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Volumn 14, Issue 1-2, 2005, Pages 46-60

Multifunctional activities of green tea catechins in neuroprotection: Modulation of cell survival genes, iron-dependent oxidative stress and PKC signaling pathway

Author keywords

( ) Epigallocatechin 3 gallate; Cell signaling; Green tea catechins; Iron chelation; Neurite outgrowth; Neurodegeneration; Neuroprotection; Neurorescue; Parkinson's disease; Protein kinase C

Indexed keywords

CATECHIN; EPIGALLOCATECHIN GALLATE; FLAVONOID; GREEN TEA EXTRACT; HYDROXYL RADICAL; IRON CHELATING AGENT; NITRIC OXIDE; REACTIVE OXYGEN METABOLITE; SCAVENGER;

EID: 20944444111     PISSN: 1424862X     EISSN: None     Source Type: Journal    
DOI: 10.1159/000085385     Document Type: Review
Times cited : (342)

References (129)
  • 2
    • 0028360527 scopus 로고
    • Inhibitory effects of black tea, green tea, decaffeinated black tea, and decaffeinated green tea on ultraviolet B light-induced skin carcinogenesis in 7,12-dimethylbenz[a]anthra cene-initiated SKH-1 mice
    • Wang ZY, Huang MT, Lou YR, Xie JG, Reuhl KR, Newmark HL, Ho CT, Yang CS, Conney AH: Inhibitory effects of black tea, green tea, decaffeinated black tea, and decaffeinated green tea on ultraviolet B light-induced skin carcinogenesis in 7,12-dimethylbenz[a]anthra cene-initiated SKH-1 mice. Cancer Res 1994;54:3428-3455.
    • (1994) Cancer Res , vol.54 , pp. 3428-3455
    • Wang, Z.Y.1    Huang, M.T.2    Lou, Y.R.3    Xie, J.G.4    Reuhl, K.R.5    Newmark, H.L.6    Ho, C.T.7    Yang, C.S.8    Conney, A.H.9
  • 5
    • 0038121053 scopus 로고    scopus 로고
    • Tea catechins and polyphenols: Health effects, metabolism, and antioxidant functions
    • Higdon JV, Frei B: Tea catechins and polyphenols: health effects, metabolism, and antioxidant functions. Crit Rev Food Sci Nutr 2003;43:89-143.
    • (2003) Crit Rev Food Sci Nutr , vol.43 , pp. 89-143
    • Higdon, J.V.1    Frei, B.2
  • 6
    • 3042759124 scopus 로고    scopus 로고
    • Natural phenolic compounds as cardiovascular therapeutics: Potential role of their anti-inflammatory effects
    • Jiang F, Dusting GJ: Natural phenolic compounds as cardiovascular therapeutics: Potential role of their anti-inflammatory effects. Curr Vasc Pharmacol 2003;1:135-156.
    • (2003) Curr Vasc Pharmacol , vol.1 , pp. 135-156
    • Jiang, F.1    Dusting, G.J.2
  • 7
    • 0033050624 scopus 로고    scopus 로고
    • ESR study on the structure-antioxidant activity relationship of tea catechins and their epimers
    • Guo Q, Zhao B, Shen S, Hou J, Hu J, Xin W: ESR study on the structure-antioxidant activity relationship of tea catechins and their epimers. Biochim Biophys Acta 1999;1427:13-23.
    • (1999) Biochim Biophys Acta , vol.1427 , pp. 13-23
    • Guo, Q.1    Zhao, B.2    Shen, S.3    Hou, J.4    Hu, J.5    Xin, W.6
  • 9
    • 0030582664 scopus 로고    scopus 로고
    • Studies on protective mechanisms of four components of green tea polyphenols against lipid peroxidation in synaptosomes
    • Guo Q, Zhao B, Li M, Shen S, Xin W: Studies on protective mechanisms of four components of green tea polyphenols against lipid peroxidation in synaptosomes. Biochim Biophys Acta 1996;1304:210-222.
    • (1996) Biochim Biophys Acta , vol.1304 , pp. 210-222
    • Guo, Q.1    Zhao, B.2    Li, M.3    Shen, S.4    Xin, W.5
  • 10
  • 12
    • 1642382889 scopus 로고    scopus 로고
    • Cell signaling pathways in the neuroprotective actions of the green tea polyphenol (-)-epigallocatechin-3-gallate: Implications for neurodegenerative diseases
    • Mandel S, Weinreb O, Amit T, Youdim MBH: Cell signaling pathways in the neuroprotective actions of the green tea polyphenol (-)-epigallocatechin-3- gallate: implications for neurodegenerative diseases. J Neurochem 2004;88:1555-1569.
    • (2004) J Neurochem , vol.88 , pp. 1555-1569
    • Mandel, S.1    Weinreb, O.2    Amit, T.3    Youdim, M.B.H.4
  • 13
    • 4444226105 scopus 로고    scopus 로고
    • Neurological mechanisms of green tea polyphenols in Alzheimer's and Parkinson's diseases
    • Weinreb O, Mandel S, Amit T, Youdim MB: Neurological mechanisms of green tea polyphenols in Alzheimer's and Parkinson's diseases. J Nutr Biochem 2004;15:506-516.
    • (2004) J Nutr Biochem , vol.15 , pp. 506-516
    • Weinreb, O.1    Mandel, S.2    Amit, T.3    Youdim, M.B.4
  • 15
    • 0031441473 scopus 로고    scopus 로고
    • Absorption and distribution of tea catechin, (-)-epigallocatechin-3- gallate, in the rat
    • Tokyo
    • Nakagawa K, Miyazawa T: Absorption and distribution of tea catechin, (-)-epigallocatechin-3-gallate, in the rat. J Nutr Sci Vitaminol (Tokyo) 1997;43:679-684.
    • (1997) J Nutr Sci Vitaminol , vol.43 , pp. 679-684
    • Nakagawa, K.1    Miyazawa, T.2
  • 18
    • 0034993599 scopus 로고    scopus 로고
    • Molecular pathways involved in the neurotoxicity of 6-OHDA, dopamine and MPTP: Contribution to the apoptotic theory in Parkinson's disease
    • Blum D, Torch S, Lambeng N, Nissou M, Benabid AL, Sadoul R, Verna JM: Molecular pathways involved in the neurotoxicity of 6-OHDA, dopamine and MPTP: Contribution to the apoptotic theory in Parkinson's disease. Prog Neurobiol 2001;65:135-172.
    • (2001) Prog Neurobiol , vol.65 , pp. 135-172
    • Blum, D.1    Torch, S.2    Lambeng, N.3    Nissou, M.4    Benabid, A.L.5    Sadoul, R.6    Verna, J.M.7
  • 19
    • 0036285744 scopus 로고    scopus 로고
    • Neuroprotection in Parkinson's disease: Love story or mission impossible?
    • Linazasoro G: Neuroprotection in Parkinson's disease: Love story or mission impossible? Expert Rev Neurotherapeut 2002;2:403-416.
    • (2002) Expert Rev Neurotherapeut , vol.2 , pp. 403-416
    • Linazasoro, G.1
  • 20
    • 0037025111 scopus 로고    scopus 로고
    • Selective loss of 20S proteasome alpha-subunits in the substantia nigra pars compacta in Parkinson's disease
    • McNaught KS, Belizaire R, Jenner P, Olanow CW, Isacson O: Selective loss of 20S proteasome alpha-subunits in the substantia nigra pars compacta in Parkinson's disease. Neurosci Lett 2002;326:155-158.
    • (2002) Neurosci Lett , vol.326 , pp. 155-158
    • McNaught, K.S.1    Belizaire, R.2    Jenner, P.3    Olanow, C.W.4    Isacson, O.5
  • 21
    • 0002563935 scopus 로고    scopus 로고
    • Iron and neurodegeneration: Prospects for neuroprotection
    • Olanow CW, Jenner P, Youdim MB (eds): London, Academic Press
    • Olanow CW, Youdim MB: Iron and neurodegeneration: Prospects for neuroprotection; in Olanow CW, Jenner P, Youdim MB (eds): Neurodegeneration and Neuroprotection in Parkinson's Disease. London, Academic Press, 1996, pp 55-69.
    • (1996) Neurodegeneration and Neuroprotection in Parkinson's Disease , pp. 55-69
    • Olanow, C.W.1    Youdim, M.B.2
  • 22
    • 0034517802 scopus 로고    scopus 로고
    • cDNA microarray to study gene expression of dopaminergic neurodegeneration and neuroprotection in MPTP and 6-hydroxydopamine models: Implications for idiopathic Parkinson's disease
    • Mandel S, Grunblatt E, Youdim MBH: cDNA microarray to study gene expression of dopaminergic neurodegeneration and neuroprotection in MPTP and 6-hydroxydopamine models: Implications for idiopathic Parkinson's disease. J Neural Transm Suppl 2000;60:117-124.
    • (2000) J Neural Transm Suppl , vol.60 , pp. 117-124
    • Mandel, S.1    Grunblatt, E.2    Youdim, M.B.H.3
  • 23
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer W, Przedborski S: Parkinson's disease: Mechanisms and models. Neuron 2003;39:889-909.
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 28
    • 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 1996;47:S161-170.
    • (1996) Neurology , vol.47
    • Jenner, P.1    Olanow, C.W.2
  • 29
    • 19944428747 scopus 로고    scopus 로고
    • Gene expression profiling of parkinsonian substantia nigra pars compacta: Alterations in ubiquitin-proteasome, heat shock protein, iron and oxidative stress regulated proteins, cell adhesion/cellular matrix and vesicle trafficking genes
    • Grunblatt E, Mandel S, Jacob-Hirsch J, Zeligson S, Amariglo N, Rechavi G, Li J, Ravid R, Roggendorf W, Riederer P, Youdim MB: Gene expression profiling of parkinsonian substantia nigra pars compacta: Alterations in ubiquitin-proteasome, heat shock protein, iron and oxidative stress regulated proteins, cell adhesion/cellular matrix and vesicle trafficking genes. J Neural Transm 2004;111:1543-1573.
    • (2004) J Neural Transm , vol.111 , pp. 1543-1573
    • Grunblatt, E.1    Mandel, S.2    Jacob-Hirsch, J.3    Zeligson, S.4    Amariglo, N.5    Rechavi, G.6    Li, J.7    Ravid, R.8    Roggendorf, W.9    Riederer, P.10    Youdim, M.B.11
  • 30
    • 0034851553 scopus 로고    scopus 로고
    • Green tea polyphenol (-)-epigallocatechin-3-gallate prevents N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced dopaminergic neurodegeneration
    • Levites Y, Weinreb O, Maor G, Youdim MBH, Mandel S: Green tea polyphenol (-)-epigallocatechin-3-gallate prevents N-methyl-4-phenyl-1,2,3,6- tetrahydropyridine-induced dopaminergic neurodegeneration. J Neurochem 2001;78:1073-1082.
    • (2001) J Neurochem , vol.78 , pp. 1073-1082
    • Levites, Y.1    Weinreb, O.2    Maor, G.3    Youdim, M.B.H.4    Mandel, S.5
  • 31
    • 0034617960 scopus 로고    scopus 로고
    • The efficacy of an antioxidant cocktail on lipid peroxide level and superoxide dismutase activity in aged rat brain and DNA damage in iron-induced epileptogenic foci
    • Komatsu M, Hiramatsu M: The efficacy of an antioxidant cocktail on lipid peroxide level and superoxide dismutase activity in aged rat brain and DNA damage in iron-induced epileptogenic foci. Toxicology 2000;148:143-148.
    • (2000) Toxicology , vol.148 , pp. 143-148
    • Komatsu, M.1    Hiramatsu, M.2
  • 33
    • 0037403751 scopus 로고    scopus 로고
    • Enzymology of methylation of tea catechins and inhibition of catechol-O-methyltransferase by (-)-epigallocatechin gallate
    • Lu H, Meng X, Yang CS: Enzymology of methylation of tea catechins and inhibition of catechol-O-methyltransferase by (-)-epigallocatechin gallate. Drug Metab Dispos 2003;31:572-579.
    • (2003) Drug Metab Dispos , vol.31 , pp. 572-579
    • Lu, H.1    Meng, X.2    Yang, C.S.3
  • 34
    • 0034733810 scopus 로고    scopus 로고
    • Protective effects of the green tea polyphenol (-)-epigallocatechin gallate against hippocampal neuronal damage after transient global ischemia in gerbils
    • Lee S, Suh S, Kim S: Protective effects of the green tea polyphenol (-)-epigallocatechin gallate against hippocampal neuronal damage after transient global ischemia in gerbils. Neurosci Lett 2000;287:191-194.
    • (2000) Neurosci Lett , vol.287 , pp. 191-194
    • Lee, S.1    Suh, S.2    Kim, S.3
  • 35
    • 4444326084 scopus 로고    scopus 로고
    • Protective effect of green tea polyphenol EGCG against neuronal damage and brain edema after unilateral cerebral ischemia in gerbils
    • Lee H, Bae JH, Lee SR: Protective effect of green tea polyphenol EGCG against neuronal damage and brain edema after unilateral cerebral ischemia in gerbils. J Neurosci Res 2004;77:892-900.
    • (2004) J Neurosci Res , vol.77 , pp. 892-900
    • Lee, H.1    Bae, J.H.2    Lee, S.R.3
  • 36
  • 37
    • 19544375313 scopus 로고    scopus 로고
    • Neuroprotective effects of (-)-epigallocatechin gallate after hypoxia-ischemia-induced brain damage: Novel mechanisms of action
    • Sutherland BA, Shaw OM, Clarkson AN, Jackson DM, Sammut IA, Appleton I: Neuroprotective effects of (-)-epigallocatechin gallate after hypoxia-ischemia-induced brain damage: novel mechanisms of action. Faseb J 2004.
    • (2004) Faseb J
    • Sutherland, B.A.1    Shaw, O.M.2    Clarkson, A.N.3    Jackson, D.M.4    Sammut, I.A.5    Appleton, I.6
  • 40
    • 0035884625 scopus 로고    scopus 로고
    • Flavonoids protect neurons from oxidized low-density-lipoprotein-induced apoptosis involving c-Jun N-terminal kinase (JNK), c-Jun and caspase-3
    • Schroeter H, Spencer JP, Rice-Evans C, Williams RJ: Flavonoids protect neurons from oxidized low-density-lipoprotein-induced apoptosis involving c-Jun N-terminal kinase (JNK), c-Jun and caspase-3. Biochem J 2001; 358:547-557.
    • (2001) Biochem J , vol.358 , pp. 547-557
    • Schroeter, H.1    Spencer, J.P.2    Rice-Evans, C.3    Williams, R.J.4
  • 41
    • 0035868353 scopus 로고    scopus 로고
    • Epicatechin and its in vivo metabolite, 3′-O-methyl epicatechin, protect human fibroblasts from oxidative-stress-induced cell death involving caspase-3 activation
    • Spencer JP, Schroeter H, Kuhnle G, Srai SK, Tyrrell RM, Hahn U, Rice-Evans C: Epicatechin and its in vivo metabolite, 3′-O-methyl epicatechin, protect human fibroblasts from oxidative-stress-induced cell death involving caspase-3 activation. Biochem J 2001;354:493-500.
    • (2001) Biochem J , vol.354 , pp. 493-500
    • Spencer, J.P.1    Schroeter, H.2    Kuhnle, G.3    Srai, S.K.4    Tyrrell, R.M.5    Hahn, U.6    Rice-Evans, C.7
  • 42
  • 43
    • 13844271390 scopus 로고    scopus 로고
    • Dietary polyphenols protect dopamine neurons from oxidative insults and apoptosis: Investigations in primary rat mesencephalic cultures
    • Mercer LD, Kelly BL, Horne MK, Beart PM: Dietary polyphenols protect dopamine neurons from oxidative insults and apoptosis: Investigations in primary rat mesencephalic cultures. Biochem Pharmacol 2005;69:339-345.
    • (2005) Biochem Pharmacol , vol.69 , pp. 339-345
    • Mercer, L.D.1    Kelly, B.L.2    Horne, M.K.3    Beart, P.M.4
  • 44
    • 0037163110 scopus 로고    scopus 로고
    • Involvement of protein kinase C activation and cell survival/cell cycle genes in green tea polyphenol (-)-epigallocatechin-3-gallate neuroprotective action
    • Levites Y, Amit T, Youdim MBH, Mandel S: Involvement of protein kinase C activation and cell survival/cell cycle genes in green tea polyphenol (-)-epigallocatechin-3-gallate neuroprotective action. J Biol Chem 2002;277:30574-30580.
    • (2002) J Biol Chem , vol.277 , pp. 30574-30580
    • Levites, Y.1    Amit, T.2    Youdim, M.B.H.3    Mandel, S.4
  • 45
    • 0035930961 scopus 로고    scopus 로고
    • The green tea polyphenol (-)-epigallocatechin gallate attenuates beta-amyloid-induced neurotoxicity in cultured hippocampal neurons
    • Choi YT, Jung CH, Lee SR, Bae JH, Baek WK, Suh MH, Park J, Park CW, Suh SI: The green tea polyphenol (-)-epigallocatechin gallate attenuates beta-amyloid-induced neurotoxicity in cultured hippocampal neurons. Life Sci 2001;70:603-614.
    • (2001) Life Sci , vol.70 , pp. 603-614
    • Choi, Y.T.1    Jung, C.H.2    Lee, S.R.3    Bae, J.H.4    Baek, W.K.5    Suh, M.H.6    Park, J.7    Park, C.W.8    Suh, S.I.9
  • 46
    • 0038661168 scopus 로고    scopus 로고
    • Neuroprotection and neurorescue against amyloid beta toxicity and PKC-dependent release of non-amyloidogenic soluble precusor protein by green tea polyphenol (-)-epigallocatechin-3-gallate
    • Levites Y, Amit T, Mandel S, Youdim MBH: Neuroprotection and neurorescue against amyloid beta toxicity and PKC-dependent release of non-amyloidogenic soluble precusor protein by green tea polyphenol (-)-epigallocatechin-3-gallate. FASEB J 2003;17:952-954.
    • (2003) FASEB J , vol.17 , pp. 952-954
    • Levites, Y.1    Amit, T.2    Mandel, S.3    Youdim, M.B.H.4
  • 47
    • 20144371838 scopus 로고    scopus 로고
    • Green tea polyphenol (-)-epigallocatechin-3-gallate induces neurorescue of long-term serum-deprived PC12 cells and promotes neurite outgrowth
    • in press
    • Reznichenko L, Amit T, Youdim MB, Mandel S: Green tea polyphenol (-)-epigallocatechin-3-gallate induces neurorescue of long-term serum-deprived PC12 cells and promotes neurite outgrowth. J Neurochem 2005;in press.
    • (2005) J Neurochem
    • Reznichenko, L.1    Amit, T.2    Youdim, M.B.3    Mandel, S.4
  • 48
    • 0038322479 scopus 로고    scopus 로고
    • cDNA gene expression profile homology of antioxidants and their anti-apoptotic and pro-apoptotic activities in human neuroblastoma cells
    • Weinreb O, Mandel S, Youdim MBH: cDNA gene expression profile homology of antioxidants and their anti-apoptotic and pro-apoptotic activities in human neuroblastoma cells. FASEB J 2003;17:935-937.
    • (2003) FASEB J , vol.17 , pp. 935-937
    • Weinreb, O.1    Mandel, S.2    Youdim, M.B.H.3
  • 49
    • 0029910233 scopus 로고    scopus 로고
    • Vitamin C: Antioxidant or pro-oxidant in vivo?
    • Halliwell B: Vitamin C: antioxidant or pro-oxidant in vivo? Free Rad Res 1996;25:439-454.
    • (1996) Free Rad Res , vol.25 , pp. 439-454
    • Halliwell, B.1
  • 52
    • 3042574709 scopus 로고    scopus 로고
    • Potential toxicity of flavonoids and other dietary phenolics: Significance for their chemopreventive and anticancer properties
    • Galati G, O'Brien PJ: Potential toxicity of flavonoids and other dietary phenolics: Significance for their chemopreventive and anticancer properties. Free Radic Biol Med 2004;37:287-303.
    • (2004) Free Radic Biol Med , vol.37 , pp. 287-303
    • Galati, G.1    O'Brien, P.J.2
  • 53
    • 0035666414 scopus 로고    scopus 로고
    • Tea flavonoids: Bioavailability in vivo and effects on cell signaling pathways in vitro
    • Wiseman S, Mulder T, Rietveld A: Tea flavonoids: Bioavailability in vivo and effects on cell signaling pathways in vitro. Antioxid Redox Signal 2001;3:1009-1021.
    • (2001) Antioxid Redox Signal , vol.3 , pp. 1009-1021
    • Wiseman, S.1    Mulder, T.2    Rietveld, A.3
  • 54
    • 0030982798 scopus 로고    scopus 로고
    • Evidence that the early loss of membrane protein kinase C is a necessary step in the excitatory amino acid-induced death of primary cortical neurons
    • Durkin JP, Tremblay R, Chakravarthy B, Mealing G, Morley P, Small D, Song D: Evidence that the early loss of membrane protein kinase C is a necessary step in the excitatory amino acid-induced death of primary cortical neurons. J Neurochem 1997;68:1400-1412.
    • (1997) J Neurochem , vol.68 , pp. 1400-1412
    • Durkin, J.P.1    Tremblay, R.2    Chakravarthy, B.3    Mealing, G.4    Morley, P.5    Small, D.6    Song, D.7
  • 55
    • 0035341268 scopus 로고    scopus 로고
    • How protein kinase C activation protects nerve cells from oxidative stress-induced cell death
    • Maher P: How protein kinase C activation protects nerve cells from oxidative stress-induced cell death. J Neurosci 2001;21:2929-2938.
    • (2001) J Neurosci , vol.21 , pp. 2929-2938
    • Maher, P.1
  • 56
    • 0034041345 scopus 로고    scopus 로고
    • Pharmacological demonstration of the differential involvement of protein kinase C isoforms in short- and long-term memory formation and retrieval of one-trial avoidance in rats
    • Berl
    • Vianna MR, Barros DM, Silva T, Choi H, Madche C, Rodrigues C, Medina JH, Izquierdo I: Pharmacological demonstration of the differential involvement of protein kinase C isoforms in short- and long-term memory formation and retrieval of one-trial avoidance in rats. Psychopharmacology (Berl) 2000;150: 77-84.
    • (2000) Psychopharmacology , vol.150 , pp. 77-84
    • Vianna, M.R.1    Barros, D.M.2    Silva, T.3    Choi, H.4    Madche, C.5    Rodrigues, C.6    Medina, J.H.7    Izquierdo, I.8
  • 57
    • 2642545057 scopus 로고    scopus 로고
    • Epsilon protein kinase C mediated ischemic tolerance requires activation of the extracellular regulated kinase pathway in the organotypic hippocampal slice
    • Lange-Asschenfeldt C, Raval AP, Dave KR, Mochly-Rosen D, Sick TJ, Perez-Pinzon MA: Epsilon protein kinase C mediated ischemic tolerance requires activation of the extracellular regulated kinase pathway in the organotypic hippocampal slice. J Cereb Blood Flow Metab 2004;24:636-645.
    • (2004) J Cereb Blood Flow Metab , vol.24 , pp. 636-645
    • Lange-Asschenfeldt, C.1    Raval, A.P.2    Dave, K.R.3    Mochly-Rosen, D.4    Sick, T.J.5    Perez-Pinzon, M.A.6
  • 58
    • 0037345781 scopus 로고    scopus 로고
    • Estrogen activates protein kinase C in neurons: Role in neuroprotection
    • Cordey M, Gundimeda U, Gopalakrishna R, Pike CJ: Estrogen activates protein kinase C in neurons: Role in neuroprotection. J Neurochem 2003;84:1340-1348.
    • (2003) J Neurochem , vol.84 , pp. 1340-1348
    • Cordey, M.1    Gundimeda, U.2    Gopalakrishna, R.3    Pike, C.J.4
  • 59
    • 1942472491 scopus 로고    scopus 로고
    • Neuroprotective effects of resveratrol against beta-amyloid-induced neurotoxicity in rat hippocampal neurons: Involvement of protein kinase C
    • Han YS, Zheng WH, Bastianetto S, Chabot JG, Quirion R: Neuroprotective effects of resveratrol against beta-amyloid-induced neurotoxicity in rat hippocampal neurons: involvement of protein kinase C. Br J Pharmacol 2004;141:997-1005.
    • (2004) Br J Pharmacol , vol.141 , pp. 997-1005
    • Han, Y.S.1    Zheng, W.H.2    Bastianetto, S.3    Chabot, J.G.4    Quirion, R.5
  • 60
    • 0345308381 scopus 로고    scopus 로고
    • Rasagiline: An anti-Parkinson drug with neuroprotective activity
    • Youdim MBH: Rasagiline: An anti-Parkinson drug with neuroprotective activity. Expert Rev Neurotherapeut 2003;3:737-749.
    • (2003) Expert Rev Neurotherapeut , vol.3 , pp. 737-749
    • Youdim, M.B.H.1
  • 61
    • 6944242126 scopus 로고    scopus 로고
    • Neuroprotection via prosurvival protein kinase C isoforms associated with Bcl-2 family members
    • Weinreb O, Bar-Am O, Amit T, Chillag-Talmor O, Youdim MB: Neuroprotection via prosurvival protein kinase C isoforms associated with Bcl-2 family members. FASEB J 2004;18:1471-1473.
    • (2004) FASEB J , vol.18 , pp. 1471-1473
    • Weinreb, O.1    Bar-Am, O.2    Amit, T.3    Chillag-Talmor, O.4    Youdim, M.B.5
  • 62
    • 1842621154 scopus 로고    scopus 로고
    • Iron and alpha-synuclein in the substantia Nigra of MPTP-treated mice: Effect of neuroprotective drugs R-apomorphine and green tea polyphenol (-)-epigallocatechin-3-gallate
    • Mandel S, Maor G, Youdim MBH: Iron and alpha-synuclein in the substantia Nigra of MPTP-treated mice: Effect of neuroprotective drugs R-apomorphine and green tea polyphenol (-)-epigallocatechin-3-gallate. J Mol Neurosci 2004;24:401-416.
    • (2004) J Mol Neurosci , vol.24 , pp. 401-416
    • Mandel, S.1    Maor, G.2    Youdim, M.B.H.3
  • 63
    • 0032566717 scopus 로고    scopus 로고
    • A functional role for mitochondrial protein kinase Calpha in Bcl2 phosphorylation and suppression of apoptosis
    • Ruvolo PP, Deng X, Carr BK, May WS: A functional role for mitochondrial protein kinase Calpha in Bcl2 phosphorylation and suppression of apoptosis. J Biol Chem 1998;273:25436-25442.
    • (1998) J Biol Chem , vol.273 , pp. 25436-25442
    • Ruvolo, P.P.1    Deng, X.2    Carr, B.K.3    May, W.S.4
  • 67
    • 0021242923 scopus 로고
    • Direct evidence of incorporation of 12-O-[20-2H1]tetradecanoylphorbol-13- acetate into artificial membranes as determined by deuterium magnetic resonance
    • Saito H, Tabeta R, Kodama M, Nagata C, Sato Y: Direct evidence of incorporation of 12-O-[20-2H1]tetradecanoylphorbol-13-acetate into artificial membranes as determined by deuterium magnetic resonance. Cancer Lett 1984;22:65-69.
    • (1984) Cancer Lett , vol.22 , pp. 65-69
    • Saito, H.1    Tabeta, R.2    Kodama, M.3    Nagata, C.4    Sato, Y.5
  • 68
    • 0037315101 scopus 로고    scopus 로고
    • Essential role for integrin linked kinase in Akt-mediated integrin survival signaling in hippocampal neurons
    • Gary DS, Milhavet O, Camandola S, Mattson MP: Essential role for integrin linked kinase in Akt-mediated integrin survival signaling in hippocampal neurons. J Neurochem 2003;84:878-890.
    • (2003) J Neurochem , vol.84 , pp. 878-890
    • Gary, D.S.1    Milhavet, O.2    Camandola, S.3    Mattson, M.P.4
  • 69
    • 0342927484 scopus 로고    scopus 로고
    • Insulin-like growth factor-I protects axotomized rat retinal ganglion cells from secondary death via PI3-K-dependent Akt phosphorylation and inhibition of caspase-3 in vivo
    • Kermer P, Klocker N, Labes M, Bahr M: Insulin-like growth factor-I protects axotomized rat retinal ganglion cells from secondary death via PI3-K-dependent Akt phosphorylation and inhibition of caspase-3 in vivo. J Neurosci 2000;20:2-8.
    • (2000) J Neurosci , vol.20 , pp. 2-8
    • Kermer, P.1    Klocker, N.2    Labes, M.3    Bahr, M.4
  • 70
    • 0033118665 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase pathway mediates estrogen neuroprotection after glutamate toxicity in primary cortical neurons
    • Singer CA, Figueroa-Masot XA, Batchelor RH, Dorsa DM: The mitogen-activated protein kinase pathway mediates estrogen neuroprotection after glutamate toxicity in primary cortical neurons. J Neurosci 1999;19:2455-2463.
    • (1999) J Neurosci , vol.19 , pp. 2455-2463
    • Singer, C.A.1    Figueroa-Masot, X.A.2    Batchelor, R.H.3    Dorsa, D.M.4
  • 72
    • 0037205044 scopus 로고    scopus 로고
    • Signaling pathways for PC12 cell differentiation: Making the right connections
    • Vaudry D, Stork PJ, Lazarovici P, Eiden LE: Signaling pathways for PC12 cell differentiation: Making the right connections. Science 2002;296:1648-1649.
    • (2002) Science , vol.296 , pp. 1648-1649
    • Vaudry, D.1    Stork, P.J.2    Lazarovici, P.3    Eiden, L.E.4
  • 73
    • 0036139987 scopus 로고    scopus 로고
    • Inhibition of the c-Jun N-terminal kinase signaling pathway by the mixed lineage kinase inhibitor CEP-1347 (KT7515) preserves metabolism and growth of trophic factor-deprived neurons
    • Harris CA, Deshmukh M, Tsui-Pierchala B, Maroney AC, Johnson EM Jr: Inhibition of the c-Jun N-terminal kinase signaling pathway by the mixed lineage kinase inhibitor CEP-1347 (KT7515) preserves metabolism and growth of trophic factor-deprived neurons. J Neurosci 2002;22:103-113.
    • (2002) J Neurosci , vol.22 , pp. 103-113
    • Harris, C.A.1    Deshmukh, M.2    Tsui-Pierchala, B.3    Maroney, A.C.4    Johnson Jr., E.M.5
  • 74
    • 0033607259 scopus 로고    scopus 로고
    • MEK1 protein kinase inhibition protects against damage resulting from focal cerebral ischemia
    • Alessandrini A, Namura S, Moskowitz MA, Bonventre JV: MEK1 protein kinase inhibition protects against damage resulting from focal cerebral ischemia. Proc Natl Acad Sci USA 1999;96:12866-12869.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12866-12869
    • Alessandrini, A.1    Namura, S.2    Moskowitz, M.A.3    Bonventre, J.V.4
  • 75
  • 76
    • 0031408813 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinases by green tea polyphenols: Potential signaling pathways in the regulation of antioxidant-responsive element-mediated phase II enzyme gene expression
    • Yu R, Jiao JJ, Duh JL, Gudehithlu K, Tan TH, Kong AN: Activation of mitogen-activated protein kinases by green tea polyphenols: Potential signaling pathways in the regulation of antioxidant-responsive element-mediated phase II enzyme gene expression. Carcinogenesis 1997;18:451-456.
    • (1997) Carcinogenesis , vol.18 , pp. 451-456
    • Yu, R.1    Jiao, J.J.2    Duh, J.L.3    Gudehithlu, K.4    Tan, T.H.5    Kong, A.N.6
  • 77
    • 0034573074 scopus 로고    scopus 로고
    • Activation of antioxidant-response element (ARE), mitogen-activated protein kinases (MAPKs) and caspases by major green tea polyphenol components during cell survival and death
    • Chen C, Yu R, Owuor ED, Kong AN: Activation of antioxidant-response element (ARE), mitogen-activated protein kinases (MAPKs) and caspases by major green tea polyphenol components during cell survival and death. Arch Pharm Res 2000;23:605-612.
    • (2000) Arch Pharm Res , vol.23 , pp. 605-612
    • Chen, C.1    Yu, R.2    Owuor, E.D.3    Kong, A.N.4
  • 78
    • 0036708902 scopus 로고    scopus 로고
    • Antioxidants and oxidants regulated signal transduction pathways
    • Owuor ED, Kong AN: Antioxidants and oxidants regulated signal transduction pathways. Biochem Pharmacol 2002;64:765-770.
    • (2002) Biochem Pharmacol , vol.64 , pp. 765-770
    • Owuor, E.D.1    Kong, A.N.2
  • 80
    • 20944448841 scopus 로고    scopus 로고
    • A constituent of green tea, epigallocatechin-3-gallate, activates endothelial nitric oxide synthase by a PI3K-, PKA-, and Akt-dependent pathway, and leads to endothelial-dependent vasorelaxation
    • Lorenz M, Wessler S, Follmann E, Michaelis W, Dusterhoft T, Baumann G, Stangl K, Stangl V: A constituent of green tea, epigallocatechin-3-gallate, activates endothelial nitric oxide synthase by a PI3K-, PKA-, and Akt-dependent pathway, and leads to endothelial-dependent vasorelaxation. J Biol Chem 2003.
    • (2003) J Biol Chem
    • Lorenz, M.1    Wessler, S.2    Follmann, E.3    Michaelis, W.4    Dusterhoft, T.5    Baumann, G.6    Stangl, K.7    Stangl, V.8
  • 81
    • 1642454583 scopus 로고    scopus 로고
    • Green tea inhibits human inducible nitric-oxide synthase expression by down-regulating signal transducer and activator of transcription-1alpha activation
    • Tedeschi E, Menegazzi M, Yao Y, Suzuki H, Forstermann U, Kleinert H: Green tea inhibits human inducible nitric-oxide synthase expression by down-regulating signal transducer and activator of transcription-1alpha activation. Mol Pharmacol 2004;65:111-120.
    • (2004) Mol Pharmacol , vol.65 , pp. 111-120
    • Tedeschi, E.1    Menegazzi, M.2    Yao, Y.3    Suzuki, H.4    Forstermann, U.5    Kleinert, H.6
  • 83
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: Regulators of the cellular life-or-death switch
    • Cory S, Adams JM: The Bcl2 family: Regulators of the cellular life-or-death switch. Nat Rev Cancer 2002;2:647-656.
    • (2002) Nat Rev Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 84
    • 0031057656 scopus 로고    scopus 로고
    • Bcl-2 gene family in the nervous system
    • Merry DE, Korsmeyer SJ: Bcl-2 gene family in the nervous system. Annu Rev Neurosci 1997;20:245-267.
    • (1997) Annu Rev Neurosci , vol.20 , pp. 245-267
    • Merry, D.E.1    Korsmeyer, S.J.2
  • 85
    • 0034232147 scopus 로고    scopus 로고
    • Ginkgo biloba extract (EGb 761) and CNS functions: Basic studies and clinical applications
    • DeFeudis FV, Drieu K: Ginkgo biloba extract (EGb 761) and CNS functions: Basic studies and clinical applications. Curr Drug Targets 2000;1:25-58.
    • (2000) Curr Drug Targets , vol.1 , pp. 25-58
    • DeFeudis, F.V.1    Drieu, K.2
  • 86
    • 0035865819 scopus 로고    scopus 로고
    • Flavonoids protect neuronal cells from oxidative stress by three distinct mechanisms
    • Ishige K, Schubert D, Sagara Y: Flavonoids protect neuronal cells from oxidative stress by three distinct mechanisms. Free Radic Biol Med 2001;30:433-446.
    • (2001) Free Radic Biol Med , vol.30 , pp. 433-446
    • Ishige, K.1    Schubert, D.2    Sagara, Y.3
  • 88
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • Bush AI: The metallobiology of Alzheimer's disease. Trends Neurosci 2003;26:207-214.
    • (2003) Trends Neurosci , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 91
    • 2642555563 scopus 로고    scopus 로고
    • HIF1 and oxygen sensing in the brain
    • Sharp FR, Bernaudin M: HIF1 and oxygen sensing in the brain. Nat Rev Neurosci 2004;5:437-448.
    • (2004) Nat Rev Neurosci , vol.5 , pp. 437-448
    • Sharp, F.R.1    Bernaudin, M.2
  • 92
    • 1642387020 scopus 로고    scopus 로고
    • Hypoxia-inducible factor (HIF-1)alpha: Its protein stability and biological functions
    • Lee JW, Bae SH, Jeong JW, Kim SH, Kim KW: Hypoxia-inducible factor (HIF-1)alpha: Its protein stability and biological functions. Exp Mol Med 2004;36:1-12.
    • (2004) Exp Mol Med , vol.36 , pp. 1-12
    • Lee, J.W.1    Bae, S.H.2    Jeong, J.W.3    Kim, S.H.4    Kim, K.W.5
  • 94
    • 0242710750 scopus 로고    scopus 로고
    • Hypoxic regulation of the 6-phosphofructo-2-kinase/fructose-2,6- bisphosphatase gene family (PFKFB-1-4) expression in vivo
    • Minchenko O, Opentanova I, Caro J: Hypoxic regulation of the 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene family (PFKFB-1-4) expression in vivo. FEBS Lett 2003;554:264-270.
    • (2003) FEBS Lett , vol.554 , pp. 264-270
    • Minchenko, O.1    Opentanova, I.2    Caro, J.3
  • 95
    • 0032812762 scopus 로고    scopus 로고
    • Regulation of the iron regulatory proteins by reactive nitrogen and oxygen species
    • Hanson ES, Leibold EA: Regulation of the iron regulatory proteins by reactive nitrogen and oxygen species. Gene Expr 1999;7:367-376.
    • (1999) Gene Expr , vol.7 , pp. 367-376
    • Hanson, E.S.1    Leibold, E.A.2
  • 96
    • 1642458415 scopus 로고    scopus 로고
    • Iron-mediated degradation of IRP2, an unexpected pathway involving a 2-oxoglutarate-dependent oxygenase activity
    • Wang J, Chen G, Muckenthaler M, Galy B, Hentze MW, Pantopoulos K: Iron-mediated degradation of IRP2, an unexpected pathway involving a 2-oxoglutarate-dependent oxygenase activity. Mol Cell Biol 2004;24:954-965.
    • (2004) Mol Cell Biol , vol.24 , pp. 954-965
    • Wang, J.1    Chen, G.2    Muckenthaler, M.3    Galy, B.4    Hentze, M.W.5    Pantopoulos, K.6
  • 99
    • 0016791488 scopus 로고
    • Subacute myelo-optic neuropathy and clioquinol: An epidemiological case-history for diagnosis
    • Meade TW: Subacute myelo-optic neuropathy and clioquinol: An epidemiological case-history for diagnosis. Br J Prev Soc Med 1975;29:157-169.
    • (1975) Br J Prev Soc Med , vol.29 , pp. 157-169
    • Meade, T.W.1
  • 100
    • 4644275696 scopus 로고    scopus 로고
    • Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer's disease animal models
    • Baum L, Ng A: Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer's disease animal models. J Alzheimers Dis 2004;6:367-377; discussion 443-369.
    • (2004) J Alzheimers Dis , vol.6 , pp. 367-377
    • Baum, L.1    Ng, A.2
  • 101
    • 0035503597 scopus 로고    scopus 로고
    • The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse
    • Lim GP, Chu T, Yang F, Beech W, Frautschy SA, Cole GM: The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse. J Neurosci 2001;21:8370-8377.
    • (2001) J Neurosci , vol.21 , pp. 8370-8377
    • Lim, G.P.1    Chu, T.2    Yang, F.3    Beech, W.4    Frautschy, S.A.5    Cole, G.M.6
  • 103
    • 11144316146 scopus 로고    scopus 로고
    • Bifunctional drug derivatives of MAO-B inhibitor rasagiline and iron chelator VK-28 as a more effective approach to treatment of brain ageing and ageing neurodegenerative diseases
    • Youdim MB, Fridkin M, Zheng H: Bifunctional drug derivatives of MAO-B inhibitor rasagiline and iron chelator VK-28 as a more effective approach to treatment of brain ageing and ageing neurodegenerative diseases. Mech Age Dev 2005;126:317-326.
    • (2005) Mech Age Dev , vol.126 , pp. 317-326
    • Youdim, M.B.1    Fridkin, M.2    Zheng, H.3
  • 104
    • 0346849912 scopus 로고    scopus 로고
    • Neuroprotection by a novel brain permeable iron chelator, VK-28, against 6-hydroxydopamine lesion in rats
    • Shachar DB, Kahana N, Kampel V, Warshawsky A, Youdim MB: Neuroprotection by a novel brain permeable iron chelator, VK-28, against 6-hydroxydopamine lesion in rats. Neuropharmacology 2004;46:254-263.
    • (2004) Neuropharmacology , vol.46 , pp. 254-263
    • Shachar, D.B.1    Kahana, N.2    Kampel, V.3    Warshawsky, A.4    Youdim, M.B.5
  • 105
    • 7944235232 scopus 로고    scopus 로고
    • Novel bifunctional drugs targeting monoamine oxidase inhibition and iron chelation as an approach to neuroprotection in Parkinson's disease and other neurodegenerative diseases
    • Youdim MB, Fridkin M, Zheng H: Novel bifunctional drugs targeting monoamine oxidase inhibition and iron chelation as an approach to neuroprotection in Parkinson's disease and other neurodegenerative diseases. J Neural Transm 2004;111:1455-1471.
    • (2004) J Neural Transm , vol.111 , pp. 1455-1471
    • Youdim, M.B.1    Fridkin, M.2    Zheng, H.3
  • 106
    • 11144245220 scopus 로고    scopus 로고
    • Multi-functional drugs for various CNS targets in the treatment of neurodegenerative disorders
    • Youdim MBH, Buccafusco JJ: Multi-functional drugs for various CNS targets in the treatment of neurodegenerative disorders. Trends Pharmacol Sci 2005;26:27-35.
    • (2005) Trends Pharmacol Sci , vol.26 , pp. 27-35
    • Youdim, M.B.H.1    Buccafusco, J.J.2
  • 107
    • 11844255676 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of novel bifunctional iron-chelators as potential agents for neuroprotection in Alzheimer's, Parkinson's, and other neurodegenerative diseases
    • Zheng H, Weiner LM, Bar-Am O, Epsztejn S, Cabantchik ZI, Warshawsky A, Youdim MB, Fridkin M: Design, synthesis, and evaluation of novel bifunctional iron-chelators as potential agents for neuroprotection in Alzheimer's, Parkinson's, and other neurodegenerative diseases. Bioorg Med Chem 2005;13:773-783.
    • (2005) Bioorg Med Chem , vol.13 , pp. 773-783
    • Zheng, H.1    Weiner, L.M.2    Bar-Am, O.3    Epsztejn, S.4    Cabantchik, Z.I.5    Warshawsky, A.6    Youdim, M.B.7    Fridkin, M.8
  • 108
    • 0141642253 scopus 로고    scopus 로고
    • Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: Implications for the prevention and therapeutics of Alzheimer's disease
    • Ono K, Yoshiike Y, Takashima A, Hasegawa K, Naiki H, Yamada M: Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: Implications for the prevention and therapeutics of Alzheimer's disease. J Neurochem 2003;87:172-181.
    • (2003) J Neurochem , vol.87 , pp. 172-181
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5    Yamada, M.6
  • 109
  • 110
    • 0033595020 scopus 로고    scopus 로고
    • Wild-type but not Alzheimer-mutant amyloid precursor protein confers resistance against p53-mediated apoptosis
    • Xu X, Yang D, Wyss-Coray T, Yan J, Gan L, Sun Y, Mucke L: Wild-type but not Alzheimer-mutant amyloid precursor protein confers resistance against p53-mediated apoptosis. Proc Natl Acad Sci USA 1999;96:7547-7552.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7547-7552
    • Xu, X.1    Yang, D.2    Wyss-Coray, T.3    Yan, J.4    Gan, L.5    Sun, Y.6    Mucke, L.7
  • 111
    • 0028213567 scopus 로고
    • A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth
    • Small DH, Nurcombe V, Reed G, Clarris H, Moir R, Beyreuther K, Masters CL: A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth. J Neurosci 1994;14:2117-2127.
    • (1994) J Neurosci , vol.14 , pp. 2117-2127
    • Small, D.H.1    Nurcombe, V.2    Reed, G.3    Clarris, H.4    Moir, R.5    Beyreuther, K.6    Masters, C.L.7
  • 112
    • 0032518240 scopus 로고    scopus 로고
    • Involvement of amyloid precursor protein in functional synapse formation in cultured hippocampal neurons
    • Morimoto T, Ohsawa I, Takamura C, Ishiguro M, Kohsaka S: Involvement of amyloid precursor protein in functional synapse formation in cultured hippocampal neurons. J Neurosci Res 1998;51:185-195.
    • (1998) J Neurosci Res , vol.51 , pp. 185-195
    • Morimoto, T.1    Ohsawa, I.2    Takamura, C.3    Ishiguro, M.4    Kohsaka, S.5
  • 113
    • 0036724204 scopus 로고    scopus 로고
    • Iron (III) induces aggregation of hyperphosphorylated tau and its reduction to iron (II) reverses the aggregation: Implications in the formation of neurofibrillary tangles of Alzheimer's disease
    • Yamamoto A, Shin RW, Hasegawa K, Naiki H, Sato H, Yoshimasu F, Kitamoto T: Iron (III) induces aggregation of hyperphosphorylated tau and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease. J Neurochem 2002;82:1137-1147.
    • (2002) J Neurochem , vol.82 , pp. 1137-1147
    • Yamamoto, A.1    Shin, R.W.2    Hasegawa, K.3    Naiki, H.4    Sato, H.5    Yoshimasu, F.6    Kitamoto, T.7
  • 114
    • 0028000825 scopus 로고
    • Altered brain metabolism of iron as a cause of neurodegenerative diseases?
    • Gerlach M, Ben-Shachar D, Riederer P, Youdim MB: Altered brain metabolism of iron as a cause of neurodegenerative diseases? J Neurochem 1994;63:793-807.
    • (1994) J Neurochem , vol.63 , pp. 793-807
    • Gerlach, M.1    Ben-Shachar, D.2    Riederer, P.3    Youdim, M.B.4
  • 115
    • 0141725659 scopus 로고    scopus 로고
    • Neuropathological spectrum of synucleinopathies
    • Jellinger KA: Neuropathological spectrum of synucleinopathies. Mov Disord 2003;18 (suppl 6):2-12.
    • (2003) Mov Disord , vol.18 , Issue.6 SUPPL. , pp. 2-12
    • Jellinger, K.A.1
  • 116
    • 0035873812 scopus 로고    scopus 로고
    • Alpha-Synuclein implicated in Parkinson's disease catalyses the formation of hydrogen peroxide in vitro
    • Turnbull S, Tabner BJ, El-Agnaf OM, Moore S, Davies Y, Allsop D: Alpha-Synuclein implicated in Parkinson's disease catalyses the formation of hydrogen peroxide in vitro. Free Radic Biol Med 2001;30:1163-1170.
    • (2001) Free Radic Biol Med , vol.30 , pp. 1163-1170
    • Turnbull, S.1    Tabner, B.J.2    El-Agnaf, O.M.3    Moore, S.4    Davies, Y.5    Allsop, D.6
  • 119
    • 1842608738 scopus 로고    scopus 로고
    • Hereditary causes of disturbed iron homeostasis in the central nervous system
    • Ponka P: Hereditary causes of disturbed iron homeostasis in the central nervous system. Ann NY Acad Sci 2004;1012:267-281.
    • (2004) Ann NY Acad Sci , vol.1012 , pp. 267-281
    • Ponka, P.1
  • 122
    • 0032879452 scopus 로고    scopus 로고
    • Role of cytochrome c as a stimulator of alpha-synuclein aggregation in Lewy body disease
    • Hashimoto M, Takeda A, Hsu LJ, Takenouchi T, Masliah E: Role of cytochrome c as a stimulator of alpha-synuclein aggregation in Lewy body disease. J Biol Chem 1999;274:28849-28852.
    • (1999) J Biol Chem , vol.274 , pp. 28849-28852
    • Hashimoto, M.1    Takeda, A.2    Hsu, L.J.3    Takenouchi, T.4    Masliah, E.5
  • 123
    • 0025980955 scopus 로고
    • The iron chelator desferrioxamine (Desferal) retards 6-hydroxydopamine- induced degeneration of nigrostriatal dopamine neurons
    • Ben-Shachar D, Eshel G, Finberg JP, Youdim MB: The iron chelator desferrioxamine (Desferal) retards 6-hydroxydopamine-induced degeneration of nigrostriatal dopamine neurons. J Neurochem 1991;56:1441-1444.
    • (1991) J Neurochem , vol.56 , pp. 1441-1444
    • Ben-Shachar, D.1    Eshel, G.2    Finberg, J.P.3    Youdim, M.B.4
  • 124
    • 0030864433 scopus 로고    scopus 로고
    • Desferrioxamine and vitamin e protect against iron and MPTP-induced neurodegeneration in mice
    • Budapest
    • Lan J, Jiang DH: Desferrioxamine and vitamin E protect against iron and MPTP-induced neurodegeneration in mice. J Neural Transm (Budapest) 1997;104:469-481.
    • (1997) J Neural Transm , vol.104 , pp. 469-481
    • Lan, J.1    Jiang, D.H.2
  • 127
    • 0027358350 scopus 로고
    • Worldwide occurrence of Parkinson's disease: An updated review
    • Zhang ZX, Roman GC: Worldwide occurrence of Parkinson's disease: An updated review. Neuroepidemiology 1993;12:195-208.
    • (1993) Neuroepidemiology , vol.12 , pp. 195-208
    • Zhang, Z.X.1    Roman, G.C.2
  • 129
    • 1842504330 scopus 로고    scopus 로고
    • Nutritional iron deprivation attenuates kainate-induced neurotoxicity in rats: Implications for involvement of iron in neurodegeneration
    • Shoham S, Youdim MB: Nutritional iron deprivation attenuates kainate-induced neurotoxicity in rats: implications for involvement of iron in neurodegeneration. Ann NY Acad Sci 2004;1012:94-114.
    • (2004) Ann NY Acad Sci , vol.1012 , pp. 94-114
    • Shoham, S.1    Youdim, M.B.2


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