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Volumn 78, Issue 21, 2004, Pages 11926-11938

Activation of transcription factor Nrf-2 and its downstream targets in response to Moloney murine leukemia virus ts1-induced thiol depletion and oxidative stress in astrocytes

Author keywords

[No Author keywords available]

Indexed keywords

ANTIPORTER; BUTHIONINE SULFOXIMINE; CHAPERONE; CYSTEINE; GLUCOSE REGULATED PROTEIN 78; GLUCOSE REGULATED PROTEIN 94; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; REACTIVE OXYGEN METABOLITE; THIOL; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR NRF 2; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN;

EID: 6344291668     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.21.11926-11938.2004     Document Type: Article
Times cited : (76)

References (84)
  • 1
    • 0021215013 scopus 로고
    • Transport of cystine and cysteine in mammalian cells
    • Bannai, S. 1984. Transport of cystine and cysteine in mammalian cells. Biochim. Biophys. Acta 779:289-306.
    • (1984) Biochim. Biophys. Acta , vol.779 , pp. 289-306
    • Bannai, S.1
  • 2
    • 0037593888 scopus 로고    scopus 로고
    • Redox regulation of cAMP-responsive element-binding protein and induction of manganous superoxide dismutase in nerve growth factor-dependent cell survival
    • Bedogni, B., G. Pani, R. Colavitti, A. Riccio, S. Borrello, M. Murphy, R. Smith, M. L. Eboli, and T. Galeotti. 2003. Redox regulation of cAMP-responsive element-binding protein and induction of manganous superoxide dismutase in nerve growth factor-dependent cell survival. J. Biol. Chem. 278:16510-16519.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16510-16519
    • Bedogni, B.1    Pani, G.2    Colavitti, R.3    Riccio, A.4    Borrello, S.5    Murphy, M.6    Smith, R.7    Eboli, M.L.8    Galeotti, T.9
  • 3
    • 0034672595 scopus 로고    scopus 로고
    • Impaired expression of glutathione synthetic enzyme genes in mice with targeted deletion of the Nrf2 basic-leucine zipper protein
    • Chan, J. Y., and M. Kwong. 2000. Impaired expression of glutathione synthetic enzyme genes in mice with targeted deletion of the Nrf2 basic-leucine zipper protein. Biochim. Biophys. Acta 1517:19-26.
    • (2000) Biochim. Biophys. Acta , vol.1517 , pp. 19-26
    • Chan, J.Y.1    Kwong, M.2
  • 4
    • 0034603123 scopus 로고    scopus 로고
    • Molecular mechanism of decreased glutathione content in human immunodeficiency virus type 1 Tat-transgenic mice
    • Choi, J., R. M. Liu, R. K. Kundu, F. Sangiorgi, W. Wu, R. Maxson, and H. J. Forman. 2000. Molecular mechanism of decreased glutathione content in human immunodeficiency virus type 1 Tat-transgenic mice. J. Biol. Chem. 275:3693-3698.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3693-3698
    • Choi, J.1    Liu, R.M.2    Kundu, R.K.3    Sangiorgi, F.4    Wu, W.5    Maxson, R.6    Forman, H.J.7
  • 5
    • 0025095302 scopus 로고
    • Role of amino acid transport and countertransport in nutrition and metabolism
    • Christensen, H. N. 1990. Role of amino acid transport and countertransport in nutrition and metabolism. Physiol. Rev. 70:43-77.
    • (1990) Physiol. Rev. , vol.70 , pp. 43-77
    • Christensen, H.N.1
  • 7
    • 0034743763 scopus 로고    scopus 로고
    • ts1 and LP-BM5: A comparison of two murine retrovirus models for HIV
    • Clark, S., J. Duggan, and J. Chakraborty. 2001. ts1 and LP-BM5: a comparison of two murine retrovirus models for HIV. Viral Immunol. 14:95-109.
    • (2001) Viral Immunol. , vol.14 , pp. 95-109
    • Clark, S.1    Duggan, J.2    Chakraborty, J.3
  • 8
    • 0034694871 scopus 로고    scopus 로고
    • Knockout of the mouse glutamate cysteine ligase catalytic subunit (Gclc) gene: Embryonic lethal when homozygous, and proposed model for moderate glutathione deficiency when heterozygous
    • Dalton, T. P., M. Z. Dieter, Y. Yang, H. G. Shertzer, and D. W. Nebert. 2000. Knockout of the mouse glutamate cysteine ligase catalytic subunit (Gclc) gene: embryonic lethal when homozygous, and proposed model for moderate glutathione deficiency when heterozygous. Biochem. Biophys. Res. Commun. 279:324-329.
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 324-329
    • Dalton, T.P.1    Dieter, M.Z.2    Yang, Y.3    Shertzer, H.G.4    Nebert, D.W.5
  • 9
    • 0029990439 scopus 로고    scopus 로고
    • Astrocytes protect neurons from hydrogen peroxide toxicity
    • Desagher, S., J. Glowinski, and J. Premont. 1996. Astrocytes protect neurons from hydrogen peroxide toxicity. J. Neurosci. 16:2553-2562.
    • (1996) J. Neurosci. , vol.16 , pp. 2553-2562
    • Desagher, S.1    Glowinski, J.2    Premont, J.3
  • 10
    • 0242492706 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is a determinant of retrovirus-induced spongiform neurodegeneration
    • Dimcheff, D. E., S. Askovic, A. H. Baker, C. Johnson-Fowler, and J. L. Portis. 2003. Endoplasmic reticulum stress is a determinant of retrovirus-induced spongiform neurodegeneration. J. Virol. 77:12617-12629.
    • (2003) J. Virol. , vol.77 , pp. 12617-12629
    • Dimcheff, D.E.1    Askovic, S.2    Baker, A.H.3    Johnson-Fowler, C.4    Portis, J.L.5
  • 11
    • 0033876436 scopus 로고    scopus 로고
    • Glutathione metabolism and oxidative stress in neurodegeneration
    • Dringen, R. 2000. Glutathione metabolism and oxidative stress in neurodegeneration. Eur. J. Biochem. 267:4903.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4903
    • Dringen, R.1
  • 12
    • 0034672943 scopus 로고    scopus 로고
    • Metabolism and functions of glutathione in brain
    • Dringen, R. 2000. Metabolism and functions of glutathione in brain. Prog. Neurobiol. 62:649-671.
    • (2000) Prog. Neurobiol. , vol.62 , pp. 649-671
    • Dringen, R.1
  • 13
    • 0033899176 scopus 로고    scopus 로고
    • Glutathione metabolism in brain metabolic interaction between astrocytes and neurons in the defense against reactive oxygen species
    • Dringen, R., J. M. Gutterer, and J. Hirrlinger. 2000. Glutathione metabolism in brain metabolic interaction between astrocytes and neurons in the defense against reactive oxygen species. Eur. J. Biochem. 267:4912-4916.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4912-4916
    • Dringen, R.1    Gutterer, J.M.2    Hirrlinger, J.3
  • 14
    • 0030852097 scopus 로고    scopus 로고
    • Involvement of glutathione peroxidase and catalase in the disposal of exogenous hydrogen peroxide by cultured astroglial cells
    • Dringen, R., and B. Hamprecht. 1997. Involvement of glutathione peroxidase and catalase in the disposal of exogenous hydrogen peroxide by cultured astroglial cells. Brain Res. 759:67-75.
    • (1997) Brain Res. , vol.759 , pp. 67-75
    • Dringen, R.1    Hamprecht, B.2
  • 15
    • 0038636003 scopus 로고    scopus 로고
    • Glutathione pathways in the brain
    • Dringen, R., and J. Hirrlinger. 2003. Glutathione pathways in the brain. Biol. Chem. 384:505-516.
    • (2003) Biol. Chem. , vol.384 , pp. 505-516
    • Dringen, R.1    Hirrlinger, J.2
  • 16
    • 0032974143 scopus 로고    scopus 로고
    • The glutathione system of peroxide detoxification is less efficient in neurons than in astroglial cells
    • Dringen, R., L. Kussmaul, J. M. Gutterer, J. Hirrlinger, and B. Hamprecht. 1999. The glutathione system of peroxide detoxification is less efficient in neurons than in astroglial cells. J. Neurochem. 72:2523-2530.
    • (1999) J. Neurochem. , vol.72 , pp. 2523-2530
    • Dringen, R.1    Kussmaul, L.2    Gutterer, J.M.3    Hirrlinger, J.4    Hamprecht, B.5
  • 17
    • 0024595926 scopus 로고
    • Low concentrations of acid-soluble thiol (cysteine) in the blood plasma of HIV-1-infected patients
    • Eck, H. P., H. Gmunder, M. Hartmann, D. Petzoldt, V. Daniel, and W. Droge. 1989. Low concentrations of acid-soluble thiol (cysteine) in the blood plasma of HIV-1-infected patients. Biol. Chem. Hoppe-Seyler 370:101-108.
    • (1989) Biol. Chem. Hoppe-Seyler , vol.370 , pp. 101-108
    • Eck, H.P.1    Gmunder, H.2    Hartmann, M.3    Petzoldt, D.4    Daniel, V.5    Droge, W.6
  • 18
    • 0142089055 scopus 로고    scopus 로고
    • Oxidative signaling and glutathione synthesis
    • Forman, H. J., and D. A. Dickinson. 2003. Oxidative signaling and glutathione synthesis. Biofactors 17:1-12.
    • (2003) Biofactors , vol.17 , pp. 1-12
    • Forman, H.J.1    Dickinson, D.A.2
  • 19
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M. J., and J. Sambrook. 1992. Protein folding in the cell. Nature 355:33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 20
    • 18244385536 scopus 로고    scopus 로고
    • Protein glutathionylation: Coupling and uncoupling of glutathione to protein thiol groups in lymphocytes under oxidative stress and HIV infection
    • Ghezzi, P., B. Romines, M. Fratelli, I. Eberini, E. Gianazza, S. Casagrande, T. Laragione, M. Mengozzi, and L. A. Herzenberg. 2002. Protein glutathionylation: coupling and uncoupling of glutathione to protein thiol groups in lymphocytes under oxidative stress and HIV infection. Mol. Immunol. 38:773-780.
    • (2002) Mol. Immunol. , vol.38 , pp. 773-780
    • Ghezzi, P.1    Romines, B.2    Fratelli, M.3    Eberini, I.4    Gianazza, E.5    Casagrande, S.6    Laragione, T.7    Mengozzi, M.8    Herzenberg, L.A.9
  • 21
    • 0346271905 scopus 로고    scopus 로고
    • Cross-talk between reactive oxygen species and calcium in living cells
    • Moscow
    • Gordeeva, A. V., R. A. Zvyagilskaya, and Y. A. Labas. 2003. Cross-talk between reactive oxygen species and calcium in living cells. Biochemistry (Moscow) 68:1077-1080.
    • (2003) Biochemistry , vol.68 , pp. 1077-1080
    • Gordeeva, A.V.1    Zvyagilskaya, R.A.2    Labas, Y.A.3
  • 22
    • 0142210179 scopus 로고    scopus 로고
    • Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria
    • Han, D., R. Canali, D. Rettori, and N. Kaplowitz. 2003. Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria. Mol. Pharmacol. 64:1136-1144.
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1136-1144
    • Han, D.1    Canali, R.2    Rettori, D.3    Kaplowitz, N.4
  • 23
    • 0034717329 scopus 로고    scopus 로고
    • Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages
    • Ishii, T., K. Itoh, S. Takahashi, H. Sato, T. Yanagawa, Y. Katoh, S. Bannai, and M. Yamamoto. 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
  • 24
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh, K., N. Wakabayashi, Y. Katoh, T. Ishii, K. Igarashi, J. D. Engel, and M. Yamamoto. 1999. Keap1 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
  • 25
    • 12444257799 scopus 로고    scopus 로고
    • Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles
    • Itoh, K., N. Wakabayashi, Y. Katoh, T. Ishii, T. O'Connor, and M. Yamamoto. 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
  • 26
    • 0033800922 scopus 로고    scopus 로고
    • Regulation of genes encoding NAD(P)H:quinone oxidoreductases
    • Jaiswal, A. K. 2000. Regulation of genes encoding NAD(P)H:quinone oxidoreductases. Free Radic. Biol. Med. 29:254-262.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 254-262
    • Jaiswal, A.K.1
  • 27
    • 0030570278 scopus 로고    scopus 로고
    • NAC: First controlled trial, positive results
    • James, J. S. 1996. NAC: first controlled trial, positive results. AIDS Treat. News 250:1-3.
    • (1996) AIDS Treat. News , vol.250 , pp. 1-3
    • James, J.S.1
  • 28
    • 0142010013 scopus 로고    scopus 로고
    • General aspects of neurodegeneration
    • Jellinger, K. A. 2003. General aspects of neurodegeneration. J. Neural Transm. Suppl. 65:101-144.
    • (2003) J. Neural Transm. Suppl. , vol.65 , pp. 101-144
    • Jellinger, K.A.1
  • 30
    • 0001111364 scopus 로고    scopus 로고
    • Management of oxidative stress in the CNS: The many roles of glutathione
    • Juurlink, B. H. 1999. Management of oxidative stress in the CNS: the many roles of glutathione. Neurotox. Res. 1:119-140.
    • (1999) Neurotox. Res. , vol.1 , pp. 119-140
    • Juurlink, B.H.1
  • 31
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman, R. J. 1999. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13:1211-1233.
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 32
    • 3042638296 scopus 로고    scopus 로고
    • Activation of endoplasmic reticulum stress signaling pathway is associated with neuronal degeneration in MoMuLV-ts1-induced spongiform encephalomyelopathy
    • Kim, H. T., K. Waters, G. Stoica, W. Qiang, N. Liu, V. L. Scofield, and P. K. Y. Wong. 2004. Activation of endoplasmic reticulum stress signaling pathway is associated with neuronal degeneration in MoMuLV-ts1-induced spongiform encephalomyelopathy. Lab. Investig. 84:816-827.
    • (2004) Lab. Investig. , vol.84 , pp. 816-827
    • Kim, H.T.1    Waters, K.2    Stoica, G.3    Qiang, W.4    Liu, N.5    Scofield, V.L.6    Wong, P.K.Y.7
  • 33
    • 0344406145 scopus 로고    scopus 로고
    • Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders
    • Krapfenbauer, K., E. Engidawork, N. Cairns, M. Fountoulakis, and G. Lubec. 2003. Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders. Brain Res. 967:152-160.
    • (2003) Brain Res. , vol.967 , pp. 152-160
    • Krapfenbauer, K.1    Engidawork, E.2    Cairns, N.3    Fountoulakis, M.4    Lubec, G.5
  • 34
    • 0025313038 scopus 로고
    • Organometal-induced increases in oxygen reactive species: The potential of 2′,7′-dichlorofluorescin diacetate as an index of neurotoxic damage
    • LeBel, C. P., S. F. Ali, M. McKee, and S. C. Bondy. 1990. Organometal-induced increases in oxygen reactive species: the potential of 2′,7′-dichlorofluorescin diacetate as an index of neurotoxic damage. Toxicol. Appl. Pharmacol. 104:17-24.
    • (1990) Toxicol. Appl. Pharmacol. , vol.104 , pp. 17-24
    • LeBel, C.P.1    Ali, S.F.2    McKee, M.3    Bondy, S.C.4
  • 35
    • 0035423875 scopus 로고    scopus 로고
    • The glucose-regulated proteins: Stress induction and clinical applications
    • Lee, A. S. 2001. The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem. Sci. 26:504-510.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 504-510
    • Lee, A.S.1
  • 36
    • 0038146898 scopus 로고    scopus 로고
    • Identification of the NF-E2-related factor-2-dependent genes conferring protection against oxidative stress in primary cortical astrocytes using oligonucleotide microarray analysis
    • Lee, J. M., M. J. Calkins, K. Chan, Y. W. Kan, and J. A. Johnson. 2003. Identification of the NF-E2-related factor-2-dependent genes conferring protection against oxidative stress in primary cortical astrocytes using oligonucleotide microarray analysis. J. Biol. Chem. 278:12029-12038.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12029-12038
    • Lee, J.M.1    Calkins, M.J.2    Chan, K.3    Kan, Y.W.4    Johnson, J.A.5
  • 37
    • 0031058105 scopus 로고    scopus 로고
    • Establishment and characterization of conditionally immortalized astrocytes to study their interaction with ts1, a neuropathogenic mutant of Moloney murine leukemia virus
    • Lin, Y. C., C. W. Chow, P. H. Yuen, W. S. Lynn, and P. K. Y. Wong. 1997. Establishment and characterization of conditionally immortalized astrocytes to study their interaction with ts1, a neuropathogenic mutant of Moloney murine leukemia virus. J. Neurovirol. 3:28-37.
    • (1997) J. Neurovirol. , vol.3 , pp. 28-37
    • Lin, Y.C.1    Chow, C.W.2    Yuen, P.H.3    Lynn, W.S.4    Wong, P.K.Y.5
  • 38
    • 3042847441 scopus 로고    scopus 로고
    • Possible involvement of both endoplasmic reticulum-and mitochondria-dependent pathways in MoMuLV-ts1-induced apoptosis in astrocytes
    • Liu, N., X. Kuang, H.-T. Kim, G. Stoica, W. Qiang, V. L. Scofield, and P. K. Y. Wong. 2004. Possible involvement of both endoplasmic reticulum-and mitochondria-dependent pathways in MoMuLV-ts1-induced apoptosis in astrocytes. J. Neurovirol. 10:189-198.
    • (2004) J. Neurovirol. , vol.10 , pp. 189-198
    • Liu, N.1    Kuang, X.2    Kim, H.-T.3    Stoica, G.4    Qiang, W.5    Scofield, V.L.6    Wong, P.K.Y.7
  • 39
    • 0032435501 scopus 로고    scopus 로고
    • Regulation of hepatic glutathione synthesis
    • Lu, S. C. 1998. Regulation of hepatic glutathione synthesis. Semin. Liver Dis. 18:331-343.
    • (1998) Semin. Liver Dis. , vol.18 , pp. 331-343
    • Lu, S.C.1
  • 40
    • 0031664004 scopus 로고    scopus 로고
    • Neuroimmunopathogenesis of ts1 MoMuLV infection
    • Lynn, W. S., and P. K. Y. Wong. 1998. Neuroimmunopathogenesis of ts1 MoMuLV infection. Neuroimmunomodulation 5:248-260.
    • (1998) Neuroimmunomodulation , vol.5 , pp. 248-260
    • Lynn, W.S.1    Wong, P.K.Y.2
  • 42
    • 0030911678 scopus 로고    scopus 로고
    • Regulation of catalases in Arabidopsis
    • McClung, C. R. 1997. Regulation of catalases in Arabidopsis. Free Radic. Biol. Med. 23:489-496.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 489-496
    • McClung, C.R.1
  • 43
    • 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., K. Itoh, M. Yamamoto, and J. D. Hayes. 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
  • 44
    • 0032126145 scopus 로고    scopus 로고
    • Expression and purification of human gamma-glutamylcysteine synthetase
    • Misra, I., and O. W. Griffith. 1998. Expression and purification of human gamma-glutamylcysteine synthetase. Protein Expr. Purif. 13:268-276.
    • (1998) Protein Expr. Purif. , vol.13 , pp. 268-276
    • Misra, I.1    Griffith, O.W.2
  • 45
    • 0028061444 scopus 로고
    • Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region
    • Moi, P., K. Chan, I. Asunis, A. Cao, and Y. W. Kan. 1994. Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region. Proc. Natl. Acad. Sci. USA 91:9926-9930.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9926-9930
    • Moi, P.1    Chan, K.2    Asunis, I.3    Cao, A.4    Kan, Y.W.5
  • 48
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • Nakagawa, T., H. Zhu, N. Morishima, E. Li, J. Xu, B. A. Yankner, and J. Yuan. 2000. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β. Nature 403:98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 50
    • 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., P. J. Sherratt, H. C. Huang, C. S. Yang, and C. B. Pickett. 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
  • 51
    • 0036708902 scopus 로고    scopus 로고
    • Antioxidants and oxidants regulated signal transduction pathways
    • Owuor, E. D., and A. N. Kong. 2002. Antioxidants and oxidants regulated signal transduction pathways. Biochem. Pharmacol. 64:765-770.
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 765-770
    • Owuor, E.D.1    Kong, A.N.2
  • 52
    • 0034319169 scopus 로고    scopus 로고
    • Role of calcium in neuronal cell injury: Which subcellular compartment is involved?
    • Paschen, W. 2000. Role of calcium in neuronal cell injury: which subcellular compartment is involved? Brain Res. Bull. 53:409-413.
    • (2000) Brain Res. Bull. , vol.53 , pp. 409-413
    • Paschen, W.1
  • 53
    • 0029027838 scopus 로고
    • Electrophile and antioxidant regulation of enzymes that detoxify carcinogens
    • Prestera, T., and P. Talalay. 1995. Electrophile and antioxidant regulation of enzymes that detoxify carcinogens. Proc. Natl. Acad. Sci. USA 92:8965-8969.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8965-8969
    • Prestera, T.1    Talalay, P.2
  • 54
    • 0031000480 scopus 로고    scopus 로고
    • Increase of manganese superoxide dismutase, but not of Cu/Zn-SOD, in experimental optic neuritis
    • Qi, X., J. Guy, H. Nick, J. Valentine, and N. Rao. 1997. Increase of manganese superoxide dismutase, but not of Cu/Zn-SOD, in experimental optic neuritis. Investig. Ophthalmol. Vis. Sci. 38:1203-1212.
    • (1997) Investig. Ophthalmol. Vis. Sci. , vol.38 , pp. 1203-1212
    • Qi, X.1    Guy, J.2    Nick, H.3    Valentine, J.4    Rao, N.5
  • 55
    • 0141705360 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and reactive oxygen species in excitotoxicity and apoptosis: Implications for the pathogenesis of neurodegenerative diseases
    • Rego, A. C., and C. R. Oliveira. 2003. Mitochondrial dysfunction and reactive oxygen species in excitotoxicity and apoptosis: implications for the pathogenesis of neurodegenerative diseases. Neurochem. Res. 28:1563-1574.
    • (2003) Neurochem. Res. , vol.28 , pp. 1563-1574
    • Rego, A.C.1    Oliveira, C.R.2
  • 57
    • 0029988384 scopus 로고    scopus 로고
    • Glutathione efflux from cultured astrocytes
    • Sagara, J., N. Makino, and S. Bannai. 1996. Glutathione efflux from cultured astrocytes. J. Neurochem. 66:1876-1881.
    • (1996) J. Neurochem. , vol.66 , pp. 1876-1881
    • Sagara, J.1    Makino, N.2    Bannai, S.3
  • 59
    • 0033597349 scopus 로고    scopus 로고
    • Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins
    • Sato, H., M. Tamba, T. Ishii, and S. Bannai. 1999. Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins. J. Biol. Chem. 274:11455-11458.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11455-11458
    • Sato, H.1    Tamba, M.2    Ishii, T.3    Bannai, S.4
  • 60
    • 0023956565 scopus 로고
    • An assay for the detection of superoxide dismutase in individual Escherichia coli colonies
    • Schiavone, J. R., and H. M. Hassan. 1988. An assay for the detection of superoxide dismutase in individual Escherichia coli colonies. Anal. Biochem. 168:455-461.
    • (1988) Anal. Biochem. , vol.168 , pp. 455-461
    • Schiavone, J.R.1    Hassan, H.M.2
  • 61
    • 0029984062 scopus 로고    scopus 로고
    • Antioxidant and redox regulation of gene transcription
    • Sen, C. K., and L. Packer. 1996. Antioxidant and redox regulation of gene transcription. FASEB J. 10:709-720.
    • (1996) FASEB J. , vol.10 , pp. 709-720
    • Sen, C.K.1    Packer, L.2
  • 63
    • 0037996661 scopus 로고    scopus 로고
    • Coordinate regulation of glutathione biosynthesis and release by Nrf2-expressing glia potently protects neurons from oxidative stress
    • Shih, A. Y., D. A. Johnson, G. Wong, A. D. Kraft, L. Jiang, H. Erb, J. A. Johnson, and T. H. Murphy. 2003. Coordinate regulation of glutathione biosynthesis and release by Nrf2-expressing glia potently protects neurons from oxidative stress. J. Neurosci. 23:3394-3406.
    • (2003) J. Neurosci. , vol.23 , pp. 3394-3406
    • Shih, A.Y.1    Johnson, D.A.2    Wong, G.3    Kraft, A.D.4    Jiang, L.5    Erb, H.6    Johnson, J.A.7    Murphy, T.H.8
  • 64
    • 0027408211 scopus 로고
    • Correlation of specific virus-astrocyte interactions and cytopathic effects induced by ts1, a neurovirulent mutant of Moloney murine leukemia virus
    • Shikova, E., Y. C. Lin, K. Saha, B. R. Brooks, and P. K. Wong. 1993. Correlation of specific virus-astrocyte interactions and cytopathic effects induced by ts1, a neurovirulent mutant of Moloney murine leukemia virus. J. Virol. 67:1137-1147.
    • (1993) J. Virol. , vol.67 , pp. 1137-1147
    • Shikova, E.1    Lin, Y.C.2    Saha, K.3    Brooks, B.R.4    Wong, P.K.5
  • 66
    • 0036570346 scopus 로고    scopus 로고
    • Glutamate-cysteine ligase modifier subunit: Mouse Gclm gene structure and regulation by agents that cause oxidative stress
    • Solis, W. A., T. P. Dalton, M. Z. Dieter, S. Freshwater, J. M. Harrer, L. He, H. G. Shertzer, and D. W. Nebert. 2002. Glutamate-cysteine ligase modifier subunit: mouse Gclm gene structure and regulation by agents that cause oxidative stress. Biochem. Pharmacol. 63:1739-1754.
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 1739-1754
    • Solis, W.A.1    Dalton, T.P.2    Dieter, M.Z.3    Freshwater, S.4    Harrer, J.M.5    He, L.6    Shertzer, H.G.7    Nebert, D.W.8
  • 67
    • 0026647062 scopus 로고
    • Temporal central and peripheral nervous system changes induced by a paralytogenic mutant of Moloney murine leukemia virus TB
    • Stoica, G., O. Illanes, S. I. Tasca, and P. K. Y. Wong. 1993. Temporal central and peripheral nervous system changes induced by a paralytogenic mutant of Moloney murine leukemia virus TB. Lab. Investig. 66:427-436.
    • (1993) Lab. Investig. , vol.66 , pp. 427-436
    • Stoica, G.1    Illanes, O.2    Tasca, S.I.3    Wong, P.K.Y.4
  • 68
    • 0033981697 scopus 로고    scopus 로고
    • Motor neuronal loss and neurofilament-ubiquitin alteration in MoMuLV-ts1 encephalopathy
    • Berlin
    • Stoica, G., S. I. Tasca, and P. K. Y. Wong. 2000. Motor neuronal loss and neurofilament-ubiquitin alteration in MoMuLV-ts1 encephalopathy. Acta Neuropathol. (Berlin) 99:238-244.
    • (2000) Acta Neuropathol. , vol.99 , pp. 238-244
    • Stoica, G.1    Tasca, S.I.2    Wong, P.K.Y.3
  • 69
    • 0347695007 scopus 로고    scopus 로고
    • Reduction of calcium release from the endoplasmic reticulum could only provide partial neuroprotection against beta-amyloid peptide toxicity
    • Suen, K. C., K. F. Lin, W. Elyaman, K. F. So, R. C. Chang, and J. Hugon. 2003. Reduction of calcium release from the endoplasmic reticulum could only provide partial neuroprotection against beta-amyloid peptide toxicity. J. Neurochem. 87:1413-1426.
    • (2003) J. Neurochem. , vol.87 , pp. 1413-1426
    • Suen, K.C.1    Lin, K.F.2    Elyaman, W.3    So, K.F.4    Chang, R.C.5    Hugon, J.6
  • 70
    • 0034754762 scopus 로고    scopus 로고
    • Protective effect of glutathione in HIV-1 lytic peptide 1-induced cell death in human neuronal cells
    • Sung, J. H., S. A. Shin, H. K. Park, R. C. Montelaro, and Y. H. Chong. 2001. Protective effect of glutathione in HIV-1 lytic peptide 1-induced cell death in human neuronal cells. J. Neurovirol. 7:454-465.
    • (2001) J. Neurovirol. , vol.7 , pp. 454-465
    • Sung, J.H.1    Shin, S.A.2    Park, H.K.3    Montelaro, R.C.4    Chong, Y.H.5
  • 71
    • 0025049023 scopus 로고
    • env alters the neurovirulence of ts1, a mutant of Moloney murine leukemia virus TB
    • env alters the neurovirulence of ts1, a mutant of Moloney murine leukemia virus TB. J. Virol. 64:5241-5249.
    • (1990) J. Virol. , vol.64 , pp. 5241-5249
    • Szurek, P.F.1    Floyd, E.2    Yuen, P.H.3    Wong, P.K.Y.4
  • 72
    • 0025169836 scopus 로고
    • env, and neurovirulence of ts1, a mutant of Moloney murine leukemia virus TB
    • env, and neurovirulence of ts1, a mutant of Moloney murine leukemia virus TB. J. Virol. 64:467-475.
    • (1990) J. Virol. , vol.64 , pp. 467-475
    • Szurek, P.F.1    Yuen, P.H.2    Ball, J.K.3    Wong, P.K.Y.4
  • 73
    • 0023882059 scopus 로고
    • Identification of point mutations in the envelope gene of Moloney murine leukemia virus TB temperature-sensitive paralytogenic mutant ts1: Molecular determinants for neurovirulence
    • Szurek, P. F., P. H. Yuen, R. Jerzy, and P. K. Y. Wong. 1988. Identification of point mutations in the envelope gene of Moloney murine leukemia virus TB temperature-sensitive paralytogenic mutant ts1: molecular determinants for neurovirulence. J. Virol. 62:357-360.
    • (1988) J. Virol. , vol.62 , pp. 357-360
    • Szurek, P.F.1    Yuen, P.H.2    Jerzy, R.3    Wong, P.K.Y.4
  • 74
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor, J. P., J. Hardy, and K. H. Fischbeck. 2002. Toxic proteins in neurodegenerative disease. Science 296:1991-1995.
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 75
    • 0032741568 scopus 로고    scopus 로고
    • Induction of glutamate-cysteine ligase (gamma-glutamylcysteine synthetase) in the brains of adult female mice subchronically exposed to methylmercury
    • Thompson, S. A., C. C. White, C. M. Krejsa, D. Diaz, J. S. Woods, D. L. Eaton, and T. J. Kavanagh. 1999. Induction of glutamate-cysteine ligase (gamma-glutamylcysteine synthetase) in the brains of adult female mice subchronically exposed to methylmercury. Toxicol. Lett. 110:1-9.
    • (1999) Toxicol. Lett. , vol.110 , pp. 1-9
    • Thompson, S.A.1    White, C.C.2    Krejsa, C.M.3    Diaz, D.4    Woods, J.S.5    Eaton, D.L.6    Kavanagh, T.J.7
  • 76
  • 77
    • 0013002323 scopus 로고    scopus 로고
    • Manganese superoxide dismutase induction during measles virus infection
    • Wang, M., J. M. Howell, J. E. Libbey, J. A. Tainer, and R. S. Fujinami. 2003. Manganese superoxide dismutase induction during measles virus infection. J. Med. Virol. 70:470-474.
    • (2003) J. Med. Virol. , vol.70 , pp. 470-474
    • Wang, M.1    Howell, J.M.2    Libbey, J.E.3    Tainer, J.A.4    Fujinami, R.S.5
  • 78
    • 0001412747 scopus 로고    scopus 로고
    • Astrocytes provide cysteine to neurons by releasing glutathione
    • Wang, X. F., and M. S. Cynader. 2000. Astrocytes provide cysteine to neurons by releasing glutathione. J. Neurochem. 74:1434-1442.
    • (2000) J. Neurochem. , vol.74 , pp. 1434-1442
    • Wang, X.F.1    Cynader, M.S.2
  • 79
    • 0022197275 scopus 로고
    • ts1, a paralytogenic mutant of Moloney murine leukemia virus TB. has an enhanced ability to replicate in the central nervous system and primary nerve cell culture
    • Wong, P. K. Y., C. Knupp, P. H. Yuen, M. M. Soong, J. F. Zachary, and W. A. Tompkins. 1985. ts1, a paralytogenic mutant of Moloney murine leukemia virus TB. has an enhanced ability to replicate in the central nervous system and primary nerve cell culture. J. Virol. 55:760-767.
    • (1985) J. Virol. , vol.55 , pp. 760-767
    • Wong, P.K.Y.1    Knupp, C.2    Yuen, P.H.3    Soong, M.M.4    Zachary, J.F.5    Tompkins, W.A.6
  • 80
    • 0003029344 scopus 로고    scopus 로고
    • ts1 MoMuLV: A murine model of neuroimmunodegeneration
    • P. K. Y. Wong and W. S. Lynn (ed.). R. G. Landes, Austin, Tex.
    • Wong, P. K. Y., W. S. Lynn, Y. C. Lin, W. Choe, and P. H. Yuen. 1998. ts1 MoMuLV: a murine model of neuroimmunodegeneration, p. 75-93. In P. K. Y. Wong and W. S. Lynn (ed.). Neuroimmunodegeneration. R. G. Landes, Austin, Tex.
    • (1998) Neuroimmunodegeneration , pp. 75-93
    • Wong, P.K.Y.1    Lynn, W.S.2    Lin, Y.C.3    Choe, W.4    Yuen, P.H.5
  • 81
    • 0019423424 scopus 로고
    • Replication of murine leukemia virus in heterologous cells: Interaction between ecotropic and xenotropic virus
    • Wong, P. K. Y., M. M. Soong, and P. H. Yuen. 1981. Replication of murine leukemia virus in heterologous cells: interaction between ecotropic and xenotropic virus. Virology 109:366-378.
    • (1981) Virology , vol.109 , pp. 366-378
    • Wong, P.K.Y.1    Soong, M.M.2    Yuen, P.H.3
  • 82
    • 0031447041 scopus 로고    scopus 로고
    • Endogenous synthesis of arginine plays an important role in maintaining arginine homeostasis in postweaning growing pigs
    • Wu, G., P. K. Davis, N. E. Flynn, D. A. Knabe, and J. T. Davidson. 1997. Endogenous synthesis of arginine plays an important role in maintaining arginine homeostasis in postweaning growing pigs. J. Nutr. 127:2342-2349.
    • (1997) J. Nutr. , vol.127 , pp. 2342-2349
    • Wu, G.1    Davis, P.K.2    Flynn, N.E.3    Knabe, D.A.4    Davidson, J.T.5
  • 83
    • 0022494858 scopus 로고
    • The neurovirulent determinants of tsl, a paralytogenic mutant of Moloney murine leukemia virus TB, are localized in at least two functionally distinct regions of the genome
    • Yuen, P. H., E. Tzeng, C. Knupp, and P. K. Y. Wong. 1986. The neurovirulent determinants of tsl, a paralytogenic mutant of Moloney murine leukemia virus TB, are localized in at least two functionally distinct regions of the genome. J. Virol. 59:59-65.
    • (1986) J. Virol. , vol.59 , pp. 59-65
    • Yuen, P.H.1    Tzeng, E.2    Knupp, C.3    Wong, P.K.Y.4
  • 84
    • 0022515980 scopus 로고
    • Noninflammatory spongiform polioencephalomyelopathy caused by a neurotropic temperature-sensitive mutant of Moloney murine leukemia virus TB
    • Zachary, J. F., C. J. Knupp, and P. K. Y. Wong. 1986. Noninflammatory spongiform polioencephalomyelopathy caused by a neurotropic temperature- sensitive mutant of Moloney murine leukemia virus TB. Am. J. Pathol. 124:457-468.
    • (1986) Am. J. Pathol. , vol.124 , pp. 457-468
    • Zachary, J.F.1    Knupp, C.J.2    Wong, P.K.Y.3


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