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Volumn 5, Issue 6, 1998, Pages 401-414

Oxidative stress and neurodegenerative disorders

Author keywords

Antioxidants; Apoptosis; Excitotoxicity; Hydroxyl radical; Neurodegenerative disorders; Oxidative stress; Peroxynitrite; Polyphenols; Reactive oxygen species

Indexed keywords

ACETYLCYSTEINE; ALPHA TOCOPHEROL; AMYLOID PROTEIN; ANTIOXIDANT; APOLIPOPROTEIN E; ASCORBIC ACID; CATALASE; CATECHIN; FREE RADICAL; GLUTATHIONE; GLUTATHIONE PEROXIDASE; IRON CHELATING AGENT; POLYPHENOL; PROBUCOL; QUERCETIN; REACTIVE OXYGEN METABOLITE; RESVERATROL; SELEGILINE; SUPEROXIDE DISMUTASE;

EID: 0031773098     PISSN: 10217770     EISSN: 14230127     Source Type: Journal    
DOI: 10.1007/BF02255928     Document Type: Review
Times cited : (182)

References (196)
  • 1
    • 0027243086 scopus 로고
    • The proiooncogene Bcl 2 can selectively rescue neurotrophic factor-dependent neurons from apoptosis
    • Allsopp TE, Wyatt S, Peterson HF, Davies AM. The proiooncogene Bcl 2 can selectively rescue neurotrophic factor-dependent neurons from apoptosis Cell 73:295-307;1993.
    • (1993) Cell , vol.73 , pp. 295-307
    • Allsopp, T.E.1    Wyatt, S.2    Peterson, H.F.3    Davies, A.M.4
  • 2
    • 0000293742 scopus 로고
    • Über eine eigenartige Erkrankung der Himrinde
    • Alzheimer A. Über eine eigenartige Erkrankung der Himrinde. All Z Psychiatr 64:146-148;1907.
    • (1907) All Z Psychiatr , vol.64 , pp. 146-148
    • Alzheimer, A.1
  • 3
    • 0027171266 scopus 로고
    • Oxidants. antioxidants, and the degenerative diseases of aging
    • Ames BN, Shigenaga MK, Hagen TM. Oxidants. antioxidants, and the degenerative diseases of aging. Proc Natl Acad Sci USA 90: 7915-7922;1993.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7915-7922
    • Ames, B.N.1    Shigenaga, M.K.2    Hagen, T.M.3
  • 4
    • 0030989926 scopus 로고    scopus 로고
    • ApoE genotyping and cerebrospinal fluid tau protein: Implication for the clinical diagnosis of Alzheimer's disease
    • Arai H, Higuchi S, Sasaki H. ApoE genotyping and cerebrospinal fluid tau protein: Implication for the clinical diagnosis of Alzheimer's disease. Gerontology-13 (suppl 1):2-10;1997.
    • (1997) Gerontology , vol.13 , Issue.1 SUPPL. , pp. 2-10
    • Arai, H.1    Higuchi, S.2    Sasaki, H.3
  • 6
    • 0029125857 scopus 로고
    • Aging, energy and oxidative stress in neurodegeneratue diseases
    • Beal MF. Aging, energy and oxidative stress in neurodegeneratue diseases. Neural 38:357-366;1995
    • (1995) Neural , vol.38 , pp. 357-366
    • Beal, M.F.1
  • 7
    • 0028641246 scopus 로고
    • Peroxynitrite versus hydroxyl radical: The role of nitric oxide in superoxidedependent cerebral injury
    • Beckman JS. Peroxynitrite versus hydroxyl radical: The role of nitric oxide in superoxidedependent cerebral injury. Ann NY Acad Sci 738:69-75;1994.
    • (1994) Ann NY Acad Sci , vol.738 , pp. 69-75
    • Beckman, J.S.1
  • 8
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite. Implication for endothelial injury from nitric oxide and Superoxide
    • Beckman TW, Chen J, Marshall PA, Freeman BA. Apparent hydroxyl radical production by peroxynitrite. Implication for endothelial injury from nitric oxide and Superoxide. Proc Natl Acad Sci USA 87:1620-1624;1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1620-1624
    • Beckman, T.W.1    Chen, J.2    Marshall, P.A.3    Freeman, B.A.4
  • 9
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C, Davis JB, Lesley R, Schubert D. Hydrogen peroxide mediates amyloid beta protein toxicity Cell 77:817-827;1994.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 10
    • 0030612205 scopus 로고    scopus 로고
    • Mechanism of amyloid beta protein-induced neuronal cell death: Current concepts and future perspectives
    • Behl C, Sagara Y. Mechanism of amyloid beta protein-induced neuronal cell death: Current concepts and future perspectives. J Neural Transm 49 (suppl):125-134;1997.
    • (1997) J Neural Transm , vol.49 , Issue.SUPPL. , pp. 125-134
    • Behl, C.1    Sagara, Y.2
  • 11
    • 0020404759 scopus 로고
    • An EPR study of the production of Superoxide radicals by neutrophil NADPH oxidase
    • Bennister JV, Ballanate P, Sema MC, Thomalley PJ, Rossi F. An EPR study of the production of Superoxide radicals by neutrophil NADPH oxidase. FEBS Lett 145:323-326; 1982.
    • (1982) FEBS Lett , vol.145 , pp. 323-326
    • Bennister, J.V.1    Ballanate, P.2    Sema, M.C.3    Thomalley, P.J.4    Rossi, F.5
  • 12
    • 0029620665 scopus 로고
    • Posttraumatic differences in the titer of autoantibodies against oxidized low density lipoproteins (OLDL) in the sera of patients with bone fracture and traumatic brain injury
    • Borovic S, Zarkovic N, Wildburger R, Tatzber F, Jurin M. Posttraumatic differences in the titer of autoantibodies against oxidized low density lipoproteins (OLDL) in the sera of patients with bone fracture and traumatic brain injury. Periodicum Biol 97:209-293;1995.
    • (1995) Periodicum Biol , vol.97 , pp. 209-293
    • Borovic, S.1    Zarkovic, N.2    Wildburger, R.3    Tatzber, F.4    Jurin, M.5
  • 13
    • 0030043994 scopus 로고    scopus 로고
    • 1 Gamma radiation-induced cell death in the fetal rat brain possesses molecular characteristics of apoptosis and is associated with specific messenger RNA elevation
    • Borovitskaya AE, Evtushenko VI, Sabol SL. 1 Gamma radiation-induced cell death in the fetal rat brain possesses molecular characteristics of apoptosis and is associated with specific messenger RNA elevation. Mol Brain Res 35: 19-30;1996.
    • (1996) Mol Brain Res , vol.35 , pp. 19-30
    • Borovitskaya, A.E.1    Evtushenko, V.I.2    Sabol, S.L.3
  • 14
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbasic oxygen
    • Boveries A, Chance B. The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbasic oxygen. Biochem J 134:707-716;1973.
    • (1973) Biochem J , vol.134 , pp. 707-716
    • Boveries, A.1    Chance, B.2
  • 15
    • 0019532613 scopus 로고
    • DNA strand scission by enzymicaily generated oxygen radicals
    • Brawn K, Fridovich I. DNA strand scission by enzymicaily generated oxygen radicals. Arch Biochem Biophys 206:414-419;1981.
    • (1981) Arch Biochem Biophys , vol.206 , pp. 414-419
    • Brawn, K.1    Fridovich, I.2
  • 17
    • 0029161636 scopus 로고
    • Nitric oxide regulates mitochondrial respiration and cell function by inhibitory cytochrome oxidase
    • Brown GC, Nitric oxide regulates mitochondrial respiration and cell function by inhibitory cytochrome oxidase. FEBS Lett 369:136-139; 1995.
    • (1995) FEBS Lett , vol.369 , pp. 136-139
    • Brown, G.C.1
  • 18
    • 0028176651 scopus 로고
    • Oxidative stress as a mediator of apoptosis
    • Buttke TM, Sandstrom PA. Oxidative stress as a mediator of apoptosis. Immunol Today 15: 7-10;1994.
    • (1994) Immunol Today , vol.15 , pp. 7-10
    • Buttke, T.M.1    Sandstrom, P.A.2
  • 19
    • 0030917448 scopus 로고    scopus 로고
    • Amelioration of oxidative stress by antioxidants and resveratrol in PC12 cells
    • Chanvitayapongs S, Draczynska-Lusiak B, Sun AY. Amelioration of oxidative stress by antioxidants and resveratrol in PC12 cells. Neuroreport 8:1499-1502;1997.
    • (1997) Neuroreport , vol.8 , pp. 1499-1502
    • Chanvitayapongs, S.1    Draczynska-Lusiak, B.2    Sun, A.Y.3
  • 21
    • 0031979220 scopus 로고    scopus 로고
    • Activation of transcription factor AP-1 by extracellular ATP in PC12 cells
    • Chen YM, Sun AY. Activation of transcription factor AP-1 by extracellular ATP in PC12 cells. Neurochem Res 23:543-550;1998.
    • (1998) Neurochem Res , vol.23 , pp. 543-550
    • Chen, Y.M.1    Sun, A.Y.2
  • 23
    • 0028639260 scopus 로고
    • Extra-cellular ATP may induce neuronal degeneration by a free-radical mechanism
    • Cheng Y, Chen M, Wixom P. Sun AY. Extra-cellular ATP may induce neuronal degeneration by a free-radical mechanism. Ann NY Acad Sci 738:431-435;1994.
    • (1994) Ann NY Acad Sci , vol.738 , pp. 431-435
    • Cheng, Y.1    Chen, M.2    Wixom, P.3    Sun, A.Y.4
  • 26
    • 0026497926 scopus 로고
    • Excitotoxic cell death
    • Choi DW. Excitotoxic cell death. J Neurobiol 23:1261-1276;1992.
    • (1992) J Neurobiol , vol.23 , pp. 1261-1276
    • Choi, D.W.1
  • 27
    • 0028799654 scopus 로고
    • Calcium: Still center-stage in hypoxic-ischemic neuronal death
    • Choi DW. Calcium: Still center-stage in hypoxic-ischemic neuronal death. Trends Neurosci 18:58-60;1995.
    • (1995) Trends Neurosci , vol.18 , pp. 58-60
    • Choi, D.W.1
  • 29
    • 0031010596 scopus 로고    scopus 로고
    • Parkinson's disease: A new link between monoamine oxidase and mitochondrial electron flow
    • Cohen G, Farooqui R. Kesler N. Parkinson's disease: A new link between monoamine oxidase and mitochondrial electron flow. Proc Natl Acad Sci USA 94:4890-4894;1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4890-4894
    • Cohen, G.1    Farooqui, R.2    Kesler, N.3
  • 31
    • 0026513756 scopus 로고
    • A histochemical study of iron, transferrin and ferrtin in Alzheimer's disease brain
    • Connor JR, Menzies SL, St Mann SM, Murison EJ. A histochemical study of iron, transferrin and ferrtin in Alzheimer's disease brain. J Neurosci Res 31:75-83;1992.
    • (1992) J Neurosci Res , vol.31 , pp. 75-83
    • Connor, J.R.1    Menzies, S.L.2    St Mann, S.M.3    Murison, E.J.4
  • 32
    • 0027194791 scopus 로고
    • Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families
    • Corder EH, Soundes AM, Strittmatter WJ, et al. Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families. Science 261:921-923;1993.
    • (1993) Science , vol.261 , pp. 921-923
    • Corder, E.H.1    Soundes, A.M.2    Strittmatter, W.J.3
  • 33
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate, and neurodegenerative disorders
    • Coyle JT, Puttfarcken P. Oxidative stress, glutamate, and neurodegenerative disorders. Science 262:689-695;1993.
    • (1993) Science , vol.262 , pp. 689-695
    • Coyle, J.T.1    Puttfarcken, P.2
  • 34
    • 0027985453 scopus 로고
    • Attenuation of p53 expression protects against focal ischemic damage in transgenic mice
    • Crumrine RC, Thomas AL, Morgan PF. Attenuation of p53 expression protects against focal ischemic damage in transgenic mice. J Cereb Blood Flow Metab 14:887-891;1994.
    • (1994) J Cereb Blood Flow Metab , vol.14 , pp. 887-891
    • Crumrine, R.C.1    Thomas, A.L.2    Morgan, P.F.3
  • 35
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals. I. general aspects
    • Davies KJ. Protein damage and degradation by oxygen radicals. I. general aspects. J Biol Chem 262:9895-9901;1987.
    • (1987) J Biol Chem , vol.262 , pp. 9895-9901
    • Davies, K.J.1
  • 37
    • 0027485950 scopus 로고
    • Temporal analysis of events associated with programmed cell death (apoptosis) of sympathetic neurons deprived of nerve growth factor
    • Deckwerth TL, Johnson EM, Jr. Temporal analysis of events associated with programmed cell death (apoptosis) of sympathetic neurons deprived of nerve growth factor. J Cell Biol 123:1207-1222;1993.
    • (1993) J Cell Biol , vol.123 , pp. 1207-1222
    • Deckwerth, T.L.1    Johnson Jr., E.M.2
  • 38
    • 0030610502 scopus 로고    scopus 로고
    • Role of oxidative stress in the manganese and l-methyl-4-(2′-ethylphenyl)-1,2,3,6-tetrahydropyridine-induced apoptosis in PC 12 cells
    • Desole MS, Sciola L, Delogue MR, Siacana S, Migheli R, Miele E. Role of oxidative stress in the manganese and l-methyl-4-(2′-ethylphenyl)-1,2,3,6-tetrahydropyridine-induced apoptosis in PC 12 cells. Neurochem Int 31:169-176;1997.
    • (1997) Neurochem int , vol.31 , pp. 169-176
    • Desole, M.S.1    Sciola, L.2    Delogue, M.R.3    Siacana, S.4    Migheli, R.5    Miele, E.6
  • 39
    • 0024585155 scopus 로고
    • Basal lipid peroxidation in substantia nigra is increased in Parkinson's disease
    • Dexter DT, Carter CJ, Wekks FR. Basal lipid peroxidation in substantia nigra is increased in Parkinson's disease. J Neurochem 52:381-389; 1989.
    • (1989) J Neurochem , vol.52 , pp. 381-389
    • Dexter, D.T.1    Carter, C.J.2    Wekks, F.R.3
  • 40
    • 0026704075 scopus 로고
    • Alterations m level of iron, femtin, and other trace metals m neuronal degenerative diseases affecting the basal ganglia
    • The Royal Kings and Queens Parkinson's Disease Research Group
    • Dexter DT, Jenner P, Schapira AH, Marsden CD. Alterations m level of iron, femtin, and other trace metals m neuronal degenerative diseases affecting the basal ganglia. The Royal Kings and Queens Parkinson's Disease Research Group. Ann Neurol 32 (suppl S9):4-100;1992.
    • (1992) Ann Neurol , vol.32 , Issue.SUPPL. S9 , pp. 4-100
    • Dexter, D.T.1    Jenner, P.2    Schapira, A.H.3    Marsden, C.D.4
  • 41
    • 0028091176 scopus 로고
    • Indices of oxidative stress and mitochondrial function in individuals with incidental Lewy body disease
    • Dexter DT, Sian J, Rose S, et al. indices of oxidative stress and mitochondrial function in individuals with incidental Lewy body disease. Ann Neurol 35:38-44;1994.
    • (1994) Ann Neurol , vol.35 , pp. 38-44
    • Dexter, D.T.1    Sian, J.2    Rose, S.3
  • 42
    • 0027354484 scopus 로고
    • Microglia and cytokines in neurological disease with special reference to AIDS and Alzheimer's disease
    • Dickson DW, Lee SC, Mattiace L, Yen SHC, Brosnan C. Microglia and cytokines in neurological disease with special reference to AIDS and Alzheimer's disease. Glia 7:75-83;1993.
    • (1993) Glia , vol.7 , pp. 75-83
    • Dickson, D.W.1    Lee, S.C.2    Mattiace, L.3    Yen, S.H.C.4    Brosnan, C.5
  • 43
    • 0031947574 scopus 로고    scopus 로고
    • Oxidized lipoproteins may play a role in neuronal cell death in Alzheimer's disease
    • Draczynska-Lusiak B, Doung A, Sun A. Oxidized lipoproteins may play a role in neuronal cell death in Alzheimer's disease. Mol Chem Neuropathol 33:139-148;1998.
    • (1998) Mol Chem Neuropathol , vol.33 , pp. 139-148
    • Draczynska-Lusiak, B.1    Doung, A.2    Sun, A.3
  • 44
    • 0032536359 scopus 로고    scopus 로고
    • Oxidized lipoproteins activate NT-κB binding activity and apoptosis in PC12 cells
    • Draczynska-Lusiak B, Chen YM, Sun AY. Oxidized lipoproteins activate NT-κB binding activity and apoptosis in PC12 cells. Neuroreport 9:527-532;1998.
    • (1998) Neuroreport , vol.9 , pp. 527-532
    • Draczynska-Lusiak, B.1    Chen, Y.M.2    Sun, A.Y.3
  • 45
    • 0027933701 scopus 로고
    • +: Implications for neurodegeneration
    • +: Implications for neurodegeneration. J Neurochem 63:584-591; 1994.
    • (1994) J Neurochem , vol.63 , pp. 584-591
    • Dykens, J.A.1
  • 47
    • 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 PP, Agid Y, Ruberg M. Mitochondrial free radical signal in ceramide-dependent apoptosis: A putative mechanism for neuronal death in Parkinson's disease. J Neurochem 69:1612-1621;1997.
    • (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
  • 48
    • 0027447124 scopus 로고
    • Inhibition of human low density lipoprotein oxidation by resveratrol
    • Frankel EN, Waterhouse AL, Kinsella JE. Inhibition of human low density lipoprotein oxidation by resveratrol. Lancet 341:1103-1104; 1993.
    • (1993) Lancet , vol.341 , pp. 1103-1104
    • Frankel, E.N.1    Waterhouse, A.L.2    Kinsella, J.E.3
  • 49
    • 0020427486 scopus 로고
    • Free radical and tissue injury
    • Freeman BA, Crapo JD. Free radical and tissue injury. Lab Invest 47:412-426;1982.
    • (1982) Lab Invest , vol.47 , pp. 412-426
    • Freeman, B.A.1    Crapo, J.D.2
  • 50
    • 0016414528 scopus 로고
    • Superoxide dismutase
    • Fridovich I. Superoxide dismutase. Science 44: 147-159;1975.
    • (1975) Science , vol.44 , pp. 147-159
    • Fridovich, I.1
  • 51
    • 0026596478 scopus 로고
    • Molecular neurobiology of glutamate receptors
    • Gasic GP, Hollmann M. Molecular neurobiology of glutamate receptors. Annu Rev Physiol 54:507-536;1992.
    • (1992) Annu Rev Physiol , vol.54 , pp. 507-536
    • Gasic, G.P.1    Hollmann, M.2
  • 53
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization on a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CN. Alzheimer's disease: Initial report of the purification and characterization on a novel cerebrovascular amyloid protein. Biochem Biophys Res Comman 120: 885-890;1984.
    • (1984) Biochem Biophys Res Comman , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.N.2
  • 54
    • 0009627006 scopus 로고
    • Binding site on macrophages that mediates uptake and degradation of acetylated LDL, producing massive cholesterol deposition
    • Goldstein JL, Ho YK, Basu SK, Brown MS. Binding site on macrophages that mediates uptake and degradation of acetylated LDL, producing massive cholesterol deposition. Proc Natl Acad Sci USA 96:333-337;1979.
    • (1979) Proc Natl Acad Sci USA , vol.96 , pp. 333-337
    • Goldstein, J.L.1    Ho, Y.K.2    Basu, S.K.3    Brown, M.S.4
  • 55
    • 0020973547 scopus 로고
    • Receptor mediated endocytosis of low density lipoprotein in cultured cells
    • Goldstein JL, Basu SK, Brown MS. Receptor mediated endocytosis of low density lipoprotein in cultured cells. Methods Enzymol 98: 241-261;1983.
    • (1983) Methods Enzymol , vol.98 , pp. 241-261
    • Goldstein, J.L.1    Basu, S.K.2    Brown, M.S.3
  • 56
    • 0026573467 scopus 로고
    • Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: A laser microprobe study
    • Good PF, Perl D, Bigrer LM, Schmeidler J. Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: A laser microprobe study. Ann Neurol 31:286-292;1992.
    • (1992) Ann Neurol , vol.31 , pp. 286-292
    • Good, P.F.1    Perl, D.2    Bigrer, L.M.3    Schmeidler, J.4
  • 57
    • 0029809731 scopus 로고    scopus 로고
    • Oxidative stress and apoptosis in neurodegeneration
    • Gorman AM, McGowan A, O'Neill C, Cotter T. Oxidative stress and apoptosis in neurodegeneration. J Neurol Sci 139 (suppl):45-52; 1996.
    • (1996) J Neurol Sci , vol.139 , Issue.SUPPL. , pp. 45-52
    • Gorman, A.M.1    McGowan, A.2    O'Neill, C.3    Cotter, T.4
  • 58
    • 0018095085 scopus 로고
    • Oxidative pathway for catecholamines in the genesis of neuromelanin and cytotoxic qumones
    • Graham DG. Oxidative pathway for catecholamines in the genesis of neuromelanin and cytotoxic qumones. Mol Pharmacol 14:633-643;1978.
    • (1978) Mol Pharmacol , vol.14 , pp. 633-643
    • Graham, D.G.1
  • 59
    • 0029996997 scopus 로고    scopus 로고
    • Apolipoprotein E and low-density lipoprotein binding and intemalization in primary culture of rat astrocytes: Isoform specific alterations
    • Guillaume D, Bertrand P, Dea D, Davignon J. Poirier J. Apolipoprotein E and low-density lipoprotein binding and intemalization in primary culture of rat astrocytes: Isoform specific alterations. J Neurochem 66:2410-2418;1997.
    • (1997) J Neurochem , vol.66 , pp. 2410-2418
    • Guillaume, D.1    Bertrand, P.2    Dea, D.3    Davignon, J.4    Poirier, J.5
  • 60
    • 0028095807 scopus 로고
    • Mitochondrial calcium transport: Physiological and pathological relevance
    • Gunter TE, Gunter KK, Shen SS, Gavin CE. Mitochondrial calcium transport: Physiological and pathological relevance. Am J Physiol 267C:313-339;1994.
    • (1994) Am J Physiol , vol.267 C , pp. 313-339
    • Gunter, T.E.1    Gunter, K.K.2    Shen, S.S.3    Gavin, C.E.4
  • 61
    • 0026735070 scopus 로고
    • Targeting of cell surface β-amyloid precursor protein to lysosomes: Altername processing into amyloid bearing fragments
    • Haas C, Koo EH, Mellon A, Selkoe DJ. Targeting of cell surface β-amyloid precursor protein to lysosomes: Altername processing into amyloid bearing fragments. Nature 357:500-503; 1992.
    • (1992) Nature , vol.357 , pp. 500-503
    • Haas, C.1    Koo, E.H.2    Mellon, A.3    Selkoe, D.J.4
  • 63
    • 4244087065 scopus 로고
    • Reactive oxygen species in living systems: Source, biochemistry, and role in human disease
    • Halliwell B. Reactive oxygen species in living systems: Source, biochemistry, and role in human disease. Am J Med 91:14S-22S;1991.
    • (1991) Am J Med , vol.91
    • Halliwell, B.1
  • 64
    • 0027991050 scopus 로고
    • Free radicals and antioxidants: A personal view
    • Halliwell B. Free radicals and antioxidants: A personal view. Nutr Rev 52:253-265;1995.
    • (1995) Nutr Rev , vol.52 , pp. 253-265
    • Halliwell, B.1
  • 66
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell B, Gutteridge JM. Role of free radicals and catalytic metal ions in human disease: An overview. Methods Enzymol 186:1-85; 1990.
    • (1990) Methods Enzymol , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.2
  • 67
    • 0029012476 scopus 로고
    • A c-jun dominant negative mutant protects sympathetic neurons against programmed cell death
    • Ham J, Bahyi C, Whitfield J, Pfarr CM, Lallemand D, Yaniv M, Rubin LL. A c-jun dominant negative mutant protects sympathetic neurons against programmed cell death. Neuron 14:927-939;1995.
    • (1995) Neuron , vol.14 , pp. 927-939
    • Ham, J.1    Bahyi, C.2    Whitfield, J.3    Pfarr, C.M.4    Lallemand, D.5    Yaniv, M.6    Rubin, L.L.7
  • 68
    • 0025274652 scopus 로고
    • Intraceuular iron redistribution. An important determinant of reperfusion damage to rabbit kidneys
    • Healing G, Gower J, Fuller B, Green C. Intraceuular iron redistribution. An important determinant of reperfusion damage to rabbit kidneys. Biochem Pharmacol 39:1239-1245; 1990.
    • (1990) Biochem Pharmacol , vol.39 , pp. 1239-1245
    • Healing, G.1    Gower, J.2    Fuller, B.3    Green, C.4
  • 70
    • 0030794309 scopus 로고    scopus 로고
    • Inibition of the electrostatic interaction between β-amyloid peptide and membranes prevents β-amyloid-induced toxicity
    • Hertel C, Terzi E, Hauser N, Jakob Rome R, Seelig J, Kemp JA. Inibition of the electrostatic interaction between β-amyloid peptide and membranes prevents β-amyloid-induced toxicity. Proc Natl Acad Sci USA 94:9412-9416; 1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9412-9416
    • Hertel, C.1    Terzi, E.2    Hauser, N.3    Jakob Rome, R.4    Seelig, J.5    Kemp, J.A.6
  • 71
    • 0023740954 scopus 로고
    • Melanised dopaminergic neurons are differentially susceptible to degeneration in Parkinson's disease
    • Hirsch EC, Grabiel AM, Agid Y, Melanised dopaminergic neurons are differentially susceptible to degeneration in Parkinson's disease. Nature 334:345-348;1988.
    • (1988) Nature , vol.334 , pp. 345-348
    • Hirsch, E.C.1    Grabiel, A.M.2    Agid, Y.3
  • 73
    • 0028322364 scopus 로고
    • Chronic electroconvulsive seizure (ECS) treatment results in expression of long-lasting AP-1 complex in brain with altered composition and characteristics
    • Hope BT, Kelz MB, Duman RS, Nestler EJ. Chronic electroconvulsive seizure (ECS) treatment results in expression of long-lasting AP-1 complex in brain with altered composition and characteristics. J Neurosci 14:4318-1328: 1994.
    • (1994) J Neurosci , vol.14 , pp. 4318-11328
    • Hope, B.T.1    Kelz, M.B.2    Duman, R.S.3    Nestler, E.J.4
  • 74
    • 0031020172 scopus 로고    scopus 로고
    • Bright and dark sides of nitric oxide in ischemic brain injury
    • Iadecola C. Bright and dark sides of nitric oxide in ischemic brain injury. Trends Neurosci 20:132-139;1997.
    • (1997) Trends Neurosci , vol.20 , pp. 132-139
    • Iadecola, C.1
  • 75
    • 0026447129 scopus 로고
    • Retinoic acids inhibit activation-induced apoptosis in T cell hybridomas and thymocytes
    • Iwata M, Mukai M, Nakai Y, Iseki R. Retinoic acids inhibit activation-induced apoptosis in T cell hybridomas and thymocytes. J Immunol 149:3302-3308;1992.
    • (1992) J Immunol , vol.149 , pp. 3302-3308
    • Iwata, M.1    Mukai, M.2    Nakai, Y.3    Iseki, R.4
  • 76
    • 0028268215 scopus 로고
    • Programmed cell death and Bcl-2 protection in the absence of nucleus
    • Jacobson MG, Burne JF, Raff MC. Programmed cell death and Bcl-2 protection in the absence of nucleus. EMBO J 13:1899-1910; 1994.
    • (1994) EMBO J , vol.13 , pp. 1899-1910
    • Jacobson, M.G.1    Burne, J.F.2    Raff, M.C.3
  • 78
    • 0029751104 scopus 로고    scopus 로고
    • Oxidative stress and the pathogenesis of Parkinson's disease
    • Jenner P, Olanow CW. Oxidative stress and the pathogenesis of Parkinson's disease. Neurology 47 (6 suppl 3):S161-S170;1996.
    • (1996) Neurology , vol.47 , Issue.6 SUPPL. 3
    • Jenner, P.1    Olanow, C.W.2
  • 79
    • 0024447098 scopus 로고
    • Diffuse senile plaques occur commonly in the cerebellum in Alzheimer's disease
    • Joachim CL, Morris JH, Selkoe DJ. Diffuse senile plaques occur commonly in the cerebellum in Alzheimer's disease. Am J Pathol 135: 309-320;1989.
    • (1989) Am J Pathol , vol.135 , pp. 309-320
    • Joachim, C.L.1    Morris, J.H.2    Selkoe, D.J.3
  • 80
    • 0028075436 scopus 로고
    • Dynamic changes in the composition of the AP-1 transcription factor DNA-binding activity in rat brain following kainate-induced seizures and cell death
    • Kaminska B. Filipkowski RK, Zurkoska G, Lason W, Przenlocki R, Kaczmareki L. Dynamic changes in the composition of the AP-1 transcription factor DNA-binding activity in rat brain following kainate-induced seizures and cell death. Eur J Neurosci 6:1558-1566;1994.
    • (1994) Eur J Neurosci , vol.6 , pp. 1558-1566
    • Kaminska, B.1    Filipkowski, R.K.2    Zurkoska, G.3    Lason, W.4    Przenlocki, R.5    Kaczmareki, L.6
  • 81
    • 0031456035 scopus 로고    scopus 로고
    • Genistein, the dietary-derived angiotenesis inhibitor, prevents LDL oxidation and protects endothelial cells from damage by atherogenic LDL
    • Kapiotis S, Hermann M, Held I, Seelos C, Ehringer IT, Gmeiner BMK. Genistein, the dietary-derived angiotenesis inhibitor, prevents LDL oxidation and protects endothelial cells from damage by atherogenic LDL. Arterioscler Thromb Vasc Biol 17:2868-2874;1997
    • (1997) Arterioscler Thromb Vasc Biol , vol.17 , pp. 2868-2874
    • Kapiotis, S.1    Hermann, M.2    Held, I.3    Seelos, C.4    Ehringer, I.T.5    Gmeiner, B.M.K.6
  • 82
    • 0029025008 scopus 로고
    • Kainic acid-induced neuronal death is associated with DNA damage and a unique immediate-early gene response in c-fos-lacZ transgenic rats
    • Kasof GM, Mandelzys A, Maika SD, Hammer RE, Cuirau T, Morgan JC. Kainic acid-induced neuronal death is associated with DNA damage and a unique immediate-early gene response in c-fos-lacZ transgenic rats. J Neurosci 15:4238-4247;1995.
    • (1995) J Neurosci , vol.15 , pp. 4238-4247
    • Kasof, G.M.1    Mandelzys, A.2    Maika, S.D.3    Hammer, R.E.4    Cuirau, T.5    Morgan, J.C.6
  • 83
    • 17344371804 scopus 로고    scopus 로고
    • Mitochondrial manganese Superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: Suppression of peroxynitrite production, lipid peroxidation, and mitochondnal dysfunction
    • Keller N, Kindy MS, Holtsberg FW, St. Clair DK, Yen H-C, Germeyer A, Steiner SM, Bruce-Keller AJ, Hutchins JB, Mattson MP. Mitochondrial manganese Superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: Suppression of peroxynitrite production, lipid peroxidation, and mitochondnal dysfunction. J Neurosci 18:687-697;1998.
    • (1998) J Neurosci , vol.18 , pp. 687-697
    • Keller, N.1    Kindy, M.S.2    Holtsberg, F.W.3    St Clair, D.K.4    Yen, H.-C.5    Germeyer, A.6    Steiner, S.M.7    Bruce-Keller, A.J.8    Hutchins, J.B.9    Mattson, M.P.10
  • 84
    • 0032171625 scopus 로고    scopus 로고
    • Protection of PC 12 cells by glutathione peroxidase in L-DOPA induced cytotoxicity
    • Kim-Han J, Sun AY. Protection of PC 12 cells by glutathione peroxidase in L-DOPA induced cytotoxicity. Free Radic Biol Med 25:512-518; 1998.
    • (1998) Free Radic Biol Med , vol.25 , pp. 512-518
    • Kim-Han, J.1    Sun, A.Y.2
  • 85
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome C from mitochondria: A primary site for the Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR. Newmeyer DD. The release of cytochrome C from mitochondria: A primary site for the Bcl-2 regulation of apoptosis. Science 275:1132-1136; 1997.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 86
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 resembles a cell surface receptor
    • Kong J, Lemaire HG. Unterbeck A et al: The precursor of Alzheimer's disease amyloid A4 resembles a cell surface receptor. Nature 325-733-736;1987.
    • (1987) Nature , vol.325 , pp. 733-736
    • Kong, J.1    Lemaire, H.G.2    Unterbeck, A.3
  • 87
    • 14044251695 scopus 로고    scopus 로고
    • Mitochondrial implication in apoptosis - Towards an endosymbiont hypothesis of apoptosis evolution
    • Kroemer G. Mitochondrial implication in apoptosis - towards an endosymbiont hypothesis of apoptosis evolution. Cell Death Differ 4: 443-456;1997.
    • (1997) Cell Death Differ , vol.4 , pp. 443-456
    • Kroemer, G.1
  • 90
    • 0031020172 scopus 로고    scopus 로고
    • Bright and dark sides of nitric oxide in ischemic brain injury
    • Ladecola C. Bright and dark sides of nitric oxide in ischemic brain injury. Trends Neurosci 20:132-139;1997.
    • (1997) Trends Neurosci , vol.20 , pp. 132-139
    • Ladecola, C.1
  • 92
    • 0030748833 scopus 로고    scopus 로고
    • Association of human, rat and rabbit apolipoprotein E with β-amyloid
    • LaDu MJ, Luken JR, Reardon CA, Getz GS. Association of human, rat and rabbit apolipoprotein E with β-amyloid. J Neurosci Res 49: 9-18;1997.
    • (1997) J Neurosci Res , vol.49 , pp. 9-18
    • Ladu, M.J.1    Luken, J.R.2    Reardon, C.A.3    Getz, G.S.4
  • 93
    • 0027221998 scopus 로고
    • NMDA-dependent Superoxide production and neurotoxicity
    • Lafon-Cazal M, Pietri S, Culcasi M, Bockaert J. NMDA-dependent Superoxide production and neurotoxicity. Nature 364:535-537; 1993.
    • (1993) Nature , vol.364 , pp. 535-537
    • Lafon-Cazal, M.1    Pietri, S.2    Culcasi, M.3    Bockaert, J.4
  • 94
    • 0030614650 scopus 로고    scopus 로고
    • R(-)-deprenyl potentiates dopamine-induced cytotoxicity toward catecholaminergic neuroblastoma SH-SY5Y cells
    • Lai CT, Yu PH. R(-)-deprenyl potentiates dopamine-induced cytotoxicity toward catecholaminergic neuroblastoma SH-SY5Y cells. Toxicol Appl Pharmacol 142:186-191;1997.
    • (1997) Toxicol Appl Pharmacol , vol.142 , pp. 186-191
    • Lai, C.T.1    Yu, P.H.2
  • 95
    • 0031059975 scopus 로고    scopus 로고
    • Glutamate receptors of the kainate type and synaptic transmission
    • Lerma J, Morales M. Vicente MA, Herreras O. Glutamate receptors of the kainate type and synaptic transmission. Trends Neurosci 20:9-12;1997.
    • (1997) Trends Neurosci , vol.20 , pp. 9-12
    • Lerma, J.1    Morales, M.2    Vicente, M.A.3    Herreras, O.4
  • 96
    • 0028762647 scopus 로고
    • Excitatory amino acids as a final common pathway for neurologic disorders
    • Lipton SA, Rosenberg PA. Excitatory amino acids as a final common pathway for neurologic disorders. New Engl J Med 330:613-622;1994.
    • (1994) New Engl J Med , vol.330 , pp. 613-622
    • Lipton, S.A.1    Rosenberg, P.A.2
  • 97
    • 0029795517 scopus 로고    scopus 로고
    • Inflammation, A-beta deposition and neurofibrillary tangle formation as correlates of Alzheimer's disease neurodegeneration
    • Liu LF, Brachova L, Civin WH, Rogers J. Inflammation, A-beta deposition and neurofibrillary tangle formation as correlates of Alzheimer's disease neurodegeneration. J Neuropathol Exp Neurol 55:1083-1088; 1996.
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 1083-1088
    • Liu, L.F.1    Brachova, L.2    Civin, W.H.3    Rogers, J.4
  • 98
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptosis program in cell-free extracts: Requirement for dATP and cytochromeC
    • Liu X, Kim CM, Yang J, Jemmerson R, Wang X. Induction of apoptosis program in cell-free extracts: Requirement for dATP and cytochromeC. Cell 86:147-157;1996.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.M.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 99
    • 0027988579 scopus 로고
    • Inhibitors of free radical formation fail to attenuate direct b-amyloid peptide-mediated neurotoxicity in rat hippocampal cultures
    • Lockhart BP, Bemcourt C, Junien JL, Privat A. Inhibitors of free radical formation fail to attenuate direct b-amyloid peptide-mediated neurotoxicity in rat hippocampal cultures. J Neurosci Res 39:494-505;1994.
    • (1994) J Neurosci Res , vol.39 , pp. 494-505
    • Lockhart, B.P.1    Bemcourt, C.2    Junien, J.L.3    Privat, A.4
  • 100
    • 0026716547 scopus 로고
    • Hippocampal lesions induced by microinjection of the nitric oxide donor nitropmsside
    • Loiacono RE, Bean PM. Hippocampal lesions induced by microinjection of the nitric oxide donor nitropmsside. Eur J Pharmacol 216:331-333;1992.
    • (1992) Eur J Pharmacol , vol.216 , pp. 331-333
    • Loiacono, R.E.1    Bean, P.M.2
  • 101
    • 0029989760 scopus 로고    scopus 로고
    • The intracellular fate of apolipoprotein E is tau dependent and apo allele-specific
    • Lovestone S, Anderton BH, Hartley C, Jensen TG, Horgeusen AL. The intracellular fate of apolipoprotein E is tau dependent and apo allele-specific. Neuroreport 7:1005-1008;1996.
    • (1996) Neuroreport , vol.7 , pp. 1005-1008
    • Lovestone, S.1    Anderton, B.H.2    Hartley, C.3    Jensen, T.G.4    Horgeusen, A.L.5
  • 102
    • 84948011844 scopus 로고    scopus 로고
    • The toxic effect of sodium L-glutamate on the inner layers of the retina
    • Lucas DR, Newhouse JP. The toxic effect of sodium L-glutamate on the inner layers of the retina. Arch Ophthalmol 58:193-201;1997.
    • (1997) Arch Ophthalmol , vol.58 , pp. 193-201
    • Lucas, D.R.1    Newhouse, J.P.2
  • 103
    • 0026498607 scopus 로고
    • Ethanol and excitotoxicity in cultured cortical neurons: Differential sensitivity of N-methyk-D-aspartate and sodium nitroprusside toxicity
    • Lustig HS, von Brauchitsch KL, Chan J, Greenberg DA. Ethanol and excitotoxicity in cultured cortical neurons: Differential sensitivity of N-methyk-D-aspartate and sodium nitroprusside toxicity. J Neurochem 59: 2193-2200;1992.
    • (1992) J Neurochem , vol.59 , pp. 2193-2200
    • Lustig, H.S.1    Von Brauchitsch, K.L.2    Chan, J.3    Greenberg, D.A.4
  • 104
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal. an aldehydic product of Hpid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid β-peptide
    • Mark RJ, Lovell MA, Markesbery WR, Uchida K, Mattson MP. A role for 4-hydroxynonenal. an aldehydic product of Hpid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid β-peptide. J Neurochem 68:255-264;1997.
    • (1997) J Neurochem , vol.68 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesbery, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 105
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesberry WR. Oxidative stress hypothesis in Alzheimer's disease. Free Radie Biol Med 23:134-147;1997.
    • (1997) Free Radie Biol Med , vol.23 , pp. 134-147
    • Markesberry, W.R.1
  • 106
    • 0027297138 scopus 로고
    • Calcium destabilizing and neurodegenerative effects of aggregated β-amyloid peptide are attenuated by basic FGF
    • Mattson MP, Tomaselli KJ, Tydel RE. Calcium destabilizing and neurodegenerative effects of aggregated β-amyloid peptide are attenuated by basic FGF. Brain Res 621:35-49; 1993.
    • (1993) Brain Res , vol.621 , pp. 35-49
    • Mattson, M.P.1    Tomaselli, K.J.2    Tydel, R.E.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 65:1740-1751;1995.
    • (1995) J Neurochem , vol.65 , pp. 1740-1751
    • Mattson, M.P.1    Lovell, M.A.2    Furukawa, K.3    Markesbery, W.R.4
  • 108
    • 0028179069 scopus 로고
    • N-methyk-D-aspartic acid receptor structure and function
    • !08 McBain CJ, Mayer ML. N-methyk-D-aspartic acid receptor structure and function. Physiol Rev 74:723-760;1994.
    • (1994) Physiol Rev , vol.74 , pp. 723-760
    • McBain, C.J.1    Mayer, M.L.2
  • 109
    • 0030910847 scopus 로고    scopus 로고
    • Increased susceptibility of Alzheimer's disease temporal cortex to oxygen free radical-mediated process
    • McIntosh LF, Trush MA, Troncoso JC. Increased susceptibility of Alzheimer's disease temporal cortex to oxygen free radical-mediated process. Free Radic Biol Med 23:183-190;1997.
    • (1997) Free Radic Biol Med , vol.23 , pp. 183-190
    • McIntosh, L.F.1    Trush, M.A.2    Troncoso, J.C.3
  • 111
    • 0031948327 scopus 로고    scopus 로고
    • Antioxidant interaction of catechin, cyanidin, caffeic acid, quercatin and ellagic acid on human LDL oxidation
    • Meyer AS, Heinonen M, Frankel EN. Antioxidant interaction of catechin, cyanidin, caffeic acid, quercatin and ellagic acid on human LDL oxidation. Food Chem 61:71-75;1998.
    • (1998) Food Chem , vol.61 , pp. 71-75
    • Meyer, A.S.1    Heinonen, M.2    Frankel, E.N.3
  • 112
    • 0026597915 scopus 로고
    • Redoxcycling of iron and lipid peroxidation
    • Minotti G, Aust SD. Redoxcycling of iron and lipid peroxidation. Lipids 27:219-226; 1992.
    • (1992) Lipids , vol.27 , pp. 219-226
    • Minotti, G.1    Aust, S.D.2
  • 114
    • 0028810883 scopus 로고
    • Structure and function of the NMDA receptor channel
    • Mori H, Mishma M. Structure and function of the NMDA receptor channel. Neuropharmacology 34:1219-1237;1995.
    • (1995) Neuropharmacology , vol.34 , pp. 1219-1237
    • Mori, H.1    Mishma, M.2
  • 115
    • 0028897733 scopus 로고
    • Clinical experience with excitatory amino acid antagonist drugs
    • Muir KW. Lees KR. Clinical experience with excitatory amino acid antagonist drugs. Stroke 26:503-513;1995.
    • (1995) Stroke , vol.26 , pp. 503-513
    • Muir, K.W.1    Lees, K.R.2
  • 117
    • 0029564967 scopus 로고
    • Age-related changes in the lipofuscin accumulation of brain and heart
    • Nakano M, Cenzil F, Mizuno R, Gotoh S. Age-related changes in the lipofuscin accumulation of brain and heart. Gerontology 41 (suppl 2):69-79;1995.
    • (1995) Gerontology , vol.41 , Issue.2 SUPPL. , pp. 69-79
    • Nakano, M.1    Cenzil, F.2    Mizuno, R.3    Gotoh, S.4
  • 118
    • 0030758614 scopus 로고    scopus 로고
    • Comparative studies of enhanced iron-mediated production of hydroxyl radical by glutathione. cysteine, ascorbic acid and selective catechols
    • Nappi AJ, Vass E. Comparative studies of enhanced iron-mediated production of hydroxyl radical by glutathione. cysteine, ascorbic acid and selective catechols. Biochim Bicphys Cata 1336:295-301;1997.
    • (1997) Biochim Bicphys Cata , vol.1336 , pp. 295-301
    • Nappi, A.J.1    Vass, E.2
  • 119
    • 0025940118 scopus 로고
    • Nitric oxide mediates neuronal death after focal cerebral ischemia in the mouse
    • Nowicki JP, Duval D, Poignet H, Scatton B. Nitric oxide mediates neuronal death after focal cerebral ischemia in the mouse. Eur J Pharmacol 204:339-340;1991.
    • (1991) Eur J Pharmacol , vol.204 , pp. 339-340
    • Nowicki, J.P.1    Duval, D.2    Poignet, H.3    Scatton, B.4
  • 120
    • 0027496238 scopus 로고
    • A radical hypothesis for neurodegeneration
    • Olanow CW. A radical hypothesis for neurodegeneration. Trends Neurosci 16:439-444; 1993.
    • (1993) Trends Neurosci , vol.16 , pp. 439-444
    • Olanow, C.W.1
  • 121
    • 0031172065 scopus 로고    scopus 로고
    • NF-κB: A crucial transcription factor for glial and neuronal cell formation
    • O'Neill LAJ, Kaltschmidt C. NF-κB: A crucial transcription factor for glial and neuronal cell formation. Trends Neurosci 20:252-258; 1997.
    • (1997) Trends Neurosci , vol.20 , pp. 252-258
    • O'Neill, L.A.J.1    Kaltschmidt, C.2
  • 123
    • 0028224781 scopus 로고
    • Pharmacological regulation of AP-1 transcription factor DNA binding activity
    • Pennypacker KR, Hong J. McMiliian MK. Pharmacological regulation of AP-1 transcription factor DNA binding activity. FA-SEB J 8:475-478;1994.
    • (1994) FA-SEB J , vol.8 , pp. 475-478
    • Pennypacker, K.R.1    Hong, J.2    McMiliian, M.K.3
  • 125
    • 0030924506 scopus 로고    scopus 로고
    • βAmyloid neurotoxicity in vitro: Evidence of oxidative stress but not protection by antioxidants
    • Pike CJ, Ramezan-Arab N, Cotman CW. βAmyloid neurotoxicity in vitro: Evidence of oxidative stress but not protection by antioxidants. J Neurochem 69:1601-1611;1997.
    • (1997) J Neurochem , vol.69 , pp. 1601-1611
    • Pike, C.J.1    Ramezan-Arab, N.2    Cotman, C.W.3
  • 126
    • 0023080585 scopus 로고
    • Astrocytes synthesize apolipoprotein E and metabolize apolipoprotein E-containing lipoproteins
    • Pitas RE, Bayles JK, Lee SH, Foss D, Mahley RW. Astrocytes synthesize apolipoprotein E and metabolize apolipoprotein E-containing lipoproteins. Biochim Biophys Acta 917:148-161;1984.
    • (1984) Biochim Biophys Acta , vol.917 , pp. 148-161
    • Pitas, R.E.1    Bayles, J.K.2    Lee, S.H.3    Foss, D.4    Mahley, R.W.5
  • 127
  • 128
    • 0030772342 scopus 로고    scopus 로고
    • Changes in amyloid precursor proteins and apolipoprotein E immunoreactivity following ischemic injury m rat with long-term survival: Influence of idebenone treatment
    • Pluta R, Barcikowska M, Debicki G, Ryba M, Januszewski S. Changes in amyloid precursor proteins and apolipoprotein E immunoreactivity following ischemic injury m rat with long-term survival: Influence of idebenone treatment. Neurosci Lett 232:95-98;1997.
    • (1997) Neurosci Lett , vol.232 , pp. 95-98
    • Pluta, R.1    Barcikowska, M.2    Debicki, G.3    Ryba, M.4    Januszewski, S.5
  • 129
    • 0030092881 scopus 로고    scopus 로고
    • Apolipoprotein E in the brain and its role in Alzheimer's disease
    • Poirier J. Apolipoprotein E in the brain and its role in Alzheimer's disease. J Psychiat Neurosci 21:128-134;1996.
    • (1996) J Psychiat Neurosci , vol.21 , pp. 128-134
    • Poirier, J.1
  • 132
    • 0030005401 scopus 로고    scopus 로고
    • Function of metabotropic glutamate receptors in learning and memory
    • Riedel G. Function of metabotropic glutamate receptors in learning and memory. Trends Neurosci 19:219-224;1996.
    • (1996) Trends Neurosci , vol.19 , pp. 219-224
    • Riedel, G.1
  • 133
    • 0024557734 scopus 로고
    • Transition metals, ferritin, glutathione and ascorbic acid in Parkinsonian brain
    • Riederer P, Sofic E, Rausch W. Transition metals, ferritin, glutathione and ascorbic acid in Parkinsonian brain. J Neurochem 52:515-521;1989.
    • (1989) J Neurochem , vol.52 , pp. 515-521
    • Riederer, P.1    Sofic, E.2    Rausch, W.3
  • 134
    • 0027080934 scopus 로고
    • Cellular pool of transient feme iron, chelatable by deferoxamine and distinct from femtin. that is involved in oxidative cell injury
    • Rothman RJ, Serron: A, Farber JI. Cellular pool of transient feme iron, chelatable by deferoxamine and distinct from femtin. that is involved in oxidative cell injury. Mol Pharmacol 42:703-710;1992.
    • (1992) Mol Pharmacol , vol.42 , pp. 703-710
    • Rothman, R.J.1    Serron, A.2    Farber, J.I.3
  • 135
    • 0030030030 scopus 로고    scopus 로고
    • Increased antioxidant enzymes activity in amyloid βprotein-resistant cells
    • Sagara Y, Dargasch R, Klier FG, Schuhen D, Behl C. Increased antioxidant enzymes activity in amyloid βprotein-resistant cells. J Neurosci 16:497-505;1996.
    • (1996) J Neurosci , vol.16 , pp. 497-505
    • Sagara, Y.1    Dargasch, R.2    Klier, F.G.3    Schuhen, D.4    Behl, C.5
  • 136
    • 0023755121 scopus 로고
    • Superoxide production from nonenzymatically glycated protein
    • Sakurai T, Tsuchiya S. Superoxide production from nonenzymatically glycated protein. FEBS Leu 236:406-410;1988.
    • (1988) FEBS Leu , vol.236 , pp. 406-410
    • Sakurai, T.1    Tsuchiya, S.2
  • 138
    • 0028274216 scopus 로고
    • Evidence for mitochondrial disfunction in Parkinson's disease - A critical appraisal
    • Schapira AHV. Evidence for mitochondrial disfunction in Parkinson's disease - a critical appraisal. Mov Disord 9:125-138;1994.
    • (1994) Mov Disord , vol.9 , pp. 125-138
    • Schapira, A.H.V.1
  • 139
    • 0030868480 scopus 로고    scopus 로고
    • The role of mitochondrial dysfunction and neuronal nitric oxide in animal models of neurodegenerative diseases
    • Schulz JB, Matthews RT, Klockgether T, Dichgans J, Beal MF. The role of mitochondrial dysfunction and neuronal nitric oxide in animal models of neurodegenerative diseases. Mol Cell Biochem 174:193-197;1997.
    • (1997) Mol Cell Biochem , vol.174 , pp. 193-197
    • Schulz, J.B.1    Matthews, R.T.2    Klockgether, T.3    Dichgans, J.4    Beal, M.F.5
  • 140
    • 0029126754 scopus 로고
    • Redox signalling by transcription factors NF-kappa B and AP-1 in lymphocytes
    • Schulze-Osthoff K, Los M, Bauerle PA. Redox signalling by transcription factors NF-kappa B and AP-1 in lymphocytes. Biochem Pharmacol 50:735-741;1995.
    • (1995) Biochem Pharmacol , vol.50 , pp. 735-741
    • Schulze-Osthoff, K.1    Los, M.2    Bauerle, P.A.3
  • 141
    • 0025114688 scopus 로고
    • The metabolism of L-arginine and its significance for the biosynthesis of endothelium-derived relaxing factor: L-Glutamine inhibits the generation of L-arginine by cultured endothelial cells
    • Sessa WC, Hecker M, Mitchell JA, Vane JR. The metabolism of L-arginine and its significance for the biosynthesis of endothelium-derived relaxing factor: L-Glutamine inhibits the generation of L-arginine by cultured endothelial cells. Proc Natl Acad Sci USA 87: 8607-8611;1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8607-8611
    • Sessa, W.C.1    Hecker, M.2    Mitchell, J.A.3    Vane, J.R.4
  • 142
    • 0026646605 scopus 로고
    • Isolation and quantitation of soluble Alzheimer's β-peptide from biological fluids
    • Seubert P, Urgo-Pelfrey C, Esch F, et al. Isolation and quantitation of soluble Alzheimer's β-peptide from biological fluids. Nature 359: 325-327;1992.
    • (1992) Nature , vol.359 , pp. 325-327
    • Seubert, P.1    Urgo-Pelfrey, C.2    Esch, F.3
  • 143
    • 0030927075 scopus 로고    scopus 로고
    • Glutamate, excitotoxicity and amyotrophic lateral sclerosis
    • Shaw PJ, Ince PG. Glutamate, excitotoxicity and amyotrophic lateral sclerosis. J Neurol 247(suppl 2):S3-S14;1997.
    • (1997) J Neurol , vol.247 , Issue.2 SUPPL.
    • Shaw, P.J.1    Ince, P.G.2
  • 144
    • 0001507543 scopus 로고    scopus 로고
    • The role of oxidative processes and metal ions in aging and Alzheimer's disease
    • Connor JR. ed. New York, Plenum Press
    • Shinobu LA, Beal MF. The role of oxidative processes and metal ions in aging and Alzheimer's disease. In: Connor JR. ed. Metals and Oxidative Damage in Neurological Disorders. New York, Plenum Press. 237-275; 1997.
    • (1997) Metals and Oxidative Damage in Neurological Disorders , pp. 237-275
    • Shinobu, L.A.1    Beal, M.F.2
  • 145
    • 0030770947 scopus 로고    scopus 로고
    • Oxidative stress in closed-head injury. Brain antioxidant capacity as an indicator of functional outcome
    • Shohami E, Beit-Yannai E, Horowitz M, Kohen R. Oxidative stress in closed-head injury. Brain antioxidant capacity as an indicator of functional outcome. J Cereb Blood FIowMetab 17:1007-1019;1997.
    • (1997) J Cereb Blood FIowMetab , vol.17 , pp. 1007-1019
    • Shohami, E.1    Beit-Yannai, E.2    Horowitz, M.3    Kohen, R.4
  • 148
    • 0027328852 scopus 로고
    • Protein oxidative damage is associated with life expectancy of house flies
    • Sohal RS, Agarwal S, Dubey A, Orr WC Protein oxidative damage is associated with life expectancy of house flies. Proc Natl Acad Sci USA 90:7255-7259;1993.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7255-7259
    • Sohal, R.S.1    Agarwal, S.2    Dubey, A.3    Orr, W.C.4
  • 149
    • 0345724066 scopus 로고
    • Dopamine turnover and glutathione oxidation: Implications for Parkinson's disease
    • Spina MB, Cohen G. Dopamine turnover and glutathione oxidation: implications for Parkinson's disease. Proc Natl Acad Sci USA 86: 1398-1400;1989.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1398-1400
    • Spina, M.B.1    Cohen, G.2
  • 150
    • 0027183423 scopus 로고
    • Oxidation of free ammo acids and amino acid residues in proteins by radiolysis and by metal-cataiyzed reactions
    • Stadtman ER Oxidation of free ammo acids and amino acid residues in proteins by radiolysis and by metal-cataiyzed reactions. Annu Rev Biochem 62:797-821, 1993.
    • (1993) Annu Rev Biochem , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 151
    • 0024603895 scopus 로고
    • Beyond cholesterol: Modifications of low density lipoprotein that increases its alherogenicin
    • Steinberg D, Parthasarathy S, Carew TE, Khoo JC, Witztum JL. Beyond cholesterol: Modifications of low density lipoprotein that increases its alherogenicin. N Engl J Med 320:915-924;1989.
    • (1989) N Engl J Med , vol.320 , pp. 915-924
    • Steinberg, D.1    Parthasarathy, S.2    Carew, T.E.3    Khoo, J.C.4    Witztum, J.L.5
  • 152
    • 0028929328 scopus 로고
    • Mechanism and gene of cellular suicide
    • Steller H. Mechanism and gene of cellular suicide. Science 267:1445-1449;1995.
    • (1995) Science , vol.267 , pp. 1445-1449
    • Steller, H.1
  • 154
    • 12044254746 scopus 로고
    • Binding of human apohpoprotein E to synthetic amyloid beta peptides: Isoform specific effects and implication for late-onset Alzheimer's disease
    • Strittmatter WJ, Weisgraber KH, Huang DY. et al. Binding of human apohpoprotein E to synthetic amyloid beta peptides: Isoform specific effects and implication for late-onset Alzheimer's disease. Proc Natl Acad Sci USA 90:8098-8102;1993.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8098-8102
    • Strittmatter, W.J.1    Weisgraber, K.H.2    Huang, D.Y.3
  • 156
    • 0024584020 scopus 로고
    • Nitric oxide. A macrophage product responsible for cytostasis and respiratory inhibition in tumor target cells
    • Stuehr DJ, Nathan CF. Nitric oxide. A macrophage product responsible for cytostasis and respiratory inhibition in tumor target cells. J Exp Med 169:1543-1555;1989.
    • (1989) J Exp Med , vol.169 , pp. 1543-1555
    • Stuehr, D.J.1    Nathan, C.F.2
  • 159
    • 0026687022 scopus 로고
    • The biochemical mechanism of the excitotoxicity of kainic acid. Free radical formation
    • Sun AY, Cheng Y, Bu Q, Oldfield F. The biochemical mechanism of the excitotoxicity of kainic acid. Free radical formation. Mol Chem Neuropathol 17:51-63;1992.
    • (1992) Mol Chem Neuropathol , vol.17 , pp. 51-63
    • Sun, A.Y.1    Cheng, Y.2    Bu, Q.3    Oldfield, F.4
  • 160
    • 0027235477 scopus 로고
    • Free radical and lipid peroxidation in manganese-induced neuronal cell injury
    • Sun AY, Yang WL, Kim HD. Free radical and lipid peroxidation in manganese-induced neuronal cell injury. Ann NY Acad Sci 679: 359-363;1993.
    • (1993) Ann NY Acad Sci , vol.679 , pp. 359-363
    • Sun, A.Y.1    Yang, W.L.2    Kim, H.D.3
  • 161
    • 0002952315 scopus 로고    scopus 로고
    • The protective action of resveratral on apoptotic cell death induced by oxidized lipoproteins
    • Packard L, ed. Champaign, AOCS Press
    • Sun AY, Chen YM, Lusiak B. The protective action of resveratral on apoptotic cell death induced by oxidized lipoproteins. In: Packard L, ed. Biological Oxidants and Antioxidants: Molecular Mechanism and Health Effect. Champaign, AOCS Press 210-222;1998.
    • (1998) Biological Oxidants and Antioxidants: Molecular Mechanism and Health Effect , pp. 210-222
    • Sun, A.Y.1    Chen, Y.M.2    Lusiak, B.3
  • 163
    • 0000354585 scopus 로고
    • Structural basis of the cognitive alterations in Alzheimer's disease
    • Terry RD, Katzman R, Bick KL, eds. New York, Raven Press
    • Terry RD, Masliah E, Hansen LA. Structural basis of the cognitive alterations in Alzheimer's disease. In: Terry RD, Katzman R, Bick KL, eds. Alzheimer's Disease. New York, Raven Press, 179-196;1994.
    • (1994) Alzheimer's Disease , pp. 179-196
    • Terry, R.D.1    Masliah, E.2    Hansen, L.A.3
  • 165
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson CB. Apoptosis in the pathogenesis and treatment of disease. Science 267:1456-1462;1995.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 166
    • 0029001909 scopus 로고
    • The transcription factor DNA binding activity in PC12 cells undergoing apoptosis after glucose deprivation
    • Tong L, Perez-Polo JB. The transcription factor DNA binding activity in PC12 cells undergoing apoptosis after glucose deprivation. NeurosciLett 191:137-140;1995.
    • (1995) NeurosciLett , vol.191 , pp. 137-140
    • Tong, L.1    Perez-Polo, J.B.2
  • 168
    • 0343812110 scopus 로고    scopus 로고
    • Oxidative stress and antioxidant treatment in diabetic neuropathy
    • Van Dam PS, Bravenbaer B. Oxidative stress and antioxidant treatment in diabetic neuropathy. Neurosci Res Commun 21:41-48; 1997.
    • (1997) Neurosci Res Commun , vol.21 , pp. 41-48
    • Van Dam, P.S.1    Bravenbaer, B.2
  • 169
    • 0028326952 scopus 로고
    • An evolutionary perspective on apoptosis
    • Vaux DL, Haecker G, Strasser A. An evolutionary perspective on apoptosis. Cell 76: 777-779;1994.
    • (1994) Cell , vol.76 , pp. 777-779
    • Vaux, D.L.1    Haecker, G.2    Strasser, A.3
  • 170
    • 0030959281 scopus 로고    scopus 로고
    • Antioxidant constituents from licorice roots: Isolation, structure elucidation and antioxidative capacity toward LDL oxidation
    • Vaya J, Belinky PA, Aviram M. Antioxidant constituents from licorice roots: Isolation, structure elucidation and antioxidative capacity toward LDL oxidation. Free Radie Biol Med 23:302-313;1997.
    • (1997) Free Radie Biol Med , vol.23 , pp. 302-313
    • Vaya, J.1    Belinky, P.A.2    Aviram, M.3
  • 173
    • 0027931558 scopus 로고
    • Exposure to hydrogen peroxide induces cell death via apoptosis in cultured rat cortical neurons
    • Whittemore ER, Loo DT. Cotman CW. Exposure to hydrogen peroxide induces cell death via apoptosis in cultured rat cortical neurons. Neuroreport 5:1485-1488;1994.
    • (1994) Neuroreport , vol.5 , pp. 1485-1488
    • Whittemore, E.R.1    Loo, D.T.2    Cotman, C.W.3
  • 174
    • 0030049032 scopus 로고    scopus 로고
    • Damage to DNA by reactive oxygen and nitrogen species: Role in inflammatory disease and progression to cancer
    • Wiseman H, Halliweil B. Damage to DNA by reactive oxygen and nitrogen species: Role in inflammatory disease and progression to cancer. Biochem J 313:17-29;1996.
    • (1996) Biochem J , vol.313 , pp. 17-29
    • Wiseman, H.1    Halliweil, B.2
  • 176
  • 177
    • 84878729739 scopus 로고    scopus 로고
    • Baxinduced cell death may not require interleukin 1-beta-converting enzyme-like proteases
    • Xiang J, Chao DT, Korsmeyer SJ. Baxinduced cell death may not require interleukin 1-beta-converting enzyme-like proteases. Proc Natl Acad Sci 29:2431-2439;1996.
    • (1996) Proc Natl Acad Sci , vol.29 , pp. 2431-2439
    • Xiang, J.1    Chao, D.T.2    Korsmeyer, S.J.3
  • 178
    • 84878719243 scopus 로고    scopus 로고
    • Paraquat-induced cell death m PC12 cells
    • in press
    • Yang W, Sun AY. Paraquat-induced cell death m PC12 cells. Neurochem Res, in press.
    • Neurochem Res
    • Yang, W.1    Sun, A.Y.2
  • 179
    • 0031943867 scopus 로고    scopus 로고
    • Paraquat-induced free radical reaction in mouse brain microsomes
    • Yang W, Sun AY. Paraquat-induced free radical reaction in mouse brain microsomes. Neurochem Res 23:47-53;1998.
    • (1998) Neurochem Res , vol.23 , pp. 47-53
    • Yang, W.1    Sun, A.Y.2
  • 180
    • 0028809209 scopus 로고
    • Bad. a heterodimeric partner for bcl-x1 and bcl-2 displace Bax and promotes cell death
    • Yang E, Zha J, Jockel J, Boisi LG, Thompson CB, Korsmeyer SJ. Bad. a heterodimeric partner for bcl-x1 and bcl-2 displace Bax and promotes cell death. Cell 80:285-291;1995.
    • (1995) Cell , vol.80 , pp. 285-291
    • Yang, E.1    Zha, J.2    Jockel, J.3    Boisi, L.G.4    Thompson, C.B.5    Korsmeyer, S.J.6
  • 181
    • 0029896354 scopus 로고    scopus 로고
    • Mechanisms of neuronal degeneration in Alzheimer's disease
    • Yankner BA. Mechanisms of neuronal degeneration in Alzheimer's disease. Neuron 16: 921-932;1996.
    • (1996) Neuron , vol.16 , pp. 921-932
    • Yankner, B.A.1
  • 182
    • 0029058571 scopus 로고
    • Alzheimer's neurofibrillary lesions: Molecular nature and potential roles of different compounds
    • Yen SH, Liu WK, Hall FL, Yan SD, Stern D, Dickson DW. Alzheimer's neurofibrillary lesions: Molecular nature and potential roles of different compounds. Neurobiol Aging 16: 381-387;1995.
    • (1995) Neurobiol Aging , vol.16 , pp. 381-387
    • Yen, S.H.1    Liu, W.K.2    Hall, F.L.3    Yan, S.D.4    Stern, D.5    Dickson, D.W.6
  • 183
    • 0028885795 scopus 로고
    • Free radicals generated during the glycation reaction of amino acid by methvlglyoxal
    • Yim HS, Rang SO, Hah YC, Chock PB, Yim MB. Free radicals generated during the glycation reaction of amino acid by methvlglyoxal. J Biol Chem 270:28228-28233;1995.
    • (1995) J Biol Chem , vol.270 , pp. 28228-28233
    • Yim, H.S.1    Rang, S.O.2    Hah, Y.C.3    Chock, P.B.4    Yim, M.B.5
  • 184
    • 0029042778 scopus 로고
    • Test tube stimulated lipofiscinogenesis. Effect of oxidative stress on autophagocytotic degradation
    • Yin D, Yeian X, Brunk UT. Test tube stimulated lipofiscinogenesis. Effect of oxidative stress on autophagocytotic degradation. Mech Ageing Dev 81:37-50;1995.
    • (1995) Mech Ageing Dev , vol.81 , pp. 37-50
    • Yin, D.1    Yeian, X.2    Brunk, U.T.3
  • 185
    • 0029972278 scopus 로고    scopus 로고
    • Biochemical basis of lipofuscin, ceroid and age pigment-like fluorophores
    • Yin D. Biochemical basis of lipofuscin, ceroid and age pigment-like fluorophores. Free Radie Biol Med 21:871-888;1996.
    • (1996) Free Radie Biol Med , vol.21 , pp. 871-888
    • Yin, D.1
  • 186
    • 0028206341 scopus 로고
    • BHa and BH2 domains of bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax
    • Yin XM, Oltval ZN, Korsmeyer SJ. BHa and BH2 domains of bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax. Nature 369:321-323;1994.
    • (1994) Nature , vol.369 , pp. 321-323
    • Yin, X.M.1    Oltval, Z.N.2    Korsmeyer, S.J.3
  • 187
    • 0031081488 scopus 로고    scopus 로고
    • Deleterious network hypothesis of aging
    • Ying W. Deleterious network hypothesis of aging, Med Hypotheses 48:143-148;1997.
    • (1997) Med Hypotheses , vol.48 , pp. 143-148
    • Ying, W.1
  • 188
    • 0027942138 scopus 로고
    • The NOS inhibitor, 7-nitroindazole, decreases focal infarct volume but not the response to topical acethylcholine in pial vessels
    • Yoshida T, Limmroth V, Irikura K, Moskowitz MA. The NOS inhibitor, 7-nitroindazole, decreases focal infarct volume but not the response to topical acethylcholine in pial vessels. J Cereb Blood Flow Metab 14:924-929;1994.
    • (1994) J Cereb Blood Flow Metab , vol.14 , pp. 924-929
    • Yoshida, T.1    Limmroth, V.2    Irikura, K.3    Moskowitz, M.A.4
  • 190
    • 0031929586 scopus 로고    scopus 로고
    • Role of oxidative stress and glutathione system in loss of dopamine neurons due to impairment of energy metabolism
    • Zeevalk GD, Bernard LP, Nicklas WJ. Role of oxidative stress and glutathione system in loss of dopamine neurons due to impairment of energy metabolism. J Neurochem 70: 1421-1430;1998.
    • (1998) J Neurochem , vol.70 , pp. 1421-1430
    • Zeevalk, G.D.1    Bernard, L.P.2    Nicklas, W.J.3
  • 191
    • 0026509485 scopus 로고
    • Induction of nitric oxide synthase activity by toxic shock syndrome ia a macrophage-monocytic cell line
    • Zembonicz AC, Vane JR. Induction of nitric oxide synthase activity by toxic shock syndrome ia a macrophage-monocytic cell line. Proc Natl Acad Sci: USA 89:2051-2055; 1992.
    • (1992) Proc Natl Acad Sci: USA , vol.89 , pp. 2051-2055
    • Zembonicz, A.C.1    Vane, J.R.2
  • 195
    • 0029754637 scopus 로고    scopus 로고
    • Alzheimer's amyloid-β peptide forms denaturant-resistant complex with type E3 but not type E4 isoforms of native apolipoprotein E
    • Zhou Z, Smith JD, Greengard P, Gandy S. Alzheimer's amyloid-β peptide forms denaturant-resistant complex with type E3 but not type E4 isoforms of native apolipoprotein E. Mol Med 2:175-180;1996.
    • (1996) Mol Med , vol.2 , pp. 175-180
    • Zhou, Z.1    Smith, J.D.2    Greengard, P.3    Gandy, S.4
  • 196
    • 0029593549 scopus 로고
    • Induction of age pigment accumulation in the brain cells of young male rats through iron-injection into the cerebrospinal fluid
    • Zs-Nagy I, Steiber J, Janey F. Induction of age pigment accumulation in the brain cells of young male rats through iron-injection into the cerebrospinal fluid. Gerontology 41 (suppl 2):145-158;1995.
    • (1995) Gerontology , vol.41 , Issue.2 SUPPL. , pp. 145-158
    • Zs-Nagy, I.1    Steiber, J.2    Janey, F.3


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