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Volumn 75, Issue 2, 2007, Pages 220-228

Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences

Author keywords

Glutathione; Nitric oxide; Oxidative stress; Post translational modifications

Indexed keywords

CASPASE 3; CYSTEINE; DNA; ENDOTHELIAL NITRIC OXIDE SYNTHASE; ENZYME; GLUTATHIONE; GLUTATHIONE DISULFIDE; HEMOGLOBIN; INDUCIBLE NITRIC OXIDE SYNTHASE; NEURONAL NITRIC OXIDE SYNTHASE; NITRIC OXIDE; PROTEIN P21; RAS PROTEIN; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; SARCOPLASMIC ENDOPLASMIC RETICULUM CALCIUM ATPASE; THIOL; UNCLASSIFIED DRUG;

EID: 34250738347     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cardiores.2007.03.016     Document Type: Review
Times cited : (165)

References (121)
  • 1
    • 1542328892 scopus 로고    scopus 로고
    • S-nitrosylation: a potential new paradigm in signal transduction
    • Martínez-Ruiz A., and Lamas S. S-nitrosylation: a potential new paradigm in signal transduction. Cardiovasc Res 62 (2004) 43-52
    • (2004) Cardiovasc Res , vol.62 , pp. 43-52
    • Martínez-Ruiz, A.1    Lamas, S.2
  • 2
    • 3242712276 scopus 로고    scopus 로고
    • Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers
    • Forman H.J., Fukuto J.M., and Torres M. Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am J Physiol Cell Physiol 287 (2004) C246-C256
    • (2004) Am J Physiol Cell Physiol , vol.287
    • Forman, H.J.1    Fukuto, J.M.2    Torres, M.3
  • 3
    • 0037365968 scopus 로고    scopus 로고
    • Specificity of a third kind: reactive oxygen and nitrogen intermediates in cell signaling
    • Nathan C. Specificity of a third kind: reactive oxygen and nitrogen intermediates in cell signaling. J Clin Invest 111 (2003) 769-778
    • (2003) J Clin Invest , vol.111 , pp. 769-778
    • Nathan, C.1
  • 5
    • 0242668688 scopus 로고    scopus 로고
    • Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
    • Woo H.A., Chae H.Z., Hwang S.C., Yang K.-S., Kang S.W., Kim K., et al. 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
  • 6
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
    • Biteau B., Labarre J., and Toledano M.B. 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
  • 7
    • 0028355875 scopus 로고
    • Protein S-thiolation in hepatocytes stimulated by t-butyl hydroperoxide, menadione, and neutrophils
    • Chai Y.C., Hendrich S., and Thomas J.A. Protein S-thiolation in hepatocytes stimulated by t-butyl hydroperoxide, menadione, and neutrophils. Arch Biochem Biophys 310 (1994) 264-272
    • (1994) Arch Biochem Biophys , vol.310 , pp. 264-272
    • Chai, Y.C.1    Hendrich, S.2    Thomas, J.A.3
  • 8
    • 0028170673 scopus 로고
    • S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes
    • Ravichandran V., Seres T., Moriguchi T., Thomas J.A., and Johnston Jr. R.B. S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes. J Biol Chem 269 (1994) 25010-25015
    • (1994) J Biol Chem , vol.269 , pp. 25010-25015
    • Ravichandran, V.1    Seres, T.2    Moriguchi, T.3    Thomas, J.A.4    Johnston Jr., R.B.5
  • 9
  • 10
    • 0037465761 scopus 로고    scopus 로고
    • Mechanism of S-nitrosation of recombinant human brain calbindin D28K
    • Tao L., and English A.M. Mechanism of S-nitrosation of recombinant human brain calbindin D28K. Biochemistry 42 (2003) 3326-3334
    • (2003) Biochemistry , vol.42 , pp. 3326-3334
    • Tao, L.1    English, A.M.2
  • 11
    • 0027396852 scopus 로고
    • Reactions of the bioregulatory agent nitric oxide in oxygenated aqueous media: determination of the kinetics for oxidation and nitrosation by intermediates generated in the NO/O2 reaction
    • Wink D.A., Darbyshire J.F., Nims R.W., Saavedra J.E., and Ford P.C. Reactions of the bioregulatory agent nitric oxide in oxygenated aqueous media: determination of the kinetics for oxidation and nitrosation by intermediates generated in the NO/O2 reaction. Chem Res Toxicol 6 (1993) 23-27
    • (1993) Chem Res Toxicol , vol.6 , pp. 23-27
    • Wink, D.A.1    Darbyshire, J.F.2    Nims, R.W.3    Saavedra, J.E.4    Ford, P.C.5
  • 12
    • 0036174890 scopus 로고    scopus 로고
    • The biochemistry and physiology of S-nitrosothiols
    • Hogg N. The biochemistry and physiology of S-nitrosothiols. Annu Rev Pharmacol Toxicol 42 (2002) 585-600
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 585-600
    • Hogg, N.1
  • 13
    • 0023257674 scopus 로고
    • Formation and reduction of glutathione-protein mixed disulfides during oxidative stress. A study with isolated hepatocytes and menadione (2-methyl-1,4-naphthoquinone)
    • Bellomo G., Mirabelli F., DiMonte D., Richelmi P., Thor H., Orrenius C., et al. Formation and reduction of glutathione-protein mixed disulfides during oxidative stress. A study with isolated hepatocytes and menadione (2-methyl-1,4-naphthoquinone). Biochem Pharmacol 36 (1987) 1313-1320
    • (1987) Biochem Pharmacol , vol.36 , pp. 1313-1320
    • Bellomo, G.1    Mirabelli, F.2    DiMonte, D.3    Richelmi, P.4    Thor, H.5    Orrenius, C.6
  • 14
    • 0024458535 scopus 로고
    • Dependence of mixed disulfide formation in alveolar macrophages upon production of oxidized glutathione: effect of selenium depletion
    • Loeb G.A., Skelton D.C., and Forman H.J. Dependence of mixed disulfide formation in alveolar macrophages upon production of oxidized glutathione: effect of selenium depletion. Biochem Pharmacol 38 (1989) 3119-3121
    • (1989) Biochem Pharmacol , vol.38 , pp. 3119-3121
    • Loeb, G.A.1    Skelton, D.C.2    Forman, H.J.3
  • 15
    • 0026459935 scopus 로고
    • Protein-specific S-thiolation in human endothelial cells during oxidative stress
    • Schuppe I., Moldeus P., and Cotgreave I.A. Protein-specific S-thiolation in human endothelial cells during oxidative stress. Biochem Pharmacol 44 (1992) 1757-1764
    • (1992) Biochem Pharmacol , vol.44 , pp. 1757-1764
    • Schuppe, I.1    Moldeus, P.2    Cotgreave, I.A.3
  • 16
    • 0029015864 scopus 로고
    • Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas J.A., Poland B., and Honzatko R. Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch Biochem Biophys 319 (1995) 1-9
    • (1995) Arch Biochem Biophys , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 17
    • 0032488513 scopus 로고    scopus 로고
    • Recent trends in glutathione biochemistry-glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation?
    • Cotgreave I.A., and Gerdes R.G. Recent trends in glutathione biochemistry-glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation?. Biochem Biophys Res Commun 242 (1998) 1-9
    • (1998) Biochem Biophys Res Commun , vol.242 , pp. 1-9
    • Cotgreave, I.A.1    Gerdes, R.G.2
  • 18
    • 0028298361 scopus 로고
    • S-thiolation of individual human neutrophil proteins including actin by stimulation of the respiratory burst: evidence against a role for glutathione disulfide
    • Chai Y.C., Ashraf S.S., Rokutan K., Johnston Jr. R.B., and Thomas J.A. S-thiolation of individual human neutrophil proteins including actin by stimulation of the respiratory burst: evidence against a role for glutathione disulfide. Arch Biochem Biophys 310 (1994) 273-281
    • (1994) Arch Biochem Biophys , vol.310 , pp. 273-281
    • Chai, Y.C.1    Ashraf, S.S.2    Rokutan, K.3    Johnston Jr., R.B.4    Thomas, J.A.5
  • 19
    • 0035831445 scopus 로고    scopus 로고
    • Different metabolizing ability of thiol reactants in human and rat blood. Biochemical and pharmacological implications
    • Rossi R., Milzani A., Dalle-Donne I., Giannerini F., Giustarini D., Lusini L., et al. Different metabolizing ability of thiol reactants in human and rat blood. Biochemical and pharmacological implications. J Biol Chem 276 (2001) 7004-7010
    • (2001) J Biol Chem , vol.276 , pp. 7004-7010
    • Rossi, R.1    Milzani, A.2    Dalle-Donne, I.3    Giannerini, F.4    Giustarini, D.5    Lusini, L.6
  • 20
    • 18844427352 scopus 로고    scopus 로고
    • S-glutathionylation in human platelets by a thiol-disulfide exchange-independent mechanism
    • Dalle-Donne I., Giustarini D., Colombo R., Milzani A., and Rossi R. S-glutathionylation in human platelets by a thiol-disulfide exchange-independent mechanism. Free Radic Biol Med 38 (2005) 1501-1510
    • (2005) Free Radic Biol Med , vol.38 , pp. 1501-1510
    • Dalle-Donne, I.1    Giustarini, D.2    Colombo, R.3    Milzani, A.4    Rossi, R.5
  • 21
    • 0031574042 scopus 로고    scopus 로고
    • A method to study kinetics of transnitrosation with nitrosoglutathione: reactions with hemoglobin and other thiols
    • Rossi R., Lusini L., Giannerini F., Giustarini D., Lungarella G., and Simplicio P.D. A method to study kinetics of transnitrosation with nitrosoglutathione: reactions with hemoglobin and other thiols. Anal Biochem 254 (1997) 215-220
    • (1997) Anal Biochem , vol.254 , pp. 215-220
    • Rossi, R.1    Lusini, L.2    Giannerini, F.3    Giustarini, D.4    Lungarella, G.5    Simplicio, P.D.6
  • 22
    • 0031931823 scopus 로고    scopus 로고
    • S-transnitrosation reactions are involved in the metabolic fate and biological actions of nitric oxide
    • Liu Z., Rudd M.A., Freedman J.E., and Loscalzo J. S-transnitrosation reactions are involved in the metabolic fate and biological actions of nitric oxide. J Pharmacol Exp Ther 284 (1998) 526-534
    • (1998) J Pharmacol Exp Ther , vol.284 , pp. 526-534
    • Liu, Z.1    Rudd, M.A.2    Freedman, J.E.3    Loscalzo, J.4
  • 23
    • 0029065402 scopus 로고
    • Thiol/disulfide exchange equilibria and disulfide bond stability
    • Gilbert H.F. Thiol/disulfide exchange equilibria and disulfide bond stability. Methods Enzymol 251 (1995) 8-28
    • (1995) Methods Enzymol , vol.251 , pp. 8-28
    • Gilbert, H.F.1
  • 24
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee S.-R., Kwon K.-S., Kim S.-R., and Rhee S.G. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J Biol Chem 273 (1998) 15366-15372
    • (1998) J Biol Chem , vol.273 , pp. 15366-15372
    • Lee, S.-R.1    Kwon, K.-S.2    Kim, S.-R.3    Rhee, S.G.4
  • 25
    • 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 Tanner K.G. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37 (1998) 5633-5642
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 26
    • 0033521019 scopus 로고    scopus 로고
    • Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B
    • Barrett W.C., DeGnore J.P., Keng Y.F., Zhang Z.Y., Yim M.B., and Chock P.B. 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
  • 28
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen A., Andersen J.N., Myers M.P., Meng T.C., Hinks J.A., Tonks N.K., et al. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423 (2003) 769-773
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6
  • 29
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • van Montfort R.L., Congreve M., Tisi D., Carr R., and Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423 (2003) 773-777
    • (2003) Nature , vol.423 , pp. 773-777
    • van Montfort, R.L.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 30
    • 17644386593 scopus 로고    scopus 로고
    • Inhibition of protein-tyrosine phosphatases by mild oxidative stresses is dependent on S-nitrosylation
    • Barrett D.M., Black S.M., Todor H., Schmidt-Ullrich R.K., Dawson K.S., and Mikkelsen R.B. Inhibition of protein-tyrosine phosphatases by mild oxidative stresses is dependent on S-nitrosylation. J Biol Chem 280 (2005) 14453-14461
    • (2005) J Biol Chem , vol.280 , pp. 14453-14461
    • Barrett, D.M.1    Black, S.M.2    Todor, H.3    Schmidt-Ullrich, R.K.4    Dawson, K.S.5    Mikkelsen, R.B.6
  • 33
    • 0024299403 scopus 로고
    • Reaction of S-nitrosoglutathione with sulfhydryl groups in protein
    • Park J.-W. Reaction of S-nitrosoglutathione with sulfhydryl groups in protein. Biochem Biophys Res Commun 152 (1988) 916-920
    • (1988) Biochem Biophys Res Commun , vol.152 , pp. 916-920
    • Park, J.-W.1
  • 34
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • Klatt P., and Lamas S. Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur J Biochem 267 (2000) 4928-4944
    • (2000) Eur J Biochem , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 35
    • 0033080394 scopus 로고    scopus 로고
    • S-nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitroso glutathione
    • Ji Y., Akerboom T.P., Sies H., and Thomas J.A. S-nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitroso glutathione. Arch Biochem Biophys 362 (1999) 67-78
    • (1999) Arch Biochem Biophys , vol.362 , pp. 67-78
    • Ji, Y.1    Akerboom, T.P.2    Sies, H.3    Thomas, J.A.4
  • 36
    • 0034209724 scopus 로고    scopus 로고
    • Modification of creatine kinase by S-nitrosothiols: S-nitrosation vs. S-thiolation
    • Konorev E.A., Kalyanaraman B., and Hogg N. Modification of creatine kinase by S-nitrosothiols: S-nitrosation vs. S-thiolation. Free Radic Biol Med 28 (2000) 1671-1678
    • (2000) Free Radic Biol Med , vol.28 , pp. 1671-1678
    • Konorev, E.A.1    Kalyanaraman, B.2    Hogg, N.3
  • 37
    • 0035310359 scopus 로고    scopus 로고
    • Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines
    • Mallis R.J., Buss J.E., and Thomas J.A. Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines. Biochem J 355 (2001) 145-153
    • (2001) Biochem J , vol.355 , pp. 145-153
    • Mallis, R.J.1    Buss, J.E.2    Thomas, J.A.3
  • 39
    • 33846003833 scopus 로고    scopus 로고
    • Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in RyR1
    • Aracena-Parks P., Goonasekera S.A., Gilman C., Dirksen R.T., Hidalgo C., and Hamilton S.L. Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in RyR1. J Biol Chem 281 (2006) 40354-40368
    • (2006) J Biol Chem , vol.281 , pp. 40354-40368
    • Aracena-Parks, P.1    Goonasekera, S.A.2    Gilman, C.3    Dirksen, R.T.4    Hidalgo, C.5    Hamilton, S.L.6
  • 40
    • 0031829139 scopus 로고    scopus 로고
    • Differential effects of nitric oxide-mediated S-nitrosylation on p50 and c-jun DNA binding
    • DelaTorre A., Schroeder R.A., Bartlett S.T., and Kuo P.C. Differential effects of nitric oxide-mediated S-nitrosylation on p50 and c-jun DNA binding. Surgery 124 (1998) 137-141
    • (1998) Surgery , vol.124 , pp. 137-141
    • DelaTorre, A.1    Schroeder, R.A.2    Bartlett, S.T.3    Kuo, P.C.4
  • 42
    • 0032983979 scopus 로고    scopus 로고
    • Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation
    • Klatt P., Pineda Molina E., and Lamas S. Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation. J Biol Chem 274 (1999) 15857-15864
    • (1999) J Biol Chem , vol.274 , pp. 15857-15864
    • Klatt, P.1    Pineda Molina, E.2    Lamas, S.3
  • 43
    • 0035960648 scopus 로고    scopus 로고
    • Glutathionylation of the p50 subunit of NF-kappaB: a mechanism for redox-induced inhibition of DNA binding
    • Pineda-Molina E., Klatt P., Vázquez J., Marina A., García de Lacoba M., Pérez-Sala D., et al. Glutathionylation of the p50 subunit of NF-kappaB: a mechanism for redox-induced inhibition of DNA binding. Biochemistry 40 (2001) 14134-14142
    • (2001) Biochemistry , vol.40 , pp. 14134-14142
    • Pineda-Molina, E.1    Klatt, P.2    Vázquez, J.3    Marina, A.4    García de Lacoba, M.5    Pérez-Sala, D.6
  • 44
    • 0035852845 scopus 로고    scopus 로고
    • Inhibition of NF-kappa B by S-nitrosylation
    • Marshall H.E., and Stamler J.S. Inhibition of NF-kappa B by S-nitrosylation. Biochemistry 40 (2001) 1688-1693
    • (2001) Biochemistry , vol.40 , pp. 1688-1693
    • Marshall, H.E.1    Stamler, J.S.2
  • 45
    • 0035949671 scopus 로고    scopus 로고
    • Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
    • Sun J., Xin C., Eu J.P., Stamler J.S., and Meissner G. Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO. Proc Natl Acad Sci U S A 98 (2001) 11158-11162
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11158-11162
    • Sun, J.1    Xin, C.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 47
    • 0034326826 scopus 로고    scopus 로고
    • Effect of S-nitrosothiols on cellular glutathione and reactive protein sulfhydryls
    • Mallis R.J., and Thomas J.A. Effect of S-nitrosothiols on cellular glutathione and reactive protein sulfhydryls. Arch Biochem Biophys 383 (2000) 60-69
    • (2000) Arch Biochem Biophys , vol.383 , pp. 60-69
    • Mallis, R.J.1    Thomas, J.A.2
  • 48
    • 33845600791 scopus 로고    scopus 로고
    • Protein glutathiolation by nitric oxide: an intracellular mechanism regulating redox protein modification
    • West M.B., Hill B.G., Xuan Y.T., and Bhatnagar A. Protein glutathiolation by nitric oxide: an intracellular mechanism regulating redox protein modification. FASEB J 20 (2006) 1715-1717
    • (2006) FASEB J , vol.20 , pp. 1715-1717
    • West, M.B.1    Hill, B.G.2    Xuan, Y.T.3    Bhatnagar, A.4
  • 50
    • 0032522535 scopus 로고    scopus 로고
    • S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme
    • Jensen D.E., Belka G.K., and Du Bois G.C. S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme. Biochem J 331 (1998) 659-668
    • (1998) Biochem J , vol.331 , pp. 659-668
    • Jensen, D.E.1    Belka, G.K.2    Du Bois, G.C.3
  • 51
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • Liu L., Hausladen A., Zeng M., Que L., Heitman J., and Stamler J.S. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410 (2001) 490-494
    • (2001) Nature , vol.410 , pp. 490-494
    • Liu, L.1    Hausladen, A.2    Zeng, M.3    Que, L.4    Heitman, J.5    Stamler, J.S.6
  • 52
    • 14044257843 scopus 로고    scopus 로고
    • Glutaredoxin: role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation
    • Shelton M.D., Chock P.B., and Mieyal J.J. Glutaredoxin: role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxid Redox Signal 7 (2005) 348-366
    • (2005) Antioxid Redox Signal , vol.7 , pp. 348-366
    • Shelton, M.D.1    Chock, P.B.2    Mieyal, J.J.3
  • 53
    • 31044455445 scopus 로고    scopus 로고
    • Redox modifications of protein-thiols: emerging roles in cell signaling
    • Biswas S., Chida A.S., and Rahman I. Redox modifications of protein-thiols: emerging roles in cell signaling. Biochem Pharmacol 71 (2006) 551-564
    • (2006) Biochem Pharmacol , vol.71 , pp. 551-564
    • Biswas, S.1    Chida, A.S.2    Rahman, I.3
  • 54
  • 55
    • 33947381788 scopus 로고    scopus 로고
    • Redox in redux: emergent roles for glutathione S-transferase P (GSTP) in regulation of cell signaling and S-glutathionylation
    • Tew K.D. Redox in redux: emergent roles for glutathione S-transferase P (GSTP) in regulation of cell signaling and S-glutathionylation. Biochem Pharmacol 73 (2007) 1257-1269
    • (2007) Biochem Pharmacol , vol.73 , pp. 1257-1269
    • Tew, K.D.1
  • 56
    • 0026623110 scopus 로고
    • Endothelial nitric oxide synthase: molecular cloning and characterization of a distinct constitutive enzyme isoform
    • Lamas S., Marsden P.A., Li G.K., Tempst P., and Michel T. Endothelial nitric oxide synthase: molecular cloning and characterization of a distinct constitutive enzyme isoform. Proc Natl Acad Sci U S A 89 (1992) 6348-6352
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 6348-6352
    • Lamas, S.1    Marsden, P.A.2    Li, G.K.3    Tempst, P.4    Michel, T.5
  • 58
    • 2942685631 scopus 로고    scopus 로고
    • Caveolae and caveolins in the cardiovascular system
    • Gratton J.-P., Bernatchez P., and Sessa W.C. Caveolae and caveolins in the cardiovascular system. Circ Res 94 (2004) 1408-1417
    • (2004) Circ Res , vol.94 , pp. 1408-1417
    • Gratton, J.-P.1    Bernatchez, P.2    Sessa, W.C.3
  • 59
    • 11244352052 scopus 로고    scopus 로고
    • Palmitoylation of inducible nitric-oxide synthase at Cys-3 is required for proper intracellular traffic and nitric oxide synthesis
    • Navarro-Lérida I., Corvi M.M., Alvarez-Barrientos A., Gavilanes F., Berthiaume L.G., and Rodríguez-Crespo I. Palmitoylation of inducible nitric-oxide synthase at Cys-3 is required for proper intracellular traffic and nitric oxide synthesis. J Biol Chem 279 (2004) 55682-55689
    • (2004) J Biol Chem , vol.279 , pp. 55682-55689
    • Navarro-Lérida, I.1    Corvi, M.M.2    Alvarez-Barrientos, A.3    Gavilanes, F.4    Berthiaume, L.G.5    Rodríguez-Crespo, I.6
  • 60
    • 20444365874 scopus 로고    scopus 로고
    • Direct interaction between the reductase domain of endothelial nitric oxide synthase and the ryanodine receptor
    • Martínez-Moreno M., Alvarez-Barrientos A., Roncal F., Albar J.P., Gavilanes F., Lamas S., et al. Direct interaction between the reductase domain of endothelial nitric oxide synthase and the ryanodine receptor. FEBS Lett 579 (2005) 3159-3163
    • (2005) FEBS Lett , vol.579 , pp. 3159-3163
    • Martínez-Moreno, M.1    Alvarez-Barrientos, A.2    Roncal, F.3    Albar, J.P.4    Gavilanes, F.5    Lamas, S.6
  • 61
    • 1442330336 scopus 로고    scopus 로고
    • S-nitrosylation of endothelial nitric oxide synthase is associated with monomerization and decreased enzyme activity
    • Ravi K., Brennan L.A., Levic S., Ross P.A., and Black S.M. S-nitrosylation of endothelial nitric oxide synthase is associated with monomerization and decreased enzyme activity. Proc Natl Acad Sci U S A 101 (2004) 2619-2624
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 2619-2624
    • Ravi, K.1    Brennan, L.A.2    Levic, S.3    Ross, P.A.4    Black, S.M.5
  • 62
    • 20444409884 scopus 로고    scopus 로고
    • Receptor-regulated dynamic S-nitrosylation of endothelial nitric oxide synthase in vascular endothelial cells
    • Erwin P.A., Lin A.J., Golan D.E., and Michel T. Receptor-regulated dynamic S-nitrosylation of endothelial nitric oxide synthase in vascular endothelial cells. J Biol Chem 280 (2005) 19888-19894
    • (2005) J Biol Chem , vol.280 , pp. 19888-19894
    • Erwin, P.A.1    Lin, A.J.2    Golan, D.E.3    Michel, T.4
  • 63
    • 33644864135 scopus 로고    scopus 로고
    • Subcellular targeting and differential S-nitrosylation of endothelial nitric oxide synthase
    • Erwin P.A., Mitchell D.A., Sartoretto J., Marletta M.A., and Michel T. Subcellular targeting and differential S-nitrosylation of endothelial nitric oxide synthase. J Biol Chem 281 (2006) 151-157
    • (2006) J Biol Chem , vol.281 , pp. 151-157
    • Erwin, P.A.1    Mitchell, D.A.2    Sartoretto, J.3    Marletta, M.A.4    Michel, T.5
  • 64
    • 33845960772 scopus 로고    scopus 로고
    • Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking
    • Iwakiri Y., Satoh A., Chatterjee S., Toomre D.K., Chalouni C.M., Fulton D., et al. Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking. Proc Natl Acad Sci U S A 103 (2006) 19777-19782
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 19777-19782
    • Iwakiri, Y.1    Satoh, A.2    Chatterjee, S.3    Toomre, D.K.4    Chalouni, C.M.5    Fulton, D.6
  • 65
    • 11844295419 scopus 로고    scopus 로고
    • S-nitrosoprotein formation and localization in endothelial cells
    • Yang Y., and Loscalzo J. S-nitrosoprotein formation and localization in endothelial cells. Proc Natl Acad Sci U S A 102 (2005) 117-122
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 117-122
    • Yang, Y.1    Loscalzo, J.2
  • 66
    • 9644290748 scopus 로고    scopus 로고
    • In situ detection and visualization of S-nitrosylated proteins following chemical derivatization: identification of Ran GTPase as a target for S-nitrosylation
    • Ckless K., Reynaert N.L., Taatjes D.J., Lounsbury K.M., van der Vliet A., and Janssen-Heininger Y. In situ detection and visualization of S-nitrosylated proteins following chemical derivatization: identification of Ran GTPase as a target for S-nitrosylation. Nitric Oxide 11 (2004) 216-227
    • (2004) Nitric Oxide , vol.11 , pp. 216-227
    • Ckless, K.1    Reynaert, N.L.2    Taatjes, D.J.3    Lounsbury, K.M.4    van der Vliet, A.5    Janssen-Heininger, Y.6
  • 67
    • 20444365814 scopus 로고    scopus 로고
    • Nitrosylation of thiols in vascular homeostasis and disease
    • Martínez-Ruiz A., and Lamas S. Nitrosylation of thiols in vascular homeostasis and disease. Curr Atheroscl Rep 7 (2005) 213-218
    • (2005) Curr Atheroscl Rep , vol.7 , pp. 213-218
    • Martínez-Ruiz, A.1    Lamas, S.2
  • 68
    • 0028215113 scopus 로고
    • Antisera to glutathione: characterization and immunocytochemical application to the rat cerebellum
    • Hjelle O.P., Chaudhry F.A., and Ottersen O.P. Antisera to glutathione: characterization and immunocytochemical application to the rat cerebellum. Eur J Neurosci 6 (1994) 793-804
    • (1994) Eur J Neurosci , vol.6 , pp. 793-804
    • Hjelle, O.P.1    Chaudhry, F.A.2    Ottersen, O.P.3
  • 70
    • 0037270885 scopus 로고    scopus 로고
    • Visualization of the compartmentalization of glutathione and protein-glutathione mixed disulfides in cultured cells
    • Söderdahl T., Enoksson M., Lundberg M., Holmgren A., Ottersen O.P., Orrenius S., et al. Visualization of the compartmentalization of glutathione and protein-glutathione mixed disulfides in cultured cells. FASEB J 17 (2003) 124-126
    • (2003) FASEB J , vol.17 , pp. 124-126
    • Söderdahl, T.1    Enoksson, M.2    Lundberg, M.3    Holmgren, A.4    Ottersen, O.P.5    Orrenius, S.6
  • 71
    • 33144490305 scopus 로고    scopus 로고
    • Nuclear and mitochondrial compartmentation of oxidative stress and redox signaling
    • Hansen J.M., Go Y.M., and Jones D.P. Nuclear and mitochondrial compartmentation of oxidative stress and redox signaling. Annu Rev Pharmacol Toxicol 46 (2006) 215-234
    • (2006) Annu Rev Pharmacol Toxicol , vol.46 , pp. 215-234
    • Hansen, J.M.1    Go, Y.M.2    Jones, D.P.3
  • 72
    • 0036401454 scopus 로고    scopus 로고
    • Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis
    • Lind C., Gerdes R., Hamnell Y., Schuppe-Koistinen I., von Löwenhielm H.B., Holmgren A., et al. 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 Löwenhielm, H.B.5    Holmgren, A.6
  • 74
    • 18344390036 scopus 로고    scopus 로고
    • Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes
    • Fratelli M., Demol H., Puype M., Casagrande S., Eberini I., Salmona M., et al. Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes. Proc Natl Acad Sci U S A 99 (2002) 3505-3510
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 3505-3510
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4    Eberini, I.5    Salmona, M.6
  • 75
    • 0037155862 scopus 로고    scopus 로고
    • Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion
    • Eaton P., Byers H.L., Leeds N., Ward M.A., and Shattock M.J. Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. J Biol Chem 277 (2002) 9806-9811
    • (2002) J Biol Chem , vol.277 , pp. 9806-9811
    • Eaton, P.1    Byers, H.L.2    Leeds, N.3    Ward, M.A.4    Shattock, M.J.5
  • 76
    • 34250806432 scopus 로고    scopus 로고
    • Thiol-disulfide oxidoreduction of protein cysteines: old methods revisited for proteomics
    • Dalle-Donne I., Scaloni A., and Butterfield D.A. (Eds), Wiley-Interscience
    • Bonetto V., and Ghezzi P. Thiol-disulfide oxidoreduction of protein cysteines: old methods revisited for proteomics. In: Dalle-Donne I., Scaloni A., and Butterfield D.A. (Eds). Redox Proteomics (2006), Wiley-Interscience 101-122
    • (2006) Redox Proteomics , pp. 101-122
    • Bonetto, V.1    Ghezzi, P.2
  • 77
    • 84889442289 scopus 로고    scopus 로고
    • Use of a proteomic technique to identify oxidant-sensitive thiol proteins in cultured cells
    • Dalle-Donne I., Scaloni A., and Butterfield D.A. (Eds), Wiley-Interscience
    • Hampton M.B., Baty J.W., and Winterbourn C.C. Use of a proteomic technique to identify oxidant-sensitive thiol proteins in cultured cells. In: Dalle-Donne I., Scaloni A., and Butterfield D.A. (Eds). Redox Proteomics (2006), Wiley-Interscience 253-265
    • (2006) Redox Proteomics , pp. 253-265
    • Hampton, M.B.1    Baty, J.W.2    Winterbourn, C.C.3
  • 78
    • 33646745126 scopus 로고    scopus 로고
    • Protein thiol oxidation in health and disease: techniques for measuring disulfides and related modifications in complex protein mixtures
    • Eaton P. Protein thiol oxidation in health and disease: techniques for measuring disulfides and related modifications in complex protein mixtures. Free Radic Biol Med 40 (2006) 1889-1899
    • (2006) Free Radic Biol Med , vol.40 , pp. 1889-1899
    • Eaton, P.1
  • 80
    • 14044272119 scopus 로고    scopus 로고
    • S-glutathionylation: from redox regulation of protein functions to human diseases
    • Giustarini D., Rossi R., Milzani A., Colombo R., and Dalle-Donne I. S-glutathionylation: from redox regulation of protein functions to human diseases. J Cell Mol Med 8 (2004) 201-212
    • (2004) J Cell Mol Med , vol.8 , pp. 201-212
    • Giustarini, D.1    Rossi, R.2    Milzani, A.3    Colombo, R.4    Dalle-Donne, I.5
  • 81
    • 24144493633 scopus 로고    scopus 로고
    • Structural insights into Alzheimer filament assembly pathways based on site-directed mutagenesis and S-glutathionylation of three-repeat neuronal Tau protein
    • Dinoto L., Deture M.A., and Purich D.L. Structural insights into Alzheimer filament assembly pathways based on site-directed mutagenesis and S-glutathionylation of three-repeat neuronal Tau protein. Microsc Res Tech 67 (2005) 156-163
    • (2005) Microsc Res Tech , vol.67 , pp. 156-163
    • Dinoto, L.1    Deture, M.A.2    Purich, D.L.3
  • 83
    • 0033592423 scopus 로고    scopus 로고
    • Peroxynitrite modification of protein thiols: oxidation, nitrosylation, and S-glutathiolation of functionally important cysteine residue(s) in the sarcoplasmic reticulum Ca-ATPase
    • Viner R.I., Williams T.D., and Schöneich C. Peroxynitrite modification of protein thiols: oxidation, nitrosylation, and S-glutathiolation of functionally important cysteine residue(s) in the sarcoplasmic reticulum Ca-ATPase. Biochemistry 38 (1999) 12408-12415
    • (1999) Biochemistry , vol.38 , pp. 12408-12415
    • Viner, R.I.1    Williams, T.D.2    Schöneich, C.3
  • 84
    • 0034665152 scopus 로고    scopus 로고
    • Nitric oxide-dependent modification of the sarcoplasmic reticulum Ca-ATPase: localization of cysteine target sites
    • Viner R.I., Williams T.D., and Schöneich C. Nitric oxide-dependent modification of the sarcoplasmic reticulum Ca-ATPase: localization of cysteine target sites. Free Radic Biol Med 29 (2000) 489-496
    • (2000) Free Radic Biol Med , vol.29 , pp. 489-496
    • Viner, R.I.1    Williams, T.D.2    Schöneich, C.3
  • 85
    • 9144266981 scopus 로고    scopus 로고
    • S-glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
    • Adachi T., Weisbrod R.M., Pimentel D.R., Ying J., Sharov V.S., Schöneich C., et al. S-glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide. Nat Med 10 (2004) 1200-1207
    • (2004) Nat Med , vol.10 , pp. 1200-1207
    • Adachi, T.1    Weisbrod, R.M.2    Pimentel, D.R.3    Ying, J.4    Sharov, V.S.5    Schöneich, C.6
  • 86
    • 0031054520 scopus 로고    scopus 로고
    • A molecular redox switch on p21ras. Structrural basis for the nitric oxide-p21ras interaction
    • Lander H.M., Hajjar D.P., Hempstead B.L., Mirza U.A., Chait B.T., Campbell S., et al. A molecular redox switch on p21ras. Structrural basis for the nitric oxide-p21ras interaction. J Biol Chem 272 (1997) 4323-4326
    • (1997) J Biol Chem , vol.272 , pp. 4323-4326
    • Lander, H.M.1    Hajjar, D.P.2    Hempstead, B.L.3    Mirza, U.A.4    Chait, B.T.5    Campbell, S.6
  • 87
    • 34250816732 scopus 로고    scopus 로고
    • Nitric oxide and cell signaling: redox regulation of Ras superfamiliy GTPases
    • Lamas S., and Cadenas E. (Eds), CRC Press - Taylor and Francis
    • Heo J., and Campbell S.L. Nitric oxide and cell signaling: redox regulation of Ras superfamiliy GTPases. In: Lamas S., and Cadenas E. (Eds). Nitric Oxide, Cell Signaling and Gene Expression (2006), CRC Press - Taylor and Francis 263-289
    • (2006) Nitric Oxide, Cell Signaling and Gene Expression , pp. 263-289
    • Heo, J.1    Campbell, S.L.2
  • 88
    • 3142663363 scopus 로고    scopus 로고
    • S-glutathiolation of Ras mediates redox-sensitive signaling by Angiotensin ii in vascular smooth muscle cells
    • Adachi T., Pimentel D.R., Heibeck T., Hou X., Lee Y.J., Jiang B., et al. S-glutathiolation of Ras mediates redox-sensitive signaling by Angiotensin ii in vascular smooth muscle cells. J Biol Chem 279 (2004) 29857-29862
    • (2004) J Biol Chem , vol.279 , pp. 29857-29862
    • Adachi, T.1    Pimentel, D.R.2    Heibeck, T.3    Hou, X.4    Lee, Y.J.5    Jiang, B.6
  • 89
    • 33645806282 scopus 로고    scopus 로고
    • S-glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells
    • Clavreul N., Adachi T., Pimental D.R., Ido Y., Schoneich C., and Cohen R.A. S-glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells. FASEB J 20 (2006) 518-520
    • (2006) FASEB J , vol.20 , pp. 518-520
    • Clavreul, N.1    Adachi, T.2    Pimental, D.R.3    Ido, Y.4    Schoneich, C.5    Cohen, R.A.6
  • 90
    • 14944371448 scopus 로고    scopus 로고
    • alpha-adrenergic receptor-stimulated hypertrophy in adult rat ventricular myocytes is mediated via thioredoxin-1-sensitive oxidative modification of thiols on Ras
    • Kuster G.M., Pimentel D.R., Adachi T., Ido Y., Brenner D.A., Cohen R.A., et al. alpha-adrenergic receptor-stimulated hypertrophy in adult rat ventricular myocytes is mediated via thioredoxin-1-sensitive oxidative modification of thiols on Ras. Circulation 111 (2005) 1192-1198
    • (2005) Circulation , vol.111 , pp. 1192-1198
    • Kuster, G.M.1    Pimentel, D.R.2    Adachi, T.3    Ido, Y.4    Brenner, D.A.5    Cohen, R.A.6
  • 91
    • 33748526792 scopus 로고    scopus 로고
    • Strain-stimulated hypertrophy in cardiac myocytes is mediated by reactive oxygen species-dependent Ras S-glutathiolation
    • Pimentel D.R., Adachi T., Ido Y., Heibeck T., Jiang B., Lee Y., et al. Strain-stimulated hypertrophy in cardiac myocytes is mediated by reactive oxygen species-dependent Ras S-glutathiolation. J Mol Cell Cardiol 41 (2006) 613-622
    • (2006) J Mol Cell Cardiol , vol.41 , pp. 613-622
    • Pimentel, D.R.1    Adachi, T.2    Ido, Y.3    Heibeck, T.4    Jiang, B.5    Lee, Y.6
  • 92
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
    • Jia L., Bonaventura C., Bonaventura J., and Stamler J.S. S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature 380 (1996) 221-226
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 93
    • 11244316895 scopus 로고    scopus 로고
    • Chemical physiology of blood flow regulation by red blood cells: the role of nitric oxide and S-nitrosohemoglobin
    • Singel D.J., and Stamler J.S. Chemical physiology of blood flow regulation by red blood cells: the role of nitric oxide and S-nitrosohemoglobin. Annu Rev Physiol 67 (2005) 99-145
    • (2005) Annu Rev Physiol , vol.67 , pp. 99-145
    • Singel, D.J.1    Stamler, J.S.2
  • 94
    • 0022828370 scopus 로고
    • Covalent binding of glutathione to hemoglobin. I. Inhibition of hemoglobin S polymerization
    • Garel M.C., Domenget C., Caburi-Martin J., Prehu C., Galacteros F., and Beuzard Y. Covalent binding of glutathione to hemoglobin. I. Inhibition of hemoglobin S polymerization. J Biol Chem 261 (1986) 14704-14709
    • (1986) J Biol Chem , vol.261 , pp. 14704-14709
    • Garel, M.C.1    Domenget, C.2    Caburi-Martin, J.3    Prehu, C.4    Galacteros, F.5    Beuzard, Y.6
  • 95
    • 0022829566 scopus 로고
    • Covalent binding of glutathione to hemoglobin. II. Functional consequences and structural changes reflected in NMR spectra
    • Craescu C.T., Poyart C., Schaeffer C., Garel M.C., Kister J., and Beuzard Y. Covalent binding of glutathione to hemoglobin. II. Functional consequences and structural changes reflected in NMR spectra. J Biol Chem 261 (1986) 14710-14716
    • (1986) J Biol Chem , vol.261 , pp. 14710-14716
    • Craescu, C.T.1    Poyart, C.2    Schaeffer, C.3    Garel, M.C.4    Kister, J.5    Beuzard, Y.6
  • 96
    • 0030982523 scopus 로고    scopus 로고
    • Low concentrations of nitric oxide increase oxygen affinity of sickle erythrocytes in vitro and in vivo
    • Head C.A., Brugnara C., Martinez-Ruiz R., Kacmarek R.M., Bridges K.R., Kuter D., et al. Low concentrations of nitric oxide increase oxygen affinity of sickle erythrocytes in vitro and in vivo. J Clin Invest 100 (1997) 1193-1198
    • (1997) J Clin Invest , vol.100 , pp. 1193-1198
    • Head, C.A.1    Brugnara, C.2    Martinez-Ruiz, R.3    Kacmarek, R.M.4    Bridges, K.R.5    Kuter, D.6
  • 97
    • 34250794356 scopus 로고    scopus 로고
    • Proteome analysis of oxidative stress: glutathionyl hemoglobin in diabetic and uremic patients
    • Dalle-Donne I., Scaloni A., and Butterfield D.A. (Eds), Wiley-Interscience
    • Niwa T. Proteome analysis of oxidative stress: glutathionyl hemoglobin in diabetic and uremic patients. In: Dalle-Donne I., Scaloni A., and Butterfield D.A. (Eds). Redox Proteomics (2006), Wiley-Interscience 651-667
    • (2006) Redox Proteomics , pp. 651-667
    • Niwa, T.1
  • 98
    • 0030662226 scopus 로고    scopus 로고
    • Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms
    • Kim Y.-M., Talanian R.V., and Billiar T.R. Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms. J Biol Chem 272 (1997) 31138-31148
    • (1997) J Biol Chem , vol.272 , pp. 31138-31148
    • Kim, Y.-M.1    Talanian, R.V.2    Billiar, T.R.3
  • 99
    • 0030827880 scopus 로고    scopus 로고
    • Nitric oxide inhibits Fas-induced apoptosis
    • Mannick J.B., Miao X.Q., and Stamler J.S. Nitric oxide inhibits Fas-induced apoptosis. J Biol Chem 272 (1997) 24125-24128
    • (1997) J Biol Chem , vol.272 , pp. 24125-24128
    • Mannick, J.B.1    Miao, X.Q.2    Stamler, J.S.3
  • 102
    • 33644818614 scopus 로고    scopus 로고
    • Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine
    • Mitchell D.A., and Marletta M.A. Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine. Nat Chem Biol 1 (2005) 154-158
    • (2005) Nat Chem Biol , vol.1 , pp. 154-158
    • Mitchell, D.A.1    Marletta, M.A.2
  • 103
    • 34250734460 scopus 로고    scopus 로고
    • Design and characterization of an active site selective caspase-3 transnitrosating agent
    • Mitchell D.A., Morton S.U., and Marletta M.A. Design and characterization of an active site selective caspase-3 transnitrosating agent. ACS Chem Biol 1 (2006) 659-665
    • (2006) ACS Chem Biol , vol.1 , pp. 659-665
    • Mitchell, D.A.1    Morton, S.U.2    Marletta, M.A.3
  • 104
    • 0033597924 scopus 로고    scopus 로고
    • Mass spectrometric analysis of nitric oxide-modified caspase-3
    • Zech B., Wilm M., van Eldik R., and Brüne B. Mass spectrometric analysis of nitric oxide-modified caspase-3. J Biol Chem 274 (1999) 20931-20936
    • (1999) J Biol Chem , vol.274 , pp. 20931-20936
    • Zech, B.1    Wilm, M.2    van Eldik, R.3    Brüne, B.4
  • 105
    • 0034662178 scopus 로고    scopus 로고
    • Novel application of S-nitrosoglutathione-Sepharose to identify proteins that are potential targets for S-nitrosoglutathione-induced mixed-disulphide formation
    • Klatt P., Pineda Molina E., Pérez-Sala D., and Lamas S. Novel application of S-nitrosoglutathione-Sepharose to identify proteins that are potential targets for S-nitrosoglutathione-induced mixed-disulphide formation. Biochem J 349 (2000) 567-578
    • (2000) Biochem J , vol.349 , pp. 567-578
    • Klatt, P.1    Pineda Molina, E.2    Pérez-Sala, D.3    Lamas, S.4
  • 106
    • 33846809031 scopus 로고    scopus 로고
    • Glutathiolation regulates tumor necrosis factor-{alpha}-induced caspase-3 cleavage and apoptosis: key role for glutaredoxin in the death pathway
    • Pan S., and Berk B.C. Glutathiolation regulates tumor necrosis factor-{alpha}-induced caspase-3 cleavage and apoptosis: key role for glutaredoxin in the death pathway. Circ Res 100 (2007) 213-219
    • (2007) Circ Res , vol.100 , pp. 213-219
    • Pan, S.1    Berk, B.C.2
  • 107
    • 0033550050 scopus 로고    scopus 로고
    • Inhibition of cathepsin K by nitric oxide donors: evidence for the formation of mixed disulfides and a sulfenic acid
    • Percival M.D., Ouellet M., Campagnolo C., Claveau D., and Li C. Inhibition of cathepsin K by nitric oxide donors: evidence for the formation of mixed disulfides and a sulfenic acid. Biochemistry 38 (1999) 13574-13583
    • (1999) Biochemistry , vol.38 , pp. 13574-13583
    • Percival, M.D.1    Ouellet, M.2    Campagnolo, C.3    Claveau, D.4    Li, C.5
  • 110
  • 111
    • 21344446613 scopus 로고    scopus 로고
    • Effects of S-glutathionylation and S-nitrosylation on calmodulin binding to triads and FKBP12 binding to type 1 calcium release channels
    • Aracena P., Tang W., Hamilton S.L., and Hidalgo C. Effects of S-glutathionylation and S-nitrosylation on calmodulin binding to triads and FKBP12 binding to type 1 calcium release channels. Antioxid Redox Signal 7 (2005) 870-881
    • (2005) Antioxid Redox Signal , vol.7 , pp. 870-881
    • Aracena, P.1    Tang, W.2    Hamilton, S.L.3    Hidalgo, C.4
  • 112
    • 0034617146 scopus 로고    scopus 로고
    • Inhibition of Papain by S-Nitrosothiols. Formation of mixed disulfides
    • Xian M., Chen X., Liu Z., Wang K., and Wang P.G. Inhibition of Papain by S-Nitrosothiols. Formation of mixed disulfides. J Biol Chem 275 (2000) 20467-20473
    • (2000) J Biol Chem , vol.275 , pp. 20467-20473
    • Xian, M.1    Chen, X.2    Liu, Z.3    Wang, K.4    Wang, P.G.5
  • 113
    • 13544274436 scopus 로고    scopus 로고
    • Reversible silencing of CFTR chloride channels by glutathionylation
    • Wang W., Oliva C., Li G., Holmgren A., Lillig C.H., and Kirk K.L. Reversible silencing of CFTR chloride channels by glutathionylation. J Gen Physiol 125 (2005) 127-141
    • (2005) J Gen Physiol , vol.125 , pp. 127-141
    • Wang, W.1    Oliva, C.2    Li, G.3    Holmgren, A.4    Lillig, C.H.5    Kirk, K.L.6
  • 114
    • 0033515479 scopus 로고    scopus 로고
    • Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase
    • Mohr S., Hallak H., de Boitte A., Lapetina E.G., and Brüne B. Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 274 (1999) 9427-9430
    • (1999) J Biol Chem , vol.274 , pp. 9427-9430
    • Mohr, S.1    Hallak, H.2    de Boitte, A.3    Lapetina, E.G.4    Brüne, B.5
  • 115
    • 1842486832 scopus 로고    scopus 로고
    • Protein S-glutathiolation triggered by decomposed S-nitrosoglutathione
    • Tao L., and English A.M. Protein S-glutathiolation triggered by decomposed S-nitrosoglutathione. Biochemistry 43 (2004) 4028-4038
    • (2004) Biochemistry , vol.43 , pp. 4028-4038
    • Tao, L.1    English, A.M.2
  • 116
    • 33646187917 scopus 로고    scopus 로고
    • Reactive nitrogen species derived activation of rat liver microsomal glutathione S-transferase
    • Imaizumi N., Miyagi S., and Aniya Y. Reactive nitrogen species derived activation of rat liver microsomal glutathione S-transferase. Life Sci 78 (2006) 2998-3006
    • (2006) Life Sci , vol.78 , pp. 2998-3006
    • Imaizumi, N.1    Miyagi, S.2    Aniya, Y.3
  • 117
    • 0034691305 scopus 로고    scopus 로고
    • Calcium-sensitive interaction between calmodulin and modified forms of rat brain neurogranin/RC3
    • Huang K.P., Huang F.L., Li J., Schuck P., and McPhie P. Calcium-sensitive interaction between calmodulin and modified forms of rat brain neurogranin/RC3. Biochemistry 39 (2000) 7291-7299
    • (2000) Biochemistry , vol.39 , pp. 7291-7299
    • Huang, K.P.1    Huang, F.L.2    Li, J.3    Schuck, P.4    McPhie, P.5
  • 118
    • 0035793599 scopus 로고    scopus 로고
    • Glutathiolation of proteins by glutathione disulfide S-oxide derived from S-nitrosoglutathione. Modifications of rat brain neurogranin/RC3 and neuromodulin/GAP-43
    • Li J., Huang F.L., and Huang K.-P. Glutathiolation of proteins by glutathione disulfide S-oxide derived from S-nitrosoglutathione. Modifications of rat brain neurogranin/RC3 and neuromodulin/GAP-43. J Biol Chem 276 (2001) 3098-3105
    • (2001) J Biol Chem , vol.276 , pp. 3098-3105
    • Li, J.1    Huang, F.L.2    Huang, K.-P.3
  • 119
    • 0035800858 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation
    • Okamoto T., Akaike T., Sawa T., Miyamoto Y., van der Vliet A., and Maeda H. Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation. J Biol Chem 276 (2001) 29596-29602
    • (2001) J Biol Chem , vol.276 , pp. 29596-29602
    • Okamoto, T.1    Akaike, T.2    Sawa, T.3    Miyamoto, Y.4    van der Vliet, A.5    Maeda, H.6
  • 120
    • 22044436241 scopus 로고    scopus 로고
    • S-thiolation of tyrosine hydroxylase by reactive nitrogen species in the presence of cysteine or glutathione
    • Sadidi M., Geddes T.J., and Kuhn D.M. S-thiolation of tyrosine hydroxylase by reactive nitrogen species in the presence of cysteine or glutathione. Antioxid Redox Signal 7 (2005) 863-869
    • (2005) Antioxid Redox Signal , vol.7 , pp. 863-869
    • Sadidi, M.1    Geddes, T.J.2    Kuhn, D.M.3
  • 121
    • 23944468310 scopus 로고    scopus 로고
    • Redox regulation of PTEN by S-nitrosothiols
    • Yu C.X., Li S., and Whorton A.R. Redox regulation of PTEN by S-nitrosothiols. Mol Pharmacol 68 (2005) 847-854
    • (2005) Mol Pharmacol , vol.68 , pp. 847-854
    • Yu, C.X.1    Li, S.2    Whorton, A.R.3


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