메뉴 건너뛰기




Volumn 21, Issue 10, 2008, Pages 2051-2060

Prospective type 1 and type 2 disulfides of keap1 protein

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DISULFIDE; GLUTATHIONE; GLUTATHIONE DISULFIDE; KELCH LIKE ECH ASSOCIATED PROTEIN 1; TRANSCRIPTION FACTOR NRF2;

EID: 55949088750     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx800226m     Document Type: Article
Times cited : (84)

References (60)
  • 2
    • 0030868098 scopus 로고    scopus 로고
    • Chemoprevention by inducers of carcinogen detoxication enzymes
    • Kensler, T. W. (1997) Chemoprevention by inducers of carcinogen detoxication enzymes. Environ Health Perspect. 105 (Suppl 4), 965-70.
    • (1997) Environ Health Perspect , vol.105 , Issue.SUPPL. 4 , pp. 965-970
    • Kensler, T.W.1
  • 3
    • 0038378322 scopus 로고    scopus 로고
    • Importance of phase 2 gene regulation in protection against electrophile and reactive oxygen toxicity and carcinogenesis
    • Talalay, P., Dinkova-Kostova, A. T., and Holtzclaw, W. D. (2003) Importance of phase 2 gene regulation in protection against electrophile and reactive oxygen toxicity and carcinogenesis. Adv. Enzyme Regul. 43, 121-34.
    • (2003) Adv. Enzyme Regul , vol.43 , pp. 121-134
    • Talalay, P.1    Dinkova-Kostova, A.T.2    Holtzclaw, W.D.3
  • 4
    • 0037183998 scopus 로고    scopus 로고
    • The Keapl BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
    • Zipper, L. M., and Mulcahy, R. T. (2002) The Keapl BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm. J. Biol. Chem. 277, 36544-52.
    • (2002) J. Biol. Chem , vol.277 , pp. 36544-36552
    • Zipper, L.M.1    Mulcahy, R.T.2
  • 5
    • 18244377997 scopus 로고    scopus 로고
    • Keapl, the sensor for electrophiles and oxidants that regulates the phase 2 response, is a zinc metalloprotein
    • Dinkova-Kostova, A. T., Holtzclaw, W. D., and Wakabayashi, N. (2005) Keapl, the sensor for electrophiles and oxidants that regulates the phase 2 response, is a zinc metalloprotein. Biochemistry 44, 6889-99.
    • (2005) Biochemistry , vol.44 , pp. 6889-6899
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Wakabayashi, N.3
  • 7
    • 33747728194 scopus 로고    scopus 로고
    • Dimerization of substrate adaptors can facilitate cullin-mediated ubiquitylation of proteins by a "tethering" mechanism: A two-site interaction model for the Nrf2-Keapl complex
    • McMahon, M., Thomas, N., Itoh, K., Yamamoto, M., and Hayes, J. D. (2006) Dimerization of substrate adaptors can facilitate cullin-mediated ubiquitylation of proteins by a "tethering" mechanism: a two-site interaction model for the Nrf2-Keapl complex. J. Biol. Chem. 281, 24756-68.
    • (2006) J. Biol. Chem , vol.281 , pp. 24756-24768
    • McMahon, M.1    Thomas, N.2    Itoh, K.3    Yamamoto, M.4    Hayes, J.D.5
  • 8
    • 0032953192 scopus 로고    scopus 로고
    • Keapl represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., and Yamamoto, M. (1999) Keapl represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal 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
  • 9
    • 0035963293 scopus 로고    scopus 로고
    • Functional characterization and role of INrf2 in antioxidant response element-mediated expression and antioxidant induction of NAD(P)H:quinone oxidoreductasel gene
    • Dhakshinamoorthy, S., and Jaiswal, A. K. (2001) Functional characterization and role of INrf2 in antioxidant response element-mediated expression and antioxidant induction of NAD(P)H:quinone oxidoreductasel gene. Oncogene 20, 3906-17.
    • (2001) Oncogene , vol.20 , pp. 3906-3917
    • Dhakshinamoorthy, S.1    Jaiswal, A.K.2
  • 10
    • 12444257799 scopus 로고    scopus 로고
    • Keapl 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) Keapl regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles. Genes Cells 8, 379-91.
    • (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
  • 11
    • 10044228504 scopus 로고    scopus 로고
    • Keapl is a redox-regulated substrate adaptor protein for a Cu13-dependent ubiquitin ligase complex
    • Zhang, D. D., Lo, S. C., Cross, J. V., Templeton, D. J., and Hannink, M. (2004) Keapl is a redox-regulated substrate adaptor protein for a Cu13-dependent ubiquitin ligase complex. Mol. Cell. Biol. 24, 10941-53.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 10941-10953
    • Zhang, D.D.1    Lo, S.C.2    Cross, J.V.3    Templeton, D.J.4    Hannink, M.5
  • 12
    • 3543008924 scopus 로고    scopus 로고
    • Oxidative stress sensor Keapl functions as an adaptor for Cu13-based E3 ligase to regulate proteasomal degradation of Nrf2
    • Kobayashi, A., Kang, M. I., Okawa, H., Ohtsuji, M., Zenke, Y., Chiba, T., Igarashi, K., and Yamamoto, M. (2004) Oxidative stress sensor Keapl functions as an adaptor for Cu13-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol. Cell. Biol. 24, 7130-9.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 7130-7139
    • Kobayashi, A.1    Kang, M.I.2    Okawa, H.3    Ohtsuji, M.4    Zenke, Y.5    Chiba, T.6    Igarashi, K.7    Yamamoto, M.8
  • 13
    • 11144264663 scopus 로고    scopus 로고
    • BTB protein Keapl targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase
    • Furukawa, M., and Xiong, Y. (2005) BTB protein Keapl targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase. Mol. Cell. Biol. 25, 162-71.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 162-171
    • Furukawa, M.1    Xiong, Y.2
  • 14
    • 34548772935 scopus 로고    scopus 로고
    • Keap1 controls postinduction repression of the Nrf2-mediated antioxidant response by escorting nuclear export of Nrf2
    • Sun, Z., Zhang, S., Chan, J. Y., and Zhang, D. D. (2007) Keap1 controls postinduction repression of the Nrf2-mediated antioxidant response by escorting nuclear export of Nrf2. Mol. Cell. Biol. 27, 6334-49.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 6334-6349
    • Sun, Z.1    Zhang, S.2    Chan, J.Y.3    Zhang, D.D.4
  • 16
    • 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., Kobayashi, 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, 2046-51.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 2046-2051
    • Kang, M.I.1    Kobayashi, A.2    Wakabayashi, N.3    Kim, S.G.4    Yamamoto, M.5
  • 17
    • 22544464124 scopus 로고    scopus 로고
    • Modifying specific cysteines of the electrophile-sensing human Keapl 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 Keapl protein is insufficient to disrupt binding to the Nrf2 domain Neh2. Proc. Nail. Acad. Sci. U.S.A. 102, 10070-5.
    • (2005) Proc. Nail. 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
  • 18
    • 0037015035 scopus 로고    scopus 로고
    • Direct evidence that sulfhydryl groups of Keapl 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 Keapl are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc. Natl. Acad. Sci. U.S.A. 99, 11908-13.
    • (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
  • 19
    • 76449118748 scopus 로고    scopus 로고
    • Site-Specific Modification of the Electrophile Sensor Protein Keapl and Activation of Nrf2-Dependent Gene Expression
    • Liebler, D. C., Hong, F., Sekhar, K. R., and Freeman, M. L. (2006) Site-Specific Modification of the Electrophile Sensor Protein Keapl and Activation of Nrf2-Dependent Gene Expression. Adv. Mol. Toxicol. 1, 55-71.
    • (2006) Adv. Mol. Toxicol , vol.1 , pp. 55-71
    • Liebler, D.C.1    Hong, F.2    Sekhar, K.R.3    Freeman, M.L.4
  • 20
    • 29644443964 scopus 로고    scopus 로고
    • Identification of sensor cysteines in human Keap1 modified by the cancer chemopreventive agent sulforaphane
    • Hong, F., Freeman, M. L., and Liebler, D. C. (2005) Identification of sensor cysteines in human Keap1 modified by the cancer chemopreventive agent sulforaphane. Chem. Res. Toxicol. 18, 1917-26.
    • (2005) Chem. Res. Toxicol , vol.18 , pp. 1917-1926
    • Hong, F.1    Freeman, M.L.2    Liebler, D.C.3
  • 21
    • 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, 31768-75.
    • (2005) J. Biol. Chem , vol.280 , pp. 31768-31775
    • Hong, F.1    Sekhar, K.R.2    Freeman, M.L.3    Liebler, D.C.4
  • 23
    • 33344469643 scopus 로고    scopus 로고
    • Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keapl
    • Kobayashi, A., Kang, M. I., Watai, Y., Tong, K. I., Shibata, T., Uchida, K., and Yamamoto, M. (2006) Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keapl. Mol. Cell. Biol. 26, 221-9.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 221-229
    • Kobayashi, A.1    Kang, M.I.2    Watai, Y.3    Tong, K.I.4    Shibata, T.5    Uchida, K.6    Yamamoto, M.7
  • 24
    • 33750613056 scopus 로고    scopus 로고
    • Two-site substrate recognition model for the Keapl-Nrf2 system: A hinge and latch mechanism
    • Tong, K. I., Kobayashi, A., Katsuoka, F., and Yamamoto, M. (2006) Two-site substrate recognition model for the Keapl-Nrf2 system: a hinge and latch mechanism. Biol Chem 387, 1311-20.
    • (2006) Biol Chem , vol.387 , pp. 1311-1320
    • Tong, K.I.1    Kobayashi, A.2    Katsuoka, F.3    Yamamoto, M.4
  • 25
    • 36349019109 scopus 로고    scopus 로고
    • Identification of the highly reactive cysteine 151 in the chemopreventive agent-sensor Keap1 protein is method-dependent
    • Eggler, A. L., Luo, Y., van Breemen, R. B., and Mesecar, A. D. (2007) Identification of the highly reactive cysteine 151 in the chemopreventive agent-sensor Keap1 protein is method-dependent. Chem. Res. Toxicol. 20, 1878-84.
    • (2007) Chem. Res. Toxicol , vol.20 , pp. 1878-1884
    • Eggler, A.L.1    Luo, Y.2    van Breemen, R.B.3    Mesecar, A.D.4
  • 26
    • 0242580049 scopus 로고    scopus 로고
    • Distinct cysteine residues in Keap1 are required for Keap 1-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 Keap 1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol. Cell. Biol. 23, 8137-51.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 8137-8151
    • Zhang, D.D.1    Hannink, M.2
  • 27
    • 31444447800 scopus 로고    scopus 로고
    • Activation of the Keap1/ Nrf2 pathway for neuroprotection by electrophilic [correction of electrophillic] phase II inducers
    • Satoh, T., Okamoto, S. I., Cui, J., Watanabe, Y., Furuta, K., Suzuki, M., Tohyama, K., and Lipton, S. A. (2006) Activation of the Keap1/ Nrf2 pathway for neuroprotection by electrophilic [correction of electrophillic] phase II inducers. Proc. Natl. Acad. Sci. U.S.A. 103, 768-73.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 768-773
    • Satoh, T.1    Okamoto, S.I.2    Cui, J.3    Watanabe, Y.4    Furuta, K.5    Suzuki, M.6    Tohyama, K.7    Lipton, S.A.8
  • 30
    • 41849146057 scopus 로고    scopus 로고
    • Covalent modification at Cys151 dissociates the electrophile sensor Keap1 from the ubiquitin ligase CUL3
    • Rachakonda, G., Xiong, Y., Sekhar, K. R., Stamer, S. L., Liebler, D. C., and Freeman, M. L. (2008) Covalent modification at Cys151 dissociates the electrophile sensor Keap1 from the ubiquitin ligase CUL3. Chem. Res. Toxicol. 21, 705-10.
    • (2008) Chem. Res. Toxicol , vol.21 , pp. 705-710
    • Rachakonda, G.1    Xiong, Y.2    Sekhar, K.R.3    Stamer, S.L.4    Liebler, D.C.5    Freeman, M.L.6
  • 31
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/ glutathione couple
    • Schafer, F. Q., and Buettner, G. R. (2001) Redox environment of the cell as viewed through the redox state of the glutathione disulfide/ glutathione couple. Free Radical Biol. Med. 30, 1191-212.
    • (2001) Free Radical Biol. Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 32
    • 14844298802 scopus 로고    scopus 로고
    • Corapartmental oxidation of thiol-disulphide redox couples during epidermal growth factor signalling
    • Halvey, P. J., Watson, W. H., Hansen, J. M., Go, Y. M., Samali, A., and Jones, D. P. (2005) Corapartmental oxidation of thiol-disulphide redox couples during epidermal growth factor signalling. Biochem. J. 386, 215-9.
    • (2005) Biochem. J , vol.386 , pp. 215-219
    • Halvey, P.J.1    Watson, W.H.2    Hansen, J.M.3    Go, Y.M.4    Samali, A.5    Jones, D.P.6
  • 33
    • 8444228527 scopus 로고    scopus 로고
    • Compartmentation of Nrf-2 redox control: Regulation of cytoplasmic activation by glutathione and DNA binding by thioredoxin-1
    • Hansen, J. M., Watson, W. H., and Jones, D. P. (2004) Compartmentation of Nrf-2 redox control: regulation of cytoplasmic activation by glutathione and DNA binding by thioredoxin-1. Toxicol. Sci. 82, 308-17.
    • (2004) Toxicol. Sci , vol.82 , pp. 308-317
    • Hansen, J.M.1    Watson, W.H.2    Jones, D.P.3
  • 35
    • 0038393058 scopus 로고    scopus 로고
    • Oxidation of nuclear thioredoxin during oxidative stress
    • Watson, W. H., and Jones, D. P. (2003) Oxidation of nuclear thioredoxin during oxidative stress. FEBS Lett. 543, 144-7.
    • (2003) FEBS Lett , vol.543 , pp. 144-147
    • Watson, W.H.1    Jones, D.P.2
  • 36
    • 33746073706 scopus 로고    scopus 로고
    • Hydrogen peroxide and redox modulation sensitize primary mouse hepatocytes to TNF-induced apoptosis
    • Han, D., Hanawa, N., Saberi, B., and Kaplowitz, N. (2006) Hydrogen peroxide and redox modulation sensitize primary mouse hepatocytes to TNF-induced apoptosis. Free Radic Biol Med 41, 627-39.
    • (2006) Free Radic Biol Med , vol.41 , pp. 627-639
    • Han, D.1    Hanawa, N.2    Saberi, B.3    Kaplowitz, N.4
  • 37
    • 0031868230 scopus 로고    scopus 로고
    • Correlation between glutathione oxidation and trimerization of heat shock factor 1, an early step in stress induction of the Hsp response
    • Zou, J., Salminen, W. F., Roberts, S. M., and Voellmy, R. (1998) Correlation between glutathione oxidation and trimerization of heat shock factor 1, an early step in stress induction of the Hsp response. Cell Stress Chaperones 3, 130-41.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 130-141
    • Zou, J.1    Salminen, W.F.2    Roberts, S.M.3    Voellmy, R.4
  • 40
    • 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, 4928-44.
    • (2000) Eur. J. Biochem , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 41
    • 33744949848 scopus 로고    scopus 로고
    • Extracellular redox state: Refining the definition of oxidative stress in aging
    • Jones, D. P. (2006) Extracellular redox state: refining the definition of oxidative stress in aging. Rejuvenation Res. 9, 169-81.
    • (2006) Rejuvenation Res , vol.9 , pp. 169-181
    • Jones, D.P.1
  • 42
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function
    • Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., and Olson, A. J. (1998) Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function. Comput. Chem. 19, 1639-1662.
    • (1998) Comput. Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 43
    • 11144244006 scopus 로고    scopus 로고
    • Crystal structure of the Kelch domain of human Keapl
    • Li, X., Zhang, D., Hannink, M., and Beamer, L. J. (2004) Crystal structure of the Kelch domain of human Keapl. J. Biol. Chem. 279, 54750-8.
    • (2004) J. Biol. Chem , vol.279 , pp. 54750-54758
    • Li, X.1    Zhang, D.2    Hannink, M.3    Beamer, L.J.4
  • 45
    • 33847087446 scopus 로고
    • Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione
    • Szajewski, R. P., and Whitesides, G. M. (1980) Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione. J. Am. Chem. Soc. 102, 2011-2025.
    • (1980) J. Am. Chem. Soc , vol.102 , pp. 2011-2025
    • Szajewski, R.P.1    Whitesides, G.M.2
  • 46
    • 0001317229 scopus 로고
    • Rates of thiol disulfide interchange reactions between mono- and di-thiols and Ellman's reagent
    • Whitesides, G. M., Lilburn, J. E., and Szajewski, R. P. (1977) Rates of thiol disulfide interchange reactions between mono- and di-thiols and Ellman's reagent. J. Org. Chem. 42, 332-338.
    • (1977) J. Org. Chem , vol.42 , pp. 332-338
    • Whitesides, G.M.1    Lilburn, J.E.2    Szajewski, R.P.3
  • 47
    • 0041994595 scopus 로고
    • Nuclear magnetic resonance studies of thiol/disulfide chemistry. 2. Kinetics of symmetrical thiol/disulfide interchange reactions
    • Guo, W., Pleasants, J., and Rabenstein, D. L. (1990) Nuclear magnetic resonance studies of thiol/disulfide chemistry. 2. Kinetics of symmetrical thiol/disulfide interchange reactions. J. Org. Chem. 55, 373-376.
    • (1990) J. Org. Chem , vol.55 , pp. 373-376
    • Guo, W.1    Pleasants, J.2    Rabenstein, D.L.3
  • 48
    • 33751392287 scopus 로고
    • Kinetics and equilibria of thiol/disulfide interchange reactions of selected biological tiols and related molecules with oxidized glutathione
    • Keire, D. A., Strauss, E., Guo, W., Noszal, B., and Rabenstein, D. L. (1992) Kinetics and equilibria of thiol/disulfide interchange reactions of selected biological tiols and related molecules with oxidized glutathione. J. Org. Chem. 57, 123-127.
    • (1992) J. Org. Chem , vol.57 , pp. 123-127
    • Keire, D.A.1    Strauss, E.2    Guo, W.3    Noszal, B.4    Rabenstein, D.L.5
  • 50
    • 0019315391 scopus 로고
    • Rates of thiol-disulfide interchange reactions involving proteins and kinetic measurements of thiol pKa values
    • Shaked, Z., Szajewski, R. P., and Whitesides, G. M. (1980) Rates of thiol-disulfide interchange reactions involving proteins and kinetic measurements of thiol pKa values. Biochemistry 19, 4156-66.
    • (1980) Biochemistry , vol.19 , pp. 4156-4166
    • Shaked, Z.1    Szajewski, R.P.2    Whitesides, G.M.3
  • 51
    • 0035960648 scopus 로고    scopus 로고
    • Glutathionylation of the p50 subunit of NF-kappaB: A mechanism for redox-induced inhibition of DNA binding
    • Pineda-Molina, E., Klatt, P., Vazquez, J., Marina, A., Garcia de Lacoba, M., Perez-Sala, D., and Lamas, S. (2001) Glutathionylation of the p50 subunit of NF-kappaB: a mechanism for redox-induced inhibition of DNA binding. Biochemistry 40, 14134-42.
    • (2001) Biochemistry , vol.40 , pp. 14134-14142
    • Pineda-Molina, E.1    Klatt, P.2    Vazquez, J.3    Marina, A.4    Garcia de Lacoba, M.5    Perez-Sala, D.6    Lamas, S.7
  • 52
    • 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
    • Levonen, A. L., Landar, A., Ramachandran, A., Ceaser, E. K., Dickinson, D. A., Zanoni, G., Morrow, J. D., and Darley-Usmar, V. M. (2004) Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products. Biochem. J. 378, 373-82.
    • (2004) Biochem. J , vol.378 , pp. 373-382
    • Levonen, A.L.1    Landar, A.2    Ramachandran, A.3    Ceaser, E.K.4    Dickinson, D.A.5    Zanoni, G.6    Morrow, J.D.7    Darley-Usmar, V.M.8
  • 53
    • 46749152185 scopus 로고    scopus 로고
    • Activation of Nrf2 by arsenite and monomethylarsonous acid is independent of Keapl-C151: Enhanced Keapl-Cul3 interaction
    • Wang, X. J., Sun, Z., Chen, W., Li, Y., Villeneuve, N. F. and Zhang, D. D. (2008) Activation of Nrf2 by arsenite and monomethylarsonous acid is independent of Keapl-C151: enhanced Keapl-Cul3 interaction. Toxicol. Appl. Pharmacol. 230, 383-389.
    • (2008) Toxicol. Appl. Pharmacol , vol.230 , pp. 383-389
    • Wang, X.J.1    Sun, Z.2    Chen, W.3    Li, Y.4    Villeneuve, N.F.5    Zhang, D.D.6
  • 54
    • 34548577395 scopus 로고    scopus 로고
    • A mutation of Keapl found in breast cancer impairs its ability to repress Nrf2 activity
    • Nioi, P., and Nguyen, T. (2007) A mutation of Keapl found in breast cancer impairs its ability to repress Nrf2 activity. Biochem. Biophys. Res. Commun. 362, 816-21.
    • (2007) Biochem. Biophys. Res. Commun , vol.362 , pp. 816-821
    • Nioi, P.1    Nguyen, T.2
  • 56
    • 33747606306 scopus 로고    scopus 로고
    • Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling
    • Lo, S. C., Li, X., Henzl, M. T., Beamer, L. J., and Hannink, M. (2006) Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling. EMBO J. 25, 3605-17.
    • (2006) EMBO J , vol.25 , pp. 3605-3617
    • Lo, S.C.1    Li, X.2    Henzl, M.T.3    Beamer, L.J.4    Hannink, M.5
  • 57
  • 58
    • 33645455893 scopus 로고    scopus 로고
    • Effect of isothiocyanates on nuclear accumulation of NF-kappaB, Nrf2, and thioredoxin in caco-2 cells
    • Jakubikova, J., Sedlak, J., Bod'o, J., and Bao, Y. (2006) Effect of isothiocyanates on nuclear accumulation of NF-kappaB, Nrf2, and thioredoxin in caco-2 cells. J. Agric. Food Chem. 54, 1656-62.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 1656-1662
    • Jakubikova, J.1    Sedlak, J.2    Bod'o, J.3    Bao, Y.4
  • 59
    • 32944475745 scopus 로고    scopus 로고
    • Sulforaphane sensitizes tumor necrosis factor-related appptosis-inducing ligand (TRAIL)-resistant hepatoma cells to TRAIL-induced apoptosis through reactive oxygen species-mediated up-regulation of DR5
    • Kim, H., Kim, E. H., Eom, Y. W., Kim, W. H., Kwon, T. K., Lee, S. J., and Choi, K. S. (2006) Sulforaphane sensitizes tumor necrosis factor-related appptosis-inducing ligand (TRAIL)-resistant hepatoma cells to TRAIL-induced apoptosis through reactive oxygen species-mediated up-regulation of DR5. Cancer Res. 66, 1740-50.
    • (2006) Cancer Res , vol.66 , pp. 1740-1750
    • Kim, H.1    Kim, E.H.2    Eom, Y.W.3    Kim, W.H.4    Kwon, T.K.5    Lee, S.J.6    Choi, K.S.7
  • 60
    • 0034815141 scopus 로고    scopus 로고
    • Reactive oxygen species-related induction of multidrug resistance-associated protein 2 expression in primary hepatocytes exposed to sulforaphane
    • Payen, L., Courtois, A., Loewert, M., Guillouzo, A., and Fardel, O. (2001) Reactive oxygen species-related induction of multidrug resistance-associated protein 2 expression in primary hepatocytes exposed to sulforaphane. Biochem. Biophys. Res. Commun. 282, 257-63.
    • (2001) Biochem. Biophys. Res. Commun , vol.282 , pp. 257-263
    • Payen, L.1    Courtois, A.2    Loewert, M.3    Guillouzo, A.4    Fardel, O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.