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Volumn 25, Issue 9-10, 2000, Pages 1315-1341

NO Synthase and NO-Dependent Signal Pathways in Brain Aging and Neurodegenerative Disorders: The Role of Oxidant/Antioxidant Balance

Author keywords

Aging; CO; Heat shock proteins; Neurodegeneartive disorders; NO synthase; Oxidative stress; Signal transduction

Indexed keywords

ANTIOXIDANT; HEAT SHOCK PROTEIN; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; OXIDIZING AGENT;

EID: 0034304391     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/a:1007604414773     Document Type: Article
Times cited : (273)

References (245)
  • 1
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell, B. 1992. Reactive oxygen species and the central nervous system. J. Neurochem. 59:1609-1623.
    • (1992) J. Neurochem. , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 2
    • 0032823769 scopus 로고    scopus 로고
    • Antioxidant defence mechanisms: From the beginning to the end (of the beginning)
    • Halliwell, B. 1999 Antioxidant defence mechanisms: from the beginning to the end (of the beginning). Free Radie. Res. 31:261-272.
    • (1999) Free Radie. Res. , vol.31 , pp. 261-272
    • Halliwell, B.1
  • 3
    • 0031031920 scopus 로고    scopus 로고
    • Reactive oxygen species and the neurodegenerative disorders
    • Knight, A. J. 1997. Reactive oxygen species and the neurodegenerative disorders. Ann. Clin. Lab. Sci. 27:11-25.
    • (1997) Ann. Clin. Lab. Sci. , vol.27 , pp. 11-25
    • Knight, A.J.1
  • 4
    • 0032557511 scopus 로고    scopus 로고
    • Energy thresholds in brain mitochondria
    • Davey, G. P., Peuchen, S., and Clark, J. B. 1998. Energy thresholds in brain mitochondria. J. Biol. Chem. 273:12753-12757.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12753-12757
    • Davey, G.P.1    Peuchen, S.2    Clark, J.B.3
  • 5
    • 0026594669 scopus 로고
    • OxyR: A regulator of antioxidant genes
    • Storz, G. and Tartaglia, L. A. 1992. OxyR: a regulator of antioxidant genes. J. Nutr. 122:627-639.
    • (1992) J. Nutr. , vol.122 , pp. 627-639
    • Storz, G.1    Tartaglia, L.A.2
  • 7
    • 0034602776 scopus 로고    scopus 로고
    • The Nef protein of HIV-1 associates with rafts and primes T cells for activation
    • Wang, J. K., Kiyokawa, E., Verdin, E., and Trono, D. 2000. The Nef protein of HIV-1 associates with rafts and primes T cells for activation. Proc. Natl. Acad. Sci. USA 97:394-399.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 394-399
    • Wang, J.K.1    Kiyokawa, E.2    Verdin, E.3    Trono, D.4
  • 8
    • 3542995049 scopus 로고    scopus 로고
    • Stress-inducible response and heat shock proteins: New pharmacologic targets for cytoprotection
    • Morimoto, R. I. and Santoro, M. G. 1998. Stress-inducible response and heat shock proteins: new pharmacologic targets for cytoprotection. Nature Biotechnol. 16:833-838.
    • (1998) Nature Biotechnol. , vol.16 , pp. 833-838
    • Morimoto, R.I.1    Santoro, M.G.2
  • 9
    • 0033990336 scopus 로고    scopus 로고
    • Heat shock and the control of the stress response
    • Santoro, M. G. 2000. Heat shock and the control of the stress response. Biochem. Pharmacol. 59:55-63.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 55-63
    • Santoro, M.G.1
  • 10
    • 0034607632 scopus 로고    scopus 로고
    • Endothelial Heme oxygenase-1 induction by hypoxia: Modulation by inducible nitric oxide synthase (iNOS) and S-nitrosothiols
    • Motterlini, R., Foresti, R., Bassi, R., Calabrese, V., Clark, J. E., and Green, C. J. 2000. Endothelial Heme oxygenase-1 induction by hypoxia: modulation by inducible nitric oxide synthase (iNOS) and S-nitrosothiols. J. Biol. Chem. 275:13613-13620.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13613-13620
    • Motterlini, R.1    Foresti, R.2    Bassi, R.3    Calabrese, V.4    Clark, J.E.5    Green, C.J.6
  • 11
    • 0033969903 scopus 로고    scopus 로고
    • Reduced glutathione oxidation ratio and 8 ohdG accumulation by mild ischemic pretreatment
    • Baek, S. H., Kim, J. Y., Choi, J. H., Park, E. M., Han, M. Y., Kim, C. H., Ahn, Y. S., and Park, Y. M. 2000. Reduced glutathione oxidation ratio and 8 ohdG accumulation by mild ischemic pretreatment. Brain. Res. 856:28-36.
    • (2000) Brain. Res. , vol.856 , pp. 28-36
    • Baek, S.H.1    Kim, J.Y.2    Choi, J.H.3    Park, E.M.4    Han, M.Y.5    Kim, C.H.6    Ahn, Y.S.7    Park, Y.M.8
  • 12
    • 0034212699 scopus 로고    scopus 로고
    • Nitric oxide synthase induction in astroglial cell cultures: Effect on heat shock protein 70 synthesis and oxidant/antioxidant balance
    • Calabrese, V., Copani, A., Testa, D., Ravagna, A., Spadaro, F., Tendi, E., Nicoletti, V. G., and Giuffrida Stella, A. M. 2000 Nitric oxide synthase induction in astroglial cell cultures: Effect on heat shock protein 70 synthesis and oxidant/antioxidant balance. J. Neurosci. Res. 60:613-622.
    • (2000) J. Neurosci. Res. , vol.60 , pp. 613-622
    • Calabrese, V.1    Copani, A.2    Testa, D.3    Ravagna, A.4    Spadaro, F.5    Tendi, E.6    Nicoletti, V.G.7    Giuffrida Stella, A.M.8
  • 13
    • 0034673535 scopus 로고    scopus 로고
    • HSP70 induction in the brain following ethanol administration in the rat: Regulation by glutathione redox state
    • Calabrese, V., Testa, D., Ravagna, A., Bates, T. E., and Giuffrida Stella, A. M. 2000. HSP70 induction in the brain following ethanol administration in the rat: regulation by glutathione redox state. Biochem. Biophys. Res. Comm. 269: 397-400.
    • (2000) Biochem. Biophys. Res. Comm. , vol.269 , pp. 397-400
    • Calabrese, V.1    Testa, D.2    Ravagna, A.3    Bates, T.E.4    Giuffrida Stella, A.M.5
  • 14
    • 0004104070 scopus 로고
    • Macromolecular changes in the aging brain
    • Timiras, P. S. et al., (eds), Plenum Press, New York
    • Giuffrida Stella, A. M. 1991. Macromolecular changes in the aging brain. Pages 317-328, in: Timiras, P. S. et al., (eds), Plasticity and Regeneration of the nervous system, Plenum Press, New York.
    • (1991) Plasticity and Regeneration of the Nervous System , pp. 317-328
    • Giuffrida Stella, A.M.1
  • 15
    • 0023234186 scopus 로고
    • Macromolecular turnover in brain during aging
    • Giuffrida Stella, A. M. and Lajtha, A. 1987. Macromolecular turnover in brain during aging. Gerontology 33:136-48.
    • (1987) Gerontology , vol.33 , pp. 136-148
    • Giuffrida Stella, A.M.1    Lajtha, A.2
  • 16
  • 17
    • 0003162860 scopus 로고    scopus 로고
    • Role of mitochondria and oxidative stress in the aging process
    • Flint Beal, M., Howell, N., Bodis-Wollner, I. (eds), Wiley-Liss, New York
    • Sohal, R. S. 1997. Role of mitochondria and oxidative stress in the aging process. Pages 91-107, in: Flint Beal, M., Howell, N., Bodis-Wollner, I. (eds), Mitochondria and Free Radicals in Neurodegenerative diseases, Wiley-Liss, New York.
    • (1997) Mitochondria and Free Radicals in Neurodegenerative Diseases , pp. 91-107
    • Sohal, R.S.1
  • 18
    • 0026600596 scopus 로고
    • The mitochondrial electron transfer alteration as a factor involved in the brain aging
    • Benzi, G., Pastoris, O., Marzatico, F., Villa, R. F., Dagani, F., and Curti, D. 1992. The mitochondrial electron transfer alteration as a factor involved in the brain aging. Neurobiol. Aging 13: 361-368.
    • (1992) Neurobiol. Aging , vol.13 , pp. 361-368
    • Benzi, G.1    Pastoris, O.2    Marzatico, F.3    Villa, R.F.4    Dagani, F.5    Curti, D.6
  • 19
    • 0029147191 scopus 로고    scopus 로고
    • Mitochondria superoxide and hydrogen peroxide generation, protein oxidative damage, and longevity in different species of flies
    • Sohal, R. S., Sohal, B. H., and Orr, W. C., Mitochondria superoxide and hydrogen peroxide generation, protein oxidative damage, and longevity in different species of flies. Free Rad. Biol. Med. 19:499-504.
    • Free Rad. Biol. Med. , vol.19 , pp. 499-504
    • Sohal, R.S.1    Sohal, B.H.2    Orr, W.C.3
  • 20
    • 0032694302 scopus 로고    scopus 로고
    • The broad spectrum of responses to oxidants in proliferating cells: A new paradigm for oxidative stress
    • Davies, K. J. 1999. The broad spectrum of responses to oxidants in proliferating cells: a new paradigm for oxidative stress. IUBMB Life 48:41-47.
    • (1999) IUBMB Life , vol.48 , pp. 41-47
    • Davies, K.J.1
  • 21
    • 0001204988 scopus 로고    scopus 로고
    • Inhibitors of mitochondrial respiration, iron (II) and hydroxyl radical evoke release and extracellular hydrolysis of glutathione in rat striatum and substantia nigra: Potential implications to Parkinson's disease
    • Han, J., Cheng F., Yang, Z., and Dryhurst G. 1999. Inhibitors of mitochondrial respiration, iron (II) and hydroxyl radical evoke release and extracellular hydrolysis of glutathione in rat striatum and substantia nigra: potential implications to Parkinson's disease. J. Neurochem. 73:1683-1695.
    • (1999) J. Neurochem. , vol.73 , pp. 1683-1695
    • Han, J.1    Cheng, F.2    Yang, Z.3    Dryhurst, G.4
  • 22
    • 0031754202 scopus 로고    scopus 로고
    • Increased nuclear DNA oxidation in the brain in Alzheimer's disease
    • Gabbita, S. P., Lovell, M. A., and Markesbery, W. R. 1998. Increased nuclear DNA oxidation in the brain in Alzheimer's disease. J. Neurochem. 71:2034-2040.
    • (1998) J. Neurochem. , vol.71 , pp. 2034-2040
    • Gabbita, S.P.1    Lovell, M.A.2    Markesbery, W.R.3
  • 23
    • 0031110054 scopus 로고    scopus 로고
    • Terminal dUTP nick end labeling (TUNEL) positive cells in the different regions of the brain in normal aging and Alzheimer patients
    • Li, W. P., Chan, W. Y., Lai, H. W., and Yew, D. T. 1997. Terminal dUTP nick end labeling (TUNEL) positive cells in the different regions of the brain in normal aging and Alzheimer patients. J. Mol. Neurosci. 8:75-82.
    • (1997) J. Mol. Neurosci. , vol.8 , pp. 75-82
    • Li, W.P.1    Chan, W.Y.2    Lai, H.W.3    Yew, D.T.4
  • 25
    • 0025651008 scopus 로고
    • Steady- State levels of 7-methylguanine increase in nuclear DNA of postmitotic mouse tissues during aging
    • Tan, B. H., Bencsath, F. A., and Gaubatz, J. W. 1990. Steady- state levels of 7-methylguanine increase in nuclear DNA of postmitotic mouse tissues during aging. Mutat. Res. 237: 229-238.
    • (1990) Mutat. Res. , vol.237 , pp. 229-238
    • Tan, B.H.1    Bencsath, F.A.2    Gaubatz, J.W.3
  • 26
    • 0027400458 scopus 로고
    • Age-related studies on the removal of 7-methylguanine from DNA of mouse kidney tissue following N-methyl-N-nitrosourea treatment
    • Gaubatz, J. W. and Tan, B. H. 1993. Age-related studies on the removal of 7-methylguanine from DNA of mouse kidney tissue following N-methyl-N-nitrosourea treatment. Mutat. Res. 295:81-91.
    • (1993) Mutat. Res. , vol.295 , pp. 81-91
    • Gaubatz, J.W.1    Tan, B.H.2
  • 27
    • 0028301537 scopus 로고
    • Aging affects the levels of DNA damage in postmitotic cells
    • Gaubatz, J. W. and Tan, B. H. 1994. Aging affects the levels of DNA damage in postmitotic cells. Ann. N. Y. Acad. Sci. 719:97-107.
    • (1994) Ann. N. Y. Acad. Sci. , vol.719 , pp. 97-107
    • Gaubatz, J.W.1    Tan, B.H.2
  • 28
    • 0029814125 scopus 로고    scopus 로고
    • Accumulation of DNA damage in aging neurons occurs through a mechanism other than apoptosis
    • Mandavilli, B. S. and Rao, K. S. 1996. Accumulation of DNA damage in aging neurons occurs through a mechanism other than apoptosis. J. Neurochem. 67:1559-1565.
    • (1996) J. Neurochem. , vol.67 , pp. 1559-1565
    • Mandavilli, B.S.1    Rao, K.S.2
  • 29
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: Enzymology and biology
    • Demple, B. and Harrison, L. 1994. Repair of oxidative damage to DNA: enzymology and biology. Annu. Rev. Biochem. 63: 915-948.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 30
    • 0029758774 scopus 로고    scopus 로고
    • The mechanisms of aging and perspective for elimination of deleterious effects
    • Fujiwara, Y. 1996. The mechanisms of aging and perspective for elimination of deleterious effects. Nippon. Ronen. Igakkai. Zasshi. 33:499-502.
    • (1996) Nippon. Ronen. Igakkai. Zasshi. , vol.33 , pp. 499-502
    • Fujiwara, Y.1
  • 32
    • 0033535365 scopus 로고    scopus 로고
    • Endogenous oxidative damage of mtDNA
    • Beckman, K. B. and Ames, B. N. 1999. Endogenous oxidative damage of mtDNA. Mutat. Res. 424:51-58.
    • (1999) Mutat. Res. , vol.424 , pp. 51-58
    • Beckman, K.B.1    Ames, B.N.2
  • 33
    • 0029654349 scopus 로고
    • Editing DNA replication and recombination by mismatch repair: From bacterial genetics to mechanisms of predisposition to cancer in humans
    • Radman, M., Matic, I., Halliday, J. A., and Taddei, F. 1995. Editing DNA replication and recombination by mismatch repair: from bacterial genetics to mechanisms of predisposition to cancer in humans. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 347:97-103.
    • (1995) Philos. Trans. R. Soc. Lond. B. Biol. Sci. , vol.347 , pp. 97-103
    • Radman, M.1    Matic, I.2    Halliday, J.A.3    Taddei, F.4
  • 35
    • 0032693322 scopus 로고    scopus 로고
    • Oxidative DNA damage processing in nuclear and mitochondrial DNA
    • Bohr, V. A. and Dianov, G. L. 1999. Oxidative DNA damage processing in nuclear and mitochondrial DNA. Biochimie 81: 155-160.
    • (1999) Biochimie , vol.81 , pp. 155-160
    • Bohr, V.A.1    Dianov, G.L.2
  • 36
    • 0032413244 scopus 로고    scopus 로고
    • Mitochondrial aging: Open questions
    • Beckman, K. B. and Ames, B. N. 1998. Mitochondrial aging: open questions. Ann. N. Y. Acad. Sci. 854:118-127.
    • (1998) Ann. N. Y. Acad. Sci. , vol.854 , pp. 118-127
    • Beckman, K.B.1    Ames, B.N.2
  • 37
    • 0032504622 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative disorders
    • Schapira, A. H. 1998. Mitochondrial dysfunction in neurodegenerative disorders. Biochim. Biophys. Acta 1366:225-233.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 225-233
    • Schapira, A.H.1
  • 39
    • 0345596416 scopus 로고    scopus 로고
    • Alterations of antioxidant enzymes and oxidative damage to macromolecules in different organs of rats during aging
    • Tian, L., Cai, Q., and Wei, H. 1998. Alterations of antioxidant enzymes and oxidative damage to macromolecules in different organs of rats during aging. Free Radic. Biol. Med. 24: 1477-1484.
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 1477-1484
    • Tian, L.1    Cai, Q.2    Wei, H.3
  • 40
    • 0025832844 scopus 로고
    • Reversal of age- Related increase in brain protein oxidation, decrease in enzyme activity, and loss in temporal and spatial memory by chronic administration of the spin-trapping compound N-tert-butyl-alpha- phenylnitrone
    • Carney, J. M., Starke-Reed, P. E., Oliver, C. N., Landum. R. W., Cheng, M. S., Wu, J. F., and Floyd, R. A. 1991. Reversal of age- related increase in brain protein oxidation, decrease in enzyme activity, and loss in temporal and spatial memory by chronic administration of the spin-trapping compound N-tert-butyl-alpha- phenylnitrone. Proc. Natl. Acad. Sci. USA 88: 3633-3636.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3633-3636
    • Carney, J.M.1    Starke-Reed, P.E.2    Oliver, C.N.3    Landum, R.W.4    Cheng, M.S.5    Wu, J.F.6    Floyd, R.A.7
  • 41
    • 0034185616 scopus 로고    scopus 로고
    • Protein oxidation and age-dependent alterations in calcium homeostasis
    • Squier, T. C. and Bigelow, D. J. 2000 Protein oxidation and age-dependent alterations in calcium homeostasis. Front. Biosci. 5:504-526.
    • (2000) Front. Biosci. , vol.5 , pp. 504-526
    • Squier, T.C.1    Bigelow, D.J.2
  • 42
    • 0002575630 scopus 로고    scopus 로고
    • Calcium and neuronal ageing
    • Verkhratsky, A. and Toescu E. 1998. Calcium and neuronal ageing. TINS 21:2-7.
    • (1998) TINS , vol.21 , pp. 2-7
    • Verkhratsky, A.1    Toescu, E.2
  • 43
    • 0032850682 scopus 로고    scopus 로고
    • Irregular distribution of cytochrome c oxidase protein subunits in aging and Alzheimer's disease
    • Ojaimi, J., Masters, C. L., McLean, C., Opeskin, K., McKelvie, P., and Byrne, E. 1999. Irregular distribution of cytochrome c oxidase protein subunits in aging and Alzheimer's disease. Ann. Neurol. 46:656-660.
    • (1999) Ann. Neurol. , vol.46 , pp. 656-660
    • Ojaimi, J.1    Masters, C.L.2    McLean, C.3    Opeskin, K.4    McKelvie, P.5    Byrne, E.6
  • 44
    • 0033369476 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical generation and leak: Sites of production in states 4 and 3, organ specificity, and relation to aging and longevity
    • Barja, G. 1999. Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity, and relation to aging and longevity. J. Bioenerg. Biomembr. 31:347-366.
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 347-366
    • Barja, G.1
  • 45
    • 0026752775 scopus 로고
    • Lipid composition in synaptic and nonsynaptic mitochondria from rat brains and effect of aging
    • Ruggiero, F. M., Cafagna, F., Petruzzella, V., Gadaleta, M. N., and Quagliariello, E. 1992. Lipid composition in synaptic and nonsynaptic mitochondria from rat brains and effect of aging. J. Neurochem. 59:487-491.
    • (1992) J. Neurochem. , vol.59 , pp. 487-491
    • Ruggiero, F.M.1    Cafagna, F.2    Petruzzella, V.3    Gadaleta, M.N.4    Quagliariello, E.5
  • 46
    • 0020677095 scopus 로고
    • Perspectives for neural regeneration with changes in macromolecular metabolism
    • Haber, B., Perez-Polo, R., Hashim, G. A., Giuffrida Stella, A. M., Nervous system regeneration, Alan Liss, New York
    • Giuffrida Stella, A. M. and Lajtha, A. 1983. Perspectives for neural regeneration with changes in macromolecular metabolism. Birth Defects: Original Article Series 19, vol.4, Pages 23-32, in: Haber, B., Perez-Polo, R., Hashim, G. A., Giuffrida Stella, A. M., Nervous system regeneration, Alan Liss, New York.
    • (1983) Birth Defects: Original Article Series 19 , vol.4 , pp. 23-32
    • Giuffrida Stella, A.M.1    Lajtha, A.2
  • 47
    • 0030294728 scopus 로고    scopus 로고
    • Cytochrome c oxidase defects of the human substantia nigra in normal aging
    • Itoh K., Weis, S., Mehraein, P., and Muller-Hocker, J. 1996. Cytochrome c oxidase defects of the human substantia nigra in normal aging. Neurobiol. Aging 17:843-848.
    • (1996) Neurobiol. Aging , vol.17 , pp. 843-848
    • Itoh, K.1    Weis, S.2    Mehraein, P.3    Muller-Hocker, J.4
  • 48
    • 0041943622 scopus 로고
    • Long term ethanol abuse enhances age dependent modulation of redox state in central and peripheral organs of rat: Protection by L-carnitine
    • Calabrese, V., Distefano, A., Ricciardi, R., Calderone, A., and Rizza, V. 1992. Long term ethanol abuse enhances age dependent modulation of redox state in central and peripheral organs of rat: protection by L-carnitine. Neurosci. Lett. 43:18-21.
    • (1992) Neurosci. Lett. , vol.43 , pp. 18-21
    • Calabrese, V.1    Distefano, A.2    Ricciardi, R.3    Calderone, A.4    Rizza, V.5
  • 49
    • 0024207352 scopus 로고
    • Action of L-acetylcarnitine on age-dependent modifications of mitochondrial membrane proteins from rat cerebellum
    • Villa, R. F., Turpeenoja, L., Benzi, G., and Giuffrida Stella, A. M. 1988. Action of L-acetylcarnitine on age-dependent modifications of mitochondrial membrane proteins from rat cerebellum. Neurochem. Res. 13:909-916.
    • (1988) Neurochem. Res. , vol.13 , pp. 909-916
    • Villa, R.F.1    Turpeenoja, L.2    Benzi, G.3    Giuffrida Stella, A.M.4
  • 50
    • 0031769321 scopus 로고    scopus 로고
    • Energy metabolism of synaptosomal subpopulations from different neuronal systems of rat hippocampus: Effect of L-acetylcarnitine administration in vivo
    • Gorini, A., D'Angelo, A., and Villa, R. F. 1998. Energy metabolism of synaptosomal subpopulations from different neuronal systems of rat hippocampus: effect of L-acetylcarnitine administration in vivo. Neurochem. Res. 23:1485-1491.
    • (1998) Neurochem. Res. , vol.23 , pp. 1485-1491
    • Gorini, A.1    D'Angelo, A.2    Villa, R.F.3
  • 51
    • 0027534583 scopus 로고
    • Modulation of membrane phospholipid fatty acid composition by age and food restriction
    • Laganiere, S., and Yu, B. P. 1993. Modulation of membrane phospholipid fatty acid composition by age and food restriction. Gerontology 39:7-18.
    • (1993) Gerontology , vol.39 , pp. 7-18
    • Laganiere, S.1    Yu, B.P.2
  • 52
    • 0028342438 scopus 로고
    • Oxidative damage, mitochondrial oxidant generation and antioxidant defenses during aging and in response to food restriction in the mouse
    • Sohal, R. S., Ku, H. H., Agarwal, S., Forster, M. J., and Lal, H. 1994. Oxidative damage, mitochondrial oxidant generation and antioxidant defenses during aging and in response to food restriction in the mouse. Mech. Ageing Dev. 74:121-133.
    • (1994) Mech. Ageing Dev. , vol.74 , pp. 121-133
    • Sohal, R.S.1    Ku, H.H.2    Agarwal, S.3    Forster, M.J.4    Lal, H.5
  • 53
    • 0030927437 scopus 로고    scopus 로고
    • Aging and caloric restriction affect mitochondrial respiration and lipid membrane status: An electron paramagnetic resonance investigation
    • Gabbita, S. P., Butterfield, D. A., Hensley, K., Shaw, W., and Carney, J. M. 1997. Aging and caloric restriction affect mitochondrial respiration and lipid membrane status: an electron paramagnetic resonance investigation. Free Radic. Biol. Med. 23:191-201.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 191-201
    • Gabbita, S.P.1    Butterfield, D.A.2    Hensley, K.3    Shaw, W.4    Carney, J.M.5
  • 54
    • 0032032686 scopus 로고    scopus 로고
    • Caloric restriction retards the aging associated changes in gamma-aminobutyric acidA receptor gene expression in rat cerebellum
    • Mhatre, M. C. and Ticku, M. K. 1998. Caloric restriction retards the aging associated changes in gamma-aminobutyric acidA receptor gene expression in rat cerebellum. Brain Res. Mo.1 Brain Res. 54:270-275.
    • (1998) Brain Res. Mo.1 Brain Res. , vol.54 , pp. 270-275
    • Mhatre, M.C.1    Ticku, M.K.2
  • 55
    • 0032423287 scopus 로고    scopus 로고
    • Membrane and receptor modifications of oxidative stress vulnerability in aging. Nutritional considerations
    • Joseph, J. A., Denisova, N., Fisher, D., Shukitt-Hale, B., Bickford, P., Prior, R., and Cao, G. 1998. Membrane and receptor modifications of oxidative stress vulnerability in aging. Nutritional considerations. Ann. NY Acad. Sci. 854:268-276.
    • (1998) Ann. NY Acad. Sci. , vol.854 , pp. 268-276
    • Joseph, J.A.1    Denisova, N.2    Fisher, D.3    Shukitt-Hale, B.4    Bickford, P.5    Prior, R.6    Cao, G.7
  • 58
    • 0029147523 scopus 로고
    • Excitotoxins, aging, and environmental neurotoxins: Implications for understanding human neurodegenerative diseases
    • Dawson, R., Jr., Beal, M. F., Bondy, S. C., Di Monte, D. A., and Isom, G. E. 1995. Excitotoxins, aging, and environmental neurotoxins: implications for understanding human neurodegenerative diseases. Toxicol. Appl. Pharmacol. 134:1-17.
    • (1995) Toxicol. Appl. Pharmacol. , vol.134 , pp. 1-17
    • Dawson R., Jr.1    Beal, M.F.2    Bondy, S.C.3    Di Monte, D.A.4    Isom, G.E.5
  • 59
  • 63
    • 0029677843 scopus 로고    scopus 로고
    • Alzheimer disease: Protein- Protein interaction and oxidative stress
    • Smith, M. A. and Perry, G. 1996. Alzheimer disease: protein- protein interaction and oxidative stress. Bol. Estud. Med. Biol. 44:5-10.
    • (1996) Bol. Estud. Med. Biol. , vol.44 , pp. 5-10
    • Smith, M.A.1    Perry, G.2
  • 64
    • 0029978498 scopus 로고    scopus 로고
    • Age-related losses of cognitive function and motor skills in mice are associated with oxidative protein damage in the brain
    • Forster, M. J., Dubey, A., Dawson, K. M., Stutts, W. A., Lal, H., and Sohal, R. S. 1996. Age-related losses of cognitive function and motor skills in mice are associated with oxidative protein damage in the brain. Proc. Natl. Acad. Sci. USA 93: 4765-4769.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4765-4769
    • Forster, M.J.1    Dubey, A.2    Dawson, K.M.3    Stutts, W.A.4    Lal, H.5    Sohal, R.S.6
  • 65
    • 0026647763 scopus 로고
    • Free radical damage to protein and DNA: Mechanisms involved and relevant observations on brain undergoing oxidative stress
    • Floyd, R. A. and Carney, J. M. 1992. Free radical damage to protein and DNA: mechanisms involved and relevant observations on brain undergoing oxidative stress. Ann. Neurol. 32:22-27.
    • (1992) Ann. Neurol. , vol.32 , pp. 22-27
    • Floyd, R.A.1    Carney, J.M.2
  • 68
    • 0034090710 scopus 로고    scopus 로고
    • Characteristics of the calcium-triggered mitochondrial permeability transition in non-synaptic brain mitochondria: Effect of cyclosporin A and ubiquinone O
    • Kristiián, T., Gertsch, J., Bates, T. E., and Siesjö., B. K. 2000. Characteristics of the calcium-triggered mitochondrial permeability transition in non-synaptic brain mitochondria: effect of cyclosporin A and ubiquinone O. J. Neurochem. 74: 1999-2009.
    • (2000) J. Neurochem. , vol.74 , pp. 1999-2009
    • Kristiián, T.1    Gertsch, J.2    Bates, T.E.3    Siesjö, B.K.4
  • 69
    • 0031008555 scopus 로고    scopus 로고
    • The effects of oxidative stress on in vivo brain GSH turnover in young and mature mice
    • Chang, M. L., Klaidman, L. K., and Adams, J. D.,Jr. 1997. The effects of oxidative stress on in vivo brain GSH turnover in young and mature mice. Mol. Chem. Neuropathol. 30:187-197.
    • (1997) Mol. Chem. Neuropathol. , vol.30 , pp. 187-197
    • Chang, M.L.1    Klaidman, L.K.2    Adams J.D., Jr.3
  • 71
    • 0032704101 scopus 로고    scopus 로고
    • Antioxidants, oxidative stress, and degenerative neurological disorders
    • Floyd, R. A. 1999. Antioxidants, oxidative stress, and degenerative neurological disorders. Proc. Soc. Exp. Biol. Med. 222: 236-245.
    • (1999) Proc. Soc. Exp. Biol. Med. , vol.222 , pp. 236-245
    • Floyd, R.A.1
  • 72
    • 0032973861 scopus 로고    scopus 로고
    • Glial cells protect neurons against oxidative stress via transcriptional up-regulation of the glutathione synthesis
    • Iwata Ichikawa, E., Kondo, Y., Miyazaki, I., Asanuma, M., and Ogawa, N. 1999. Glial cells protect neurons against oxidative stress via transcriptional up-regulation of the glutathione synthesis. J. Neurochem. 72:2334-2344.
    • (1999) J. Neurochem. , vol.72 , pp. 2334-2344
    • Iwata Ichikawa, E.1    Kondo, Y.2    Miyazaki, I.3    Asanuma, M.4    Ogawa, N.5
  • 73
    • 1842371505 scopus 로고    scopus 로고
    • Protection of flupirtine on beta-amyloid- Induced apoptosis in neuronal cells in vitro: Prevention of amyloid-induced glutathione depletion
    • Muller, W. E., Romero, F. J., Perovic, S., Pergande, G., and Pialoglou, P. 1997. Protection of flupirtine on beta-amyloid- induced apoptosis in neuronal cells in vitro: prevention of amyloid-induced glutathione depletion. J. Neurochem. 68: 2371-2377.
    • (1997) J. Neurochem. , vol.68 , pp. 2371-2377
    • Muller, W.E.1    Romero, F.J.2    Perovic, S.3    Pergande, G.4    Pialoglou, P.5
  • 75
    • 0030792637 scopus 로고    scopus 로고
    • Multiple roles og glutathione in the central nervous system
    • Cooper, A. J. and Kristal, B. S. (1997). Multiple roles og glutathione in the central nervous system. Biol. Chem. 378: 793-802.
    • (1997) Biol. Chem. , vol.378 , pp. 793-802
    • Cooper, A.J.1    Kristal, B.S.2
  • 76
    • 0032707717 scopus 로고    scopus 로고
    • Nitric oxide as a signaling molecule in the vascular system: An overview
    • Ignarro, L. J., Cirino, G., Casini, A., and Napoli, C. 1999. Nitric oxide as a signaling molecule in the vascular system: an overview. J. Cardiovasc. Pharmacol. 34:879-886.
    • (1999) J. Cardiovasc. Pharmacol. , vol.34 , pp. 879-886
    • Ignarro, L.J.1    Cirino, G.2    Casini, A.3    Napoli, C.4
  • 77
    • 0033378598 scopus 로고    scopus 로고
    • Nitric oxide is the predominant mediator of cerebellar hyperemia during somatosensory activation in rats
    • Yang, G., Chen, G., Ebner, T. J., and Iadecola, C. 1999. Nitric oxide is the predominant mediator of cerebellar hyperemia during somatosensory activation in rats. Am. J. Physiol. 277: R1760-70.
    • (1999) Am. J. Physiol. , vol.277
    • Yang, G.1    Chen, G.2    Ebner, T.J.3    Iadecola, C.4
  • 78
    • 0028349156 scopus 로고
    • Nitric oxide synthases in mammals
    • Knowles, R. G. and Moncada, S. 1994. Nitric oxide synthases in mammals. Biochem. J. 298:249-258.
    • (1994) Biochem. J. , vol.298 , pp. 249-258
    • Knowles, R.G.1    Moncada, S.2
  • 79
    • 0032740245 scopus 로고    scopus 로고
    • Endogenous nitric oxide synthesis: Biological functions and pathophysiology
    • Bredt, D. S. 1999. Endogenous nitric oxide synthesis: biological functions and pathophysiology. Free Radic. Res. 31: 577-596.
    • (1999) Free Radic. Res. , vol.31 , pp. 577-596
    • Bredt, D.S.1
  • 81
    • 0029447861 scopus 로고
    • Physiological and toxicological actions of nitric oxide in the central nervous system
    • Dawson, V.L. and Dawson, T. M. 1995. Physiological and toxicological actions of nitric oxide in the central nervous system. Adv. Pharmacol. 34:323-342.
    • (1995) Adv. Pharmacol. , vol.34 , pp. 323-342
    • Dawson, V.L.1    Dawson, T.M.2
  • 82
    • 0031965295 scopus 로고    scopus 로고
    • Brain derived neurotrophic factor and insulin like growth factor-1 attenuate upregulation of nitric oxide synthase and cell injury following trauma to the spinal cord. An immunohistochemical study in the rat
    • Sharma, H. S., Nyberg, F., Westman, J., Aim, P., Gordh, T., and Lindholm, D. 1998. Brain derived neurotrophic factor and insulin like growth factor-1 attenuate upregulation of nitric oxide synthase and cell injury following trauma to the spinal cord. An immunohistochemical study in the rat. Amino. Acids. 14:121-129.
    • (1998) Amino. Acids , vol.14 , pp. 121-129
    • Sharma, H.S.1    Nyberg, F.2    Westman, J.3    Aim, P.4    Gordh, T.5    Lindholm, D.6
  • 84
    • 0031826286 scopus 로고    scopus 로고
    • Peroxynitrite reactions and diffusion in biology
    • Radi, R. 1998. Peroxynitrite reactions and diffusion in biology. Chem. Res. Toxicol. 11:720-721.
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 720-721
    • Radi, R.1
  • 85
    • 0030049032 scopus 로고    scopus 로고
    • Damage to DNA by reactive oxygen and nitrogen species: Role in inflammatory disease and progression to cancer
    • Wiseman, H. and Halliwell, B. 1996. Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer. Biochem. J. 313:17-29.
    • (1996) Biochem. J. , vol.313 , pp. 17-29
    • Wiseman, H.1    Halliwell, B.2
  • 86
    • 0031776230 scopus 로고    scopus 로고
    • Oxidation and antioxidation of human low-density lipoprotein and plasma exposed to 3-morpholinosydnonimine and reagent peroxynitrite
    • Thomas, S. R., Davies, M. J., and Stocker, R. 1998. Oxidation and antioxidation of human low-density lipoprotein and plasma exposed to 3-morpholinosydnonimine and reagent peroxynitrite. Chem. Res. Toxicol. 11:484-494.
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 484-494
    • Thomas, S.R.1    Davies, M.J.2    Stocker, R.3
  • 87
    • 0032948006 scopus 로고    scopus 로고
    • Peroxynitrite-induced alterations in synaptosomal membrane proteins: Insight into oxidative stress in Alzheimer's disease
    • Koppal, T., Drake, J., Yatin, S., Jordan, B., Varadarajan, S., Bettenhausen, L., and Butterfield, D. A. 1999. Peroxynitrite-induced alterations in synaptosomal membrane proteins: insight into oxidative stress in Alzheimer's disease. J. Neurochem. 72:310-317.
    • (1999) J. Neurochem. , vol.72 , pp. 310-317
    • Koppal, T.1    Drake, J.2    Yatin, S.3    Jordan, B.4    Varadarajan, S.5    Bettenhausen, L.6    Butterfield, D.A.7
  • 88
    • 0030010723 scopus 로고    scopus 로고
    • Peroxynitrite mediated oxidation of purine bases of nucleosides and isolated DNA
    • Douki, T. and Cadet, J. 1996. Peroxynitrite mediated oxidation of purine bases of nucleosides and isolated DNA. Free Radic. Res. 24:369-380.
    • (1996) Free Radic. Res. , vol.24 , pp. 369-380
    • Douki, T.1    Cadet, J.2
  • 90
    • 0032813952 scopus 로고    scopus 로고
    • S-nitrosylation of proteins
    • Broillet, M. C. 1999. S-nitrosylation of proteins. Cell Mol. Life Sci. 55:1036-1042.
    • (1999) Cell Mol. Life Sci. , vol.55 , pp. 1036-1042
    • Broillet, M.C.1
  • 92
    • 0026686667 scopus 로고
    • Nitric oxide stimulates auto- ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase
    • Zhang, J. and Snyder, S. H. 1992. Nitric oxide stimulates auto- ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase. Proc. Natl. Acad. Sci. USA 89:9382-9385.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9382-9385
    • Zhang, J.1    Snyder, S.H.2
  • 93
    • 0033515479 scopus 로고    scopus 로고
    • Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase
    • Mohr, S., Hallak, H., de Boitte, A., Lapetina, E. G., and Brune, B. 1999. Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 274:9427-9430.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9427-9430
    • Mohr, S.1    Hallak, H.2    De Boitte, A.3    Lapetina, E.G.4    Brune, B.5
  • 94
    • 0028799706 scopus 로고
    • Depletion of brain glutathione is accompanied by impaired mitochondrial function and decreased N-acetyl aspartate concentration
    • Heales, S. J., Davies, S. E., Bates, T. E., and Clark, J. B. 1995. Depletion of brain glutathione is accompanied by impaired mitochondrial function and decreased N-acetyl aspartate concentration. Neurochem. Res. 20:31-38.
    • (1995) Neurochem. Res. , vol.20 , pp. 31-38
    • Heales, S.J.1    Davies, S.E.2    Bates, T.E.3    Clark, J.B.4
  • 95
    • 0032179726 scopus 로고    scopus 로고
    • Effect of nitric oxide synthase induction on the expression of mitochondrial respiratory chain subunits in mixed cortical and astroglial cell cultures
    • Nicoletti, V., Caruso, A., Tendi, E., Privitera, A., Console, A., Calabrese, V., Spadaro, F., Ravagna, A., Copani, A., and Giuffrida Stella, A. M. 1998. Effect of nitric oxide synthase induction on the expression of mitochondrial respiratory chain subunits in mixed cortical and astroglial cell cultures. Biochimie 80: 871-881.
    • (1998) Biochimie , vol.80 , pp. 871-881
    • Nicoletti, V.1    Caruso, A.2    Tendi, E.3    Privitera, A.4    Console, A.5    Calabrese, V.6    Spadaro, F.7    Ravagna, A.8    Copani, A.9    Giuffrida Stella, A.M.10
  • 96
    • 0024352104 scopus 로고
    • Heme-dependent activation of soluble guanylate cyclase by nitric oxide: Regulation of enzyme activity by porphyrins and metalloporphyrins
    • Ignarro, L. J. 1989. Heme-dependent activation of soluble guanylate cyclase by nitric oxide: regulation of enzyme activity by porphyrins and metalloporphyrins. Semin. Hematol. 26:63-76.
    • (1989) Semin. Hematol. , vol.26 , pp. 63-76
    • Ignarro, L.J.1
  • 97
    • 0030998378 scopus 로고    scopus 로고
    • Nitric oxide prevents oxidative damage produced by tertbutyl hydroperoxide in erythroleukemia cells via nitrosylation of heme and non-heme iron. Electron paramagnetic resonance evidence
    • Gorbunov, N. V., Yalowich, J. C., Gaddam, A., Thampatty, P., Ritov, V. B., Kisin, E. R., Elsayed, N. M., and Kagan, V. E. 1997. Nitric oxide prevents oxidative damage produced by tertbutyl hydroperoxide in erythroleukemia cells via nitrosylation of heme and non-heme iron. Electron paramagnetic resonance evidence. J. Biol. Chem. 272:12328-12341.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12328-12341
    • Gorbunov, N.V.1    Yalowich, J.C.2    Gaddam, A.3    Thampatty, P.4    Ritov, V.B.5    Kisin, E.R.6    Elsayed, N.M.7    Kagan, V.E.8
  • 99
    • 0027959803 scopus 로고
    • Actions of redox-related congeners of nitric oxide at the NMDA receptor
    • Lipton, S. A. and Stamler, J. S. 1994. Actions of redox-related congeners of nitric oxide at the NMDA receptor. Neuropharmacology 33:1229-1233.
    • (1994) Neuropharmacology , vol.33 , pp. 1229-1233
    • Lipton, S.A.1    Stamler, J.S.2
  • 100
    • 0028856368 scopus 로고
    • NMDA receptor activation produces concurrent generation of nitric oxide and reactive oxygen species: Implication for cell death
    • Gunasekar, P. G., Kanthasamy, A. G., Borowitz, J. L., and Isom, G. E. 1995. NMDA receptor activation produces concurrent generation of nitric oxide and reactive oxygen species: implication for cell death. J. Neurochem. 65:2016-2021.
    • (1995) J. Neurochem. , vol.65 , pp. 2016-2021
    • Gunasekar, P.G.1    Kanthasamy, A.G.2    Borowitz, J.L.3    Isom, G.E.4
  • 101
    • 0029125857 scopus 로고
    • Aging, energy, and oxidative stress in neurodegenerative diseases
    • Beal, M. F. 1995. Aging, energy, and oxidative stress in neurodegenerative diseases. Ann. Neurol. 38:357-366.
    • (1995) Ann. Neurol. , vol.38 , pp. 357-366
    • Beal, M.F.1
  • 102
    • 0030581498 scopus 로고    scopus 로고
    • Mitochondrial oxidative phosphorylation changes in the life span. Molecular aspects and physiopathological implications
    • Papa, S. 1996. Mitochondrial oxidative phosphorylation changes in the life span. Molecular aspects and physiopathological implications. Biochim. Biophys. Acta 1276:87-105.
    • (1996) Biochim. Biophys. Acta , vol.1276 , pp. 87-105
    • Papa, S.1
  • 103
    • 0030809576 scopus 로고    scopus 로고
    • Reactive oxygen species, mitochondria, apoptosis and aging
    • Papa, S. and Skulachev, V. P. 1997. Reactive oxygen species, mitochondria, apoptosis and aging. Mol Cell. Biochem. 174: 305-319.
    • (1997) Mol Cell. Biochem. , vol.174 , pp. 305-319
    • Papa, S.1    Skulachev, V.P.2
  • 105
    • 0032504657 scopus 로고    scopus 로고
    • Role of mitochondria in oxidative stress and ageing
    • Lenaz, G. 1998. Role of mitochondria in oxidative stress and ageing. Biochim. Biophys. Acta 1336:53-67.
    • (1998) Biochim. Biophys. Acta , vol.1336 , pp. 53-67
    • Lenaz, G.1
  • 106
    • 0038233014 scopus 로고    scopus 로고
    • Nitric oxide-mediated mitochondrial damage in the brain: Mechanisms and implications for neurodegenerative diseases
    • Bolanos, J. P., Almeida, A., Stewart, V., Peuchen, S., Land, J. M., Clark, J. B., and Heales, S. J. 1997. Nitric oxide-mediated mitochondrial damage in the brain: mechanisms and implications for neurodegenerative diseases. J. Neurochem. 68: 2227-2240.
    • (1997) J. Neurochem. , vol.68 , pp. 2227-2240
    • Bolanos, J.P.1    Almeida, A.2    Stewart, V.3    Peuchen, S.4    Land, J.M.5    Clark, J.B.6    Heales, S.J.7
  • 107
    • 28044464985 scopus 로고
    • Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases
    • Cleeter, M. W., Cooper, J. M., Darley Usmar, V. M., Moncada, S., and Schapira, A. H. 1994. Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases. FEBS Lett. 345:50-54.
    • (1994) FEBS Lett. , vol.345 , pp. 50-54
    • Cleeter, M.W.1    Cooper, J.M.2    Darley Usmar, V.M.3    Moncada, S.4    Schapira, A.H.5
  • 108
    • 0028952832 scopus 로고
    • Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary culture
    • Bolanos, J. P., Heales, S. J., Land, J. M., and Clark, J. B. 1995. Effect of peroxynitrite on the mitochondrial respiratory chain: differential susceptibility of neurones and astrocytes in primary culture. J. Neurochem. 64:1965-1972.
    • (1995) J. Neurochem. , vol.64 , pp. 1965-1972
    • Bolanos, J.P.1    Heales, S.J.2    Land, J.M.3    Clark, J.B.4
  • 109
    • 0029962693 scopus 로고    scopus 로고
    • Glutathione protects astrocytes from peroxynitrite-mediated mitochondrial damage: Implications for neuronal/astrocytic trafficking and neurodegeneration
    • Barker, J. E., Bolanos, J. P., Land, J. M., Clark, J. B., and Heales, S. J. 1996. Glutathione protects astrocytes from peroxynitrite-mediated mitochondrial damage: implications for neuronal/astrocytic trafficking and neurodegeneration. Dev. Neurosci. 18:391-396.
    • (1996) Dev. Neurosci. , vol.18 , pp. 391-396
    • Barker, J.E.1    Bolanos, J.P.2    Land, J.M.3    Clark, J.B.4    Heales, S.J.5
  • 110
    • 0028604337 scopus 로고
    • Trolox protects mitochondrial complex IV from nitric oxidemediated damage in astrocytes
    • Heales, S. J., Bolanos, J. P., Land, J. M., and Clark, J. B. 1994. Trolox protects mitochondrial complex IV from nitric oxidemediated damage in astrocytes. Brain Res. 668:243-245.
    • (1994) Brain Res. , vol.668 , pp. 243-245
    • Heales, S.J.1    Bolanos, J.P.2    Land, J.M.3    Clark, J.B.4
  • 111
    • 0029970099 scopus 로고    scopus 로고
    • Depletion of brain glutathione results in a decrease of glutathione reductase activity; an enzyme susceptible to oxidative damage
    • Barker, J. E., Heales, S. J., Cassidy, A., Bolanos, J. P., Land, J. M., and Clark, J. B. 1996. Depletion of brain glutathione results in a decrease of glutathione reductase activity; an enzyme susceptible to oxidative damage. Brain Res. 716:118-122.
    • (1996) Brain Res. , vol.716 , pp. 118-122
    • Barker, J.E.1    Heales, S.J.2    Cassidy, A.3    Bolanos, J.P.4    Land, J.M.5    Clark, J.B.6
  • 112
    • 0032810909 scopus 로고    scopus 로고
    • beta-Amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria
    • Canevari, L., Clark, J. B., and Bates, T. E. 1999. beta-Amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria. FEBS Lett. 457:131-134.
    • (1999) FEBS Lett. , vol.457 , pp. 131-134
    • Canevari, L.1    Clark, J.B.2    Bates, T.E.3
  • 113
    • 0029862743 scopus 로고    scopus 로고
    • Reduction in the number of NADPH-diaphorase-positive cells in the cerebral cortex and striatum in aged rats
    • Yamada, K., Noda, Y., Komori, Y., Sugihara, H., Hasegawa, T., and Nabeshima, T. 1996. Reduction in the number of NADPH-diaphorase-positive cells in the cerebral cortex and striatum in aged rats. Neurosci. Res. 24:393-402.
    • (1996) Neurosci. Res. , vol.24 , pp. 393-402
    • Yamada, K.1    Noda, Y.2    Komori, Y.3    Sugihara, H.4    Hasegawa, T.5    Nabeshima, T.6
  • 115
    • 0031760291 scopus 로고    scopus 로고
    • Spontaneous expression of inducible nitric oxide synthase in the hypothalamus and other brain regions of aging rats
    • Vernet, D., Bonavera, J. J., Swerdloff, R. S., Gonzalez-Cadavid, N. F., and Wang, C. 1998. Spontaneous expression of inducible nitric oxide synthase in the hypothalamus and other brain regions of aging rats. Endocrinology 139:3254-3261.
    • (1998) Endocrinology , vol.139 , pp. 3254-3261
    • Vernet, D.1    Bonavera, J.J.2    Swerdloff, R.S.3    Gonzalez-Cadavid, N.F.4    Wang, C.5
  • 116
    • 0030890486 scopus 로고    scopus 로고
    • The effects of chronic administration of nimodipine on age- Related changes in nitric oxide and its synthase in senescence-accelerated mouse brain
    • Inada, K., Yokoi, I., Kabuto, H., Namba, Y., and Ogawa, N. 1997 The effects of chronic administration of nimodipine on age- related changes in nitric oxide and its synthase in senescence-accelerated mouse brain. Biochem. Mol, Biol. Int. 41:753-765.
    • (1997) Biochem. Mol, Biol. Int. , vol.41 , pp. 753-765
    • Inada, K.1    Yokoi, I.2    Kabuto, H.3    Namba, Y.4    Ogawa, N.5
  • 117
  • 118
    • 0029550811 scopus 로고
    • Role of the cytokines in the hypothalamic-pituitary-adrenal and gonadal axes
    • Spangelo, B. L., Judd, A.M., Call, G. B., Zumwalt, J., and Gorospe, W. C. 1995. Role of the cytokines in the hypothalamic-pituitary-adrenal and gonadal axes. Neuroimmunomod. 2: 299-312.
    • (1995) Neuroimmunomod. , vol.2 , pp. 299-312
    • Spangelo, B.L.1    Judd, A.M.2    Call, G.B.3    Zumwalt, J.4    Gorospe, W.C.5
  • 119
    • 0030846399 scopus 로고    scopus 로고
    • The nitric oxide hypothesis of brain aging
    • McCann, S. M. 1997. The nitric oxide hypothesis of brain aging. Exp. Gerontol. 32:431-440.
    • (1997) Exp. Gerontol. , vol.32 , pp. 431-440
    • McCann, S.M.1
  • 122
    • 0028948660 scopus 로고
    • Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases
    • Chagnon, P., Betard, C., Robitaille, Y., Cholette, A., and Gauvreau, D. 1995. Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases. NeuroReport. 6:711-715.
    • (1995) NeuroReport , vol.6 , pp. 711-715
    • Chagnon, P.1    Betard, C.2    Robitaille, Y.3    Cholette, A.4    Gauvreau, D.5
  • 123
    • 0032504622 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative disorders
    • Schapira, A. H. 1998. Mitochondrial dysfunction in neurodegenerative disorders. Biochim. Biophys. Acta 1366:225-233.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 225-233
    • Schapira, A.H.1
  • 124
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery, W. R. 1997. Oxidative stress hypothesis in Alzheimer's disease. Free Radie. Biol. Med. 23:134-147.
    • (1997) Free Radie. Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 125
    • 0028364696 scopus 로고
    • Immunocytochemical analysis of tumor necrosis factor and its receptors in Parkinson's disease
    • Boka, G., Anglade, P., Wallach, D., Javoy Agid, F., Agid, Y., and Hirsch, E. C. 1994. Immunocytochemical analysis of tumor necrosis factor and its receptors in Parkinson's disease. Neurosci. Lett. 172:151-154.
    • (1994) Neurosci. Lett. , vol.172 , pp. 151-154
    • Boka, G.1    Anglade, P.2    Wallach, D.3    Javoy Agid, F.4    Agid, Y.5    Hirsch, E.C.6
  • 126
    • 0029161781 scopus 로고
    • Glial cytokines in Alzheimer's disease: Review and pathogenic implications
    • Mrak, R. E., Sheng, J. G., and Griffin, W. S. 1995. Glial cytokines in Alzheimer's disease: review and pathogenic implications. Hum. Pathol. 26:816-823.
    • (1995) Hum. Pathol. , vol.26 , pp. 816-823
    • Mrak, R.E.1    Sheng, J.G.2    Griffin, W.S.3
  • 129
    • 0031687793 scopus 로고    scopus 로고
    • Understanding cell death in Parkinson's disease
    • Jenner, P. and Olanow, C. W. 1998. Understanding cell death in Parkinson's disease. Ann. Neurol. 44:872-84.
    • (1998) Ann. Neurol. , vol.44 , pp. 872-884
    • Jenner, P.1    Olanow, C.W.2
  • 130
    • 0029984860 scopus 로고    scopus 로고
    • Role of neuronal nitric oxide in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced dopaminergic neurotoxicity
    • Przedborski, S., Jackson Lewis, V., Yokoyama, R., Shibata, T., Dawson, V. L., and Dawson, T. M. 1996. Role of neuronal nitric oxide in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced dopaminergic neurotoxicity. Proc. Natl. Acad. Sci. USA 93:4565-4571.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4565-4571
    • Przedborski, S.1    Jackson Lewis, V.2    Yokoyama, R.3    Shibata, T.4    Dawson, V.L.5    Dawson, T.M.6
  • 131
    • 0028173033 scopus 로고
    • S100 beta protein expression in Alzheimer disease: Potential role in the pathogenesis of neuritic plaques
    • Sheng, J. G., Mrak, R. E., and Griffin, W. S. 1994. S100 beta protein expression in Alzheimer disease: potential role in the pathogenesis of neuritic plaques. J. Neurosci. Res. 39: 398-404.
    • (1994) J. Neurosci. Res. , vol.39 , pp. 398-404
    • Sheng, J.G.1    Mrak, R.E.2    Griffin, W.S.3
  • 132
    • 0029671449 scopus 로고    scopus 로고
    • S100 beta stimulates inducible nitric oxide synthase activity and mRNA levels in rat cortical astrocytes
    • Hu, J., Castets, F., Guevara, J. L., and Van Eldik, L. J. 1996. S100 beta stimulates inducible nitric oxide synthase activity and mRNA levels in rat cortical astrocytes. J. Biol. Chem. 271:2543-2547.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2543-2547
    • Hu, J.1    Castets, F.2    Guevara, J.L.3    Van Eldik, L.J.4
  • 133
    • 0026500329 scopus 로고
    • Production of hydroxyl radicals from the simultaneous generation of Superoxide and nitric oxide
    • Hogg, N., Darley Usmar, V. M., Wilson, M. T., and Moncada, S. 1992. Production of hydroxyl radicals from the simultaneous generation of Superoxide and nitric oxide. Biochem. J. 281:419-424.
    • (1992) Biochem. J. , vol.281 , pp. 419-424
    • Hogg, N.1    Darley Usmar, V.M.2    Wilson, M.T.3    Moncada, S.4
  • 134
    • 0031012323 scopus 로고    scopus 로고
    • Effect of nitric oxide on iron-mediated oxidative stress in primary rat hepatocyte culture
    • Sergent, O., Griffon, B., Morel, I., Chevanne, M., Dubos, M. P., Cillard, P., and Cillard, J. 1997. Effect of nitric oxide on iron-mediated oxidative stress in primary rat hepatocyte culture. Hepatology 25:122-127.
    • (1997) Hepatology , vol.25 , pp. 122-127
    • Sergent, O.1    Griffon, B.2    Morel, I.3    Chevanne, M.4    Dubos, M.P.5    Cillard, P.6    Cillard, J.7
  • 135
    • 0031128377 scopus 로고    scopus 로고
    • Inhibition of ferritin- Stimulated microsomal production of reactive oxygen intermediates by nitric oxide
    • Puntarulo, S. and Cederbaum, A. I. 1997. Inhibition of ferritin- stimulated microsomal production of reactive oxygen intermediates by nitric oxide. Arch. Biochem. Biophys. 340:19-26.
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 19-26
    • Puntarulo, S.1    Cederbaum, A.I.2
  • 138
    • 0029994840 scopus 로고    scopus 로고
    • Nitric oxide delays the death of trophic factor-deprived PC12 cells and sympathetic neurons by a cGMP-mediated mechanism
    • Farinelli, S. E., Park, D. S., and Greene, L. A. 1996. Nitric oxide delays the death of trophic factor-deprived PC12 cells and sympathetic neurons by a cGMP-mediated mechanism. J. Neurosci. 16:2325-2334.
    • (1996) J. Neurosci. , vol.16 , pp. 2325-2334
    • Farinelli, S.E.1    Park, D.S.2    Greene, L.A.3
  • 139
    • 0031059681 scopus 로고    scopus 로고
    • Nitric oxide regulates nitric oxide synthase-2 gene expression by inhibiting NF-kappaB binding to DNA
    • Park, S. K., Lin, H. L., and Murphy, S. 1997. Nitric oxide regulates nitric oxide synthase-2 gene expression by inhibiting NF-kappaB binding to DNA. Biochem. J. 322:609-613.
    • (1997) Biochem. J. , vol.322 , pp. 609-613
    • Park, S.K.1    Lin, H.L.2    Murphy, S.3
  • 140
    • 0033515479 scopus 로고    scopus 로고
    • Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase
    • Mohr, S., Hallak, H., de Boitte, A., Lapetina, E. G., and Brune, B. 1999. Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 274:9427-9430.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9427-9430
    • Mohr, S.1    Hallak, H.2    De Boitte, A.3    Lapetina, E.G.4    Brune, B.5
  • 141
    • 0031968628 scopus 로고    scopus 로고
    • Nuclear localization of overexpressed glyceraldehyde-3-phosphate dehydrogenase in cultured cerebellar neurons undergoing apoptosis
    • Ishitani, R., Tanaka, M., Sunaga, K., Katsube, N., and Chuang, D. M. 1998. Nuclear localization of overexpressed glyceraldehyde-3-phosphate dehydrogenase in cultured cerebellar neurons undergoing apoptosis. Mol. Pharmacol. 53:701-707.
    • (1998) Mol. Pharmacol. , vol.53 , pp. 701-707
    • Ishitani, R.1    Tanaka, M.2    Sunaga, K.3    Katsube, N.4    Chuang, D.M.5
  • 142
    • 0032778865 scopus 로고    scopus 로고
    • Intracellular redox state determines whether nitric oxide is toxic or protective to rat oligodendrocytes in culture
    • Rosenberg, P. A., Li, Y., Ali, S., Altiok, N., Back, S. A., and Volpe, J. J. 1999. Intracellular redox state determines whether nitric oxide is toxic or protective to rat oligodendrocytes in culture. J. Neurochem. 73:476-484.
    • (1999) J. Neurochem. , vol.73 , pp. 476-484
    • Rosenberg, P.A.1    Li, Y.2    Ali, S.3    Altiok, N.4    Back, S.A.5    Volpe, J.J.6
  • 143
    • 0029865996 scopus 로고    scopus 로고
    • Secretion of nitrite by Schwann cells and its effect on T-cell activation in vitro
    • Gold, R., Zielasek, J., Kiefer, R., Toyka, K. V., and Hartung, H. P. 1996. Secretion of nitrite by Schwann cells and its effect on T-cell activation in vitro. Cell Immunol. 168:69-77.
    • (1996) Cell Immunol. , vol.168 , pp. 69-77
    • Gold, R.1    Zielasek, J.2    Kiefer, R.3    Toyka, K.V.4    Hartung, H.P.5
  • 145
    • 0032510832 scopus 로고    scopus 로고
    • Multiple NFkB enhancer elements regulate cytokine induction of the human of the human inducible nitric oxide synthase gene
    • Taylor, B. S., de Vera, M. E., Ganster, R. W., Wang, Q., Shapiro, R. A., Morris, S. M., Billiar, T. R., and Geller, D. A. 1998. Multiple NFkB enhancer elements regulate cytokine induction of the human of the human inducible nitric oxide synthase gene. J. Biol. Chem. 273:15148-15156.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15148-15156
    • Taylor, B.S.1    De Vera, M.E.2    Ganster, R.W.3    Wang, Q.4    Shapiro, R.A.5    Morris, S.M.6    Billiar, T.R.7    Geller, D.A.8
  • 147
    • 0033558215 scopus 로고    scopus 로고
    • The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis
    • Zong, W. X., Edelstein, L. C., Chen, C., Bash, J., and Gelinas, C. 1999. The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis. Genes. Dev. 13:382-387.
    • (1999) Genes. Dev. , vol.13 , pp. 382-387
    • Zong, W.X.1    Edelstein, L.C.2    Chen, C.3    Bash, J.4    Gelinas, C.5
  • 148
    • 0030611750 scopus 로고    scopus 로고
    • Activation of NF-kappaB protects hippocampal neurons against oxidative stress-induced apoptosis: Evidence for induction of manganese superoxide dismutase and suppression of peroxynitrite production and protein tyrosine nitration
    • Mattson, M. P., Goodman, Y., Luo, H., Fu, W., and Furukawa, K. 1997. Activation of NF-kappaB protects hippocampal neurons against oxidative stress-induced apoptosis: evidence for induction of manganese superoxide dismutase and suppression of peroxynitrite production and protein tyrosine nitration. J. Neurosci. Res. 49:681-697.
    • (1997) J. Neurosci. Res. , vol.49 , pp. 681-697
    • Mattson, M.P.1    Goodman, Y.2    Luo, H.3    Fu, W.4    Furukawa, K.5
  • 150
    • 0032971367 scopus 로고    scopus 로고
    • Kainic acid-induced activation of nuclear factor-kB in rat hippocampus
    • Matsuoka, K., Kitamura, Y., Okazaki, M., Terai, K., and Taniguchi, T. 1999. Kainic acid-induced activation of nuclear factor-kB in rat hippocampus. Exp. Brain Res. 124:215-222.
    • (1999) Exp. Brain Res. , vol.124 , pp. 215-222
    • Matsuoka, K.1    Kitamura, Y.2    Okazaki, M.3    Terai, K.4    Taniguchi, T.5
  • 151
    • 0029100808 scopus 로고
    • Increased cortical nuclear factor-kB DNA binding activity after traumatic brain injury in rats
    • Yang, R., Mu, X., and Hayes, R. L. 1995. Increased cortical nuclear factor-kB DNA binding activity after traumatic brain injury in rats. Neurosci. Lett. 197:101-104.
    • (1995) Neurosci. Lett. , vol.197 , pp. 101-104
    • Yang, R.1    Mu, X.2    Hayes, R.L.3
  • 152
    • 0030983079 scopus 로고    scopus 로고
    • Transcription factor NF-kappaB is activated in primary neurons by amyloid beta peptides and in neurons surrounding early plaques from patients with Alzheimer disease
    • Kaltschmidt, B., Uherek, M., Volk, B., Baeuerle, P. A., and Kaltschmidt, C. 1997. Transcription factor NF-kappaB is activated in primary neurons by amyloid beta peptides and in neurons surrounding early plaques from patients with Alzheimer disease. Proc. Natl. Acad. Sci. USA 94:2642-2647.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2642-2647
    • Kaltschmidt, B.1    Uherek, M.2    Volk, B.3    Baeuerle, P.A.4    Kaltschmidt, C.5
  • 153
    • 0031469483 scopus 로고    scopus 로고
    • c-Jun, JNK/SAPK kinases and transcription factor NF- Kappa B are selectively activated in astrocytes, but not motor neurons, in amyotrophic lateral sclerosis
    • Migheli, A., Piva, R., Atzori, C., Troost, D., and Schiffer, D. 1997. c-Jun, JNK/SAPK kinases and transcription factor NF- kappa B are selectively activated in astrocytes, but not motor neurons, in amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 56:1314-1322.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 1314-1322
    • Migheli, A.1    Piva, R.2    Atzori, C.3    Troost, D.4    Schiffer, D.5
  • 155
    • 0033593574 scopus 로고    scopus 로고
    • Expression of calbindin-D28k in C6 glial cells stabilizes intracellular calcium levels and protects against apoptosis induced by calcium ionophore and amyloid beta-peptide
    • Wernyj, R. P., Mattson, M. P., and Christakos, S. 1999. Expression of calbindin-D28k in C6 glial cells stabilizes intracellular calcium levels and protects against apoptosis induced by calcium ionophore and amyloid beta-peptide. Brain Res. Mol. Brain. Res. 64:69-79.
    • (1999) Brain Res. Mol. Brain. Res. , vol.64 , pp. 69-79
    • Wernyj, R.P.1    Mattson, M.P.2    Christakos, S.3
  • 156
    • 0032508414 scopus 로고    scopus 로고
    • NF-kappaB antiapoptosis: Induction of TRAF1 and TRAF2 and c-IAP1 and C-IAP2 to suppress caspase-8 activation
    • Wang, C. Y., Mayo, M. W., Korneluk, R. G., Goeddel, D. V., and Baldwin, A. S. 1998. NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and C-IAP2 to suppress caspase-8 activation. Science 281:1680-1683.
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin, A.S.5
  • 157
    • 0031938280 scopus 로고    scopus 로고
    • Nuclear factor-kappa B contributes to excitotoxin-induced apoptosis in rat striatum
    • Qin, Z. H., Wang, Y., Nakai, M., and Chase, T. N. 1998. Nuclear factor-kappa B contributes to excitotoxin-induced apoptosis in rat striatum. Mol. Pharmacol. 53:33-42.
    • (1998) Mol. Pharmacol. , vol.53 , pp. 33-42
    • Qin, Z.H.1    Wang, Y.2    Nakai, M.3    Chase, T.N.4
  • 158
    • 0032014073 scopus 로고    scopus 로고
    • DNA damaging agents induce expression of Fas ligand and subsequent apoptosis in T lymphocytes via the activation of NF-kappaB and AP-1
    • Kasibhatla, S., Brunner, T., Genestier, L., Echeverri, F., Mahboubi, A., and Green, D. R. (1998) DNA damaging agents induce expression of Fas ligand and subsequent apoptosis in T lymphocytes via the activation of NF-kappaB and AP-1. Mol. Cell 4:543-551.
    • (1998) Mol. Cell , vol.4 , pp. 543-551
    • Kasibhatla, S.1    Brunner, T.2    Genestier, L.3    Echeverri, F.4    Mahboubi, A.5    Green, D.R.6
  • 159
    • 0034054249 scopus 로고    scopus 로고
    • Adenoviral vector-mediated transfer of human heme oxygenase in rats decreases renal heme-dependent arachidonic acid epoxygenase activity
    • Abraham, N. G., Jiang, S., Yang, L., Zand, B. A., Laniado- Schwartzman, M., Marji, J., Drummond, G. S., and Kappas, A. 2000. Adenoviral vector-mediated transfer of human heme oxygenase in rats decreases renal heme-dependent arachidonic acid epoxygenase activity. J. Pharmacol. Exp. Ther. 293:494-500.
    • (2000) J. Pharmacol. Exp. Ther. , vol.293 , pp. 494-500
    • Abraham, N.G.1    Jiang, S.2    Yang, L.3    Zand, B.A.4    Laniado-Schwartzman, M.5    Marji, J.6    Drummond, G.S.7    Kappas, A.8
  • 160
    • 0032755381 scopus 로고    scopus 로고
    • The neuroprotective potential of heat shock protein (HSP70)
    • Yenay, M. A., Giffard, R., Sapolsky, R. M., and Steinberg, G. K. 1999. The neuroprotective potential of heat shock protein (HSP70). Mol. Med. Tod. 51:525-531.
    • (1999) Mol. Med. Tod. , vol.51 , pp. 525-531
    • Yenay, M.A.1    Giffard, R.2    Sapolsky, R.M.3    Steinberg, G.K.4
  • 162
    • 0031773001 scopus 로고    scopus 로고
    • Attenuated c-fos mRNA induction after middle cerebral artery occlusion in CREB knockout mice does not modulate focal ischemic injury
    • Hata, R., Gass, P., Mies, G., Wiessner, C., and Hossmann, K. A. 1998. Attenuated c-fos mRNA induction after middle cerebral artery occlusion in CREB knockout mice does not modulate focal ischemic injury. J. Cereb. Blood. Flow. Metab. 18:1325-1335.
    • (1998) J. Cereb. Blood. Flow. Metab. , vol.18 , pp. 1325-1335
    • Hata, R.1    Gass, P.2    Mies, G.3    Wiessner, C.4    Hossmann, K.A.5
  • 163
    • 0029563171 scopus 로고
    • Pharmacological induction of heat shock protein 68 synthesis in cultured rat astrocytes
    • Nishimura, R. N. and Dwyer, B. E. 1995. Pharmacological induction of heat shock protein 68 synthesis in cultured rat astrocytes. J. Biol. Chem. 270:29967-29970.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29967-29970
    • Nishimura, R.N.1    Dwyer, B.E.2
  • 164
    • 0031020041 scopus 로고    scopus 로고
    • Defective herpes simplex virus vectors expressing the rat brain stress-inducible heat shock protein 72 protect cultured neurons from severe heat shock
    • Fink, S. L., Chang, L. K., Ho, D. Y., and Sapolsky, R. M. 1997. Defective herpes simplex virus vectors expressing the rat brain stress-inducible heat shock protein 72 protect cultured neurons from severe heat shock. J. Neurochem. 68:961-969.
    • (1997) J. Neurochem. , vol.68 , pp. 961-969
    • Fink, S.L.1    Chang, L.K.2    Ho, D.Y.3    Sapolsky, R.M.4
  • 165
    • 0031057892 scopus 로고    scopus 로고
    • Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells
    • Huot, J., Houle, F., Marceau, F., and Landry, J. 1997. Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells. Circ. Res. 80:383-392.
    • (1997) Circ. Res. , vol.80 , pp. 383-392
    • Huot, J.1    Houle, F.2    Marceau, F.3    Landry, J.4
  • 167
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • Laney, J. D. and Hochstrasser, M. 1999. Substrate targeting in the ubiquitin system. Cell 97:427-430.
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 168
    • 0031795906 scopus 로고    scopus 로고
    • Expression of HSP27 results in increased sensitivity to tumor necrosis factor, etoposide, and H2O2 in an oxidative stress-resistant cell line
    • Mairesse, N., Bernaert, D., Del Bino, G., Herman, S., Mosselmans, R., Robaye, B., and Galand, P. 1998. Expression of HSP27 results in increased sensitivity to tumor necrosis factor, etoposide, and H2O2 in an oxidative stress-resistant cell line. J. Cell Physiol. 177:606-617.
    • (1998) J. Cell Physiol. , vol.177 , pp. 606-617
    • Mairesse, N.1    Bernaert, D.2    Del Bino, G.3    Herman, S.4    Mosselmans, R.5    Robaye, B.6    Galand, P.7
  • 169
    • 0033582784 scopus 로고    scopus 로고
    • Anti-oxidants prevent focal rat brain injury as assessed by induction of heat shock proteins (HSP70, HO-1/HSP32, HSP47) following subarachnoid injections of lysed blood
    • Turner, C. P., Panter, S. S., and Sharp, F. R. 1999. Anti-oxidants prevent focal rat brain injury as assessed by induction of heat shock proteins (HSP70, HO-1/HSP32, HSP47) following subarachnoid injections of lysed blood. Brain Res. Mol. Brain Res. 65:87-102.
    • (1999) Brain Res. Mol. Brain Res. , vol.65 , pp. 87-102
    • Turner, C.P.1    Panter, S.S.2    Sharp, F.R.3
  • 170
    • 0033104877 scopus 로고    scopus 로고
    • Heat shock protein protection
    • Sharp, F. R., Massa, S., and Swanson R. A. 1999. Heat shock protein protection. TINS 22:97-99.
    • (1999) TINS , vol.22 , pp. 97-99
    • Sharp, F.R.1    Massa, S.2    Swanson, R.A.3
  • 171
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system; a regulator of second messenger gases
    • Maines, M. D. 1997. The heme oxygenase system; a regulator of second messenger gases. Annu. Rev. Pharmacol. Toxicol. 37:517-554.
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 172
    • 0032780311 scopus 로고    scopus 로고
    • Heat shock factor function and regulation in response to cellular stress, growth, and differentiation signals
    • Morano, K. A. and Thiele, D. J. 1999. Heat shock factor function and regulation in response to cellular stress, growth, and differentiation signals. Gene Expr. 7:271-282.
    • (1999) Gene Expr. , vol.7 , pp. 271-282
    • Morano, K.A.1    Thiele, D.J.2
  • 173
    • 0032972686 scopus 로고    scopus 로고
    • Overexpression of heme oxygenase-1 is neuroprotective in a model of permanent middle cerebral artery occlusion in transgenic mice
    • Panahian, N., Yoshiura, M., and Maines, M. D. 1999. Overexpression of heme oxygenase-1 is neuroprotective in a model of permanent middle cerebral artery occlusion in transgenic mice. J. Neurochem. 72:1187-1203.
    • (1999) J. Neurochem. , vol.72 , pp. 1187-1203
    • Panahian, N.1    Yoshiura, M.2    Maines, M.D.3
  • 174
    • 0029032632 scopus 로고
    • Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain
    • Schipper, H. M., Cissè, S., and Stopa, E. G. 1995. Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain. Ann. Neurol. 37:758-768.
    • (1995) Ann. Neurol. , vol.37 , pp. 758-768
    • Schipper, H.M.1    Cissè, S.2    Stopa, E.G.3
  • 175
    • 0032031011 scopus 로고    scopus 로고
    • Neural Heme oxygenase-1 expression in idiopathic Parkinson's disease
    • Schipper, H. M., Liberman, A., and Stopa, E. G. 1998. Neural Heme oxygenase-1 expression in idiopathic Parkinson's disease. Exp. Neurol. 150:60-68.
    • (1998) Exp. Neurol. , vol.150 , pp. 60-68
    • Schipper, H.M.1    Liberman, A.2    Stopa, E.G.3
  • 177
    • 0033847184 scopus 로고    scopus 로고
    • The indispensability of heme oxygenase-1 in protecting against acute heme protein-induced toxicity in vivo
    • Nath, K. A., Haggard, J. J., Croatt, A. J., Grande, J. P., Poss, K. D., and Alam, J. 2000. The indispensability of heme oxygenase-1 in protecting against acute heme protein-induced toxicity in vivo. Am. J. Pathol. 156:1527-1535.
    • (2000) Am. J. Pathol. , vol.156 , pp. 1527-1535
    • Nath, K.A.1    Haggard, J.J.2    Croatt, A.J.3    Grande, J.P.4    Poss, K.D.5    Alam, J.6
  • 178
    • 0026012324 scopus 로고
    • Rapid induction of heme oxygenase 1 mRNa and protein by hyperhermia in rat brain: Heme oxygenase 2 is not a heat shock protein
    • Ewing, J. F. and Maines, M. D. 1991. Rapid induction of heme oxygenase 1 mRNA and protein by hyperhermia in rat brain: heme oxygenase 2 is not a heat shock protein. Proc. Natl. Acad. Sci. USA 88:5364-5368.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5364-5368
    • Ewing, J.F.1    Maines, M.D.2
  • 179
    • 0031238801 scopus 로고    scopus 로고
    • Apoptosis and delayed neuronal damage after carbon monoxide poisoning in the rat
    • Piantadosi, C. A., Zhang, J., Levin, E. D., Folz, R. J., and Schmechel, D. E. 1997. Apoptosis and delayed neuronal damage after carbon monoxide poisoning in the rat. Exp. Neurol. 147:103-114.
    • (1997) Exp. Neurol. , vol.147 , pp. 103-114
    • Piantadosi, C.A.1    Zhang, J.2    Levin, E.D.3    Folz, R.J.4    Schmechel, D.E.5
  • 180
    • 0028656497 scopus 로고
    • Molecular mechanisms of nitric oxide actions in the brain
    • Dawson, T. M., Dawson, V. L., and Snyder, S. H. 1994. Molecular mechanisms of nitric oxide actions in the brain. Ann. NY Acad. Sci. 738:76-85.
    • (1994) Ann. NY Acad. Sci. , vol.738 , pp. 76-85
    • Dawson, T.M.1    Dawson, V.L.2    Snyder, S.H.3
  • 181
    • 0025153308 scopus 로고
    • Study on the mechanism of carbon monoxide induced endothelium-independent relaxation in porcine coronary artery and vein
    • Graser, T., vedernikov, Y. P., and Li, D. S. 1990. Study on the mechanism of carbon monoxide induced endothelium-independent relaxation in porcine coronary artery and vein. Biomed. Biochim. Acta 49:293-296.
    • (1990) Biomed. Biochim. Acta , vol.49 , pp. 293-296
    • Graser, T.1    Vedernikov, Y.P.2    Li, D.S.3
  • 182
    • 0027288834 scopus 로고
    • Zinc protoporphyrin-IX blocks the effects of metabotropic glutamate receptor activation in the rat nucleus tractus solitarii
    • Glaum, S. R. and Miller, R. J. 1993. Zinc protoporphyrin-IX blocks the effects of metabotropic glutamate receptor activation in the rat nucleus tractus solitarii. Mol. Pharmacol. 43:965-969.
    • (1993) Mol. Pharmacol. , vol.43 , pp. 965-969
    • Glaum, S.R.1    Miller, R.J.2
  • 184
    • 0026735580 scopus 로고
    • Nitric oxide synthase is a cytochrome P-450 hemoprotein
    • White, L. A. and Marletta, M. A. 1992. Nitric oxide synthase is a cytochrome P-450 hemoprotein. Biochemistry 31:6627-6631.
    • (1992) Biochemistry , vol.31 , pp. 6627-6631
    • White, L.A.1    Marletta, M.A.2
  • 185
    • 0031747888 scopus 로고    scopus 로고
    • Pathophysiology of brain edema and cell changes following hypertermic brain injury
    • Sharma, H. S., Westman, J. (eds) Elsevier, Amsterdam
    • Sharma, H. S., Westman, J., and Nyberg, F. 1998. Pathophysiology of brain edema and cell changes following hypertermic brain injury. Pages 351-412, in: Sharma, H. S., Westman, J. (eds) Brain function in hot environment (Vol. 115) Progress in brain research, Elsevier, Amsterdam.
    • (1998) Brain Function in Hot Environment (Vol. 115) Progress in Brain Research , vol.115 , pp. 351-412
    • Sharma, H.S.1    Westman, J.2    Nyberg, F.3
  • 186
    • 0032757252 scopus 로고    scopus 로고
    • The heme oxygenase pathway and its interaction with nitric oxide in the control of cellular homeostasis
    • Foresti, R. and Motterlini R. 1999. The heme oxygenase pathway and its interaction with nitric oxide in the control of cellular homeostasis. Free Rad. Res. 31:459-475.
    • (1999) Free Rad. Res. , vol.31 , pp. 459-475
    • Foresti, R.1    Motterlini, R.2
  • 187
    • 0032322227 scopus 로고    scopus 로고
    • Nitric oxide synthase inhibition by haeme oxigenase decreases macrophage nitric oxide-dependent cytotoxicity: A negative feedback mechanism for the regulation of nitric oxide production
    • Turcanu, V., Dhouib, M., and Poindron, P. 1998. Nitric oxide synthase inhibition by haeme oxigenase decreases macrophage nitric oxide-dependent cytotoxicity: a negative feedback mechanism for the regulation of nitric oxide production. Res. Immunol. 149:741-744.
    • (1998) Res. Immunol. , vol.149 , pp. 741-744
    • Turcanu, V.1    Dhouib, M.2    Poindron, P.3
  • 188
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn SOD gene are associated with familial amyotrophic lateral sclerosis
    • Rosen, D. R., Siddique, T., and Patterson, D. 1993. Mutations in Cu/Zn SOD gene are associated with familial amyotrophic lateral sclerosis. Nature 362:59-62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3
  • 189
    • 0042945215 scopus 로고
    • Clinical implications of basic research: A transgenic-mouse model of amyothrophic lateral sclerosis
    • Brwon, R. H. 1994. Clinical implications of basic research: a transgenic-mouse model of amyothrophic lateral sclerosis. N. Engl. J. Med. 331:1091-1092.
    • (1994) N. Engl. J. Med. , vol.331 , pp. 1091-1092
    • Brwon, R.H.1
  • 191
    • 0032858753 scopus 로고    scopus 로고
    • Cholinergic neuro- Modulation and Alzheimer's disease: From single cells to network simulations
    • Menschik, E. D. and Finkel, L. H. 1999 Cholinergic neuro- modulation and Alzheimer's disease: from single cells to network simulations. Prog. Brain Res. 121:19-45.
    • (1999) Prog. Brain Res. , vol.121 , pp. 19-45
    • Menschik, E.D.1    Finkel, L.H.2
  • 192
    • 0033954991 scopus 로고    scopus 로고
    • Oxidative stress and Alzheimer disease
    • Christen, Y. 2000. Oxidative stress and Alzheimer disease. Am. J. Clin. Nutr. 71:6218-6298.
    • (2000) Am. J. Clin. Nutr. , vol.71 , pp. 6218-6298
    • Christen, Y.1
  • 195
    • 0033964859 scopus 로고    scopus 로고
    • In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: A central role for bound transition metals
    • Sayre, L. M., Perry, G., Harris, P. L., Liu, Y., Schubert, K. A., and Smith, M. A. 2000. In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: a central role for bound transition metals. J. Neurochem. 74:270-279.
    • (2000) J. Neurochem. , vol.74 , pp. 270-279
    • Sayre, L.M.1    Perry, G.2    Harris, P.L.3    Liu, Y.4    Schubert, K.A.5    Smith, M.A.6
  • 197
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery, W. R. 1997. Oxidative stress hypothesis in Alzheimer's disease. Free Rad. Biol. Med. 23:134-147.
    • (1997) Free Rad. Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 199
    • 0032799823 scopus 로고    scopus 로고
    • Vitamin E as an antioxidant/free radical scavenger against amyloid β-peptide-induced oxidative stress in neocortical synaptosomal membranes and hippocampal neurons in culture: Insights into Alzheimer's disease
    • Butterfield, D. A., Koppal, T., Subramaniam, R., and Yatin, S. 1999. Vitamin E as an antioxidant/free radical scavenger against amyloid β-peptide-induced oxidative stress in neocortical synaptosomal membranes and hippocampal neurons in culture: Insights into Alzheimer's disease. Rev. Neurosci. 10:141-149.
    • (1999) Rev. Neurosci. , vol.10 , pp. 141-149
    • Butterfield, D.A.1    Koppal, T.2    Subramaniam, R.3    Yatin, S.4
  • 200
    • 0032498829 scopus 로고    scopus 로고
    • Vitamin E protects against Alzheimer's amyloid peptide (25-35)-induced changes in neocortical synaptosomal membrane lipid structure and composition
    • Koppal, T., Subramaniam, R., Drake, J., Prasad, R. P., Dhillon, H., and Butterfield, D. A. 1998 Vitamin E protects against Alzheimer's amyloid peptide (25-35)-induced changes in neocortical synaptosomal membrane lipid structure and composition. Brain Res. 786:270-273.
    • (1998) Brain Res. , vol.786 , pp. 270-273
    • Koppal, T.1    Subramaniam, R.2    Drake, J.3    Prasad, R.P.4    Dhillon, H.5    Butterfield, D.A.6
  • 201
    • 0033133579 scopus 로고    scopus 로고
    • In-vitro and in-vivo oxidative stress associated with Alzheimer's amyloid β-peptide (1-42)
    • Yatin, S. M., Kink, C. D., and Butterfield, D. A. 1999 In-vitro and in-vivo oxidative stress associated with Alzheimer's amyloid β-peptide (1-42). Neurobiol. of Aging 20:325-330.
    • (1999) Neurobiol. of Aging , vol.20 , pp. 325-330
    • Yatin, S.M.1    Kink, C.D.2    Butterfield, D.A.3
  • 202
    • 0032696045 scopus 로고    scopus 로고
    • On methionine and Alzheimer's amyloid, β-peptide (1-42)-induced oxidative stress
    • Butterfield, D. A. 1999. On methionine and Alzheimer's amyloid, β-peptide (1-42)-induced oxidative stress. Neurobiol. of Aging 20:339-342.
    • (1999) Neurobiol. of Aging , vol.20 , pp. 339-342
    • Butterfield, D.A.1
  • 203
    • 0028908516 scopus 로고
    • Direct evidence of oxidative injury by the Alzheimer's amyloid β-peptide in cultured hippocampal neurons
    • Harris, M. E., Hensley, K., Butterfield, D. A., Leedle, R. E., and Carney, J. M. 1995. Direct evidence of oxidative injury by the Alzheimer's amyloid β-peptide in cultured hippocampal neurons. Exp. Neurol. 131:193-202.
    • (1995) Exp. Neurol. , vol.131 , pp. 193-202
    • Harris, M.E.1    Hensley, K.2    Butterfield, D.A.3    Leedle, R.E.4    Carney, J.M.5
  • 204
    • 0030928406 scopus 로고    scopus 로고
    • β-Amyloid-associated free radical oxidative stress and neurotoxicity: Implications for Alzheimer's disease
    • Butterfield, D. A. 1997 β-Amyloid-associated free radical oxidative stress and neurotoxicity: Implications for Alzheimer's disease. Chem. Res. Toxicol. 10:495-506.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 495-506
    • Butterfield, D.A.1
  • 205
    • 0032510580 scopus 로고    scopus 로고
    • Alzheimer's peptide kills cells of retina in vivo
    • Jen, L. S., Hart, A. J., Jen, A., Relvas, J. B., and Gentleman, S. M. 1998 Alzheimer's peptide kills cells of retina in vivo. Nature. 392:140-141.
    • (1998) Nature , vol.392 , pp. 140-141
    • Jen, L.S.1    Hart, A.J.2    Jen, A.3    Relvas, J.B.4    Gentleman, S.M.5
  • 207
    • 0029670094 scopus 로고    scopus 로고
    • β-amyloid-mediated vasoactivity and vascular endothelial damage
    • Thomas, T., Thomas, G., McLendon, C., Sutton, T., and Mullan, M. 1996 β-amyloid-mediated vasoactivity and vascular endothelial damage. Nature 380:168-171.
    • (1996) Nature , vol.380 , pp. 168-171
    • Thomas, T.1    Thomas, G.2    McLendon, C.3    Sutton, T.4    Mullan, M.5
  • 208
    • 0026547646 scopus 로고
    • Plasma concentrations of vitamin A and E and carotenoids in Alzheimer's disease
    • Zaman, Z., Roche, S., Fielden, P., Niriella, D. C., and Cayley, A. C. 1992. Plasma concentrations of vitamin A and E and carotenoids in Alzheimer's disease. Age Ageing 21:91-94.
    • (1992) Age Ageing , vol.21 , pp. 91-94
    • Zaman, Z.1    Roche, S.2    Fielden, P.3    Niriella, D.C.4    Cayley, A.C.5
  • 211
    • 0031010921 scopus 로고    scopus 로고
    • Lou Gehrig and amyotrophic lateral sclerosis. Is vitamin E to be revisited?
    • Reider, C. R. and Paulson, G. W. 1997 Lou Gehrig and amyotrophic lateral sclerosis. Is vitamin E to be revisited? Arch. Neurol. 54:527-528.
    • (1997) Arch. Neurol. , vol.54 , pp. 527-528
    • Reider, C.R.1    Paulson, G.W.2
  • 212
    • 0032786731 scopus 로고    scopus 로고
    • Oxidative stress indicators are elevated in de novo Parkinson's disease patients
    • Ilic, T. V., Jovanovic, M., Jovicic, A., and Tomovic, M. 1999. Oxidative stress indicators are elevated in de novo Parkinson's disease patients. Funct. Neurol. 14:141-147.
    • (1999) Funct. Neurol. , vol.14 , pp. 141-147
    • Ilic, T.V.1    Jovanovic, M.2    Jovicic, A.3    Tomovic, M.4
  • 214
    • 0031722906 scopus 로고    scopus 로고
    • Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: Possible mechanisms of formation involving reactive oxygen species
    • Spencer, J. P., Jenner, P., Daniel, S. E., Lees, A. J., Marsden, D. C., and Halliwell, B. 1998. Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: possible mechanisms of formation involving reactive oxygen species. J. Neurochem. 71:2112-2122.
    • (1998) J. Neurochem. , vol.71 , pp. 2112-2122
    • Spencer, J.P.1    Jenner, P.2    Daniel, S.E.3    Lees, A.J.4    Marsden, D.C.5    Halliwell, B.6
  • 215
    • 0025821265 scopus 로고
    • Alterations in the levels of iron ferritin and other trace metals in Parkinson's diseases affecting the basal ganglia
    • Dexter, D. T., Carayon, A., Javoy-Agid, F., Agid, Y., Wells, F. R., Daniel, S., Lees, A. J., Jenner, P., and Marsden, C. D. 1991. Alterations in the levels of iron ferritin and other trace metals in Parkinson's diseases affecting the basal ganglia. Brain 114: 1953-1975.
    • (1991) Brain , vol.114 , pp. 1953-1975
    • Dexter, D.T.1    Carayon, A.2    Javoy-Agid, F.3    Agid, Y.4    Wells, F.R.5    Daniel, S.6    Lees, A.J.7    Jenner, P.8    Marsden, C.D.9
  • 217
    • 0030886119 scopus 로고    scopus 로고
    • Irreversible inhibition of mitochondrial complex I by 2-aminoethyl-3,4-dyhydro-5-hydroxy-2-benzothiazine-3-carboxylic acid (DHBT): A putative nigral endotoxin of relevance to Parkinson's disease
    • Li H., Dryhurst, G. 1997. Irreversible inhibition of mitochondrial complex I by 2-aminoethyl-3,4-dyhydro-5-hydroxy-2-benzothiazine-3-carboxylic acid (DHBT): a putative nigral endotoxin of relevance to Parkinson's disease. J. Neurochem. 69:1530-1541.
    • (1997) J. Neurochem. , vol.69 , pp. 1530-1541
    • Li, H.1    Dryhurst, G.2
  • 218
    • 0028081018 scopus 로고
    • Intense oxidative DNA damage promoted by L-DOPA and its metabolites. Implication for neurodegenerative diseases
    • Spencer, J., Jenner, A., Aruoma, O., Evans, P., Jenner, P., Lees, A., Marsden, D., and Halliwell, B. 1994. Intense oxidative DNA damage promoted by L-DOPA and its metabolites. Implication for neurodegenerative diseases. FEBS Lett. 353:246-250.
    • (1994) FEBS Lett. , vol.353 , pp. 246-250
    • Spencer, J.1    Jenner, A.2    Aruoma, O.3    Evans, P.4    Jenner, P.5    Lees, A.6    Marsden, D.7    Halliwell, B.8
  • 219
    • 0020308323 scopus 로고
    • Parkinson's disease: A disorder due to nigral glutathione deficiency?
    • Perry, T. L., Godin, D. V., and Hansen, S. 1982. Parkinson's disease: a disorder due to nigral glutathione deficiency? Neurosci. Lett. 33:305-310.
    • (1982) Neurosci. Lett. , vol.33 , pp. 305-310
    • Perry, T.L.1    Godin, D.V.2    Hansen, S.3
  • 220
    • 0028075410 scopus 로고
    • Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting the basal ganglia
    • Sian, J., Dexter, D. T., and Lees, A. J. 1994. Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting the basal ganglia. Ann. Neurol. 36: 348-355.
    • (1994) Ann. Neurol. , vol.36 , pp. 348-355
    • Sian, J.1    Dexter, D.T.2    Lees, A.J.3
  • 222
    • 0030885945 scopus 로고    scopus 로고
    • Mitochondrial free radical signal in ceramide- Dependent apoptosis: A putative mechanism for neuronal death in Parkinson's disease
    • France-Lanord, V., Brugg, B., Michel, P. P., Agid, Y., and Ruberg, M. 1997. Mitochondrial free radical signal in ceramide- dependent apoptosis: a putative mechanism for neuronal death in Parkinson's disease. J. Neurochem. 69:1612-1621.
    • (1997) J. Neurochem. , vol.69 , pp. 1612-1621
    • France-Lanord, V.1    Brugg, B.2    Michel, P.P.3    Agid, Y.4    Ruberg, M.5
  • 223
    • 0025254401 scopus 로고
    • Mitochondrial complex I deficiency in Parkinson disease
    • Schapira, A. H. V., Cooper, J. M., and Dexter, D. 1990. Mitochondrial complex I deficiency in Parkinson disease. J. Neurochem. 54:823-827.
    • (1990) J. Neurochem. , vol.54 , pp. 823-827
    • Schapira, A.H.V.1    Cooper, J.M.2    Dexter, D.3
  • 224
    • 0031711224 scopus 로고    scopus 로고
    • Excitotoxicity and nitric oxide in Parkinson's disease pathogenesis
    • Beal, M. F. 1998 Excitotoxicity and nitric oxide in Parkinson's disease pathogenesis Ann. Neurol. 44:8110-4.
    • (1998) Ann. Neurol. , vol.44 , pp. 8110-8114
    • Beal, M.F.1
  • 225
    • 0029741063 scopus 로고    scopus 로고
    • The future of genetic studies of complex human diseases
    • Risch, N. and Merikangas, K. 1996. The future of genetic studies of complex human diseases. Science 273:1516-1517.
    • (1996) Science , vol.273 , pp. 1516-1517
    • Risch, N.1    Merikangas, K.2
  • 226
    • 0031748566 scopus 로고    scopus 로고
    • Multiple sclerosis: In situ evidence for antibody- And complement-mediated demyelination
    • Storch, M. K., Piddlesden, S., Haltia, M., livanainen, M., Morgan, P., and Lassmann, H. 1998. Multiple sclerosis: in situ evidence for antibody- and complement-mediated demyelination. Ann. Neurol. 43:465-471.
    • (1998) Ann. Neurol. , vol.43 , pp. 465-471
    • Storch, M.K.1    Piddlesden, S.2    Haltia, M.3    Livanainen, M.4    Morgan, P.5    Lassmann, H.6
  • 227
    • 0030723381 scopus 로고    scopus 로고
    • T cell- T cell activation in multiple sclerosis
    • Lindsey, J. W., Kerman, R. H., and Wolinsky, J. S. 1997. T cell- T cell activation in multiple sclerosis, Mult. Scler. 3:238-242.
    • (1997) Mult. Scler. , vol.3 , pp. 238-242
    • Lindsey, J.W.1    Kerman, R.H.2    Wolinsky, J.S.3
  • 228
    • 0031774301 scopus 로고    scopus 로고
    • The small heat shock protein alpha B- Crystallin as key autoantigen in multiple sclerosis
    • van Noort, J. M., van Sechel, A. C., van Stipdonk M. J., and Bajramovic, J. J. 1998 The small heat shock protein alpha B- crystallin as key autoantigen in multiple sclerosis. Prog. Brain Res. 117:435-452.
    • (1998) Prog. Brain Res. , vol.117 , pp. 435-452
    • Van Noort, J.M.1    Van Sechel, A.C.2    Van Stipdonk, M.J.3    Bajramovic, J.J.4
  • 229
    • 0029945794 scopus 로고    scopus 로고
    • Multiple sclerosis: An altered immune response or an altered stress response?
    • van Noort, J. M. 1996 Multiple sclerosis: an altered immune response or an altered stress response? J. Mol. Med. 74:285-296.
    • (1996) J. Mol. Med. , vol.74 , pp. 285-296
    • Van Noort, J.M.1
  • 230
    • 0026500136 scopus 로고
    • Evidence for increased lipid peroxidation in multiple sclerosis
    • Toshniwal, P. K. and Zarling, E. J. 1992. Evidence for increased lipid peroxidation in multiple sclerosis. Neurochem. Res. 17: 205-207.
    • (1992) Neurochem. Res. , vol.17 , pp. 205-207
    • Toshniwal, P.K.1    Zarling, E.J.2
  • 233
    • 0027265381 scopus 로고
    • Free radical in brain metabolism and pathology
    • Evans, P. H. 1993. Free radical in brain metabolism and pathology. Br. Med. Bull. 49:577-587.
    • (1993) Br. Med. Bull. , vol.49 , pp. 577-587
    • Evans, P.H.1
  • 234
    • 0023918725 scopus 로고
    • Brain glucose utilization in childhood Huntington's disease studied with positron emission tomography (PET)
    • De Voldr, A., Bol, A., Michel, C., Cogneau, M., Evrard, P., Lyon, G., and Goffinet, A. M. 1988. Brain glucose utilization in childhood Huntington's disease studied with positron emission tomography (PET). Brain Dev. 10:47-50.
    • (1988) Brain Dev. , vol.10 , pp. 47-50
    • De Voldr, A.1    Bol, A.2    Michel, C.3    Cogneau, M.4    Evrard, P.5    Lyon, G.6    Goffinet, A.M.7
  • 235
    • 0001984611 scopus 로고
    • Cerebral circulation, energy metabolism, and protein synthesis: General characteristics and principles of measurement
    • Phelps, M. E., Mazziotta, J. C., Schelbert, H. R. (eds), Raven press, New York
    • Sokoloff, L. 1986. Cerebral circulation, energy metabolism, and protein synthesis: general characteristics and principles of measurement. Pages 1-71, in Phelps, M. E., Mazziotta, J. C., Schelbert, H. R. (eds), Positron Emission Tomography and Autoradiography: Principles and applications for the brain and heart. Raven press, New York.
    • (1986) Positron Emission Tomography and Autoradiography: Principles and Applications for the Brain and Heart , pp. 1-71
    • Sokoloff, L.1
  • 236
    • 0027741301 scopus 로고
    • Evidence for an energy metabolism defect in Huntington's disease using localized proton spectroscopy
    • Jenkins, B., Koroshetz, W., Beal, M. F., and Rosen, B. 1993. Evidence for an energy metabolism defect in Huntington's disease using localized proton spectroscopy. Neurol. 43:2689-2695.
    • (1993) Neurol. , vol.43 , pp. 2689-2695
    • Jenkins, B.1    Koroshetz, W.2    Beal, M.F.3    Rosen, B.4
  • 237
    • 0027272037 scopus 로고
    • CSF and serum metabolic profile of patients with Huntington' s chorea: A study by high resolution proton NMR spectroscopy and HPLC
    • Nicoli, F., Vion-Dury, J., Maloteaux, J. M., Delwaide, C., Confort-Gouny, S., Sciaky, M., and Cozzone, P. J. 1993. CSF and serum metabolic profile of patients with Huntington' s chorea: a study by high resolution proton NMR spectroscopy and HPLC. Neurosci. Lett. 154:47-51.
    • (1993) Neurosci. Lett. , vol.154 , pp. 47-51
    • Nicoli, F.1    Vion-Dury, J.2    Maloteaux, J.M.3    Delwaide, C.4    Confort-Gouny, S.5    Sciaky, M.6    Cozzone, P.J.7
  • 238
    • 0003759727 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative damage in Huntington's disease
    • Flint Beal, M., Howell, N., Bodis-Wollner, I. (eds), Wiley-Liss, New York
    • Browne, S. E. 1997. Mitochondrial dysfunction and oxidative damage in Huntington's disease, in Flint Beal, M., Howell, N., Bodis-Wollner, I. (eds), Mitochondria and Free Radicals in Neurodegenerative diseases, Wiley-Liss, New York.
    • (1997) Mitochondria and Free Radicals in Neurodegenerative Diseases
    • Browne, S.E.1
  • 240
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace, D. C. 1999. Mitochondrial diseases in man and mouse. Science 283:1482-1488.
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 241
    • 0030961030 scopus 로고    scopus 로고
    • Nitric oxide induces heat-shock protein 70 expression in vascular smooth muscle cells via activation of heat shock factor 1
    • Xu, Q., Hu, Y., Kleindienst, M., and Wick, G. 1997. Nitric oxide induces heat-shock protein 70 expression in vascular smooth muscle cells via activation of heat shock factor 1. J. Clin. Invest. 100:1089-1097.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1089-1097
    • Xu, Q.1    Hu, Y.2    Kleindienst, M.3    Wick, G.4
  • 242
  • 244
    • 0032748502 scopus 로고    scopus 로고
    • Serch for novel cytoprotective and antiviral prostanoids
    • Santoro, M. G. and Roberts, S. M. Serch for novel cytoprotective and antiviral prostanoids. 1999. Drug News Perspect 12: 395-400.
    • (1999) Drug News Perspect , vol.12 , pp. 395-400
    • Santoro, M.G.1    Roberts, S.M.2
  • 245
    • 0033555548 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription-1 and heat shock factor-1 interact and activate the transcription of the Hsp-70 and Hsp-90beta gene promoters
    • Stephanou, A., Isenberg, D. A., Nakajima, K., and Latchman, D. S. 1999. Signal transducer and activator of transcription-1 and heat shock factor-1 interact and activate the transcription of the Hsp-70 and Hsp-90beta gene promoters. J. Biol. Chem. 274:1723-1728.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1723-1728
    • Stephanou, A.1    Isenberg, D.A.2    Nakajima, K.3    Latchman, D.S.4


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