus 로고
    • Generating disulfides enzymatically: Reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p
    • E. Gross, C.S. Sevier, N. Heldman, E. Vitu, M. Bentzur, C.A. Kaiser, C. Thorpe, and D. Fass Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p Proc. Natl. Acad. Sci. USA 103 2006 299 304
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 299-304
    • Gross, E.1    Sevier, C.S.2    Heldman, N.3    Vitu, E.4    Bentzur, M.5    Kaiser, C.A.6    Thorpe, C.7    Fass, D.8
  • 38
    • 78049374613 scopus 로고    scopus 로고
    • The use of thiols by ribonucleotide reductase
    • A. Holmgren, and R. Sengupta The use of thiols by ribonucleotide reductase Free Radic. Biol. Med. 49 2010 1617 1628
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 1617-1628
    • Holmgren, A.1    Sengupta, R.2
  • 39
    • 33847753939 scopus 로고    scopus 로고
    • Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes
    • S. Jang, and J.A. Imlay Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes J. Biol. Chem. 282 2007 929 937
    • (2007) J. Biol. Chem. , vol.282 , pp. 929-937
    • Jang, S.1    Imlay, J.A.2
  • 40
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • J.A. Imlay Cellular defenses against superoxide and hydrogen peroxide Annu. Rev. Biochem. 77 2008 755 776
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 41
    • 43049173503 scopus 로고    scopus 로고
    • Mammalian heme peroxidases: From molecular mechanisms to health implications
    • M.J. Davies, C.L. Hawkins, D.I. Pattison, and M.D. Rees Mammalian heme peroxidases: from molecular mechanisms to health implications Antioxid. Redox Signal. 10 2008 1199 1234
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1199-1234
    • Davies, M.J.1    Hawkins, C.L.2    Pattison, D.I.3    Rees, M.D.4
  • 42
    • 84894188910 scopus 로고    scopus 로고
    • Redox control of human mitochondrial outer membrane protein MitoNEET [2Fe-2S] clusters by biological thiols and hydrogen peroxide
    • A.P. Landry, and H. Ding Redox control of human mitochondrial outer membrane protein MitoNEET [2Fe-2S] clusters by biological thiols and hydrogen peroxide J. Biol. Chem. 289 2014 4307 4315
    • (2014) J. Biol. Chem. , vol.289 , pp. 4307-4315
    • Landry, A.P.1    Ding, H.2
  • 43
    • 64749101531 scopus 로고    scopus 로고
    • Chemical biology of peroxynitrite: Kinetics, diffusion, and radicals
    • G. Ferrer-Sueta, and R. Radi Chemical biology of peroxynitrite: kinetics, diffusion, and radicals ACS Chem. Biol. 4 2009 161 177
    • (2009) ACS Chem. Biol. , vol.4 , pp. 161-177
    • Ferrer-Sueta, G.1    Radi, R.2
  • 44
    • 79953793364 scopus 로고    scopus 로고
    • Manganese superoxide dismutase (Sod2) and redox-control of signaling events that drive metastasis
    • N. Hempel, P.M. Carrico, and J.A. Melendez Manganese superoxide dismutase (Sod2) and redox-control of signaling events that drive metastasis Anticancer Agents Med. Chem 11 2011 191 201
    • (2011) Anticancer Agents Med. Chem , vol.11 , pp. 191-201
    • Hempel, N.1    Carrico, P.M.2    Melendez, J.A.3
  • 46
    • 42349117302 scopus 로고    scopus 로고
    • Manganese superoxide dismutase modulates hypoxia-inducible factor-1 alpha induction via superoxide
    • S. Kaewpila, S. Venkataraman, G.R. Buettner, and L.W. Oberley Manganese superoxide dismutase modulates hypoxia-inducible factor-1 alpha induction via superoxide Cancer Res. 68 2008 2781 2788
    • (2008) Cancer Res. , vol.68 , pp. 2781-2788
    • Kaewpila, S.1    Venkataraman, S.2    Buettner, G.R.3    Oberley, L.W.4
  • 49
    • 79251582896 scopus 로고    scopus 로고
    • Redox control of GTPases: From molecular mechanisms to functional significance in health and disease
    • J. Heo Redox control of GTPases: from molecular mechanisms to functional significance in health and disease Antioxid. Redox Signal. 14 2011 689 724
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 689-724
    • Heo, J.1
  • 50
    • 84890120403 scopus 로고    scopus 로고
    • Sulfenic acid chemistry, detection and cellular lifetime
    • V. Gupta, and K.S. Carroll Sulfenic acid chemistry, detection and cellular lifetime Biochim. Biophys. Acta 1840 2014 847 875
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 847-875
    • Gupta, V.1    Carroll, K.S.2
  • 51
    • 77954221839 scopus 로고    scopus 로고
    • Redox chemistry of biological thiols
    • Fishbein, J. C., editor. New York: Elsevier
    • Nagy, P.; Winterbourn, C.C. Redox chemistry of biological thiols. In: Fishbein, J. C., editor. Adv. Mol. Toxicol. New York: Elsevier; 2010. p. 183-222.
    • (2010) Adv. Mol. Toxicol. , pp. 183-222
    • Nagy, P.1    Winterbourn, C.C.2
  • 52
    • 0029002385 scopus 로고
    • Kinetic factors that control the fate of thiyl radicals in cells
    • P. Wardman, and C. von Sonntag Kinetic factors that control the fate of thiyl radicals in cells Methods Enzymol. 251 1995 31 45
    • (1995) Methods Enzymol. , vol.251 , pp. 31-45
    • Wardman, P.1    Von Sonntag, C.2
  • 53
    • 84932168613 scopus 로고    scopus 로고
    • Radical scavenging by thiols and the fate of thiyl radicals
    • Jacob, U., Reichman, D., editors. Dordrecht: Springer
    • Winterbourn, C.C. Radical scavenging by thiols and the fate of thiyl radicals. In: Jacob, U., Reichman, D., editors. Oxidative stress and redox regulation. Dordrecht: Springer; 2013. p. 43-58.
    • (2013) Oxidative Stress and Redox Regulation , pp. 43-58
    • Winterbourn, C.C.1
  • 54
    • 0035844279 scopus 로고    scopus 로고
    • 2. Electron transfer between tyrosine 103 phenoxyl radical and cysteine 110 yields a protein-thiyl radical
    • 2. Electron transfer between tyrosine 103 phenoxyl radical and cysteine 110 yields a protein-thiyl radical J. Biol. Chem. 276 2001 16540 16547
    • (2001) J. Biol. Chem. , vol.276 , pp. 16540-16547
    • Witting, P.K.1    Mauk, A.G.2
  • 55
    • 47049096866 scopus 로고    scopus 로고
    • Mechanisms of protein damage induced by cysteine thiyl radical formation
    • C. Schoneich Mechanisms of protein damage induced by cysteine thiyl radical formation Chem. Res. Toxicol. 21 2008 1175 1179
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 1175-1179
    • Schoneich, C.1
  • 56
    • 80051698652 scopus 로고    scopus 로고
    • Superoxide induces endothelial nitric-oxide synthase protein thiyl radical formation, a novel mechanism regulating eNOS function and coupling
    • C.A. Chen, C.H. Lin, L.J. Druhan, T.Y. Wang, Y.R. Chen, and J.L. Zweier Superoxide induces endothelial nitric-oxide synthase protein thiyl radical formation, a novel mechanism regulating eNOS function and coupling J. Biol. Chem. 286 2011 29098 29107
    • (2011) J. Biol. Chem. , vol.286 , pp. 29098-29107
    • Chen, C.A.1    Lin, C.H.2    Druhan, L.J.3    Wang, T.Y.4    Chen, Y.R.5    Zweier, J.L.6
  • 57
    • 0026599052 scopus 로고
    • Oxidation of polyunsaturated fatty acids and lipids through thiyl and sulfonyl radicals: Reaction kinetics, and influence of oxygen and structure of thiyl radicals
    • C. Schöneich, U. Dillinger, F. von Bruchhausen, and K.D. Asmus Oxidation of polyunsaturated fatty acids and lipids through thiyl and sulfonyl radicals: Reaction kinetics, and influence of oxygen and structure of thiyl radicals Arch. Biochem. Biophys. 292 1992 456 467
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 456-467
    • Schöneich, C.1    Dillinger, U.2    Von Bruchhausen, F.3    Asmus, K.D.4
  • 58
    • 0027390329 scopus 로고
    • Superoxide as an intracellular radical sink
    • C.C. Winterbourn Superoxide as an intracellular radical sink Free Radic. Biol. Med. 14 1993 85 90
    • (1993) Free Radic. Biol. Med. , vol.14 , pp. 85-90
    • Winterbourn, C.C.1
  • 60
    • 0038015010 scopus 로고    scopus 로고
    • Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction
    • D.W. Starke, P.B. Chock, and J.J. Mieyal Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction J. Biol. Chem. 278 2003 14607 14613
    • (2003) J. Biol. Chem. , vol.278 , pp. 14607-14613
    • Starke, D.W.1    Chock, P.B.2    Mieyal, J.J.3
  • 61
    • 79957933470 scopus 로고    scopus 로고
    • Nitric oxide signaling: Classical, less classical, and nonclassical mechanisms
    • A. Martinez-Ruiz, S. Cadenas, and S. Lamas Nitric oxide signaling: classical, less classical, and nonclassical mechanisms Free Radic. Biol. Med. 51 2011 17 29
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 17-29
    • Martinez-Ruiz, A.1    Cadenas, S.2    Lamas, S.3
  • 62
    • 84872277775 scopus 로고    scopus 로고
    • Mechanisms of S-nitrosothiol formation and selectivity in nitric oxide signaling
    • B.C. Smith, and M.A. Marletta Mechanisms of S-nitrosothiol formation and selectivity in nitric oxide signaling Curr. Opin. Chem. Biol. 16 2012 498 506
    • (2012) Curr. Opin. Chem. Biol. , vol.16 , pp. 498-506
    • Smith, B.C.1    Marletta, M.A.2
  • 63
    • 47049113679 scopus 로고    scopus 로고
    • Protein cysteine thiol nitrosation: Maker or marker of reactive nitrogen species-induced nonerythroid cellular signaling?
    • J.R. Lancaster Jr. Protein cysteine thiol nitrosation: maker or marker of reactive nitrogen species-induced nonerythroid cellular signaling? Nitric Oxide 19 2008 68 72
    • (2008) Nitric Oxide , vol.19 , pp. 68-72
    • Lancaster, J.R.1
  • 64
    • 43849090222 scopus 로고    scopus 로고
    • Thiyl radicals react with nitric oxide to form S-nitrosothiols with rate constants near the diffusion-controlled limit
    • E. Madej, L.K. Folkes, P. Wardman, G. Czapski, and S. Goldstein Thiyl radicals react with nitric oxide to form S-nitrosothiols with rate constants near the diffusion-controlled limit Free Radic. Biol. Med. 44 2008 2013 2018
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 2013-2018
    • Madej, E.1    Folkes, L.K.2    Wardman, P.3    Czapski, G.4    Goldstein, S.5
  • 65
    • 33749005136 scopus 로고    scopus 로고
    • Nitroxidative, nitrosative, and nitrative stress: Kinetic predictions of reactive nitrogen species chemistry under biological conditions
    • J.R. Lancaster Jr. Nitroxidative, nitrosative, and nitrative stress: kinetic predictions of reactive nitrogen species chemistry under biological conditions Chem. Res. Toxicol. 19 2006 1160 1174
    • (2006) Chem. Res. Toxicol. , vol.19 , pp. 1160-1174
    • Lancaster, J.R.1
  • 66
    • 0037093679 scopus 로고    scopus 로고
    • Electron paramagnetic resonance spin trapping investigation into the kinetics of glutathione oxidation by the superoxide radical: Re-evaluation of the rate constant
    • C.M. Jones, A. Lawrence, P. Wardman, and M.J. Burkitt Electron paramagnetic resonance spin trapping investigation into the kinetics of glutathione oxidation by the superoxide radical: re-evaluation of the rate constant Free Radic. Biol. Med. 32 2002 982 990
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 982-990
    • Jones, C.M.1    Lawrence, A.2    Wardman, P.3    Burkitt, M.J.4
  • 67
    • 0001380631 scopus 로고
    • The reaction of superoxide radical anion with dithiothreitol: A chain process
    • N. Zhang, H.-P. Schuchmann, and C. von Sonntag The reaction of superoxide radical anion with dithiothreitol: a chain process J. Phys. Chem. 95 1991 4718 4722
    • (1991) J. Phys. Chem. , vol.95 , pp. 4718-4722
    • Zhang, N.1    Schuchmann, H.-P.2    Von Sonntag, C.3
  • 68
    • 0028114890 scopus 로고
    • The reaction of superoxide with reduced glutathione
    • C.C. Winterbourn, and D. Metodiewa The reaction of superoxide with reduced glutathione Arch. Biochem. Biophys. 314 1994 284 290
    • (1994) Arch. Biochem. Biophys. , vol.314 , pp. 284-290
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 69
    • 67650072766 scopus 로고    scopus 로고
    • Cysteine oxidation by the superoxide radical: A theoretical study
    • B. Cardey, and M. Enescu Cysteine oxidation by the superoxide radical: a theoretical study Chemphyschem 10 2009 1642 1648
    • (2009) Chemphyschem , vol.10 , pp. 1642-1648
    • Cardey, B.1    Enescu, M.2
  • 70
    • 84898959572 scopus 로고    scopus 로고
    • The basic biology of redoxosomes in cytokine-mediated signal transduction and implications for disease-specific therapies
    • N.Y. Spencer, and J.F. Engelhardt The basic biology of redoxosomes in cytokine-mediated signal transduction and implications for disease-specific therapies Biochemistry 53 2014 1551 1564
    • (2014) Biochemistry , vol.53 , pp. 1551-1564
    • Spencer, N.Y.1    Engelhardt, J.F.2
  • 71
    • 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 J. Biol. Chem. 274 1999 34543 34546
    • (1999) J. Biol. Chem. , vol.274 , 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
  • 72
    • 84893874904 scopus 로고    scopus 로고
    • Peroxynitrite induced mitochondrial biogenesis following MnSOD knockdown in normal rat kidney (NRK) cells
    • A. Marine, K.J. Krager, N. Aykin-Burns, and L.A. Macmillan-Crow Peroxynitrite induced mitochondrial biogenesis following MnSOD knockdown in normal rat kidney (NRK) cells Redox Biol 2 2014 348 357
    • (2014) Redox Biol , vol.2 , pp. 348-357
    • Marine, A.1    Krager, K.J.2    Aykin-Burns, N.3    Macmillan-Crow, L.A.4
  • 73
    • 83455170695 scopus 로고    scopus 로고
    • Nitric oxide-derived oxidants with a focus on peroxynitrite: Molecular targets, cellular responses and therapeutic implications
    • P. Calcerrada, G. Peluffo, and R. Radi Nitric oxide-derived oxidants with a focus on peroxynitrite: molecular targets, cellular responses and therapeutic implications Curr. Pharm. Des 17 2011 3905 3932
    • (2011) Curr. Pharm. Des , vol.17 , pp. 3905-3932
    • Calcerrada, P.1    Peluffo, G.2    Radi, R.3
  • 74
    • 84890124303 scopus 로고    scopus 로고
    • Kinetic and mechanistic considerations to assess the biological fate of peroxynitrite
    • S. Carballal, S. Bartesaghi, and R. Radi Kinetic and mechanistic considerations to assess the biological fate of peroxynitrite Biochim. Biophys. Acta 1840 2014 768 780
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 768-780
    • Carballal, S.1    Bartesaghi, S.2    Radi, R.3
  • 75
    • 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 Arch. Biochem. Biophys. 422 2004 119 124
    • (2004) Arch. Biochem. Biophys. , vol.422 , pp. 119-124
    • Stone, J.R.1
  • 76
    • 0012017460 scopus 로고
    • The steady state level of catalase compound I in isolated hemoglobin-free perfused rat liver
    • H. Sies, and B. Chance The steady state level of catalase compound I in isolated hemoglobin-free perfused rat liver FEBS Lett. 11 1970 172 176
    • (1970) FEBS Lett. , vol.11 , pp. 172-176
    • Sies, H.1    Chance, B.2


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