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Volumn 23, Issue 1, 1997, Pages 134-147

Oxidative stress hypothesis in Alzheimer's disease

Author keywords

4 Hydroxynonenal; Aluminum; Alzheimer's disease; Amyloid beta peptide; Antioxidants; Brain iron; Lipid peroxidation; Mercury; Oxidative stress; Protein and DNA oxidation

Indexed keywords

4 HYDROXYNONENAL; AMYLOID P COMPONENT; CYTOCHROME C OXIDASE; HEME OXYGENASE; MALONALDEHYDE; PEROXYNITRITE; POLYUNSATURATED FATTY ACID; SUPEROXIDE DISMUTASE;

EID: 0030915855     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(96)00629-6     Document Type: Article
Times cited : (2082)

References (155)
  • 1
    • 0000293742 scopus 로고
    • Uber eine eigenartige Erkrankung der Hirnride
    • Alzheimer A. Uber eine eigenartige Erkrankung der Hirnride. Allg. Z. Psychiatr. 64:1907;146-148.
    • (1907) Allg. Z. Psychiatr. , vol.64 , pp. 146-148
    • Alzheimer, A.1
  • 3
    • 0016942101 scopus 로고
    • The prevalence and malignancy of Alzheimer's disease: A major killer
    • Katzman R. The prevalence and malignancy of Alzheimer's disease: A major killer. Arch. Neurol. 33:1976;217-218.
    • (1976) Arch. Neurol. , vol.33 , pp. 217-218
    • Katzman, R.1
  • 4
    • 0011191383 scopus 로고
    • National Institute on Aging. Progress report on Alzheimer's disease (NIH publications no. 95-3994) Washington DC: US Government Printing Office.
    • National Institute on Aging. Progress report on Alzheimer's disease (NIH publications no. 95-3994) 1995, Washington DC: US Government Printing Office.
    • (1995)
  • 5
    • 0021271971 scopus 로고
    • Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDA Work Group under the auspices of the Department of Health and Human Services Task Force on Alzheimer's Disease
    • McKhann G. D., Drachman D. A., Folstein M. F., Katzman R., Price D., Stadlan E. M. Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDA Work Group under the auspices of the Department of Health and Human Services Task Force on Alzheimer's Disease. Neurology. 34:1984;939-944.
    • (1984) Neurology , vol.34 , pp. 939-944
    • McKhann, G.D.1    Drachman, D.A.2    Folstein, M.F.3    Katzman, R.4    Price, D.5    Stadlan, E.M.6
  • 6
    • 0022414054 scopus 로고
    • Diagnosis of Alzheimer's disease
    • Khachaturian Z. S. Diagnosis of Alzheimer's disease. Arch. Neurol. 42:1985;1097-1105.
    • (1985) Arch. Neurol. , vol.42 , pp. 1097-1105
    • Khachaturian, Z.S.1
  • 7
    • 0025908356 scopus 로고
    • The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • Mirra S. S., Heyman A., McKeel D., Sumi S. M., Crain B. J., Brownlee L. M., Vogel F. S., Hughes J. P., Van Belle G., Berg L. The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology. 41:1991;479-486.
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3    Sumi, S.M.4    Crain, B.J.5    Brownlee, L.M.6    Vogel, F.S.7    Hughes, J.P.8    Van Belle, G.9    Berg, L.10
  • 8
    • 0019972810 scopus 로고
    • The cholinergic hypothesis of geriatric memory dysfunction
    • Bartus R. T., Dean R. L., Beer B., Lippa A. S. The cholinergic hypothesis of geriatric memory dysfunction. Science. 217:1982;408-414.
    • (1982) Science , vol.217 , pp. 408-414
    • Bartus, R.T.1    Dean, R.L.2    Beer, B.3    Lippa, A.S.4
  • 11
    • 0019256571 scopus 로고
    • Reduced somatostatin-like immunoreactivity in cerebral cortex from cases of Alzheimer disease and Alzheimer senile dementia
    • Davies P., Katzman R., Terry R. D. Reduced somatostatin-like immunoreactivity in cerebral cortex from cases of Alzheimer disease and Alzheimer senile dementia. Nature. 288:1980;279-280.
    • (1980) Nature , vol.288 , pp. 279-280
    • Davies, P.1    Katzman, R.2    Terry, R.D.3
  • 12
    • 84944358442 scopus 로고
    • Corticotropin-releasing factor-like immunoreactivity in senile dementia of the Alzheimer type reduced cortical and striatal concentrations
    • Bissette G., Reynolds G. P., Kilts C. A., Widerlov E., Nemeroff C. B. Corticotropin-releasing factor-like immunoreactivity in senile dementia of the Alzheimer type reduced cortical and striatal concentrations. JAMA. 254:1985;3067-3069.
    • (1985) JAMA , vol.254 , pp. 3067-3069
    • Bissette, G.1    Reynolds, G.P.2    Kilts, C.A.3    Widerlov, E.4    Nemeroff, C.B.5
  • 14
    • 0013461669 scopus 로고
    • The molecular genetics of Alzheimer disease
    • R.D. Terry, R. Katzman, & K.L. Bick. New York: Raven Press
    • St. George-Hyslop P. H. The molecular genetics of Alzheimer disease. Terry R. D., Katzman R., Bick K. L. Alzheimer disease. 1993;345-352 Raven Press, New York.
    • (1993) Alzheimer disease , pp. 345-352
    • St. George-Hyslop, P.H.1
  • 21
    • 0022636502 scopus 로고
    • The epidemiology of Alzheimer's disease
    • Henderson A. S. The epidemiology of Alzheimer's disease. Brit. Med. Bull. 42:1986;3-10.
    • (1986) Brit. Med. Bull. , vol.42 , pp. 3-10
    • Henderson, A.S.1
  • 22
    • 0002759709 scopus 로고
    • Epidemiology and etiology of Alzheimer's disease
    • J.T. Hutton, & A.D. Kenny. New York: Alan R. Liss, Inc
    • Mortimer J. A., Hutton J. T. Epidemiology and etiology of Alzheimer's disease. Hutton J. T., Kenny A. D. Senile dementia of the Alzheimer's type. 1985;177-196 Alan R. Liss, Inc, New York.
    • (1985) Senile dementia of the Alzheimer's type , pp. 177-196
    • Mortimer, J.A.1    Hutton, J.T.2
  • 23
  • 24
    • 0030066467 scopus 로고    scopus 로고
    • Linguistic ability in early life and cognitive function and Alzheimer's disease in late life: Findings from the Nun study
    • Snowdon D. A., Kemper S. J., Mortimer J. A., Greiner L. H., Wekstein D. R., Markesbery W. R. Linguistic ability in early life and cognitive function and Alzheimer's disease in late life: findings from the Nun study. JAMA. 275:1996;528-532.
    • (1996) JAMA , vol.275 , pp. 528-532
    • Snowdon, D.A.1    Kemper, S.J.2    Mortimer, J.A.3    Greiner, L.H.4    Wekstein, D.R.5    Markesbery, W.R.6
  • 25
    • 0001115832 scopus 로고
    • Alzheimer's disease
    • A.K. Asbury, G.M. McKhann, & W.I. McDonald. Philadelphia: W. B. Saunders Co
    • Markesbery W. R. Alzheimer's disease. Asbury A. K., McKhann G. M., McDonald W. I. Diseases of the nervous system: Clinical neurobiology. 1992;795-803 W. B. Saunders Co, Philadelphia.
    • (1992) Diseases of the nervous system: Clinical neurobiology , pp. 795-803
    • Markesbery, W.R.1
  • 26
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate and neurodegenerative disorders
    • Coyle J. T., Puttfarcken P. Oxidative stress, glutamate and neurodegenerative disorders. Science. 262:1993;689-695.
    • (1993) Science , vol.262 , pp. 689-695
    • Coyle, J.T.1    Puttfarcken, P.2
  • 27
    • 0027496238 scopus 로고
    • A radical hypothesis for neurodegeneration
    • Olanow C. W. A radical hypothesis for neurodegeneration. Trends Neurosci. 16:1993;439-444.
    • (1993) Trends Neurosci. , vol.16 , pp. 439-444
    • Olanow, C.W.1
  • 32
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD-1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong P., Pardo C. A., Borchelt D. R., Lee M. K., Copeland N. G., Jenkins N. A., Sisodia S. S., Cleveland D. W., Price D. L. An adverse property of a familial ALS-linked SOD-1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron. 14:1995;1105-1116.
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.1    Pardo, C.A.2    Borchelt, D.R.3    Lee, M.K.4    Copeland, N.G.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9
  • 36
    • 0001367060 scopus 로고
    • Brain trace elements in Alzheimer disease
    • R.D. Terry, R. Katzman, & K.L. Bick. New York: Raven Press
    • Markesbery W. R., Ehmann W. D. Brain trace elements in Alzheimer disease. Terry R. D., Katzman R., Bick K. L. Alzheimer disease. 1993;353-367 Raven Press, New York.
    • (1993) Alzheimer disease , pp. 353-367
    • Markesbery, W.R.1    Ehmann, W.D.2
  • 37
    • 0003536299 scopus 로고
    • B. Halliwell, & J.M.C. Gutteridge. Oxford: Clarendon Press
    • Halliwell B., Gutteridge J. M. C. Free radicals in biology and medicine. ed 2:1989;Clarendon Press, Oxford.
    • (1989) Free radicals in biology and medicine ed 2
  • 38
    • 84938039523 scopus 로고
    • Alzheimer's disease: A clinico-pathologic analysis of twenty-three cases with a theory on pathogenesis
    • Goodman L. Alzheimer's disease: A clinico-pathologic analysis of twenty-three cases with a theory on pathogenesis. J. Nerv. Ment. Dis. 117:1953;97-130.
    • (1953) J. Nerv. Ment. Dis. , vol.117 , pp. 97-130
    • Goodman, L.1
  • 42
    • 0026573467 scopus 로고
    • Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: A laser microprobe (LAMMA) study
    • Good P. F., Perl D. P., Bierer L. M., Schmeidler J. Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: A laser microprobe (LAMMA) study. Ann. Neurol. 31:1992;286-292.
    • (1992) Ann. Neurol. , vol.31 , pp. 286-292
    • Good, P.F.1    Perl, D.P.2    Bierer, L.M.3    Schmeidler, J.4
  • 43
    • 0023448968 scopus 로고
    • Ferritin: Isolation of aluminum-ferritin complex from brain
    • Fleming J., Joshi J. G. Ferritin: Isolation of aluminum-ferritin complex from brain. Proc. Natl. Acad. Sci. USA. 84:1987;7866-7870.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7866-7870
    • Fleming, J.1    Joshi, J.G.2
  • 48
    • 0029955035 scopus 로고    scopus 로고
    • Serum levels of the iron binding protein p97 are elevated in Alzheimer's disease
    • Kennard M. L., Feldman H., Yamada T., Jefferies W. A. Serum levels of the iron binding protein p97 are elevated in Alzheimer's disease. Nature Med. 2:1996;1230-1235.
    • (1996) Nature Med. , vol.2 , pp. 1230-1235
    • Kennard, M.L.1    Feldman, H.2    Yamada, T.3    Jefferies, W.A.4
  • 49
    • 0029935613 scopus 로고    scopus 로고
    • Reactive microglia specifically associated with amyloid plaques in Alzheimer's disease brain tissue express melanotransferrin
    • Jefferies W. A., Food M. R., Gabathuler R., Rothenberger S., Yamada T., Yasuhara O., McGeer P. L. Reactive microglia specifically associated with amyloid plaques in Alzheimer's disease brain tissue express melanotransferrin. Brain Res. 712:1996;122-126.
    • (1996) Brain Res. , vol.712 , pp. 122-126
    • Jefferies, W.A.1    Food, M.R.2    Gabathuler, R.3    Rothenberger, S.4    Yamada, T.5    Yasuhara, O.6    McGeer, P.L.7
  • 50
    • 0027082739 scopus 로고
    • Brain aluminum in Alzhemier's disease using improved GFAAS method
    • Xu N., Majidi V., Markesbery W. R., Ehmann W. D. Brain aluminum in Alzhemier's disease using improved GFAAS method. Neurotoxicology. 13:1992;735-744.
    • (1992) Neurotoxicology , vol.13 , pp. 735-744
    • Xu, N.1    Majidi, V.2    Markesbery, W.R.3    Ehmann, W.D.4
  • 51
    • 0026598228 scopus 로고
    • Aluminosilicate-induced free radical generation by murine brain glial cells in vitro: Potential significance in the aetiopathogenesis of Alzheimer's dementia
    • Evans P. H., Peterhan E., Bürge T., Klinowski J. Aluminosilicate-induced free radical generation by murine brain glial cells in vitro: Potential significance in the aetiopathogenesis of Alzheimer's dementia. Dementia. 3:1992;1-6.
    • (1992) Dementia , vol.3 , pp. 1-6
    • Evans, P.H.1    Peterhan, E.2    Bürge, T.3    Klinowski, J.4
  • 53
    • 0021823762 scopus 로고
    • Aluminum salts accelaerate peroxidation of membrane lipids stimulated by iron salts
    • Gutteridge J. M. C., Quinlan G. J., Clark I., Halliwell B. Aluminum salts accelaerate peroxidation of membrane lipids stimulated by iron salts. Biochem. Biophys. Acta. 835:1985;441-447.
    • (1985) Biochem. Biophys. Acta , vol.835 , pp. 441-447
    • Gutteridge, J.M.C.1    Quinlan, G.J.2    Clark, I.3    Halliwell, B.4
  • 54
    • 0028302137 scopus 로고
    • A mechanism for the stimulatory effect of aluminum on iron-induced lipid peroxidation
    • Oteiza P. I. A mechanism for the stimulatory effect of aluminum on iron-induced lipid peroxidation. Arch. Biochem. Biophys. 308:1994;374-379.
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 374-379
    • Oteiza, P.I.1
  • 55
    • 0020031220 scopus 로고
    • Cellular toxicity and lipid peroxidation in response to mercury
    • Stacey N. H., Kappus H. Cellular toxicity and lipid peroxidation in response to mercury. Toxiocol. App. Pharmacol. 63:1982;29-35.
    • (1982) Toxiocol. App. Pharmacol. , vol.63 , pp. 29-35
    • Stacey, N.H.1    Kappus, H.2
  • 56
    • 0030297178 scopus 로고    scopus 로고
    • Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer's disease: Possible relation to oxidative stress
    • Deibel M. A., Ehmann W. D., Markesbery W. R. Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer's disease: possible relation to oxidative stress. J. Neurol. Sci. in press. 143:1996;137-142.
    • (1996) J. Neurol. Sci. in press , vol.143 , pp. 137-142
    • Deibel, M.A.1    Ehmann, W.D.2    Markesbery, W.R.3
  • 57
    • 0027327899 scopus 로고
    • Ceruloplasmin levels in the human superior temporal gyrus in aging and Alzheimer's disease
    • Connor J. R., Tucker P., Johnson M., Snyder B. Ceruloplasmin levels in the human superior temporal gyrus in aging and Alzheimer's disease. Neurosci. Lett. 159:1993;88-90.
    • (1993) Neurosci. Lett. , vol.159 , pp. 88-90
    • Connor, J.R.1    Tucker, P.2    Johnson, M.3    Snyder, B.4
  • 58
    • 0025788446 scopus 로고
    • Effects of ceruloplasmin on superoxide dependent iron release from ferritin and lipid peroxidation
    • Samokyszyn V. M., Reif D. W., Miller D. M., Aust S. D. Effects of ceruloplasmin on superoxide dependent iron release from ferritin and lipid peroxidation. Free Radic. Res. Comms. 12-13:1991;153-159.
    • (1991) Free Radic. Res. Comms. , vol.1213 , pp. 153-159
    • Samokyszyn, V.M.1    Reif, D.W.2    Miller, D.M.3    Aust, S.D.4
  • 59
    • 0029935396 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease in the reduction of Copper (II) to Copper (I)
    • Multhaup G., Schlicksupp A., Hesse L., Beher D., Ruppert T., Masters C. L., Beyreuther K. The amyloid precursor protein of Alzheimer's disease in the reduction of Copper (II) to Copper (I). Science. 271:1996;1406-1409.
    • (1996) Science , vol.271 , pp. 1406-1409
    • Multhaup, G.1    Schlicksupp, A.2    Hesse, L.3    Beher, D.4    Ruppert, T.5    Masters, C.L.6    Beyreuther, K.7
  • 62
    • 0027936618 scopus 로고
    • Electron paramagnetic resonance investigations of free radical induced alterations in neocortical synaptosomal membrane protein infrastructure
    • Hensley K., Carney J. M., Hall N., Shaus W., Butterfield D. A. Electron paramagnetic resonance investigations of free radical induced alterations in neocortical synaptosomal membrane protein infrastructure. Free Radic. Biol. Med. 17:1994;321-331.
    • (1994) Free Radic. Biol. Med. , vol.17 , pp. 321-331
    • Hensley, K.1    Carney, J.M.2    Hall, N.3    Shaus, W.4    Butterfield, D.A.5
  • 64
    • 0028152717 scopus 로고
    • Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease
    • Mecocci P., MacGarvey U., Beal M. F. Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease. Ann. Neurol. 36:1994;747-751.
    • (1994) Ann. Neurol. , vol.36 , pp. 747-751
    • Mecocci, P.1    MacGarvey, U.2    Beal, M.F.3
  • 65
    • 0029073455 scopus 로고
    • Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease
    • Lovell M. A., Ehmann W. D., Butler S. M., Markesbery W. R. Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease. Neurology. 45:1995;1594-1601.
    • (1995) Neurology , vol.45 , pp. 1594-1601
    • Lovell, M.A.1    Ehmann, W.D.2    Butler, S.M.3    Markesbery, W.R.4
  • 66
    • 0025334082 scopus 로고
    • Autopsy samples of Alzheimer's cortex show increased peroxidation in vitro
    • Subbarao K. V., Richardson J. S., Ang L. C. Autopsy samples of Alzheimer's cortex show increased peroxidation in vitro. J. Neurochem. 55:1990;342-345.
    • (1990) J. Neurochem. , vol.55 , pp. 342-345
    • Subbarao, K.V.1    Richardson, J.S.2    Ang, L.C.3
  • 67
    • 0028129137 scopus 로고
    • Evidence of an oxidative challenge in the Alzheimer's brain
    • Balazs L., Leon M. Evidence of an oxidative challenge in the Alzheimer's brain. Neurochem. Res. 19:1994;1131-1137.
    • (1994) Neurochem. Res. , vol.19 , pp. 1131-1137
    • Balazs, L.1    Leon, M.2
  • 68
    • 0025699758 scopus 로고
    • Brain membrane fluidity and lipid peroxidation in Alzheimer's disease
    • Hajimohammadreza I., Brammer M. Brain membrane fluidity and lipid peroxidation in Alzheimer's disease. Neurosci. Lett. 112:1990;333-337.
    • (1990) Neurosci. Lett. , vol.112 , pp. 333-337
    • Hajimohammadreza, I.1    Brammer, M.2
  • 69
    • 0028181782 scopus 로고
    • Selective increase in lipid peroxidation in the inferior temporal cortex in Alzheimer's disease
    • Palmer A. M., Burns M. A. Selective increase in lipid peroxidation in the inferior temporal cortex in Alzheimer's disease. Brain Res. 645:1994;338-342.
    • (1994) Brain Res. , vol.645 , pp. 338-342
    • Palmer, A.M.1    Burns, M.A.2
  • 70
    • 0000341879 scopus 로고
    • Free radicals, oxidative stress and neurodegeneration
    • D.B. Calne. Philadelphia: WB Saunders Co
    • Cohen G., Werner P. Free radicals, oxidative stress and neurodegeneration. Calne D. B. Neurodegenerative diseases. 1994;139-161 WB Saunders Co, Philadelphia.
    • (1994) Neurodegenerative diseases , pp. 139-161
    • Cohen, G.1    Werner, P.2
  • 71
    • 0029417023 scopus 로고
    • Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro
    • Busciglio J., Yankner B. A. Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro. Nature. 378:1995;776-779.
    • (1995) Nature , vol.378 , pp. 776-779
    • Busciglio, J.1    Yankner, B.A.2
  • 72
    • 0025571476 scopus 로고
    • The role of alterations in membrane lipid composition in enabling physiological adaptation of organisms to their physical environment
    • Hazel J. R., Williams E. E. The role of alterations in membrane lipid composition in enabling physiological adaptation of organisms to their physical environment. Prog. Lipid. Res. 29:1990;167-227.
    • (1990) Prog. Lipid. Res. , vol.29 , pp. 167-227
    • Hazel, J.R.1    Williams, E.E.2
  • 73
    • 84996120592 scopus 로고
    • Oxidants and the central nervous system: Some fundamental questions. Is oxidant damage relevant to Parkinson's disease, Alzheimer's disease, traumatic injury or stroke?
    • Halliwell B. Oxidants and the central nervous system: some fundamental questions. Is oxidant damage relevant to Parkinson's disease, Alzheimer's disease, traumatic injury or stroke? Acta Neurol. Scand. 126:1989;23-33.
    • (1989) Acta Neurol. Scand. , vol.126 , pp. 23-33
    • Halliwell, B.1
  • 75
    • 0022931005 scopus 로고
    • In vitro 31p NMR spectroscopy detects altered phospholipid metabolism in Alzheimer's disease
    • Miatto O., Gonzalez R. G., Buonanno F., Growdon J. H. In vitro 31p NMR spectroscopy detects altered phospholipid metabolism in Alzheimer's disease. Can. J. Neurol. Sci. 13:1986;535-539.
    • (1986) Can. J. Neurol. Sci. , vol.13 , pp. 535-539
    • Miatto, O.1    Gonzalez, R.G.2    Buonanno, F.3    Growdon, J.H.4
  • 78
    • 0028157335 scopus 로고
    • Membrane lipids, selectively diminished in Alzheimer brains, suggest synapse loss as a primary event in early-onset (type I) and demyelination in late-onset form (type II)
    • Svennerholm L., Gottfries C. G. Membrane lipids, selectively diminished in Alzheimer brains, suggest synapse loss as a primary event in early-onset (type I) and demyelination in late-onset form (type II). J. Neurochem. 62:1994;1039-1047.
    • (1994) J. Neurochem. , vol.62 , pp. 1039-1047
    • Svennerholm, L.1    Gottfries, C.G.2
  • 79
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehyes
    • Esterbauer H., Schaur R. J., Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehyes. Free Radic. Biol. Med. 11:1991;81-128.
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 80
    • 0030714092 scopus 로고    scopus 로고
    • Elevated 4-hydroxynonenal in ventricular fluid in Alzheimer's disease
    • (submitted).
    • Lovell, M. A.; Ehmann, W. D.; Markesbery, W. R. Elevated 4-hydroxynonenal in ventricular fluid in Alzheimer's disease.Neurobiology of Aging (submitted).
    • Neurobiology of Aging
    • Lovell, M.A.1    Ehmann, W.D.2    Markesbery, W.R.3
  • 81
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid β -peptide
    • Mark R. J., Lovell M. A., Markesbery W. R., Uchida K., Mattson M. P. A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid β -peptide. Journal of Neurochemistry. 68:1997;255-264.
    • (1997) Journal of Neurochemistry , vol.68 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesbery, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 83
    • 0030040310 scopus 로고    scopus 로고
    • E-4-hydroxy-2-nonenal is cytotoxic and cross-links cytoskeletal proteins in P19 neuroglial cultures
    • Montine T. J., Amarnath V., Martin M. E., Strittmatter W. J., Graham D. G. E-4-hydroxy-2-nonenal is cytotoxic and cross-links cytoskeletal proteins in P19 neuroglial cultures. Am. J. Pathol. 148:1996;89-93.
    • (1996) Am. J. Pathol. , vol.148 , pp. 89-93
    • Montine, T.J.1    Amarnath, V.2    Martin, M.E.3    Strittmatter, W.J.4    Graham, D.G.5
  • 85
    • 0022665705 scopus 로고
    • Brain glutathione peroxidase in neurodegenerative disorders
    • Kish S. J., Morito C. L., Hornykiewicz O. Brain glutathione peroxidase in neurodegenerative disorders. Neurochem. Pathol. 4:1986;23-28.
    • (1986) Neurochem. Pathol. , vol.4 , pp. 23-28
    • Kish, S.J.1    Morito, C.L.2    Hornykiewicz, O.3
  • 87
    • 0026286747 scopus 로고
    • Concentrations of several proteins characteristic of nervous tissue in cerebral cortex of patients with Alzheimer's disease
    • Kato K., Kurobe N., Suzuki R., Morishita R., Asano T., Sato T., Inagaki T. Concentrations of several proteins characteristic of nervous tissue in cerebral cortex of patients with Alzheimer's disease. J. Mol. Neurosci. 3:1991;95-99.
    • (1991) J. Mol. Neurosci. , vol.3 , pp. 95-99
    • Kato, K.1    Kurobe, N.2    Suzuki, R.3    Morishita, R.4    Asano, T.5    Sato, T.6    Inagaki, T.7
  • 88
    • 0027500793 scopus 로고
    • Free radicals in the genesis of Alzheimer's disease
    • Richardson J. S. Free radicals in the genesis of Alzheimer's disease. Ann. NY Acad. Sci. 695:1993;73-76.
    • (1993) Ann. NY Acad. Sci. , vol.695 , pp. 73-76
    • Richardson, J.S.1
  • 89
    • 0021984002 scopus 로고
    • Superoxide dismutase isoenzymes in normal brains and in brains from patients with dementia of Alzheimer type
    • Marklund S. L., Adolfsson R., Gottfries C. G., Winblad B. Superoxide dismutase isoenzymes in normal brains and in brains from patients with dementia of Alzheimer type. J. Neurol. Sci. 67:1985;319-325.
    • (1985) J. Neurol. Sci. , vol.67 , pp. 319-325
    • Marklund, S.L.1    Adolfsson, R.2    Gottfries, C.G.3    Winblad, B.4
  • 90
    • 0019475899 scopus 로고
    • Nonenzymatic browning in vivo: Possible process for aging of long-lived proteins
    • Monnier V. M., Cerami A. Nonenzymatic browning in vivo: possible process for aging of long-lived proteins. Science. 211:1981;491-493.
    • (1981) Science , vol.211 , pp. 491-493
    • Monnier, V.M.1    Cerami, A.2
  • 92
    • 0024852380 scopus 로고
    • Structure elucidation of a senescence cross-link from human extracellular matrix: Implication of pentoses in the aging process
    • Sell D. R., Monnier V. M. Structure elucidation of a senescence cross-link from human extracellular matrix: implication of pentoses in the aging process. J. Biol. Chem. 264:1989;21597-21602.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21597-21602
    • Sell, D.R.1    Monnier, V.M.2
  • 93
    • 0025930287 scopus 로고
    • Oxidative glycation and free radical production: A causal mechanism of diabetic complications
    • Hunt J. V., Wolff S. P. Oxidative glycation and free radical production: a causal mechanism of diabetic complications. Free Radic. Res. Commun. 12-13 Pt. 1:1991;115-123.
    • (1991) Free Radic. Res. Commun. , vol.12-13 PART 1 , pp. 115-123
    • Hunt, J.V.1    Wolff, S.P.2
  • 99
    • 0023809230 scopus 로고
    • Alzheimer's disease: A double-labeling immunohistochemical study of senile plaques
    • Dickson D. W., Farlo J., Davies P., Crystal H., Field P., Yen S. H. Alzheimer's disease: a double-labeling immunohistochemical study of senile plaques. Am. J. Pathol. 132:1988;86-101.
    • (1988) Am. J. Pathol. , vol.132 , pp. 86-101
    • Dickson, D.W.1    Farlo, J.2    Davies, P.3    Crystal, H.4    Field, P.5    Yen, S.H.6
  • 100
    • 0028658439 scopus 로고
    • Induction of superoxide anion and nitric oxide production in cultural microglia
    • Colton C. A., Snell J., Chernyshev O., Gilbert D. L. Induction of superoxide anion and nitric oxide production in cultural microglia. Ann. NY Acad. Sci. 78:1994;54-63.
    • (1994) Ann. NY Acad. Sci. , vol.78 , pp. 54-63
    • Colton, C.A.1    Snell, J.2    Chernyshev, O.3    Gilbert, D.L.4
  • 101
    • 0029087650 scopus 로고
    • Microglia release of nitric oxide by the synergistic action of β -amyloid and IFN-g
    • Goodwin J. L., Uemura E., Cunnick J. E. Microglia release of nitric oxide by the synergistic action of β -amyloid and IFN-g. Brain Res. 692:1995;207-214.
    • (1995) Brain Res. , vol.692 , pp. 207-214
    • Goodwin, J.L.1    Uemura, E.2    Cunnick, J.E.3
  • 102
    • 0029902166 scopus 로고    scopus 로고
    • Evidence for neuronal oxidative damage in Alzheimer's disease
    • Good P. F., Werner P., Hsu A., Olanow C. W., Perl D. P. Evidence for neuronal oxidative damage in Alzheimer's disease. Am. J. Pathol. 149:1996;21-28.
    • (1996) Am. J. Pathol. , vol.149 , pp. 21-28
    • Good, P.F.1    Werner, P.2    Hsu, A.3    Olanow, C.W.4    Perl, D.P.5
  • 103
    • 0026823074 scopus 로고
    • Immunohistochemical evidence of antioxidant stress in Alzheimer's disease
    • Pappolla M. A., Omar R. A., Kim K. S., Robakis N. K. Immunohistochemical evidence of antioxidant stress in Alzheimer's disease. Am. J. Pathol. 140:1992;621-628.
    • (1992) Am. J. Pathol. , vol.140 , pp. 621-628
    • Pappolla, M.A.1    Omar, R.A.2    Kim, K.S.3    Robakis, N.K.4
  • 105
    • 0029032632 scopus 로고
    • Expression of heme oxygenase-1 in the senescent and Alzheimer-disease brain
    • Schipper H. M., Cissé S., Stopa E. G. Expression of heme oxygenase-1 in the senescent and Alzheimer-disease brain. Ann. Neurol. 37:1995;758-768.
    • (1995) Ann. Neurol. , vol.37 , pp. 758-768
    • Schipper, H.M.1    Cissé, S.2    Stopa, E.G.3
  • 107
    • 0029150526 scopus 로고
    • 2+ concentration, and neurotoxicity and increase antioxidant enzyme activities in hippocampal neurons
    • 2+ concentration, and neurotoxicity and increase antioxidant enzyme activities in hippocampal neurons. J. Neurochem. 65:1995;1740-1751.
    • (1995) J. Neurochem. , vol.65 , pp. 1740-1751
    • Mattson, M.P.1    Lovell, M.A.2    Furukawa, K.3    Markesbery, W.R.4
  • 108
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl C., Davis J. B., Lesley R., Schubert D. Hydrogen peroxide mediates amyloid β protein toxicity. Cell. 77:1994;817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 109
    • 0028178837 scopus 로고
    • β -amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: Implications to Alzheimer's disease
    • Butterfield D. A., Hensley K., Harris M., Mattson M. P., Carney J. β -amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: implications to Alzheimer's disease. Biochem. Biophys. Res. Commun. 200:1994;710-715.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 710-715
    • Butterfield, D.A.1    Hensley, K.2    Harris, M.3    Mattson, M.P.4    Carney, J.5
  • 110
    • 0026730350 scopus 로고
    • Amyloidogenicity of βA4 and βA4 -bearing amyloid protein precursor fragments by metal-catalyzed oxidation
    • Dyrks T., Dyrks E., Hartmann R., Masters C., Beyreuther K. Amyloidogenicity of βA4 and βA4 -bearing amyloid protein precursor fragments by metal-catalyzed oxidation. J. Biol. Chem. 267:1992;18210-18217.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18210-18217
    • Dyrks, T.1    Dyrks, E.2    Hartmann, R.3    Masters, C.4    Beyreuther, K.5
  • 111
  • 112
    • 0028908516 scopus 로고
    • Direct evidence of oxidative injury produced by the Alzheimer's β -amyloid peptide (1-40) in cultured hippocampal neurons
    • Harris M. E., Hensley K., Butterfield D. A., Leedle R. A., Carney J. M. Direct evidence of oxidative injury produced by the Alzheimer's β -amyloid peptide (1-40) in cultured hippocampal neurons. Exp. Neurol. 131:1995;193-202.
    • (1995) Exp. Neurol. , vol.131 , pp. 193-202
    • Harris, M.E.1    Hensley, K.2    Butterfield, D.A.3    Leedle, R.A.4    Carney, J.M.5
  • 113
    • 0028169905 scopus 로고
    • Secreted forms of β -amyloid precursor protein protect hippocampal neurons against amyloid β -peptide-induced oxidative injury
    • Goodman Y., Mattson M. P. Secreted forms of β -amyloid precursor protein protect hippocampal neurons against amyloid β -peptide-induced oxidative injury. Exp. Neurol. 128:1994;1-12.
    • (1994) Exp. Neurol. , vol.128 , pp. 1-12
    • Goodman, Y.1    Mattson, M.P.2
  • 114
    • 0029670094 scopus 로고    scopus 로고
    • β -amyloid-mediated vasoactivity and vascular endothelial damage
    • Thomas T., Thomas G., McLendon C., Sutton T., Mullan M. β -amyloid-mediated vasoactivity and vascular endothelial damage. Nature. 380:1996;168-171.
    • (1996) Nature , vol.380 , pp. 168-171
    • Thomas, T.1    Thomas, G.2    McLendon, C.3    Sutton, T.4    Mullan, M.5
  • 115
    • 0029125857 scopus 로고
    • Aging, energy, and oxidative stress in neurodegenerative diseases
    • Beal M. F. Aging, energy, and oxidative stress in neurodegenerative diseases. Ann. Neurol. 38:1995;357-366.
    • (1995) Ann. Neurol. , vol.38 , pp. 357-366
    • Beal, M.F.1
  • 116
    • 0027413399 scopus 로고
    • Brain oxidative energy and related metabolism, neuronal stress and Alzheimer's disease: A speculative synthesis
    • Hoyer S. Brain oxidative energy and related metabolism, neuronal stress and Alzheimer's disease: A speculative synthesis. J. Geriatr. Psychiatry Neurol. 6:1993;3-13.
    • (1993) J. Geriatr. Psychiatry Neurol. , vol.6 , pp. 3-13
    • Hoyer, S.1
  • 117
    • 0026584524 scopus 로고
    • Does impairment of energy metabolism result in excitotoxic neuronal death in neurodegenerative illnesses?
    • Beal M. F. Does impairment of energy metabolism result in excitotoxic neuronal death in neurodegenerative illnesses? Ann. Neurol. 31:1992;119-130.
    • (1992) Ann. Neurol. , vol.31 , pp. 119-130
    • Beal, M.F.1
  • 118
    • 0026624980 scopus 로고
    • Diseases of the mitochondrial DNA
    • Wallace D. C. Diseases of the mitochondrial DNA. Ann. Rev. Biochem. 61:1992;1175-1212.
    • (1992) Ann. Rev. Biochem. , vol.61 , pp. 1175-1212
    • Wallace, D.C.1
  • 120
    • 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., Curti D. The mitochondrial electron transfer alteration as a factor involved in the brain aging. Neurobiol. Aging. 13:1992;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
  • 121
    • 0025006293 scopus 로고
    • Age-related modifications of cytochrome c oxidase activity in discrete brain regions
    • Curti D., Giangaré M. C., Redolfi M. E., Fugaccia I., Benzi G. Age-related modifications of cytochrome c oxidase activity in discrete brain regions. Mech. Ageing Dev. 55:1990;171-180.
    • (1990) Mech. Ageing Dev. , vol.55 , pp. 171-180
    • Curti, D.1    Giangaré, M.C.2    Redolfi, M.E.3    Fugaccia, I.4    Benzi, G.5
  • 124
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • Mutisya E. M., Bowling A. C., Beal M. F. Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J. Neurochem. 63:1994;2179-2184.
    • (1994) J. Neurochem. , vol.63 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 125
    • 0028948660 scopus 로고
    • Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases
    • Chagnon P., Bétard C., Robitaille Y., Cholette A., Gauvreau D. Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases. NeuroReport. 6:1995;711-715.
    • (1995) NeuroReport , vol.6 , pp. 711-715
    • Chagnon, P.1    Bétard, C.2    Robitaille, Y.3    Cholette, A.4    Gauvreau, D.5
  • 126
    • 0027420891 scopus 로고
    • Functional alterations in Alzheimer's disease: Diminution of cytochrome oxidase in the hippocampal formation
    • Simonian N. A., Hyman B. T. Functional alterations in Alzheimer's disease: diminution of cytochrome oxidase in the hippocampal formation. J. Neuropathol. Exp. Neurol. 52:1993;580-585.
    • (1993) J. Neuropathol. Exp. Neurol. , vol.52 , pp. 580-585
    • Simonian, N.A.1    Hyman, B.T.2
  • 127
    • 0028023533 scopus 로고
    • Functional alterations in Alzheimer's disease: Selective loss of mitochondrial-encoded cytochrome oxidase mRNA in the hippocampal formation
    • Simonian N. A., Hyman B. T. Functional alterations in Alzheimer's disease: selective loss of mitochondrial-encoded cytochrome oxidase mRNA in the hippocampal formation. J. Neuropathol. Exp. Neurol. 53:1994;508-512.
    • (1994) J. Neuropathol. Exp. Neurol. , vol.53 , pp. 508-512
    • Simonian, N.A.1    Hyman, B.T.2
  • 129
    • 0029055772 scopus 로고
    • Cytochrome c oxidase in Alzheimer's disease brain: Purification and characterization
    • Parker W. D., Parks J. K. Cytochrome c oxidase in Alzheimer's disease brain: purification and characterization. Neurology. 45:1995;482-486.
    • (1995) Neurology , vol.45 , pp. 482-486
    • Parker, W.D.1    Parks, J.K.2
  • 131
    • 0028762647 scopus 로고
    • Excitatory amino acids as a final common pathway for neurologic disorders
    • Lipton S. A., Rosenberg P. A. Excitatory amino acids as a final common pathway for neurologic disorders. N. Engl. J. Med. 330:1994;613-622.
    • (1994) N. Engl. J. Med. , vol.330 , pp. 613-622
    • Lipton, S.A.1    Rosenberg, P.A.2
  • 133
    • 0023895734 scopus 로고
    • Glutamate become neurotoxic via the N-methyl-D-aspartate receptor when intracellular energy levels are reduced
    • Novelli A., Reilly J. A., Lysko P. G., Henneberry R. C. Glutamate become neurotoxic via the N-methyl-D-aspartate receptor when intracellular energy levels are reduced. Brain Res. 451:1988;205-212.
    • (1988) Brain Res. , vol.451 , pp. 205-212
    • Novelli, A.1    Reilly, J.A.2    Lysko, P.G.3    Henneberry, R.C.4
  • 134
    • 0027162954 scopus 로고
    • Mechanisms of phospholipase A2 activation and neuronal injury
    • Verity M. A. Mechanisms of phospholipase A2 activation and neuronal injury. Ann. NY Acad. Sci. 679:1993;110-120.
    • (1993) Ann. NY Acad. Sci. , vol.679 , pp. 110-120
    • Verity, M.A.1
  • 135
    • 0021984681 scopus 로고
    • Oxygen-derived free radicals in postischemic tissue injury
    • McCord J. Oxygen-derived free radicals in postischemic tissue injury. N. Engl. J. Med. 312:1985;159-163.
    • (1985) N. Engl. J. Med. , vol.312 , pp. 159-163
    • McCord, J.1
  • 136
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer's disease: A potential molecular basis for neuronal degeneration
    • Saito K.-I., Elce J. S., Hamos J. E., Nixon R. A. Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer's disease: a potential molecular basis for neuronal degeneration. Proc. Natl. Acad. Sci. USA. 90:1993;2628-2632.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2628-2632
    • Saito, K.-I.1    Elce, J.S.2    Hamos, J.E.3    Nixon, R.A.4
  • 137
    • 0027194540 scopus 로고
    • A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds
    • Lipton S. A., Choi Y. B., Pan Z.-H., Lei S. Z., Chen H.-S. U., Sucher N. J., Loscalzo J., Singel D. J., Stamler J. S. A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds. Nature. 364:1993;626-632.
    • (1993) Nature , vol.364 , pp. 626-632
    • Lipton, S.A.1    Choi, Y.B.2    Pan, Z.-H.3    Lei, S.Z.4    Chen H.-S., U.5    Sucher, N.J.6    Loscalzo, J.7    Singel, D.J.8    Stamler, J.S.9
  • 138
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yanker B. A., Duffy L. K., Kirschner D. A. Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides. Science. 250:1990;279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yanker, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 139
    • 0025110182 scopus 로고
    • β -amyloid protein increases the vulnerability of cultured cortical neurons to excitotoxic damage
    • Koh J.-Y., Yang L. L., Cotman C. W. β -amyloid protein increases the vulnerability of cultured cortical neurons to excitotoxic damage. Brain Res. 533:1990;315-320.
    • (1990) Brain Res. , vol.533 , pp. 315-320
    • Koh, J.-Y.1    Yang, L.L.2    Cotman, C.W.3
  • 140
    • 0026570528 scopus 로고
    • β -amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M. P., Cheng B., Davis D., Bryant K., Lieberburg I., Rydel R. E. β -amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12:1992;376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 141
    • 0026333250 scopus 로고
    • β -amyloid increases neuronal susceptibility to injury by glucose deprivation
    • Copani A., Koh J.-Y., Cotman C. W. β -amyloid increases neuronal susceptibility to injury by glucose deprivation. NeuroReport. 2:1991;763-765.
    • (1991) NeuroReport , vol.2 , pp. 763-765
    • Copani, A.1    Koh, J.-Y.2    Cotman, C.W.3
  • 142
    • 0027959041 scopus 로고
    • Nordihydroguaiaretic acid protects hippocampal neurons against amyloid β -peptide toxicity, and attenuates free radical and calcium accumulation
    • Goodman Y., Steiner M. R., Steiner S. M., Mattson M. P. Nordihydroguaiaretic acid protects hippocampal neurons against amyloid β -peptide toxicity, and attenuates free radical and calcium accumulation. Brain Res. 654:1994;171-176.
    • (1994) Brain Res. , vol.654 , pp. 171-176
    • Goodman, Y.1    Steiner, M.R.2    Steiner, S.M.3    Mattson, M.P.4
  • 143
    • 0023197336 scopus 로고
    • Mechanism of kainate toxicity to cerebellar neurons in vitro is analogous to reperfusion tissue injury
    • Dykens J. A., Stern A., Trenkner E. Mechanism of kainate toxicity to cerebellar neurons in vitro is analogous to reperfusion tissue injury. J. Neurochem. 49:1987;1222-1228.
    • (1987) J. Neurochem. , vol.49 , pp. 1222-1228
    • Dykens, J.A.1    Stern, A.2    Trenkner, E.3
  • 145
    • 0030155860 scopus 로고    scopus 로고
    • Amyloid β -peptide and oxidative cellular injury in Alzheimer's disease
    • Mark R. J., Blanc E. M., Mattson M. P. Amyloid β -peptide and oxidative cellular injury in Alzheimer's disease. Mol. Neurobiol. 12:1996;211-224.
    • (1996) Mol. Neurobiol. , vol.12 , pp. 211-224
    • Mark, R.J.1    Blanc, E.M.2    Mattson, M.P.3
  • 146
    • 0029682544 scopus 로고    scopus 로고
    • Calcium and free radicals: Mediators of neurotrophic factor and excitatory transmitter-regulated developmental plasticity and cell death
    • Mattson M. P. Calcium and free radicals: Mediators of neurotrophic factor and excitatory transmitter-regulated developmental plasticity and cell death. Pers. Dev. Neurobiol. 3:1996;79-91.
    • (1996) Pers. Dev. Neurobiol. , vol.3 , pp. 79-91
    • Mattson, M.P.1
  • 147
    • 0027268505 scopus 로고
    • Growth factor-mediated protection from excitotoxicity and disturbances in calcium and free radical metabolism
    • Mattson M. P., Cheng B., Smith-Swintosky V. L. Growth factor-mediated protection from excitotoxicity and disturbances in calcium and free radical metabolism. Semin. Neurosci. 5:1993;295-307.
    • (1993) Semin. Neurosci. , vol.5 , pp. 295-307
    • Mattson, M.P.1    Cheng, B.2    Smith-Swintosky, V.L.3
  • 148
    • 0025240761 scopus 로고
    • Role of nerve growth factor in oxidant-antioxidant balance and neuronal injury stimulation of hydrogen peroxide resistance
    • Jackson G. R., Apffel L., Werrback-Perez K., Perez-Polo J. R. Role of nerve growth factor in oxidant-antioxidant balance and neuronal injury stimulation of hydrogen peroxide resistance. J. Neurosci. Res. 25:1990;360-368.
    • (1990) J. Neurosci. Res. , vol.25 , pp. 360-368
    • Jackson, G.R.1    Apffel, L.2    Werrback-Perez, K.3    Perez-Polo, J.R.4
  • 149
    • 0027424797 scopus 로고
    • Role of nerve growth factor in oxidant homeostasis: Glutathione metabolism
    • Pan Z., Perez-Polo R. Role of nerve growth factor in oxidant homeostasis: glutathione metabolism. J. Neurochem. 61:1993;1713-1721.
    • (1993) J. Neurochem. , vol.61 , pp. 1713-1721
    • Pan, Z.1    Perez-Polo, R.2
  • 150
    • 0028862867 scopus 로고
    • PDGFs protect hippocampal neurons against energy deprevation and oxidative injury: Evidence for induction of antioxidant pathways
    • Cheng B., Mattson M. P. PDGFs protect hippocampal neurons against energy deprevation and oxidative injury: evidence for induction of antioxidant pathways. J. Neurosci. 15:1995;7095-7104.
    • (1995) J. Neurosci. , vol.15 , pp. 7095-7104
    • Cheng, B.1    Mattson, M.P.2
  • 151
    • 0028221169 scopus 로고
    • Down-regulation of copper/zinc superoxide dismutase (SOD1) causes apoptotic death in PC12 neuronal cells
    • Troy C. M., Shelanski M. L. Down-regulation of copper/zinc superoxide dismutase (SOD1) causes apoptotic death in PC12 neuronal cells. Proc. Natl. Acad. Sci. USA. 91:1994;6384-6387.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6384-6387
    • Troy, C.M.1    Shelanski, M.L.2
  • 152
    • 0030071721 scopus 로고    scopus 로고
    • Down-regulation of Cu/Zn superoxide dismutase leads to cell death via the nitric oxide-peroxynitrite pathway
    • Troy C. M., Derossi D., Prochiantz A., Greene L. A., Shelanski M. L. Down-regulation of Cu/Zn superoxide dismutase leads to cell death via the nitric oxide-peroxynitrite pathway. J. Neurosci. 16:1996;253-261.
    • (1996) J. Neurosci. , vol.16 , pp. 253-261
    • Troy, C.M.1    Derossi, D.2    Prochiantz, A.3    Greene, L.A.4    Shelanski, M.L.5


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