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Volumn , Issue , 2010, Pages

Effects of various flavonoids on the -synuclein fibrillation process

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; ANTHRAQUINONE DERIVATIVE; APIGENIN; CATECHIN; CHRYSOERIOL; DIOSMETIN; EMODIN; ERIODICTYOL; FLAVANONE; FLAVONOID; FLAVONOL; GENISTEIN; HESPERETIN; HOMOERIODICTYOL; ISOFLAVONE; ISORHAMNETIN; LUTEOLIN; MYRICETIN; QUERCETIN; TAMARIXETIN; UNCLASSIFIED DRUG; WOGONIN;

EID: 77955946838     PISSN: None     EISSN: 20420080     Source Type: Journal    
DOI: 10.4061/2010/650794     Document Type: Article
Times cited : (95)

References (79)
  • 1
    • 0031013848 scopus 로고    scopus 로고
    • Prevalence of parkinsonism and Parkinsons disease in Europe: The EUROPARKINSON Collaborative Study. European Community Concerted Action on the Epidemiology of Parkinsons disease
    • de Rijk M. C., Tzourio C., Breteler M. M., Prevalence of parkinsonism and Parkinsons disease in Europe: the EUROPARKINSON Collaborative Study. European Community Concerted Action on the Epidemiology of Parkinsons disease Journal of Neurology, Neurosurgery Psychiatry 1997 62 1 10 15
    • (1997) Journal of Neurology, Neurosurgery Psychiatry , vol.62 , Issue.1 , pp. 10-15
    • De Rijk, M.C.1    Tzourio, C.2    Breteler, M.M.3
  • 2
    • 0040368216 scopus 로고    scopus 로고
    • Prospects for new restorative and neuroprotective treatments in Parkinsons disease
    • Dunnett S. B., Bjorklund A., Prospects for new restorative and neuroprotective treatments in Parkinsons disease Nature 1999 399 A32 A39
    • (1999) Nature , vol.399
    • Dunnett, S.B.1    Bjorklund, A.2
  • 6
    • 0345119026 scopus 로고    scopus 로고
    • Caught in the act: Synuclein is the culprit in Parkinsons disease
    • Eriksen J. L., Dawson T. M., Dickson D. W., Petrucelli L., Caught in the act: -synuclein is the culprit in Parkinsons disease Neuron 2003 40 3 453 456
    • (2003) Neuron , vol.40 , Issue.3 , pp. 453-456
    • Eriksen, J.L.1    Dawson, T.M.2    Dickson, D.W.3    Petrucelli, L.4
  • 7
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimers disease
    • Selkoe D. J., Translating cell biology into therapeutic advances in Alzheimers disease Nature 1999 399 A23 A31
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 9
    • 0038727850 scopus 로고    scopus 로고
    • Parkinsons disease and related -synucleinopathies are brain amyloidoses
    • Trojanowski J. Q., Lee V. M., Parkinsons disease and related -synucleinopathies are brain amyloidoses Annals of the New York Academy of Sciences 2003 991 107 110
    • (2003) Annals of the New York Academy of Sciences , vol.991 , pp. 107-110
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 10
    • 0038460184 scopus 로고    scopus 로고
    • Part II: Synuclein and its molecular pathophysiological role in neurodegenerative disease
    • Dev K. K., Hofele K., Barbieri S., Buchman V. L., van der Putten H., Part II: -synuclein and its molecular pathophysiological role in neurodegenerative disease Neuropharmacology 2003 45 1 14 44
    • (2003) Neuropharmacology , vol.45 , Issue.1 , pp. 14-44
    • Dev, K.K.1    Hofele, K.2    Barbieri, S.3    Buchman, V.L.4    Van Der Putten, H.5
  • 11
    • 34548620297 scopus 로고    scopus 로고
    • Neuropathology, biochemistry, and biophysics of -synuclein aggregation
    • Uversky V. N., Neuropathology, biochemistry, and biophysics of -synuclein aggregation Journal of Neurochemistry 2007 103 1 17 37
    • (2007) Journal of Neurochemistry , vol.103 , Issue.1 , pp. 17-37
    • Uversky, V.N.1
  • 12
    • 0032584686 scopus 로고    scopus 로고
    • Filamentous -synuclein inclusions link multiple system atrophy with Parkinsons disease and dementia with Lewy bodies
    • Spillantini M. G., Crowther R. A., Jakes R., Cairns N. J., Lantos P. L., Goedert M., Filamentous -synuclein inclusions link multiple system atrophy with Parkinsons disease and dementia with Lewy bodies Neuroscience Letters 1998 251 3 205 208
    • (1998) Neuroscience Letters , vol.251 , Issue.3 , pp. 205-208
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Cairns, N.J.4    Lantos, P.L.5    Goedert, M.6
  • 14
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the -synuclein gene identified in families with Parkinsons disease
    • Polymeropoulos M. H., Lavedan C., Leroy E., Mutation in the -synuclein gene identified in families with Parkinsons disease Science 1997 276 5321 2045 2047
    • (1997) Science , vol.276 , Issue.5321 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3
  • 15
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding -synuclein in Parkinsons disease
    • Kruger R., Kuhn W., Muller T., Ala30Pro mutation in the gene encoding -synuclein in Parkinsons disease Nature Genetics 1998 18 2 106 108
    • (1998) Nature Genetics , vol.18 , Issue.2 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3
  • 16
    • 10744230149 scopus 로고    scopus 로고
    • The new mutation, E46K, of -synuclein causes Parkinson and Lewy body dementia
    • Zarranz J. J., Alegre J., Gmez-Esteban J. C., The new mutation, E46K, of -synuclein causes Parkinson and Lewy body dementia Annals of Neurology 2004 55 2 164 173
    • (2004) Annals of Neurology , vol.55 , Issue.2 , pp. 164-173
    • Zarranz, J.J.1    Alegre, J.2    Gmez-Esteban, J.C.3
  • 18
    • 0035949542 scopus 로고    scopus 로고
    • Effect of familial Parkinsons disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human -synuclein
    • Li J., Uversky V. N., Fink A. L., Effect of familial Parkinsons disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human -synuclein Biochemistry 2001 40 38 11604 11613
    • (2001) Biochemistry , vol.40 , Issue.38 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 19
    • 4644290985 scopus 로고    scopus 로고
    • Synuclein locus duplication as a cause of familial Parkinsons disease
    • Chartier-Harlin M. C., Kachergus J., Roumier C., -synuclein locus duplication as a cause of familial Parkinsons disease The Lancet 2004 364 9440 1167 1169
    • (2004) The Lancet , vol.364 , Issue.9440 , pp. 1167-1169
    • Chartier-Harlin, M.C.1    Kachergus, J.2    Roumier, C.3
  • 20
    • 0242300619 scopus 로고    scopus 로고
    • Synuclein locus triplication causes Parkinsons disease
    • Singleton A. B., Farrer M., Johnson J., -synuclein locus triplication causes Parkinsons disease Science 2003 302 5646 841
    • (2003) Science , vol.302 , Issue.5646 , pp. 841
    • Singleton, A.B.1    Farrer, M.2    Johnson, J.3
  • 21
    • 0038386274 scopus 로고    scopus 로고
    • Zeroing in on the pathogenic form of -synuclein and its mechanism of neurotoxicity in Parkinsons disease
    • Volles M. J., Lansbury P. T. Jr., Zeroing in on the pathogenic form of -synuclein and its mechanism of neurotoxicity in Parkinsons disease Biochemistry 2003 42 26 7871 7878
    • (2003) Biochemistry , vol.42 , Issue.26 , pp. 7871-7878
    • Volles, M.J.1    Lansbury Jr., P.T.2
  • 22
    • 0036415838 scopus 로고    scopus 로고
    • Synuclein, especially the parkinsons disease-associated mutants, forms pore-like annular and tubular protofibrils
    • Lashuel H. A., Petre B. M., Wall J., -synuclein, especially the parkinsons disease-associated mutants, forms pore-like annular and tubular protofibrils Journal of Molecular Biology 2002 322 5 1089 1102
    • (2002) Journal of Molecular Biology , vol.322 , Issue.5 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3
  • 23
    • 0037046163 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar -synuclein is sensitive to Parkinsons disease-linked mutations and occurs by a pore-like mechanism
    • Volles M. J., Lansbury P. T. Jr., Vesicle permeabilization by protofibrillar -synuclein is sensitive to Parkinsons disease-linked mutations and occurs by a pore-like mechanism Biochemistry 2002 41 14 4595 4602
    • (2002) Biochemistry , vol.41 , Issue.14 , pp. 4595-4602
    • Volles, M.J.1    Lansbury Jr., P.T.2
  • 24
    • 0037072284 scopus 로고    scopus 로고
    • Annular -synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes
    • Ding T. T., Lee S. J., Rochet J. C., Lansbury P. T. Jr., Annular -synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes Biochemistry 2002 41 32 10209 10217
    • (2002) Biochemistry , vol.41 , Issue.32 , pp. 10209-10217
    • Ding, T.T.1    Lee, S.J.2    Rochet, J.C.3    Lansbury Jr., P.T.4
  • 25
    • 0037167613 scopus 로고    scopus 로고
    • Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes
    • Anguiano M., Nowak R. J., Lansbury P. T. Jr., Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes Biochemistry 2002 41 38 11338 11343
    • (2002) Biochemistry , vol.41 , Issue.38 , pp. 11338-11343
    • Anguiano, M.1    Nowak, R.J.2    Lansbury Jr., P.T.3
  • 26
    • 1242269712 scopus 로고    scopus 로고
    • Architecture of the Alzheimers A P ion channel pore
    • Arispe N., Architecture of the Alzheimers A P ion channel pore Journal of Membrane Biology 2004 197 1 33 48
    • (2004) Journal of Membrane Biology , vol.197 , Issue.1 , pp. 33-48
    • Arispe, N.1
  • 27
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro A., Mina E., Kayed R., Milton S. C., Parker I., Glabe C. G., Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers Journal of Biological Chemistry 2005 280 17 17294 17300
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 28
    • 4444292588 scopus 로고    scopus 로고
    • Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide
    • Green J. D., Kreplak L., Goldsbury C., Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide Journal of Molecular Biology 2004 342 3 877 887
    • (2004) Journal of Molecular Biology , vol.342 , Issue.3 , pp. 877-887
    • Green, J.D.1    Kreplak, L.2    Goldsbury, C.3
  • 29
    • 0034718206 scopus 로고    scopus 로고
    • Approaches to discovery and characterization of inhibitors of amyloid -peptide polymerization
    • Findeis M. A., Approaches to discovery and characterization of inhibitors of amyloid -peptide polymerization Biochimica et Biophysica Acta 2000 1502 1 76 84
    • (2000) Biochimica et Biophysica Acta , vol.1502 , Issue.1 , pp. 76-84
    • Findeis, M.A.1
  • 32
    • 13544251748 scopus 로고    scopus 로고
    • Anthraquinones inhibit tau aggregation and dissolve Alzheimers paired helical filaments in vitro and in cells
    • Pickhardt M., Gazova Z., von Bergen M., Anthraquinones inhibit tau aggregation and dissolve Alzheimers paired helical filaments in vitro and in cells Journal of Biological Chemistry 2005 280 5 3628 3635
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.5 , pp. 3628-3635
    • Pickhardt, M.1    Gazova, Z.2    Von Bergen, M.3
  • 33
    • 14844303721 scopus 로고    scopus 로고
    • Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins
    • Taniguchi S., Suzuki N., Masuda M., Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins Journal of Biological Chemistry 2005 280 9 7614 7623
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.9 , pp. 7614-7623
    • Taniguchi, S.1    Suzuki, N.2    Masuda, M.3
  • 34
    • 0033859612 scopus 로고    scopus 로고
    • Flavonoids as antioxidants
    • Pietta P. G., Flavonoids as antioxidants Journal of Natural Products 2000 63 7 1035 1042
    • (2000) Journal of Natural Products , vol.63 , Issue.7 , pp. 1035-1042
    • Pietta, P.G.1
  • 35
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism
    • Porat Y., Abramowitz A., Gazit E., Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism Chemical Biology and Drug Design 2006 67 1 27 37
    • (2006) Chemical Biology and Drug Design , vol.67 , Issue.1 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 36
    • 3042547187 scopus 로고    scopus 로고
    • The flavonoid baicalein inhibits fibrillation of -synuclein and disaggregates existing fibrils
    • Zhu M., Rajamani S., Kaylor J., Han S., Zhou F., Fink A. L., The flavonoid baicalein inhibits fibrillation of -synuclein and disaggregates existing fibrils Journal of Biological Chemistry 2004 279 26 26846 26857
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 26846-26857
    • Zhu, M.1    Rajamani, S.2    Kaylor, J.3    Han, S.4    Zhou, F.5    Fink, A.L.6
  • 37
    • 8844224948 scopus 로고    scopus 로고
    • Rifampicin inhibits -synuclein fibrillation and disaggregates fibrils
    • Li J., Zhu M., Rajamani S., Uversky V. N., Fink A. L., Rifampicin inhibits -synuclein fibrillation and disaggregates fibrils Chemical Biology 2004 11 11 1513 1521
    • (2004) Chemical Biology , vol.11 , Issue.11 , pp. 1513-1521
    • Li, J.1    Zhu, M.2    Rajamani, S.3    Uversky, V.N.4    Fink, A.L.5
  • 38
    • 52049098478 scopus 로고    scopus 로고
    • Structural characteristics of the -synuclein oligomers stabilized by the flavonoid baicalein
    • Hong D.-P., Fink A. L., Uversky V. N., Structural characteristics of the -synuclein oligomers stabilized by the flavonoid baicalein Journal of Molecular Biology 2008 383 1 214 223
    • (2008) Journal of Molecular Biology , vol.383 , Issue.1 , pp. 214-223
    • Hong, D.-P.1    Fink, A.L.2    Uversky, V.N.3
  • 39
    • 0033637140 scopus 로고    scopus 로고
    • The effects of plant flavonoids on mammalian cells: Implications for inflammation, heart disease, and cancer
    • Middleton E. Jr., Kandaswami C., Theoharides T. C., The effects of plant flavonoids on mammalian cells: implications for inflammation, heart disease, and cancer Pharmacological Reviews 2000 52 4 673 751
    • (2000) Pharmacological Reviews , vol.52 , Issue.4 , pp. 673-751
    • Middleton Jr., E.1    Kandaswami, C.2    Theoharides, T.C.3
  • 40
    • 0000531523 scopus 로고
    • The antioxidants of higher plants
    • Larson R. A., The antioxidants of higher plants Phytochemistry 1988 27 4 969 978
    • (1988) Phytochemistry , vol.27 , Issue.4 , pp. 969-978
    • Larson, R.A.1
  • 41
    • 24644495344 scopus 로고    scopus 로고
    • Reduction potentials of flavonoid and model phenoxyl radicals. Which ring in flavonoids is responsible for antioxidant activity?
    • Jovanovic S. V., Steenken S., Hara Y., Simic M. G., Reduction potentials of flavonoid and model phenoxyl radicals. Which ring in flavonoids is responsible for antioxidant activity? Journal of the Chemical Society, Perkin Transactions 1996 2 2497 2504
    • (1996) Journal of the Chemical Society, Perkin Transactions , vol.2 , pp. 2497-2504
    • Jovanovic, S.V.1    Steenken, S.2    Hara, Y.3    Simic, M.G.4
  • 42
    • 0027251053 scopus 로고
    • The pecking order of free radicals and antioxidants: Lipid peroxidation, -tocopherol, and ascorbate
    • Buettner G. R., The pecking order of free radicals and antioxidants: lipid peroxidation, -tocopherol, and ascorbate Archives of Biochemistry and Biophysics 1993 300 2 535 543
    • (1993) Archives of Biochemistry and Biophysics , vol.300 , Issue.2 , pp. 535-543
    • Buettner, G.R.1
  • 43
    • 0023864255 scopus 로고
    • Flavonoids are scavengers of superoxide anions
    • Robak J., Gryglewski R. J., Flavonoids are scavengers of superoxide anions Biochemical Pharmacology 1988 37 5 837 841
    • (1988) Biochemical Pharmacology , vol.37 , Issue.5 , pp. 837-841
    • Robak, J.1    Gryglewski, R.J.2
  • 44
    • 0009538299 scopus 로고
    • Hydroxyl radical scavenging activity of flavonoids
    • Husain S. R., Cillard J., Cillard P., Hydroxyl radical scavenging activity of flavonoids Phytochemistry 1987 26 9 2489 2491
    • (1987) Phytochemistry , vol.26 , Issue.9 , pp. 2489-2491
    • Husain, S.R.1    Cillard, J.2    Cillard, P.3
  • 45
    • 46149138568 scopus 로고
    • Antioxidant activity of flavonoids and reactivity with peroxy radical
    • Torel J., Cillard J., Cillard P., Antioxidant activity of flavonoids and reactivity with peroxy radical Phytochemistry 1986 25 2 383 385
    • (1986) Phytochemistry , vol.25 , Issue.2 , pp. 383-385
    • Torel, J.1    Cillard, J.2    Cillard, P.3
  • 46
    • 0034079862 scopus 로고    scopus 로고
    • Free radicals and antioxidants in the year 2000. A historical look to the future
    • Gutteridge J. M., Halliwell B., Free radicals and antioxidants in the year 2000. A historical look to the future Annals of the New York Academy of Sciences 2000 899 136 147
    • (2000) Annals of the New York Academy of Sciences , vol.899 , pp. 136-147
    • Gutteridge, J.M.1    Halliwell, B.2
  • 48
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg J., Arner E. S., Reactive oxygen species, antioxidants, and the mammalian thioredoxin system Free Radical Biology and Medicine 2001 31 11 1287 1312
    • (2001) Free Radical Biology and Medicine , vol.31 , Issue.11 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.2
  • 49
    • 0036827635 scopus 로고    scopus 로고
    • Oxidative stress, mitochondrial dysfunction, and epilepsy
    • Patel M. N., Oxidative stress, mitochondrial dysfunction, and epilepsy Free Radical Research 2002 36 11 1139 1146
    • (2002) Free Radical Research , vol.36 , Issue.11 , pp. 1139-1146
    • Patel, M.N.1
  • 50
    • 0035880007 scopus 로고    scopus 로고
    • Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins
    • Butterfield D. A., Kanski J., Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins Mechanisms of Ageing and Development 2001 122 9 945 962
    • (2001) Mechanisms of Ageing and Development , vol.122 , Issue.9 , pp. 945-962
    • Butterfield, D.A.1    Kanski, J.2
  • 51
    • 0034602442 scopus 로고    scopus 로고
    • Oxidative damage linked to neurodegeneration by selective -synuclein nitration in synucleinopathy lesions
    • Giasson B. I., Duda J. E., Murray I. V., Oxidative damage linked to neurodegeneration by selective -synuclein nitration in synucleinopathy lesions Science 2000 290 5493 985 989
    • (2000) Science , vol.290 , Issue.5493 , pp. 985-989
    • Giasson, B.I.1    Duda, J.E.2    Murray, I.V.3
  • 52
    • 0037096193 scopus 로고    scopus 로고
    • The relationship between oxidative/nitrative stress and pathological inclusions in Alzheimers and Parkinsons diseases
    • Giasson B. I., Ischiropoulos H., Lee V. M., Trojanowski J. Q., The relationship between oxidative/nitrative stress and pathological inclusions in Alzheimers and Parkinsons diseases Free Radical Biology and Medicine 2002 32 12 1264 1275
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.12 , pp. 1264-1275
    • Giasson, B.I.1    Ischiropoulos, H.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 53
    • 0033825627 scopus 로고    scopus 로고
    • Oxidative stress and genetics in the pathogenesis of parkinsons disease
    • Zhang Y., Dawson V. L., Dawson T. M., Oxidative stress and genetics in the pathogenesis of parkinsons disease Neurobiology of Disease 2000 7 4 240 250
    • (2000) Neurobiology of Disease , vol.7 , Issue.4 , pp. 240-250
    • Zhang, Y.1    Dawson, V.L.2    Dawson, T.M.3
  • 54
    • 0035171808 scopus 로고    scopus 로고
    • DPPH (1,1-diphenyl-2-Picrylhydrazyl) radical scavenging activity of flavonoids obtained from some medicinal plants
    • Okawa M., Kinjo J., Nohara T., Ono M., DPPH (1,1-diphenyl-2- Picrylhydrazyl) radical scavenging activity of flavonoids obtained from some medicinal plants Biological and Pharmaceutical Bulletin 2001 24 10 1202 1205
    • (2001) Biological and Pharmaceutical Bulletin , vol.24 , Issue.10 , pp. 1202-1205
    • Okawa, M.1    Kinjo, J.2    Nohara, T.3    Ono, M.4
  • 56
    • 0036589679 scopus 로고    scopus 로고
    • Protection of flavonoids against lipid peroxidation: The structure activity relationship revisited
    • Heijnen C. G., Haenen G. R., Oostveen R. M., Stalpers E. M., Bast A., Protection of flavonoids against lipid peroxidation: the structure activity relationship revisited Free Radical Research 2002 36 5 575 581
    • (2002) Free Radical Research , vol.36 , Issue.5 , pp. 575-581
    • Heijnen, C.G.1    Haenen, G.R.2    Oostveen, R.M.3    Stalpers, E.M.4    Bast, A.5
  • 57
    • 0031864258 scopus 로고    scopus 로고
    • Structure-activity relationships for antioxidant activities of a series of flavonoids in a liposomal system
    • Arora A., Nair M. G., Strasburg G. M., Structure-activity relationships for antioxidant activities of a series of flavonoids in a liposomal system Free Radical Biology and Medicine 1998 24 9 1355 1363
    • (1998) Free Radical Biology and Medicine , vol.24 , Issue.9 , pp. 1355-1363
    • Arora, A.1    Nair, M.G.2    Strasburg, G.M.3
  • 58
    • 0004580398 scopus 로고    scopus 로고
    • Flavonoids: Old and new aspects of a class of natural therapeutic drugs
    • Di Carlo G., Mascolo N., Izzo A. A., Capasso F., Flavonoids: old and new aspects of a class of natural therapeutic drugs Life Sciences 1999 65 4 337 353
    • (1999) Life Sciences , vol.65 , Issue.4 , pp. 337-353
    • Di Carlo, G.1    Mascolo, N.2    Izzo, A.A.3    Capasso, F.4
  • 60
    • 0025004502 scopus 로고
    • Flavonoids as antioxidants: Determination of radical-scavenging efficiencies
    • Bors W., Heller W., Michel C., Saran M., Flavonoids as antioxidants: determination of radical-scavenging efficiencies Methods in Enzymology 1990 186 343 355
    • (1990) Methods in Enzymology , vol.186 , pp. 343-355
    • Bors, W.1    Heller, W.2    Michel, C.3    Saran, M.4
  • 61
    • 0035902492 scopus 로고    scopus 로고
    • Probing the mechanism of insulin fibril formation with insulin mutants
    • Nielsen L., Frokjaer S., Brange J., Uversky V. N., Fink A. L., Probing the mechanism of insulin fibril formation with insulin mutants Biochemistry 2001 40 28 8397 8409
    • (2001) Biochemistry , vol.40 , Issue.28 , pp. 8397-8409
    • Nielsen, L.1    Frokjaer, S.2    Brange, J.3    Uversky, V.N.4    Fink, A.L.5
  • 62
    • 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., Reversals of age-related declines in neuronal signal transduction, cognitive, and motor behavioral deficits with blueberry, spinach, or strawberry dietary supplementation Journal of Neuroscience 1999 19 18 8114 8121
    • (1999) Journal of Neuroscience , vol.19 , Issue.18 , pp. 8114-8121
    • Joseph, J.A.1    Shukitt-Hale, B.2    Denisova, N.A.3
  • 64
    • 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., Mandel S., Green tea polyphenol (-)-epigallocatechin-3-gallate prevents N-methyl-4-phenyl-1,2,3,6- tetrahydropyridine-induced dopaminergic neurodegeneration Journal of Neurochemistry 2001 78 5 1073 1082
    • (2001) Journal of Neurochemistry , vol.78 , Issue.5 , pp. 1073-1082
    • Levites, Y.1    Weinreb, O.2    Maor, G.3    Youdim, M.B.4    Mandel, S.5
  • 65
    • 31644443193 scopus 로고    scopus 로고
    • A yeast-based model of -synucleinopathy identifies compounds with therapeutic potential
    • Griffioen G., Duhamel H., van Damme N., A yeast-based model of -synucleinopathy identifies compounds with therapeutic potential Biochimica et Biophysica Acta 2006 1762 3 312 318
    • (2006) Biochimica et Biophysica Acta , vol.1762 , Issue.3 , pp. 312-318
    • Griffioen, G.1    Duhamel, H.2    Van Damme, N.3
  • 66
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant -synuclein linked to early-onset Parkinson disease
    • Conway K. A., Harper J. D., Lansbury P. T., Accelerated in vitro fibril formation by a mutant -synuclein linked to early-onset Parkinson disease Nature Medicine 1998 4 11 1318 1320
    • (1998) Nature Medicine , vol.4 , Issue.11 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 67
    • 33750631721 scopus 로고    scopus 로고
    • Bioavailability and stability issues in understanding the cancer preventive effects of tea polyphenols
    • Sang S., Lambert J. D., Yang C. S., Bioavailability and stability issues in understanding the cancer preventive effects of tea polyphenols Journal of the Science of Food and Agriculture 2006 86 14 2256 2265
    • (2006) Journal of the Science of Food and Agriculture , vol.86 , Issue.14 , pp. 2256-2265
    • Sang, S.1    Lambert, J.D.2    Yang, C.S.3
  • 68
    • 69249141470 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the flavonoid-induced inhibition of -synuclein fibrillation
    • Meng X., Munishkina L. A., Fink A. L., Uversky V. N., Molecular mechanisms underlying the flavonoid-induced inhibition of -synuclein fibrillation Biochemistry 2009 48 34 8206 8224
    • (2009) Biochemistry , vol.48 , Issue.34 , pp. 8206-8224
    • Meng, X.1    Munishkina, L.A.2    Fink, A.L.3    Uversky, V.N.4
  • 69
    • 0035919828 scopus 로고    scopus 로고
    • Baicalein protects cortical neurons from -amyloid (2535) induced toxicity
    • Lebeau A., Esclaire F., Rostene W., Pelaprat D., Baicalein protects cortical neurons from -amyloid (2535) induced toxicity Neuroreport 2001 12 10 2199 2202
    • (2001) Neuroreport , vol.12 , Issue.10 , pp. 2199-2202
    • Lebeau, A.1    Esclaire, F.2    Rostene, W.3    Pelaprat, D.4
  • 72
    • 0027504187 scopus 로고
    • Dietary antioxidant flavonoids and risk of coronary heart disease: The Zutphen Elderly Study
    • Hertog M. G., Feskens E. J., Hollman P. C., Katan M. B., Kromhout D., Dietary antioxidant flavonoids and risk of coronary heart disease: the Zutphen Elderly Study The Lancet 1993 342 8878 1007 1011
    • (1993) The Lancet , vol.342 , Issue.8878 , pp. 1007-1011
    • Hertog, M.G.1    Feskens, E.J.2    Hollman, P.C.3    Katan, M.B.4    Kromhout, D.5
  • 73
    • 0028925089 scopus 로고
    • Flavonoid intake and long-term risk of coronary heart disease and cancer in the seven countries study
    • Hertog M. G., Kromhout D., Aravanis C., Flavonoid intake and long-term risk of coronary heart disease and cancer in the seven countries study Archives of Internal Medicine 1995 155 4 381 386
    • (1995) Archives of Internal Medicine , vol.155 , Issue.4 , pp. 381-386
    • Hertog, M.G.1    Kromhout, D.2    Aravanis, C.3
  • 74
    • 0030240388 scopus 로고    scopus 로고
    • Relation between intake of flavonoids and risk for coronary heart disease in male health professionals
    • Rimm E. B., Katan M. B., Ascherio A., Stampfer M. J., Willett W. C., Relation between intake of flavonoids and risk for coronary heart disease in male health professionals Annals of Internal Medicine 1996 125 5 384 389
    • (1996) Annals of Internal Medicine , vol.125 , Issue.5 , pp. 384-389
    • Rimm, E.B.1    Katan, M.B.2    Ascherio, A.3    Stampfer, M.J.4    Willett, W.C.5
  • 76
    • 0141639855 scopus 로고    scopus 로고
    • Antioxidant activity of tea polyphenols in vivo: Evidence from animal studies
    • Frei B., Higdon J. V., Antioxidant activity of tea polyphenols in vivo: evidence from animal studies Journal of Nutrition 2003 133 10 3275S 3284S
    • (2003) Journal of Nutrition , vol.133 , Issue.10
    • Frei, B.1    Higdon, J.V.2
  • 77
    • 24344458570 scopus 로고    scopus 로고
    • Natural antioxidants for neurodegenerative diseases
    • Zhao B., Natural antioxidants for neurodegenerative diseases Molecular Neurobiology 2005 31 13 283 293
    • (2005) Molecular Neurobiology , vol.31 , Issue.13 , pp. 283-293
    • Zhao, B.1
  • 78
    • 0041816456 scopus 로고    scopus 로고
    • Modulation of pro-survival Akt/protein kinase B and ERK1/2 signaling cascades by quercetin and its in vivo metabolites underlie their action on neuronal viability
    • Spencer J. P., Rice-Evans C., Williams R. J., Modulation of pro-survival Akt/protein kinase B and ERK1/2 signaling cascades by quercetin and its in vivo metabolites underlie their action on neuronal viability Journal of Biological Chemistry 2003 278 37 34783 34793
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.37 , pp. 34783-34793
    • Spencer, J.P.1    Rice-Evans, C.2    Williams, R.J.3
  • 79
    • 33646570598 scopus 로고    scopus 로고
    • Small molecule inhibitors of -synuclein filament assembly
    • Masuda M., Suzuki N., Taniguchi S., Small molecule inhibitors of -synuclein filament assembly Biochemistry 2006 45 19 6085 6094
    • (2006) Biochemistry , vol.45 , Issue.19 , pp. 6085-6094
    • Masuda, M.1    Suzuki, N.2    Taniguchi, S.3


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