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Volumn 88, Issue 4, 2010, Pages 1297-1306

Redox regulation of cysteine-dependent enzymes

Author keywords

Aging; Antioxidant; Diet; Methionine; Oxidative stress; Postmortem

Indexed keywords

ANTIOXIDANT; CYSTEINE; REACTIVE OXYGEN METABOLITE;

EID: 77949667860     PISSN: 00218812     EISSN: 15253163     Source Type: Journal    
DOI: 10.2527/jas.2009-2381     Document Type: Article
Times cited : (22)

References (68)
  • 1
    • 4644305109 scopus 로고    scopus 로고
    • N-Acetyl cysteine, l-cysteine, and beta-mercaptoethanol augment selenium-glutathione peroxidase activity in glucose-6-phosphate dehydrogenase-deficient human erythrocytes
    • Aliciguzel, Y., and M. Aslan. 2004. N-Acetyl cysteine, l-cysteine, and beta-mercaptoethanol augment selenium-glutathione peroxidase activity in glucose-6-phosphate dehydrogenase-deficient human erythrocytes. Clin. Exp. Med. 4:50-55.
    • (2004) Clin. Exp. Med , vol.4 , pp. 50-55
    • Aliciguzel, Y.1    Aslan, M.2
  • 2
    • 64249169355 scopus 로고    scopus 로고
    • N-Acetylcysteineamide (NACA) prevents inflammation and oxidative stress in animals exposed to diesel engine exhaust
    • Banerjee, A., M. B. Trueblood, X. Zhang, K. R. Manda, P. Lobo, P. D. Whitefield, D. E. Hagen, and N. Ercal. 2009. N-Acetylcysteineamide (NACA) prevents inflammation and oxidative stress in animals exposed to diesel engine exhaust. Toxicol. Lett. 187:187-193.
    • (2009) Toxicol. Lett , vol.187 , pp. 187-193
    • Banerjee, A.1    Trueblood, M.B.2    Zhang, X.3    Manda, K.R.4    Lobo, P.5    Whitefield, P.D.6    Hagen, D.E.7    Ercal, N.8
  • 3
    • 9944235916 scopus 로고    scopus 로고
    • The role of cysteine residues as redox-sensitive regulatory switches
    • Barford, D. 2004. The role of cysteine residues as redox-sensitive regulatory switches. Curr. Opin. Struct. Biol. 14:679-686.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 679-686
    • Barford, D.1
  • 4
    • 0033521019 scopus 로고    scopus 로고
    • Roles of superoxide radical anion in signal transduction mediated by reversible regulation of proteintyrosine phosphatase 1B
    • Barrett, W. C., J. P. DeGnore, Y. F. Keng, Z. Y. Zhang, M. B. Yim, and P. B. Chock. 1999a. Roles of superoxide radical anion in signal transduction mediated by reversible regulation of proteintyrosine phosphatase 1B. J. Biol. Chem. 274:34543-34546.
    • (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
  • 6
    • 0032152137 scopus 로고    scopus 로고
    • Changes in the calpains and calpastatin during postmortem storage of bovine muscle
    • Boehm, M. L., T. L. Kendall, V. F. Thompson, and D. E. Goll. 1998. Changes in the calpains and calpastatin during postmortem storage of bovine muscle. J. Anim. Sci. 76:2415-2434.
    • (1998) J. Anim. Sci , vol.76 , pp. 2415-2434
    • Boehm, M.L.1    Kendall, T.L.2    Thompson, V.F.3    Goll, D.E.4
  • 7
    • 69249131714 scopus 로고    scopus 로고
    • Redox regulation of the dual specificity phosphatase YVH1 through disulfide bond formation
    • Bonham, C. A., and P. O. Vacratsis. 2009. Redox regulation of the dual specificity phosphatase YVH1 through disulfide bond formation. J. Biol. Chem. 284:22853-22864.
    • (2009) J. Biol. Chem , vol.284 , pp. 22853-22864
    • Bonham, C.A.1    Vacratsis, P.O.2
  • 8
    • 64549097266 scopus 로고    scopus 로고
    • Thiol-based redox switches in eukaryotic proteins
    • Brandes, N., S. Schmitt, and U. Jakob. 2009. Thiol-based redox switches in eukaryotic proteins. Antioxid. Redox Signal. 11:997-1014.
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 997-1014
    • Brandes, N.1    Schmitt, S.2    Jakob, U.3
  • 9
    • 53649111181 scopus 로고    scopus 로고
    • Protease activity in post-mortem red swamp crayfish (Procambarus clarkii) muscle stored in modified atmosphere packaging
    • Chen, G., R. P. Guttmann, Y. L. Xiong, C. D. Webster, and R. P. Romaire. 2008. Protease activity in post-mortem red swamp crayfish (Procambarus clarkii) muscle stored in modified atmosphere packaging. J. Agric. Food Chem. 56:8658-8663.
    • (2008) J. Agric. Food Chem , vol.56 , pp. 8658-8663
    • Chen, G.1    Guttmann, R.P.2    Xiong, Y.L.3    Webster, C.D.4    Romaire, R.P.5
  • 10
    • 67649213960 scopus 로고    scopus 로고
    • Effects of N-acetylcysteine on semen parameters and oxidative/antioxidant status
    • Ciftci, H., A. Verit, M. Savas, E. Yeni, and O. Erel. 2009. Effects of N-acetylcysteine on semen parameters and oxidative/antioxidant status. Urology 74:73-76.
    • (2009) Urology , vol.74 , pp. 73-76
    • Ciftci, H.1    Verit, A.2    Savas, M.3    Yeni, E.4    Erel, O.5
  • 11
    • 0034792157 scopus 로고    scopus 로고
    • Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation
    • Claiborne, A., T. C. Mallett, J. I. Yeh, J. Luba, and D. Parsonage. 2001. Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation. Adv. Protein Chem. 58:215-276.
    • (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
  • 12
    • 0037031899 scopus 로고    scopus 로고
    • Human mitochondrial thioredoxin. Involvement in mitochondrial membrane potential and cell death
    • Damdimopoulos, A. E., A. Miranda-Vizuete, M. Pelto-Huikko, J. A. Gustafsson, and G. Spyrou. 2002. Human mitochondrial thioredoxin. Involvement in mitochondrial membrane potential and cell death. J. Biol. Chem. 277:33249-33257.
    • (2002) J. Biol. Chem , vol.277 , pp. 33249-33257
    • Damdimopoulos, A.E.1    Miranda-Vizuete, A.2    Pelto-Huikko, M.3    Gustafsson, J.A.4    Spyrou, G.5
  • 13
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu, J. M., and K. G. Tanner. 1998. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37:5633-5642.
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 14
    • 58749103645 scopus 로고    scopus 로고
    • Attenuation of doxorubicin-induced cardiac injury by mitochondrial glutaredoxin 2
    • Diotte, N. M., Y. Xiong, J. Gao, B. H. Chua, and Y. S. Ho. 2009. Attenuation of doxorubicin-induced cardiac injury by mitochondrial glutaredoxin 2. Biochim. Biophys. Acta 1793:427-438.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 427-438
    • Diotte, N.M.1    Xiong, Y.2    Gao, J.3    Chua, B.H.4    Ho, Y.S.5
  • 15
    • 41549110976 scopus 로고    scopus 로고
    • Muscle-derived ROS and thiol regulation in muscle fatigue
    • Ferreira, L. F., and M. B. Reid. 2008. Muscle-derived ROS and thiol regulation in muscle fatigue. J. Appl. Physiol. 104:853-860.
    • (2008) J. Appl. Physiol , vol.104 , pp. 853-860
    • Ferreira, L.F.1    Reid, M.B.2
  • 18
    • 49349085256 scopus 로고    scopus 로고
    • Redox compartmentalization in eukaryotic cells
    • Go, Y. M., and D. P. Jones. 2008. Redox compartmentalization in eukaryotic cells. Biochim. Biophys. Acta 1780:1273-1290.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1273-1290
    • Go, Y.M.1    Jones, D.P.2
  • 20
    • 0031019885 scopus 로고    scopus 로고
    • Oxidation inhibits substrate proteolysis by calpain I but not autolysis
    • Guttmann, R. P., J. S. Elce, P. D. Bell, J. C. Isbell, and G. V. Johnson. 1997. Oxidation inhibits substrate proteolysis by calpain I but not autolysis. J. Biol. Chem. 272:2005-2012.
    • (1997) J. Biol. Chem , vol.272 , pp. 2005-2012
    • Guttmann, R.P.1    Elce, J.S.2    Bell, P.D.3    Isbell, J.C.4    Johnson, G.V.5
  • 21
    • 0032557513 scopus 로고    scopus 로고
    • Oxidative stress inhibits calpain activity in situ
    • Guttmann, R. P., and G. V. Johnson. 1998. Oxidative stress inhibits calpain activity in situ. J. Biol. Chem. 273:13331-13338.
    • (1998) J. Biol. Chem , vol.273 , pp. 13331-13338
    • Guttmann, R.P.1    Johnson, G.V.2
  • 22
    • 33750604604 scopus 로고    scopus 로고
    • Aspects of the biological redox chemistry of cysteine: From simple redox responses to sophisticated signalling pathways
    • Jacob, C., I. Knight, and P. G. Winyard. 2006. Aspects of the biological redox chemistry of cysteine: From simple redox responses to sophisticated signalling pathways. Biol. Chem. 387:1385-1397.
    • (2006) Biol. Chem , vol.387 , pp. 1385-1397
    • Jacob, C.1    Knight, I.2    Winyard, P.G.3
  • 25
    • 55149107716 scopus 로고    scopus 로고
    • Radical-free biology of oxidative stress
    • Jones, D. P. 2008. Radical-free biology of oxidative stress. Am. J. Physiol. Cell Physiol. 295:C849-C868.
    • (2008) Am. J. Physiol. Cell Physiol , vol.295
    • Jones, D.P.1
  • 26
    • 0031278114 scopus 로고    scopus 로고
    • Role of the sulfhydryl redox state and disulfide bonds in processing and assembly of 11S seed globulins
    • Jung, R., Y. W. Nam, I. Saalbach, K. Muntz, and N. C. Nielsen. 1997. Role of the sulfhydryl redox state and disulfide bonds in processing and assembly of 11S seed globulins. Plant Cell 9:2037-2050.
    • (1997) Plant Cell , vol.9 , pp. 2037-2050
    • Jung, R.1    Nam, Y.W.2    Saalbach, I.3    Muntz, K.4    Nielsen, N.C.5
  • 27
    • 0029875931 scopus 로고    scopus 로고
    • The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins
    • Keck, R. G. 1996. The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins. Anal. Biochem. 236:56-62.
    • (1996) Anal. Biochem , vol.236 , pp. 56-62
    • Keck, R.G.1
  • 28
    • 0033833952 scopus 로고    scopus 로고
    • Nitric oxide inhibits calpainmediated proteolysis of talin in skeletal muscle cells
    • Koh, T. J., and J. G. Tidball. 2000. Nitric oxide inhibits calpainmediated proteolysis of talin in skeletal muscle cells. Am. J. Physiol. Cell Physiol. 279:C806-C812.
    • (2000) Am. J. Physiol. Cell Physiol , vol.279
    • Koh, T.J.1    Tidball, J.G.2
  • 29
    • 0034209724 scopus 로고    scopus 로고
    • Modification of creatine kinase by S-nitrosothiols: S-Nitrosation vs. S-thiolation
    • Konorev, E. A., B. Kalyanaraman, and N. Hogg. 2000. Modification of creatine kinase by S-nitrosothiols: S-Nitrosation vs. S-thiolation. Free Radic. Biol. Med. 28:1671-1678.
    • (2000) Free Radic. Biol. Med , vol.28 , pp. 1671-1678
    • Konorev, E.A.1    Kalyanaraman, B.2    Hogg, N.3
  • 30
    • 0026591107 scopus 로고
    • 2+-dependent proteases (calpains) in post mortem proteolysis and meat tenderness
    • 2+-dependent proteases (calpains) in post mortem proteolysis and meat tenderness. Biochimie 74:239-245.
    • (1992) Biochimie , vol.74 , pp. 239-245
    • Koohmaraie, M.1
  • 31
    • 0025442365 scopus 로고
    • Alterations in postmortem degradation of myofibrillar proteins in muscle of lambs fed a beta-adrenergic agonist
    • Kretchmar, D. H., M. R. Hathaway, R. J. Epley, and W. R. Dayton. 1990. Alterations in postmortem degradation of myofibrillar proteins in muscle of lambs fed a beta-adrenergic agonist. J. Anim. Sci. 68:1760-1772.
    • (1990) J. Anim. Sci , vol.68 , pp. 1760-1772
    • Kretchmar, D.H.1    Hathaway, M.R.2    Epley, R.J.3    Dayton, W.R.4
  • 32
    • 0032402945 scopus 로고    scopus 로고
    • Caloric restriction prevents age-associated accrual of oxidative damage to mouse skeletal muscle mitochondria
    • Lass, A., B. H. Sohal, R. Weindruch, M. J. Forster, and R. S. Sohal. 1998. Caloric restriction prevents age-associated accrual of oxidative damage to mouse skeletal muscle mitochondria. Free Radic. Biol. Med. 25:1089-1097.
    • (1998) Free Radic. Biol. Med , vol.25 , pp. 1089-1097
    • Lass, A.1    Sohal, B.H.2    Weindruch, R.3    Forster, M.J.4    Sohal, R.S.5
  • 33
    • 70349284540 scopus 로고    scopus 로고
    • Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells
    • Leonard, S. E., K. G. Reddie, and K. S. Carroll. 2009. Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. ACS Chem. Biol. 4:783-799
    • (2009) Acs Chem. Biol , vol.4 , pp. 783-799
    • Leonard, S.E.1    Reddie, K.G.2    Carroll, K.S.3
  • 35
    • 54549089754 scopus 로고    scopus 로고
    • The conserved Cys254 plays a crucial role in creatine kinase refolding under non-reduced conditions but not in its activity or stability
    • Liu, Y. M., S. Feng, T. J. Zhao, X. L. Ding, and Y. B. Yan. 2008. The conserved Cys254 plays a crucial role in creatine kinase refolding under non-reduced conditions but not in its activity or stability. Biochim. Biophys. Acta 1784:2071-2078.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 2071-2078
    • Liu, Y.M.1    Feng, S.2    Zhao, T.J.3    Ding, X.L.4    Yan, Y.B.5
  • 36
    • 62549140078 scopus 로고    scopus 로고
    • N-Acetylcysteine suppresses oxidative stress in experimental rats with subarachnoid hemorrhage
    • Lu, H., D. M. Zhang, H. L. Chen, Y. X. Lin, C. H. Hang, H. X. Yin, and J. X. Shi. 2009. N-Acetylcysteine suppresses oxidative stress in experimental rats with subarachnoid hemorrhage. J. Clin. Neurosci. 16:684-688.
    • (2009) J. Clin. Neurosci , vol.16 , pp. 684-688
    • Lu, H.1    Zhang, D.M.2    Chen, H.L.3    Lin, Y.X.4    Hang, C.H.5    Yin, H.X.6    Shi, J.X.7
  • 37
    • 59449105695 scopus 로고    scopus 로고
    • Selenoproteins
    • Lu, J., and A. Holmgren. 2009. Selenoproteins. J. Biol. Chem. 284:723-727.
    • (2009) J. Biol. Chem , vol.284 , pp. 723-727
    • Lu, J.1    Holmgren, A.2
  • 38
    • 44449116745 scopus 로고    scopus 로고
    • Two distinct disulfide bonds formed in human heat shock transcription factor 1 act in opposition to regulate its DNA binding activity
    • Lu, M., H. E. Kim, C. R. Li, S. Kim, I. J. Kwak, Y. J. Lee, S. S. Kim, J. Y. Moon, C. H. Kim, D. K. Kim, H. S. Kang, and J. S. Park. 2008. Two distinct disulfide bonds formed in human heat shock transcription factor 1 act in opposition to regulate its DNA binding activity. Biochemistry 47:6007-6015.
    • (2008) Biochemistry , vol.47 , pp. 6007-6015
    • Lu, M.1    Kim, H.E.2    Li, C.R.3    Kim, S.4    Kwak, I.J.5    Lee, Y.J.6    Kim, S.S.7    Moon, J.Y.8    Kim, C.H.9    Kim, D.K.10    Kang, H.S.11    Park, J.S.12
  • 39
    • 70350337093 scopus 로고    scopus 로고
    • Vitamin C: Update on physiology and pharmacology
    • Mandl, J., A. Szarka, and G. Banhegyi. 2009. Vitamin C: Update on physiology and pharmacology. Br. J. Pharmacol. 157:1097-1110.
    • (2009) Br. J. Pharmacol , vol.157 , pp. 1097-1110
    • Mandl, J.1    Szarka, A.2    Banhegyi, G.3
  • 41
    • 65349123918 scopus 로고    scopus 로고
    • Reduced energy intake: The secret to a long and healthy life?
    • Martin, B., E. Golden, J. M. Egan, M. P. Mattson, and S. Maudsley. 2007. Reduced energy intake: The secret to a long and healthy life? IBS J. Sci. 2:35-39.
    • (2007) Ibs J. Sci , vol.2 , pp. 35-39
    • Martin, B.1    Golden, E.2    Egan, J.M.3    Mattson, M.P.4    Maudsley, S.5
  • 43
    • 34247604468 scopus 로고    scopus 로고
    • Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C
    • Monteiro, G., B. B. Horta, D. C. Pimenta, O. Augusto, and L. E. Netto. 2007. Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C. Proc. Natl. Acad. Sci. USA 104:4886-4891.
    • (2007) Proc. Natl. Acad. Sci. Usa , vol.104 , pp. 4886-4891
    • Monteiro, G.1    Horta, B.B.2    Pimenta, D.C.3    Augusto, O.4    Netto, L.E.5
  • 44
    • 3142685079 scopus 로고    scopus 로고
    • Extracellular thiols and thiol/disulfide redox in metabolism
    • Moriarty-Craige, S. E., and D. P. Jones. 2004. Extracellular thiols and thiol/disulfide redox in metabolism. Annu. Rev. Nutr. 24:481-509.
    • (2004) Annu. Rev. Nutr , vol.24 , pp. 481-509
    • Moriarty-Craige, S.E.1    Jones, D.P.2
  • 45
    • 69949086846 scopus 로고    scopus 로고
    • Redox reaction at ASK1-Cys250 is essential for activation of JNK and induction of apoptosis
    • Nadeau, P. J., S. J. Charette, and J. Landry. 2009. Redox reaction at ASK1-Cys250 is essential for activation of JNK and induction of apoptosis. Mol. Biol. Cell 20:3628-3637.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3628-3637
    • Nadeau, P.J.1    Charette, S.J.2    Landry, J.3
  • 46
    • 39849097748 scopus 로고    scopus 로고
    • Redox regulation in the extracellular environment
    • Ottaviano, F. G., D. E. Handy, and J. Loscalzo. 2008. Redox regulation in the extracellular environment. Circ. J. 72:1-16.
    • (2008) Circ. J , vol.72 , pp. 1-16
    • Ottaviano, F.G.1    Handy, D.E.2    Loscalzo, J.3
  • 47
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • Pacher, P., J. S. Beckman, and L. Liaudet. 2007. Nitric oxide and peroxynitrite in health and disease. Physiol. Rev. 87:315-424.
    • (2007) Physiol. Rev , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 48
    • 35448993279 scopus 로고    scopus 로고
    • What is the functional significance of the unique location of glutaredoxin 1 (GRx1) in the intermembrane space of mitochondria?
    • Pai, H. V., D. W. Starke, E. J. Lesnefsky, C. L. Hoppel, and J. J. Mieyal. 2007. What is the functional significance of the unique location of glutaredoxin 1 (GRx1) in the intermembrane space of mitochondria? Antioxid. Redox Signal. 9:2027-2033.
    • (2007) Antioxid. Redox Signal , vol.9 , pp. 2027-2033
    • Pai, H.V.1    Starke, D.W.2    Lesnefsky, E.J.3    Hoppel, C.L.4    Mieyal, J.J.5
  • 49
    • 69949115433 scopus 로고    scopus 로고
    • Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin
    • Park, J. W., J. J. Mieyal, S. G. Rhee, and P. B. Chock. 2009. Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin. J. Biol. Chem. 284:23364-23374.
    • (2009) J. Biol. Chem , vol.284 , pp. 23364-23374
    • Park, J.W.1    Mieyal, J.J.2    Rhee, S.G.3    Chock, P.B.4
  • 52
    • 70350685238 scopus 로고    scopus 로고
    • Oxidative stress regulation of stem and progenitor cells
    • Pervaiz, S., R. Taneja, and S. Ghaffari. 2009. Oxidative stress regulation of stem and progenitor cells. Antioxid. Redox Signal. 11:2777-2789.
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 2777-2789
    • Pervaiz, S.1    Taneja, R.2    Ghaffari, S.3
  • 53
    • 70350068501 scopus 로고    scopus 로고
    • Redox mechanisms involved in the selective activation of Nrf2-mediated resistance versus p53-dependent apoptosis in adenocarcinoma gastric cells
    • Piccirillo, S., G. Filomeni, B. Brune, G. Rotilio, and M. R. Ciriolo. 2009. Redox mechanisms involved in the selective activation of Nrf2-mediated resistance versus p53-dependent apoptosis in adenocarcinoma gastric cells. J. Biol. Chem. 284:27721-27733.
    • (2009) J. Biol. Chem , vol.284 , pp. 27721-27733
    • Piccirillo, S.1    Filomeni, G.2    Brune, B.3    Rotilio, G.4    Ciriolo, M.R.5
  • 54
    • 2542486403 scopus 로고    scopus 로고
    • Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue
    • Reddy, S., A. D. Jones, C. E. Cross, P. S. Wong, and A. Van Der Vliet. 2000. Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue. Biochem. J. 347:821-827.
    • (2000) Biochem. J , vol.347 , pp. 821-827
    • Reddy, S.1    Jones, A.D.2    Cross, C.E.3    Wong, P.S.4    van der Vliet, A.5
  • 55
    • 0027443868 scopus 로고
    • Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione
    • Ren, X., M. Bjornstedt, B. Shen, M. L. Ericson, and A. Holmgren. 1993. Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione. Biochemistry 32:9701-9708.
    • (1993) Biochemistry , vol.32 , pp. 9701-9708
    • Ren, X.1    Bjornstedt, M.2    Shen, B.3    Ericson, M.L.4    Holmgren, A.5
  • 56
    • 7244260588 scopus 로고    scopus 로고
    • Oxidative environments decrease tenderization of beef steaks through inactivation of μ-calpain
    • Rowe, L. J., K. R. Maddock, S. M. Lonergan, and E. Huff-Lonergan. 2004. Oxidative environments decrease tenderization of beef steaks through inactivation of μ-calpain. J. Anim. Sci. 82:3254-3266.
    • (2004) J. Anim. Sci , vol.82 , pp. 3254-3266
    • Rowe, L.J.1    Maddock, K.R.2    Lonergan, S.M.3    Huff-Lonergan, E.4
  • 57
    • 50649095897 scopus 로고    scopus 로고
    • Determination of sulfur amino acids in foods as related to bioavailability
    • Rutherfurd, S. M., and P. J. Moughan. 2008. Determination of sulfur amino acids in foods as related to bioavailability. J. AOAC Int. 91:907-913.
    • (2008) J. Aoac Int , vol.91 , pp. 907-913
    • Rutherfurd, S.M.1    Moughan, P.J.2
  • 58
    • 0037015682 scopus 로고    scopus 로고
    • Nrf2 degradation by the ubiquitin proteasome pathway is inhibited by KIAA0132, the human homolog to INrf2
    • Sekhar, K. R., X. X. Yan, and M. L. Freeman. 2002. Nrf2 degradation by the ubiquitin proteasome pathway is inhibited by KIAA0132, the human homolog to INrf2. Oncogene 21:6829-6834.
    • (2002) Oncogene , vol.21 , pp. 6829-6834
    • Sekhar, K.R.1    Yan, X.X.2    Freeman, M.L.3
  • 59
    • 0030038103 scopus 로고    scopus 로고
    • Oxidative stress, caloric restriction, and aging
    • Sohal, R. S., and R. Weindruch. 1996. Oxidative stress, caloric restriction, and aging. Science 273:59-63.
    • (1996) Science , vol.273 , pp. 59-63
    • Sohal, R.S.1    Weindruch, R.2
  • 61
    • 63849131592 scopus 로고    scopus 로고
    • Protective effect of sulfhydryl-containing antioxidants against ischemia/reperfusion injury of prepubertal rat intestine
    • Tunc, T., S. Oter, A. Guven, T. Topal, M. Kul, A. Korkmaz, O. Onguru, and U. Sarici. 2009. Protective effect of sulfhydryl-containing antioxidants against ischemia/reperfusion injury of prepubertal rat intestine. J. Gastroenterol. Hepatol. 24:681-687.
    • (2009) J. Gastroenterol. Hepatol , vol.24 , pp. 681-687
    • Tunc, T.1    Oter, S.2    Guven, A.3    Topal, T.4    Kul, M.5    Korkmaz, A.6    Onguru, O.7    Sarici, U.8
  • 62
    • 0026950706 scopus 로고
    • The effect of postmortem time of injection and freezing on the effectiveness of calcium chloride for improving beef tenderness
    • Wheeler, T. L., J. D. Crouse, and M. Koohmaraie. 1992. The effect of postmortem time of injection and freezing on the effectiveness of calcium chloride for improving beef tenderness. J. Anim. Sci. 70:3451-3457.
    • (1992) J. Anim. Sci , vol.70 , pp. 3451-3457
    • Wheeler, T.L.1    Crouse, J.D.2    Koohmaraie, M.3
  • 63
    • 0026825122 scopus 로고
    • Effects of lamb age, muscle type, and 24-hour activity of endogenous proteinases on postmortem proteolysis
    • Whipple, G., and M. Koohmaraie. 1992. Effects of lamb age, muscle type, and 24-hour activity of endogenous proteinases on postmortem proteolysis. J. Anim. Sci. 70:798-804.
    • (1992) J. Anim. Sci , vol.70 , pp. 798-804
    • Whipple, G.1    Koohmaraie, M.2
  • 64
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • Winterbourn, C. C., and M. B. Hampton. 2008. Thiol chemistry and specificity in redox signaling. Free Radic. Biol. Med. 45:549-561.
    • (2008) Free Radic. Biol. Med , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 66
    • 0034838039 scopus 로고    scopus 로고
    • Redox changes accompanying the degradation of seed storage proteins in germinating rice
    • Yano, H., J. H. Wong, M. J. Cho, and B. B. Buchanan. 2001. Redox changes accompanying the degradation of seed storage proteins in germinating rice. Plant Cell Physiol. 42:879-883.
    • (2001) Plant Cell Physiol , vol.42 , pp. 879-883
    • Yano, H.1    Wong, J.H.2    Cho, M.J.3    Buchanan, B.B.4
  • 67
    • 0033817976 scopus 로고    scopus 로고
    • Caloric restriction of rhesus monkeys lowers oxidative damage in skeletal muscle
    • Zainal, T. A., T. D. Oberley, D. B. Allison, L. I. Szweda, and R. Weindruch. 2000. Caloric restriction of rhesus monkeys lowers oxidative damage in skeletal muscle. FASEB J. 14:1825-1836.
    • (2000) Faseb J , vol.14 , pp. 1825-1836
    • Zainal, T.A.1    Oberley, T.D.2    Allison, D.B.3    Szweda, L.I.4    Weindruch, R.5
  • 68
    • 68149149835 scopus 로고    scopus 로고
    • The HIF-1 hypoxia-inducible factor modulates lifespan in C. elegans
    • Zhang, Y., Z. Shao, Z. Zhai, C. Shen, and J. A. Powell-Coffman. 2009. The HIF-1 hypoxia-inducible factor modulates lifespan in C. elegans. PLoS ONE 4:e6348.
    • (2009) Plos One , vol.4
    • Zhang, Y.1    Shao, Z.2    Zhai, Z.3    Shen, C.4    Powell-Coffman, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.