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Volumn 80, Issue , 2015, Pages 148-157

The basics of thiols and cysteines in redox biology and chemistry

Author keywords

Cysteine; Free radicals; Redox potential; Redox regulation; Thiols pKa

Indexed keywords

AMINO ACID; CYSTEINE; CYSTEINE DERIVATIVE; DISULFIDE; THIOL DERIVATIVE; THIOL GROUP; FREE RADICAL; GLUTATHIONE; OXIDOREDUCTASE;

EID: 84923919258     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.11.013     Document Type: Review
Times cited : (731)

References (138)
  • 1
    • 0014143854 scopus 로고
    • Comparison of the chemical properties of selenocysteine and selenocystine with their sulfur analogs
    • R.E. Huber, and R.S. Criddle Comparison of the chemical properties of selenocysteine and selenocystine with their sulfur analogs Arch. Biochem. Biophys. 122 1967 164 173
    • (1967) Arch. Biochem. Biophys. , vol.122 , pp. 164-173
    • Huber, R.E.1    Criddle, R.S.2
  • 2
    • 35348902569 scopus 로고    scopus 로고
    • Selenium in chemistry and biochemistry in comparison to sulfur
    • L.A. Wessjohann, A. Schneider, M. Abbas, and W. Brandt Selenium in chemistry and biochemistry in comparison to sulfur Biol. Chem. 388 2007 997 1006
    • (2007) Biol. Chem. , vol.388 , pp. 997-1006
    • Wessjohann, L.A.1    Schneider, A.2    Abbas, M.3    Brandt, W.4
  • 3
    • 33846635882 scopus 로고    scopus 로고
    • High-throughput identification of catalytic redox-active cysteine residues
    • D.E. Fomenko, W. Xing, B.M. Adair, D.J. Thomas, and V.N. Gladyshev High-throughput identification of catalytic redox-active cysteine residues Science 315 2007 387 389
    • (2007) Science , vol.315 , pp. 387-389
    • Fomenko, D.E.1    Xing, W.2    Adair, B.M.3    Thomas, D.J.4    Gladyshev, V.N.5
  • 4
    • 77952563903 scopus 로고    scopus 로고
    • Selenoproteins - What unique properties can arise with selenocysteine in place of cysteine?
    • E.S. Arner Selenoproteins - what unique properties can arise with selenocysteine in place of cysteine? Exp. Cell Res. 316 2010 1296 1303
    • (2010) Exp. Cell Res. , vol.316 , pp. 1296-1303
    • Arner, E.S.1
  • 5
    • 77954221839 scopus 로고    scopus 로고
    • Redox chemistry of biological thiols
    • J.C. Fishbein, editor. Elsevier San Diego
    • P. Nagy, and C.C. Winterbourn Redox chemistry of biological thiols J.C. Fishbein, editor. Advances in Molecular Toxicology 2010 Elsevier San Diego 183 222
    • (2010) Advances in Molecular Toxicology , pp. 183-222
    • Nagy, P.1    Winterbourn, C.C.2
  • 6
    • 84875715041 scopus 로고    scopus 로고
    • Glutathione analogs in prokaryotes
    • R.C. Fahey Glutathione analogs in prokaryotes Biochim. Biophys. Acta 1830 2013 3182 3198
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3182-3198
    • Fahey, R.C.1
  • 8
    • 0035219754 scopus 로고    scopus 로고
    • Biosynthesis of the methanogenic cofactors
    • R.H. White Biosynthesis of the methanogenic cofactors Vitam. Horm. 61 2001 299 337
    • (2001) Vitam. Horm. , vol.61 , pp. 299-337
    • White, R.H.1
  • 9
    • 78649529306 scopus 로고    scopus 로고
    • Cysteine function governs its conservation and degeneration and restricts its utilization on protein surfaces
    • S.M. Marino, and V.N. Gladyshev Cysteine function governs its conservation and degeneration and restricts its utilization on protein surfaces J. Mol. Biol. 404 2010 902 916
    • (2010) J. Mol. Biol. , vol.404 , pp. 902-916
    • Marino, S.M.1    Gladyshev, V.N.2
  • 10
    • 0018784438 scopus 로고
    • Surface and inside volumes in globular proteins
    • J. Janin Surface and inside volumes in globular proteins Nature 277 1979 491 492
    • (1979) Nature , vol.277 , pp. 491-492
    • Janin, J.1
  • 11
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte, and R.F. Doolittle A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157 1982 105 132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 14
    • 0028886558 scopus 로고
    • Ionisation of cysteine residues at the termini of model alpha-helical peptides: Relevance to unusual thiol pKa values in proteins of the thioredoxin family
    • T. Kortemme, and T.E. Creighton Ionisation of cysteine residues at the termini of model alpha-helical peptides: relevance to unusual thiol pKa values in proteins of the thioredoxin family J. Mol. Biol. 253 1995 799 812
    • (1995) J. Mol. Biol. , vol.253 , pp. 799-812
    • Kortemme, T.1    Creighton, T.E.2
  • 16
    • 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 J. Mol. Biol. 402 2010 194 209
    • (2010) J. Mol. Biol. , vol.402 , pp. 194-209
    • Hall, A.1    Parsonage, D.2    Poole, L.B.3    Karplus, P.A.4
  • 17
    • 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 Radic. Biol. Med. 27 1999 322 328
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 322-328
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 19
    • 23244466487 scopus 로고    scopus 로고
    • Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin
    • D. Parsonage, D.S. Youngblood, G.N. Sarma, Z.A. Wood, P.A. Karplus, and L.B. Poole Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin Biochemistry 44 2005 10583 10592
    • (2005) Biochemistry , vol.44 , pp. 10583-10592
    • Parsonage, D.1    Youngblood, D.S.2    Sarma, G.N.3    Wood, Z.A.4    Karplus, P.A.5    Poole, L.B.6
  • 20
    • 84875712387 scopus 로고    scopus 로고
    • Kinetics and mechanisms of thiol-disulfide exchange covering direct substitution and thiol oxidation-mediated pathways
    • P. Nagy Kinetics and mechanisms of thiol-disulfide exchange covering direct substitution and thiol oxidation-mediated pathways Antioxid. Redox Signaling 18 2013 1623 1641
    • (2013) Antioxid. Redox Signaling , vol.18 , pp. 1623-1641
    • Nagy, P.1
  • 21
    • 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
  • 22
    • 84857833776 scopus 로고    scopus 로고
    • Cell signalling by reactive lipid species: New concepts and molecular mechanisms
    • A. Higdon, A.R. Diers, J.Y. Oh, A. Landar, and V.M. Darley-Usmar Cell signalling by reactive lipid species: new concepts and molecular mechanisms Biochem. J. 442 2012 453 464
    • (2012) Biochem. J. , vol.442 , pp. 453-464
    • Higdon, A.1    Diers, A.R.2    Oh, J.Y.3    Landar, A.4    Darley-Usmar, V.M.5
  • 23
    • 84890128084 scopus 로고    scopus 로고
    • Quantification of thiols and disulfides
    • J.R. Winther, and C. Thorpe Quantification of thiols and disulfides Biochim. Biophys. Acta 1840 2014 838 846
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 838-846
    • Winther, J.R.1    Thorpe, C.2
  • 24
    • 84924045221 scopus 로고    scopus 로고
    • Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats
    • in press
    • N.O. Devarie Baez, J.A. Reisz, and C.M. Furdui Mass spectrometry in studies of protein thiol chemistry and signaling: opportunities and caveats Free Radic. Biol. Med. 2014 (in press), 10.1016/j.freeradbiomed.2014.09.016
    • (2014) Free Radic. Biol. Med.
    • Devarie Baez, N.O.1    Reisz, J.A.2    Furdui, C.M.3
  • 27
    • 77955048966 scopus 로고    scopus 로고
    • Methods for detection and measurement of hydrogen peroxide inside and outside of cells
    • S.G. Rhee, T.S. Chang, W. Jeong, and D. Kang Methods for detection and measurement of hydrogen peroxide inside and outside of cells Mol. Cells 29 2010 539 549
    • (2010) Mol. Cells , vol.29 , pp. 539-549
    • Rhee, S.G.1    Chang, T.S.2    Jeong, W.3    Kang, D.4
  • 28
    • 84880105471 scopus 로고    scopus 로고
    • Cysteine-mediated redox signaling: Chemistry, biology, and tools for discovery
    • C.E. Paulsen, and K.S. Carroll Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery Chem. Rev. 113 2013 4633 4679
    • (2013) Chem. Rev. , vol.113 , pp. 4633-4679
    • Paulsen, C.E.1    Carroll, K.S.2
  • 30
    • 0031033048 scopus 로고    scopus 로고
    • Influence of acidic residues and the kink in the active-site helix on the properties of the disulfide oxidoreductase DsbA
    • J. Hennecke, C. Spleiss, and R. Glockshuber Influence of acidic residues and the kink in the active-site helix on the properties of the disulfide oxidoreductase DsbA J. Biol. Chem. 272 1997 189 195
    • (1997) J. Biol. Chem. , vol.272 , pp. 189-195
    • Hennecke, J.1    Spleiss, C.2    Glockshuber, R.3
  • 31
    • 0029832481 scopus 로고    scopus 로고
    • Studies on the enhancement of the reactivity of the (Cys-25)-S-/(His159)-Im+H ion-pair of papain by deprotonation across pKa 4
    • S. Pinitglang, M. Noble, C. Verma, E.W. Thomas, and K. Brocklehurst Studies on the enhancement of the reactivity of the (Cys-25)-S-/(His159)-Im+H ion-pair of papain by deprotonation across pKa 4 Biochem. Soc. Trans. 24 1996 468S
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 468S
    • Pinitglang, S.1    Noble, M.2    Verma, C.3    Thomas, E.W.4    Brocklehurst, K.5
  • 32
    • 0031024788 scopus 로고    scopus 로고
    • Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: Structural and functional characterization of mutants of Asp 26 and Lys 57
    • H.J. Dyson, M.F. Jeng, L.L. Tennant, I. Slaby, M. Lindell, D.S. Cui, S. Kuprin, and A. Holmgren Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: structural and functional characterization of mutants of Asp 26 and Lys 57 Biochemistry 36 1997 2622 2636
    • (1997) Biochemistry , vol.36 , pp. 2622-2636
    • Dyson, H.J.1    Jeng, M.F.2    Tennant, L.L.3    Slaby, I.4    Lindell, M.5    Cui, D.S.6    Kuprin, S.7    Holmgren, A.8
  • 34
    • 0001317229 scopus 로고
    • Rates of thiol-disulfide interchange reactions between mono- and dithiols and Ellman's reagent
    • G.M. Whitesides, J.E. Liburn, and R.P. Szajewski Rates of thiol-disulfide interchange reactions between mono- and dithiols and Ellman's reagent J. Org. Chem. 42 1977 332 338
    • (1977) J. Org. Chem. , vol.42 , pp. 332-338
    • Whitesides, G.M.1    Liburn, J.E.2    Szajewski, R.P.3
  • 35
    • 0001494424 scopus 로고
    • Structure-reactivity correlations for the thiol-disulfide interchange reaction
    • J.M. Wilson, R.J. Bayer, and D.J. Hupe Structure-reactivity correlations for the thiol-disulfide interchange reaction J. Am. Chem. Soc. 99 1977 7922 7926
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 7922-7926
    • Wilson, J.M.1    Bayer, R.J.2    Hupe, D.J.3
  • 37
    • 0013506276 scopus 로고
    • The sulfhydryl groups of crystalline proteins. I. Some albumins, enzymes, and hemoglobins
    • R.E. Benesch, H.A. Lardy, and R. Benesch The sulfhydryl groups of crystalline proteins. I. Some albumins, enzymes, and hemoglobins J. Biol. Chem. 216 1955 663 676
    • (1955) J. Biol. Chem. , vol.216 , pp. 663-676
    • Benesch, R.E.1    Lardy, H.A.2    Benesch, R.3
  • 38
    • 0030446158 scopus 로고    scopus 로고
    • Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase
    • T. Kortemme, N.J. Darby, and T.E. Creighton Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase Biochemistry 35 1996 14503 14511
    • (1996) Biochemistry , vol.35 , pp. 14503-14511
    • Kortemme, T.1    Darby, N.J.2    Creighton, T.E.3
  • 40
    • 0039714219 scopus 로고    scopus 로고
    • Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol-disulfide oxidoreductases
    • E. Mössner, M. Huber-Wunderlich, and R. Glockshuber Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol-disulfide oxidoreductases Prot. Sci. 7 1998 1233 1244
    • (1998) Prot. Sci. , vol.7 , pp. 1233-1244
    • Mössner, E.1    Huber-Wunderlich, M.2    Glockshuber, R.3
  • 41
    • 0028360184 scopus 로고
    • Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo
    • J.W. Nelson, and T.E. Creighton Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo Biochemistry 33 1994 5974 5983
    • (1994) Biochemistry , vol.33 , pp. 5974-5983
    • Nelson, J.W.1    Creighton, T.E.2
  • 43
    • 33845917628 scopus 로고    scopus 로고
    • Reactions of yeast thioredoxin peroxidases i and II with hydrogen peroxide and peroxynitrite: Rate constants by competitive kinetics
    • R. Ogusucu, D. Rettori, D.C. Munhoz, L.E. Soares Netto, and O. Augusto Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: rate constants by competitive kinetics Free Radic. Biol. Med. 42 2007 326 334
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 326-334
    • Ogusucu, R.1    Rettori, D.2    Munhoz, D.C.3    Soares Netto, L.E.4    Augusto, O.5
  • 47
    • 80054771975 scopus 로고    scopus 로고
    • Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin
    • S.A. Reeves, D. Parsonage, K.J. Nelson, and L.B. Poole Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin Biochemistry 50 2011 8970 8981
    • (2011) Biochemistry , vol.50 , pp. 8970-8981
    • Reeves, S.A.1    Parsonage, D.2    Nelson, K.J.3    Poole, L.B.4
  • 48
    • 84875709337 scopus 로고    scopus 로고
    • The fairytale of the GSSG/GSH redox potential
    • L. Flohe The fairytale of the GSSG/GSH redox potential Biochim. Biophys. Acta 1830 2013 3139 3142
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3139-3142
    • Flohe, L.1
  • 49
    • 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
  • 50
    • 84924179685 scopus 로고    scopus 로고
    • Oxidative protein folding: From thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum
    • in press
    • D.A. Hudson, S.A. Gannon, and C. Thorpe Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum Free Radic. Biol. Med. 2014 (in press), 10.1016/j.freeradbiomed.2014.07.037
    • (2014) Free Radic. Biol. Med.
    • Hudson, D.A.1    Gannon, S.A.2    Thorpe, C.3
  • 51
    • 0037646517 scopus 로고    scopus 로고
    • Catalytic mechanism of thiol peroxidase from Escherichia coli: Sulfenic acid formation and overoxidation of essential CYS61
    • L.M. Baker, and L.B. Poole Catalytic mechanism of thiol peroxidase from Escherichia coli: sulfenic acid formation and overoxidation of essential CYS61 J. Biol. Chem. 278 2003 9203 9211
    • (2003) J. Biol. Chem. , vol.278 , pp. 9203-9211
    • Baker, L.M.1    Poole, L.B.2
  • 52
    • 84893738731 scopus 로고    scopus 로고
    • Chemical approaches to detect and analyze protein sulfenic acids
    • C.M. Furdui, and L.B. Poole Chemical approaches to detect and analyze protein sulfenic acids Mass Spectrom. Rev. 33 2014 126 146
    • (2014) Mass Spectrom. Rev. , vol.33 , pp. 126-146
    • Furdui, C.M.1    Poole, L.B.2
  • 53
    • 84888301385 scopus 로고    scopus 로고
    • Thiol-blocking electrophiles interfere with labeling and detection of protein sulfenic acids
    • J.A. Reisz, E. Bechtold, S.B. King, L.B. Poole, and C.M. Furdui Thiol-blocking electrophiles interfere with labeling and detection of protein sulfenic acids FEBS J. 280 2013 6150 6161
    • (2013) FEBS J. , vol.280 , pp. 6150-6161
    • Reisz, J.A.1    Bechtold, E.2    King, S.B.3    Poole, L.B.4    Furdui, C.M.5
  • 55
    • 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
  • 57
    • 79951906200 scopus 로고    scopus 로고
    • Thiol-based redox switches and gene regulation
    • H. Antelmann, and J.D. Helmann Thiol-based redox switches and gene regulation Antioxid. Redox Signaling 14 2011 1049 1063
    • (2011) Antioxid. Redox Signaling , vol.14 , pp. 1049-1063
    • Antelmann, H.1    Helmann, J.D.2
  • 58
    • 0024339293 scopus 로고
    • The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid
    • L.B. Poole, and A. Claiborne The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid J. Biol. Chem. 264 1989 12330 12338
    • (1989) J. Biol. Chem. , vol.264 , pp. 12330-12338
    • Poole, L.B.1    Claiborne, A.2
  • 59
    • 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, L.E. Netto, B. Alvarez, R. Radi, and M. Trujillo Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: kinetics, acidity constants, and conformational dynamics Biochemistry 48 2009 9416 9426
    • (2009) Biochemistry , vol.48 , pp. 9416-9426
    • Hugo, M.1    Turell, L.2    Manta, B.3    Botti, H.4    Monteiro, G.5    Netto, L.E.6    Alvarez, B.7    Radi, R.8    Trujillo, M.9
  • 60
    • 84877886960 scopus 로고    scopus 로고
    • Hyperoxidation of peroxiredoxins 2 and 3: Rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine
    • A.V. Peskin, N. Dickerhof, R.A. Poynton, L.N. Paton, P.E. Pace, M.B. Hampton, and C.C. Winterbourn Hyperoxidation of peroxiredoxins 2 and 3: rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine J. Biol. Chem. 288 2013 14170 14177
    • (2013) J. Biol. Chem. , vol.288 , pp. 14170-14177
    • Peskin, A.V.1    Dickerhof, N.2    Poynton, R.A.3    Paton, L.N.4    Pace, P.E.5    Hampton, M.B.6    Winterbourn, C.C.7
  • 61
    • 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 2003 980 984
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 62
    • 20544438121 scopus 로고    scopus 로고
    • Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxin
    • T.J. Jönsson, M.S. Murray, L.C. Johnson, L.B. Poole, and W.T. Lowther Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxin Biochemistry 44 2005 8634 8642
    • (2005) Biochemistry , vol.44 , pp. 8634-8642
    • Jönsson, T.J.1    Murray, M.S.2    Johnson, L.C.3    Poole, L.B.4    Lowther, W.T.5
  • 63
    • 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, K. Kim, and S.G. Rhee Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation Science 300 2003 653 656
    • (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
  • 64
    • 0027131771 scopus 로고
    • Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation
    • A. Claiborne, H. Miller, D. Parsonage, and R.P. Ross Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation FASEB J. 7 1993 1483 1490
    • (1993) FASEB J. , vol.7 , pp. 1483-1490
    • Claiborne, A.1    Miller, H.2    Parsonage, D.3    Ross, R.P.4
  • 66
    • 0037373455 scopus 로고    scopus 로고
    • Endogenous generation of reactive oxidants and electrophiles and their reactions with DNA and protein
    • L.J. Marnett, J.N. Riggins, and J.D. West Endogenous generation of reactive oxidants and electrophiles and their reactions with DNA and protein J. Clin. Invest. 111 2003 583 593
    • (2003) J. Clin. Invest. , vol.111 , pp. 583-593
    • Marnett, L.J.1    Riggins, J.N.2    West, J.D.3
  • 68
    • 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
  • 69
    • 77953442398 scopus 로고    scopus 로고
    • Forgotten radicals in biology
    • R. Luc, and C. Vergely Forgotten radicals in biology Int. J. Biomed. Sci. 4 2008 255 259
    • (2008) Int. J. Biomed. Sci. , vol.4 , pp. 255-259
    • Luc, R.1    Vergely, C.2
  • 70
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • B. Chance, H. Sies, and A. Boveris Hydroperoxide metabolism in mammalian organs Physiol. Rev. 59 1979 527 605
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 71
    • 77956207316 scopus 로고    scopus 로고
    • Changing paradigms in thiology from antioxidant defense toward redox regulation
    • L. Flohé Changing paradigms in thiology from antioxidant defense toward redox regulation Methods Enzymol. 473 2010 1 39
    • (2010) Methods Enzymol. , vol.473 , pp. 1-39
    • Flohé, L.1
  • 72
    • 84897019491 scopus 로고    scopus 로고
    • Nox enzymes and new thinking on reactive oxygen: A double-edged sword revisited
    • J.D. Lambeth, and A.S. Neish Nox enzymes and new thinking on reactive oxygen: a double-edged sword revisited Annu. Rev. Pathol. 9 2014 119 145
    • (2014) Annu. Rev. Pathol. , vol.9 , pp. 119-145
    • Lambeth, J.D.1    Neish, A.S.2
  • 73
    • 47749151450 scopus 로고    scopus 로고
    • Biological roles for the NOX family NADPH oxidases
    • W.M. Nauseef Biological roles for the NOX family NADPH oxidases J. Biol. Chem. 283 2008 16961 16965
    • (2008) J. Biol. Chem. , vol.283 , pp. 16961-16965
    • Nauseef, W.M.1
  • 74
    • 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 Signaling 10 2008 1199 1234
    • (2008) Antioxid. Redox Signaling , vol.10 , pp. 1199-1234
    • Davies, M.J.1    Hawkins, C.L.2    Pattison, D.I.3    Rees, M.D.4
  • 76
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • P. Pacher, J.S. Beckman, and L. Liaudet Nitric oxide and peroxynitrite in health and disease Physiol. Rev. 87 2007 315 424
    • (2007) Physiol. Rev. , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 77
    • 36448943959 scopus 로고    scopus 로고
    • Oxidation of 2-Cys-peroxiredoxins by arachidonic acid peroxide metabolites of lipoxygenases and cyclooxygenase-2
    • P. Cordray, K. Doyle, K. Edes, P.J. Moos, and F.A. Fitzpatrick Oxidation of 2-Cys-peroxiredoxins by arachidonic acid peroxide metabolites of lipoxygenases and cyclooxygenase-2 J. Biol. Chem. 282 2007 32623 32629
    • (2007) J. Biol. Chem. , vol.282 , pp. 32623-32629
    • Cordray, P.1    Doyle, K.2    Edes, K.3    Moos, P.J.4    Fitzpatrick, F.A.5
  • 78
    • 9744232974 scopus 로고    scopus 로고
    • Bacterial defenses against oxidants: Mechanistic features of cysteine-based peroxidases and their flavoprotein reductases
    • L.B. Poole Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases Arch. Biochem. Biophys. 433 2005 240 254
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 240-254
    • Poole, L.B.1
  • 79
    • 0033771859 scopus 로고    scopus 로고
    • AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase
    • L.B. Poole, C.M. Reynolds, Z.A. Wood, P.A. Karplus, H.R. Ellis, and M. Li Calzi AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase Eur. J. Biochem. 267 2000 6126 6133
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6126-6133
    • Poole, L.B.1    Reynolds, C.M.2    Wood, Z.A.3    Karplus, P.A.4    Ellis, H.R.5    Li Calzi, M.6
  • 81
    • 49349112856 scopus 로고    scopus 로고
    • Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism
    • R.L. Krauth-Siegel, and M.A. Comini Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism Biochim. Biophys. Acta 1780 2008 1236 1248
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1236-1248
    • Krauth-Siegel, R.L.1    Comini, M.A.2
  • 82
    • 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
    • C.M. Reynolds, J. Meyer, and L.B. Poole 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 2002 1990 2001
    • (2002) Biochemistry , vol.41 , pp. 1990-2001
    • Reynolds, C.M.1    Meyer, J.2    Poole, L.B.3
  • 84
    • 84904720579 scopus 로고    scopus 로고
    • Thioredoxin and glutaredoxin-mediated redox regulation of ribonucleotide reductase
    • R. Sengupta, and A. Holmgren Thioredoxin and glutaredoxin-mediated redox regulation of ribonucleotide reductase World J. Biol. Chem. 5 2014 68 74
    • (2014) World J. Biol. Chem. , vol.5 , pp. 68-74
    • Sengupta, R.1    Holmgren, A.2
  • 85
    • 33744962865 scopus 로고    scopus 로고
    • Redefining oxidative stress
    • D.P. Jones Redefining oxidative stress Antioxid. Redox Signaling 8 2006 1865 1879
    • (2006) Antioxid. Redox Signaling , vol.8 , pp. 1865-1879
    • Jones, D.P.1
  • 86
    • 33744543755 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae proteome of oxidized protein thiols: Contrasted functions for the thioredoxin and glutathione pathways
    • N. Le Moan, G. Clement, S. Le Maout, F. Tacnet, and M.B. Toledano The Saccharomyces cerevisiae proteome of oxidized protein thiols: contrasted functions for the thioredoxin and glutathione pathways J. Biol. Chem. 281 2006 10420 10430
    • (2006) J. Biol. Chem. , vol.281 , pp. 10420-10430
    • Le Moan, N.1    Clement, G.2    Le Maout, S.3    Tacnet, F.4    Toledano, M.B.5
  • 88
    • 49349085256 scopus 로고    scopus 로고
    • Redox compartmentalization in eukaryotic cells
    • Y.M. Go, and D.P. Jones Redox compartmentalization in eukaryotic cells Biochim. Biophys. Acta 1780 2008 1273 1290
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1273-1290
    • Go, Y.M.1    Jones, D.P.2
  • 89
    • 77956312086 scopus 로고    scopus 로고
    • Structure, function, and mechanism of thioredoxin proteins
    • J.F. Collet, and J. Messens Structure, function, and mechanism of thioredoxin proteins Antioxid. Redox Signaling 13 2010 1205 1216
    • (2010) Antioxid. Redox Signaling , vol.13 , pp. 1205-1216
    • Collet, J.F.1    Messens, J.2
  • 90
    • 64549106959 scopus 로고    scopus 로고
    • Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation
    • M.M. Gallogly, D.W. Starke, and J.J. Mieyal Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation Antioxid. Redox Signaling 11 2009 1059 1081
    • (2009) Antioxid. Redox Signaling , vol.11 , pp. 1059-1081
    • Gallogly, M.M.1    Starke, D.W.2    Mieyal, J.J.3
  • 92
    • 79953709713 scopus 로고    scopus 로고
    • Novel regulators in photosynthetic redox control of plant metabolism and gene expression
    • K.J. Dietz, and T. Pfannschmidt Novel regulators in photosynthetic redox control of plant metabolism and gene expression Plant Physiol. 155 2011 1477 1485
    • (2011) Plant Physiol. , vol.155 , pp. 1477-1485
    • Dietz, K.J.1    Pfannschmidt, T.2
  • 93
    • 84879047011 scopus 로고    scopus 로고
    • Cellular metabolic and autophagic pathways: Traffic control by redox signaling
    • M. Dodson, V. Darley-Usmar, and J. Zhang Cellular metabolic and autophagic pathways: traffic control by redox signaling Free Radic. Biol. Med. 63 2013 207 221
    • (2013) Free Radic. Biol. Med. , vol.63 , pp. 207-221
    • Dodson, M.1    Darley-Usmar, V.2    Zhang, J.3
  • 94
    • 84868603203 scopus 로고    scopus 로고
    • Peroxide-sensing transcriptional regulators in bacteria
    • J.M. Dubbs, and S. Mongkolsuk Peroxide-sensing transcriptional regulators in bacteria J. Bacteriol. 194 2012 5495 5503
    • (2012) J. Bacteriol. , vol.194 , pp. 5495-5503
    • Dubbs, J.M.1    Mongkolsuk, S.2
  • 95
    • 79957992260 scopus 로고    scopus 로고
    • Peroxide stress elicits adaptive changes in bacterial metal ion homeostasis
    • M.J. Faulkner, and J.D. Helmann Peroxide stress elicits adaptive changes in bacterial metal ion homeostasis Antioxid. Redox Signaling 15 2011 175 189
    • (2011) Antioxid. Redox Signaling , vol.15 , pp. 175-189
    • Faulkner, M.J.1    Helmann, J.D.2
  • 96
    • 84897114854 scopus 로고    scopus 로고
    • Oxidative stress sensing by the iron-sulfur cluster in the transcription factor, SoxR
    • K. Kobayashi, M. Fujikawa, and T. Kozawa Oxidative stress sensing by the iron-sulfur cluster in the transcription factor, SoxR J. Inorg. Biochem. 133 2014 87 91
    • (2014) J. Inorg. Biochem. , vol.133 , pp. 87-91
    • Kobayashi, K.1    Fujikawa, M.2    Kozawa, T.3
  • 97
    • 69949138465 scopus 로고    scopus 로고
    • Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus
    • C.B. Poor, P.R. Chen, E. Duguid, P.A. Rice, and C. He Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus J. Biol. Chem. 284 2009 23517 23524
    • (2009) J. Biol. Chem. , vol.284 , pp. 23517-23524
    • Poor, C.B.1    Chen, P.R.2    Duguid, E.3    Rice, P.A.4    He, C.5
  • 100
    • 77954935933 scopus 로고    scopus 로고
    • A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses
    • N.J. Adimora, D.P. Jones, and M.L. Kemp A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses Antioxid. Redox Signaling 13 2010 731 743
    • (2010) Antioxid. Redox Signaling , vol.13 , pp. 731-743
    • Adimora, N.J.1    Jones, D.P.2    Kemp, M.L.3
  • 101
    • 84899867980 scopus 로고    scopus 로고
    • Integrated redox proteomics and metabolomics of mitochondria to identify mechanisms of cd toxicity
    • Y.M. Go, J.R. Roede, M. Orr, Y. Liang, and D.P. Jones Integrated redox proteomics and metabolomics of mitochondria to identify mechanisms of cd toxicity Toxicol. Sci. 139 2014 59 73
    • (2014) Toxicol. Sci. , vol.139 , pp. 59-73
    • Go, Y.M.1    Roede, J.R.2    Orr, M.3    Liang, Y.4    Jones, D.P.5
  • 102
    • 84884179284 scopus 로고    scopus 로고
    • The redox proteome
    • Y.M. Go, and D.P. Jones The redox proteome J. Biol. Chem. 288 2013 26512 26520
    • (2013) J. Biol. Chem. , vol.288 , pp. 26512-26520
    • Go, Y.M.1    Jones, D.P.2
  • 103
  • 104
    • 84866272849 scopus 로고    scopus 로고
    • Quantitative in vivo redox sensors uncover oxidative stress as an early event in life
    • D. Knoefler, M. Thamsen, M. Koniczek, N.J. Niemuth, A.K. Diederich, and U. Jakob Quantitative in vivo redox sensors uncover oxidative stress as an early event in life Mol. Cell 47 2012 767 776
    • (2012) Mol. Cell , vol.47 , pp. 767-776
    • Knoefler, D.1    Thamsen, M.2    Koniczek, M.3    Niemuth, N.J.4    Diederich, A.K.5    Jakob, U.6
  • 106
    • 70349284540 scopus 로고    scopus 로고
    • Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells
    • S.E. Leonard, K.G. Reddie, and K.S. Carroll Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells ACS Chem. Biol. 4 2009 783 799
    • (2009) ACS Chem. Biol. , vol.4 , pp. 783-799
    • Leonard, S.E.1    Reddie, K.G.2    Carroll, K.S.3
  • 109
    • 75749123115 scopus 로고    scopus 로고
    • Orchestrating redox signaling networks through regulatory cysteine switches
    • C.E. Paulsen, and K.S. Carroll Orchestrating redox signaling networks through regulatory cysteine switches ACS Chem. Biol. 5 2010 47 62
    • (2010) ACS Chem. Biol. , vol.5 , pp. 47-62
    • Paulsen, C.E.1    Carroll, K.S.2
  • 111
    • 0016256290 scopus 로고
    • The inactivation of the acyl phosphatase activity catalyzed by the sulfenic acid form of glyceraldehyde 3-phosphate dehydrogenase by dimedone and olefins
    • L.V. Benitez, and W.S. Allison The inactivation of the acyl phosphatase activity catalyzed by the sulfenic acid form of glyceraldehyde 3-phosphate dehydrogenase by dimedone and olefins J. Biol. Chem. 249 1974 6234 6243
    • (1974) J. Biol. Chem. , vol.249 , pp. 6234-6243
    • Benitez, L.V.1    Allison, W.S.2
  • 112
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • H. Choi, S. Kim, P. Mukhopadhyay, S. Cho, J. Woo, G. Storz, and S. Ryu Structural basis of the redox switch in the OxyR transcription factor Cell 105 2001 103 113
    • (2001) Cell , vol.105 , pp. 103-113
    • Choi, H.1    Kim, S.2    Mukhopadhyay, P.3    Cho, S.4    Woo, J.5    Storz, G.6    Ryu, S.7
  • 114
  • 117
    • 84870199000 scopus 로고    scopus 로고
    • Nox4- and Nox2-dependent oxidant production is required for VEGF-induced SERCA cysteine-674 S-glutathiolation and endothelial cell migration
    • A.M. Evangelista, M.D. Thompson, V.M. Bolotina, X. Tong, and R.A. Cohen Nox4- and Nox2-dependent oxidant production is required for VEGF-induced SERCA cysteine-674 S-glutathiolation and endothelial cell migration Free Radic. Biol. Med. 53 2012 2327 2334
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 2327-2334
    • Evangelista, A.M.1    Thompson, M.D.2    Bolotina, V.M.3    Tong, X.4    Cohen, R.A.5
  • 118
    • 0035798684 scopus 로고    scopus 로고
    • Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7): A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase
    • X. Fu, S.Y. Kassim, W.C. Parks, and J.W. Heinecke Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7): a mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase J. Biol. Chem. 276 2001 41279 41287
    • (2001) J. Biol. Chem. , vol.276 , pp. 41279-41287
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 120
    • 34447623403 scopus 로고    scopus 로고
    • Characterization by tandem mass spectrometry of stable cysteine sulfenic acid in a cysteine switch peptide of matrix metalloproteinases
    • V. Shetty, D.S. Spellman, and T.A. Neubert Characterization by tandem mass spectrometry of stable cysteine sulfenic acid in a cysteine switch peptide of matrix metalloproteinases J. Am. Soc. Mass Spectrom. 18 2007 1544 1551
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 1544-1551
    • Shetty, V.1    Spellman, D.S.2    Neubert, T.A.3
  • 122
    • 70350043513 scopus 로고    scopus 로고
    • Structural basis for catalytic activation of thiocyanate hydrolase involving metal-ligated cysteine modification
    • T. Arakawa, Y. Kawano, Y. Katayama, H. Nakayama, N. Dohmae, M. Yohda, and M. Odaka Structural basis for catalytic activation of thiocyanate hydrolase involving metal-ligated cysteine modification J. Am. Chem. Soc. 131 2009 14838 14843
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 14838-14843
    • Arakawa, T.1    Kawano, Y.2    Katayama, Y.3    Nakayama, H.4    Dohmae, N.5    Yohda, M.6    Odaka, M.7
  • 123
    • 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 2003 650 653
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 124
    • 0028840890 scopus 로고
    • Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme forms
    • E.J. Crane 3rd, D. Parsonage, L.B. Poole, and A. Claiborne Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme forms Biochemistry 34 1995 14114 14124
    • (1995) Biochemistry , vol.34 , pp. 14114-14124
    • Crane, E.J.1    Parsonage, D.2    Poole, L.B.3    Claiborne, A.4
  • 125
    • 38649084667 scopus 로고    scopus 로고
    • Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid
    • F.R. Salsbury Jr, S.T. Knutson, L.B. Poole, and J.S. Fetrow Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid Protein Sci. 17 2008 299 312
    • (2008) Protein Sci. , vol.17 , pp. 299-312
    • Salsbury, F.R.1    Knutson, S.T.2    Poole, L.B.3    Fetrow, J.S.4
  • 126
    • 0034792157 scopus 로고    scopus 로고
    • Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation
    • A. Claiborne, T.C. Mallett, J.I. Yeh, J. Luba, and D. Parsonage Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation Adv. Protein Chem. 58 2001 215 276
    • (2001) Adv. Protein Chem. , vol.58 , pp. 215-276
    • Claiborne, A.1    Mallett, T.C.2    Yeh, J.I.3    Luba, J.4    Parsonage, D.5
  • 127
    • 79851510345 scopus 로고    scopus 로고
    • Chemical 'omics' approaches for understanding protein cysteine oxidation in biology
    • S.E. Leonard, and K.S. Carroll Chemical 'omics' approaches for understanding protein cysteine oxidation in biology Curr. Opin. Chem. Biol. 15 2011 88 102
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 88-102
    • Leonard, S.E.1    Carroll, K.S.2
  • 129
    • 33646580362 scopus 로고    scopus 로고
    • Identification of S-nitrosylation motifs by site-specific mapping of the S-nitrosocysteine proteome in human vascular smooth muscle cells
    • T.M. Greco, R. Hodara, I. Parastatidis, H.F. Heijnen, M.K. Dennehy, D.C. Liebler, and H. Ischiropoulos Identification of S-nitrosylation motifs by site-specific mapping of the S-nitrosocysteine proteome in human vascular smooth muscle cells Proc. Natl. Acad. Sci. USA 103 2006 7420 7425
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7420-7425
    • Greco, T.M.1    Hodara, R.2    Parastatidis, I.3    Heijnen, H.F.4    Dennehy, M.K.5    Liebler, D.C.6    Ischiropoulos, H.7
  • 131
    • 45549108466 scopus 로고    scopus 로고
    • Disparate proteome reactivity profiles of carbon electrophiles
    • E. Weerapana, G.M. Simon, and B.F. Cravatt Disparate proteome reactivity profiles of carbon electrophiles Nat. Chem. Biol. 4 2008 405 407
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 405-407
    • Weerapana, E.1    Simon, G.M.2    Cravatt, B.F.3
  • 132
    • 0036401454 scopus 로고    scopus 로고
    • Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis
    • C. Lind, R. Gerdes, Y. Hamnell, I. Schuppe-Koistinen, H.B. von Lowenhielm, A. Holmgren, and I.A. Cotgreave Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis Arch. Biochem. Biophys. 406 2002 229 240
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 229-240
    • Lind, C.1    Gerdes, R.2    Hamnell, Y.3    Schuppe-Koistinen, I.4    Von Lowenhielm, H.B.5    Holmgren, A.6    Cotgreave, I.A.7
  • 137
    • 40849136587 scopus 로고    scopus 로고
    • Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin
    • D. Parsonage, P.A. Karplus, and L.B. Poole Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin Proc. Natl. Acad. Sci. USA 105 2008 8209 8214
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8209-8214
    • Parsonage, D.1    Karplus, P.A.2    Poole, L.B.3
  • 138
    • 0030695902 scopus 로고    scopus 로고
    • Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria
    • F. Åslund, K.D. Berndt, and A. Holmgren Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria J. Biol. Chem. 272 1997 30780 30786
    • (1997) J. Biol. Chem. , vol.272 , pp. 30780-30786
    • Åslund, F.1    Berndt, K.D.2    Holmgren, A.3


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