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Volumn 394, Issue 10, 2013, Pages 1263-1280

S-glutathionylation: Relevance in diabetes and potential role as a biomarker

Author keywords

Diabetes; Glutathione; Hyperglycemia; Oxidative stress; Posttranslational modification; Signaling

Indexed keywords

BIOLOGICAL MARKER; GLUTATHIONE; REACTIVE OXYGEN METABOLITE;

EID: 84888084094     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2013-0150     Document Type: Article
Times cited : (34)

References (159)
  • 1
    • 3142663363 scopus 로고    scopus 로고
    • S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells
    • DOI 10.1074/jbc.M313320200
    • Adachi, T., Pimentel, D.R., Heibeck, T., Hou, X., Lee, Y.J., Jiang, B., Ido, Y., and Cohen, R.A. (2004). S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells. J. Biol. Chem. 279, 29857-29862. (Pubitemid 38915870)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.28 , pp. 29857-29862
    • Adachi, T.1    Pimentel, D.R.2    Heibeck, T.3    Hou, X.4    Lee, Y.J.5    Jiang, B.6    Ido, Y.7    Cohen, R.A.8
  • 2
    • 0020080046 scopus 로고
    • Competition between transport of glutathione disulfide (GSSG) and glutathione S-conjugates from perfused rat liver into bile
    • DOI 10.1016/0014-5793(82)80523-1
    • Akerboom, T.P., Bilzer, M., and Sies, H. (1982). Competition between transport of glutathione disulfide (GSSG) and glutathione S-conjugates from perfused rat liver into bile. FEBS Lett. 140, 73-76. (Pubitemid 12123454)
    • (1982) FEBS Letters , vol.140 , Issue.1 , pp. 73-76
    • Akerboom, T.P.M.1    Bilzer, M.2    Sies, H.3
  • 3
    • 80052548067 scopus 로고    scopus 로고
    • Redox homeostasis and posttranslational modifications/ activity of phosphatase and tensin homolog in hepatocytes from rats with diet-induced hepatosteatosis
    • Alisi, A., Bruscalupi, G., Pastore, A., Petrini, S., Panera, N., Massimi, M., Tozzi, G., Leoni, S., Piemonte, F., and Nobili, V. (2012). Redox homeostasis and posttranslational modifications/ activity of phosphatase and tensin homolog in hepatocytes from rats with diet-induced hepatosteatosis. J. Nutr. Biochem. 23, 169-178.
    • (2012) J. Nutr. Biochem , vol.23 , pp. 169-178
    • Alisi, A.1    Bruscalupi, G.2    Pastore, A.3    Petrini, S.4    Panera, N.5    Massimi, M.6    Tozzi, G.7    Leoni, S.8    Piemonte, F.9    Nobili, V.10
  • 4
    • 1542283780 scopus 로고    scopus 로고
    • Regulation of endothelial nitric oxide synthase by tetrahydrobiopterin in vascular disease
    • DOI 10.1161/01.ATV.0000110785.96039.f6
    • Alp, N.J. and Channon, K.M. (2004). Regulation of endothelial nitric oxide synthase by tetrahydrobiopterin in vascular disease. Arterioscler. Thromb. Vasc. Biol. 24, 413-420. (Pubitemid 38326132)
    • (2004) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.24 , Issue.3 , pp. 413-420
    • Alp, N.J.1    Channon, K.M.2
  • 6
    • 22044433408 scopus 로고    scopus 로고
    • NF-κB, Nrf2, and HO-1 interplay in redox-regulated VCAM-1 expression
    • DOI 10.1089/ars.2005.7.889
    • Banning, A. and Brigelius-Flohe, R. (2005). NF-κB, Nrf2, and HO-1 interplay in redox-regulated VCAM-1 expression. Antioxid. Redox Signal. 7, 889-899. (Pubitemid 40967140)
    • (2005) Antioxidants and Redox Signaling , vol.7 , Issue.7-8 , pp. 889-899
    • Banning, A.1    Brigelius-Flohe, R.2
  • 8
    • 0027236637 scopus 로고
    • A glutathione S-transferase with glutathione-peroxidase activity from Arabidopsis thaliana. Molecular cloning and functional characterization
    • Bartling, D., Radzio, R., Steiner, U., and Weiler, E.W. (1993). A glutathione S-transferase with glutathione-peroxidase activity from Arabidopsis thaliana. Molecular cloning and functional characterization. Eur. J. Biochem. 216, 579-586. (Pubitemid 23276306)
    • (1993) European Journal of Biochemistry , vol.216 , Issue.2 , pp. 579-586
    • Bartling, D.1    Radzio, R.2    Steiner, U.3    Weiler, E.W.4
  • 9
    • 32444444938 scopus 로고    scopus 로고
    • C-myc phosphorylation is required for cellular response to oxidative stress
    • DOI 10.1016/j.molcel.2006.01.009, PII S1097276506000104
    • Benassi, B., Fanciulli, M., Fiorentino, F., Porrello, A., Chiorino, G., Loda, M., Zupi, G., and Biroccio, A. (2006). c-Myc phosphorylation is required for cellular response to oxidative stress. Mol. Cell. 21, 509-519. (Pubitemid 43228006)
    • (2006) Molecular Cell , vol.21 , Issue.4 , pp. 509-519
    • Benassi, B.1    Fanciulli, M.2    Fiorentino, F.3    Porrello, A.4    Chiorino, G.5    Loda, M.6    Zupi, G.7    Biroccio, A.8
  • 11
    • 0017348934 scopus 로고
    • Mitochondrial production of superoxide radical and hydrogen peroxide
    • Boveris, A. (1977). Mitochondrial production of superoxide radical and hydrogen peroxide. Adv. Exp. Med. Biol. 78, 67-82.
    • (1977) Adv. Exp. Med. Biol , vol.78 , pp. 67-82
    • Boveris, A.1
  • 12
    • 33750629812 scopus 로고    scopus 로고
    • Glutathione peroxidases and redox-regulated transcription factors
    • DOI 10.1515/BC.2006.166, PII BCHM38710111329
    • Brigelius-Flohe, R. (2006). Glutathione peroxidases and redoxregulated transcription factors. Biol. Chem. 387, 1329-1335. (Pubitemid 44691411)
    • (2006) Biological Chemistry , vol.387 , Issue.10-11 , pp. 1329-1335
    • Brigelius-Flohe, R.1
  • 13
    • 14644427890 scopus 로고    scopus 로고
    • Local and systemic insulin resistance resulting from hepatic activation of IKK-β and NF-κB
    • DOI 10.1038/nm1166
    • Cai, D., Yuan, M., Frantz, D.F., Melendez, P.A., Hansen, L., Lee, J., and Shoelson, S.E. (2005). Local and systemic insulin resistance resulting from hepatic activation of IKK-beta and NF-κB. Nat. Med. 11, 183-190. (Pubitemid 40321354)
    • (2005) Nature Medicine , vol.11 , Issue.2 , pp. 183-190
    • Cai, D.1    Yuan, M.2    Frantz, D.F.3    Melendez, P.A.4    Hansen, L.5    Lee, J.6    Shoelson, S.E.7
  • 15
    • 34249815532 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein stimulates p53-dependent activation of proapoptotic Bax leading to apoptosis of differentiated endothelial progenitor cells
    • DOI 10.1210/en.2006-1709
    • Cheng, J., Cui, R., Chen, C.H., and Du, J. (2007). Oxidized low-density lipoprotein stimulates p53-dependent activation of proapoptotic Bax leading to apoptosis of differentiated endothelial progenitor cells. Endocrinology 148, 2085-2094. (Pubitemid 46997036)
    • (2007) Endocrinology , vol.148 , Issue.5 , pp. 2085-2094
    • Cheng, J.1    Cui, R.2    Chen, C.-H.3    Du, J.4
  • 16
    • 11444261268 scopus 로고    scopus 로고
    • Gene expression profiling of NRF2-mediated protection against oxidative injury
    • DOI 10.1016/j.freeradbiomed.2004.10.013, PII S0891584904008354
    • Cho, H.Y., Reddy, S.P., Debiase, A., Yamamoto, M., and Kleeberger, S.R. (2005). Gene expression profiling of NRF2-mediated protection against oxidative injury. Free Radic. Biol. Med. 38, 325-343. (Pubitemid 40081112)
    • (2005) Free Radical Biology and Medicine , vol.38 , Issue.3 , pp. 325-343
    • Cho, H.-Y.1    Reddy, S.P.2    DeBiase, A.3    Yamamoto, M.4    Kleeberger, S.R.5
  • 17
    • 0029983347 scopus 로고    scopus 로고
    • Relationship between glutathione and sorbitol concentrations in erythrocytes from diabetic patients
    • DOI 10.1016/S0026-0495(96)90032-3
    • Ciuchi, E., Odetti, P., and Prando, R. (1996). Relationship between glutathione and sorbitol concentrations in erythrocytes from diabetic patients. Metabolism 45, 611-613. (Pubitemid 26146114)
    • (1996) Metabolism: Clinical and Experimental , vol.45 , Issue.5 , pp. 611-613
    • Ciuchi, E.1    Odetti, P.2    Prando, R.3
  • 18
    • 0031127932 scopus 로고    scopus 로고
    • Detoxification of xenobiotics by plants: Chemical modification and vacuolar compartmentation
    • DOI 10.1016/S1360-1385(97)01019-4
    • Coleman, J., Blake-Kalff, M., and Davies, E. (1997). Detoxification of xenobiotics by plants: chemical modification and vacuolar compartmentation. Trends Plant. Sci. 2, 144-151. (Pubitemid 27158897)
    • (1997) Trends in Plant Science , vol.2 , Issue.4 , pp. 144-151
    • Coleman, J.O.D.1    Blake-Kalff, M.M.A.2    Davies, T.G.E.3
  • 19
    • 79952935338 scopus 로고    scopus 로고
    • Redox regulation of insulin degradation by insulin-degrading enzyme
    • Cordes, C.M., Bennett, R.G., Siford, G.L., and Hamel, F.G. (2011). Redox regulation of insulin degradation by insulin-degrading enzyme. PLoS One 6, e18138.
    • (2011) PLoS One , vol.6
    • Cordes, C.M.1    Bennett, R.G.2    Siford, G.L.3    Hamel, F.G.4
  • 20
    • 84872094899 scopus 로고    scopus 로고
    • Integrated redox sensor and effector functions for tetrahydrobiopterin- and glutathionylation-dependent endothelial nitric-oxide synthase uncoupling
    • Crabtree, M.J., Brixey, R., Batchelor, H., Hale, A.B., and Channon, K.M. (2013). Integrated redox sensor and effector functions for tetrahydrobiopterin- and glutathionylation-dependent endothelial nitric-oxide synthase uncoupling. J. Biol. Chem. 288, 561-569.
    • (2013) J. Biol. Chem , vol.288 , pp. 561-569
    • Crabtree, M.J.1    Brixey, R.2    Batchelor, H.3    Hale, A.B.4    Channon, K.M.5
  • 21
    • 0028039015 scopus 로고
    • Impaired nitric oxide-dependent cyclic guanosine monophosphate generation in glomeruli from diabetic rats. Evidence for protein kinase C-mediated suppression of the cholinergic response
    • Craven, P.A., Studer, R.K., and DeRubertis, F.R. (1994). Impaired nitric oxide-dependent cyclic guanosine monophosphate generation in glomeruli from diabetic rats. Evidence for protein kinase C-mediated suppression of the cholinergic response. J. Clin. Invest. 93, 311-320.
    • (1994) J. Clin. Invest , vol.93 , pp. 311-320
    • Craven, P.A.1    Studer, R.K.2    Derubertis, F.R.3
  • 22
    • 4344686072 scopus 로고    scopus 로고
    • Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain
    • DOI 10.1042/BJ20040591
    • Cross, J.V. and Templeton, D.J. (2004). Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain. Biochem. J. 381, 675-683. (Pubitemid 39120476)
    • (2004) Biochemical Journal , vol.381 , Issue.3 , pp. 675-683
    • Cross, J.V.1    Templeton, D.J.2
  • 24
    • 12144274310 scopus 로고    scopus 로고
    • Evidence for accelerated rates of glutathione utilization and glutathione depletion in adolescents with poorly controlled type 1 diabetes
    • DOI 10.2337/diabetes.54.1.190
    • Darmaun, D., Smith, S.D., Sweeten, S., Sager, B.K., Welch, S., and Mauras, N. (2005). Evidence for accelerated rates of glutathione utilization and glutathione depletion in adolescents with poorly controlled type 1 diabetes. Diabetes 54, 190-196. (Pubitemid 40105112)
    • (2005) Diabetes , vol.54 , Issue.1 , pp. 190-196
    • Darmaun, D.1    Smith, S.D.2    Sweeten, S.3    Sager, B.K.4    Welch, S.5    Mauras, N.6
  • 25
    • 56649092631 scopus 로고    scopus 로고
    • Poorly controlled type 1 diabetes is associated with altered glutathione homeostasis in adolescents: Apparent resistance to N-acetylcysteine supplementation
    • Darmaun, D., Smith, S.D., Sweeten, S., Hartman, B.K., Welch, S., and Mauras, N. (2008). Poorly controlled type 1 diabetes is associated with altered glutathione homeostasis in adolescents: apparent resistance to N-acetylcysteine supplementation. Pediatr. Diabetes 9, 577-582.
    • (2008) Pediatr. Diabetes , vol.9 , pp. 577-582
    • Darmaun, D.1    Smith, S.D.2    Sweeten, S.3    Hartman, B.K.4    Welch, S.5    Mauras, N.6
  • 26
    • 33846818811 scopus 로고    scopus 로고
    • Thyroid hormone promotes glutathione synthesis in astrocytes by up regulation of glutamate cysteine ligase through differential stimulation of its catalytic and modulator subunit mRNAs
    • DOI 10.1016/j.freeradbiomed.2006.11.030, PII S0891584906007696
    • Dasgupta, A., Das, S., and Sarkar, P.K. (2007). Thyroid hormone promotes glutathione synthesis in astrocytes by up regulation of glutamate cysteine ligase through differential stimulation of its catalytic and modulator subunit mRNAs. Free Radic. Biol. Med. 42, 617-626. (Pubitemid 46210131)
    • (2007) Free Radical Biology and Medicine , vol.42 , Issue.5 , pp. 617-626
    • Dasgupta, A.1    Das, S.2    Kumar Sarkar, P.3
  • 28
    • 0015880169 scopus 로고
    • Glutathione peroxidase: A selenoenzyme
    • Flohe, L., Gunzler, W.A., and Schock, H.H. (1973). Glutathione peroxidase: a selenoenzyme. FEBS Lett. 32, 132-134.
    • (1973) FEBS Lett , vol.32 , pp. 132-134
    • Flohe, L.1    Gunzler, W.A.2    Schock, H.H.3
  • 29
    • 75749136883 scopus 로고    scopus 로고
    • Signaling functions of reactive oxygen species
    • Forman, H.J., Maiorino, M., and Ursini, F. (2010). Signaling functions of reactive oxygen species. Biochemistry 49, 835-842.
    • (2010) Biochemistry , vol.49 , pp. 835-842
    • Forman, H.J.1    Maiorino, M.2    Ursini, F.3
  • 30
    • 0036095124 scopus 로고    scopus 로고
    • Caspase-3-dependent cleavage of the glutamate-L-cysteine ligase catalytic subunit during apoptotic cell death
    • Franklin, C.C., Krejsa, C.M., Pierce, R.H., White, C.C., Fausto, N., and Kavanagh, T.J. (2002). Caspase-3-dependent cleavage of the glutamate-L-cysteine ligase catalytic subunit during apoptotic cell death. Am. J. Pathol. 160, 1887-1894. (Pubitemid 34525668)
    • (2002) American Journal of Pathology , vol.160 , Issue.5 , pp. 1887-1894
    • Franklin, C.C.1    Krejsa, C.M.2    Pierce, R.H.3    White, C.C.4    Fausto, N.5    Kavanagh, T.J.6
  • 31
    • 0017687764 scopus 로고
    • Severe generalized glutathione reductase deficiency after antitumor chemotherapy with BCNU [1,3 bis(chloroethyl) 1 nitrosourea]
    • Frischer, H. and Ahmad, T. (1977). Severe generalized glutathione reductase deficiency after antitumor chemotherapy with BCNU [1,3- bis(chloroethyl)-1-nitrosourea]. J. Lab. Clin. Med. 89, 1080-1091. (Pubitemid 8107524)
    • (1977) Journal of Laboratory and Clinical Medicine , vol.89 , Issue.5 , pp. 1080-1091
    • Frischer, H.1    Ahmad, T.2
  • 32
    • 33645454310 scopus 로고    scopus 로고
    • Leukocyte recruitment and vascular injury in diabetic nephropathy
    • Galkina, E. and Ley, K. (2006). Leukocyte recruitment and vascular injury in diabetic nephropathy. J. Am. Soc. Nephrol. 17, 368-377.
    • (2006) J. Am. Soc. Nephrol , vol.17 , pp. 368-377
    • Galkina, E.1    Ley, K.2
  • 33
    • 0033048630 scopus 로고    scopus 로고
    • Ajoene is an inhibitor and subversive substrate of human glutathione reductase and Trypanosoma cruzi trypanothione reductase: Crystallographic, kinetic, and spectroscopic studies
    • DOI 10.1021/jm980471k
    • Gallwitz, H., Bonse, S., Martinez-Cruz, A., Schlichting, I., Schumacher, K., and Krauth-Siegel, R.L. (1999). Ajoene is an inhibitor and subversive substrate of human glutathione reductase and Trypanosoma cruzi trypanothione reductase: crystallographic, kinetic, and spectroscopic studies. J. Med. Chem. 42, 364-372. (Pubitemid 29085096)
    • (1999) Journal of Medicinal Chemistry , vol.42 , Issue.3 , pp. 364-372
    • Gallwitz, H.1    Bonse, S.2    Martinez-Cruz, A.3    Schlichting, I.4    Schumacher, K.5    Krauth-Siegel, R.L.6
  • 34
    • 0031467818 scopus 로고    scopus 로고
    • A diverse superfamily of enzymes with ATP-dependent carboxylate- amine/thiol ligase activity
    • Galperin, M.Y. and Koonin, E.V. (1997). A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Sci. 6, 2639-2643. (Pubitemid 28006703)
    • (1997) Protein Science , vol.6 , Issue.12 , pp. 2639-2643
    • Galperin, M.Y.1    Koonin, E.V.2
  • 35
    • 33747618005 scopus 로고    scopus 로고
    • Mitochondrial glutathione: Hepatocellular survival-death switch
    • DOI 10.1111/j.1440-1746.2006.04570.x
    • Garcia-Ruiz, C. and Fernandez-Checa, J.C. (2006). Mitochondrial glutathione: hepatocellular survival-death switch. J. Gastroenterol. Hepatol. 21 (Suppl 3), S3-S6. (Pubitemid 44266539)
    • (2006) Journal of Gastroenterology and Hepatology , vol.21 , Issue.SUPPL. 3
    • Garcia-Ruiz, C.1    Fernandez-Checa, J.C.2
  • 36
    • 78349297565 scopus 로고    scopus 로고
    • Oxidative stress and diabetic complications
    • Giacco, F. and Brownlee, M. (2010). Oxidative stress and diabetic complications. Circ. Res. 107, 1058-1070.
    • (2010) Circ. Res , vol.107 , pp. 1058-1070
    • Giacco, F.1    Brownlee, M.2
  • 37
    • 40949100047 scopus 로고    scopus 로고
    • Regulation of smooth muscle by inducible nitric oxide synthase and NADPH oxidase in vascular proliferative diseases
    • Ginnan, R., Guikema, B.J., Halligan, K.E., Singer, H.A., and Jourd'heuil, D. (2008). Regulation of smooth muscle by inducible nitric oxide synthase and NADPH oxidase in vascular proliferative diseases. Free Radic. Biol. Med. 44, 1232-1245.
    • (2008) Free Radic. Biol. Med , vol.44 , pp. 1232-1245
    • Ginnan, R.1    Guikema, B.J.2    Halligan, K.E.3    Singer, H.A.4    Jourd'Heuil, D.5
  • 39
    • 0035502381 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B (PTP1B): A novel therapeutic target for type 2 diabetes mellitus, obesity and related states of insulin resistance
    • Goldstein, B.J. (2001). Protein-tyrosine phosphatase 1B (PTP1B): a novel therapeutic target for type 2 diabetes mellitus, obesity and related states of insulin resistance. Curr. Drug Targets Immune. Endocr. Metabol. Disord. 1, 265-275.
    • (2001) Curr. Drug Targets Immune. Endocr. Metabol. Disord , vol.1 , pp. 265-275
    • Goldstein, B.J.1
  • 40
    • 12744279326 scopus 로고    scopus 로고
    • Redox paradox: Insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets
    • Goldstein, B.J., Mahadev, K., and Wu, X. (2005). Redox paradox: insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets. Diabetes 54, 311-321.
    • (2005) Diabetes , vol.54 , pp. 311-321
    • Goldstein, B.J.1    Mahadev, K.2    Wu, X.3
  • 41
    • 0019023638 scopus 로고
    • Excretion of cysteine and γ-glutamylcysteine moieties in human and experimental animal γ-glutamyl transpeptidase deficiency
    • DOI 10.1073/pnas.77.6.3384
    • Griffith, O.W. and Meister, A. (1980). Excretion of cysteine and gamma-glutamylcysteine moieties in human and experimental animal γ-glutamyl transpeptidase deficiency. Proc. Natl. Acad. Sci. USA 77, 3384-3387. (Pubitemid 10016950)
    • (1980) Proceedings of the National Academy of Sciences of the United States of America , vol.77 , Issue.6 , pp. 3384-3387
    • Griffith, O.W.1    Meister, A.2
  • 42
    • 0032562525 scopus 로고    scopus 로고
    • γ-Glutamyl transpeptidase, a glutathionase: Its expression and function in carcinogenesis
    • DOI 10.1016/S0009-2797(97)00170-1, PII S0009279797001701
    • Hanigan, M.H. (1998). γ-Glutamyl transpeptidase, a glutathionase: its expression and function in carcinogenesis. Chem. Biol. Interact. 111-112, 333-342. (Pubitemid 28271953)
    • (1998) Chemico-Biological Interactions , vol.111-112 , pp. 333-342
    • Hanigan, M.H.1
  • 43
    • 80052283310 scopus 로고    scopus 로고
    • Reduced neutrophil apoptosis in diabetic mice during staphylococcal infection leads to prolonged TNFα production and reduced neutrophil clearance
    • Hanses, F., Park, S., Rich, J., and Lee, J.C. (2011). Reduced neutrophil apoptosis in diabetic mice during staphylococcal infection leads to prolonged TNFα production and reduced neutrophil clearance. PLoS One 6, e23633.
    • (2011) PLoS One , vol.6
    • Hanses, F.1    Park, S.2    Rich, J.3    Lee, J.C.4
  • 48
    • 0001500697 scopus 로고
    • The Amadori rearrangement
    • Hodge, J.E. (1955). The Amadori rearrangement. Adv. Carbohydr. Chem. 10, 169-205.
    • (1955) Adv. Carbohydr. Chem , vol.10 , pp. 169-205
    • Hodge, J.E.1
  • 50
    • 2042476756 scopus 로고
    • Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione
    • Holmgren, A. (1976). Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc. Natl. Acad. Sci. USA 73, 2275-2279.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2275-2279
    • Holmgren, A.1
  • 51
    • 0842303109 scopus 로고    scopus 로고
    • Effects of vitamin E on oxidative stress and membrane fluidity in brain of streptozotocin-induced diabetic rats
    • DOI 10.1016/j.cccn.2003.10.003
    • Hong, J.H., Kim, M.J., Park, M.R., Kwag, O.G., Lee, I.S., Byun, B.H., Lee, S.C., Lee, K.B., and Rhee, S.J. (2004). Effects of vitamin E on oxidative stress and membrane fluidity in brain of streptozotocin- induced diabetic rats. Clin. Chim. Acta 340, 107-115. (Pubitemid 38167514)
    • (2004) Clinica Chimica Acta , vol.340 , Issue.1-2 , pp. 107-115
    • Hong, J.-H.1    Kim, M.-J.2    Park, M.-R.3    Kwag, O.-G.4    Lee, I.-S.5    Byun, B.H.6    Lee, S.-C.7    Lee, K.-B.8    Rhee, S.-J.9
  • 52
    • 0027171195 scopus 로고
    • Catalytic and regulatory properties of the heavy subunit of rat kidney γ- glutamylcysteine synthetase
    • Huang, C.S., Chang, L.S., Anderson, M.E., and Meister, A. (1993). Catalytic and regulatory properties of the heavy subunit of rat kidney γ-glutamylcysteine synthetase. J. Biol. Chem. 268, 19675-19680. (Pubitemid 23270758)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.26 , pp. 19675-19680
    • Huang, C.-S.1    Chang, L.-S.2    Anderson, M.E.3    Meister, A.4
  • 55
    • 0037077204 scopus 로고    scopus 로고
    • 1-induced glutathione depletion in alveolar epithelial cells. Involvement of AP-1/ARE and Fra-1
    • DOI 10.1074/jbc.M112145200
    • Jardine, H., MacNee, W., Donaldson, K., and Rahman, I. (2002). Molecular mechanism of transforming growth factor (TGF)-β1- induced glutathione depletion in alveolar epithelial cells. Involvement of AP-1/ARE and Fra-1. J. Biol. Chem. 277, 21158-21166. (Pubitemid 34952251)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.24 , pp. 21158-21166
    • Jardine, H.1    MacNee, W.2    Donaldson, K.3    Rahman, I.4
  • 56
    • 30344486998 scopus 로고    scopus 로고
    • Oxidative stress and diabetic cardiovascular complications
    • DOI 10.1016/j.freeradbiomed.2005.06.018, PII S0891584905003503
    • Jay, D., Hitomi, H., and Griendling, K.K. (2006). Oxidative stress and diabetic cardiovascular complications. Free Radic. Biol. Med. 40, 183-192. (Pubitemid 43069343)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.2 , pp. 183-192
    • Jay, D.1    Hitomi, H.2    Griendling, K.K.3
  • 60
    • 4644276707 scopus 로고    scopus 로고
    • Insulin signaling regulates γ-glutamylcysteine ligase catalytic subunit expression in primary cultured rat hepatocytes
    • DOI 10.1124/jpet.104.070375
    • Kim, S.K., Woodcroft, K.J., Khodadadeh, S.S., and Novak, R.F. (2004). Insulin signaling regulates γ-glutamylcysteine ligase catalytic subunit expression in primary cultured rat hepatocytes. J. Pharmacol. Exp. Ther. 311, 99-108. (Pubitemid 39287788)
    • (2004) Journal of Pharmacology and Experimental Therapeutics , vol.311 , Issue.1 , pp. 99-108
    • Kim, S.K.1    Woodcraft, K.J.2    Khodadadeh, S.S.3    Novak, R.F.4
  • 61
    • 17844381920 scopus 로고    scopus 로고
    • Neutrophils are associated with capillary closure in spontaneously diabetic monkey retinas
    • DOI 10.2337/diabetes.54.5.1534
    • Kim, S.Y., Johnson, M.A., McLeod, D.S., Alexander, T., Hansen, B.C., and Lutty, G.A. (2005). Neutrophils are associated with capillary closure in spontaneously diabetic monkey retinas. Diabetes 54, 1534-1542. (Pubitemid 40586687)
    • (2005) Diabetes , vol.54 , Issue.5 , pp. 1534-1542
    • Kim, S.Y.1    Johnson, M.A.2    McLeod, D.S.3    Alexander, T.4    Hansen, B.C.5    Lutty, G.A.6
  • 62
    • 84863137295 scopus 로고    scopus 로고
    • Glutathione s-transferase omega 1 activity is sufficient to suppress neurodegeneration in a Drosophila model of Parkinson disease
    • Kim, K., Kim, S.H., Kim, J., Kim, H., and Yim, J. (2012a). Glutathione s-transferase omega 1 activity is sufficient to suppress neurodegeneration in a Drosophila model of Parkinson disease. J. Biol. Chem. 287, 6628-6641.
    • (2012) J. Biol. Chem , vol.287 , pp. 6628-6641
    • Kim, K.1    Kim, S.H.2    Kim, J.3    Kim, H.4    Yim, J.5
  • 63
    • 84867339768 scopus 로고    scopus 로고
    • Redox regulation of MAPK phosphatase 1 controls monocyte migration and macrophage recruitment
    • Kim, H.S., Ullevig, S.L., Zamora, D., Lee, C.F., and Asmis, R. (2012b). Redox regulation of MAPK phosphatase 1 controls monocyte migration and macrophage recruitment. Proc. Natl. Acad. Sci. USA 109, E2803-E2812.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109
    • Kim, H.S.1    Ullevig, S.L.2    Zamora, D.3    Lee, C.F.4    Asmis, R.5
  • 64
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • DOI 10.1046/j.1432-1327.2000.01601.x
    • Klatt, P. and Lamas, S. (2000). Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur. J. Biochem. 267, 4928-4944. (Pubitemid 30641289)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.16 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 66
    • 0032983979 scopus 로고    scopus 로고
    • Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation
    • Klatt, P., Molina, E.P., and Lamas, S. (1999b). Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation. J. Biol. Chem. 274, 15857-15864.
    • (1999) J. Biol. Chem , vol.274 , pp. 15857-15864
    • Klatt, P.1    Molina, E.P.2    Lamas, S.3
  • 67
    • 0037213776 scopus 로고    scopus 로고
    • Effects of diabetes, insulin and antioxidants on No synthase abundance and No interaction with reactive oxygen species
    • DOI 10.1046/j.1523-1755.2003.00728.x
    • Koo, J.R. and Vaziri, N.D. (2003). Effects of diabetes, insulin and antioxidants on NO synthase abundance and NO interaction with reactive oxygen species. Kidney Int. 63, 195-201. (Pubitemid 35463921)
    • (2003) Kidney International , vol.63 , Issue.1 , pp. 195-201
    • Koo, J.-R.1    Vaziri, N.D.2
  • 68
    • 80053006895 scopus 로고    scopus 로고
    • Cell signaling and receptors in toxicity of advanced glycation end products (AGEs): α-dicarbonyls, radicals, oxidative stress and antioxidants
    • Kovacic, P. and Somanathan, R. (2011). Cell signaling and receptors in toxicity of advanced glycation end products (AGEs): α-dicarbonyls, radicals, oxidative stress and antioxidants. J. Recept. Signal. Tr. R. 31, 332-339.
    • (2011) J. Recept. Signal. Tr. R , vol.31 , pp. 332-339
    • Kovacic, P.1    Somanathan, R.2
  • 69
    • 25144440916 scopus 로고    scopus 로고
    • Cloning and characterization of the human glutathione synthetase 5'-flanking region
    • DOI 10.1042/BJ20050439
    • Lee, T.D., Yang, H., Whang, J., and Lu, S.C. (2005). Cloning and characterization of the human glutathione synthetase 5'-flanking region. Biochem. J. 390, 521-528. (Pubitemid 41337114)
    • (2005) Biochemical Journal , vol.390 , Issue.2 , pp. 521-528
    • Lee, T.D.1    Yang, H.2    Whang, J.3    Lu, S.C.4
  • 72
    • 77951979741 scopus 로고    scopus 로고
    • S-glutathionylation regulates inflammatory activities of S100A9
    • Lim, S.Y., Raftery, M.J., Goyette, J., and Geczy, C.L. (2010). S-glutathionylation regulates inflammatory activities of S100A9. J. Biol. Chem. 285, 14377-14388.
    • (2010) J. Biol. Chem , vol.285 , pp. 14377-14388
    • Lim, S.Y.1    Raftery, M.J.2    Goyette, J.3    Geczy, C.L.4
  • 73
    • 0037071875 scopus 로고    scopus 로고
    • Molecular diagnosis of colorectal tumors by expression profiles of 50 genes expressed differentially in adenomas and carcinomas
    • DOI 10.1038/sj.onc.1205518
    • Lin, Y.M., Furukawa, Y., Tsunoda, T., Yue, C.T., Yang, K.C., and Nakamura, Y. (2002). Molecular diagnosis of colorectal tumors by expression profiles of 50 genes expressed differentially in adenomas and carcinomas. Oncogene 21, 4120-4128. (Pubitemid 34712879)
    • (2002) Oncogene , vol.21 , Issue.26 , pp. 4120-4128
    • Lin, Y.-M.1    Furukawa, Y.2    Tsunoda, T.3    Yue, C.-T.4    Yang, K.-C.5    Nakamura, Y.6
  • 74
    • 84859081898 scopus 로고    scopus 로고
    • The glutathionylation of p65 modulates NF-kappaB activity in 15-deoxy-Delta(1)(2),(1)(4)-prostaglandin J(2)-treated endothelial cells
    • Lin, Y.C., Huang, G.D., Hsieh, C.W., and Wung, B.S. (2012). The glutathionylation of p65 modulates NF-kappaB activity in 15-deoxy-Delta(1)(2), (1)(4)-prostaglandin J(2)-treated endothelial cells. Free Radic. Biol. Med. 52, 1844-1853.
    • (2012) Free Radic Biol Med , vol.52 , pp. 1844-1853
    • Lin, Y.C.1    Huang, G.D.2    Hsieh, C.W.3    Wung, B.S.4
  • 75
    • 0014422738 scopus 로고
    • An intracellular GSH-peroxidase with a lipid peroxide substrate
    • Little, C. and O'Brien, P.J. (1968). An intracellular GSH-peroxidase with a lipid peroxide substrate. Biochem. Biophys. Res. Commun. 31, 145-150.
    • (1968) Biochem. Biophys. Res. Commun , vol.31 , pp. 145-150
    • Little, C.1    O'Brien, P.J.2
  • 77
    • 54049150064 scopus 로고    scopus 로고
    • Modulation of methylglyoxal and glutathione by soybean isoflavones in mild streptozotocin-induced diabetic rats
    • Lu, M.P., Wang, R., Song, X., Wang, X., Wu, L., and Meng, Q.H. (2008). Modulation of methylglyoxal and glutathione by soybean isoflavones in mild streptozotocin-induced diabetic rats. Nutr. Metab. Cardiovasc. Dis. 18, 618-623.
    • (2008) Nutr. Metab. Cardiovasc. Dis , vol.18 , pp. 618-623
    • Lu, M.P.1    Wang, R.2    Song, X.3    Wang, X.4    Wu, L.5    Meng, Q.H.6
  • 78
    • 0033067354 scopus 로고    scopus 로고
    • Regulation of hepatic glutathione synthesis: Current concepts and controversies
    • Lu, S.C. (1999). Regulation of hepatic glutathione synthesis: current concepts and controversies. FASEB J. 13, 1169-1183. (Pubitemid 29300363)
    • (1999) FASEB Journal , vol.13 , Issue.10 , pp. 1169-1183
    • Lu, S.C.1
  • 79
    • 0026674198 scopus 로고
    • Insulin and glucocorticoid dependence of hepatic γ-glutamylcysteine synthetase and glutathione synthesis in the rat. Studies in cultured hepatocytes and in vivo
    • Lu, S.C., Ge, J.L., Kuhlenkamp, J., and Kaplowitz, N. (1992). Insulin and glucocorticoid dependence of hepatic γ-glutamylcysteine synthetase and glutathione synthesis in the rat. Studies in cultured hepatocytes and in vivo. J. Clin. Invest. 90, 524-532.
    • (1992) J. Clin. Invest , vol.90 , pp. 524-532
    • Lu, S.C.1    Ge, J.L.2    Kuhlenkamp, J.3    Kaplowitz, N.4
  • 83
    • 0016765005 scopus 로고
    • Reduction of disulphide bonds in proteins mixed disulphides catalysed by a thioltransferase in rat liver cytosol
    • Mannervik, B. and Axelsson, K. (1975). Reduction of disulphide bonds in proteins mixed disulphides catalysed by a thioltransferase in rat liver cytosol. Biochem. J. 149, 785-788.
    • (1975) Biochem. J , vol.149 , pp. 785-788
    • Mannervik, B.1    Axelsson, K.2
  • 84
    • 40449086667 scopus 로고    scopus 로고
    • Rapid detection, discovery, and identification of post-translationally myristoylated proteins during apoptosis using a bio-orthogonal azidomyristate analog
    • DOI 10.1096/fj.07-9198com
    • Martin, D.D., Vilas, G.L., Prescher, J.A., Rajaiah, G., Falck, J.R., Bertozzi, C.R., and Berthiaume, L.G. (2008). Rapid detection, discovery, and identification of post-translationally myristoylated proteins during apoptosis using a bio-orthogonal azidomyristate analog. FASEB J. 22, 797-806. (Pubitemid 351348132)
    • (2008) FASEB Journal , vol.22 , Issue.3 , pp. 797-806
    • Martin, D.D.O.1    Vilas, G.L.2    Prescher, J.A.3    Rajaiah, G.4    Falck, J.R.5    Bertozzi, C.R.6    Berthiaume, L.G.7
  • 85
    • 20444365814 scopus 로고    scopus 로고
    • Nitrosylation of thiols in vascular homeostasis and disease
    • Martinez-Ruiz, A. and Lamas, S. (2005). Nitrosylation of thiols in vascular homeostasis and disease. Curr. Atheroscler. Rep. 7, 213-218. (Pubitemid 40796754)
    • (2005) Current Atherosclerosis Reports , vol.7 , Issue.3 , pp. 213-218
    • Martinez-Ruiz, A.1    Lamas, S.2
  • 86
    • 34250738347 scopus 로고    scopus 로고
    • Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences
    • DOI 10.1016/j.cardiores.2007.03.016, PII S0008636307001411
    • Martinez-Ruiz, A. and Lamas, S. (2007). Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: convergences and divergences. Cardiovasc. Res. 75, 220-228. (Pubitemid 46970703)
    • (2007) Cardiovascular Research , vol.75 , Issue.2 , pp. 220-228
    • Martinez-Ruiz, A.1    Lamas, S.2
  • 90
    • 33645111448 scopus 로고    scopus 로고
    • Glutathione S-transferase polymorphisms: Cancer incidence and therapy
    • McIlwain, C.C., Townsend, D.M., and Tew, K.D. (2006). Glutathione S-transferase polymorphisms: cancer incidence and therapy. Oncogene 25, 1639-1648.
    • (2006) Oncogene , vol.25 , pp. 1639-1648
    • McIlwain, C.C.1    Townsend, D.M.2    Tew, K.D.3
  • 91
    • 0016231940 scopus 로고
    • The γ-glutamyl cycle. Diseases associated with specific enzyme deficiencies
    • Meister, A. (1974). The γ-glutamyl cycle. Diseases associated with specific enzyme deficiencies. Ann. Intern. Med. 81, 247-253.
    • (1974) Ann. Intern. Med , vol.81 , pp. 247-253
    • Meister, A.1
  • 92
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister, A. (1988). Glutathione metabolism and its selective modification. J. Biol. Chem. 263, 17205-17208. (Pubitemid 19029311)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.33 , pp. 17205-17208
    • Meister, A.1
  • 94
    • 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., and Shelton, M.D. (2008). Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid. Redox Signal. 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
  • 95
    • 70449174079 scopus 로고
    • Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown
    • Mills, G.C. (1957). Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. J. Biol. Chem. 229, 189-197.
    • (1957) J. Biol. Chem , vol.229 , pp. 189-197
    • Mills, G.C.1
  • 96
    • 84872687926 scopus 로고    scopus 로고
    • Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis
    • Morgan, B., Ezerina, D., Amoako, T.N., Riemer, J., Seedorf, M., and Dick, T.P. (2013). Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis. Nat. Chem. Biol. 9, 119-125.
    • (2013) Nat. Chem. Biol , vol.9 , pp. 119-125
    • Morgan, B.1    Ezerina, D.2    Amoako, T.N.3    Riemer, J.4    Seedorf, M.5    Dick, T.P.6
  • 97
    • 0031798883 scopus 로고    scopus 로고
    • Glutathione reverses the growth abnormalities of skin fibroblasts from insulin-dependent diabetic patients with nephropathy
    • Morocutti, A., Sethi, M., Hayward, A., Lee, A., and Viberti, G. (1998). Glutathione reverses the growth abnormalities of skin fibroblasts from insulin-dependent diabetic patients with nephropathy. J. Am. Soc. Nephrol. 9, 1060-1066. (Pubitemid 28264733)
    • (1998) Journal of the American Society of Nephrology , vol.9 , Issue.6 , pp. 1060-1066
    • Morocutti, A.1    Sethi, M.2    Hayward, A.3    Lee, A.4    Viberti, G.5
  • 99
    • 0346749513 scopus 로고    scopus 로고
    • Glutaredoxin Exerts an Antiapoptotic Effect by Regulating the Redox State of Akt
    • DOI 10.1074/jbc.M310171200
    • Murata, H., Ihara, Y., Nakamura, H., Yodoi, J., Sumikawa, K., and Kondo, T. (2003). Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt. J. Biol. Chem. 278, 50226-50233. (Pubitemid 37548863)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50226-50233
    • Murata, H.1    Ihara, Y.2    Nakamura, H.3    Yodoi, J.4    Sumikawa, K.5    Kondo, T.6
  • 100
    • 0034283810 scopus 로고    scopus 로고
    • Analysis of glutathionyl hemoglobin levels in diabetic patients by electrospray ionization liquid chromatography-mass spectrometry: Effect of vitamin e administration
    • Naito, C. and Niwa, T. (2000). Analysis of glutathionyl hemoglobin levels in diabetic patients by electrospray ionization liquid chromatography-mass spectrometry: effect of vitamin E administration. J. Chromatogr. B Biomed. Sci. Appl. 746, 91-94.
    • (2000) J. Chromatogr. B Biomed. Sci. Appl , vol.746 , pp. 91-94
    • Naito, C.1    Niwa, T.2
  • 101
    • 0032810171 scopus 로고    scopus 로고
    • Determination of glutathionyl hemoglobin in hemodialysis patients using electrospray ionization liquid chromatography-mass spectrometry
    • DOI 10.1016/S0378-4347(99)00139-5, PII S0378434799001395
    • Naito, C., Kajita, M., and Niwa, T. (1999). Determination of glutathionyl hemoglobin in hemodialysis patients using electrospray ionization liquid chromatography-mass spectrometry. J. Chromatogr. B Biomed. Sci. Appl. 731, 121-124. (Pubitemid 29376421)
    • (1999) Journal of Chromatography B: Biomedical Sciences and Applications , vol.731 , Issue.1 , pp. 121-124
    • Naito, C.1    Kajita, M.2    Niwa, T.3
  • 102
    • 0017355242 scopus 로고
    • Novel free radicals formed by the amino-carbonyl reactions of sugars with amino acids, amines, and proteins
    • Namiki, M., Hayashi, T., and Ohta, Y. (1977). Novel free radicals formed by the amino-carbonyl reactions of sugars with amino acids, amines, and proteins. Adv. Exp. Med. Biol. 86B, 471-501.
    • (1977) Adv. Exp. Med. Biol , vol.86 B , pp. 471-501
    • Namiki, M.1    Hayashi, T.2    Ohta, Y.3
  • 104
    • 0033952927 scopus 로고    scopus 로고
    • Increased glutathionyl hemoglobin in diabetes mellitus and hyperlipidemia demonstrated by liquid chromatography/electrospray ionization- mass spectrometry
    • Niwa, T., Naito, C., Mawjood, A.H., and Imai, K. (2000). Increased glutathionyl hemoglobin in diabetes mellitus and hyperlipidemia demonstrated by liquid chromatography/ electrospray ionization-mass spectrometry. Clin. Chem. 46, 82-88. (Pubitemid 30090963)
    • (2000) Clinical Chemistry , vol.46 , Issue.1 , pp. 82-88
    • Niwa, T.1    Naito, C.2    Mawjood, A.H.M.3    Imai, K.4
  • 105
    • 0037438946 scopus 로고    scopus 로고
    • Early oxidative stress in the diabetic kidney: Effect of DL-α-lipoic acid
    • DOI 10.1016/S0891-5849(02)01195-4, PII S0891584902011954
    • Obrosova, I.G., Fathallah, L., Liu, E., and Nourooz-Zadeh, J. (2003). Early oxidative stress in the diabetic kidney: effect of DL-α-lipoic acid. Free Radic. Biol. Med. 34, 186-195. (Pubitemid 36084322)
    • (2003) Free Radical Biology and Medicine , vol.34 , Issue.2 , pp. 186-195
    • Obrosova, I.G.1    Fathallah, L.2    Liu, E.3    Nourooz-Zadeh, J.4
  • 106
    • 33750734665 scopus 로고    scopus 로고
    • NRF2-dependent glutamate-L-cysteine ligase catalytic subunit expression mediates insulin protection against hyperglycemia-induced brain endothelial cell apoptosis
    • DOI 10.2174/156720206778792876
    • Okouchi, M., Okayama, N., Alexander, J.S., and Aw, T.Y. (2006). NRF2-dependent glutamate-L-cysteine ligase catalytic subunit expression mediates insulin protection against hyperglycemiainduced brain endothelial cell apoptosis. Curr. Neurovasc. Res. 3, 249-261. (Pubitemid 44706249)
    • (2006) Current Neurovascular Research , vol.3 , Issue.4 , pp. 249-261
    • Okouchi, M.1    Okayama, N.2    Alexander, J.S.3    Tak, Y.A.4
  • 108
    • 0036145348 scopus 로고    scopus 로고
    • Oxidative stress and nitric oxide synthase in rat diabetic nephropathy: Effects of ACEI and ARB
    • DOI 10.1046/j.1523-1755.2002.00123.x
    • Onozato, M.L., Tojo, A., Goto, A., Fujita, T., and Wilcox, C.S. (2002). Oxidative stress and nitric oxide synthase in rat diabetic nephropathy: effects of ACEI and ARB. Kidney Int. 61, 186-194. (Pubitemid 34075146)
    • (2002) Kidney International , vol.61 , Issue.1 , pp. 186-194
    • Onozato, M.L.1    Tojo, A.2    Goto, A.3    Fujita, T.4    Wilcox, C.S.5
  • 109
    • 0021099182 scopus 로고
    • The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates
    • Pai, E.F. and Schulz, G.E. (1983). The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates. J. Biol. Chem. 258, 1752-1757.
    • (1983) J. Biol. Chem , vol.258 , pp. 1752-1757
    • Pai, E.F.1    Schulz, G.E.2
  • 110
    • 33846809031 scopus 로고    scopus 로고
    • Glutathiolation regulates tumor necrosis factor-α-induced caspase-3 cleavage and apoptosis: Key role for glutaredoxin in the death pathway
    • DOI 10.1161/01.RES.0000256089.30318.20, PII 0000301220070202000008
    • Pan, S. and Berk, B.C. (2007). Glutathiolation regulates tumor necrosis factor-alpha-induced caspase-3 cleavage and apoptosis: key role for glutaredoxin in the death pathway. Circ. Res. 100, 213-219. (Pubitemid 46208721)
    • (2007) Circulation Research , vol.100 , Issue.2 , pp. 213-219
    • Pan, S.1    Berk, B.C.2
  • 114
    • 0035960648 scopus 로고    scopus 로고
    • Glutathionylation of the p50 subunit of NF-κB: A mechanism for redox-induced inhibition of DNA binding
    • DOI 10.1021/bi011459o
    • Pineda-Molina, E., Klatt, P., Vazquez, J., Marina, A., Garcia de Lacoba, M., Perez-Sala, D., and Lamas, S. (2001). Glutathionylation of the p50 subunit of NF-kappaB: a mechanism for redox-induced inhibition of DNA binding. Biochemistry 40, 14134-14142. (Pubitemid 33081616)
    • (2001) Biochemistry , vol.40 , Issue.47 , 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    Lamas, S.7
  • 115
    • 0033564203 scopus 로고    scopus 로고
    • Molecular basis of glutathione synthetase deficiency and a rare gene permutation event
    • DOI 10.1093/emboj/18.12.3204
    • Polekhina, G., Board, P.G., Gali, R.R., Rossjohn, J., and Parker, M.W. (1999). Molecular basis of glutathione synthetase deficiency and a rare gene permutation event. EMBO J. 18, 3204-3213. (Pubitemid 29276567)
    • (1999) EMBO Journal , vol.18 , Issue.12 , pp. 3204-3213
    • Polekhina, G.1    Board, P.G.2    Gali, R.R.3    Rossjohn, J.4    Parker, M.W.5
  • 116
    • 34547128886 scopus 로고    scopus 로고
    • Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFκB
    • DOI 10.1074/jbc.M610934200
    • Qanungo, S., Starke, D.W., Pai, H.V., Mieyal, J.J., and Nieminen, A.L. (2007). Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFkappaB. J. Biol. Chem. 282, 18427-18436. (Pubitemid 47100260)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.25 , pp. 18427-18436
    • Qanungo, S.1    Starke, D.W.2    Pai, H.V.3    Mieyal, J.J.4    Nieminen, A.-L.5
  • 117
    • 0034661024 scopus 로고    scopus 로고
    • Superoxides from mitochondrial complex III: The role of manganese superoxide dismutase
    • Raha, S., McEachern, G.E., Myint, A.T., and Robinson, B.H. (2000). Superoxides from mitochondrial complex III: the role of manganese superoxide dismutase. Free Radic. Biol. Med. 29, 170-180.
    • (2000) Free Radic. Biol. Med , vol.29 , pp. 170-180
    • Raha, S.1    McEachern, G.E.2    Myint, A.T.3    Robinson, B.H.4
  • 118
    • 0034964577 scopus 로고    scopus 로고
    • Long-term clinical outcome in patients with glutathione synthetase deficiency
    • DOI 10.1067/mpd.2001.114480
    • Ristoff, E., Mayatepek, E., and Larsson, A. (2001). Long-term clinical outcome in patients with glutathione synthetase deficiency. J. Pediatr. 139, 79-84. (Pubitemid 32613991)
    • (2001) Journal of Pediatrics , vol.139 , Issue.1 , pp. 79-84
    • Ristoff, E.1    Mayatepek, E.2    Larsson, A.3
  • 119
    • 78651477193 scopus 로고    scopus 로고
    • Glycated albumin, a precursor of advanced glycation end-products, up-regulates NADPH oxidase and enhances oxidative stress in human endothelial cells: Molecular correlate of diabetic vasculopathy
    • Rodino-Janeiro, B.K., Gonzalez-Peteiro, M., Ucieda-Somoza, R., Gonzalez-Juanatey, J.R., and Alvarez, E. (2010). Glycated albumin, a precursor of advanced glycation end-products, up-regulates NADPH oxidase and enhances oxidative stress in human endothelial cells: molecular correlate of diabetic vasculopathy. Diabetes Metab. Res. Rev. 26, 550-558.
    • (2010) Diabetes Metab. Res. Rev , vol.26 , pp. 550-558
    • Rodino-Janeiro, B.K.1    Gonzalez-Peteiro, M.2    Ucieda-Somoza, R.3    Gonzalez-Juanatey, J.R.4    Alvarez, E.5
  • 120
    • 0021087584 scopus 로고
    • Modelling cortical cataractogenesis: VI. Induction by glucose in vitro or in diabetic rats: Prevention and reversal by glutathione
    • Ross, W.M., Creighton, M.O., Trevithick, J.R., Stewart-DeHaan, P.J., and Sanwal, M. (1983). Modelling cortical cataractogenesis: VI. Induction by glucose in vitro or in diabetic rats: prevention and reversal by glutathione. Exp. Eye Res. 37, 559-573. (Pubitemid 14191828)
    • (1983) Experimental Eye Research , vol.37 , Issue.6 , pp. 559-573
    • Ross, W.M.1    Creighton, M.O.2    Trevithick, J.R.3
  • 121
    • 84856745322 scopus 로고    scopus 로고
    • Mechanisms of altered redox regulation in neurodegenerative diseases - Focus on S-glutathionylation
    • Sabens Liedhegner, E.A., Gao, X.H., and Mieyal, J.J. (2012). Mechanisms of altered redox regulation in neurodegenerative diseases - focus on S-glutathionylation. Antioxid. Redox Signal. 16, 543-566.
    • (2012) Antioxid. Redox Signal , vol.16 , pp. 543-566
    • Sabens Liedhegner, E.A.1    Gao, X.H.2    Mieyal, J.J.3
  • 123
    • 24944573462 scopus 로고    scopus 로고
    • Increased glutathionylated hemoglobin (HbSSG) in type 2 diabetes subjects with microangiopathy
    • DOI 10.1016/j.clinbiochem.2005.06.009, PII S0009912005001682
    • Sampathkumar, R., Balasubramanyam, M., Sudarslal, S., Rema, M., Mohan, V., and Balaram, P. (2005). Increased glutathionylated hemoglobin (HbSSG) in type 2 diabetes subjects with microangiopathy. Clin. Biochem. 38, 892-899. (Pubitemid 41319684)
    • (2005) Clinical Biochemistry , vol.38 , Issue.10 , pp. 892-899
    • Sampathkumar, R.1    Balasubramanyam, M.2    Sudarslal, S.3    Rema, M.4    Mohan, V.5    Balaram, P.6
  • 124
    • 0029088742 scopus 로고
    • Advanced glycation endproducts interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice. A potential mechanism for the accelerated vasculopathy of diabetes
    • Schmidt, A.M., Hori, O., Chen, J.X., Li, J.F., Crandall, J., Zhang, J., Cao, R., Yan, S.D., Brett, J., and Stern, D. (1995). Advanced glycation endproducts interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice. A potential mechanism for the accelerated vasculopathy of diabetes. J. Clin. Invest. 96, 1395-1403.
    • (1995) J. Clin. Invest , vol.96 , pp. 1395-1403
    • Schmidt, A.M.1    Hori, O.2    Chen, J.X.3    Li, J.F.4    Crandall, J.5    Zhang, J.6    Cao, R.7    Yan, S.D.8    Brett, J.9    Stern, D.10
  • 125
    • 80053425581 scopus 로고    scopus 로고
    • Vascular dysfunction in experimental diabetes is improved by pentaerithrityl tetranitrate but not isosorbide-5- mononitrate therapy
    • Schuhmacher, S., Oelze, M., Bollmann, F., Kleinert, H., Otto, C., Heeren, T., Steven, S., Hausding, M., Knorr, M., Pautz, A., et al. (2011). Vascular dysfunction in experimental diabetes is improved by pentaerithrityl tetranitrate but not isosorbide-5- mononitrate therapy. Diabetes 60, 2608-2616.
    • (2011) Diabetes , vol.60 , pp. 2608-2616
    • Schuhmacher, S.1    Oelze, M.2    Bollmann, F.3    Kleinert, H.4    Otto, C.5    Heeren, T.6    Steven, S.7    Hausding, M.8    Knorr, M.9    Pautz, A.10
  • 126
    • 0021149767 scopus 로고
    • Reversible dissociation of γ-glutamylcysteine synthetase into two subunits
    • Seelig, G.F., Simondsen, R.P., and Meister, A. (1984). Reversible dissociation of gamma-glutamylcysteine synthetase into two subunits. J. Biol. Chem. 259, 9345-9347. (Pubitemid 14060486)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.15 , pp. 9345-9347
    • Seelig, G.F.1    Simondsen, R.P.2    Meister, A.3
  • 127
    • 34250328361 scopus 로고    scopus 로고
    • Glutaredoxin regulates nuclear factor κ-B and intercellular adhesion molecule in Müller cells: Model of diabetic retinopathy
    • DOI 10.1074/jbc.M610863200
    • Shelton, M.D., Kern, T.S., and Mieyal, J.J. (2007). Glutaredoxin regulates nuclear factor kappa-B and intercellular adhesion molecule in Muller cells: model of diabetic retinopathy. J. Biol. Chem. 282, 12467-12474. (Pubitemid 47100623)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 12467-12474
    • Shelton, M.D.1    Kern, T.S.2    Mieyal, J.J.3
  • 128
    • 64149130388 scopus 로고    scopus 로고
    • Glutaredoxin regulates autocrine and paracrine proinflammatory responses in retinal glial (Muller) cells
    • Shelton, M.D., Distler, A.M., Kern, T.S., and Mieyal, J.J. (2009). Glutaredoxin regulates autocrine and paracrine proinflammatory responses in retinal glial (Muller) cells. J. Biol. Chem. 284, 4760-4766.
    • (2009) J. Biol. Chem , vol.284 , pp. 4760-4766
    • Shelton, M.D.1    Distler, A.M.2    Kern, T.S.3    Mieyal, J.J.4
  • 129
    • 34848892187 scopus 로고    scopus 로고
    • Reactive nitrogen species induced by hyperglycemia suppresses Akt signaling and triggers apoptosis by upregulating phosphatase PTEN (phosphatase and tensin homologue deleted on chromosome 10) in an LKB1-dependent manner
    • DOI 10.1161/CIRCULATIONAHA.107.716498
    • Song, P., Wu, Y., Xu, J., Xie, Z., Dong, Y., Zhang, M., and Zou, M.H. (2007). Reactive nitrogen species induced by hyperglycemia suppresses Akt signaling and triggers apoptosis by upregulating phosphatase PTEN (phosphatase and tensin homologue deleted on chromosome 10) in an LKB1-dependent manner. Circulation 116, 1585-1595. (Pubitemid 47511422)
    • (2007) Circulation , vol.116 , Issue.14 , pp. 1585-1595
    • Song, P.1    Wu, Y.2    Xu, J.3    Xie, Z.4    Dong, Y.5    Zhang, M.6    Zou, M.-H.7
  • 130
    • 0017852992 scopus 로고
    • Biochemical heterogeneity in glutathione synthetase deficiency
    • Spielberg, S.P., Garrick, M.D., Corash, L.M., Butler, J.D., Tietze, F., Rogers, L., and Schulman, J.D. (1978). Biochemical heterogeneity in glutathione synthetase deficiency. J. Clin. Invest. 61, 1417-1420. (Pubitemid 8361866)
    • (1978) Journal of Clinical Investigation , vol.61 , Issue.6 , pp. 1417-1420
    • Spielberg, S.P.1    Garrick, M.D.2    Corash, L.M.3
  • 131
    • 0038015010 scopus 로고    scopus 로고
    • Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase): Potential role in redox signal transduction
    • DOI 10.1074/jbc.M210434200
    • Starke, D.W., Chock, P.B., and Mieyal, J.J. (2003). Glutathionethiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction. J. Biol. Chem. 278, 14607-14613. (Pubitemid 36799782)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.17 , pp. 14607-14613
    • Starke, D.W.1    Chock, P.B.2    Mieyal, J.J.3
  • 132
    • 52149112705 scopus 로고    scopus 로고
    • Gene-environment interaction and oxidative stress in cardiovascular disease
    • Stephens, J.W., Bain, S.C., and Humphries, S.E. (2008). Gene-environment interaction and oxidative stress in cardiovascular disease. Atherosclerosis 200, 229-238.
    • (2008) Atherosclerosis , vol.200 , pp. 229-238
    • Stephens, J.W.1    Bain, S.C.2    Humphries, S.E.3
  • 134
    • 0029848066 scopus 로고    scopus 로고
    • Regulation of γ-glutamylcysteine synthetase by protein phosphorylation
    • Sun, W.M., Huang, Z.Z., and Lu, S.C. (1996). Regulation of gammaglutamylcysteine synthetase by protein phosphorylation. Biochem. J. 320, 321-328. (Pubitemid 26400197)
    • (1996) Biochemical Journal , vol.320 , Issue.1 , pp. 321-328
    • Sun, W.-M.1    Huang, Z.-Z.2    Lu, S.C.3
  • 135
    • 0026669169 scopus 로고
    • Effect of insulin on impaired antioxidant activities in aortic endothelial cells from diabetic rabbits
    • Tagami, S., Kondo, T., Yoshida, K., Hirokawa, J., Ohtsuka, Y., and Kawakami, Y. (1992). Effect of insulin on impaired antioxidant activities in aortic endothelial cells from diabetic rabbits. Metabolism 41, 1053-1058.
    • (1992) Metabolism , vol.41 , pp. 1053-1058
    • Tagami, S.1    Kondo, T.2    Yoshida, K.3    Hirokawa, J.4    Ohtsuka, Y.5    Kawakami, Y.6
  • 136
    • 77649131958 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein-activated c-Jun NH2-terminal kinase regulates manganese superoxide dismutase ubiquitination: Implication for mitochondrial redox status and apoptosis
    • Takabe, W., Li, R., Ai, L., Yu, F., Berliner, J.A., and Hsiai, T.K. (2010). Oxidized low-density lipoprotein-activated c-Jun NH2-terminal kinase regulates manganese superoxide dismutase ubiquitination: implication for mitochondrial redox status and apoptosis. Arterioscler Thromb. Vasc. Biol. 30, 436-441.
    • (2010) Arterioscler Thromb. Vasc. Biol , vol.30 , pp. 436-441
    • Takabe, W.1    Li, R.2    Ai, L.3    Yu, F.4    Berliner, J.A.5    Hsiai, T.K.6
  • 137
    • 0019888435 scopus 로고
    • Gamma-Glutamyl transpeptidase: Catalytic, structural and functional aspects
    • Tate, S.S. and Meister, A. (1981). gamma-Glutamyl transpeptidase: catalytic, structural and functional aspects. Mol. Cell. Biochem. 39, 357-368.
    • (1981) Mol. Cell. Biochem , vol.39 , pp. 357-368
    • Tate, S.S.1    Meister, A.2
  • 138
    • 0021361665 scopus 로고
    • The autoxidation of glyceraldehyde and other simple monosaccharides under physiological conditions catalysed by buffer ions
    • DOI 10.1016/0304-4165(84)90131-4
    • Thornalley, P., Wolff, S., Crabbe, J., and Stern, A. (1984). The autoxidation of glyceraldehyde and other simple monosaccharides under physiological conditions catalysed by buffer ions. Biochim. Biophys. Acta. 797, 276-287. (Pubitemid 14197639)
    • (1984) Biochimica et Biophysica Acta - General Subjects , vol.797 , Issue.2 , pp. 276-287
    • Thornalley, P.1    Wolff, S.2    Crabbe, J.3    Stern, A.4
  • 139
    • 0038199726 scopus 로고    scopus 로고
    • PTP1B: From the sidelines to the front lines!
    • DOI 10.1016/S0014-5793(03)00603-3
    • Tonks, N.K. (2003). PTP1B: from the sidelines to the front lines! FEBS Lett. 546, 140-148. (Pubitemid 36782295)
    • (2003) FEBS Letters , vol.546 , Issue.1 , pp. 140-148
    • Tonks, N.K.1
  • 140
    • 4544226082 scopus 로고    scopus 로고
    • Generation of reactive oxygen species in the reaction catalyzed by α-ketoglutarate dehydrogenase
    • DOI 10.1523/JNEUROSCI.1842-04.2004
    • Tretter, L. and Adam-Vizi, V. (2004). Generation of reactive oxygen species in the reaction catalyzed by α-ketoglutarate dehydrogenase. J. Neurosci. 24, 7771-7778. (Pubitemid 39215680)
    • (2004) Journal of Neuroscience , vol.24 , Issue.36 , pp. 7771-7778
    • Tretter, L.1    Adam-Vizi, V.2
  • 142
    • 0028297696 scopus 로고
    • Activation of the Ras/mitogen-activated protein kinase signaling pathway alone is not sufficient to induce glucose uptake in 3T3-L1 adipocytes
    • van den Berghe, N., Ouwens, D.M., Maassen, J.A., van Mackelenbergh, M.G., Sips, H.C., and Krans, H.M. (1994). Activation of the Ras/mitogen-activated protein kinase signaling pathway alone is not sufficient to induce glucose uptake in 3T3-L1 adipocytes. Mol. Cell. Biol. 14, 2372-2377. (Pubitemid 24108219)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.4 , pp. 2372-2377
    • Van Den Berghe, N.1    Ouwens, D.M.2    Maassen, J.A.3    Van Mackelenbergh, M.G.H.4    Sips, H.C.M.5    Krans, H.M.J.6
  • 143
    • 0019730109 scopus 로고
    • γ-Glutamyltranspeptidase: A tumor cell marker with a pharmacological function
    • Vanderlaan, M. and Phares, W. (1981). γ-Glutamyltranspeptidase: a tumour cell marker with a pharmacological function. Histochem. J. 13, 865-877. (Pubitemid 12176654)
    • (1981) Histochemical Journal , vol.13 , Issue.5 , pp. 865-877
    • Vanderlaan, M.1    Phares, W.2
  • 144
    • 0039174315 scopus 로고    scopus 로고
    • Mitochondrial aconitase is a source of hydroxyl radical. An electron spin resonance investigation
    • DOI 10.1074/jbc.275.19.14064
    • Vasquez-Vivar, J., Kalyanaraman, B., and Kennedy, M.C. (2000). Mitochondrial aconitase is a source of hydroxyl radical. An electron spin resonance investigation. J. Biol. Chem. 275, 14064-14069. (Pubitemid 30339680)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.19 , pp. 14064-14069
    • Vasquez-Vivar, J.1    Kalyanaraman, B.2    Kennedy, M.C.3
  • 145
    • 0032493812 scopus 로고    scopus 로고
    • Increasing complexity of the Ras signaling pathway
    • DOI 10.1074/jbc.273.32.19925
    • Vojtek, A.B. and Der, C.J. (1998). Increasing complexity of the Ras signaling pathway. J. Biol. Chem. 273, 19925-19928. (Pubitemid 28377538)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.32 , pp. 19925-19928
    • Vojtek, A.B.1    Der, C.J.2
  • 146
    • 34249309215 scopus 로고    scopus 로고
    • Glutaredoxin mediates Akt and eNOS activation by flow in a glutathione reductase-dependent manner
    • DOI 10.1161/ATVBAHA.107.144659
    • Wang, J., Pan, S., and Berk, B.C. (2007). Glutaredoxin mediates Akt and eNOS activation by flow in a glutathione reductasedependent manner. Arterioscler. Thromb. Vasc. Biol. 27, 1283-1288. (Pubitemid 46809416)
    • (2007) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.27 , Issue.6 , pp. 1283-1288
    • Wang, J.1    Pan, S.2    Berk, B.C.3
  • 149
    • 0033584867 scopus 로고    scopus 로고
    • Regulation of γ-glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2
    • Wild, A.C., Moinova, H.R., and Mulcahy, R.T. (1999). Regulation of γ-glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2. J. Biol. Chem. 274, 33627-33636. (Pubitemid 129511675)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.47 , pp. 33627-33636
    • Wild, A.C.1    Moinova, H.R.2    Mulcahy, R.T.3
  • 150
    • 2342466734 scopus 로고    scopus 로고
    • Global Prevalence of Diabetes: Estimates for the year 2000 and projections for 2030
    • DOI 10.2337/diacare.27.5.1047
    • Wild, S., Roglic, G., Green, A., Sicree, R., and King, H. (2004). Global prevalence of diabetes: estimates for the year 2000 and projections for 2030. Diabetes Care 27, 1047-1053. (Pubitemid 38579764)
    • (2004) Diabetes Care , vol.27 , Issue.5 , pp. 1047-1053
    • Wild, S.1    Roglic, G.2    Green, A.3    Sicree, R.4    King, H.5
  • 151
    • 0030789179 scopus 로고    scopus 로고
    • The level of intracellular glutathione is a key regulator for the induction of stress-activated signal transduction pathways including Jun N- terminal protein kinases and p38 kinase by alkylating agents
    • Wilhelm, D., Bender, K., Knebel, A., and Angel, P. (1997). The level of intracellular glutathione is a key regulator for the induction of stress-activated signal transduction pathways including Jun N-terminal protein kinases and p38 kinase by alkylating agents. Mol. Cell. Biol. 17, 4792-4800. (Pubitemid 27318154)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.8 , pp. 4792-4800
    • Wilhelm, D.1    Bender, K.2    Knebel, A.3    Angel, P.4
  • 152
    • 0001855256 scopus 로고
    • Flavin-containing dehydrogenases
    • P.D. Boyer, 3rd ed. Chapter 3.IV (New York: Academic Press)
    • Williams, C.H., Jr. (1976). Flavin-containing dehydrogenases. In: The enzymes, P.D. Boyer, 3rd ed. Chapter 3.IV (New York: Academic Press), pp. 129-142.
    • (1976) The Enzymes , pp. 129-142
    • Williams Jr., C.H.1
  • 153
    • 0023259759 scopus 로고
    • Glucose autoxidation and protein modification. The potential role of 'autoxidative glycosylation' in diabetes
    • Wolff, S.P. and Dean, R.T. (1987). Glucose autoxidation and protein modification. The potential role of 'autoxidative glycosylation' in diabetes. Biochem. J. 245, 243-250. (Pubitemid 17089839)
    • (1987) Biochemical Journal , vol.245 , Issue.1 , pp. 243-250
    • Wolff, S.P.1    Dean, R.T.2
  • 154
    • 21944452087 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 regulate rat glutamate-cysteine ligase catalytic subunit transcription indirectly via NF-κB and AP-1
    • DOI 10.1128/MCB.25.14.5933-5946.2005
    • Yang, H., Magilnick, N., Lee, C., Kalmaz, D., Ou, X., Chan, J.Y., and Lu, S.C. (2005). Nrf1 and Nrf2 regulate rat glutamate-cysteine ligase catalytic subunit transcription indirectly via NF-κB and AP-1. Mol. Cell. Biol. 25, 5933-5946. (Pubitemid 40949988)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.14 , pp. 5933-5946
    • Yang, H.1    Magilnick, N.2    Lee, C.3    Kalmaz, D.4    Ou, X.5    Chan, J.Y.6    Lu, S.C.7
  • 155
    • 0033037930 scopus 로고    scopus 로고
    • Hyperglycemia-induced activation of nuclear transcription factor κB in vascular smooth muscle cells
    • Yerneni, K.K., Bai, W., Khan, B.V., Medford, R.M., and Natarajan, R. (1999). Hyperglycemia-induced activation of nuclear transcription factor κB in vascular smooth muscle cells. Diabetes 48, 855-864. (Pubitemid 29153087)
    • (1999) Diabetes , vol.48 , Issue.4 , pp. 855-864
    • Yerneni, K.K.V.1    Bai, W.2    Khan, B.V.3    Medford, R.M.4    Natarajan, R.5
  • 156
    • 33845984333 scopus 로고    scopus 로고
    • Epidemic obesity and type 2 diabetes in Asia
    • DOI 10.1016/S0140-6736(06)69703-1, PII S0140673606697031
    • Yoon, K.H., Lee, J.H., Kim, J.W., Cho, J.H., Choi, Y.H., Ko, S.H., Zimmet, P., and Son, H.Y. (2006). Epidemic obesity and type 2 diabetes in Asia. Lancet 368, 1681-1688. (Pubitemid 46048556)
    • (2006) Lancet , vol.368 , Issue.9548 , pp. 1681-1688
    • Yoon, K.-H.1    Lee, J.-H.2    Kim, J.-W.3    Cho, J.H.4    Choi, Y.-H.5    Ko, S.-H.6    Zimmet, P.7    Son, H.-Y.8
  • 157
    • 0028037601 scopus 로고
    • Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins
    • Yoshitake, S., Nanri, H., Fernando, M.R., and Minakami, S. (1994). Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins. J. Biochem. 116, 42-46. (Pubitemid 24230780)
    • (1994) Journal of Biochemistry , vol.116 , Issue.1 , pp. 42-46
    • Yoshitake, S.1    Nanri, H.2    Fernando, M.R.3    Minakami, S.4
  • 158
    • 30344481701 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase in glutathione biosynthesis
    • Zhang, H., Forman, H.J., and Choi, J. (2005). Gamma-glutamyl transpeptidase in glutathione biosynthesis. Methods Enzymol. 401, 468-483.
    • (2005) Methods Enzymol , vol.401 , pp. 468-483
    • Zhang, H.1    Forman, H.J.2    Choi, J.3
  • 159
    • 69249099667 scopus 로고    scopus 로고
    • S-glutathionylation of the Rpn2 regulatory subunit inhibits 26 S proteasomal function
    • Zmijewski, J.W., Banerjee, S., and Abraham, E. (2009). S-glutathionylation of the Rpn2 regulatory subunit inhibits 26 S proteasomal function. J. Biol. Chem. 284, 22213-22221.
    • (2009) J. Biol. Chem , vol.284 , pp. 22213-22221
    • Zmijewski, J.W.1    Banerjee, S.2    Abraham, E.3


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