메뉴 건너뛰기




Volumn 52, Issue 3, 2012, Pages 559-567

Protein S-glutathiolation: Redox-sensitive regulation of protein function

Author keywords

Glutathionylation; Heart; Nitric oxide; Oxidative stress; Protein mixed disulfides; Vasculature

Indexed keywords

ARYLDIALKYLPHOSPHATASE 1; ENDOTHELIAL NITRIC OXIDE SYNTHASE; GLUTAREDOXIN; GLUTATHIONE; GLUTATHIONE DISULFIDE; MYOSIN HEAVY CHAIN; NITRIC OXIDE; OXIDIZED LOW DENSITY LIPOPROTEIN; PROTEIN KINASE C; PROTEIN S; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 84857630703     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2011.07.009     Document Type: Review
Times cited : (106)

References (150)
  • 2
    • 65049087190 scopus 로고    scopus 로고
    • Glutathione: overview of its protective roles, measurement, and biosynthesis
    • Forman H.J., Zhang H., Rinna A. Glutathione: overview of its protective roles, measurement, and biosynthesis. Mol Aspects Med 2009, 30:1-12.
    • (2009) Mol Aspects Med , vol.30 , pp. 1-12
    • Forman, H.J.1    Zhang, H.2    Rinna, A.3
  • 3
    • 0027935268 scopus 로고
    • The redox couple between glutathione and ascorbic acid: a chemical and physiological perspective
    • Winkler B.S., Orselli S.M., Rex T.S. The redox couple between glutathione and ascorbic acid: a chemical and physiological perspective. Free Radic Biol Med 1994, 17:333-349.
    • (1994) Free Radic Biol Med , vol.17 , pp. 333-349
    • Winkler, B.S.1    Orselli, S.M.2    Rex, T.S.3
  • 4
    • 0016773981 scopus 로고
    • Effects of pH and thiols on the kinetics of yeast glyoxalase I. An evaluation of the random pathway mechanism
    • Vander Jagt D.L., Daub E., Krohn J.A., Han L.P. Effects of pH and thiols on the kinetics of yeast glyoxalase I. An evaluation of the random pathway mechanism. Biochemistry 1975, 14:3669-3675.
    • (1975) Biochemistry , vol.14 , pp. 3669-3675
    • Vander Jagt, D.L.1    Daub, E.2    Krohn, J.A.3    Han, L.P.4
  • 6
    • 77951299314 scopus 로고    scopus 로고
    • RLIP76: a versatile transporter and an emerging target for cancer therapy
    • Vatsyayan R., Lelsani P.C., Awasthi S., Singhal S.S. RLIP76: a versatile transporter and an emerging target for cancer therapy. Biochem Pharmacol 2010, 79:1699-1705.
    • (2010) Biochem Pharmacol , vol.79 , pp. 1699-1705
    • Vatsyayan, R.1    Lelsani, P.C.2    Awasthi, S.3    Singhal, S.S.4
  • 7
    • 0014458353 scopus 로고
    • The role of glutathione and glutathione S-transferases in mercapturic acid biosynthesis
    • Boyland E., Chasseaud L.F. The role of glutathione and glutathione S-transferases in mercapturic acid biosynthesis. Adv Enzymol Relat Areas Mol Biol 1969, 32:173-219.
    • (1969) Adv Enzymol Relat Areas Mol Biol , vol.32 , pp. 173-219
    • Boyland, E.1    Chasseaud, L.F.2
  • 8
    • 47649128397 scopus 로고    scopus 로고
    • Modulating GSH synthesis using glutamate cysteine ligase transgenic and gene-targeted mice
    • Botta D., White C.C., Vliet-Gregg P., Mohar I., Shi S., McGrath M.B., et al. Modulating GSH synthesis using glutamate cysteine ligase transgenic and gene-targeted mice. Drug Metab Rev 2008, 40:465-477.
    • (2008) Drug Metab Rev , vol.40 , pp. 465-477
    • Botta, D.1    White, C.C.2    Vliet-Gregg, P.3    Mohar, I.4    Shi, S.5    McGrath, M.B.6
  • 9
    • 65049090568 scopus 로고    scopus 로고
    • Plasma membrane glutathione transporters and their roles in cell physiology and pathophysiology
    • Ballatori N., Krance S.M., Marchan R., Hammond C.L. Plasma membrane glutathione transporters and their roles in cell physiology and pathophysiology. Mol Aspects Med 2009, 30:13-28.
    • (2009) Mol Aspects Med , vol.30 , pp. 13-28
    • Ballatori, N.1    Krance, S.M.2    Marchan, R.3    Hammond, C.L.4
  • 10
    • 0021284165 scopus 로고
    • Redox control of enzyme activities by thiol/disulfide exchange
    • Gilbert H.F. Redox control of enzyme activities by thiol/disulfide exchange. Methods Enzymol 1984, 107:330-351.
    • (1984) Methods Enzymol , vol.107 , pp. 330-351
    • Gilbert, H.F.1
  • 11
    • 38349049487 scopus 로고    scopus 로고
    • S-glutathionylation: indicator of cell stress and regulator of the unfolded protein response
    • Townsend D.M. S-glutathionylation: indicator of cell stress and regulator of the unfolded protein response. Mol Interv 2007, 7:313-324.
    • (2007) Mol Interv , vol.7 , pp. 313-324
    • Townsend, D.M.1
  • 12
    • 39749200944 scopus 로고    scopus 로고
    • Assessment of endoplasmic reticulum glutathione redox status is confounded by extensive ex vivo oxidation
    • Dixon B.M., Heath S.H., Kim R., Suh J.H., Hagen T.M. Assessment of endoplasmic reticulum glutathione redox status is confounded by extensive ex vivo oxidation. Antioxid Redox Signal 2008, 10(5):963-972.
    • (2008) Antioxid Redox Signal , vol.10 , Issue.5 , pp. 963-972
    • Dixon, B.M.1    Heath, S.H.2    Kim, R.3    Suh, J.H.4    Hagen, T.M.5
  • 13
    • 78650068036 scopus 로고    scopus 로고
    • Regulation of mitochondrial glutathione redox status and protein glutathionylation by respiratory substrates
    • Garcia J., Han D., Sancheti H., Yap L.P., Kaplowitz N., Cadenas E. Regulation of mitochondrial glutathione redox status and protein glutathionylation by respiratory substrates. J Biol Chem 2010, 285:39646-39654.
    • (2010) J Biol Chem , vol.285 , pp. 39646-39654
    • Garcia, J.1    Han, D.2    Sancheti, H.3    Yap, L.P.4    Kaplowitz, N.5    Cadenas, E.6
  • 14
    • 34547383742 scopus 로고
    • Glutathione: its influence in the oxidation of fats and proteins
    • Hopkins F.G. Glutathione: its influence in the oxidation of fats and proteins. Biochem J 1925, 19:787-819.
    • (1925) Biochem J , vol.19 , pp. 787-819
    • Hopkins, F.G.1
  • 15
    • 0001131999 scopus 로고
    • On an autoxidisable constituent of the cell
    • Hopkins F.G. On an autoxidisable constituent of the cell. Biochem J 1921, 15:286-305.
    • (1921) Biochem J , vol.15 , pp. 286-305
    • Hopkins, F.G.1
  • 16
    • 33847021426 scopus 로고    scopus 로고
    • Role of glutathiolation in preservation, restoration and regulation of protein function
    • Hill B.G., Bhatnagar A. Role of glutathiolation in preservation, restoration and regulation of protein function. IUBMB Life 2007, 59:21-26.
    • (2007) IUBMB Life , vol.59 , pp. 21-26
    • Hill, B.G.1    Bhatnagar, A.2
  • 17
    • 31044455445 scopus 로고    scopus 로고
    • Redox modifications of protein-thiols: emerging roles in cell signaling
    • Biswas S., Chida A.S., Rahman I. Redox modifications of protein-thiols: emerging roles in cell signaling. Biochem Pharmacol 2006, 71:551-564.
    • (2006) Biochem Pharmacol , vol.71 , pp. 551-564
    • Biswas, S.1    Chida, A.S.2    Rahman, I.3
  • 20
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • Klatt P., Lamas S. Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur J Biochem 2000, 267:4928-4944.
    • (2000) Eur J Biochem , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 21
    • 0029015864 scopus 로고
    • Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas J.A., Poland B., Honzatko R. Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch Biochem Biophys 1995, 319:1-9.
    • (1995) Arch Biochem Biophys , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 22
    • 0021891877 scopus 로고
    • Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation
    • Ziegler D.M. Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation. Annu Rev Biochem 1985, 54:305-329.
    • (1985) Annu Rev Biochem , vol.54 , pp. 305-329
    • Ziegler, D.M.1
  • 23
    • 1242294484 scopus 로고    scopus 로고
    • A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein
    • Bass R., Ruddock L.W., Klappa P., Freedman R.B. A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein. J Biol Chem 2004, 279:5257-5262.
    • (2004) J Biol Chem , vol.279 , pp. 5257-5262
    • Bass, R.1    Ruddock, L.W.2    Klappa, P.3    Freedman, R.B.4
  • 24
    • 0017339770 scopus 로고
    • Glutathione dependent control of protein disulfide-sulfhydryl content by subcellular fractions of hepatic tissue
    • Isaacs J., Binkley F. Glutathione dependent control of protein disulfide-sulfhydryl content by subcellular fractions of hepatic tissue. Biochim Biophys Acta 1977, 497:192-204.
    • (1977) Biochim Biophys Acta , vol.497 , pp. 192-204
    • Isaacs, J.1    Binkley, F.2
  • 25
    • 0023131131 scopus 로고
    • Glutathione levels in cultured heart cells. Influence of buthionine sulfoximine, an inhibitor of glutathione synthesis
    • Lewko W.M. Glutathione levels in cultured heart cells. Influence of buthionine sulfoximine, an inhibitor of glutathione synthesis. Biochem Pharmacol 1987, 36:219-223.
    • (1987) Biochem Pharmacol , vol.36 , pp. 219-223
    • Lewko, W.M.1
  • 26
    • 0019948316 scopus 로고
    • The relationship of biliary glutathione disulfide efflux and intracellular glutathione disulfide content in perfused rat liver
    • Akerboom T.P., Bilzer M., Sies H. The relationship of biliary glutathione disulfide efflux and intracellular glutathione disulfide content in perfused rat liver. J Biol Chem 1982, 257:4248-4252.
    • (1982) J Biol Chem , vol.257 , pp. 4248-4252
    • Akerboom, T.P.1    Bilzer, M.2    Sies, H.3
  • 27
    • 0021969405 scopus 로고
    • Detection of oxidized and reduced glutathione with a recycling postcolumn reaction
    • Alpert A.J., Gilbert H.F. Detection of oxidized and reduced glutathione with a recycling postcolumn reaction. Anal Biochem 1985, 144:553-562.
    • (1985) Anal Biochem , vol.144 , pp. 553-562
    • Alpert, A.J.1    Gilbert, H.F.2
  • 29
    • 65049090568 scopus 로고    scopus 로고
    • Plasma membrane glutathione transporters and their roles in cell physiology and pathophysiology
    • Ballatori N., Krance S.M., Marchan R., Hammond C.L. Plasma membrane glutathione transporters and their roles in cell physiology and pathophysiology. Mol Aspects Med 2009, 30:13-28.
    • (2009) Mol Aspects Med , vol.30 , pp. 13-28
    • Ballatori, N.1    Krance, S.M.2    Marchan, R.3    Hammond, C.L.4
  • 30
    • 0025298423 scopus 로고
    • Glutathione depletion and formation of glutathione-protein mixed disulfide following exposure of brain mitochondria to oxidative stress
    • Ravindranath V., Reed D.J. Glutathione depletion and formation of glutathione-protein mixed disulfide following exposure of brain mitochondria to oxidative stress. Biochem Biophys Res Commun 1990, 169:1075-1079.
    • (1990) Biochem Biophys Res Commun , vol.169 , pp. 1075-1079
    • Ravindranath, V.1    Reed, D.J.2
  • 31
    • 58249083482 scopus 로고    scopus 로고
    • Myocardial ischaemia inhibits mitochondrial metabolism of 4-hydroxy-trans-2-nonenal
    • Hill B.G., Awe S.O., Vladykovskaya E., Ahmed Y., Liu S.Q., Bhatnagar A., et al. Myocardial ischaemia inhibits mitochondrial metabolism of 4-hydroxy-trans-2-nonenal. Biochem J 2009, 417:513-524.
    • (2009) Biochem J , vol.417 , pp. 513-524
    • Hill, B.G.1    Awe, S.O.2    Vladykovskaya, E.3    Ahmed, Y.4    Liu, S.Q.5    Bhatnagar, A.6
  • 33
    • 70249123518 scopus 로고    scopus 로고
    • Hemoglobin glutathionylation can occur through cysteine sulfenic acid intermediate: electrospray ionization LTQ-Orbitrap hybrid mass spectrometry studies
    • Regazzoni L., Panusa A., Yeum K.J., Carini M., Aldini G. Hemoglobin glutathionylation can occur through cysteine sulfenic acid intermediate: electrospray ionization LTQ-Orbitrap hybrid mass spectrometry studies. J Chromatogr B Analyt Technol Biomed Life Sci 2009, 877:3456-3461.
    • (2009) J Chromatogr B Analyt Technol Biomed Life Sci , vol.877 , pp. 3456-3461
    • Regazzoni, L.1    Panusa, A.2    Yeum, K.J.3    Carini, M.4    Aldini, G.5
  • 34
    • 66349105304 scopus 로고    scopus 로고
    • Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo
    • Greetham D., Grant C.M. Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo. Mol Cell Biol 2009, 29:3229-3240.
    • (2009) Mol Cell Biol , vol.29 , pp. 3229-3240
    • Greetham, D.1    Grant, C.M.2
  • 35
    • 43549092673 scopus 로고    scopus 로고
    • Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome
    • Silva G.M., Netto L.E., Discola K.F., Piassa-Filho G.M., Pimenta D.C., Barcena J.A., et al. Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome. FEBS J 2008, 275:2942-2955.
    • (2008) FEBS J , vol.275 , pp. 2942-2955
    • Silva, G.M.1    Netto, L.E.2    Discola, K.F.3    Piassa-Filho, G.M.4    Pimenta, D.C.5    Barcena, J.A.6
  • 36
    • 0037414784 scopus 로고    scopus 로고
    • 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated
    • Demasi M., Silva G.M., Netto L.E. 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated. J Biol Chem 2003, 278:679-685.
    • (2003) J Biol Chem , vol.278 , pp. 679-685
    • Demasi, M.1    Silva, G.M.2    Netto, L.E.3
  • 37
    • 43249104849 scopus 로고    scopus 로고
    • Regulatory control of human cytosolic branched-chain aminotransferase by oxidation and S-glutathionylation and its interactions with redox sensitive neuronal proteins
    • Conway M.E., Coles S.J., Islam M.M., Hutson S.M. Regulatory control of human cytosolic branched-chain aminotransferase by oxidation and S-glutathionylation and its interactions with redox sensitive neuronal proteins. Biochemistry 2008, 47:5465-5479.
    • (2008) Biochemistry , vol.47 , pp. 5465-5479
    • Conway, M.E.1    Coles, S.J.2    Islam, M.M.3    Hutson, S.M.4
  • 38
    • 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., Bhatnagar A. Protein glutathiolation by nitric oxide: an intracellular mechanism regulating redox protein modification. FASEB J 2006, 20:1715-1717.
    • (2006) FASEB J , vol.20 , pp. 1715-1717
    • West, M.B.1    Hill, B.G.2    Xuan, Y.T.3    Bhatnagar, A.4
  • 39
    • 33748339203 scopus 로고    scopus 로고
    • Dynamic redox control of NF-kappaB through glutaredoxin-regulated S-glutathionylation of inhibitory kappaB kinase beta
    • Reynaert N.L., van der Vliet A., Guala A.S., McGovern T., Hristova M., Pantano C., et al. Dynamic redox control of NF-kappaB through glutaredoxin-regulated S-glutathionylation of inhibitory kappaB kinase beta. Proc Natl Acad Sci USA 2006, 103:13086-13091.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13086-13091
    • Reynaert, N.L.1    van der Vliet, A.2    Guala, A.S.3    McGovern, T.4    Hristova, M.5    Pantano, C.6
  • 40
    • 44049084268 scopus 로고    scopus 로고
    • Role of nitric oxide in regulating aldose reductase activation in the ischemic heart
    • Kaiserova K., Tang X.L., Srivastava S., Bhatnagar A. Role of nitric oxide in regulating aldose reductase activation in the ischemic heart. J Biol Chem 2008, 283:9101-9112.
    • (2008) J Biol Chem , vol.283 , pp. 9101-9112
    • Kaiserova, K.1    Tang, X.L.2    Srivastava, S.3    Bhatnagar, A.4
  • 41
    • 70450080716 scopus 로고    scopus 로고
    • The role of signalling molecules on actin glutathionylation and protein carbonylation induced by cadmium in haemocytes of mussel Mytilus galloprovincialis (Lmk)
    • Dailianis S., Patetsini E., Kaloyianni M. The role of signalling molecules on actin glutathionylation and protein carbonylation induced by cadmium in haemocytes of mussel Mytilus galloprovincialis (Lmk). J Exp Biol 2009, 212:3612-3620.
    • (2009) J Exp Biol , vol.212 , pp. 3612-3620
    • Dailianis, S.1    Patetsini, E.2    Kaloyianni, M.3
  • 42
    • 31044436627 scopus 로고    scopus 로고
    • A glutathione S-transferase pi-activated prodrug causes kinase activation concurrent with S-glutathionylation of proteins
    • Townsend D.M., Findlay V.J., Fazilev F., Ogle M., Fraser J., Saavedra J.E., et al. A glutathione S-transferase pi-activated prodrug causes kinase activation concurrent with S-glutathionylation of proteins. Mol Pharmacol 2006, 69:501-508.
    • (2006) Mol Pharmacol , vol.69 , pp. 501-508
    • Townsend, D.M.1    Findlay, V.J.2    Fazilev, F.3    Ogle, M.4    Fraser, J.5    Saavedra, J.E.6
  • 43
    • 59049103695 scopus 로고    scopus 로고
    • Posttranslational glutathiolation of aldose reductase (AKR1B1): a possible mechanism of protein recovery from S-nitrosylation
    • Baba S.P., Wetzelberger K., Hoetker J.D., Bhatnagar A. Posttranslational glutathiolation of aldose reductase (AKR1B1): a possible mechanism of protein recovery from S-nitrosylation. Chem Biol Interact 2009, 178:250-258.
    • (2009) Chem Biol Interact , vol.178 , pp. 250-258
    • Baba, S.P.1    Wetzelberger, K.2    Hoetker, J.D.3    Bhatnagar, A.4
  • 44
    • 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., Schoneich C., et al. S-glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide. Nat Med 2004, 10:1200-1207.
    • (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    Schoneich, C.6
  • 45
    • 33646529673 scopus 로고    scopus 로고
    • Nitric-oxide-induced vasodilatation: regulation by physiologic s-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase
    • Cohen R.A., Adachi T. Nitric-oxide-induced vasodilatation: regulation by physiologic s-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase. Trends Cardiovasc Med 2006, 16:109-114.
    • (2006) Trends Cardiovasc Med , vol.16 , pp. 109-114
    • Cohen, R.A.1    Adachi, T.2
  • 46
    • 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., Cohen R.A. S-glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells. FASEB J 2006, 20:518-520.
    • (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
  • 47
    • 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., Brune B. Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 1999, 274:9427-9430.
    • (1999) J Biol Chem , vol.274 , pp. 9427-9430
    • Mohr, S.1    Hallak, H.2    de Boitte, A.3    Lapetina, E.G.4    Brune, B.5
  • 48
    • 59249105149 scopus 로고    scopus 로고
    • S-nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and S-thiolation
    • Coles S.J., Easton P., Sharrod H., Hutson S.M., Hancock J., Patel V.B., et al. S-nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and S-thiolation. Biochemistry 2009, 48:645-656.
    • (2009) Biochemistry , vol.48 , pp. 645-656
    • Coles, S.J.1    Easton, P.2    Sharrod, H.3    Hutson, S.M.4    Hancock, J.5    Patel, V.B.6
  • 49
    • 79954992084 scopus 로고    scopus 로고
    • Modulation of cardiac ryanodine receptor activity by ROS and RNS
    • Donoso P., Sanchez G., Bull R., Hidalgo C. Modulation of cardiac ryanodine receptor activity by ROS and RNS. Front Biosci 2011, 16:553-567.
    • (2011) Front Biosci , vol.16 , pp. 553-567
    • Donoso, P.1    Sanchez, G.2    Bull, R.3    Hidalgo, C.4
  • 50
    • 47049113679 scopus 로고    scopus 로고
    • Protein cysteine thiol nitrosation: maker or marker of reactive nitrogen species-induced nonerythroid cellular signaling?
    • Lancaster J.R. Protein cysteine thiol nitrosation: maker or marker of reactive nitrogen species-induced nonerythroid cellular signaling?. Nitric Oxide 2008, 19:68-72.
    • (2008) Nitric Oxide , vol.19 , pp. 68-72
    • Lancaster, J.R.1
  • 52
    • 0036709885 scopus 로고    scopus 로고
    • Glutathionylation of proteins by glutathione disulfide S-oxide
    • Huang K.P., Huang F.L. Glutathionylation of proteins by glutathione disulfide S-oxide. Biochem Pharmacol 2002, 64:1049-1056.
    • (2002) Biochem Pharmacol , vol.64 , pp. 1049-1056
    • Huang, K.P.1    Huang, F.L.2
  • 53
    • 58649100268 scopus 로고    scopus 로고
    • Novel role for glutathione S-transferase pi. Regulator of protein S-glutathionylation following oxidative and nitrosative stress
    • Townsend D.M., Manevich Y., He L., Hutchens S., Pazoles C.J., Tew K.D. Novel role for glutathione S-transferase pi. Regulator of protein S-glutathionylation following oxidative and nitrosative stress. J Biol Chem 2009, 284:436-445.
    • (2009) J Biol Chem , vol.284 , pp. 436-445
    • Townsend, D.M.1    Manevich, Y.2    He, L.3    Hutchens, S.4    Pazoles, C.J.5    Tew, K.D.6
  • 54
    • 51349142890 scopus 로고    scopus 로고
    • Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: implications for intracellular roles
    • Gallogly M.M., Starke D.W., Leonberg A.K., Ospina S.M., Mieyal J.J. Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: implications for intracellular roles. Biochemistry 2008, 47:11144-11157.
    • (2008) Biochemistry , vol.47 , pp. 11144-11157
    • Gallogly, M.M.1    Starke, D.W.2    Leonberg, A.K.3    Ospina, S.M.4    Mieyal, J.J.5
  • 55
    • 1642326559 scopus 로고    scopus 로고
    • Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST
    • Manevich Y., Feinstein S.I., Fisher A.B. Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST. Proc Natl Acad Sci USA 2004, 101:3780-3785.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3780-3785
    • Manevich, Y.1    Feinstein, S.I.2    Fisher, A.B.3
  • 56
    • 77956205147 scopus 로고    scopus 로고
    • Postischemic deactivation of cardiac aldose reductase: role of glutathione S-transferase P and glutaredoxin in regeneration of reduced thiols from sulfenic acids
    • Wetzelberger K., Baba S.P., Thirunavukkarasu M., Ho Y.S., Maulik N., Barski O.A., et al. Postischemic deactivation of cardiac aldose reductase: role of glutathione S-transferase P and glutaredoxin in regeneration of reduced thiols from sulfenic acids. J Biol Chem 2010, 285:26135-26148.
    • (2010) J Biol Chem , vol.285 , pp. 26135-26148
    • Wetzelberger, K.1    Baba, S.P.2    Thirunavukkarasu, M.3    Ho, Y.S.4    Maulik, N.5    Barski, O.A.6
  • 58
    • 51349088530 scopus 로고    scopus 로고
    • Molecular mechanisms and clinical implications of reversible protein S-glutathionylation
    • Mieyal J.J., Gallogly M.M., Qanungo S., Sabens E.A., Shelton M.D. Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid Redox Signal 2008, 10:1941-1988.
    • (2008) Antioxid Redox Signal , vol.10 , pp. 1941-1988
    • Mieyal, J.J.1    Gallogly, M.M.2    Qanungo, S.3    Sabens, E.A.4    Shelton, M.D.5
  • 59
    • 69949115433 scopus 로고    scopus 로고
    • Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin
    • Park J.W., Mieyal J.J., Rhee S.G., Chock P.B. Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin. J Biol Chem 2009, 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
  • 60
    • 20444401524 scopus 로고    scopus 로고
    • Catalysis of thiol/disulfide exchange. Glutaredoxin 1 and protein-disulfide isomerase use different mechanisms to enhance oxidase and reductase activities
    • Xiao R., Lundstrom-Ljung J., Holmgren A., Gilbert H.F. Catalysis of thiol/disulfide exchange. Glutaredoxin 1 and protein-disulfide isomerase use different mechanisms to enhance oxidase and reductase activities. J Biol Chem 2005, 280:21099-21106.
    • (2005) J Biol Chem , vol.280 , pp. 21099-21106
    • Xiao, R.1    Lundstrom-Ljung, J.2    Holmgren, A.3    Gilbert, H.F.4
  • 62
    • 0642334387 scopus 로고    scopus 로고
    • The possible physiological function of thioltransferase in cells
    • Xing K., Lou M.F. The possible physiological function of thioltransferase in cells. FASEB J 2003, 17:2088-2090.
    • (2003) FASEB J , vol.17 , pp. 2088-2090
    • Xing, K.1    Lou, M.F.2
  • 63
    • 79956297624 scopus 로고    scopus 로고
    • FXYD proteins reverse inhibition of the Na+-K+pump mediated by glutathionylation of its β1 subunit
    • Bibert S., Liu C.C., Figtree G.A., Garcia A., Hamilton E.J., Marassi F.M., et al. FXYD proteins reverse inhibition of the Na+-K+pump mediated by glutathionylation of its β1 subunit. J Biol Chem 2011, 286:18562-18572.
    • (2011) J Biol Chem , vol.286 , pp. 18562-18572
    • Bibert, S.1    Liu, C.C.2    Figtree, G.A.3    Garcia, A.4    Hamilton, E.J.5    Marassi, F.M.6
  • 64
    • 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., Torres M. Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am J Physiol Cell Physiol 2004, 287:C246-C256.
    • (2004) Am J Physiol Cell Physiol , vol.287
    • Forman, H.J.1    Fukuto, J.M.2    Torres, M.3
  • 65
    • 0030822346 scopus 로고    scopus 로고
    • Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium
    • Ellis H.R., Poole L.B. Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium. Biochemistry 1997, 36:13349-13356.
    • (1997) Biochemistry , vol.36 , pp. 13349-13356
    • Ellis, H.R.1    Poole, L.B.2
  • 67
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • Gopalakrishna R., Jaken S. Protein kinase C signaling and oxidative stress. Free Radic Biol Med 2000, 28:1349-1361.
    • (2000) Free Radic Biol Med , vol.28 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 68
    • 0037067059 scopus 로고    scopus 로고
    • Factors governing the protonation state of cysteines in proteins: an Ab initio/CDM study
    • Dudev T., Lim C. Factors governing the protonation state of cysteines in proteins: an Ab initio/CDM study. J Am Chem Soc 2002, 124:6759-6766.
    • (2002) J Am Chem Soc , vol.124 , pp. 6759-6766
    • Dudev, T.1    Lim, C.2
  • 72
    • 0038758127 scopus 로고    scopus 로고
    • Methionine adenosyltransferase S-nitrosylation is regulated by the basic and acidic amino acids surrounding the target thiol
    • Perez-Mato I., Castro C., Ruiz F.A., Corrales F.J., Mato J.M. Methionine adenosyltransferase S-nitrosylation is regulated by the basic and acidic amino acids surrounding the target thiol. J Biol Chem 1999, 274:17075-17079.
    • (1999) J Biol Chem , vol.274 , pp. 17075-17079
    • Perez-Mato, I.1    Castro, C.2    Ruiz, F.A.3    Corrales, F.J.4    Mato, J.M.5
  • 73
    • 0030956929 scopus 로고    scopus 로고
    • (S)NO signals: translocation, regulation, and a consensus motif
    • Stamler J.S., Toone E.J., Lipton S.A., Sucher N.J. (S)NO signals: translocation, regulation, and a consensus motif. Neuron 1997, 18:691-696.
    • (1997) Neuron , vol.18 , pp. 691-696
    • Stamler, J.S.1    Toone, E.J.2    Lipton, S.A.3    Sucher, N.J.4
  • 74
    • 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 2003, 423:769-773.
    • (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
  • 75
    • 30744437425 scopus 로고    scopus 로고
    • Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes
    • Ralat L.A., Manevich Y., Fisher A.B., Colman R.F. Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes. Biochemistry 2006, 45:360-372.
    • (2006) Biochemistry , vol.45 , pp. 360-372
    • Ralat, L.A.1    Manevich, Y.2    Fisher, A.B.3    Colman, R.F.4
  • 76
    • 33645456962 scopus 로고    scopus 로고
    • Decline of contractility during ischemia-reperfusion injury: actin glutathionylation and its effect on allosteric interaction with tropomyosin
    • Chen F.C., Ogut O. Decline of contractility during ischemia-reperfusion injury: actin glutathionylation and its effect on allosteric interaction with tropomyosin. Am J Physiol Cell Physiol 2006, 290:C719-C727.
    • (2006) Am J Physiol Cell Physiol , vol.290
    • Chen, F.C.1    Ogut, O.2
  • 77
    • 68049096878 scopus 로고    scopus 로고
    • Reversible oxidative modification: a key mechanism of Na+-K+pump regulation
    • Figtree G.A., Liu C.C., Bibert S., Hamilton E.J., Garcia A., White C.N., et al. Reversible oxidative modification: a key mechanism of Na+-K+pump regulation. Circ Res 2009, 105:185-193.
    • (2009) Circ Res , vol.105 , pp. 185-193
    • Figtree, G.A.1    Liu, C.C.2    Bibert, S.3    Hamilton, E.J.4    Garcia, A.5    White, C.N.6
  • 78
    • 77951544514 scopus 로고    scopus 로고
    • Activation of cAMP-dependent signaling induces oxidative modification of the cardiac Na+-K+pump and inhibits its activity
    • White C.N., Liu C.C., Garcia A., Hamilton E.J., Chia K.K., Figtree G.A., et al. Activation of cAMP-dependent signaling induces oxidative modification of the cardiac Na+-K+pump and inhibits its activity. J Biol Chem 2010, 285:13712-13720.
    • (2010) J Biol Chem , vol.285 , pp. 13712-13720
    • White, C.N.1    Liu, C.C.2    Garcia, A.3    Hamilton, E.J.4    Chia, K.K.5    Figtree, G.A.6
  • 79
    • 27644445283 scopus 로고    scopus 로고
    • Tachycardia increases NADPH oxidase activity and RyR2 S-glutathionylation in ventricular muscle
    • Sanchez G., Pedrozo Z., Domenech R.J., Hidalgo C., Donoso P. Tachycardia increases NADPH oxidase activity and RyR2 S-glutathionylation in ventricular muscle. J Mol Cell Cardiol 2005, 39:982-991.
    • (2005) J Mol Cell Cardiol , vol.39 , pp. 982-991
    • Sanchez, G.1    Pedrozo, Z.2    Domenech, R.J.3    Hidalgo, C.4    Donoso, P.5
  • 80
    • 1842832392 scopus 로고    scopus 로고
    • Glyceraldehyde phosphate dehydrogenase oxidation during cardiac ischemia and reperfusion
    • Eaton P., Wright N., Hearse D.J., Shattock M.J. Glyceraldehyde phosphate dehydrogenase oxidation during cardiac ischemia and reperfusion. J Mol Cell Cardiol 2002, 34:1549-1560.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 1549-1560
    • Eaton, P.1    Wright, N.2    Hearse, D.J.3    Shattock, M.J.4
  • 81
    • 77449119371 scopus 로고    scopus 로고
    • Peptide-based antibodies against glutathione-binding domains suppress superoxide production mediated by mitochondrial complex I
    • Chen J., Chen C.L., Rawale S., Chen C.A., Zweier J.L., Kaumaya P.T., et al. Peptide-based antibodies against glutathione-binding domains suppress superoxide production mediated by mitochondrial complex I. J Biol Chem 2010, 285:3168-3180.
    • (2010) J Biol Chem , vol.285 , pp. 3168-3180
    • Chen, J.1    Chen, C.L.2    Rawale, S.3    Chen, C.A.4    Zweier, J.L.5    Kaumaya, P.T.6
  • 82
    • 77956174156 scopus 로고    scopus 로고
    • Attenuated cardiovascular hypertrophy and oxidant generation in response to angiotensin II infusion in glutaredoxin-1 knockout mice
    • Bachschmid M.M., Xu S., Maitland-Toolan K.A., Ho Y.S., Cohen R.A., Matsui R. Attenuated cardiovascular hypertrophy and oxidant generation in response to angiotensin II infusion in glutaredoxin-1 knockout mice. Free Radic Biol Med 2010, 49:1221-1229.
    • (2010) Free Radic Biol Med , vol.49 , pp. 1221-1229
    • Bachschmid, M.M.1    Xu, S.2    Maitland-Toolan, K.A.3    Ho, Y.S.4    Cohen, R.A.5    Matsui, R.6
  • 83
    • 33750508148 scopus 로고    scopus 로고
    • S-glutathionylation regulates HDL-associated paraoxonase 1 (PON1) activity
    • Rozenberg O., Aviram M. S-glutathionylation regulates HDL-associated paraoxonase 1 (PON1) activity. Biochem Biophys Res Commun 2006, 351:492-498.
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 492-498
    • Rozenberg, O.1    Aviram, M.2
  • 84
    • 0035816705 scopus 로고    scopus 로고
    • Apolipoprotein A-I promotes the formation of phosphatidylcholine core aldehydes that are hydrolyzed by paraoxonase (PON-1) during high density lipoprotein oxidation with a peroxynitrite donor
    • Ahmed Z., Ravandi A., Maguire G.F., Emili A., Draganov D., La Du B.N., et al. Apolipoprotein A-I promotes the formation of phosphatidylcholine core aldehydes that are hydrolyzed by paraoxonase (PON-1) during high density lipoprotein oxidation with a peroxynitrite donor. J Biol Chem 2001, 276:24473-24481.
    • (2001) J Biol Chem , vol.276 , pp. 24473-24481
    • Ahmed, Z.1    Ravandi, A.2    Maguire, G.F.3    Emili, A.4    Draganov, D.5    La Du, B.N.6
  • 85
    • 33746758797 scopus 로고    scopus 로고
    • Molecular mechanism of glutathione-mediated protection from oxidized low-density lipoprotein-induced cell injury in human macrophages: role of glutathione reductase and glutaredoxin
    • Wang Y., Qiao M., Mieyal J.J., Asmis L.M., Asmis R. Molecular mechanism of glutathione-mediated protection from oxidized low-density lipoprotein-induced cell injury in human macrophages: role of glutathione reductase and glutaredoxin. Free Radic Biol Med 2006, 41:775-785.
    • (2006) Free Radic Biol Med , vol.41 , pp. 775-785
    • Wang, Y.1    Qiao, M.2    Mieyal, J.J.3    Asmis, L.M.4    Asmis, R.5
  • 86
    • 33750217204 scopus 로고    scopus 로고
    • S-glutathiolation of p21ras by peroxynitrite mediates endothelial insulin resistance caused by oxidized low-density lipoprotein
    • Clavreul N., Bachschmid M.M., Hou X., Shi C., Idrizovic A., Ido Y., et al. S-glutathiolation of p21ras by peroxynitrite mediates endothelial insulin resistance caused by oxidized low-density lipoprotein. Arterioscler Thromb Vasc Biol 2006, 26:2454-2461.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 2454-2461
    • Clavreul, N.1    Bachschmid, M.M.2    Hou, X.3    Shi, C.4    Idrizovic, A.5    Ido, Y.6
  • 88
    • 33846017353 scopus 로고    scopus 로고
    • Serum levels of S-glutathionylated proteins as a risk-marker for arteriosclerosis obliterans
    • Nonaka K., Kume N., Urata Y., Seto S., Kohno T., Honda S., et al. Serum levels of S-glutathionylated proteins as a risk-marker for arteriosclerosis obliterans. Circ J 2007, 71:100-105.
    • (2007) Circ J , vol.71 , pp. 100-105
    • Nonaka, K.1    Kume, N.2    Urata, Y.3    Seto, S.4    Kohno, T.5    Honda, S.6
  • 89
    • 78650810596 scopus 로고    scopus 로고
    • S-glutathionylation uncouples eNOS and regulates its cellular and vascular function
    • Chen C.A., Wang T.Y., Varadharaj S., Reyes L.A., Hemann C., Talukder M.A., et al. S-glutathionylation uncouples eNOS and regulates its cellular and vascular function. Nature 2010, 468:1115-1118.
    • (2010) Nature , vol.468 , pp. 1115-1118
    • Chen, C.A.1    Wang, T.Y.2    Varadharaj, S.3    Reyes, L.A.4    Hemann, C.5    Talukder, M.A.6
  • 90
    • 78649778002 scopus 로고    scopus 로고
    • Diazeniumdiolate mediated nitrosative stress alters nitric oxide homeostasis through intracellular calcium and S-glutathionylation of nitric oxide synthetase
    • Manevich Y., Townsend D.M., Hutchens S., Tew K.D. Diazeniumdiolate mediated nitrosative stress alters nitric oxide homeostasis through intracellular calcium and S-glutathionylation of nitric oxide synthetase. PLoS One 2010, 5:e14151.
    • (2010) PLoS One , vol.5
    • Manevich, Y.1    Townsend, D.M.2    Hutchens, S.3    Tew, K.D.4
  • 91
    • 79952070504 scopus 로고    scopus 로고
    • Simultaneous measurement of protein oxidation and S-nitrosylation during preconditioning and ischemia/reperfusion injury with resin-assisted capture
    • Kohr M.J., Sun J., Aponte A., Wang G., Gucek M., Murphy E., et al. Simultaneous measurement of protein oxidation and S-nitrosylation during preconditioning and ischemia/reperfusion injury with resin-assisted capture. Circ Res 2011, 108:418-426.
    • (2011) Circ Res , vol.108 , pp. 418-426
    • Kohr, M.J.1    Sun, J.2    Aponte, A.3    Wang, G.4    Gucek, M.5    Murphy, E.6
  • 92
    • 77955175462 scopus 로고    scopus 로고
    • Oxidative posttranslational modifications mediate decreased SERCA activity and myocyte dysfunction in Galphaq-overexpressing mice
    • Lancel S., Qin F., Lennon S.L., Zhang J., Tong X., Mazzini M.J., et al. Oxidative posttranslational modifications mediate decreased SERCA activity and myocyte dysfunction in Galphaq-overexpressing mice. Circ Res 2010, 107:228-232.
    • (2010) Circ Res , vol.107 , pp. 228-232
    • Lancel, S.1    Qin, F.2    Lennon, S.L.3    Zhang, J.4    Tong, X.5    Mazzini, M.J.6
  • 93
    • 33847074105 scopus 로고    scopus 로고
    • Quantification of oxidative posttranslational modifications of cysteine thiols of p21ras associated with redox modulation of activity using isotope-coded affinity tags and mass spectrometry
    • Sethuraman M., Clavreul N., Huang H., McComb M.E., Costello C.E., Cohen R.A. Quantification of oxidative posttranslational modifications of cysteine thiols of p21ras associated with redox modulation of activity using isotope-coded affinity tags and mass spectrometry. Free Radic Biol Med 2007, 42:823-829.
    • (2007) Free Radic Biol Med , vol.42 , pp. 823-829
    • Sethuraman, M.1    Clavreul, N.2    Huang, H.3    McComb, M.E.4    Costello, C.E.5    Cohen, R.A.6
  • 95
    • 77953809222 scopus 로고    scopus 로고
    • Gas6-Axl pathway: the role of redox-dependent association of Axl with nonmuscle myosin IIB
    • Cavet M.E., Smolock E.M., Menon P., Konishi A., Korshunov V.A., Berk B.C. Gas6-Axl pathway: the role of redox-dependent association of Axl with nonmuscle myosin IIB. Hypertension 2010, 56:105-111.
    • (2010) Hypertension , vol.56 , pp. 105-111
    • Cavet, M.E.1    Smolock, E.M.2    Menon, P.3    Konishi, A.4    Korshunov, V.A.5    Berk, B.C.6
  • 96
    • 67649407767 scopus 로고    scopus 로고
    • Modifications of superoxide dismutase (SOD1) in human erythrocytes: a possible role in amyotrophic lateral sclerosis
    • Wilcox K.C., Zhou L., Jordon J.K., Huang Y., Yu Y., Redler R.L., et al. Modifications of superoxide dismutase (SOD1) in human erythrocytes: a possible role in amyotrophic lateral sclerosis. J Biol Chem 2009, 284:13940-13947.
    • (2009) J Biol Chem , vol.284 , pp. 13940-13947
    • Wilcox, K.C.1    Zhou, L.2    Jordon, J.K.3    Huang, Y.4    Yu, Y.5    Redler, R.L.6
  • 98
    • 40549121595 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation
    • Reinhardt C., von Bruhl M.L., Manukyan D., Grahl L., Lorenz M., Altmann B., et al. Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation. J Clin Invest 2008, 118:1110-1122.
    • (2008) J Clin Invest , vol.118 , pp. 1110-1122
    • Reinhardt, C.1    von Bruhl, M.L.2    Manukyan, D.3    Grahl, L.4    Lorenz, M.5    Altmann, B.6
  • 99
    • 40949103595 scopus 로고    scopus 로고
    • S-glutathionylation of IRF3 regulates IRF3-CBP interaction and activation of the IFN beta pathway
    • Prinarakis E., Chantzoura E., Thanos D., Spyrou G. S-glutathionylation of IRF3 regulates IRF3-CBP interaction and activation of the IFN beta pathway. EMBO J 2008, 27:865-875.
    • (2008) EMBO J , vol.27 , pp. 865-875
    • Prinarakis, E.1    Chantzoura, E.2    Thanos, D.3    Spyrou, G.4
  • 101
    • 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., 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 2007, 100:213-219.
    • (2007) Circ Res , vol.100 , pp. 213-219
    • Pan, S.1    Berk, B.C.2
  • 102
    • 57349120623 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase regulates endothelin-1 expression by a novel, redox-sensitive mechanism involving mRNA stability
    • Rodriguez-Pascual F., Redondo-Horcajo M., Magan-Marchal N., Lagares D., Martinez-Ruiz A., Kleinert H., et al. Glyceraldehyde-3-phosphate dehydrogenase regulates endothelin-1 expression by a novel, redox-sensitive mechanism involving mRNA stability. Mol Cell Biol 2008, 28:7139-7155.
    • (2008) Mol Cell Biol , vol.28 , pp. 7139-7155
    • Rodriguez-Pascual, F.1    Redondo-Horcajo, M.2    Magan-Marchal, N.3    Lagares, D.4    Martinez-Ruiz, A.5    Kleinert, H.6
  • 103
    • 0001547757 scopus 로고
    • Origin and turnover of mitochondrial glutathione
    • Griffith O.W., Meister A. Origin and turnover of mitochondrial glutathione. Proc Natl Acad Sci USA 1985, 82:4668-4672.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4668-4672
    • Griffith, O.W.1    Meister, A.2
  • 104
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant DEFENSE
    • Beer S.M., Taylor E.R., Brown S.E., Dahm C.C., Costa N.J., Runswick M.J., et al. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant DEFENSE. J Biol Chem 2004, 279:47939-47951.
    • (2004) J Biol Chem , vol.279 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6
  • 105
    • 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 USA Mar 19, 2002, 99:3505-3510.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3505-3510
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4    Eberini, I.5    Salmona, M.6
  • 106
    • 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., Shattock M.J. Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. J Biol Chem 2002, 277:9806-9811.
    • (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
  • 107
    • 0034953329 scopus 로고    scopus 로고
    • Bcl-2-dependent oxidation of pyruvate dehydrogenase-E2, a primary biliary cirrhosis autoantigen, during apoptosis
    • Odin J.A., Huebert R.C., Casciola-Rosen L., LaRusso N.F., Rosen A. Bcl-2-dependent oxidation of pyruvate dehydrogenase-E2, a primary biliary cirrhosis autoantigen, during apoptosis. J Clin Invest 2001, 108:223-232.
    • (2001) J Clin Invest , vol.108 , pp. 223-232
    • Odin, J.A.1    Huebert, R.C.2    Casciola-Rosen, L.3    LaRusso, N.F.4    Rosen, A.5
  • 108
    • 15444367716 scopus 로고    scopus 로고
    • Regulation of mitochondrial NADP+-dependent isocitrate dehydrogenase activity by glutathionylation
    • Kil I.S., Park J.W. Regulation of mitochondrial NADP+-dependent isocitrate dehydrogenase activity by glutathionylation. J Biol Chem 2005, 280:10846-10854.
    • (2005) J Biol Chem , vol.280 , pp. 10846-10854
    • Kil, I.S.1    Park, J.W.2
  • 109
    • 77952776083 scopus 로고    scopus 로고
    • Glutathionylation of adenine nucleotide translocase induced by carbon monoxide prevents mitochondrial membrane permeabilization and apoptosis
    • Queiroga C.S., Almeida A.S., Martel C., Brenner C., Alves P.M., Vieira H.L. Glutathionylation of adenine nucleotide translocase induced by carbon monoxide prevents mitochondrial membrane permeabilization and apoptosis. J Biol Chem 2010, 285:17077-17088.
    • (2010) J Biol Chem , vol.285 , pp. 17077-17088
    • Queiroga, C.S.1    Almeida, A.S.2    Martel, C.3    Brenner, C.4    Alves, P.M.5    Vieira, H.L.6
  • 110
    • 36349016509 scopus 로고    scopus 로고
    • Mitochondrial complex II in the post-ischemic heart: oxidative injury and the role of protein S-glutathionylation
    • Chen Y.R., Chen C.L., Pfeiffer D.R., Zweier J.L. Mitochondrial complex II in the post-ischemic heart: oxidative injury and the role of protein S-glutathionylation. J Biol Chem 2007, 282:32640-32654.
    • (2007) J Biol Chem , vol.282 , pp. 32640-32654
    • Chen, Y.R.1    Chen, C.L.2    Pfeiffer, D.R.3    Zweier, J.L.4
  • 111
    • 77952776083 scopus 로고    scopus 로고
    • Glutathionylation of adenine nucleotide translocase induced by carbon monoxide prevents mitochondrial membrane permeabilization and apoptosis
    • Queiroga C.S., Almeida A.S., Martel C., Brenner C., Alves P.M., Vieira H.L. Glutathionylation of adenine nucleotide translocase induced by carbon monoxide prevents mitochondrial membrane permeabilization and apoptosis. J Biol Chem 2010, 285:17077-17088.
    • (2010) J Biol Chem , vol.285 , pp. 17077-17088
    • Queiroga, C.S.1    Almeida, A.S.2    Martel, C.3    Brenner, C.4    Alves, P.M.5    Vieira, H.L.6
  • 112
    • 77951878150 scopus 로고    scopus 로고
    • Cardioprotective and antiapoptotic effects of heme oxygenase-1 in the failing heart
    • Wang G., Hamid T., Keith R.J., Zhou G., Partridge C.R., Xiang X., et al. Cardioprotective and antiapoptotic effects of heme oxygenase-1 in the failing heart. Circulation 2010, 121:1912-1925.
    • (2010) Circulation , vol.121 , pp. 1912-1925
    • Wang, G.1    Hamid, T.2    Keith, R.J.3    Zhou, G.4    Partridge, C.R.5    Xiang, X.6
  • 113
    • 57149142916 scopus 로고    scopus 로고
    • Cardiac myocyte-specific expression of inducible nitric oxide synthase protects against ischemia/reperfusion injury by preventing mitochondrial permeability transition
    • West M.B., Rokosh G., Obal D., Velayutham M., Xuan Y.T., Hill B.G., et al. Cardiac myocyte-specific expression of inducible nitric oxide synthase protects against ischemia/reperfusion injury by preventing mitochondrial permeability transition. Circulation 2008, 118:1970-1978.
    • (2008) Circulation , vol.118 , pp. 1970-1978
    • West, M.B.1    Rokosh, G.2    Obal, D.3    Velayutham, M.4    Xuan, Y.T.5    Hill, B.G.6
  • 114
    • 33846543956 scopus 로고    scopus 로고
    • High concentration of antioxidants N-acetylcysteine and mitoquinone-Q induces intercellular adhesion molecule 1 and oxidative stress by increasing intracellular glutathione
    • Mukherjee T.K., Mishra A.K., Mukhopadhyay S., Hoidal J.R. High concentration of antioxidants N-acetylcysteine and mitoquinone-Q induces intercellular adhesion molecule 1 and oxidative stress by increasing intracellular glutathione. J Immunol 2007, 178:1835-1844.
    • (2007) J Immunol , vol.178 , pp. 1835-1844
    • Mukherjee, T.K.1    Mishra, A.K.2    Mukhopadhyay, S.3    Hoidal, J.R.4
  • 116
    • 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., Vazquez J., Marina A., Garcia de Lacoba M., Perez-Sala D. Glutathionylation of the p50 subunit of NF-kappaB: a mechanism for redox-induced inhibition of DNA binding. Biochemistry 2001, 40:14134-14142.
    • (2001) Biochemistry , vol.40 , pp. 14134-14142
    • Pineda-Molina, E.1    Klatt, P.2    Vazquez, J.3    Marina, A.4    Garcia de Lacoba, M.5    Perez-Sala, D.6
  • 117
    • 34347329257 scopus 로고    scopus 로고
    • Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress
    • Velu C.S., Niture S.K., Doneanu C.E., Pattabiraman N., Srivenugopal K.S. Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress. Biochemistry 2007, 46:7765-7780.
    • (2007) Biochemistry , vol.46 , pp. 7765-7780
    • Velu, C.S.1    Niture, S.K.2    Doneanu, C.E.3    Pattabiraman, N.4    Srivenugopal, K.S.5
  • 118
    • 33745006817 scopus 로고    scopus 로고
    • Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B
    • Rinna A., Torres M., Forman H.J. Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B. Free Radic Biol Med 2006, 41:86-91.
    • (2006) Free Radic Biol Med , vol.41 , pp. 86-91
    • Rinna, A.1    Torres, M.2    Forman, H.J.3
  • 119
    • 23944468310 scopus 로고    scopus 로고
    • Redox regulation of PTEN by S-nitrosothiols
    • Yu C.X., Li S., Whorton A.R. Redox regulation of PTEN by S-nitrosothiols. Mol Pharmacol 2005, 68:847-854.
    • (2005) Mol Pharmacol , vol.68 , pp. 847-854
    • Yu, C.X.1    Li, S.2    Whorton, A.R.3
  • 120
    • 34547128886 scopus 로고    scopus 로고
    • Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFkappaB
    • Qanungo S., Starke D.W., Pai H.V., Mieyal J.J., Nieminen A.L. Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFkappaB. J Biol Chem 2007, 282:18427-18436.
    • (2007) J Biol Chem , vol.282 , pp. 18427-18436
    • Qanungo, S.1    Starke, D.W.2    Pai, H.V.3    Mieyal, J.J.4    Nieminen, A.L.5
  • 121
    • 62349084020 scopus 로고    scopus 로고
    • Glutathionylation of the pro-apoptotic protein p53 in Alzheimer's disease brain: implications for AD pathogenesis
    • Di Domenico F., Cenini G., Sultana R., Perluigi M., Uberti D., Memo M., et al. Glutathionylation of the pro-apoptotic protein p53 in Alzheimer's disease brain: implications for AD pathogenesis. Neurochem Res 2009, 34:727-733.
    • (2009) Neurochem Res , vol.34 , pp. 727-733
    • Di Domenico, F.1    Cenini, G.2    Sultana, R.3    Perluigi, M.4    Uberti, D.5    Memo, M.6
  • 122
    • 60849086193 scopus 로고    scopus 로고
    • Redox amplification of apoptosis by caspase-dependent cleavage of glutaredoxin 1 and S-glutathionylation of Fas
    • Anathy V., Aesif S.W., Guala A.S., Havermans M., Reynaert N.L., Ho Y.S., et al. Redox amplification of apoptosis by caspase-dependent cleavage of glutaredoxin 1 and S-glutathionylation of Fas. J Cell Biol 2009, 184:241-252.
    • (2009) J Cell Biol , vol.184 , pp. 241-252
    • Anathy, V.1    Aesif, S.W.2    Guala, A.S.3    Havermans, M.4    Reynaert, N.L.5    Ho, Y.S.6
  • 124
    • 59049103695 scopus 로고    scopus 로고
    • Posttranslational glutathiolation of aldose reductase (AKR1B1): a possible mechanism of protein recovery from S-nitrosylation
    • Baba S.P., Wetzelberger K., Hoetker J.D., Bhatnagar A. Posttranslational glutathiolation of aldose reductase (AKR1B1): a possible mechanism of protein recovery from S-nitrosylation. Chem Biol Interact 2009, 178:250-258.
    • (2009) Chem Biol Interact , vol.178 , pp. 250-258
    • Baba, S.P.1    Wetzelberger, K.2    Hoetker, J.D.3    Bhatnagar, A.4
  • 125
  • 126
    • 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., Schoneich C., et al. S-glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide. Nat Med 2004, 10:1200-1207.
    • (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    Schoneich, C.6
  • 127
    • 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., Cohen R.A. S-glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells. FASEB J 2006, 20:518-520.
    • (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
  • 128
    • 33750217204 scopus 로고    scopus 로고
    • S-glutathiolation of p21ras by peroxynitrite mediates endothelial insulin resistance caused by oxidized low-density lipoprotein
    • Clavreul N., Bachschmid M.M., Hou X., Shi C., Idrizovic A., Ido Y., et al. S-glutathiolation of p21ras by peroxynitrite mediates endothelial insulin resistance caused by oxidized low-density lipoprotein. Arterioscler Thromb Vasc Biol 2006, 26:2454-2461.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 2454-2461
    • Clavreul, N.1    Bachschmid, M.M.2    Hou, X.3    Shi, C.4    Idrizovic, A.5    Ido, Y.6
  • 129
    • 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 2004, 279:29857-29862.
    • (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
  • 130
    • 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 2006, 41:613-622.
    • (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
  • 131
    • 78650703662 scopus 로고    scopus 로고
    • Beta(3) adrenergic stimulation of the cardiac Na+-K+pump by reversal of an inhibitory oxidative modification
    • Bundgaard H., Liu C.C., Garcia A., Hamilton E.J., Huang Y., Chia K.K., et al. Beta(3) adrenergic stimulation of the cardiac Na+-K+pump by reversal of an inhibitory oxidative modification. Circulation 2010, 122:2699-2708.
    • (2010) Circulation , vol.122 , pp. 2699-2708
    • Bundgaard, H.1    Liu, C.C.2    Garcia, A.3    Hamilton, E.J.4    Huang, Y.5    Chia, K.K.6
  • 132
    • 77951544514 scopus 로고    scopus 로고
    • Activation of cAMP-dependent signaling induces oxidative modification of the cardiac Na+-K+pump and inhibits its activity
    • White C.N., Liu C.C., Garcia A., Hamilton E.J., Chia K.K., Figtree G.A., et al. Activation of cAMP-dependent signaling induces oxidative modification of the cardiac Na+-K+pump and inhibits its activity. J Biol Chem 2010, 285:13712-13720.
    • (2010) J Biol Chem , vol.285 , pp. 13712-13720
    • White, C.N.1    Liu, C.C.2    Garcia, A.3    Hamilton, E.J.4    Chia, K.K.5    Figtree, G.A.6
  • 133
    • 68049096878 scopus 로고    scopus 로고
    • Reversible oxidative modification: a key mechanism of Na+-K+pump regulation
    • Figtree G.A., Liu C.C., Bibert S., Hamilton E.J., Garcia A., White C.N., et al. Reversible oxidative modification: a key mechanism of Na+-K+pump regulation. Circ Res 2009, 105:185-193.
    • (2009) Circ Res , vol.105 , pp. 185-193
    • Figtree, G.A.1    Liu, C.C.2    Bibert, S.3    Hamilton, E.J.4    Garcia, A.5    White, C.N.6
  • 134
    • 79956297624 scopus 로고    scopus 로고
    • FXYD proteins reverse inhibition of the Na+-K+pump mediated by glutathionylation of its β1 subunit
    • Bibert S., Liu C.C., Figtree G.A., Garcia A., Hamilton E.J., Marassi F.M., et al. FXYD proteins reverse inhibition of the Na+-K+pump mediated by glutathionylation of its β1 subunit. J Biol Chem 2011, 286:18562-18572.
    • (2011) J Biol Chem , vol.286 , pp. 18562-18572
    • Bibert, S.1    Liu, C.C.2    Figtree, G.A.3    Garcia, A.4    Hamilton, E.J.5    Marassi, F.M.6
  • 135
    • 1842832392 scopus 로고    scopus 로고
    • Glyceraldehyde phosphate dehydrogenase oxidation during cardiac ischemia and reperfusion
    • Eaton P., Wright N., Hearse D.J., Shattock M.J. Glyceraldehyde phosphate dehydrogenase oxidation during cardiac ischemia and reperfusion. J Mol Cell Cardiol 2002, 34:1549-1560.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 1549-1560
    • Eaton, P.1    Wright, N.2    Hearse, D.J.3    Shattock, M.J.4
  • 136
    • 57349120623 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase regulates endothelin-1 expression by a novel, redox-sensitive mechanism involving mRNA stability
    • Rodriguez-Pascual F., Redondo-Horcajo M., Magan-Marchal N., Lagares D., Martinez-Ruiz A., Kleinert H., et al. Glyceraldehyde-3-phosphate dehydrogenase regulates endothelin-1 expression by a novel, redox-sensitive mechanism involving mRNA stability. Mol Cell Biol 2008, 28:7139-7155.
    • (2008) Mol Cell Biol , vol.28 , pp. 7139-7155
    • Rodriguez-Pascual, F.1    Redondo-Horcajo, M.2    Magan-Marchal, N.3    Lagares, D.4    Martinez-Ruiz, A.5    Kleinert, H.6
  • 137
    • 77449119371 scopus 로고    scopus 로고
    • Peptide-based antibodies against glutathione-binding domains suppress superoxide production mediated by mitochondrial complex I
    • Chen J., Chen C.L., Rawale S., Chen C.A., Zweier J.L., Kaumaya P.T., et al. Peptide-based antibodies against glutathione-binding domains suppress superoxide production mediated by mitochondrial complex I. J Biol Chem 2010, 285:3168-3180.
    • (2010) J Biol Chem , vol.285 , pp. 3168-3180
    • Chen, J.1    Chen, C.L.2    Rawale, S.3    Chen, C.A.4    Zweier, J.L.5    Kaumaya, P.T.6
  • 138
    • 34248569415 scopus 로고    scopus 로고
    • Site-specific S-glutathiolation of mitochondrial NADH ubiquinone reductase
    • Chen C.L., Zhang L., Yeh A., Chen C.A., Green-Church K.B., Zweier J.L., et al. Site-specific S-glutathiolation of mitochondrial NADH ubiquinone reductase. Biochemistry 2007, 46:5754-5765.
    • (2007) Biochemistry , vol.46 , pp. 5754-5765
    • Chen, C.L.1    Zhang, L.2    Yeh, A.3    Chen, C.A.4    Green-Church, K.B.5    Zweier, J.L.6
  • 139
    • 36349016509 scopus 로고    scopus 로고
    • Mitochondrial complex II in the post-ischemic heart: oxidative injury and the role of protein S-glutathionylation
    • Chen Y.R., Chen C.L., Pfeiffer D.R., Zweier J.L. Mitochondrial complex II in the post-ischemic heart: oxidative injury and the role of protein S-glutathionylation. J Biol Chem 2007, 282:32640-32654.
    • (2007) J Biol Chem , vol.282 , pp. 32640-32654
    • Chen, Y.R.1    Chen, C.L.2    Pfeiffer, D.R.3    Zweier, J.L.4
  • 140
    • 55549123029 scopus 로고    scopus 로고
    • Protein tyrosine nitration of the flavin subunit is associated with oxidative modification of mitochondrial complex II in the post-ischemic myocardium
    • Chen C.L., Chen J., Rawale S., Varadharaj S., Kaumaya P.P., Zweier J.L., et al. Protein tyrosine nitration of the flavin subunit is associated with oxidative modification of mitochondrial complex II in the post-ischemic myocardium. J Biol Chem 2008, 283:27991-28003.
    • (2008) J Biol Chem , vol.283 , pp. 27991-28003
    • Chen, C.L.1    Chen, J.2    Rawale, S.3    Varadharaj, S.4    Kaumaya, P.P.5    Zweier, J.L.6
  • 141
    • 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., 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 2007, 100:213-219.
    • (2007) Circ Res , vol.100 , pp. 213-219
    • Pan, S.1    Berk, B.C.2
  • 142
    • 78649668520 scopus 로고    scopus 로고
    • Oxidative stress inhibits vascular K(ATP) channels by S-glutathionylation
    • Yang Y., Shi W., Cui N., Wu Z., Jiang C. Oxidative stress inhibits vascular K(ATP) channels by S-glutathionylation. J Biol Chem 2010, 285:38641-38648.
    • (2010) J Biol Chem , vol.285 , pp. 38641-38648
    • Yang, Y.1    Shi, W.2    Cui, N.3    Wu, Z.4    Jiang, C.5
  • 143
    • 79953229546 scopus 로고    scopus 로고
    • Molecular basis and structural insight of vascular K(ATP) channel gating by S-glutathionylation
    • Yang Y., Shi W., Chen X., Cui N., Konduru A.S., Shi Y., et al. Molecular basis and structural insight of vascular K(ATP) channel gating by S-glutathionylation. J Biol Chem 2011, 286:9298-9307.
    • (2011) J Biol Chem , vol.286 , pp. 9298-9307
    • Yang, Y.1    Shi, W.2    Chen, X.3    Cui, N.4    Konduru, A.S.5    Shi, Y.6
  • 144
    • 27644445283 scopus 로고    scopus 로고
    • Tachycardia increases NADPH oxidase activity and RyR2 S-glutathionylation in ventricular muscle
    • Sanchez G., Pedrozo Z., Domenech R.J., Hidalgo C., Donoso P. Tachycardia increases NADPH oxidase activity and RyR2 S-glutathionylation in ventricular muscle. J Mol Cell Cardiol 2005, 39:982-991.
    • (2005) J Mol Cell Cardiol , vol.39 , pp. 982-991
    • Sanchez, G.1    Pedrozo, Z.2    Domenech, R.J.3    Hidalgo, C.4    Donoso, P.5
  • 145
    • 0242290360 scopus 로고    scopus 로고
    • S-glutathionylation decreases Mg2+ inhibition and S-nitrosylation enhances Ca2+ activation of RyR1 channels
    • Aracena P., Sanchez G., Donoso P., Hamilton S.L., Hidalgo C. S-glutathionylation decreases Mg2+ inhibition and S-nitrosylation enhances Ca2+ activation of RyR1 channels. J Biol Chem 2003, 278:42927-42935.
    • (2003) J Biol Chem , vol.278 , pp. 42927-42935
    • Aracena, P.1    Sanchez, G.2    Donoso, P.3    Hamilton, S.L.4    Hidalgo, C.5
  • 146
    • 33748755208 scopus 로고    scopus 로고
    • A transverse tubule NADPH oxidase activity stimulates calcium release from isolated triads via ryanodine receptor type 1 S-glutathionylation
    • Hidalgo C., Sanchez G., Barrientos G., Aracena-Parks P. A transverse tubule NADPH oxidase activity stimulates calcium release from isolated triads via ryanodine receptor type 1 S-glutathionylation. J Biol Chem 2006, 281:26473-26482.
    • (2006) J Biol Chem , vol.281 , pp. 26473-26482
    • Hidalgo, C.1    Sanchez, G.2    Barrientos, G.3    Aracena-Parks, P.4
  • 147
    • 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., 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 2005, 7:870-881.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 870-881
    • Aracena, P.1    Tang, W.2    Hamilton, S.L.3    Hidalgo, C.4
  • 148
    • 33846003833 scopus 로고    scopus 로고
    • Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1
    • Aracena-Parks P., Goonasekera S.A., Gilman C.P., Dirksen R.T., Hidalgo C., Hamilton S.L. Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1. J Biol Chem 2006, 281:40354-40368.
    • (2006) J Biol Chem , vol.281 , pp. 40354-40368
    • Aracena-Parks, P.1    Goonasekera, S.A.2    Gilman, C.P.3    Dirksen, R.T.4    Hidalgo, C.5    Hamilton, S.L.6
  • 149
    • 38849083944 scopus 로고    scopus 로고
    • Exercise and tachycardia increase NADPH oxidase and ryanodine receptor-2 activity: possible role in cardioprotection
    • Sanchez G., Escobar M., Pedrozo Z., Macho P., Domenech R., Hartel S., et al. Exercise and tachycardia increase NADPH oxidase and ryanodine receptor-2 activity: possible role in cardioprotection. Cardiovasc Res 2008, 77:380-386.
    • (2008) Cardiovasc Res , vol.77 , pp. 380-386
    • Sanchez, G.1    Escobar, M.2    Pedrozo, Z.3    Macho, P.4    Domenech, R.5    Hartel, S.6
  • 150
    • 47849120473 scopus 로고    scopus 로고
    • Superoxide dismutase 1 regulates caspase-1 and endotoxic shock
    • Meissner F., Molawi K., Zychlinsky A. Superoxide dismutase 1 regulates caspase-1 and endotoxic shock. Nat Immunol 2008, 9:866-872.
    • (2008) Nat Immunol , vol.9 , pp. 866-872
    • Meissner, F.1    Molawi, K.2    Zychlinsky, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.