메뉴 건너뛰기




Volumn , Issue , 2013, Pages

The role of the Keap1/Nrf2 pathway in the cellular response to methylmercury

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR DAMAGE; CELLULAR PROTEINS; CELLULAR RESPONSE; ELECTROPHILES; METHYLMERCURY; NEGATIVE REGULATORS; PROTEIN ADDUCTS; PROTEIN MODIFICATIONS;

EID: 84880159058     PISSN: 19420900     EISSN: 19420994     Source Type: Journal    
DOI: 10.1155/2013/848279     Document Type: Review
Times cited : (56)

References (53)
  • 1
    • 33947478890 scopus 로고
    • Association constants of methylmercury with sulfhydryl and other bases
    • 2-s2.0-33947478890
    • Simpson R. B., Association constants of methylmercury with sulfhydryl and other bases. Journal of the American Chemical Society 1961 83 23 4711 4717 2-s2.0-33947478890
    • (1961) Journal of the American Chemical Society , vol.83 , Issue.23 , pp. 4711-4717
    • Simpson, R.B.1
  • 2
    • 0036802623 scopus 로고    scopus 로고
    • Transport of toxic metals by molecular mimicry
    • 2-s2.0-0036802623
    • Ballatori N., Transport of toxic metals by molecular mimicry. Environmental Health Perspectives 2002 110 supplement 5 689 694 2-s2.0-0036802623
    • (2002) Environmental Health Perspectives , vol.110 , Issue.SUPPL. 5 , pp. 689-694
    • Ballatori, N.1
  • 3
    • 34250693618 scopus 로고    scopus 로고
    • Accelerated urinary excretion of methylmercury following administration of its antidote N -acetylcysteine requires Mrp2/Abcc2, the apical multidrug resistance-associated protein
    • 2-s2.0-34250693618 10.1124/jpet.107.122812
    • Madejczyk M. S., Aremu D. A., Simmons-Willis T. A., Clarkson T. W., Ballatori N., Accelerated urinary excretion of methylmercury following administration of its antidote N -acetylcysteine requires Mrp2/Abcc2, the apical multidrug resistance-associated protein. The Journal of Pharmacology and Experimental Therapeutics 2007 322 1 378 384 2-s2.0-34250693618 10.1124/jpet.107.122812
    • (2007) The Journal of Pharmacology and Experimental Therapeutics , vol.322 , Issue.1 , pp. 378-384
    • Madejczyk, M.S.1    Aremu, D.A.2    Simmons-Willis, T.A.3    Clarkson, T.W.4    Ballatori, N.5
  • 4
    • 78751624918 scopus 로고    scopus 로고
    • MRP2 and the handling of mercuric ions in rats exposed acutely to inorganic and organic species of mercury
    • 2-s2.0-78751624918 10.1016/j.taap.2010.11.015
    • Bridges C. C., Joshee L., Zalups R. K., MRP2 and the handling of mercuric ions in rats exposed acutely to inorganic and organic species of mercury. Toxicology and Applied Pharmacology 2011 251 1 50 58 2-s2.0-78751624918 10.1016/j.taap.2010.11.015
    • (2011) Toxicology and Applied Pharmacology , vol.251 , Issue.1 , pp. 50-58
    • Bridges, C.C.1    Joshee, L.2    Zalups, R.K.3
  • 5
    • 0015268017 scopus 로고
    • The pharmacology of mercury compounds
    • 2-s2.0-0015268017
    • Clarkson T. W., The pharmacology of mercury compounds. Annual Review of Pharmacology 1972 12 375 406 2-s2.0-0015268017
    • (1972) Annual Review of Pharmacology , vol.12 , pp. 375-406
    • Clarkson, T.W.1
  • 6
    • 84984589194 scopus 로고    scopus 로고
    • Oxidative stress in MeHg-induced neurotoxicity
    • 2-s2.0-80054753707 10.1016/j.taap.2011.05.001
    • Farina M., Aschner M., Rocha J. B., Oxidative stress in MeHg-induced neurotoxicity. Toxicology and Applied Pharmacology 2011 256 3 405 417 2-s2.0-80054753707 10.1016/j.taap.2011.05.001
    • (2011) Toxicology and Applied Pharmacology , vol.256 , Issue.3 , pp. 405-417
    • Farina, M.1    Aschner, M.2    Rocha, J.B.3
  • 7
    • 0033543566 scopus 로고    scopus 로고
    • Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene
    • 2-s2.0-0033543566 10.1074/jbc.274.37.26071
    • Alam J., Stewart D., Touchard C., Boinapally S., Choi A. M., Cook J. L., Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene. Journal of Biological Chemistry 1999 274 37 26071 26078 2-s2.0-0033543566 10.1074/jbc.274.37.26071
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.37 , pp. 26071-26078
    • Alam, J.1    Stewart, D.2    Touchard, C.3    Boinapally, S.4    Choi, A.M.5    Cook, J.L.6
  • 8
    • 0033584867 scopus 로고    scopus 로고
    • Regulation of γ -glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2
    • 2-s2.0-0033584867 10.1074/jbc.274.47.33627
    • Wild A. C., Moinova H. R., Mulcahy R. T., Regulation of γ -glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2. The Journal of Biological Chemistry 1999 274 47 33627 33636 2-s2.0-0033584867 10.1074/jbc.274.47.33627
    • (1999) The Journal of Biological Chemistry , vol.274 , Issue.47 , pp. 33627-33636
    • Wild, A.C.1    Moinova, H.R.2    Mulcahy, R.T.3
  • 9
    • 0034672595 scopus 로고    scopus 로고
    • Impaired expression of glutathione synthetic enzyme genes in mice with targeted deletion of the Nrf2 basic-leucine zipper protein
    • 2-s2.0-0034672595 10.1016/S0167-4781(00)00238-4
    • Chan J. Y., Kwong M., Impaired expression of glutathione synthetic enzyme genes in mice with targeted deletion of the Nrf2 basic-leucine zipper protein. Biochimica et Biophysica Acta 2000 1517 1 19 26 2-s2.0-0034672595 10.1016/S0167-4781(00)00238-4
    • (2000) Biochimica et Biophysica Acta , vol.1517 , Issue.1 , pp. 19-26
    • Chan, J.Y.1    Kwong, M.2
  • 10
    • 0141534255 scopus 로고    scopus 로고
    • Transcription factor Nrf2 is required for the constitutive and inducible expression of multidrug resistance-associated protein 1 in mouse embryo fibroblasts
    • 2-s2.0-0141534255 10.1016/j.bbrc.2003.09.086
    • Hayashi A., Suzuki H., Itoh K., Yamamoto M., Sugiyama Y., Transcription factor Nrf2 is required for the constitutive and inducible expression of multidrug resistance-associated protein 1 in mouse embryo fibroblasts. Biochemical and Biophysical Research Communications 2003 310 3 824 829 2-s2.0-0141534255 10.1016/j.bbrc.2003.09.086
    • (2003) Biochemical and Biophysical Research Communications , vol.310 , Issue.3 , pp. 824-829
    • Hayashi, A.1    Suzuki, H.2    Itoh, K.3    Yamamoto, M.4    Sugiyama, Y.5
  • 11
    • 33646267005 scopus 로고    scopus 로고
    • Role of Nrf2 in the regulation of the Mrp2 (ABCC2) gene
    • 2-s2.0-33646267005 10.1042/BJ20051518
    • Vollrath V., Wielandt A. M., Iruretagoyena M., Chianale J., Role of Nrf2 in the regulation of the Mrp2 (ABCC2) gene. Biochemical Journal 2006 395 3 599 609 2-s2.0-33646267005 10.1042/BJ20051518
    • (2006) Biochemical Journal , vol.395 , Issue.3 , pp. 599-609
    • Vollrath, V.1    Wielandt, A.M.2    Iruretagoyena, M.3    Chianale, J.4
  • 12
    • 36349015332 scopus 로고    scopus 로고
    • Oxidative and electrophilic stress induces multidrug resistance- associated protein transporters via the nuclear factor-E2-related factor-2 transcriptional pathway
    • 2-s2.0-36349015332 10.1002/hep.21831
    • Maher J. M., Dieter M. Z., Aleksunes L. M., Oxidative and electrophilic stress induces multidrug resistance-associated protein transporters via the nuclear factor-E2-related factor-2 transcriptional pathway. Hepatology 2007 46 5 1597 1610 2-s2.0-36349015332 10.1002/hep.21831
    • (2007) Hepatology , vol.46 , Issue.5 , pp. 1597-1610
    • Maher, J.M.1    Dieter, M.Z.2    Aleksunes, L.M.3
  • 13
    • 0030596071 scopus 로고    scopus 로고
    • Selective inhibition of the mouse brain Mn-SOD by methylmercury
    • 2-s2.0-0030596071 10.1016/S1382-6689(96)00070-1
    • Shinyashiki M., Kumagai Y., Homma-Takeda S., Selective inhibition of the mouse brain Mn-SOD by methylmercury. Environmental Toxicology and Pharmacology 1996 2 4 359 366 2-s2.0-0030596071 10.1016/S1382-6689(96)00070-1
    • (1996) Environmental Toxicology and Pharmacology , vol.2 , Issue.4 , pp. 359-366
    • Shinyashiki, M.1    Kumagai, Y.2    Homma-Takeda, S.3
  • 15
    • 0032490597 scopus 로고    scopus 로고
    • Differential changes in rat brain nitric oxide synthase in vivo and in vitro by methylmercury
    • 2-s2.0-0032490597 10.1016/S0006-8993(98)00400-4
    • Shinyashiki M., Kumagai Y., Nakajima H., Differential changes in rat brain nitric oxide synthase in vivo and in vitro by methylmercury. Brain Research 1998 798 1-2 147 155 2-s2.0-0032490597 10.1016/S0006-8993(98)00400-4
    • (1998) Brain Research , vol.798 , Issue.1-2 , pp. 147-155
    • Shinyashiki, M.1    Kumagai, Y.2    Nakajima, H.3
  • 16
    • 0030774779 scopus 로고    scopus 로고
    • Chronic effects of methylmercury in rats. I. biochemical aspects
    • 2-s2.0-0030774779 10.1620/tjem.182.185
    • Yasutake A., Nakano A., Miyamoto K., Eto K., Chronic effects of methylmercury in rats. I. biochemical aspects. The Tohoku Journal of Experimental Medicine 1997 182 3 185 196 2-s2.0-0030774779 10.1620/tjem.182.185
    • (1997) The Tohoku Journal of Experimental Medicine , vol.182 , Issue.3 , pp. 185-196
    • Yasutake, A.1    Nakano, A.2    Miyamoto, K.3    Eto, K.4
  • 17
    • 78650310916 scopus 로고    scopus 로고
    • Identification and distribution of mercury species in rat tissues following administration of thimerosal or methylmercury
    • 2-s2.0-78650310916 10.1007/s00204-010-0538-4
    • Rodrigues J. L., Serpeloni J. M., Batista B. L., Souza S. S., Barbosa F. Jr., Identification and distribution of mercury species in rat tissues following administration of thimerosal or methylmercury. Archives of Toxicology 2010 84 11 891 896 2-s2.0-78650310916 10.1007/s00204-010-0538-4
    • (2010) Archives of Toxicology , vol.84 , Issue.11 , pp. 891-896
    • Rodrigues, J.L.1    Serpeloni, J.M.2    Batista, B.L.3    Souza, S.S.4    Barbosa Jr., F.5
  • 18
    • 57249116265 scopus 로고    scopus 로고
    • Reduction of arginase i activity and manganese levels in the liver during exposure of rats to methylmercury: A possible mechanism
    • 2-s2.0-57249116265 10.1007/s00204-008-0307-9
    • Kanda H., Sumi D., Endo A., Reduction of arginase I activity and manganese levels in the liver during exposure of rats to methylmercury: a possible mechanism. Archives of Toxicology 2008 82 11 803 808 2-s2.0-57249116265 10.1007/s00204-008-0307-9
    • (2008) Archives of Toxicology , vol.82 , Issue.11 , pp. 803-808
    • Kanda, H.1    Sumi, D.2    Endo, A.3
  • 19
    • 84871181842 scopus 로고    scopus 로고
    • S -mercuration of rat sorbitol dehydrogenase by methylmercury causes its aggregation and the release of the zinc ion from the active site
    • Kanda H., Toyama T., Shinohara-Kanda A., S -mercuration of rat sorbitol dehydrogenase by methylmercury causes its aggregation and the release of the zinc ion from the active site. Archives of Toxicology 2012 86 11 1693 1702
    • (2012) Archives of Toxicology , vol.86 , Issue.11 , pp. 1693-1702
    • Kanda, H.1    Toyama, T.2    Shinohara-Kanda, A.3
  • 20
    • 0025877171 scopus 로고
    • Sorbitol dehydrogenase: CDNA coding for the rat enzyme. variations within the alcohol dehydrogenase family independent of quaternary structure and metal content
    • 2-s2.0-0025877171
    • Karlsson C., Jörnvall H., Höög J. O., Sorbitol dehydrogenase: cDNA coding for the rat enzyme. variations within the alcohol dehydrogenase family independent of quaternary structure and metal content. European Journal of Biochemistry 1991 198 3 761 765 2-s2.0-0025877171
    • (1991) European Journal of Biochemistry , vol.198 , Issue.3 , pp. 761-765
    • Karlsson, C.1    Jörnvall, H.2    Höög, J.O.3
  • 21
    • 17444437443 scopus 로고    scopus 로고
    • Crystal structure of sorbitol dehydrogenase
    • 2-s2.0-17444437443 10.1016/S0009-2797(00)00260-X
    • Johansson K., El-Ahmad M., Kaiser C., Crystal structure of sorbitol dehydrogenase. Chemico-Biological Interactions 2001 130-132 1-3 351 358 2-s2.0-17444437443 10.1016/S0009-2797(00)00260-X
    • (2001) Chemico-Biological Interactions , vol.130-132 , Issue.1-3 , pp. 351-358
    • Johansson, K.1    El-Ahmad, M.2    Kaiser, C.3
  • 22
    • 0026703404 scopus 로고
    • Enhancement of γ -glutamylcysteine synthetase mRNA in rat kidney by methyl mercury
    • 2-s2.0-0026703404 10.1016/0003-9861(92)90583-I
    • Woods J. S., Davis H. A., Baer R. P., Enhancement of γ -glutamylcysteine synthetase mRNA in rat kidney by methyl mercury. Archives of Biochemistry and Biophysics 1992 296 1 350 353 2-s2.0-0026703404 10.1016/0003-9861(92)90583-I
    • (1992) Archives of Biochemistry and Biophysics , vol.296 , Issue.1 , pp. 350-353
    • Woods, J.S.1    Davis, H.A.2    Baer, R.P.3
  • 23
    • 0027930061 scopus 로고
    • Acute effects of methylmercury on hepatic and renal glutathione metabolisms in mice
    • 2-s2.0-0027930061 10.1007/s002040050104
    • Yasutake A., Hirayama K., Acute effects of methylmercury on hepatic and renal glutathione metabolisms in mice. Archives of Toxicology 1994 68 8 512 516 2-s2.0-0027930061 10.1007/s002040050104
    • (1994) Archives of Toxicology , vol.68 , Issue.8 , pp. 512-516
    • Yasutake, A.1    Hirayama, K.2
  • 24
    • 0030248169 scopus 로고    scopus 로고
    • Localization of γ -lutamylcysteine synthetase mRNA expression in mouse brain following methylmercury treatment using reverse transcription in situ PCR amplification
    • 2-s2.0-0030248169 10.1006/taap.1996.0211
    • Li S., Thompson S. A., Woods J. S., Localization of γ -lutamylcysteine synthetase mRNA expression in mouse brain following methylmercury treatment using reverse transcription in situ PCR amplification. Toxicology and Applied Pharmacology 1996 140 1 180 187 2-s2.0-0030248169 10.1006/taap.1996.0211
    • (1996) Toxicology and Applied Pharmacology , vol.140 , Issue.1 , pp. 180-187
    • Li, S.1    Thompson, S.A.2    Woods, J.S.3
  • 25
    • 0032741568 scopus 로고    scopus 로고
    • Induction of glutamate-cysteine ligase (γ -glutamylcysteine synthetase) in the brains of adult female mice subchronically exposed to methylmercury
    • 2-s2.0-0032741568 10.1016/S0378-4274(99)00133-2
    • Thompson S. A., White C. C., Krejsa C. M., Induction of glutamate-cysteine ligase (γ -glutamylcysteine synthetase) in the brains of adult female mice subchronically exposed to methylmercury. Toxicology Letters 1999 110 1-2 1 9 2-s2.0-0032741568 10.1016/S0378-4274(99)00133-2
    • (1999) Toxicology Letters , vol.110 , Issue.1-2 , pp. 1-9
    • Thompson, S.A.1    White, C.C.2    Krejsa, C.M.3
  • 26
    • 0033858373 scopus 로고    scopus 로고
    • Modulation of glutathione and glutamate-L-cysteine ligase by methylmercury during mouse development
    • 2-s2.0-0033858373
    • Thompson S. A., White C. C., Krejsa C. M., Eaton D. L., Kavanagh T. J., Modulation of glutathione and glutamate-L-cysteine ligase by methylmercury during mouse development. Toxicological Sciences 2000 57 1 141 146 2-s2.0-0033858373
    • (2000) Toxicological Sciences , vol.57 , Issue.1 , pp. 141-146
    • Thompson, S.A.1    White, C.C.2    Krejsa, C.M.3    Eaton, D.L.4    Kavanagh, T.J.5
  • 27
    • 0035918903 scopus 로고    scopus 로고
    • Tissue specific changes in the expression of glutamate-cysteine ligase mRNAs in mice exposed to methylmercury
    • 2-s2.0-0035918903 10.1016/S0378-4274(01)00341-1
    • Díaz D., Krejsa C. M., White C. C., Keener C. L., Farin F. M., Kavanagh T. J., Tissue specific changes in the expression of glutamate-cysteine ligase mRNAs in mice exposed to methylmercury. Toxicology Letters 2001 122 2 119 129 2-s2.0-0035918903 10.1016/S0378-4274(01)00341-1
    • (2001) Toxicology Letters , vol.122 , Issue.2 , pp. 119-129
    • Díaz, D.1    Krejsa, C.M.2    White, C.C.3    Keener, C.L.4    Farin, F.M.5    Kavanagh, T.J.6
  • 28
    • 4444285389 scopus 로고    scopus 로고
    • Effect of methylmercury on glutamate-cysteine ligase expression in the placenta and yolk sac during mouse development
    • 2-s2.0-4444285389 10.1016/j.reprotox.2004.06.006
    • Díaz D., Krejsa C. M., White C. C., Charleston J. S., Kavanagh T. J., Effect of methylmercury on glutamate-cysteine ligase expression in the placenta and yolk sac during mouse development. Reproductive Toxicology 2004 19 1 117 129 2-s2.0-4444285389 10.1016/j.reprotox.2004.06.006
    • (2004) Reproductive Toxicology , vol.19 , Issue.1 , pp. 117-129
    • Díaz, D.1    Krejsa, C.M.2    White, C.C.3    Charleston, J.S.4    Kavanagh, T.J.5
  • 29
    • 0031577292 scopus 로고    scopus 로고
    • An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements
    • 2-s2.0-0031577292 10.1006/bbrc.1997.6943
    • Itoh K., Chiba T., Takahashi S., An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements. Biochemical and Biophysical Research Communications 1997 236 2 313 322 2-s2.0-0031577292 10.1006/bbrc.1997.6943
    • (1997) Biochemical and Biophysical Research Communications , vol.236 , Issue.2 , pp. 313-322
    • Itoh, K.1    Chiba, T.2    Takahashi, S.3
  • 30
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • 2-s2.0-0032953192
    • Itoh K., Wakabayashi N., Katoh Y., Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes & Development 1999 13 1 76 86 2-s2.0-0032953192
    • (1999) Genes & Development , vol.13 , Issue.1 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3
  • 31
    • 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
    • 2-s2.0-0037015035 10.1073/pnas.172398899
    • Dinkova-Kostova A. T., Holtzclaw W. D., Cole R. N., Direct evidence that sulfhydryl groups of keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proceedings of the National Academy of Sciences of the United States of America 2002 99 18 11908 11913 2-s2.0-0037015035 10.1073/pnas.172398899
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.18 , pp. 11908-11913
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Cole, R.N.3
  • 32
    • 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
    • 2-s2.0-0242580049 10.1128/MCB.23.22.8137-8151.2003
    • Zhang D. D., Hannink M., Distinct cysteine residues in keap1 are required for keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Molecular and Cellular Biology 2003 23 22 8137 8151 2-s2.0-0242580049 10.1128/MCB.23.22.8137-8151.2003
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.22 , pp. 8137-8151
    • Zhang, D.D.1    Hannink, M.2
  • 33
    • 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
    • 2-s2.0-22544464124 10.1073/pnas.0502402102
    • Eggler A. L., Liu G., Pezzuto J. M., Van Breemen R. B., Mesecar A. D., Modifying specific cysteines of the electrophile-sensing human keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2. Proceedings of the National Academy of Sciences of the United States of America 2005 102 29 10070 10075 2-s2.0-22544464124 10.1073/pnas.0502402102
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.29 , pp. 10070-10075
    • Eggler, A.L.1    Liu, G.2    Pezzuto, J.M.3    Van Breemen, R.B.4    Mesecar, A.D.5
  • 34
    • 24744453945 scopus 로고    scopus 로고
    • Specific patterns of electrophile adduction trigger keap1 ubiquitination and Nrf2 activation
    • 2-s2.0-24744453945 10.1074/jbc.M503346200
    • Hong F., Sekhar K. R., Freeman M. L., Liebler D. C., Specific patterns of electrophile adduction trigger keap1 ubiquitination and Nrf2 activation. Journal of Biological Chemistry 2005 280 36 31768 31775 2-s2.0-24744453945 10.1074/jbc.M503346200
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.36 , pp. 31768-31775
    • Hong, F.1    Sekhar, K.R.2    Freeman, M.L.3    Liebler, D.C.4
  • 35
    • 42149196050 scopus 로고    scopus 로고
    • Physiological significance of reactive cysteine residues of keap1 in determining Nrf2 activity
    • 2-s2.0-42149196050 10.1128/MCB.01704-07
    • Yamamoto T., Suzuki T., Kobayashi A., Physiological significance of reactive cysteine residues of keap1 in determining Nrf2 activity. Molecular and Cellular Biology 2008 28 8 2758 2770 2-s2.0-42149196050 10.1128/MCB.01704-07
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.8 , pp. 2758-2770
    • Yamamoto, T.1    Suzuki, T.2    Kobayashi, A.3
  • 36
    • 58249117780 scopus 로고    scopus 로고
    • The antioxidant defense system keap1-Nrf2 comprises a multiple sensing mechanism for responding to a wide range of chemical compounds
    • 2-s2.0-58249117780 10.1128/MCB.01080-08
    • Kobayashi M., Li L., Iwamoto N., The antioxidant defense system keap1-Nrf2 comprises a multiple sensing mechanism for responding to a wide range of chemical compounds. Molecular and Cellular Biology 2009 29 2 493 502 2-s2.0-58249117780 10.1128/MCB.01080-08
    • (2009) Molecular and Cellular Biology , vol.29 , Issue.2 , pp. 493-502
    • Kobayashi, M.1    Li, L.2    Iwamoto, N.3
  • 37
    • 78751703950 scopus 로고    scopus 로고
    • Molecular mechanisms of the keap1-Nrf2 pathway in stress response and cancer evolution
    • 2-s2.0-78751703950 10.1111/j.1365-2443.2010.01473.x
    • Taguchi K., Motohashi H., Yamamoto M., Molecular mechanisms of the keap1-Nrf2 pathway in stress response and cancer evolution. Genes to Cells 2011 16 2 123 140 2-s2.0-78751703950 10.1111/j.1365-2443.2010.01473.x
    • (2011) Genes to Cells , vol.16 , Issue.2 , pp. 123-140
    • Taguchi, K.1    Motohashi, H.2    Yamamoto, M.3
  • 38
    • 79960835354 scopus 로고    scopus 로고
    • Participation of covalent modification of keap1 in the activation of Nrf2 by tert-butylbenzoquinone, an electrophilic metabolite of butylated hydroxyanisole
    • 2-s2.0-79960835354 10.1016/j.taap.2011.05.013
    • Abiko Y., Miura T., Phuc B. H., Shinkai Y., Kumagai Y., Participation of covalent modification of keap1 in the activation of Nrf2 by tert- butylbenzoquinone, an electrophilic metabolite of butylated hydroxyanisole. Toxicology and Applied Pharmacology 2011 255 1 32 39 2-s2.0-79960835354 10.1016/j.taap.2011.05.013
    • (2011) Toxicology and Applied Pharmacology , vol.255 , Issue.1 , pp. 32-39
    • Abiko, Y.1    Miura, T.2    Phuc, B.H.3    Shinkai, Y.4    Kumagai, Y.5
  • 39
    • 79954465791 scopus 로고    scopus 로고
    • Initial response and cellular protection through the keap1/Nrf2 system during the exposure of primary mouse hepatocytes to 1,2-naphthoquinone
    • 2-s2.0-79954465791 10.1021/tx100427p
    • Miura T., Shinkai Y., Jiang H. Y., Initial response and cellular protection through the keap1/Nrf2 system during the exposure of primary mouse hepatocytes to 1,2-naphthoquinone. Chemical Research in Toxicology 2011 24 4 559 567 2-s2.0-79954465791 10.1021/tx100427p
    • (2011) Chemical Research in Toxicology , vol.24 , Issue.4 , pp. 559-567
    • Miura, T.1    Shinkai, Y.2    Jiang, H.Y.3
  • 40
    • 1642282736 scopus 로고    scopus 로고
    • Cellular mechanisms of redox cell signalling: Role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products
    • 2-s2.0-1642282736 10.1042/BJ20031049
    • Levonen A. L., Landar A., Ramachandran A., Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products. Biochemical Journal 2004 378 2 373 382 2-s2.0-1642282736 10.1042/BJ20031049
    • (2004) Biochemical Journal , vol.378 , Issue.2 , pp. 373-382
    • Levonen, A.L.1    Landar, A.2    Ramachandran, A.3
  • 41
    • 1242296811 scopus 로고    scopus 로고
    • Protection against electrophile and oxidant stress by induction of the phase 2 response: Fate of cysteines of the keap1 sensor modified by inducers
    • 2-s2.0-1242296811 10.1073/pnas.0307301101
    • Wakabayashi N., Dinkova-Kostova A. T., Holtzclaw W. D., Protection against electrophile and oxidant stress by induction of the phase 2 response: fate of cysteines of the keap1 sensor modified by inducers. Proceedings of the National Academy of Sciences of the United States of America 2004 101 7 2040 2045 2-s2.0-1242296811 10.1073/pnas.0307301101
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.7 , pp. 2040-2045
    • Wakabayashi, N.1    Dinkova-Kostova, A.T.2    Holtzclaw, W.D.3
  • 42
    • 34848867520 scopus 로고    scopus 로고
    • Cytoprotective role of Nrf2/Keap1 system in methylmercury toxicity
    • 2-s2.0-34848867520 10.1016/j.bbrc.2007.09.017
    • Toyama T., Sumi D., Shinkai Y., Cytoprotective role of Nrf2/Keap1 system in methylmercury toxicity. Biochemical and Biophysical Research Communications 2007 363 3 645 650 2-s2.0-34848867520 10.1016/j.bbrc.2007.09.017
    • (2007) Biochemical and Biophysical Research Communications , vol.363 , Issue.3 , pp. 645-650
    • Toyama, T.1    Sumi, D.2    Shinkai, Y.3
  • 43
    • 58049198418 scopus 로고    scopus 로고
    • Methylmercury toxicity and Nrf2-dependent detoxification in astrocytes
    • 2-s2.0-58049198418 10.1093/toxsci/kfn201
    • Wang L., Jiang H., Yin Z., Aschner M., Cai J., Methylmercury toxicity and Nrf2-dependent detoxification in astrocytes. Toxicological Sciences 2009 107 1 135 143 2-s2.0-58049198418 10.1093/toxsci/kfn201
    • (2009) Toxicological Sciences , vol.107 , Issue.1 , pp. 135-143
    • Wang, L.1    Jiang, H.2    Yin, Z.3    Aschner, M.4    Cai, J.5
  • 44
    • 77952332154 scopus 로고    scopus 로고
    • Cytochrome P450 2A5 constitutive expression and induction by heavy metals is dependent on redox-sensitive transcription factor nrf2 in liver
    • 2-s2.0-77952332154 10.1021/tx100084c
    • Lämsä V., Levonen A. L., Leinonen H., Ylä-Herttuala S., Yamamoto M., Hakkola J., Cytochrome P450 2A5 constitutive expression and induction by heavy metals is dependent on redox-sensitive transcription factor nrf2 in liver. Chemical Research in Toxicology 2010 23 5 977 985 2-s2.0-77952332154 10.1021/tx100084c
    • (2010) Chemical Research in Toxicology , vol.23 , Issue.5 , pp. 977-985
    • Lämsä, V.1    Levonen, A.L.2    Leinonen, H.3    Ylä-Herttuala, S.4    Yamamoto, M.5    Hakkola, J.6
  • 45
    • 77955117592 scopus 로고    scopus 로고
    • Methylmercury induces acute oxidative stress, altering Nrf2 protein level in primary microglial cells
    • 2-s2.0-77955117592 10.1093/toxsci/kfq126
    • Ni M., Li X., Yin Z., Methylmercury induces acute oxidative stress, altering Nrf2 protein level in primary microglial cells. Toxicological Sciences 2010 116 2 590 603 2-s2.0-77955117592 10.1093/toxsci/kfq126
    • (2010) Toxicological Sciences , vol.116 , Issue.2 , pp. 590-603
    • Ni, M.1    Li, X.2    Yin, Z.3
  • 46
    • 84984559567 scopus 로고    scopus 로고
    • Comparative study on the response of rat primary astrocytes and microglia to methylmercury toxicity
    • 2-s2.0-79952729253 10.1002/glia.21153
    • Ni M., Li X., Yin Z., Comparative study on the response of rat primary astrocytes and microglia to methylmercury toxicity. Glia 2011 59 5 810 820 2-s2.0-79952729253 10.1002/glia.21153
    • (2011) Glia , vol.59 , Issue.5 , pp. 810-820
    • Ni, M.1    Li, X.2    Yin, Z.3
  • 47
    • 0035153227 scopus 로고    scopus 로고
    • High sensitivity of Nrf2 knockout mice to acetaminophen hepatotoxicity associated with decreased expression of ARE-regulated drug metabolizing enzymes and antioxidant genes
    • 2-s2.0-0035153227 10.1093/toxsci/59.1.169
    • Enomoto A., Itoh K., Nagayoshi E., High sensitivity of Nrf2 knockout mice to acetaminophen hepatotoxicity associated with decreased expression of ARE-regulated drug metabolizing enzymes and antioxidant genes. Toxicological Sciences 2001 59 1 169 177 2-s2.0-0035153227 10.1093/toxsci/59.1.169
    • (2001) Toxicological Sciences , vol.59 , Issue.1 , pp. 169-177
    • Enomoto, A.1    Itoh, K.2    Nagayoshi, E.3
  • 48
    • 0035875447 scopus 로고    scopus 로고
    • Accelerated DNA adduct formation in the lung of the Nrf2 knockout mouse exposed to diesel exhaust
    • 2-s2.0-0035875447 10.1006/taap.2001.9176
    • Aoki Y., Sato H., Nishimura N., Takahashi S., Itoh K., Yamamoto M., Accelerated DNA adduct formation in the lung of the Nrf2 knockout mouse exposed to diesel exhaust. Toxicology and Applied Pharmacology 2001 173 3 154 160 2-s2.0-0035875447 10.1006/taap.2001.9176
    • (2001) Toxicology and Applied Pharmacology , vol.173 , Issue.3 , pp. 154-160
    • Aoki, Y.1    Sato, H.2    Nishimura, N.3    Takahashi, S.4    Itoh, K.5    Yamamoto, M.6
  • 49
    • 33748089664 scopus 로고    scopus 로고
    • Inhibition of 7,12-dimethylbenz(a)anthracene-induced skin tumorigenesis in C57BL/6 mice by sulforaphane is mediated by nuclear factor E2-related factor 2
    • 2-s2.0-33748089664 10.1158/0008-5472.CAN-06-0300
    • Xu C., Huang M. T., Shen G., Inhibition of 7,12-dimethylbenz(a) anthracene-induced skin tumorigenesis in C57BL/6 mice by sulforaphane is mediated by nuclear factor E2-related factor 2. Cancer Research 2006 66 16 8293 8296 2-s2.0-33748089664 10.1158/0008-5472.CAN-06-0300
    • (2006) Cancer Research , vol.66 , Issue.16 , pp. 8293-8296
    • Xu, C.1    Huang, M.T.2    Shen, G.3
  • 50
    • 33748080476 scopus 로고    scopus 로고
    • Neuronal sensitivity to kainic acid is dependent on the Nrf2-mediated actions of the antioxidant response element
    • 2-s2.0-33748080476 10.1111/j.1471-4159.2006.04019.x
    • Kraft A. D., Lee J. M., Johnson D. A., Kan Y. W., Johnson J. A., Neuronal sensitivity to kainic acid is dependent on the Nrf2-mediated actions of the antioxidant response element. Journal of Neurochemistry 2006 98 6 1852 1865 2-s2.0-33748080476 10.1111/j.1471-4159.2006.04019.x
    • (2006) Journal of Neurochemistry , vol.98 , Issue.6 , pp. 1852-1865
    • Kraft, A.D.1    Lee, J.M.2    Johnson, D.A.3    Kan, Y.W.4    Johnson, J.A.5
  • 51
    • 33846264538 scopus 로고    scopus 로고
    • Nrf2-deficient mice have an increased susceptibility to dextran sulfate sodium-induced colitis
    • 2-s2.0-33846264538 10.1158/0008-5472.CAN-06-3562
    • Khor T. O., Huang M. T., Kwon K. H., Chan J. Y., Reddy B. S., Kong A. N., Nrf2-deficient mice have an increased susceptibility to dextran sulfate sodium-induced colitis. Cancer Research 2006 66 24 11580 11584 2-s2.0-33846264538 10.1158/0008-5472.CAN-06-3562
    • (2006) Cancer Research , vol.66 , Issue.24 , pp. 11580-11584
    • Khor, T.O.1    Huang, M.T.2    Kwon, K.H.3    Chan, J.Y.4    Reddy, B.S.5    Kong, A.N.6
  • 52
    • 34250901586 scopus 로고    scopus 로고
    • Enhanced spontaneous and benzo(a)pyrene-induced mutations in the lung of Nrf2-deficient gpt delta mice
    • 2-s2.0-34250901586 10.1158/0008-5472.CAN-06-3355
    • Aoki Y., Hashimoto A. H., Amanuma K., Enhanced spontaneous and benzo(a)pyrene-induced mutations in the lung of Nrf2-deficient gpt delta mice. Cancer Research 2007 67 12 5643 5648 2-s2.0-34250901586 10.1158/0008-5472.CAN- 06-3355
    • (2007) Cancer Research , vol.67 , Issue.12 , pp. 5643-5648
    • Aoki, Y.1    Hashimoto, A.H.2    Amanuma, K.3
  • 53
    • 79961090116 scopus 로고    scopus 로고
    • Isothiocyanates reduce mercury accumulation via an Nrf2-dependent mechanism during exposure of mice to methylmercury
    • 2-s2.0-79961090116 10.1289/ehp.1003123
    • Toyama T., Shinkai Y., Yasutake A., Uchida K., Yamamoto M., Kumagai Y., Isothiocyanates reduce mercury accumulation via an Nrf2-dependent mechanism during exposure of mice to methylmercury. Environmental Health Perspectives 2011 119 8 1117 1122 2-s2.0-79961090116 10.1289/ehp.1003123
    • (2011) Environmental Health Perspectives , vol.119 , Issue.8 , pp. 1117-1122
    • Toyama, T.1    Shinkai, Y.2    Yasutake, A.3    Uchida, K.4    Yamamoto, M.5    Kumagai, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.