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Volumn 37, Issue 3, 2004, Pages 304-317

Catechin polyphenols: Neurodegeneration and neuroprotection in neurodegenerative diseases

Author keywords

synuclein; Alzheimer's disease; Antioxidant; Bcl 2 family proteins; Cell signaling; Free radicals; Green tea catechins; Iron; Iron chelating; Neurodegenerative diseases; Neuroprotection; Parkinson's disease

Indexed keywords

1,2,3,6 TETRAHYDRO 1 METHYL 4 PHENYLPYRIDINE; ALZHEIMER DISEASE VACCINE; ANTIOXIDANT; CATECHIN; ENTACAPONE; EPICATECHIN; EPIGALLOCATECHIN GALLATE; FLAVONOID; GINKGO BILOBA EXTRACT; GREEN TEA EXTRACT; IRON; MELATONIN; MITOGEN ACTIVATED PROTEIN KINASE; NITRIC OXIDE; POLYPHENOL DERIVATIVE; PROTEASOME; PROTEIN KINASE C; RASAGILINE; SCAVENGER; SELEGILINE; TOLCAPONE; UBIQUITIN;

EID: 3042667647     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2004.04.012     Document Type: Review
Times cited : (425)

References (135)
  • 1
    • 0642376484 scopus 로고    scopus 로고
    • Neuromelanin and its interaction with iron as a potential risk factor for dopaminergic neurodegeneration underlying Parkinson's disease
    • Gerlach M., Double K.L., Ben-Shachar D., Zecca L., Youdim M.B., Riederer P. Neuromelanin and its interaction with iron as a potential risk factor for dopaminergic neurodegeneration underlying Parkinson's disease. Neurotoxicol. Res. 5:2003;35-44
    • (2003) Neurotoxicol. Res. , vol.5 , pp. 35-44
    • Gerlach, M.1    Double, K.L.2    Ben-Shachar, D.3    Zecca, L.4    Youdim, M.B.5    Riederer, P.6
  • 2
    • 0002563935 scopus 로고    scopus 로고
    • Iron and neurodegeneration: Prospects for neuroprotection
    • C.W. Olanow, P. Jenner, & M.B. Youdim. London: Academic Press
    • Olanow C.W., Youdim M.B. Iron and neurodegeneration: prospects for neuroprotection. Olanow C.W., Jenner P., Youdim M.B. Neurodegeneration and neuroprotection in Parkinson's disease. 1996;55-69 Academic Press, London
    • (1996) Neurodegeneration and Neuroprotection in Parkinson's Disease , pp. 55-69
    • Olanow, C.W.1    Youdim, M.B.2
  • 3
    • 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 M.B.H. 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. 60:2000;117-124
    • (2000) J. Neural Transm. Suppl. , vol.60 , pp. 117-124
    • Mandel, S.1    Grunblatt, E.2    Youdim, M.B.H.3
  • 4
    • 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. Neurother. 2:2002;403-416
    • (2002) Expert Rev. Neurother. , vol.2 , pp. 403-416
    • Linazasoro, G.1
  • 5
    • 0038205745 scopus 로고    scopus 로고
    • Targeting programmed cell death in neurodegenerative diseases
    • Vila M., Przedborski S. Targeting programmed cell death in neurodegenerative diseases. Nat. Rev. Neurosci. 4:2003;365-375
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 365-375
    • Vila, M.1    Przedborski, S.2
  • 6
    • 0037386720 scopus 로고    scopus 로고
    • Using cDNA microarray to assess Parkinson's disease models and the effects of neuroprotective drugs
    • Mandel S., Weinreb O., Youdim M.B. Using cDNA microarray to assess Parkinson's disease models and the effects of neuroprotective drugs. Trends Pharmacol. Sci. 24:2003;184-191
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 184-191
    • Mandel, S.1    Weinreb, O.2    Youdim, M.B.3
  • 7
    • 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 A.L., Sadoul R., Verna J.M. Molecular pathways involved in the neurotoxicity of 6-OHDA, dopamine and MPTP: contribution to the apoptotic theory in Parkinson's disease. Prog. Neurobiol. 65:2001;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
  • 10
    • 0029995757 scopus 로고    scopus 로고
    • Scavenging effects of tea catechins and their derivatives on 1,1-diphenyl-2-picrylhydrazyl radical
    • Nanjo F., Goto K., Seto R., Suzuki M., Sakai M., Hara Y. Scavenging effects of tea catechins and their derivatives on 1, 1-diphenyl-2-picrylhydrazyl radical. Free Radic. Biol. Med. 21:1996;895-902
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 895-902
    • Nanjo, F.1    Goto, K.2    Seto, R.3    Suzuki, M.4    Sakai, M.5    Hara, Y.6
  • 11
    • 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. 1304:1996;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
  • 12
    • 0033976073 scopus 로고    scopus 로고
    • Suppression of lipopolysaccharide-induced nuclear factor kappaB activity by theaflavin-3,3′-digallate from black tea and other polyphenols through down-regulation of IkappaB kinase activity in macrophages
    • Pan M.H., Lin-Shiau S.Y., Ho C.T., Lin J.H., Lin J.K. Suppression of lipopolysaccharide-induced nuclear factor kappaB activity by theaflavin-3, 3′-digallate from black tea and other polyphenols through down-regulation of IkappaB kinase activity in macrophages. Biochem. Pharmacol. 59:2000;357-367
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 357-367
    • Pan, M.H.1    Lin-Shiau, S.Y.2    Ho, C.T.3    Lin, J.H.4    Lin, J.K.5
  • 14
    • 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]anthracene-initiated SKH-1 mice
    • Wang Z.Y., Huang M.T., Lou Y.R., Xie J.G., Reuhl K.R., Newmark H.L., Ho C.T., Yang C.S., Conney A.H. 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]anthracene-initiated SKH-1 mice. Cancer Res. 54:1994;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
  • 16
    • 0038121053 scopus 로고    scopus 로고
    • Tea catechins and polyphenols: Health effects, metabolism, and antioxidant functions
    • Higdon J.V., Frei B. Tea catechins and polyphenols: health effects, metabolism, and antioxidant functions. Crit. Rev. Food Sci. Nutr. 43:2003;89-143
    • (2003) Crit. Rev. Food Sci. Nutr. , vol.43 , pp. 89-143
    • Higdon, J.V.1    Frei, B.2
  • 17
    • 0033012456 scopus 로고    scopus 로고
    • Theaflavin-3,3′-digallate from black tea blocks the nitric oxide synthase by down-regulating the activation of NF-kappaB in macrophages
    • Lin Y.L., Tsai S.H., Lin-Shiau S.Y., Ho C.T., Lin J.K. Theaflavin-3, 3′-digallate from black tea blocks the nitric oxide synthase by down-regulating the activation of NF-kappaB in macrophages. Eur. J. Pharmacol. 367:1999;379-388
    • (1999) Eur. J. Pharmacol. , vol.367 , pp. 379-388
    • Lin, Y.L.1    Tsai, S.H.2    Lin-Shiau, S.Y.3    Ho, C.T.4    Lin, J.K.5
  • 18
    • 0032807021 scopus 로고    scopus 로고
    • Cancer chemoprevention by tea polyphenols through mitotic signal transduction blockade
    • Lin J.K., Liang Y.C., Lin-Shiau S.Y. Cancer chemoprevention by tea polyphenols through mitotic signal transduction blockade. Biochem. Pharmacol. 58:1999;911-915
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 911-915
    • Lin, J.K.1    Liang, Y.C.2    Lin-Shiau, S.Y.3
  • 19
    • 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. 30:2001;433-446
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 433-446
    • Ishige, K.1    Schubert, D.2    Sagara, Y.3
  • 21
    • 0347335785 scopus 로고    scopus 로고
    • Dual mechanisms of green tea extract-induced cell survival in human epidermal keratinocytes
    • Chung J.H., Han J.H., Hwang E.J., Seo J.Y., Cho K.H., Kim K.H., Youn J.I., Eun H.C. Dual mechanisms of green tea extract-induced cell survival in human epidermal keratinocytes. FASEB J. 17:2003;1913-1915
    • (2003) FASEB J. , vol.17 , pp. 1913-1915
    • Chung, J.H.1    Han, J.H.2    Hwang, E.J.3    Seo, J.Y.4    Cho, K.H.5    Kim, K.H.6    Youn, J.I.7    Eun, H.C.8
  • 22
    • 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 E.D., Kong A.N. 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. 23:2000;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
  • 23
    • 1242294387 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. 279:2003;6190-6195
    • (2003) J. Biol. Chem. , vol.279 , pp. 6190-6195
    • Lorenz, M.1    Wessler, S.2    Follmann, E.3    Michaelis, W.4    Dusterhoft, T.5    Baumann, G.6    Stangl, K.7    Stangl, V.8
  • 24
    • 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 M.B.H., 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. 277:2002;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
  • 25
    • 0038661168 scopus 로고    scopus 로고
    • Neuroprotection and neurorescue against amyloid beta toxicity and PKC-dependent release of non-amyloidogenic soluble precursor protein by green tea polyphenol (-)-epigallocatechin-3-gallate
    • Levites Y., Amit T., Mandel S., Youdim M.B.H. Neuroprotection and neurorescue against amyloid beta toxicity and PKC-dependent release of non-amyloidogenic soluble precursor protein by green tea polyphenol (-)-epigallocatechin-3-gallate. FASEB J. 17:2003;952-954
    • (2003) FASEB J. , vol.17 , pp. 952-954
    • Levites, Y.1    Amit, T.2    Mandel, S.3    Youdim, M.B.H.4
  • 26
    • 0038727646 scopus 로고    scopus 로고
    • Gene and protein expression profiles of anti- and pro-apoptotic actions of dopamine, R-apomorphine, green tea polyphenol (-)-epigallocatechine-3- gallate, and melatonin
    • (discussion 387-393)
    • Weinreb O., Mandel S., Youdim M.B. Gene and protein expression profiles of anti- and pro-apoptotic actions of dopamine, R-apomorphine, green tea polyphenol (-)-epigallocatechine-3-gallate, and melatonin. Ann. N. Y. Acad. Sci. 993:2003;351-361. (discussion 387-393)
    • (2003) Ann. N. Y. Acad. Sci. , vol.993 , pp. 351-361
    • Weinreb, O.1    Mandel, S.2    Youdim, M.B.3
  • 27
    • 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. 87:2003;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
  • 28
    • 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 J.P., Rice-Evans C., Williams R.J. Flavonoids protect neurons from oxidized low-density-lipoprotein-induced apoptosis involving c-Jun N-terminal kinase (JNK), c-Jun and caspase-3. Biochem. J. 358:2001;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
  • 30
    • 0035930961 scopus 로고    scopus 로고
    • The green tea polyphenol (-)-epigallocatechin gallate attenuates beta-amyloid-induced neurotoxicity in cultured hippocampal neurons
    • Choi Y.T., Jung C.H., Lee S.R., Bae J.H., Baek W.K., Suh M.H., Park J., Park C.W., Suh S.I. The green tea polyphenol (-)-epigallocatechin gallate attenuates beta-amyloid-induced neurotoxicity in cultured hippocampal neurons. Life Sci. 70:2001;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
  • 31
    • 1342269755 scopus 로고    scopus 로고
    • Green tea polyphenol (-)-epigallocatechin-3-gallate protects rat PC12 cells from apoptosis induced by serum withdrawal independent of P13-Akt pathway
    • Mandel S., Reznichenko L., Amit T., Youdim M. Green tea polyphenol (-)-epigallocatechin-3-gallate protects rat PC12 cells from apoptosis induced by serum withdrawal independent of P13-Akt pathway. Neurotoxicol. Res. 5:2003;419-424
    • (2003) Neurotoxicol. Res. , vol.5 , pp. 419-424
    • Mandel, S.1    Reznichenko, L.2    Amit, T.3    Youdim, M.4
  • 32
    • 0033035855 scopus 로고    scopus 로고
    • Implications of the mechanisms of action of tea polyphenols as antioxidants in vitro for chemoprevention in humans
    • Rice-Evans C. Implications of the mechanisms of action of tea polyphenols as antioxidants in vitro for chemoprevention in humans. Proc. Soc. Exp. Biol. Med. 220:1999;262-266
    • (1999) Proc. Soc. Exp. Biol. Med. , vol.220 , pp. 262-266
    • Rice-Evans, C.1
  • 33
    • 0036145435 scopus 로고    scopus 로고
    • Attenuation of 6-hydroxydopamine (6-OHDA)-induced nuclear factor-kappaB (NF-kappaB) activation and cell death by tea extracts in neuronal cultures
    • Levites Y., Youdim M.B.H., Maor G., Mandel S. Attenuation of 6-hydroxydopamine (6-OHDA)-induced nuclear factor-kappaB (NF-kappaB) activation and cell death by tea extracts in neuronal cultures. Biochem. Pharmacol. 63:2002;21-29
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 21-29
    • Levites, Y.1    Youdim, M.B.H.2    Maor, G.3    Mandel, S.4
  • 38
    • 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 M.B.H., Mandel S. Green tea polyphenol (-)-epigallocatechin-3-gallate prevents N-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine-induced dopaminergic neurodegeneration. J. Neurochem. 78:2001;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
  • 39
    • 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. 148:2000;143-148
    • (2000) Toxicology , vol.148 , pp. 143-148
    • Komatsu, M.1    Hiramatsu, M.2
  • 40
    • 0036708902 scopus 로고    scopus 로고
    • Antioxidants and oxidants regulated signal transduction pathways
    • Owuor E.D., Kong A.N. Antioxidants and oxidants regulated signal transduction pathways. Biochem. Pharmacol. 64:2002;765-770
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 765-770
    • Owuor, E.D.1    Kong, A.N.2
  • 41
  • 42
    • 0028000825 scopus 로고
    • Altered brain metabolism of iron as a cause of neurodegenerative diseases?
    • Gerlach M., Ben-Shachar D., Riederer P., Youdim M.B. Altered brain metabolism of iron as a cause of neurodegenerative diseases? J. Neurochem. 63:1994;793-807
    • (1994) J. Neurochem. , vol.63 , pp. 793-807
    • Gerlach, M.1    Ben-Shachar, D.2    Riederer, P.3    Youdim, M.B.4
  • 44
    • 0141725659 scopus 로고    scopus 로고
    • Neuropathological spectrum of synucleinopathies
    • Jellinger K.A. Neuropathological spectrum of synucleinopathies. Mov. Disord. 18(Suppl. 6):2003;S2-S12
    • (2003) Mov. Disord. , vol.18 , Issue.SUPPL. 6 , pp. 2-S12
    • Jellinger, K.A.1
  • 45
    • 0025943571 scopus 로고
    • The rat brain synucleins; Family of proteins transiently associated with neuronal membrane
    • Maroteaux L., Scheller R.H. The rat brain synucleins; family of proteins transiently associated with neuronal membrane. Brain Res. Mol. Brain Res. 11:1991;335-343
    • (1991) Brain Res. Mol. Brain Res. , vol.11 , pp. 335-343
    • Maroteaux, L.1    Scheller, R.H.2
  • 46
    • 0032102455 scopus 로고    scopus 로고
    • The synucleins: A family of proteins involved in synaptic function, plasticity, neurodegeneration and disease
    • Clayton D.F., George J.M. The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease. Trends Neurosci. 21:1998;249-254
    • (1998) Trends Neurosci. , vol.21 , pp. 249-254
    • Clayton, D.F.1    George, J.M.2
  • 47
    • 0031763264 scopus 로고    scopus 로고
    • The synuclein family
    • Lavedan C. The synuclein family. Genome Res. 8:1998;871-880
    • (1998) Genome Res. , vol.8 , pp. 871-880
    • Lavedan, C.1
  • 48
    • 0035873812 scopus 로고    scopus 로고
    • Alpha-Synuclein implicated in Parkinson's disease catalyses the formation of hydrogen peroxide in vitro
    • Turnbull S., Tabner B.J., El-Agnaf O.M., 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. 30:2001;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
  • 51
    • 0033966487 scopus 로고    scopus 로고
    • Alpha-synuclein up-regulation in substantia nigra dopaminergic neurons following administration of the parkinsonian toxin MPTP
    • Vila M., Vukosavic S., Jackson-Lewis V., Neystat M., Jakowec M., Przedborski S. Alpha-synuclein up-regulation in substantia nigra dopaminergic neurons following administration of the parkinsonian toxin MPTP. J. Neurochem. 74:2000;721-729
    • (2000) J. Neurochem. , vol.74 , pp. 721-729
    • Vila, M.1    Vukosavic, S.2    Jackson-Lewis, V.3    Neystat, M.4    Jakowec, M.5    Przedborski, S.6
  • 52
    • 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 M.B.H. 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
    • (2004) J. Mol. Neurosci.
    • Mandel, S.1    Maor, G.2    Youdim, M.B.H.3
  • 53
    • 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 L.J., Takenouchi T., Masliah E. Role of cytochrome c as a stimulator of alpha-synuclein aggregation in Lewy body disease. J. Biol. Chem. 274:1999;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
  • 54
    • 0025980955 scopus 로고
    • The iron chelator desferrioxamine (Desferal) retards 6-hydroxydopamine- induced degeneration of nigrostriatal dopamine neurons
    • Ben-Shachar D., Eshel G., Finberg J.P., Youdim M.B. The iron chelator desferrioxamine (Desferal) retards 6-hydroxydopamine-induced degeneration of nigrostriatal dopamine neurons. J. Neurochem. 56:1991;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
  • 55
    • 0030864433 scopus 로고    scopus 로고
    • Desferrioxamine and vitamin e protect against iron and MPTP-induced neurodegeneration in mice
    • Lan J., Jiang D.H. Desferrioxamine and vitamin E protect against iron and MPTP-induced neurodegeneration in mice. J. Neural. Transm. (Budapest). 104:1997;469-481
    • (1997) J. Neural. Transm. (Budapest) , vol.104 , pp. 469-481
    • Lan, J.1    Jiang, D.H.2
  • 58
    • 0346849912 scopus 로고    scopus 로고
    • Neuroprotection by a novel brain permeable iron chelator. VK-28, against 6-hydroxydopamine lesion in rats
    • Shachar D.B., Kahana N., Kampel V., Warshawsky A., Youdim M.B. Neuroprotection by a novel brain permeable iron chelator. VK-28, against 6-hydroxydopamine lesion in rats. Neuropharmacology. 46:2004;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
  • 59
    • 1842608744 scopus 로고    scopus 로고
    • Ironing iron out in Parkinson's disease and other neurodegenerative diseases with iron chelators; A lesson from 6-hydroxydopamine and iron chelators desferal and vk-28
    • Youdim M.B.H., Stephenson G., Ben-Shachar D. Ironing iron out in Parkinson's disease and other neurodegenerative diseases with iron chelators; a lesson from 6-hydroxydopamine and iron chelators desferal and vk-28. Ann. N. Y. Acad. Sci. 2004
    • (2004) Ann. N. Y. Acad. Sci.
    • Youdim, M.B.H.1    Stephenson, G.2    Ben-Shachar, D.3
  • 60
    • 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 M.B.H. cDNA gene expression profile homology of antioxidants and their anti-apoptotic and pro-apoptotic activities in human neuroblastoma cells. FASEB J. 17:2003;935-937
    • (2003) FASEB J. , vol.17 , pp. 935-937
    • Weinreb, O.1    Mandel, S.2    Youdim, M.B.H.3
  • 61
  • 62
    • 0013198976 scopus 로고    scopus 로고
    • Mitochondria in cell death: Novel targets for neuroprotection and cardioprotection
    • Mattson M.P., Kroemer G. Mitochondria in cell death: novel targets for neuroprotection and cardioprotection. Trends Mol. Med. 9:2003;196-205
    • (2003) Trends Mol. Med. , vol.9 , pp. 196-205
    • Mattson, M.P.1    Kroemer, G.2
  • 63
    • 0034232147 scopus 로고    scopus 로고
    • Ginkgo biloba extract (EGb 761) and CNS functions: Basic studies and clinical applications
    • DeFeudis F.V., Drieu K. Ginkgo biloba extract (EGb 761) and CNS functions: basic studies and clinical applications. Curr. Drug Targets. 1:2000;25-58
    • (2000) Curr. Drug Targets , vol.1 , pp. 25-58
    • Defeudis, F.V.1    Drieu, K.2
  • 65
    • 0344154296 scopus 로고    scopus 로고
    • Naturally occurring 2′-hydroxyl-substituted flavonoids as high-affinity benzodiazepine site ligands
    • Huen M.S., Hui K.M., Leung J.W., Sigel E., Baur R., Wong J.T., Xue H. Naturally occurring 2′-hydroxyl-substituted flavonoids as high-affinity benzodiazepine site ligands. Biochem. Pharmacol. 66:2003;2397-2407
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 2397-2407
    • Huen, M.S.1    Hui, K.M.2    Leung, J.W.3    Sigel, E.4    Baur, R.5    Wong, J.T.6    Xue, H.7
  • 66
    • 0037379314 scopus 로고    scopus 로고
    • Bioenergetic approaches for neuroprotection in Parkinson's disease
    • (discussion S47-48)
    • Beal M.F. Bioenergetic approaches for neuroprotection in Parkinson's disease. Ann. Neurol. 53(Suppl. 3):2003;S39-S47. (discussion S47-48)
    • (2003) Ann. Neurol. , vol.53 , Issue.SUPPL. 3 , pp. 39-S47
    • Beal, M.F.1
  • 68
    • 0035671397 scopus 로고    scopus 로고
    • Effects of epigallocatechin-3-gallate on growth, epidermal growth factor receptor signaling pathways, gene expression, and chemosensitivity in human head and neck squamous cell carcinoma cell lines
    • Masuda M., Suzui M., Weinstein I.B. Effects of epigallocatechin-3-gallate on growth, epidermal growth factor receptor signaling pathways, gene expression, and chemosensitivity in human head and neck squamous cell carcinoma cell lines. Clin. Cancer Res. 7:2001;4220-4229
    • (2001) Clin. Cancer Res. , vol.7 , pp. 4220-4229
    • Masuda, M.1    Suzui, M.2    Weinstein, I.B.3
  • 69
    • 0043067996 scopus 로고    scopus 로고
    • Role of p53 and NF-kappaB in epigallocatechin-3-gallate-induced apoptosis of LNCaP cells
    • Hastak K., Gupta S., Ahmad N., Agarwal M.K., Agarwal M.L., Mukhtar H. Role of p53 and NF-kappaB in epigallocatechin-3-gallate-induced apoptosis of LNCaP cells. Oncogene. 22:2003;4851-4859
    • (2003) Oncogene , vol.22 , pp. 4851-4859
    • Hastak, K.1    Gupta, S.2    Ahmad, N.3    Agarwal, M.K.4    Agarwal, M.L.5    Mukhtar, H.6
  • 70
    • 0037387944 scopus 로고    scopus 로고
    • Green tea polyphenol epigallocatechin-3 gallate induces apoptosis of proliferating vascular smooth muscle cells via activation of p53
    • Hofmann C.S., Sonenshein G.E. Green tea polyphenol epigallocatechin-3 gallate induces apoptosis of proliferating vascular smooth muscle cells via activation of p53. FASEB J. 17:2003;702-704
    • (2003) FASEB J. , vol.17 , pp. 702-704
    • Hofmann, C.S.1    Sonenshein, G.E.2
  • 71
    • 0030792007 scopus 로고    scopus 로고
    • Positioning atypical protein kinase C isoforms in the UV-induced apoptotic signaling cascade
    • Berra E., Municio M.M., Sanz L., Frutos S., Diaz-Meco M.T., Moscat J. Positioning atypical protein kinase C isoforms in the UV-induced apoptotic signaling cascade. Mol. Cell. Biol. 17:1997;4346-4354
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4346-4354
    • Berra, E.1    Municio, M.M.2    Sanz, L.3    Frutos, S.4    Diaz-Meco, M.T.5    Moscat, J.6
  • 72
    • 0031786125 scopus 로고    scopus 로고
    • The sevenfold way of PKC regulation
    • Liu W.S., Heckman C.A. The sevenfold way of PKC regulation. Cell Signalling. 10:1998;529-542
    • (1998) Cell Signalling , vol.10 , pp. 529-542
    • Liu, W.S.1    Heckman, C.A.2
  • 74
    • 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. 21:2001;2929-2938
    • (2001) J. Neurosci. , vol.21 , pp. 2929-2938
    • Maher, P.1
  • 75
    • 0037345781 scopus 로고    scopus 로고
    • Estrogen activates protein kinase C in neurons: Role in neuroprotection
    • Cordey M., Gundimeda U., Gopalakrishna R., Pike C.J. Estrogen activates protein kinase C in neurons: role in neuroprotection. J. Neurochem. 84:2003;1340-1348
    • (2003) J. Neurochem. , vol.84 , pp. 1340-1348
    • Cordey, M.1    Gundimeda, U.2    Gopalakrishna, R.3    Pike, C.J.4
  • 76
    • 0345356539 scopus 로고    scopus 로고
    • Opposing roles of delta and epsilonPKC in cardiac ischemia and reperfusion: Targeting the apoptotic machinery
    • Murriel C.L., Mochly-Rosen D. Opposing roles of delta and epsilonPKC in cardiac ischemia and reperfusion: targeting the apoptotic machinery. Arch. Biochem. Biophys. 420:2003;246-254
    • (2003) Arch. Biochem. Biophys. , vol.420 , pp. 246-254
    • Murriel, C.L.1    Mochly-Rosen, D.2
  • 77
    • 0032566717 scopus 로고    scopus 로고
    • A functional role for mitochondrial protein kinase Calpha in Bcl2 phosphorylation and suppression of apoptosis
    • Ruvolo P.P., Deng X., Carr B.K., May W.S. A functional role for mitochondrial protein kinase Calpha in Bcl2 phosphorylation and suppression of apoptosis. J. Biol. Chem. 273:1998;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
  • 78
    • 0032007292 scopus 로고    scopus 로고
    • Overexpression of protein kinase C isoform epsilon but not delta in human interleukin-3-dependent cells suppresses apoptosis and induces bcl-2 expression
    • Gubina E., Rinaudo M.S., Szallasi Z., Blumberg P.M., Mufson R.A. Overexpression of protein kinase C isoform epsilon but not delta in human interleukin-3-dependent cells suppresses apoptosis and induces bcl-2 expression. Blood. 91:1998;823-829
    • (1998) Blood , vol.91 , pp. 823-829
    • Gubina, E.1    Rinaudo, M.S.2    Szallasi, Z.3    Blumberg, P.M.4    Mufson, R.A.5
  • 79
    • 0032537024 scopus 로고    scopus 로고
    • Loss of protein kinase C function induces an apoptotic response
    • Whelan R.D., Parker P.J. Loss of protein kinase C function induces an apoptotic response. Oncogene. 16:1998;1939-1944
    • (1998) Oncogene , vol.16 , pp. 1939-1944
    • Whelan, R.D.1    Parker, P.J.2
  • 80
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Xia Z., Dickens M., Raingeaud J., Davis R.J., Greenberg M.E. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science. 270:1995;1326-1331
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 81
    • 0033118665 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase pathway mediates estrogen neuroprotection after glutamate toxicity in primary cortical neurons
    • Singer C.A., Figueroa-Masot X.A., Batchelor R.H., Dorsa D.M. The mitogen-activated protein kinase pathway mediates estrogen neuroprotection after glutamate toxicity in primary cortical neurons. J. Neurosci. 19:1999;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
  • 82
    • 0034044227 scopus 로고    scopus 로고
    • Neurotrophin signal transduction in the nervous system
    • Kaplan D.R., Miller F.D. Neurotrophin signal transduction in the nervous system. Curr. Opin. Neurol. 10:2000;381-391
    • (2000) Curr. Opin. Neurol. , vol.10 , pp. 381-391
    • Kaplan, D.R.1    Miller, F.D.2
  • 83
    • 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. 20:2000;2-8
    • (2000) J. Neurosci. , vol.20 , pp. 2-8
    • Kermer, P.1    Klocker, N.2    Labes, M.3    Bahr, M.4
  • 84
    • 0037315101 scopus 로고    scopus 로고
    • Essential role for integrin linked kinase in Akt-mediated integrin survival signaling in hippocampal neurons
    • Gary D.S., Milhavet O., Camandola S., Mattson M.P. Essential role for integrin linked kinase in Akt-mediated integrin survival signaling in hippocampal neurons. J. Neurochem. 84:2003;878-890
    • (2003) J. Neurochem. , vol.84 , pp. 878-890
    • Gary, D.S.1    Milhavet, O.2    Camandola, S.3    Mattson, M.P.4
  • 85
    • 0037205044 scopus 로고    scopus 로고
    • Signaling pathways for PC12 cell differentiation: Making the right connections
    • Vaudry D., Stork P.J., Lazarovici P., Eiden L.E. Signaling pathways for PC12 cell differentiation: making the right connections. Science. 296:2002;1648-1649
    • (2002) Science , vol.296 , pp. 1648-1649
    • Vaudry, D.1    Stork, P.J.2    Lazarovici, P.3    Eiden, L.E.4
  • 86
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson G.L., Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science. 298:2002;1911-1912
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 89
    • 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. 287:2000;191-194
    • (2000) Neurosci. Lett. , vol.287 , pp. 191-194
    • Lee, S.1    Suh, S.2    Kim, S.3
  • 90
    • 0036902931 scopus 로고    scopus 로고
    • Feeding rats diets enriched in lowbush blueberries for six weeks decreases ischemia-induced brain damage
    • Sweeney M.I., Kalt W., MacKinnon S.L., Ashby J., Gottschall-Pass K.T. Feeding rats diets enriched in lowbush blueberries for six weeks decreases ischemia-induced brain damage. Nat. Neurosci. 5:2002;427-431
    • (2002) Nat. Neurosci. , vol.5 , pp. 427-431
    • Sweeney, M.I.1    Kalt, W.2    MacKinnon, S.L.3    Ashby, J.4    Gottschall-Pass, K.T.5
  • 91
    • 0242432638 scopus 로고    scopus 로고
    • Effects of green tea polyphenols on dopamine uptake and on MPP+-induced dopamine neuron injury
    • Pan T., Fei J., Zhou X., Jankovic J., Le W. Effects of green tea polyphenols on dopamine uptake and on MPP+-induced dopamine neuron injury. Life Sci. 72:2003;1073-1083
    • (2003) Life Sci. , vol.72 , pp. 1073-1083
    • Pan, T.1    Fei, J.2    Zhou, X.3    Jankovic, J.4    Le, W.5
  • 92
    • 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 C.S. Enzymology of methylation of tea catechins and inhibition of catechol-O-methyltransferase by (-)-epigallocatechin gallate. Drug Metab. Dispos. 31:2003;572-579
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 572-579
    • Lu, H.1    Meng, X.2    Yang, C.S.3
  • 93
    • 0036093898 scopus 로고    scopus 로고
    • Clinical pharmacokinetic and pharmacodynamic properties of drugs used in the treatment of Parkinson's disease
    • Deleu D., Northway M.G., Hanssens Y. Clinical pharmacokinetic and pharmacodynamic properties of drugs used in the treatment of Parkinson's disease. Clin. Pharmacokinet. 41:2002;261-309
    • (2002) Clin. Pharmacokinet. , vol.41 , pp. 261-309
    • Deleu, D.1    Northway, M.G.2    Hanssens, Y.3
  • 95
    • 0034125340 scopus 로고    scopus 로고
    • A 26-week analysis of a double-blind, placebo-controlled trial of the ginkgo biloba extract EGb 761 in dementia
    • Le Bars P.L., Kieser M., Itil K.Z. A 26-week analysis of a double-blind, placebo-controlled trial of the ginkgo biloba extract EGb 761 in dementia. Dement. Geriatr. Cognit. Disord. 11:2000;230-237
    • (2000) Dement. Geriatr. Cognit. Disord. , vol.11 , pp. 230-237
    • Le Bars, P.L.1    Kieser, M.2    Itil, K.Z.3
  • 97
    • 0033765735 scopus 로고    scopus 로고
    • Oxidative injury in diseases of the central nervous system: Focus on Alzheimer's disease
    • Pratico D., Delanty N. Oxidative injury in diseases of the central nervous system: focus on Alzheimer's disease. Am. J. Med. 109:2000;577-585
    • (2000) Am. J. Med. , vol.109 , pp. 577-585
    • Pratico, D.1    Delanty, N.2
  • 98
    • 0041884769 scopus 로고    scopus 로고
    • Protective effect of flavonoids against aging- and lipopolysaccharide- induced cognitive impairment in mice
    • Patil C.S., Singh V.P., Satyanarayan P.S., Jain N.K., Singh A., Kulkarni S.K. Protective effect of flavonoids against aging- and lipopolysaccharide- induced cognitive impairment in mice. Pharmacology. 69:2003;59-67
    • (2003) Pharmacology , vol.69 , pp. 59-67
    • Patil, C.S.1    Singh, V.P.2    Satyanarayan, P.S.3    Jain, N.K.4    Singh, A.5    Kulkarni, S.K.6
  • 99
    • 0141749421 scopus 로고    scopus 로고
    • Neuroprotective effects of Ginkgo biloba extract
    • Ahlemeyer B., Krieglstein J. Neuroprotective effects of Ginkgo biloba extract. Cell. Mol. Life Sci. 60:2003;1779-1792
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1779-1792
    • Ahlemeyer, B.1    Krieglstein, J.2
  • 100
    • 0036233802 scopus 로고    scopus 로고
    • Fruit polyphenolics and brain aging: Nutritional interventions targeting age-related neuronal and behavioral deficits
    • Galli R.L., Shukitt-Hale B., Youdim K.A., Joseph J.A. Fruit polyphenolics and brain aging: nutritional interventions targeting age-related neuronal and behavioral deficits. Ann. N. Y. Acad. Sci. 959:2002;128-132
    • (2002) Ann. N. Y. Acad. Sci. , vol.959 , pp. 128-132
    • Galli, R.L.1    Shukitt-Hale, B.2    Youdim, K.A.3    Joseph, J.A.4
  • 101
    • 0035868503 scopus 로고    scopus 로고
    • A possible emerging role of phytochemicals in improving age-related neurological dysfunctions: A multiplicity of effects
    • Youdim K.A., Joseph J.A. A possible emerging role of phytochemicals in improving age-related neurological dysfunctions: a multiplicity of effects. Free Radic. Biol. Med. 30:2001;583-594
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 583-594
    • Youdim, K.A.1    Joseph, J.A.2
  • 102
    • 0030983324 scopus 로고    scopus 로고
    • Effect of "beta CATECHIN" on the life span of senescence accelerated mice (SAM-P8 strain)
    • Kumari M.V., Yoneda T., Hiramatsu M. Effect of "beta CATECHIN" on the life span of senescence accelerated mice (SAM-P8 strain). Biochem. Mol. Biol. Int. 41:1997;1005-1011
    • (1997) Biochem. Mol. Biol. Int. , vol.41 , pp. 1005-1011
    • Kumari, M.V.1    Yoneda, T.2    Hiramatsu, M.3
  • 103
    • 0033568849 scopus 로고    scopus 로고
    • Reversals of age-related declines in neuronal signal transduction, cognitive, and motor behavioral deficits with blueberry, spinach, or strawberry dietary supplementation
    • Joseph J.A., Shukitt-Hale B., Denisova N.A., Bielinski D., Martin A., McEwen J.J., Bickford P.C. Reversals of age-related declines in neuronal signal transduction, cognitive, and motor behavioral deficits with blueberry, spinach, or strawberry dietary supplementation. J. Neurosci. 19:1999;8114-8121
    • (1999) J. Neurosci. , vol.19 , pp. 8114-8121
    • Joseph, J.A.1    Shukitt-Hale, B.2    Denisova, N.A.3    Bielinski, D.4    Martin, A.5    McEwen, J.J.6    Bickford, P.C.7
  • 105
    • 0344826082 scopus 로고    scopus 로고
    • Prevention of age-related spatial memory deficits in a transgenic mouse model of Alzheimer's disease by chronic Ginkgo biloba treatment
    • Stackman R.W., Eckenstein F., Frei B., Kulhanek D., Nowlin J., Quinn J.F. Prevention of age-related spatial memory deficits in a transgenic mouse model of Alzheimer's disease by chronic Ginkgo biloba treatment. Exp. Neurol. 184:2003;510-520
    • (2003) Exp. Neurol. , vol.184 , pp. 510-520
    • Stackman, R.W.1    Eckenstein, F.2    Frei, B.3    Kulhanek, D.4    Nowlin, J.5    Quinn, J.F.6
  • 106
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • Bush A.I. The metallobiology of Alzheimer's disease. Trends Neurosci. 26:2003;207-214
    • (2003) Trends Neurosci. , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 107
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid beta protein and the genetics of Alzheimer's disease
    • Selkoe D.J. Amyloid beta protein and the genetics of Alzheimer's disease. J. Biol. Chem. 271:1996;18295-18298
    • (1996) J. Biol. Chem. , vol.271 , pp. 18295-18298
    • Selkoe, D.J.1
  • 108
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease
    • Selkoe D.J. The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease. Trends Cell. Biol. 8:1998;447-453
    • (1998) Trends Cell. Biol. , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 109
    • 0032960305 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein cleavage
    • Mills J., Reiner P.B. Regulation of amyloid precursor protein cleavage. J. Neurochem. 72:1999;443-460
    • (1999) J. Neurochem. , vol.72 , pp. 443-460
    • Mills, J.1    Reiner, P.B.2
  • 111
    • 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. 96:1999;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
  • 112
    • 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 D.H., Nurcombe V., Reed G., Clarris H., Moir R., Beyreuther K., Masters C.L. A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth. J. Neurosci. 14:1994;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
  • 113
    • 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. 51:1998;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
  • 114
    • 0033022170 scopus 로고    scopus 로고
    • Proteolysis by presenilins and the renaissance of tau
    • Haass C., Mandelkow E. Proteolysis by presenilins and the renaissance of tau. Trends Cell. Biol. 9:1999;241-244
    • (1999) Trends Cell. Biol. , vol.9 , pp. 241-244
    • Haass, C.1    Mandelkow, E.2
  • 118
    • 0037200076 scopus 로고    scopus 로고
    • Non-steroidal anti-inflammatory drugs stimulate secretion of non-amyloidogenic precursor protein
    • Avramovich Y., Amit T., Youdim M.B. Non-steroidal anti-inflammatory drugs stimulate secretion of non-amyloidogenic precursor protein. J. Biol. Chem. 277:2002;31466-31473
    • (2002) J. Biol. Chem. , vol.277 , pp. 31466-31473
    • Avramovich, Y.1    Amit, T.2    Youdim, M.B.3
  • 119
    • 0642303109 scopus 로고    scopus 로고
    • The importance of propargylamine moiety in the anti-Parkinson drug rasagiline and its derivatives in MAPK-dependent amyloid precursor protein processing
    • Yogev-Falach M., Amit T., Bar-Am O., Youdim M.B. The importance of propargylamine moiety in the anti-Parkinson drug rasagiline and its derivatives in MAPK-dependent amyloid precursor protein processing. FASEB J. 17:2003;2325-2327
    • (2003) FASEB J. , vol.17 , pp. 2325-2327
    • Yogev-Falach, M.1    Amit, T.2    Bar-Am, O.3    Youdim, M.B.4
  • 123
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner B.A., Duffy L.K., Kirschner D.A. Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides. Science. 250:1990;279-282
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 124
    • 0029837577 scopus 로고    scopus 로고
    • Physiologic levels of beta-amyloid activate phosphatidylinositol 3-kinase with the involvement of tyrosine phosphorylation
    • Luo Y., Sunderland T., Wolozin B. Physiologic levels of beta-amyloid activate phosphatidylinositol 3-kinase with the involvement of tyrosine phosphorylation. J. Neurochem. 67:1996;978-987
    • (1996) J. Neurochem. , vol.67 , pp. 978-987
    • Luo, Y.1    Sunderland, T.2    Wolozin, B.3
  • 126
    • 0002639884 scopus 로고    scopus 로고
    • Dosing in phase II trial of Alzheimer's vaccine suspended
    • Senior K. Dosing in phase II trial of Alzheimer's vaccine suspended. Lancet Neurol. 1:2002;3
    • (2002) Lancet Neurol. , vol.1 , pp. 3
    • Senior, K.1
  • 127
    • 0038222577 scopus 로고    scopus 로고
    • Ethanol plus caffeine (caffeinol) for treatment of ischemic stroke: Preclinical experience
    • Aronowski J., Strong R., Shirzadi A., Grotta J.C. Ethanol plus caffeine (caffeinol) for treatment of ischemic stroke: preclinical experience. Stroke. 34:2003;1246-1251
    • (2003) Stroke , vol.34 , pp. 1246-1251
    • Aronowski, J.1    Strong, R.2    Shirzadi, A.3    Grotta, J.C.4
  • 128
    • 0037405378 scopus 로고    scopus 로고
    • Synergistic effects of melatonin and deprenyl against MPTP-induced mitochondrial damage and DA depletion
    • Khaldy H., Escames G., Leon J., Bikjdaouene L., Acuna-Castroviejo D. Synergistic effects of melatonin and deprenyl against MPTP-induced mitochondrial damage and DA depletion. Neurobiol. Aging. 24:2003;491-500
    • (2003) Neurobiol. Aging , vol.24 , pp. 491-500
    • Khaldy, H.1    Escames, G.2    Leon, J.3    Bikjdaouene, L.4    Acuna-Castroviejo, D.5
  • 129
    • 0142195765 scopus 로고    scopus 로고
    • Synergistic protection of PC12 cells from beta-amyloid toxicity by resveratrol and catechin
    • Conte A., Pellegrini S., Tagliazucchi D. Synergistic protection of PC12 cells from beta-amyloid toxicity by resveratrol and catechin. Brain Res. Bull. 62:2003;29-38
    • (2003) Brain Res. Bull. , vol.62 , pp. 29-38
    • Conte, A.1    Pellegrini, S.2    Tagliazucchi, D.3
  • 130
    • 0038779336 scopus 로고    scopus 로고
    • Neuroprotective, anti-apoptotic effects of apomorphine
    • Kyriazis M. Neuroprotective, anti-apoptotic effects of apomorphine. J. Anti Aging Med. 6:2003;21-28
    • (2003) J. Anti Aging Med. , vol.6 , pp. 21-28
    • Kyriazis, M.1
  • 134
    • 0033143452 scopus 로고    scopus 로고
    • Identification of the major antioxidative metabolites in biological fluids of the rat with ingested (+)-catechin and (-)-epicatechin
    • Harada M., Kan Y., Naoki H., Fukui Y., Kageyama N., Nakai M., Miki W., Kiso Y. Identification of the major antioxidative metabolites in biological fluids of the rat with ingested (+)-catechin and (-)-epicatechin. Biosci. Biotechnol. Biochem. 63:1999;973-977
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 973-977
    • Harada, M.1    Kan, Y.2    Naoki, H.3    Fukui, Y.4    Kageyama, N.5    Nakai, M.6    Miki, W.7    Kiso, Y.8
  • 135
    • 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 J.P., Schroeter H., Kuhnle G., Srai S.K., Tyrrell R.M., 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. 354:2001;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


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