메뉴 건너뛰기




Volumn 19, Issue 9, 2006, Pages 1196-1204

Ebselen, a seleno-organic antioxidant, as an electrophile

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; EBSELEN; GLUTATHIONE PEROXIDASE; ORGANOSELENIUM DERIVATIVE; PROTEIN KEAP1; REACTIVE OXYGEN METABOLITE; THIOREDOXIN; TRANSCRIPTION FACTOR NF E2; UNCLASSIFIED DRUG;

EID: 33749000604     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx0601105     Document Type: Article
Times cited : (131)

References (52)
  • 1
    • 0021185122 scopus 로고
    • A novel biologically active seleno-organic compound-I. Glutathione peroxidase-like activity in vitro and antioxidant capacity of PZ 51 (Ebselen)
    • Muller, A., Cadenas, E., Graf, P., and Sies, H. (1984) A novel biologically active seleno-organic compound-I. Glutathione peroxidase-like activity in vitro and antioxidant capacity of PZ 51 (Ebselen). Biochem. Pharmacol. 33, 3235-3239.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 3235-3239
    • Muller, A.1    Cadenas, E.2    Graf, P.3    Sies, H.4
  • 2
    • 0021135344 scopus 로고
    • A novel biologically active seleno-organic compound-II. Activity of PZ 51 in relation to glutathione peroxidase
    • Wendel, A., Fausel, M., Safayhi, H., Tiegs, G., and Otter, R. (1984) A novel biologically active seleno-organic compound-II. Activity of PZ 51 in relation to glutathione peroxidase. Biochem. Pharmacol. 33, 3241-3245.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 3241-3245
    • Wendel, A.1    Fausel, M.2    Safayhi, H.3    Tiegs, G.4    Otter, R.5
  • 3
    • 0011869643 scopus 로고    scopus 로고
    • Ebselen as a glutathione peroxidase mimic and as a scavenger of peroxynitrite
    • Sies, H., and Masumoto, H. (1997) Ebselen as a glutathione peroxidase mimic and as a scavenger of peroxynitrite. Adv. Pharmacol. 38, 229-246.
    • (1997) Adv. Pharmacol. , vol.38 , pp. 229-246
    • Sies, H.1    Masumoto, H.2
  • 4
    • 0037131424 scopus 로고    scopus 로고
    • A novel antioxidant mechanism of ebselen involving ebselen diselenide, a substrate of mammalian thioredoxin and thioredoxin reductase
    • Zhao, R., and Holmgren, A. (2002) A novel antioxidant mechanism of ebselen involving ebselen diselenide, a substrate of mammalian thioredoxin and thioredoxin reductase. J. Biol. Chem. 277, 39456-39462.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39456-39462
    • Zhao, R.1    Holmgren, A.2
  • 5
    • 0029114721 scopus 로고
    • Molecular actions of ebselen-an antiinflammatory antioxidant
    • Schewe, T. (1995) Molecular actions of ebselen-an antiinflammatory antioxidant. Gen. Pharmcol. 26, 1153-1169.
    • (1995) Gen. Pharmcol. , vol.26 , pp. 1153-1169
    • Schewe, T.1
  • 7
    • 0034821411 scopus 로고    scopus 로고
    • Ebselen protects both gray and white matter in a rodent model of focal cerebral ischemia
    • Imai, H., Masayasu, H., Dewar, D., Graham, D. I., and Macrae, I. M. (2001) Ebselen protects both gray and white matter in a rodent model of focal cerebral ischemia. Stroke (Dallas) 32, 2149-2154.
    • (2001) Stroke (Dallas) , vol.32 , pp. 2149-2154
    • Imai, H.1    Masayasu, H.2    Dewar, D.3    Graham, D.I.4    Macrae, I.M.5
  • 8
    • 0034884323 scopus 로고    scopus 로고
    • Ebselen reduces cytochrome c release from mitochondria and subsequent DNA fragmentation after transient focal cerebral ischemia in mice
    • Namura, S., Nagata, I., Takami, S., Masayasu, H., and Kikuchi, H. (2001) Ebselen reduces cytochrome c release from mitochondria and subsequent DNA fragmentation after transient focal cerebral ischemia in mice. Stroke (Dallas) 32, 1906-1911.
    • (2001) Stroke (Dallas) , vol.32 , pp. 1906-1911
    • Namura, S.1    Nagata, I.2    Takami, S.3    Masayasu, H.4    Kikuchi, H.5
  • 9
    • 0037169525 scopus 로고    scopus 로고
    • Ebselen, a glutathione peroxidase mimetic seleno-organic compound, as a multifunctional antioxidant. Implication for inflammation-associated carcinogenesis
    • Nakamura, Y., Feng, Q., Kumagai, T., Torikai, K., Ohigashi, H., Osawa, T., Noguchi, N., Niki, E., and Uchida, K. (2002) Ebselen, a glutathione peroxidase mimetic seleno-organic compound, as a multifunctional antioxidant. Implication for inflammation-associated carcinogenesis. J. Biol. Chem. 277, 2687-2694.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2687-2694
    • Nakamura, Y.1    Feng, Q.2    Kumagai, T.3    Torikai, K.4    Ohigashi, H.5    Osawa, T.6    Noguchi, N.7    Niki, E.8    Uchida, K.9
  • 10
    • 0031963836 scopus 로고    scopus 로고
    • Ebselen in acute ischemic stroke: A placebo-controlled, double-blind clinical trial
    • Ebselen Study Group
    • Yamaguchi, T., Sano, K., Takakura, K., Saito, I., Shinohara, Y., Asano, T., and Yasuhara, H. (1998) Ebselen in acute ischemic stroke: A placebo-controlled, double-blind clinical trial. Ebselen Study Group. Stroke (Dallas) 29, 12-17.
    • (1998) Stroke (Dallas) , vol.29 , pp. 12-17
    • Yamaguchi, T.1    Sano, K.2    Takakura, K.3    Saito, I.4    Shinohara, Y.5    Asano, T.6    Yasuhara, H.7
  • 11
    • 0033042957 scopus 로고    scopus 로고
    • Ebselen in acute middle cerebral artery occlusion: A placebo-controlled, double-blind clinical trial
    • Ogawa, A., Yoshimoto, T., Kikuchi, H., Sano, K., Saito, I., Yamaguchi, T., and Yasuhara, H. (1999) Ebselen in acute middle cerebral artery occlusion: A placebo-controlled, double-blind clinical trial. Cereb. Dis. 9, 112-118.
    • (1999) Cereb. Dis. , vol.9 , pp. 112-118
    • Ogawa, A.1    Yoshimoto, T.2    Kikuchi, H.3    Sano, K.4    Saito, I.5    Yamaguchi, T.6    Yasuhara, H.7
  • 12
    • 0031886421 scopus 로고    scopus 로고
    • Neuroprotective effect of an antioxidant, ebselen, in patients with delayed neurological deficits after aneurysmal subarachnoid hemorrhage
    • Saito, I., Asano, T., Sano, K., Takakura, K., Abe, H., Yoshimoto, T., Kikuchi, H., Ohta, T.. and Ishibashi, S. (1998) Neuroprotective effect of an antioxidant, ebselen, in patients with delayed neurological deficits after aneurysmal subarachnoid hemorrhage. Neurosurgery 42, 269-278.
    • (1998) Neurosurgery , vol.42 , pp. 269-278
    • Saito, I.1    Asano, T.2    Sano, K.3    Takakura, K.4    Abe, H.5    Yoshimoto, T.6    Kikuchi, H.7    Ohta, T.8    Ishibashi, S.9
  • 13
    • 0344915418 scopus 로고
    • Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis
    • Talalay, P., De Long, M. J., and Prochaska, H. J. (1988) Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis. Proc. Natl. Acad. Sci. U.S.A. 85, 8261-8265.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 8261-8265
    • Talalay, P.1    De Long, M.J.2    Prochaska, H.J.3
  • 14
    • 0026022976 scopus 로고
    • The potency of inducers of NAD(P)H:(quinone-acceptor) oxidoreductase parallels their efficiency as substrates for glutathione transferases. Structural and electronic correlations
    • Spencer, S. R., Xue, L., Klenz, E. M., and Talalay, P. (1991) The potency of inducers of NAD(P)H:(quinone-acceptor) oxidoreductase parallels their efficiency as substrates for glutathione transferases. Structural and electronic correlations. Biochem. J. 273, 711-717.
    • (1991) Biochem. J. , vol.273 , pp. 711-717
    • Spencer, S.R.1    Xue, L.2    Klenz, E.M.3    Talalay, P.4
  • 16
    • 0025368036 scopus 로고
    • Regulation of glutathione S-transferase Ya subunit gene expression: Identification of a unique xenobiotic-responsive element controlling inducible expression by planar aromatic compounds
    • Rushmore, T. H., King, R. G., Paulson, K. E., and Pickett, C. B. (1990) Regulation of glutathione S-transferase Ya subunit gene expression: Identification of a unique xenobiotic-responsive element controlling inducible expression by planar aromatic compounds. Proc. Natl. Acad. Sci. U.S.A. 87, 3826-3830.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3826-3830
    • Rushmore, T.H.1    King, R.G.2    Paulson, K.E.3    Pickett, C.B.4
  • 17
    • 0025145723 scopus 로고
    • Xenobiotic-inducible expression of murine glutathione S-transferase Ya subunit gene is controlled by an electrophile-responsive element
    • Friling, R. S., Bensimon, A., Tichauer, T., and Daniel, V. (1990) Xenobiotic-inducible expression of murine glutathione S-transferase Ya subunit gene is controlled by an electrophile-responsive element. Proc. Natl. Acad. Sci. U.S.A. 87, 6258-6262.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6258-6262
    • Friling, R.S.1    Bensimon, A.2    Tichauer, T.3    Daniel, V.4
  • 18
    • 0028947208 scopus 로고
    • cDNA cloning of murine Nrf 2 gene, coding for a p45 NF-E2 related transcription factor
    • Chui, D. H., Tang, W., and Orkin, S. H. (1995) cDNA cloning of murine Nrf 2 gene, coding for a p45 NF-E2 related transcription factor. Biochem. Biophys. Res. Commun. 209, 40-46.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 40-46
    • Chui, D.H.1    Tang, W.2    Orkin, S.H.3
  • 20
    • 0029906134 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase 1 gene
    • Venugopal, R., and Jaiswal, A. K. (1996) Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase 1 gene. Proc. Natl. Acad. Sci. U.S.A. 93, 14960-14965.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 14960-14965
    • Venugopal, R.1    Jaiswal, A.K.2
  • 21
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the aminoterminal Neh2 domain
    • Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., and Yamamoto, M. (1999) Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the aminoterminal Neh2 domain. Genes Dev. 13, 76-86.
    • (1999) Genes Dev. , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 22
    • 12444257799 scopus 로고    scopus 로고
    • Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles
    • Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., O'Connor, T., and Yamamoto, M. (2003) Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles. Genes Cells 8, 379-391.
    • (2003) Genes Cells , vol.8 , pp. 379-391
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    O'Connor, T.5    Yamamoto, M.6
  • 23
    • 0037821802 scopus 로고    scopus 로고
    • Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression
    • McMahon, M., Itoh, K., Yamamoto, M., and Hayes, J. D. (2003) Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression. J. Biol. Chem. 278, 21592-21600.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21592-21600
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Hayes, J.D.4
  • 24
    • 0013282861 scopus 로고    scopus 로고
    • Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element. Degradation of Nrf2 by the 26 S proteasome
    • Nguyen, T., Sherratt, P. J., Huang, H. C., Yang, C. S., and Pickett, C. B. (2003) Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element. Degradation of Nrf2 by the 26 S proteasome. J. Biol. Chem. 278, 4536-4541.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4536-4541
    • Nguyen, T.1    Sherratt, P.J.2    Huang, H.C.3    Yang, C.S.4    Pickett, C.B.5
  • 25
    • 0037015682 scopus 로고    scopus 로고
    • Nrf2 degradation by the ubiquitin proteasome pathway is inhibited by KIAA0132, the human homolog to INrf2
    • Sekhar, K. R., Yan, X. X., and Freeman, M. L. (2002) Nrf2 degradation by the ubiquitin proteasome pathway is inhibited by KIAA0132, the human homolog to INrf2. Oncogene 21, 6829-6834.
    • (2002) Oncogene , vol.21 , pp. 6829-6834
    • Sekhar, K.R.1    Yan, X.X.2    Freeman, M.L.3
  • 26
    • 0037462651 scopus 로고    scopus 로고
    • Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium
    • Stewart, D., Killeen, E., Naquin, R., Alam, S., and Alam, J. (2003) Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium. J. Biol. Chem. 278, 2396-2402.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2396-2402
    • Stewart, D.1    Killeen, E.2    Naquin, R.3    Alam, S.4    Alam, J.5
  • 28
    • 0242580049 scopus 로고    scopus 로고
    • Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress
    • Zhang, D. D., and Hannink, M. (2003) Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol. Cell. Biol. 23, 8137-8151.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8137-8151
    • Zhang, D.D.1    Hannink, M.2
  • 29
    • 22544464124 scopus 로고    scopus 로고
    • Modifying specific cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2
    • Eggler, A. L., Liu, G., Pezzuto, J. M., van Breemen, R. B., and Mesecar, A. D. (2005) Modifying specific cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2. Proc. Natl. Acad. Sci. U.S.A. 102, 10070-10075.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 10070-10075
    • Eggler, A.L.1    Liu, G.2    Pezzuto, J.M.3    Van Breemen, R.B.4    Mesecar, A.D.5
  • 30
    • 0037155862 scopus 로고    scopus 로고
    • Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion
    • Eaton, P., Byers, H. L., Leeds, N., Ward, M. A., and Shattock, M. J. (2002) Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. J. Biol. Chem. 277, 9806-9811.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9806-9811
    • Eaton, P.1    Byers, H.L.2    Leeds, N.3    Ward, M.A.4    Shattock, M.J.5
  • 31
    • 0037044782 scopus 로고    scopus 로고
    • Regulation of cAMP-dependent protein kinase activity by glutathionylation
    • Humphries, R. M., Juliano, C., and Taylor, S. S. (2002) Regulation of cAMP-dependent protein kinase activity by glutathionylation. J. Biol. Chem. 277, 43505-43511.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43505-43511
    • Humphries, R.M.1    Juliano, C.2    Taylor, S.S.3
  • 32
    • 0000658566 scopus 로고
    • Sorbic acid iron tricarbonyl complex as resolving agent. Chiral synthesis of 4-hydroxynonenal and coriolic acid
    • De Montarby, L., Mosset, P., and Gree, R. (1988) Sorbic acid iron tricarbonyl complex as resolving agent. Chiral synthesis of 4-hydroxynonenal and coriolic acid. Tetrahedron Lett. 29, 3895.
    • (1988) Tetrahedron Lett. , vol.29 , pp. 3895
    • De Montarby, L.1    Mosset, P.2    Gree, R.3
  • 34
    • 1242274394 scopus 로고    scopus 로고
    • Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes
    • Kang, M. I., Robayashi, A., Wakabayashi, N., Kim, S. G., and Yamamoto, M. (2004) Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes. Proc. Natl. Acad. Sci. U.S.A. 101, 2046-2051.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2046-2051
    • Kang, M.I.1    Robayashi, A.2    Wakabayashi, N.3    Kim, S.G.4    Yamamoto, M.5
  • 35
    • 0034717329 scopus 로고    scopus 로고
    • Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages
    • Ishii, T., Itoh, K., Takahashi, S., Sato, H., Yanagawa, T., Katoh, Y., Bannai, S., and Yamamoto, M. (2000) Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages. J. Biol. Chem. 275, 16023-16029.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16023-16029
    • Ishii, T.1    Itoh, K.2    Takahashi, S.3    Sato, H.4    Yanagawa, T.5    Katoh, Y.6    Bannai, S.7    Yamamoto, M.8
  • 36
    • 0037015035 scopus 로고    scopus 로고
    • Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
    • Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., and Talalay, P. (2002) Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc. Natl. Acad. Sci. U.S.A. 99, 11908-11913.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11908-11913
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Cole, R.N.3    Itoh, K.4    Wakabayashi, N.5    Katoh, Y.6    Yamamoto, M.7    Talalay, P.8
  • 37
    • 0030824455 scopus 로고    scopus 로고
    • Alpha particles initiate biological production of superoxide anions and hydrogen peroxide in human cells
    • Narayanan, P. K., Goodwin, E. H., and Lehnert, B. E. (1997) Alpha particles initiate biological production of superoxide anions and hydrogen peroxide in human cells. Cancer Res. 57, 3963-3971.
    • (1997) Cancer Res. , vol.57 , pp. 3963-3971
    • Narayanan, P.K.1    Goodwin, E.H.2    Lehnert, B.E.3
  • 38
    • 0025218905 scopus 로고
    • Flow cytometric analysis of respiratory burst activity in phagocytes with hydroethidine and 2,7′-dichlorofluorescin
    • Rothe, G., and Valet, G. (1990) Flow cytometric analysis of respiratory burst activity in phagocytes with hydroethidine and 2,7′- dichlorofluorescin. J. Leukocyte Biol. 47, 440-448.
    • (1990) J. Leukocyte Biol. , vol.47 , pp. 440-448
    • Rothe, G.1    Valet, G.2
  • 40
    • 0033593225 scopus 로고    scopus 로고
    • Activation of stress signaling pathways by the end product of lipid peroxidation. 4-Hydroxy-2-nonenal is a potential inducer of intracellular peroxide production
    • Uchida, K., Shiraishi, M., Naito, Y., Torii, Y., Nakamura, Y., and Osawa, T. (1999) Activation of stress signaling pathways by the end product of lipid peroxidation. 4-Hydroxy-2-nonenal is a potential inducer of intracellular peroxide production. J. Biol. Chem. 274, 2234-2242.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2234-2242
    • Uchida, K.1    Shiraishi, M.2    Naito, Y.3    Torii, Y.4    Nakamura, Y.5    Osawa, T.6
  • 41
    • 0037172997 scopus 로고    scopus 로고
    • Ebselen: A substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant
    • Zhao, R., Masayasu, H., and Holmgren, A. (2002) Ebselen: A substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant. Proc. Natl. Acad. Sci. U.S.A. 99, 8579-8584.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 8579-8584
    • Zhao, R.1    Masayasu, H.2    Holmgren, A.3
  • 42
    • 0025233534 scopus 로고
    • Mechanism of the reaction of ebselen with endogenous thiols: Dihydrolipoate is a better cofactor than glutathione in the peroxidase activity of ebselen
    • Haenen, G. R., De Rooij, B. M., Vermeulen, N. P., and Bast, A. (1990) Mechanism of the reaction of ebselen with endogenous thiols: Dihydrolipoate is a better cofactor than glutathione in the peroxidase activity of ebselen Mol. Pharmacol. 37, 412-422.
    • (1990) Mol. Pharmacol. , vol.37 , pp. 412-422
    • Haenen, G.R.1    De Rooij, B.M.2    Vermeulen, N.P.3    Bast, A.4
  • 43
    • 0026640860 scopus 로고
    • Characterisation and quantitation of a selenol intermediate in the reaction of ebselen with thiols
    • Cotgreave, I. A., Morgenstern, R., Engman, L., and Ahokas, J. (1992) Characterisation and quantitation of a selenol intermediate in the reaction of ebselen with thiols. Chem.-Biol. Interact. 84, 69-76.
    • (1992) Chem.-Biol. Interact. , vol.84 , pp. 69-76
    • Cotgreave, I.A.1    Morgenstern, R.2    Engman, L.3    Ahokas, J.4
  • 44
    • 5644257028 scopus 로고    scopus 로고
    • Ebselen augments its peroxidase activity by inducing nrf-2-dependent transcription
    • Tamasi, V., Jeffries, J. M., Arteel, G. E., and Falkner, K. C. (2004) Ebselen augments its peroxidase activity by inducing nrf-2-dependent transcription. Arch. Biochem. Biophys. 431, 161-168.
    • (2004) Arch. Biochem. Biophys. , vol.431 , pp. 161-168
    • Tamasi, V.1    Jeffries, J.M.2    Arteel, G.E.3    Falkner, K.C.4
  • 46
    • 24744453945 scopus 로고    scopus 로고
    • Specific patterns of electrophile adduction trigger Keap1 ubiquitination and Nrf2 activation
    • Hong, F., Sekhar, K. R., Freeman, M. L., and Liebler, D. C. (2005) Specific patterns of electrophile adduction trigger Keap1 ubiquitination and Nrf2 activation. J. Biol. Chem. 280, 31768-31775.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31768-31775
    • Hong, F.1    Sekhar, K.R.2    Freeman, M.L.3    Liebler, D.C.4
  • 47
    • 0035131144 scopus 로고    scopus 로고
    • Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions
    • Grant, C. M. (2001) Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions. Mol. Microbiol. 39, 533-541.
    • (2001) Mol. Microbiol. , vol.39 , pp. 533-541
    • Grant, C.M.1
  • 48
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • 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.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 49
    • 0032488513 scopus 로고    scopus 로고
    • Recent trends in glutathione biochemistry: Glutathione-protein interactions: A molecular link between oxidative stress and cell proliferation
    • Cotgreave, I. A., and Gerdes, R. G. (1998) Recent trends in glutathione biochemistry: Glutathione-protein interactions: A molecular link between oxidative stress and cell proliferation. Biochem. Biophys. Res. Commun. 242, 1-9.
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 1-9
    • Cotgreave, I.A.1    Gerdes, R.G.2
  • 50
    • 0028276756 scopus 로고
    • Protein S-thiolation and dethiolation
    • Thomas, J. A., Chai, Y. C., and Jung, C. H. (1994) Protein S-thiolation and dethiolation. Methods Enzymol. 233, 385-395.
    • (1994) Methods Enzymol. , vol.233 , pp. 385-395
    • Thomas, J.A.1    Chai, Y.C.2    Jung, C.H.3
  • 51
    • 0029015864 scopus 로고
    • Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas, J. A., Poland, B., and Honzatko, R. (1995) Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch. Biochem. Biophys. 319, 1-9.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 52
    • 0030057750 scopus 로고    scopus 로고
    • Protein S-thiolation and dethiolation during the respiratory burst in human monocytes. A reversible post-translational modification with potential for buffering the effects of oxidant stress
    • Seres, T., Ravichandran, V., Moriguchi, T., Rokutan, K., Thomas, J. A., and Johnston, R. B. (1996) Protein S-thiolation and dethiolation during the respiratory burst in human monocytes. A reversible post-translational modification with potential for buffering the effects of oxidant stress. J. Immunol. 156, 1973-1980.
    • (1996) J. Immunol. , vol.156 , pp. 1973-1980
    • Seres, T.1    Ravichandran, V.2    Moriguchi, T.3    Rokutan, K.4    Thomas, J.A.5    Johnston, R.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.