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Volumn , Issue , 2008, Pages 121-156

Glutaredoxin and Thioredoxin Enzyme Systems: Catalytic Mechanisms and Physiological Functions

Author keywords

Glutaredoxin and thioredoxin enzyme systems; Glutaredoxin mechanism of action; GRX expression control

Indexed keywords


EID: 77949780387     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470475973.ch7     Document Type: Chapter
Times cited : (4)

References (160)
  • 2
    • 0021891877 scopus 로고
    • Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation
    • Ziegler, D.M. (1985). Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation. Annual Review of Biochemistry, 54, 305-329.
    • (1985) Annual Review of Biochemistry , vol.54 , pp. 305-329
    • Ziegler, D.M.1
  • 3
    • 0000326249 scopus 로고
    • Glutathionyl specificity of the thioltransferases: Mechanistic and physiological implications
    • In Packer, L., and Cadenas, E., Eds., New York: Marcel Dekker
    • Mieyal, J.J., Srinivasan, U., Starke, D.W., Gravina, S.A, Mieyal, P.A. (1995). Glutathionyl specificity of the thioltransferases: Mechanistic and physiological implications. In Packer, L., and Cadenas, E., Eds., Biothiols in Health and Disease, pp. 305-372. New York: Marcel Dekker.
    • (1995) Biothiols in Health and Disease , pp. 305-372
    • Mieyal, J.J.1    Srinivasan, U.2    Starke, D.W.3    Gravina, S.A.4    Mieyal, P.A.5
  • 4
    • 33750604604 scopus 로고    scopus 로고
    • Aspects of the biological redox chemistry of cysteine: From simple redox responses to sophisticated signaling pathways
    • Jacob, C., Knight, I., Winyard, P.G. (2006). Aspects of the biological redox chemistry of cysteine: From simple redox responses to sophisticated signaling pathways. Biological Chemistry, 387, 1385-1397.
    • (2006) Biological Chemistry , vol.387 , pp. 1385-1397
    • Jacob, C.1    Knight, I.2    Winyard, P.G.3
  • 5
    • 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., Mieyal, J.J. (2005). Glutaredoxin: Role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxidants and Redox Signaling, 7, 348-366.
    • (2005) Antioxidants and Redox Signaling , vol.7 , pp. 348-366
    • Shelton, M.D.1    Chock, P.B.2    Mieyal, J.J.3
  • 6
    • 0032497928 scopus 로고    scopus 로고
    • Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity
    • Yang, Y., Jao, S., Nanduri, S., Starke, D.W., Mieyal, J.J., Qin, J. (1998). Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity. Biochemistry, 37, 17145-17156.
    • (1998) Biochemistry , vol.37 , pp. 17145-17156
    • Yang, Y.1    Jao, S.2    Nanduri, S.3    Starke, D.W.4    Mieyal, J.J.5    Qin, J.6
  • 10
    • 33845428642 scopus 로고    scopus 로고
    • Thioredoxin and related molecules: From biology to health and disease
    • Lillig, C.H., Holmgren, A. (2007). Thioredoxin and related molecules: From biology to health and disease. Antioxidants and Redox Signaling, 9, 25-47.
    • (2007) Antioxidants and Redox Signaling , vol.9 , pp. 25-47
    • Lillig, C.H.1    Holmgren, A.2
  • 11
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • Klatt, P., Lamas, S. (2000). Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. European Journal of Biochemistry, 267, 4928-4944.
    • (2000) European Journal of Biochemistry , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 12
    • 33847746679 scopus 로고    scopus 로고
    • Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: Implications for diseases in the cardiovascular system
    • Berndt, C., Lillig, C.H., Holmgren, A. (2007). Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: Implications for diseases in the cardiovascular system. American Journal of Physiology. Heart and Circulatory Physiology, 292, H1227-H1236.
    • (2007) American Journal of Physiology. Heart and Circulatory Physiology , vol.292
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 13
    • 0025887464 scopus 로고
    • Thioltransferase in human red blood cells: Kinetics and equilibrium
    • Mieyal, J.J., Starke, D.W., Gravina, S.A., Hocevar, B.A. (1991). Thioltransferase in human red blood cells: Kinetics and equilibrium. Biochemistry, 30, 8883-8891.
    • (1991) Biochemistry , vol.30 , pp. 8883-8891
    • Mieyal, J.J.1    Starke, D.W.2    Gravina, S.A.3    Hocevar, B.A.4
  • 15
    • 35448993279 scopus 로고    scopus 로고
    • What is the functional significance of the unique localization of glutaredoxin 1 (Grx1) in the intermembrane space of mitochondria?
    • Pai, H.V., Starke, D.W., Lesnefsky, E.J., Hoppel, C.L., Mieyal, J.J. (2007). What is the functional significance of the unique localization of glutaredoxin 1 (Grx1) in the intermembrane space of mitochondria? Antioxidants and Redox Signaling, 9(11), 2027-2033.
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.11 , pp. 2027-2033
    • Pai, H.V.1    Starke, D.W.2    Lesnefsky, E.J.3    Hoppel, C.L.4    Mieyal, J.J.5
  • 16
    • 34548163922 scopus 로고    scopus 로고
    • Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress
    • Gallogly, M.M., Mieyal, J.J. (2007). Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. Current Opinion in Pharmacology, 7(4), 381-391.
    • (2007) Current Opinion in Pharmacology , vol.7 , Issue.4 , pp. 381-391
    • Gallogly, M.M.1    Mieyal, J.J.2
  • 18
    • 0042834001 scopus 로고    scopus 로고
    • Immunohistochemical determination of thioredoxin and glutaredoxin distribution in the human cervix, and possible relation to cervical ripening
    • Lysell, J., Stjernholm, V.Y., Ciarlo, N., Holmgren, A., Sahlin, L. (2003). Immunohistochemical determination of thioredoxin and glutaredoxin distribution in the human cervix, and possible relation to cervical ripening. Gynecological Endocrinology, 17, 303-310.
    • (2003) Gynecological Endocrinology , vol.17 , pp. 303-310
    • Lysell, J.1    Stjernholm, V.Y.2    Ciarlo, N.3    Holmgren, A.4    Sahlin, L.5
  • 19
    • 0033669376 scopus 로고    scopus 로고
    • The expression of glutaredoxin is increased in the human cervix in term pregnancy and immediately post-partum, particularly after prostaglandin-induced delivery
    • Sahlin, L.,Wang, H., Stjernholm, Y., Lundberg, M., Ekman, G., Holmgren, A., Eriksson, H. (2000). The expression of glutaredoxin is increased in the human cervix in term pregnancy and immediately post-partum, particularly after prostaglandin-induced delivery. Molecular Human Reproduction, 6, 1147-1153.
    • (2000) Molecular Human Reproduction , vol.6 , pp. 1147-1153
    • Sahlin, L.1    Wang, H.2    Stjernholm, Y.3    Lundberg, M.4    Ekman, G.5    Holmgren, A.6    Eriksson, H.7
  • 20
    • 0035991086 scopus 로고    scopus 로고
    • Immunohistochemical localization of glutaredoxin and thioredoxin in human endometrium: A possible association with pinopodes
    • Stavreus-Evers, A., Masironi, B., Landgren, B.M., Holmgren, A., Eriksson, H., Sahlin, L. (2002). Immunohistochemical localization of glutaredoxin and thioredoxin in human endometrium: A possible association with pinopodes. Molecular Human Reproduction, 8, 546-551.
    • (2002) Molecular Human Reproduction , vol.8 , pp. 546-551
    • Stavreus-Evers, A.1    Masironi, B.2    Landgren, B.M.3    Holmgren, A.4    Eriksson, H.5    Sahlin, L.6
  • 25
    • 34047250626 scopus 로고    scopus 로고
    • Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria
    • Johansson, C., Kavanagh, K.L., Gileadi, O., Oppermann, U. (2007). Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria. Journal of Biological Chemistry, 282, 3077-3082.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 3077-3082
    • Johansson, C.1    Kavanagh, K.L.2    Gileadi, O.3    Oppermann, U.4
  • 26
    • 0040932016 scopus 로고    scopus 로고
    • Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae
    • Rodriguez-Manzaneque, M.T., Ros, J., Cabiscol, E., Sorribas, A., Herrero, E. (1999). Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Molecular and Cellular Biology, 19, 8180-8190.
    • (1999) Molecular and Cellular Biology , vol.19 , pp. 8180-8190
    • Rodriguez-Manzaneque, M.T.1    Ros, J.2    Cabiscol, E.3    Sorribas, A.4    Herrero, E.5
  • 28
    • 0027238801 scopus 로고
    • Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase
    • Gravina, S.A., Mieyal, J.J. (1993). Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry, 32, 3368-3376.
    • (1993) Biochemistry , vol.32 , pp. 3368-3376
    • Gravina, S.A.1    Mieyal, J.J.2
  • 29
    • 0020804830 scopus 로고
    • Relative contributions of thioltransferase-and thioredoxin-dependent systems in reduction of lowmolecular-mass and protein disulphides
    • Mannervik, B., Axelsson, K., Sundewall, A.C., Holmgren, A. (1983). Relative contributions of thioltransferase-and thioredoxin-dependent systems in reduction of lowmolecular-mass and protein disulphides. Biochemical Journal, 213, 519-523.
    • (1983) Biochemical Journal , vol.213 , pp. 519-523
    • Mannervik, B.1    Axelsson, K.2    Sundewall, A.C.3    Holmgren, A.4
  • 31
    • 0033796101 scopus 로고    scopus 로고
    • The role of the redox protein thioredoxin in cell growth and cancer
    • Powis, G., Mustacich, D., Coon, A. (2000). The role of the redox protein thioredoxin in cell growth and cancer. Free Radical Biology and Medicine, 29, 312-322.
    • (2000) Free Radical Biology and Medicine , vol.29 , pp. 312-322
    • Powis, G.1    Mustacich, D.2    Coon, A.3
  • 32
    • 78651146370 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B
    • Laurent, T.C., Moore, E.C., Reichard, P. (1964). Enzymatic synthesis of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B. Journal of Biological Chemistry, 239, 3436-3444.
    • (1964) Journal of Biological Chemistry , vol.239 , pp. 3436-3444
    • Laurent, T.C.1    Moore, E.C.2    Reichard, P.3
  • 36
    • 34548844721 scopus 로고    scopus 로고
    • Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia
    • Ho, Y.S., Xiong, Y., Ho, D.S., Gao, J., Chua, B.H., Pai, H., Mieyal, J.J. (2007). Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia. Free Radical Biology and Medicine, 43(9), 1299-1312.
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.9 , pp. 1299-1312
    • Ho, Y.S.1    Xiong, Y.2    Ho, D.S.3    Gao, J.4    Chua, B.H.5    Pai, H.6    Mieyal, J.J.7
  • 37
    • 0030004888 scopus 로고    scopus 로고
    • Deoxyribonucleoside triphosphate pools and growth of glutathione-depleted 3T6 mouse fibroblasts
    • Spyrou, G., Holmgren, A. (1996). Deoxyribonucleoside triphosphate pools and growth of glutathione-depleted 3T6 mouse fibroblasts. Biochemical and Biophysical Research Communications, 220, 42-46.
    • (1996) Biochemical and Biophysical Research Communications , vol.220 , pp. 42-46
    • Spyrou, G.1    Holmgren, A.2
  • 43
    • 24144433455 scopus 로고    scopus 로고
    • Link between macrophage migration inhibitory factor and cellular redox regulation
    • Thiele, M., Bernhagen, J. (2005). Link between macrophage migration inhibitory factor and cellular redox regulation. Antioxidants and Redox Signaling, 7, 1234-1248.
    • (2005) Antioxidants and Redox Signaling , vol.7 , pp. 1234-1248
    • Thiele, M.1    Bernhagen, J.2
  • 44
    • 0032197184 scopus 로고    scopus 로고
    • A novel nuclear member of the thioredoxin superfamily
    • Laughner, B.J., Sehnke, P.C., Ferl, R.J. (1998). A novel nuclear member of the thioredoxin superfamily. Plant Physiology, 118, 987-996.
    • (1998) Plant Physiology , vol.118 , pp. 987-996
    • Laughner, B.J.1    Sehnke, P.C.2    Ferl, R.J.3
  • 47
    • 0033524429 scopus 로고    scopus 로고
    • The catalytic mechanism of the glutathionedependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin)
    • Washburn, M.P., Wells, W.W. (1999). The catalytic mechanism of the glutathionedependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin). Biochemistry, 38, 268-274.
    • (1999) Biochemistry , vol.38 , pp. 268-274
    • Washburn, M.P.1    Wells, W.W.2
  • 48
    • 1542320094 scopus 로고    scopus 로고
    • Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase
    • Johansson, C., Lillig, C.H., Holmgren, A. (2004). Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. Journal of Biological Chemistry, 279, 7537-7543.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 7537-7543
    • Johansson, C.1    Lillig, C.H.2    Holmgren, A.3
  • 50
    • 33645971642 scopus 로고    scopus 로고
    • Computational and mutational analysis of human glutaredoxin (thioltransferase): Probing the molecular basis of the low pKa of cysteine 22 and its role in catalysis
    • Jao, S.C., English Ospina, S.M., Berdis, A.J., Starke, D.W., Post, C.B., Mieyal, J.J. (2006). Computational and mutational analysis of human glutaredoxin (thioltransferase): Probing the molecular basis of the low pKa of cysteine 22 and its role in catalysis. Biochemistry, 45, 4785-4796.
    • (2006) Biochemistry , vol.45 , pp. 4785-4796
    • Jao, S.C.1    English Ospina, S.M.2    Berdis, A.J.3    Starke, D.W.4    Post, C.B.5    Mieyal, J.J.6
  • 51
    • 0034714319 scopus 로고    scopus 로고
    • Acute cadmium exposure inactivates thioltransferase (glutaredoxin), inhibits intracellular reduction of protein-glutathionylmixed disulfides, and initiates apoptosis
    • Chrestensen, C.A., Starke, D.W., Mieyal, J.J. (2000). Acute cadmium exposure inactivates thioltransferase (glutaredoxin), inhibits intracellular reduction of protein-glutathionylmixed disulfides, and initiates apoptosis. Journal of Biological Chemistry, 275, 26556-26565.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 26556-26565
    • Chrestensen, C.A.1    Starke, D.W.2    Mieyal, J.J.3
  • 52
    • 0031000775 scopus 로고    scopus 로고
    • PH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis
    • Srinivasan, U., Mieyal, P.A., Mieyal, J.J. (1997). pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis. Biochemistry, 36, 3199-3206.
    • (1997) Biochemistry , vol.36 , pp. 3199-3206
    • Srinivasan, U.1    Mieyal, P.A.2    Mieyal, J.J.3
  • 53
    • 0018786716 scopus 로고
    • Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin
    • Holmgren, A. (1979). Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin. Journal of Biological Chemistry, 254, 3672-3678.
    • (1979) Journal of Biological Chemistry , vol.254 , pp. 3672-3678
    • Holmgren, A.1
  • 54
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: Glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system
    • Fernandes, A.P., Holmgren, A. (2004). Glutaredoxins: Glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxidants and Redox Signaling, 6, 63-74.
    • (2004) Antioxidants and Redox Signaling , vol.6 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 56
    • 0028289612 scopus 로고
    • Properties of the arsenate reductase of plasmid R773
    • Gladysheva, T.B., Oden, K.L., Rosen, B.P. (1994). Properties of the arsenate reductase of plasmid R773. Biochemistry, 33, 7288-7293.
    • (1994) Biochemistry , vol.33 , pp. 7288-7293
    • Gladysheva, T.B.1    Oden, K.L.2    Rosen, B.P.3
  • 57
    • 0037010116 scopus 로고    scopus 로고
    • Biochemistry of arsenic detoxification
    • Rosen, B.P. (2002). Biochemistry of arsenic detoxification. FEBS Letters, 529, 86-92.
    • (2002) FEBS Letters , vol.529 , pp. 86-92
    • Rosen, B.P.1
  • 58
    • 0033579499 scopus 로고    scopus 로고
    • Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction
    • Shi, J., Vlamis-Gardikas, A., Aslund, F., Holmgren, A., Rosen, B.P. (1999). Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction. Journal of Biological Chemistry, 274, 36039-36042.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 36039-36042
    • Shi, J.1    Vlamis-Gardikas, A.2    Aslund, F.3    Holmgren, A.4    Rosen, B.P.5
  • 59
    • 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. (2008). Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: implications for intracellular roles. Biochemistry, 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
  • 60
    • 34347204123 scopus 로고    scopus 로고
    • Oxidation and S-nitrosylation of cysteines in human cytosolic and mitochondrial glutaredoxins: Effects on structure and activity
    • Hashemy, S.I., Johansson, C., Berndt, C., Lillig, C.H., Holmgren, A. (2007). Oxidation and S-nitrosylation of cysteines in human cytosolic and mitochondrial glutaredoxins: Effects on structure and activity. Journal of Biological Chemistry, 282, 14428-14436.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 14428-14436
    • Hashemy, S.I.1    Johansson, C.2    Berndt, C.3    Lillig, C.H.4    Holmgren, A.5
  • 61
    • 0019817226 scopus 로고
    • Glutathione reductase from human erythrocytes: Amino-acid sequence of the structurally known FAD-binding domain
    • Untucht-Grau, R., Schirmer, R.H., Schirmer, I., Krauth-Siegel, R.L. (1981). Glutathione reductase from human erythrocytes: Amino-acid sequence of the structurally known FAD-binding domain. European Journal of Biochemistry, 120, 407-419.
    • (1981) European Journal of Biochemistry , vol.120 , pp. 407-419
    • Untucht-Grau, R.1    Schirmer, R.H.2    Schirmer, I.3    Krauth-Siegel, R.L.4
  • 62
    • 0025329396 scopus 로고
    • Glutathione reductase: Comparison of steady-state and rapid reaction primary kinetic isotope effects exhibited by the yeast, spinach, and Escherichia coli enzymes
    • Vanoni, M.A., Wong, K.K., Ballou, D.P., Blanchard, J.S. (1990). Glutathione reductase: Comparison of steady-state and rapid reaction primary kinetic isotope effects exhibited by the yeast, spinach, and Escherichia coli enzymes. Biochemistry, 29, 5790-5796.
    • (1990) Biochemistry , vol.29 , pp. 5790-5796
    • Vanoni, M.A.1    Wong, K.K.2    Ballou, D.P.3    Blanchard, J.S.4
  • 63
    • 0019163962 scopus 로고
    • Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli
    • Kallis, G.B., Holmgren, A. (1980). Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli. Journal of Biological Chemistry, 255, 10261-10265.
    • (1980) Journal of Biological Chemistry , vol.255 , pp. 10261-10265
    • Kallis, G.B.1    Holmgren, A.2
  • 64
    • 0020490790 scopus 로고
    • Glutaredoxin from calf thymus: Purification to homogeneity
    • Luthman, M., Holmgren, A. (1982). Glutaredoxin from calf thymus: Purification to homogeneity. Journal of Biological Chemistry, 257, 6686-6690.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 6686-6690
    • Luthman, M.1    Holmgren, A.2
  • 65
    • 0242413235 scopus 로고    scopus 로고
    • Kinetic characterization of the chemical steps involved in the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis
    • Antoine, M., Boschi-Muller, S., Branlant, G. (2003). Kinetic characterization of the chemical steps involved in the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis. Journal of Biological Chemistry, 278, 45352-45357.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 45352-45357
    • Antoine, M.1    Boschi-Muller, S.2    Branlant, G.3
  • 66
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren, A. (1979). Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. Journal of Biological Chemistry, 254, 9627-9632.
    • (1979) Journal of Biological Chemistry , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 67
    • 0029187633 scopus 로고
    • Selenite and selenodiglutathione: Reactions with thioredoxin systems
    • Bjornstedt, M., Kumar, S., Holmgren, A. (1995). Selenite and selenodiglutathione: Reactions with thioredoxin systems. Methods in Enzymology, 252, 209-219.
    • (1995) Methods in Enzymology , vol.252 , pp. 209-219
    • Bjornstedt, M.1    Kumar, S.2    Holmgren, A.3
  • 70
    • 0028856209 scopus 로고
    • Induction of phase I and phase II drug-metabolizing enzyme mRNA, protein, and activity by BHA, ethoxyquin, and oltipraz
    • Buetler, T.M., Gallagher, E.P., Wang, C., Stahl, D.L., Hayes, J.D., Eaton, D.L. (1995). Induction of phase I and phase II drug-metabolizing enzyme mRNA, protein, and activity by BHA, ethoxyquin, and oltipraz. Toxicology and Applied Pharmacology, 135, 45-57.
    • (1995) Toxicology and Applied Pharmacology , vol.135 , pp. 45-57
    • Buetler, T.M.1    Gallagher, E.P.2    Wang, C.3    Stahl, D.L.4    Hayes, J.D.5    Eaton, D.L.6
  • 71
    • 0026571238 scopus 로고
    • Two adjacent AP-1-like binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene
    • Friling, R.S., Bergelson, S., Daniel, V. (1992). Two adjacent AP-1-like binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene. Proceedings of the National Academy of Sciences USA, 89, 668-672.
    • (1992) Proceedings of the National Academy of Sciences USA , vol.89 , pp. 668-672
    • Friling, R.S.1    Bergelson, S.2    Daniel, V.3
  • 72
    • 0026560203 scopus 로고
    • Antioxidant-influenced alterations in glutathione reductase activity in different age groups of male mice
    • Khanna, S.C., Garg, S.K., Sharma, S.P. (1992). Antioxidant-influenced alterations in glutathione reductase activity in different age groups of male mice. Gerontology, 38, 9-12.
    • (1992) Gerontology , vol.38 , pp. 9-12
    • Khanna, S.C.1    Garg, S.K.2    Sharma, S.P.3
  • 73
    • 0024426965 scopus 로고
    • Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase
    • Di Simplicio, P., Jensson, H., Mannervik, B. (1989). Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase. Biochemical Journal, 263, 679-685.
    • (1989) Biochemical Journal , vol.263 , pp. 679-685
    • Di Simplicio, P.1    Jensson, H.2    Mannervik, B.3
  • 74
    • 0030799313 scopus 로고    scopus 로고
    • The human glutaredoxin gene: Determination of its organization, transcription start point, and promoter analysis
    • Park, J.B., Levine, M. (1997). The human glutaredoxin gene: Determination of its organization, transcription start point, and promoter analysis. Gene, 197, 189-193.
    • (1997) Gene , vol.197 , pp. 189-193
    • Park, J.B.1    Levine, M.2
  • 77
    • 0036813225 scopus 로고    scopus 로고
    • Thioltransferase (glutaredoxin) mediates recovery of motor neurons from excitotoxic mitochondrial injury
    • Kenchappa, R.S., Diwakar, L., Boyd, M.R., Ravindranath, V. (2002). Thioltransferase (glutaredoxin) mediates recovery of motor neurons from excitotoxic mitochondrial injury. Journal of Neurosciences, 22, 8402-8410.
    • (2002) Journal of Neurosciences , vol.22 , pp. 8402-8410
    • Kenchappa, R.S.1    Diwakar, L.2    Boyd, M.R.3    Ravindranath, V.4
  • 79
    • 0030930252 scopus 로고    scopus 로고
    • oxyR-dependent induction of Escherichia coli grx gene expression by peroxide stress
    • Tao, K. (1997). oxyR-dependent induction of Escherichia coli grx gene expression by peroxide stress. Journal of Bacteriology, 179, 5967-5970.
    • (1997) Journal of Bacteriology , vol.179 , pp. 5967-5970
    • Tao, K.1
  • 80
    • 0032824908 scopus 로고    scopus 로고
    • Induction of thioredoxin, thioredoxin reductase and glutaredoxin activity in mouse skin by TPA, a calcium ionophore and other tumor promoters
    • Kumar, S., Holmgren, A. (1999). Induction of thioredoxin, thioredoxin reductase and glutaredoxin activity in mouse skin by TPA, a calcium ionophore and other tumor promoters. Carcinogenesis, 20, 1761-1767.
    • (1999) Carcinogenesis , vol.20 , pp. 1761-1767
    • Kumar, S.1    Holmgren, A.2
  • 81
    • 0032587961 scopus 로고    scopus 로고
    • 17betaestradiol induces protein thiol/disulfide oxidoreductases and protects cultured bovine aortic endothelial cells from oxidative stress
    • Ejima, K., Nanri, H., Araki, M., Uchida, K., Kashimura, M., Ikeda, M. (1999). 17betaestradiol induces protein thiol/disulfide oxidoreductases and protects cultured bovine aortic endothelial cells from oxidative stress. European Journal of Endocrinology, 140, 608-613.
    • (1999) European Journal of Endocrinology , vol.140 , pp. 608-613
    • Ejima, K.1    Nanri, H.2    Araki, M.3    Uchida, K.4    Kashimura, M.5    Ikeda, M.6
  • 82
    • 33744955627 scopus 로고    scopus 로고
    • 17Beta-estradiol protects against oxidative stress-induced cell death through the glutathione/glutaredoxin-dependent redox regulation of Akt in myocardiac H9c2 cells
    • Urata, Y., Ihara, Y., Murata, H., Goto, S., Koji, T., Yodoi, J., Inoue, S., Kondo, T. (2006). 17Beta-estradiol protects against oxidative stress-induced cell death through the glutathione/glutaredoxin-dependent redox regulation of Akt in myocardiac H9c2 cells. Journal of Biological Chemistry, 281, 13092-13102.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 13092-13102
    • Urata, Y.1    Ihara, Y.2    Murata, H.3    Goto, S.4    Koji, T.5    Yodoi, J.6    Inoue, S.7    Kondo, T.8
  • 83
    • 0028920040 scopus 로고
    • UVB radiation-activated genes induced by transcriptional and posttranscriptional mechanisms in rat keratinocytes
    • Rosen, C.F., Poon, R., Drucker, D.J. (1995). UVB radiation-activated genes induced by transcriptional and posttranscriptional mechanisms in rat keratinocytes. American Journal of Physiology, 268, C846-C855.
    • (1995) American Journal of Physiology , vol.268
    • Rosen, C.F.1    Poon, R.2    Drucker, D.J.3
  • 84
    • 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. (2007). Glutathiolation regulates tumor necrosis factor-alpha-induced caspase-3 cleavage and apoptosis: Key role for glutaredoxin in the death pathway. Circulation Research, 100, 213-219.
    • (2007) Circulation Research , vol.100 , pp. 213-219
    • Pan, S.1    Berk, B.C.2
  • 85
    • 0029939584 scopus 로고    scopus 로고
    • A novel promoter sequence is involved in the oxidative stress-induced expression of the adult T-cell leukemia-derived factor (ADF)/human thioredoxin (Trx) gene
    • Taniguchi, Y., Taniguchi-Ueda, Y., Mori, K., Yodoi, J. (1996). A novel promoter sequence is involved in the oxidative stress-induced expression of the adult T-cell leukemia-derived factor (ADF)/human thioredoxin (Trx) gene. Nucleic Acids Research, 24, 2746-2752.
    • (1996) Nucleic Acids Research , vol.24 , pp. 2746-2752
    • Taniguchi, Y.1    Taniguchi-Ueda, Y.2    Mori, K.3    Yodoi, J.4
  • 89
    • 0032958626 scopus 로고    scopus 로고
    • Induction of thioredoxin and thioredoxin reductase gene expression in lungs of newborn primates by oxygen
    • Das, K.C., Guo, X.L., White, C.W. (1999). Induction of thioredoxin and thioredoxin reductase gene expression in lungs of newborn primates by oxygen. American Journal of Physiology, 276, L530-L539.
    • (1999) American Journal of Physiology , vol.276
    • Das, K.C.1    Guo, X.L.2    White, C.W.3
  • 90
    • 34248591499 scopus 로고    scopus 로고
    • Upregulation of thioredoxin system via Nrf2-antioxidant responsive element pathway in adaptive-retinal neuroprotection in vivo and in vitro
    • Tanito, M., Agbaga, M.P., Anderson, R.E. (2007). Upregulation of thioredoxin system via Nrf2-antioxidant responsive element pathway in adaptive-retinal neuroprotection in vivo and in vitro. Free Radical Biology and Medicine, 42, 1838-1850.
    • (2007) Free Radical Biology and Medicine , vol.42 , pp. 1838-1850
    • Tanito, M.1    Agbaga, M.P.2    Anderson, R.E.3
  • 91
    • 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., Chock, P.B. (1999). Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B. Journal of Biological Chemistry, 274, 34543-34546.
    • (1999) Journal of Biological Chemistry , 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
  • 94
    • 20544472348 scopus 로고    scopus 로고
    • Regulation of protein function by glutathionylation
    • Ghezzi, P. (2005). Regulation of protein function by glutathionylation. Free Radical Research, 39, 573-580.
    • (2005) Free Radical Research , vol.39 , pp. 573-580
    • Ghezzi, P.1
  • 95
    • 33749391618 scopus 로고    scopus 로고
    • Glutaredoxin modulates platelet-derived growth factor-dependent cell signaling by regulating the redox status of low molecular weight protein-tyrosine phosphatase
    • Kanda, M., Ihara, Y., Murata, H., Urata, Y., Kono, T., Yodoi, J., Seto, S., Yano, K., Kondo, T. (2006). Glutaredoxin modulates platelet-derived growth factor-dependent cell signaling by regulating the redox status of low molecular weight protein-tyrosine phosphatase. Journal of Biological Chemistry, 281, 8518-28528.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 8518-28528
    • Kanda, M.1    Ihara, Y.2    Murata, H.3    Urata, Y.4    Kono, T.5    Yodoi, J.6    Seto, S.7    Yano, K.8    Kondo, T.9
  • 97
    • 34250328361 scopus 로고    scopus 로고
    • Glutaredoxin regulates nuclear factor kappa-B and intercellular adhesion molecule in Muller cells: Model of diabetic retinopathy
    • Shelton, M.D., Kern, T.S., Mieyal, J.J. (2007). Glutaredoxin regulates nuclear factor kappa-B and intercellular adhesion molecule in Muller cells: Model of diabetic retinopathy. Journal of Biological Chemistry, 282(17), 12467-12474.
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 12467-12474
    • Shelton, M.D.1    Kern, T.S.2    Mieyal, J.J.3
  • 98
    • 0035960648 scopus 로고    scopus 로고
    • Glutathionylation of the p50 subunit of NF-kappaB: A mechanism for redoxinduced inhibition of DNA binding
    • Pineda-Molina, E., Klatt, P., Vazquez, J., Marina, A., Garcia, D.L., Perez-Sala, D., Lamas, S. (2001). Glutathionylation of the p50 subunit of NF-kappaB: A mechanism for redoxinduced inhibition of DNA binding. Biochemistry, 40, 14134-14142.
    • (2001) Biochemistry , vol.40 , pp. 14134-14142
    • Pineda-Molina, E.1    Klatt, P.2    Vazquez, J.3    Marina, A.4    Garcia, D.L.5    Perez-Sala, D.6    Lamas, S.7
  • 101
    • 9444251087 scopus 로고    scopus 로고
    • Estrogen and neuroprotection: Higher constitutive expression of glutaredoxin in female mice offers protection against MPTP-mediated neurodegeneration
    • Kenchappa, R.S., Diwakar, L., Annepu, J., Ravindranath, V. (2004). Estrogen and neuroprotection: Higher constitutive expression of glutaredoxin in female mice offers protection against MPTP-mediated neurodegeneration. FASEB Journal, 18, 1102-1104.
    • (2004) FASEB Journal , vol.18 , pp. 1102-1104
    • Kenchappa, R.S.1    Diwakar, L.2    Annepu, J.3    Ravindranath, V.4
  • 104
    • 34247362854 scopus 로고    scopus 로고
    • PTP1B as a drug target: Recent developments in PTP1B inhibitor discovery
    • Zhang, S., Zhang, Z.Y. (2007). PTP1B as a drug target: Recent developments in PTP1B inhibitor discovery. Drug Discovery Today, 12, 373-381.
    • (2007) Drug Discovery Today , vol.12 , pp. 373-381
    • Zhang, S.1    Zhang, Z.Y.2
  • 105
    • 0031973308 scopus 로고    scopus 로고
    • Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor I
    • Bandyopadhyay, S., Starke, D.W., Mieyal, J.J., Gronostajski, R.M. (1998). Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor I. Journal of Biological Chemistry, 273, 392-397.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 392-397
    • Bandyopadhyay, S.1    Starke, D.W.2    Mieyal, J.J.3    Gronostajski, R.M.4
  • 106
    • 64149130388 scopus 로고    scopus 로고
    • Glutaredoxin regulates autocrine and paracrine proinflammatory responses in retinal glial (Müller) cells
    • Shelton, M.D., Distler, A.M., Kern, T.S., Mieyal, J.J. (2009). Glutaredoxin regulates autocrine and paracrine proinflammatory responses in retinal glial (Müller) cells. Journal of Biological Chemistry, 284, 4760-4766.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 4760-4766
    • Shelton, M.D.1    Distler, A.M.2    Kern, T.S.3    Mieyal, J.J.4
  • 107
    • 34547128886 scopus 로고    scopus 로고
    • Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFkB
    • Qanungo, S., Starke, D.W., Pai, H.V., Mieyal, J.J., Nieminen, A.L. (2007). Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFkB. Journal of Biological Chemistry, 282, 18427-18436.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 18427-18436
    • Qanungo, S.1    Starke, D.W.2    Pai, H.V.3    Mieyal, J.J.4    Nieminen, A.L.5
  • 108
    • 0038015010 scopus 로고    scopus 로고
    • Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase): Potential role in redox signal transduction
    • Starke, D.W., Chock, P.B., Mieyal, J.J. (2003). Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase): Potential role in redox signal transduction. Journal of Biological Chemistry, 278, 14607-14613.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 14607-14613
    • Starke, D.W.1    Chock, P.B.2    Mieyal, J.J.3
  • 109
    • 0034705239 scopus 로고    scopus 로고
    • Regulation of protein kinase B and 4E-BP1 by oxidative stress in cardiac myocytes
    • Pham, F.H., Sugden, P.H., Clerk, A. (2000). Regulation of protein kinase B and 4E-BP1 by oxidative stress in cardiac myocytes. Circulation Research, 86, 1252-1258.
    • (2000) Circulation Research , vol.86 , pp. 1252-1258
    • Pham, F.H.1    Sugden, P.H.2    Clerk, A.3
  • 112
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • Shaulian, E., Karin, M. (2002). AP-1 as a regulator of cell life and death. Nature Cell Biology, 4, E131-E136.
    • (2002) Nature Cell Biology , vol.4
    • Shaulian, E.1    Karin, M.2
  • 115
    • 1542318096 scopus 로고    scopus 로고
    • Initiation of neuronal damage by complex I deficiency and oxidative stress in Parkinson's disease
    • Tretter, L., Sipos, I., Adam-Vizi, V. (2004). Initiation of neuronal damage by complex I deficiency and oxidative stress in Parkinson's disease. Neurochemical Research, 29, 569-577.
    • (2004) Neurochemical Research , vol.29 , pp. 569-577
    • Tretter, L.1    Sipos, I.2    Adam-Vizi, V.3
  • 116
    • 24944525045 scopus 로고    scopus 로고
    • Molecular pathogenesis of Parkinson's disease
    • Gandhi, S., Wood, N.W. (2005). Molecular pathogenesis of Parkinson's disease. Human Molecular Genetics, 14(Spec No. 2), 2749-2755.
    • (2005) Human Molecular Genetics , vol.14 , Issue.SPEC. 2 , pp. 2749-2755
    • Gandhi, S.1    Wood, N.W.2
  • 117
    • 54049146740 scopus 로고    scopus 로고
    • Complex I within oxidatively stressed bovine heart mitochondria is glutathionylated on Cys 531 and Cys 704 of the 75 kDa subunit: potential role of CYS residues in decreasing oxidative damage
    • Hurd, T.R., Requejo, R., Filipovska, A., Brown, S., Prime, T.A., Robinson, A.J., Fearnley, I.M., Murphy, M.P. (2008). Complex I within oxidatively stressed bovine heart mitochondria is glutathionylated on Cys 531 and Cys 704 of the 75 kDa subunit: potential role of CYS residues in decreasing oxidative damage. Journal of Biological Chemistry, 283, 24801-24815.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 24801-24815
    • Hurd, T.R.1    Requejo, R.2    Filipovska, A.3    Brown, S.4    Prime, T.A.5    Robinson, A.J.6    Fearnley, I.M.7    Murphy, M.P.8
  • 118
    • 0037390718 scopus 로고    scopus 로고
    • Glutaredoxin is essential for maintenance of brain mitochondrial complex I: Studies with MPTP
    • Kenchappa, R.S., Ravindranath, V. (2003). Glutaredoxin is essential for maintenance of brain mitochondrial complex I: Studies with MPTP. FASEB Journal, 17, 717-719.
    • (2003) FASEB Journal , vol.17 , pp. 717-719
    • Kenchappa, R.S.1    Ravindranath, V.2
  • 119
    • 34347335719 scopus 로고    scopus 로고
    • Downregulation of glutaredoxin but not glutathione loss leads to mitochondrial dysfunction in female mice CNS: Implications in excitotoxicity
    • Diwakar, L., Kenchappa, R.S., Annepu, J., Ravindranath, V. (2007), Downregulation of glutaredoxin but not glutathione loss leads to mitochondrial dysfunction in female mice CNS: Implications in excitotoxicity. Neurochemistry International, 51, 37-46.
    • (2007) Neurochemistry International , vol.51 , pp. 37-46
    • Diwakar, L.1    Kenchappa, R.S.2    Annepu, J.3    Ravindranath, V.4
  • 120
    • 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., Murphy, M.P. (2004). Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: Implications for mitochondrial redox regulation and antioxidant defense. Journal of Biological Chemistry, 279, 47939-47951.
    • (2004) Journal of Biological Chemistry , 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    Murphy, M.P.7
  • 122
    • 0030851732 scopus 로고    scopus 로고
    • Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro
    • Davis, D.A., Newcomb, F.M., Starke, D.W., Ott, D.E., Mieyal, J.J., Yarchoan, R. (1997). Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro. Journal of Biological Chemistry, 272, 25935-25940.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 25935-25940
    • Davis, D.A.1    Newcomb, F.M.2    Starke, D.W.3    Ott, D.E.4    Mieyal, J.J.5    Yarchoan, R.6
  • 123
    • 34347329257 scopus 로고    scopus 로고
    • Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNAbinding domain during oxidative stress
    • Velu, C.S., Niture, S.K., Doneanu, C.E., Pattabiraman, N., Srivenugopal, K.S. (2007). Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNAbinding domain during oxidative stress. Biochemistry, 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
  • 124
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: A historical overviewand speculative preview of novel mechanisms and emerging concepts in cell signaling
    • Rhee, S.G., Chae, H.Z., Kim, K. (2005). Peroxiredoxins: A historical overviewand speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radical Biology and Medicine, 38, 1543-1552.
    • (2005) Free Radical Biology and Medicine , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 125
  • 126
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteinesulphinic acid by S. cerevisiae sulphiredoxin
    • Biteau, B., Labarre, J., Toledano, M.B. (2003). ATP-dependent reduction of cysteinesulphinic acid by S. cerevisiae sulphiredoxin. Nature, 425, 980-984.
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 128
    • 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. (2004). Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST. Proceedings of the National Academy of Sciences USA, 101, 3780-3785.
    • (2004) Proceedings of the National Academy of Sciences USA , vol.101 , pp. 3780-3785
    • Manevich, Y.1    Feinstein, S.I.2    Fisher, A.B.3
  • 129
    • 0028139014 scopus 로고
    • The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase
    • Bjornstedt, M., Xue, J., Huang, W., Akesson, B., Holmgren, A. (1994). The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. Journal of Biological Chemistry, 269, 29382-29384.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 29382-29384
    • Bjornstedt, M.1    Xue, J.2    Huang, W.3    Akesson, B.4    Holmgren, A.5
  • 131
    • 0038701886 scopus 로고    scopus 로고
    • The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes
    • Nickel,W. (2003). The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes. European Journal of Biochemistry, 270, 2109-2119.
    • (2003) European Journal of Biochemistry , vol.270 , pp. 2109-2119
    • Nickel, W.1
  • 133
    • 33947681723 scopus 로고    scopus 로고
    • Ischemic preconditioning triggers nuclear translocation of thioredoxin and its interaction with Ref-1 potentiating a survival signal through the PI-3-kinase-Akt pathway
    • Malik, G., Gorbounov, N., Das, S., Gurusamy, N., Otani, H., Maulik, N., Goswami, S., Das, D.K. (2006). Ischemic preconditioning triggers nuclear translocation of thioredoxin and its interaction with Ref-1 potentiating a survival signal through the PI-3-kinase-Akt pathway. Antioxidants and Redox Signaling, 8, 2101-2109.
    • (2006) Antioxidants and Redox Signaling , vol.8 , pp. 2101-2109
    • Malik, G.1    Gorbounov, N.2    Das, S.3    Gurusamy, N.4    Otani, H.5    Maulik, N.6    Goswami, S.7    Das, D.K.8
  • 135
    • 28844443129 scopus 로고    scopus 로고
    • Endogenous thioredoxin is required for redox cycling of anthracyclines and p53-dependent apoptosis in cancer cells
    • Ravi, D., Muniyappa, H., Das, K.C. (2005). Endogenous thioredoxin is required for redox cycling of anthracyclines and p53-dependent apoptosis in cancer cells. Journal of Biological Chemistry, 280, 40084-40096.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 40084-40096
    • Ravi, D.1    Muniyappa, H.2    Das, K.C.3
  • 136
    • 0034544555 scopus 로고    scopus 로고
    • Thioredoxin nuclear translocation and interaction with redox factor-1 activates the activator protein-1 transcription factor in response to ionizing radiation
    • Wei, S.J., Botero, A., Hirota, K., Bradbury, C.M., Markovina, S., Laszlo, A., Spitz, D.R., Goswami, P.C., Yodoi, J., Gius, D. (2000). Thioredoxin nuclear translocation and interaction with redox factor-1 activates the activator protein-1 transcription factor in response to ionizing radiation. Cancer Research, 60, 6688-6695.
    • (2000) Cancer Research , vol.60 , pp. 6688-6695
    • Wei, S.J.1    Botero, A.2    Hirota, K.3    Bradbury, C.M.4    Markovina, S.5    Laszlo, A.6    Spitz, D.R.7    Goswami, P.C.8    Yodoi, J.9    Gius, D.10
  • 138
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg, J., Arner, E.S. (2001). Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radical Biology and Medicine, 31, 1287-1312.
    • (2001) Free Radical Biology and Medicine , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.2
  • 140
    • 0042068217 scopus 로고    scopus 로고
    • Differential role of glutaredoxin and thioredoxin in metabolic oxidative stress-induced activation of apoptosis signal-regulating kinase 1
    • Song, J.J., Lee, Y.J. (2003). Differential role of glutaredoxin and thioredoxin in metabolic oxidative stress-induced activation of apoptosis signal-regulating kinase 1. Biochemistry Journal, 373, 845-853.
    • (2003) Biochemistry Journal , vol.373 , pp. 845-853
    • Song, J.J.1    Lee, Y.J.2
  • 145
    • 0032936755 scopus 로고    scopus 로고
    • Etiology and pathogenesis of Parkinson's disease
    • Olanow, C.W., Tatton, W.G. (1999). Etiology and pathogenesis of Parkinson's disease. Annual Review of Neuroscience, 22, 123-144.
    • (1999) Annual Review of Neuroscience , vol.22 , pp. 123-144
    • Olanow, C.W.1    Tatton, W.G.2
  • 146
    • 0035877650 scopus 로고    scopus 로고
    • Glutaredoxin protects cerebellar granule neurons from dopamineinduced apoptosis by dual activation of the ras-phosphoinositide 3-kinase and jun N-terminal kinase pathways
    • Daily, D., Vlamis-Gardikas, A., Offen, D., Mittelman, L., Melamed, E., Holmgren, A., Barzilai, A. (2001). Glutaredoxin protects cerebellar granule neurons from dopamineinduced apoptosis by dual activation of the ras-phosphoinositide 3-kinase and jun N-terminal kinase pathways. Journal of Biological Chemistry, 276, 21618-21626.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 21618-21626
    • Daily, D.1    Vlamis-Gardikas, A.2    Offen, D.3    Mittelman, L.4    Melamed, E.5    Holmgren, A.6    Barzilai, A.7
  • 152
    • 2942547764 scopus 로고    scopus 로고
    • Thioredoxin, a redox-regulating protein, is expressed in spontaneous myocarditis in inbred strains of mice
    • Miyamoto, M., Kishimoto, C., Nimata, M., Nakamura, H., Yodoi, J. (2004). Thioredoxin, a redox-regulating protein, is expressed in spontaneous myocarditis in inbred strains of mice. International Journal of Cardiology, 95, 315-319.
    • (2004) International Journal of Cardiology , vol.95 , pp. 315-319
    • Miyamoto, M.1    Kishimoto, C.2    Nimata, M.3    Nakamura, H.4    Yodoi, J.5
  • 157
    • 4444335186 scopus 로고    scopus 로고
    • Thioredoxin as a neurotrophic cofactor and an important regulator of neuroprotection
    • Masutani, H., Bai, J., Kim, Y.C., Yodoi, J. (2004). Thioredoxin as a neurotrophic cofactor and an important regulator of neuroprotection. Molecular Neurobiology, 29, 229-242.
    • (2004) Molecular Neurobiology , vol.29 , pp. 229-242
    • Masutani, H.1    Bai, J.2    Kim, Y.C.3    Yodoi, J.4
  • 158
    • 0031866124 scopus 로고    scopus 로고
    • Expression of adult T cell leukemia-derived factor in human brain and peripheral nerve tissues
    • Asahina, M., Yamada, T., Yoshiyama, Y., Yodoi, J. (1998). Expression of adult T cell leukemia-derived factor in human brain and peripheral nerve tissues. Dementia and Geriatric Cognitive Disorders, 9, 181-185.
    • (1998) Dementia and Geriatric Cognitive Disorders , vol.9 , pp. 181-185
    • Asahina, M.1    Yamada, T.2    Yoshiyama, Y.3    Yodoi, J.4
  • 159
    • 0030585429 scopus 로고    scopus 로고
    • Crystal structures of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer
    • Weichsel, A., Gasdaska, J.R., Powis, G., Montfort, W.R. (1996). Crystal structures of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer. Structure, 4, 735-751.
    • (1996) Structure , vol.4 , pp. 735-751
    • Weichsel, A.1    Gasdaska, J.R.2    Powis, G.3    Montfort, W.R.4
  • 160
    • 0032563140 scopus 로고    scopus 로고
    • The NMR solution structure of human glutaredoxin in the fully reduced form
    • Sun, C., Berardi, M.J., Bushweller, J.H. (1998). The NMR solution structure of human glutaredoxin in the fully reduced form. Journal of Molecular Biology, 280, 687-701.
    • (1998) Journal of Molecular Biology , vol.280 , pp. 687-701
    • Sun, C.1    Berardi, M.J.2    Bushweller, J.H.3


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