메뉴 건너뛰기




Volumn 15, Issue 2, 2010, Pages 418-436

DNA induced folding/fibrillation of alpha-synuclein: New insights in Parkinson's disease

Author keywords

Alpha Synuclein; Alpha Synuclein conformation; Alpha Synuclein DNA interaction; Neurodegeneration; Parkinson's disease; Review

Indexed keywords

ALPHA SYNUCLEIN; DNA;

EID: 77951248437     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3628     Document Type: Article
Times cited : (42)

References (198)
  • 1
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • DOI 10.1038/35081564
    • Goedert M: Alpha-synuclein and neurodegenerative diseases. Nat Rev Neurosci 2, 492-501 (2001) (Pubitemid 33676584)
    • (2001) Nature Reviews Neuroscience , vol.2 , Issue.7 , pp. 492-501
    • Goedert, M.1
  • 2
    • 0035031135 scopus 로고    scopus 로고
    • Parkinson's disease and other alphasynucleinopathies
    • Goedert M: Parkinson's disease and other alphasynucleinopathies. Clin Chem Lab Med 39, 308-312 (2001)
    • (2001) Clin Chem Lab Med , vol.39 , pp. 308-312
    • Goedert, M.1
  • 5
    • 0032546895 scopus 로고    scopus 로고
    • α-synuclein immunoreactivity in glial cytoplasmic inclusions in multiple system atrophy
    • DOI 10.1016/S0304-3940(98)00407-8, PII S0304394098004078
    • Wakabayashi K, M Yoshimoto, S Tsuji, H Takahashi: Alpha-synuclein immunoreactivity in glial cytoplasmic inclusions in multiple system atrophy. Neurosci Lett 249, 180-182 (1998) (Pubitemid 28331545)
    • (1998) Neuroscience Letters , vol.249 , Issue.2-3 , pp. 180-182
    • Wakabayashi, K.1    Yoshimoto, M.2    Tsuji, S.3    Takahashi, H.4
  • 6
    • 59649087536 scopus 로고    scopus 로고
    • Alpha-synuclein assembly as a therapeutic target of Parkinson's disease and related disorders
    • Ono K, M Hirohata, M Yamada: Alpha-synuclein assembly as a therapeutic target of Parkinson's disease and related disorders. Curr Pharm Des 14, 3247-3266 (2008)
    • (2008) Curr Pharm des , vol.14 , pp. 3247-3266
    • Ono, K.1    Hirohata, M.2    Yamada, M.3
  • 7
    • 42149094917 scopus 로고    scopus 로고
    • Neuropsychological characteristics of dementia with Lewy bodies and Parkinson's disease with dementia: Differentiation, early detection, and implications for "mild cognitive impairment" and biomarkers
    • Troster AI: Neuropsychological characteristics of dementia with Lewy bodies and Parkinson's disease with dementia: differentiation, early detection, and implications for "mild cognitive impairment" and biomarkers. Neuropsychol Rev 18, 103-119 (2008)
    • (2008) Neuropsychol Rev , vol.18 , pp. 103-119
    • Troster, A.I.1
  • 8
    • 0023722437 scopus 로고
    • Synuclein: A neuron-specific protein localized to the nucleus and presynaptic nerve terminal
    • Maroteaux L, JT Campanelli, RH Scheller: Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J Neurosci 8, 2804-2815 (1988)
    • (1988) J Neurosci , vol.8 , pp. 2804-2815
    • Maroteaux, L.1    Campanelli, J.T.2    Scheller, R.H.3
  • 9
    • 0343527226 scopus 로고    scopus 로고
    • α-synuclein immunoreactivity in dementia with Lewy bodies: Morphological staging and comparison with ubiquitin immunostaining
    • Gomez-Tortosa E, K Newell, MC Irizarry, JL Sanders, BT Hyman: alpha-Synuclein immunoreactivity in dementia with Lewy bodies: morphological staging and comparison with ubiquitin immunostaining. Acta Neuropathol, 99, 352-357 (2000) (Pubitemid 30179572)
    • (2000) Acta Neuropathologica , vol.99 , Issue.4 , pp. 352-357
    • Gomez-Tortosa, E.1    Newell, K.2    Irizarry, M.C.3    Sanders, J.L.4    Hyman, B.T.5
  • 10
    • 0033724436 scopus 로고    scopus 로고
    • Subcellular localization of alpha-synuclein in primary neuronal cultures: Effect of missense mutations
    • McLean PJ, S Ribich, BT Hyman: Subcellular localization of alpha-synuclein in primary neuronal cultures: effect of missense mutations. J Neural Transm Suppl 53-63 (2000)
    • (2000) J Neural Transm Suppl , pp. 53-63
    • McLean, P.J.1    Ribich, S.2    Hyman, B.T.3
  • 12
    • 0035958973 scopus 로고    scopus 로고
    • Muscarinic Receptor Stimulation Induces Translocation of an α-Synuclein Oligomer from Plasma Membrane to a Light Vesicle Fraction in Cytoplasm
    • DOI 10.1074/jbc.M011121200
    • Leng Y, TN Chase, MC Bennett: Muscarinic receptor stimulation induces translocation of an alpha-synuclein oligomer from plasma membrane to a light vesicle fraction in cytoplasm. J Biol Chem 276, 28212-28218 (2001) (Pubitemid 37391526)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.30 , pp. 28212-28218
    • Leng, Y.1    Chase, T.N.2    Bennett, M.C.3
  • 13
    • 0036970672 scopus 로고    scopus 로고
    • Deferoxamine attenuates iron-induced oxidative stress and prevents mitochondrial aggregation and α-synuclein translocation in SK-N-SH cells in culture
    • DOI 10.1159/000065700
    • Sangchot P, S Sharma, B Chetsawang, J Porter, P Govitrapong, M Ebadi: Deferoxamine attenuates ironinduced oxidative stress and prevents mitochondrial aggregation and alpha-synuclein translocation in SK-N-SH cells in culture. Dev Neurosci 24, 143-153 (2002) (Pubitemid 36151444)
    • (2002) Developmental Neuroscience , vol.24 , Issue.2-3 , pp. 143-153
    • Sangchot, P.1    Sharma, S.2    Chetsawang, B.3    Porter, J.4    Govitrapong, P.5    Ebadi, M.6
  • 15
    • 0347418194 scopus 로고    scopus 로고
    • α-Synuclein immunoreactivity in neuronal nuclear inclusions and neurites in multiple system atrophy
    • DOI 10.1016/j.neulet.2003.09.075
    • Lin WL, MW DeLucia, DW Dickson: Alpha-synuclein immunoreactivity in neuronal nuclear inclusions and neurites in multiple system atrophy. Neurosci Lett 354, 99-102 (2004) (Pubitemid 38032843)
    • (2004) Neuroscience Letters , vol.354 , Issue.2 , pp. 99-102
    • Lin, W.-L.1    Delucia, M.W.2    Dickson, D.W.3
  • 16
    • 56049093847 scopus 로고    scopus 로고
    • Semi-quantitative analysis of alpha-synuclein in subcellular pools of rat brain neurons: An immunogold electron microscopic study using a C-terminal specific monoclonal antibody
    • Zhang L, C Zhang, Y Zhu, Q Cai, P Chan, K Ueda, S Yu, H Yang: Semi-quantitative analysis of alpha-synuclein in subcellular pools of rat brain neurons: an immunogold electron microscopic study using a C-terminal specific monoclonal antibody. Brain Res 1244, 40-52 (2008)
    • (2008) Brain Res , vol.1244 , pp. 40-52
    • Zhang, L.1    Zhang, C.2    Zhu, Y.3    Cai, Q.4    Chan, P.5    Ueda, K.6    Yu, S.7    Yang, H.8
  • 17
    • 0141540494 scopus 로고    scopus 로고
    • Challenges and complexities of α-synuclein toxicity: New postulates in unfolding the mystery associated with Parkinson's disease
    • DOI 10.1016/j.abb.2003.08.015
    • Hegde ML, KS Jagannatha Rao: Challenges and complexities of alpha-synuclein toxicity: new postulates in unfolding the mystery associated with Parkinson's disease. Arch Biochem Biophys 418, 169-178 (2003) (Pubitemid 37159383)
    • (2003) Archives of Biochemistry and Biophysics , vol.418 , Issue.2 , pp. 169-178
    • Hegde, M.L.1    Jagannatha Rao, K.S.2
  • 18
    • 34447628565 scopus 로고    scopus 로고
    • New evidence for DNA nuclease activity of alpha-synuclein: A molecular mechanism in understanding Parkinson's disease
    • Hegde ML, KSJ Rao: New evidence for DNA nuclease activity of alpha-synuclein: a molecular mechanism in understanding Parkinson's disease. J Neurochem 98, 114-115 (2006)
    • (2006) J Neurochem , vol.98 , pp. 114-115
    • Hegde, M.L.1    Rao, K.S.J.2
  • 19
    • 34447618598 scopus 로고    scopus 로고
    • DNA induces folding in α-synuclein: Understanding the mechanism using chaperone property of osmolytes
    • DOI 10.1016/j.abb.2007.03.042, PII S0003986107001634
    • Hegde ML, KS Rao: DNA induces folding in alphasynuclein: understanding the mechanism using chaperone property of osmolytes. Arch Biochem Biophys 464, 57-69 (2007) (Pubitemid 47088357)
    • (2007) Archives of Biochemistry and Biophysics , vol.464 , Issue.1 , pp. 57-69
    • Hegde, M.L.1    Rao, K.S.J.2
  • 20
    • 8544264563 scopus 로고    scopus 로고
    • Double-stranded DNA stimulates the fibrillation of α-synuclein in vitro and is associated with the mature fibrils: An electron microscopy study
    • DOI 10.1016/j.jmb.2004.09.096, PII S0022283604012677
    • Cherny, D., W. Hoyer, V. Subramaniam & T. M. Jovin: Double-stranded DNA stimulates the fibrillation of alphasynuclein in vitro and is associated with the mature fibrils: an electron microscopy study. J Mol Biol, 344, 929-938 (2004) (Pubitemid 39491240)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.4 , pp. 929-938
    • Cherny, D.1    Hoyer, W.2    Subramaniam, V.3    Jovin, T.M.4
  • 22
    • 0031432993 scopus 로고    scopus 로고
    • Epidemiology of Parkinson's disease
    • DOI 10.1016/S1353-8020(97)00029-1, PII S1353802097000291
    • Rajput AH, S Birdi: Epidemiology of Parkinson's disease. Parkinsonism Relat Disord 3, 175-186 (1997) (Pubitemid 28188827)
    • (1997) Parkinsonism and Related Disorders , vol.3 , Issue.4 , pp. 175-186
    • Rajput, A.H.1    Birdi, S.2
  • 24
    • 57649155208 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease: A mechanism of pathogenic and therapeutic significance
    • Zhou C, Y Huang, S Przedborski: Oxidative stress in Parkinson's disease: a mechanism of pathogenic and therapeutic significance. Ann N Y Acad Sci 1147, 93-104 (2008)
    • (2008) Ann N y Acad Sci , vol.1147 , pp. 93-104
    • Zhou, C.1    Huang, Y.2    Przedborski, S.3
  • 26
    • 0026704066 scopus 로고
    • An introduction to the free radical hypothesis in Parkinson's disease
    • Olanow CW: An introduction to the free radical hypothesis in Parkinson's disease. Ann Neurol 32 Suppl, S2-9 (1992)
    • (1992) Ann Neurol , vol.32 , Issue.SUPPL.
    • Olanow, C.W.1
  • 29
    • 0033955608 scopus 로고    scopus 로고
    • Cell death mechanisms in Parkinson's disease
    • Jellinger KA: Cell death mechanisms in Parkinson's disease. J Neural Transm 107, 1-29 (2000) (Pubitemid 30077039)
    • (2000) Journal of Neural Transmission , vol.107 , Issue.1 , pp. 1-29
    • Jellinger, K.A.1
  • 31
    • 0023188570 scopus 로고
    • Monoamine oxidase, hydrogen peroxide, and Parkinson's disease
    • Cohen G: Monoamine oxidase, hydrogen peroxide, and Parkinson's disease. Adv Neurol 45, 119-125 (1987)
    • (1987) Adv Neurol , vol.45 , pp. 119-125
    • Cohen, G.1
  • 32
    • 0024358652 scopus 로고
    • Brain monoamine oxidase (MAO) B: A unique neurotoxin and neurotransmitter producing enzyme
    • Youdim MB: Brain monoamine oxidase (MAO) B: a unique neurotoxin and neurotransmitter producing enzyme. Prog Neuropsychopharmacol Biol Psychiatry 13, 363-371 (1989) (Pubitemid 19163788)
    • (1989) Progress in Neuro-Psychopharmacology and Biological Psychiatry , vol.13 , Issue.3-4 , pp. 363-371
    • Youdim, M.B.H.1
  • 33
    • 0026704075 scopus 로고
    • Alterations in levels of iron, ferritin, and other trace metals in neurodegenerative diseases affecting the basal ganglia
    • The Royal Kings and Queens Parkinson's Disease Research Group
    • Dexter DT, P Jenner, AH Schapira, CD Marsden: Alterations in levels of iron, ferritin, and other trace metals in neurodegenerative diseases affecting the basal ganglia. The Royal Kings and Queens Parkinson's Disease Research Group. Ann Neurol 32 Suppl, S94-100 (1992)
    • (1992) Ann Neurol , vol.32 , Issue.SUPPL.
    • Dexter, D.T.1    Jenner, P.2    Schapira, A.H.3    Marsden, C.D.4
  • 34
    • 36248938279 scopus 로고    scopus 로고
    • The pathogenesis of cell death in Parkinson's disease - 2007
    • DOI 10.1002/mds.21675
    • Olanow CW: The pathogenesis of cell death in Parkinson's disease - 2007. Mov Disord 22, S335-S342 (2007) (Pubitemid 350134186)
    • (2007) Movement Disorders , vol.22 , Issue.SUPPL. 17
    • Olanow, C.W.1
  • 36
    • 0036797552 scopus 로고    scopus 로고
    • Impaired dopamine storage resulting from α-synuclein mutations may contribute to the pathogenesis of Parkinson's disease
    • Lotharius J, P Brundin: Impaired dopamine storage resulting from alpha-synuclein mutations may contribute to the pathogenesis of Parkinson's disease. Hum Mol Genet 11, 2395-2407 (2002) (Pubitemid 35174703)
    • (2002) Human Molecular Genetics , vol.11 , Issue.20 , pp. 2395-2407
    • Lotharius, J.1    Brundin, P.2
  • 37
    • 0018095085 scopus 로고
    • Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinones
    • Graham DG: Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinones. Mol Pharmacol 14, 633-643 (1978) (Pubitemid 8402469)
    • (1978) Molecular Pharmacology , vol.14 , Issue.4 , pp. 633-643
    • Graham, D.G.1
  • 38
    • 0031899172 scopus 로고    scopus 로고
    • Oxidative mechanisms in nigral cell death in Parkinson's disease
    • Jenner P: Oxidative mechanisms in nigral cell death in Parkinson's disease. Mov Disord 13 Suppl 1, 24-34 (1998)
    • (1998) Mov Disord , vol.13 , Issue.SUPPL. 1 , pp. 24-34
    • Jenner, P.1
  • 41
    • 0024356620 scopus 로고
    • Increased nigral iron content and alterations in other metal ions occurring in brain in Parkinson's disease
    • DOI 10.1111/j.1471-4159.1989.tb07264.x
    • Dexter DT, FR, Wells, AJ Lees, F Agid, Y Agid, P Jenner, CD Marsden: Increased nigral iron content and alterations in other metal ions occurring in brain in Parkinson's disease. J Neurochem 52, 1830-1836 (1989) (Pubitemid 19140770)
    • (1989) Journal of Neurochemistry , vol.52 , Issue.6 , pp. 1830-1836
    • Dexter, D.T.1    Wells, F.R.2    Lees, A.J.3    Agid, F.4    Agid, Y.5    Jenner, P.6    Marsden, C.D.7
  • 42
    • 0030878073 scopus 로고    scopus 로고
    • Oxidative DNA damage in the Parkinsonian brain: An apparent selective increase in 8-hydroxyguanine levels in substantia nigra
    • Alam ZI, A Jenner, SE Daniel, AJ Lees, N Cairns, CD Marsden, P Jenner, B Halliwell: Oxidative DNA damage in the parkinsonian brain: an apparent selective increase in 8- hydroxyguanine levels in substantia nigra. J Neurochem 69, 1196-1203 (1997) (Pubitemid 27364841)
    • (1997) Journal of Neurochemistry , vol.69 , Issue.3 , pp. 1196-1203
    • Alam, Z.I.1    Jenner, A.2    Daniel, S.E.3    Lees, A.J.4    Cairns, N.5    Marsden, C.D.6    Jenner, P.7    Halliwell, B.8
  • 43
    • 38449107680 scopus 로고    scopus 로고
    • Programmed cell death and new discoveries in the genetics of parkinsonism
    • DOI 10.1111/j.1471-4159.2007.05106.x
    • Burke RE: Programmed cell death and new discoveries in the genetics of parkinsonism. J Neurochem 104, 875-890 (2008) (Pubitemid 351143657)
    • (2008) Journal of Neurochemistry , vol.104 , Issue.4 , pp. 875-890
    • Burke, R.E.1
  • 45
    • 0026040282 scopus 로고
    • Iron-melanin interaction and lipid peroxidation: Implications for Parkinson's disease
    • Ben-Shachar D, P Riederer, MB Youdim: Iron-melanin interaction and lipid peroxidation: implications for Parkinson's disease. J Neurochem 57, 1609-1614 (1991) (Pubitemid 21922796)
    • (1991) Journal of Neurochemistry , vol.57 , Issue.5 , pp. 1609-1614
    • Ben-Shachar, D.1    Riederer, P.2    Youdim, M.B.H.3
  • 48
    • 40849135716 scopus 로고    scopus 로고
    • Apoptotic mechanisms involved in neurodegenerative diseases: Experimental and therapeutic approaches
    • DOI 10.1358/mf.2008.30.1.1090962
    • Camins A, M Pallas, JS Silvestre: Apoptotic mechanisms involved in neurodegenerative diseases: experimental and therapeutic approaches. Methods Find Exp Clin Pharmacol 30, 43-65 (2008) (Pubitemid 351397455)
    • (2008) Methods and Findings in Experimental and Clinical Pharmacology , vol.30 , Issue.1 , pp. 43-65
    • Camins, A.1    Pallas, M.2    Silvestre, J.S.3
  • 49
    • 58349085737 scopus 로고    scopus 로고
    • What causes cell death in Parkinson's disease?
    • Gupta A, VL Dawson, TM Dawson: What causes cell death in Parkinson's disease? Ann Neurol 64 Suppl 2, S3-15 (2008)
    • (2008) Ann Neurol , vol.64 , Issue.SUPPL. 2
    • Gupta, A.1    Dawson, V.L.2    Dawson, T.M.3
  • 50
    • 0031668930 scopus 로고    scopus 로고
    • Programmed cell death: Does it play a role in Parkinson's disease?
    • Burke RE, NG Kholodilov: Programmed cell death: does it play a role in Parkinson's disease? Ann Neurol 44, S126-133 (1998) (Pubitemid 28423839)
    • (1998) Annals of Neurology , vol.44 , Issue.3 SUPPL. 1
    • Burke, R.E.1    Kholodilov, N.G.2
  • 51
    • 0031738971 scopus 로고    scopus 로고
    • DNA fragmentation in human substantia nigra: Apoptosis or perimortem effect?
    • Kingsbury AE, C. D. Mardsen & O. J. Foster: DNA fragmentation in human substantia nigra: apoptosis or perimortem effect? Mov Disord 13, 877-884 (1998) (Pubitemid 28517663)
    • (1998) Movement Disorders , vol.13 , Issue.6 , pp. 877-884
    • Kingsbury, A.E.1    Mardsen, C.D.2    Foster, O.J.F.3
  • 52
    • 0030612197 scopus 로고    scopus 로고
    • Nigrostriatal neuronal death in Parkinson's disease - A passive or an active genetically-controlled process?
    • Ziv I, A Barzilai, D Offen, N Nardi, E Melamed: Nigrostriatal neuronal death in Parkinson's disease-a passive or an active genetically-controlled process? J Neural Transm Suppl 49, 69-76 (1997) (Pubitemid 27351474)
    • (1997) Journal of Neural Transmission, Supplement , Issue.49 , pp. 69-76
    • Ziv, I.1    Barzilai, A.2    Offen, D.3    Nardi, N.4    Melamed, E.5
  • 53
    • 0031696403 scopus 로고    scopus 로고
    • A fluorescent double-labeling method to detect and confirm apoptotic nuclei in Parkinson's disease
    • Tatton NA, A Maclean-Fraser, WG Tatton, DP Perl, CW Olanow: A fluorescent double-labeling method to detect and confirm apoptotic nuclei in Parkinson's disease. Ann Neurol 44, S142-148 (1998) (Pubitemid 28423841)
    • (1998) Annals of Neurology , vol.44 , Issue.3 SUPPL. 1
    • Tatton, N.A.1    Maclean-Fraser, A.2    Tatton, W.G.3    Perl, D.P.4    Olanow, C.W.5
  • 54
    • 0031739345 scopus 로고    scopus 로고
    • Role of apoptosis in the pathogenesis of Parkinson's disease: A novel therapeutic opportunity?
    • Ziv I, E Melamed: Role of apoptosis in the pathogenesis of Parkinson's disease: A novel therapeutic opportunity? Mov Disord 13, 865-70 (1998) (Pubitemid 28517661)
    • (1998) Movement Disorders , vol.13 , Issue.6 , pp. 865-870
    • Ziv, I.1    Melamed, E.2
  • 55
    • 0031687793 scopus 로고    scopus 로고
    • Understanding cell death in Parkinson's disease
    • Jenner P, CW Olanow: Understanding cell death in Parkinson's disease. Ann Neurol 44, S72-84 (1998) (Pubitemid 28423832)
    • (1998) Annals of Neurology , vol.44 , Issue.3 SUPPL. 1
    • Jenner, P.1    Olanow, C.W.2
  • 56
    • 0023320657 scopus 로고
    • Parkinson's disease, twins, and the DNAdamage hypothesis
    • Robbins JH: Parkinson's disease, twins, and the DNAdamage hypothesis. Ann Neurol 21, 412 (1987)
    • (1987) Ann Neurol , vol.21 , pp. 412
    • Robbins, J.H.1
  • 57
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • Gavrieli Y, Y Sherman, SA Ben-Sasson: Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J Cell Biol 119, 493-501 (1992)
    • (1992) J Cell Biol , vol.119 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 58
    • 0028136653 scopus 로고
    • Differentiation between cellular apoptosis and necrosis by the combined use of in situ tailing and nick translation techniques
    • Gold R, M Schmied, G Giegerich, H Breitschopf, HP Hartung, KV Toyka, H Lassmann: Differentiation between cellular apoptosis and necrosis by the combined use of in situ tailing and nick translation techniques. Lab Invest, 71, 219-225 (1994) (Pubitemid 24278174)
    • (1994) Laboratory Investigation , vol.71 , Issue.2 , pp. 219-225
    • Gold, R.1    Schmied, M.2    Giegerich, G.3    Breitschopf, H.4    Hartung, H.P.5    Toyka, K.V.6    Lassmann, H.7
  • 59
    • 0031036896 scopus 로고    scopus 로고
    • Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease
    • Anglade P, S Vyas, F Javoy-Agid, MT Herrero, PP Michel, J Marquez, A Mouatt-Prigent, M Ruberg, EC Hirsch, Y. Agid: Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease. Histol Histopathol 12, 25-31 (1997) (Pubitemid 27106916)
    • (1997) Histology and Histopathology , vol.12 , Issue.1 , pp. 25-31
    • Anglade, P.1
  • 60
    • 0030738721 scopus 로고    scopus 로고
    • Apoptosis in dopaminergic neurons of the human substantia nigra during normal aging
    • Anglade P, S Vyas, EC Hirsch, Y Agid: Apoptosis in dopaminergic neurons of the human substantia nigra during normal aging. Histol Histopathol 12, 603-10 (1997) (Pubitemid 27314689)
    • (1997) Histology and Histopathology , vol.12 , Issue.3 , pp. 603-610
    • Anglade, P.1
  • 61
    • 0031013141 scopus 로고    scopus 로고
    • Apoptotic-like changes in Lewy-body-associated disorders and normal aging in substantia nigral neurons
    • Tompkins MM, EJ Basgall, E Zamrini, WD Hill: Apoptotic-like changes in Lewy-body-associated disorders and normal aging in substantia nigral neurons. Am J Pathol, 150, 119-131 (1997) (Pubitemid 27027103)
    • (1997) American Journal of Pathology , vol.150 , Issue.1 , pp. 119-131
    • Tompkins, M.M.1    Basgall, E.J.2    Zamrini, E.3    Hill, W.D.4
  • 62
    • 0031716026 scopus 로고    scopus 로고
    • Dopamine agonists and neuroprotection in Parkinson's disease
    • Olanow CW, P Jenner, D Brooks: Dopamine agonists and neuroprotection in Parkinson's disease. Ann Neurol 44, S167-174 (1998) (Pubitemid 28423845)
    • (1998) Annals of Neurology , vol.44 , Issue.3 SUPPL. 1
    • Olanow, C.W.1    Jenner, P.2    Brooks, D.3
  • 63
    • 0032868244 scopus 로고    scopus 로고
    • Confocal microscopy as a tool to examine DNA fragmentation, chromatin condensation and other apoptotic changes in Parkinson's disease
    • DOI 10.1016/S1353-8020(99)00035-8, PII S1353802099000358
    • Tatton NA, HJ Rideout: Confocal microscopy as a tool to examine DNA fragmentation, chromatin condensation and other apoptotic changes in Parkinson's disease. Parkinsonism Relat Disord 5, 179-186 (1999) (Pubitemid 29408673)
    • (1999) Parkinsonism and Related Disorders , vol.5 , Issue.4 , pp. 179-186
    • Tatton, N.A.1    Rideout, H.J.2
  • 65
    • 0038100354 scopus 로고    scopus 로고
    • First evidence to show the topological change of DNA from B-DNA to Z-DNA conformation in the hippocampus of Alzheimer's brain
    • DOI 10.1385/NMM:2:3:289
    • Suram A, KS Rao, KS Latha, MA. Viswamitra: First evidence to show the topological change of DNA from BDNA to Z-DNA conformation in the hippocampus of Alzheimer's brain. Neuromolecular Med 2, 289-297 (2002) (Pubitemid 37070588)
    • (2002) NeuroMolecular Medicine , vol.2 , Issue.3 , pp. 289-297
    • Suram, A.1    Rao, J.K.S.2    Latha, K.S.3    Viswamitra, M.A.4
  • 67
    • 0037113341 scopus 로고    scopus 로고
    • Neuronal RNA oxidation is a prominent feature of dementia with Lewy bodies
    • DOI 10.1097/00001756-200211150-00009
    • Nunomura A, S Chiba, K Kosaka, A Takeda, RJ Castellani, MA Smith, G Perry: Neuronal RNA oxidation is a prominent feature of dementia with Lewy bodies. Neuroreport 13, 2035-2039 (2002) (Pubitemid 36005920)
    • (2002) NeuroReport , vol.13 , Issue.16 , pp. 2035-2039
    • Nunomura, A.1    Chiba, S.2    Kosaka, K.3    Takeda, A.4    Castellani, R.J.5    Smith, M.A.6    Perry, G.7
  • 69
    • 0025149002 scopus 로고
    • Quantitative determination of deleted mitochondrial DNA relative to normal DNA in parkinsonian striatum by a kinetic PCR analysis
    • Ozawa T, M Tanaka, S Ikebe, K Ohno, T Kondo, Y Mizuno: Quantitative determination of deleted mitochondrial DNA relative to normal DNA in parkinsonian striatum by a kinetic PCR analysis. Biochem Biophys Res Commun 172, 483-489 (1990) (Pubitemid 20384446)
    • (1990) Biochemical and Biophysical Research Communications , vol.172 , Issue.2 , pp. 483-489
    • Ozawa, T.1    Tanaka, M.2    Ikebe, S.-I.3    Ohno, K.4    Kondo, T.5    Mizuno, Y.6
  • 71
    • 18044381334 scopus 로고    scopus 로고
    • New aspects of genetic contributions to Parkinson's disease
    • Hofer A, T Gasser: New aspects of genetic contributions to Parkinson's disease. J Mol Neurosci 24, 417-424 (2004)
    • (2004) J Mol Neurosci , vol.24 , pp. 417-424
    • Hofer, A.1    Gasser, T.2
  • 72
    • 0022932316 scopus 로고
    • Controversies in the management of Parkinson's disease
    • Calne DB, UK Rinne: Controversies in the management of Parkinson's disease. Mov Disord 1, 159-162 (1986)
    • (1986) Mov Disord , vol.1 , pp. 159-162
    • Calne, D.B.1    Rinne, U.K.2
  • 77
    • 0026746512 scopus 로고
    • Neuromelanincontaining neurons of the substantia nigra accumulate iron and aluminum in Parkinson's disease: A LAMMA study
    • Good PF, CW Olanow, DP Perl: Neuromelanincontaining neurons of the substantia nigra accumulate iron and aluminum in Parkinson's disease: a LAMMA study. Brain Res 593, 343-346 (1992)
    • (1992) Brain Res , vol.593 , pp. 343-346
    • Good, P.F.1    Olanow, C.W.2    Perl, D.P.3
  • 78
    • 0026454505 scopus 로고
    • Calcium, magnesium and aluminum concentrations in Parkinson's disease
    • Yasui M, T Kihira, K Ota: Calcium, magnesium and aluminum concentrations in Parkinson's disease. Neurotoxicology 13, 593-600 (1992)
    • (1992) Neurotoxicology , vol.13 , pp. 593-600
    • Yasui, M.1    Kihira, T.2    Ota, K.3
  • 79
    • 0027952847 scopus 로고
    • A case-control study of Parkinson's disease in a horticultural region of British Columbia
    • DOI 10.1002/mds.870090111
    • Hertzman C, M Wiens, B Snow, S Kelly, D Calne: A case-control study of Parkinson's disease in a horticultural region of British Columbia. Mov Disord 9, 69-75 (1994) (Pubitemid 24022617)
    • (1994) Movement Disorders , vol.9 , Issue.1 , pp. 69-75
    • Hertzman, C.1    Wiens, M.2    Snow, B.3    Kelly, S.4    Calne, D.5
  • 81
    • 0033153770 scopus 로고    scopus 로고
    • Aluminium-containing antacids as a cause of idiopathic Parkinson's disease14
    • DOI 10.1054/mehy.1997.0701
    • Altschuler E: Aluminum-containing antacids as a cause of idiopathic Parkinson's disease. Med Hypotheses 53, 22-23 (1999) (Pubitemid 29391318)
    • (1999) Medical Hypotheses , vol.53 , Issue.1 , pp. 22-23
    • Altschuler, E.1
  • 84
    • 15744361815 scopus 로고    scopus 로고
    • An algorithmic approach to understand trace elemental homeostasis in serum samples of Parkinson disease
    • DOI 10.1016/j.compbiomed.2004.04.003, PII S0010482504000642
    • Pande MB, P Nagabhushan, ML Hegde, TS Rao, KS Rao: An algorithmic approach to understand trace elemental homeostasis in serum samples of Parkinson disease. Comput Biol Med 35, 475-493 (2005) (Pubitemid 40409692)
    • (2005) Computers in Biology and Medicine , vol.35 , Issue.6 , pp. 475-493
    • Pande, M.B.S.1    Nagabhushan, P.2    Hegde, M.L.3    Rao, T.S.S.4    Rao, K.S.J.5
  • 87
    • 79959770196 scopus 로고    scopus 로고
    • Altered trace elemental homeostasis in neurodegenerative (Alzheimer's and Parkinson's) and neuropsychiatric (bipolar) disorder' In. Neurodegenerative diseases: Alzheimer's disease (Abs)
    • Shanmugavelu P, TSS Rao, ML Hegde, MS Mustak, RB Menon, RV Rao, KSJ Rao. Altered trace elemental homeostasis in neurodegenerative (Alzheimer's and Parkinson's) and neuropsychiatric (bipolar) disorder' In. Neurodegenerative diseases: Alzheimer's disease (Abs). J Neurochem 88, 49 (2004)
    • (2004) J Neurochem , vol.88 , pp. 49
    • Shanmugavelu, P.1    Rao, T.2    Hegde, M.L.3    Mustak, M.S.4    Menon, R.B.5    Rao, R.V.6    Rao, K.S.J.7
  • 89
    • 0036150971 scopus 로고    scopus 로고
    • The synucleins
    • George JM: The synucleins. Genome Biol 3, REVIEWS 3002.1-3002.6 (2002)
    • (2002) Genome Biol , vol.3 , pp. 30021-30026
    • George, J.M.1
  • 90
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • DOI 10.1021/bi991447r
    • Conway KA, JD Harper, PT Lansbury, Jr.: Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry 39, 2552-2563 (2000) (Pubitemid 30148907)
    • (2000) Biochemistry , vol.39 , Issue.10 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury Jr., P.T.3
  • 91
    • 0032573289 scopus 로고    scopus 로고
    • 53 to Thr on the physical and morphological properties of α-synuclein protein implicated in Parkinson's disease
    • DOI 10.1016/S0014-5793(98)01419-7, PII S0014579398014197
    • El-Agnaf OM, R Jakes, MD Curran, A Wallace: Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of alpha-synuclein protein implicated in Parkinson's disease. FEBS Lett 440, 67-70 (1998) (Pubitemid 28558737)
    • (1998) FEBS Letters , vol.440 , Issue.1-2 , pp. 67-70
    • El-Agnaf, O.M.A.1    Jakes, R.2    Curran, M.D.3    Wallace, A.4
  • 95
    • 0030749257 scopus 로고    scopus 로고
    • Gene discovery offers tentative clues to Parkinson's
    • DOI 10.1126/science.276.5321.1973
    • Vogel G: Gene discovery offers tentative clues to Parkinson's. Science 276, 1973 (1997) (Pubitemid 27443575)
    • (1997) Science , vol.276 , Issue.5321 , pp. 1973
    • Vogel, G.1
  • 96
    • 0031203911 scopus 로고    scopus 로고
    • Phosphorylation of proteins that regulate the cell cycle and cancer: An international perspective
    • Heintz NH: Phosphorylation of proteins that regulate the cell cycle and cancer: an international perspective. Jpn J Clin Oncol 27, 288 (1997)
    • (1997) Jpn J Clin Oncol , vol.27 , pp. 288
    • Heintz, N.H.1
  • 97
    • 0035027982 scopus 로고    scopus 로고
    • Parkinson's disease and related neurodegenerative synucleinopathies linked to progressive accumulations of synuclein aggregates in brain
    • DOI 10.1016/S1353-8020(00)00065-1, PII S1353802000000651
    • Trojanowski JQ, VM Lee: Parkinson's disease and related neurodegenerative synucleinopathies linked to progressive accumulations of synuclein aggregates in brain. Parkinsonism Relat Disord 7, 247-251 (2001) (Pubitemid 32372507)
    • (2001) Parkinsonism and Related Disorders , vol.7 , Issue.3 , pp. 247-251
    • Trojanowski, J.Q.1    Lee, V.M.-Y.2
  • 100
    • 0032990543 scopus 로고    scopus 로고
    • Antibodies to α-synuclein detect lewy bodies in many down's syndrome brains with alzheimer's disease
    • DOI 10.1002/1531-8249(199903)45:3<353::AID-ANA11>3.0.CO;2-4
    • Lippa CF, ML Schmidt, VM Lee, JQ Trojanowski: Antibodies to alpha-synuclein detect Lewy bodies in many Down's syndrome brains with Alzheimer's disease. Ann Neurol 45, 353-357 (1999) (Pubitemid 29120040)
    • (1999) Annals of Neurology , vol.45 , Issue.3 , pp. 353-357
    • Lippa, C.F.1    Schmidt, M.L.2    Lee, V.M.-Y.3    Trojanowski, J.Q.4
  • 103
    • 0031661141 scopus 로고    scopus 로고
    • Abnormal distribution of the non-Aβ component of Alzheimer's disease amyloid precursor/α-synuclein in Lewy body disease as revealed by proteinase K and formic acid pretreatment
    • Takeda A, M Hashimoto, M Mallory, M Sundsumo, L Hansen, A Sisk, E Masliah: Abnormal distribution of the non-Abeta component of Alzheimer's disease amyloid precursor/alpha-synuclein in Lewy body disease as revealed by proteinase K and formic acid pretreatment. Lab Invest 78, 1169-1177 (1998) (Pubitemid 28440832)
    • (1998) Laboratory Investigation , vol.78 , Issue.9 , pp. 1169-1177
    • Takeda, A.1    Hashimoto, M.2    Mallory, M.3    Sundsumo, M.4    Hansen, L.5    Sisk, A.6    Masliah, E.7
  • 104
    • 0031566042 scopus 로고    scopus 로고
    • NACP, a presynaptic protein, immunoreactivity in lewy bodies in Parkinson's disease
    • DOI 10.1016/S0304-3940(97)00891-4, PII S0304394097008914
    • Wakabayashi K, K Matsumoto K Takayama, M Yoshimoto, H Takahashi: NACP, a presynaptic protein, immunoreactivity in Lewy bodies in Parkinson's disease. Neurosci Lett 239, 45-48 (1997) (Pubitemid 28055846)
    • (1997) Neuroscience Letters , vol.239 , Issue.1 , pp. 45-48
    • Wakabayashi, K.1    Matsumoto, K.2    Takayama, K.3    Yoshimoto, M.4    Takahashi, H.5
  • 105
    • 0032102455 scopus 로고    scopus 로고
    • The synucleins: A family of proteins involved in synaptic function, plasticity, neurodegeneration and disease
    • DOI 10.1016/S0166-2236(97)01213-7
    • Clayton DF, JM George: The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease. Trends Neurosci 21, 249-254 (1998) (Pubitemid 28239982)
    • (1998) Trends in Neurosciences , vol.21 , Issue.6 , pp. 249-254
    • Clayton, D.F.1    George, J.M.2
  • 106
    • 0029127954 scopus 로고
    • Characterization of a novel protein regulated during the critical period for song learning in the zebra finch
    • George JM, H Jin, WS Woods, DF Clayton: Characterization of a novel protein regulated during the critical period for song learning in the zebra finch. Neuron 15, 361-372 (1995)
    • (1995) Neuron , vol.15 , pp. 361-372
    • George, J.M.1    Jin, H.2    Woods, W.S.3    Clayton, D.F.4
  • 109
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using sitedirected mutagenesis
    • Perrin RJ, WS Woods, DF Clayton, JM George: Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using sitedirected mutagenesis. J Biol Chem 275, 34393-34398 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 34393-34398
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 110
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of α-Synuclein secondary structure upon binding to synthetic membranes
    • DOI 10.1074/jbc.273.16.9443
    • Davidson WS, A Jonas, DF Clayton, JM George: Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J Biol Chem, 273, 9443-9449 (1998) (Pubitemid 28183026)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.16 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 111
    • 0038054286 scopus 로고    scopus 로고
    • A structural and functional role for 11-mer repeats in α-synuclein and other exchangeable lipid binding proteins
    • DOI 10.1016/S0022-2836(03)00520-5
    • Bussell R Jr, D Eliezer: A structural and functional role for 11-mer repeats in alpha-synuclein and other exchangeable lipid binding proteins. J Mol Biol 329, 763-778 (2003) (Pubitemid 36629369)
    • (2003) Journal of Molecular Biology , vol.329 , Issue.4 , pp. 763-778
    • Bussell Jr., R.1    Eliezer, D.2
  • 113
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of α-synuclein in its free and lipid-associated states
    • DOI 10.1006/jmbi.2001.4538
    • Eliezer D, E Kutluay, R Bussell Jr, G Browne: Conformational properties of alpha-synuclein in its free and lipid-associated states. J Mol Biol 307, 1061-1073 (2001) (Pubitemid 33029953)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.4 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell Jr., R.3    Browne, G.4
  • 115
    • 0035834655 scopus 로고    scopus 로고
    • Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins
    • Perrin RJ, WS Woods, DF Clayton, JM George: Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins. J Biol Chem 276, 41958-41962 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 41958-41962
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 116
    • 0037155197 scopus 로고    scopus 로고
    • Lipid droplet binding and oligomerization properties of the Parkinson's disease protein α-synuclein
    • DOI 10.1074/jbc.M108414200
    • Cole NB, DD Murphy, T Grider, S Rueter, D Brasaemle, RL Nussbaum: Lipid droplet binding and oligomerization properties of the Parkinson's disease protein alpha-synuclein. J Biol Chem 277, 6344-6352 (2002) (Pubitemid 34968427)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.8 , pp. 6344-6352
    • Colebc, N.B.1    Murphy, D.D.2    Grider, T.3    Rueter, S.4    Brasaemle, D.5    Nussbaum, R.L.6
  • 119
    • 0037432332 scopus 로고    scopus 로고
    • Conformational behavior and aggregation of α-synuclein in organic solvents: Modeling the effects of membranes
    • DOI 10.1021/bi027166s
    • Munishkina, LA, C Phelan, VN Uversky, AL Fink: Conformational behavior and aggregation of alphasynuclein in organic solvents: modeling the effects of membranes. Biochemistry 42, 2720-2730 (2003) (Pubitemid 36330626)
    • (2003) Biochemistry , vol.42 , Issue.9 , pp. 2720-2730
    • Munishkina, L.A.1    Phelan, C.2    Uversky, V.N.3    Fink, A.L.4
  • 120
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • DOI 10.1038/35006074
    • Feany MB, WW Bender: A Drosophila model of Parkinson's disease. Nature 404, 394-398 (2000) (Pubitemid 30164341)
    • (2000) Nature , vol.404 , Issue.6776 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 122
    • 33646161379 scopus 로고    scopus 로고
    • Are monomeroligomer- aggregates of amyloidogenic peptides toxic species in neurodegeneration? A new experimental evidence (Abs)
    • Hegde ML, S Anitha, KSJ Rao: Are monomeroligomer- aggregates of amyloidogenic peptides toxic species in neurodegeneration? A new experimental evidence (Abs). Neurobiol Aging 25, 170 (2004)
    • (2004) Neurobiol Aging , vol.25 , pp. 170
    • Hegde, M.L.1    Anitha, S.2    Rao, K.3
  • 123
    • 5444249974 scopus 로고    scopus 로고
    • Overexpression of α-synuclein in rat substantia nigra results in loss of dopaminergic neurons, phosphorylation of α-synuclein and activation of caspase-9: Resemblance to pathogenetic changes in Parkinson's disease
    • DOI 10.1111/j.1471-4159.2004.02728.x
    • Yamada M, T Iwatsubo, Y Mizuno, H.Mochizuki: Overexpression of alpha-synuclein in rat substantia nigra results in loss of dopaminergic neurons, phosphorylation of alpha-synuclein and activation of caspase-9: resemblance to pathogenetic changes in Parkinson's disease. J Neurochem 91, 451-461 (2004) (Pubitemid 39363444)
    • (2004) Journal of Neurochemistry , vol.91 , Issue.2 , pp. 451-461
    • Yamada, M.1    Iwatsubo, T.2    Mizuno, Y.3    Mochizuki, H.4
  • 124
    • 37549030985 scopus 로고    scopus 로고
    • In vivo alpha-synuclein overexpression in rodents: A useful model of Parkinson's disease?
    • Chesselet MF: In vivo alpha-synuclein overexpression in rodents: a useful model of Parkinson's disease? Exp Neurol 209, 22-27 (2008)
    • (2008) Exp Neurol , vol.209 , pp. 22-27
    • Chesselet, M.F.1
  • 127
    • 0031866281 scopus 로고    scopus 로고
    • Expression pattern of synucleins (non-Aβ component of Alzheimer's disease amyloid precursor protein/α-synuclein) during murine brain development
    • Hsu LJ, M Mallory, Y Xia, I Veinbergs, M Hashimoto, M Yoshimoto, LJ Thal, T Saitoh, E Masliah: Expression pattern of synucleins (non-Abeta component of Alzheimer's disease amyloid precursor protein/alphasynuclein) during murine brain development. J Neurochem 71, 338-344 (1998) (Pubitemid 28292567)
    • (1998) Journal of Neurochemistry , vol.71 , Issue.1 , pp. 338-344
    • Hsu, L.J.1    Mallory, M.2    Xia, Y.3    Veinbergs, I.4    Hashimoto, M.5    Yoshimoto, M.6    Thal, L.J.7    Saitoh, T.8    Masliah, E.9
  • 129
    • 0035109875 scopus 로고    scopus 로고
    • Synuclein-1 is selectively up-regulated in response to nerve growth factor treatment in PC12 cells
    • DOI 10.1046/j.1471-4159.2001.00114.x
    • Stefanis L, N Kholodilov, HJ Rideout, RE Burke, LA Greene: Synuclein-1 is selectively up-regulated in response to nerve growth factor treatment in PC12 cells. J Neurochem 76, 1165-1176 (2001) (Pubitemid 32167390)
    • (2001) Journal of Neurochemistry , vol.76 , Issue.4 , pp. 1165-1176
    • Stefanis, L.1    Kholodilov, N.2    Rideout, H.J.3    Burke, R.E.4    Greene, L.A.5
  • 130
    • 0032492689 scopus 로고    scopus 로고
    • Regulation of phospholipase D2: Selective inhibition of mammalian phospholipase D isoenzymes by α- and β-synucleins
    • DOI 10.1021/bi972776r
    • Jenco JM, A Rawlingson, B Daniels, AJ Morris: Regulation of phospholipase D2: selective inhibition of mammalian phospholipase D isoenzymes by alpha- and beta-synucleins. Biochemistry 37, 4901-4909 (1998) (Pubitemid 28175972)
    • (1998) Biochemistry , vol.37 , Issue.14 , pp. 4901-4909
    • Jenco, J.M.1    Rawlingson, A.2    Daniels, B.3    Morris, A.J.4
  • 131
    • 0030460716 scopus 로고    scopus 로고
    • Muscarinic activation of phosphatidylcholine hydrolysis
    • Klein J, R Lindmar, K Loffelholz: Muscarinic activation of phosphatidylcholine hydrolysis. Prog Brain Res 109, 201-208 (1996) (Pubitemid 27047089)
    • (1996) Progress in Brain Research , vol.109 , pp. 201-208
    • Klein, J.1    Lindmar, R.2    Loffelholz, K.3
  • 132
    • 0034193399 scopus 로고    scopus 로고
    • Synucleins are developmentally expressed, and α-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons
    • Murphy DD, SM Rueter, JQ Trojanowski, VM Lee: Synucleins are developmentally expressed, and alphasynuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. J Neurosci 20, 3214-3220 (2000) (Pubitemid 30263139)
    • (2000) Journal of Neuroscience , vol.20 , Issue.9 , pp. 3214-3220
    • Murphy, D.D.1    Rueter, S.M.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4
  • 133
    • 0036364454 scopus 로고    scopus 로고
    • The cell biology of α-synuclein: A sticky problem?
    • DOI 10.1385/NMM:1:2:95
    • Cole NB, DD Murphy: The cell biology of alphasynuclein: a sticky problem? Neuromolecular Med 1, 95-109 (2002) (Pubitemid 37012519)
    • (2002) NeuroMolecular Medicine , vol.1 , Issue.2 , pp. 95-109
    • Cole, N.B.1    Murphy, D.D.2
  • 134
    • 0038460184 scopus 로고    scopus 로고
    • Part II: α-synuclein and its molecular pathophysiological role in neurodegenerative disease
    • DOI 10.1016/S0028-3908(03)00140-0
    • Dev, K. K., K. Hofele, S. Barbieri, V. L. Buchman & H. van der Putten: Part II: alpha-synuclein and its molecular pathophysiological role in neurodegenerative disease. Neuropharmacology, 45, 14-44 (2003) (Pubitemid 36695009)
    • (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
  • 135
    • 0029930181 scopus 로고    scopus 로고
    • Lewy body disease and dementia: A review
    • DOI 10.1001/archinte.156.5.487
    • Kalra S, C Bergeron, AE Lang: Lewy body disease and dementia. A review. Arch Intern Med 156, 487-493 (1996) (Pubitemid 26081734)
    • (1996) Archives of Internal Medicine , vol.156 , Issue.5 , pp. 487-493
    • Kalra, S.1    Bergeron, C.2    Lang, A.E.3
  • 137
    • 38949132572 scopus 로고    scopus 로고
    • Neuropathology of Parkinson's disease dementia and dementia with Lewy bodies with reference to striatal pathology
    • DOI 10.1016/S1353-8020(08)70005-1, PII S1353802008700051
    • Tsuboi Y, H Uchikado, DW Dickson: Neuropathology of Parkinson's disease dementia and dementia with Lewy bodies with reference to striatal pathology. Parkinsonism Relat Disor 13 Suppl 3, S221-224 (2007) (Pubitemid 351215244)
    • (2007) Parkinsonism and Related Disorders , vol.13 , Issue.SUPPL. 3
    • Tsuboi, Y.1    Uchikado, H.2    Dickson, D.W.3
  • 138
    • 19444363661 scopus 로고    scopus 로고
    • Aβ deposition is associated with enhanced cortical α-synuclein lesions in Lewy body diseases
    • DOI 10.1016/j.neurobiolaging.2004.10.006, PII S0197458004003331
    • Pletnikova O, N West, MK Lee, GL Rudow, RL Skolasky, TM Dawson, L Marsh, JC Troncoso: Abeta deposition is associated with enhanced cortical alpha-synuclein lesions in Lewy body diseases. Neurobiol Aging 26, 1183-1192 (2005) (Pubitemid 40726011)
    • (2005) Neurobiology of Aging , vol.26 , Issue.8 , pp. 1183-1192
    • Pletnikova, O.1    West, N.2    Lee, M.K.3    Rudow, G.L.4    Skolasky, R.L.5    Dawson, T.M.6    Marsh, L.7    Troncoso, J.C.8
  • 139
    • 0031763264 scopus 로고    scopus 로고
    • The synuclein family
    • Lavedan C: The synuclein family. Genome Res 8, 871-880 (1998) (Pubitemid 28495441)
    • (1998) Genome Research , vol.8 , Issue.9 , pp. 871-880
    • Lavedan, C.1
  • 140
    • 0035069311 scopus 로고    scopus 로고
    • Differential expression and distribution of α-, β-, and γ-synuclein in the developing human substantia nigra
    • DOI 10.1006/exnr.2000.7615
    • Galvin JE, TM Schuck, VM Lee, JQ Trojanowski: Differential expression and distribution of alpha-, beta-, and gamma-synuclein in the developing human substantia nigra. Exp Neurol 168, 347-355 (2001) (Pubitemid 32289770)
    • (2001) Experimental Neurology , vol.168 , Issue.2 , pp. 347-355
    • Galvin, J.E.1    Schuck, T.M.2    Lee, V.M.-Y.3    Trojanowski, J.Q.4
  • 141
    • 0032960760 scopus 로고    scopus 로고
    • Developmental expression of α-synuclein in rat hippocampus and cerebral cortex
    • DOI 10.1016/S0306-4522(98)00596-X, PII S030645229800596X
    • Petersen K, OF Olesen, JD Mikkelsen: Developmental expression of alpha-synuclein in rat hippocampus and cerebral cortex. Neuroscience 91, 651-659 (1999) (Pubitemid 29193274)
    • (1999) Neuroscience , vol.91 , Issue.2 , pp. 651-659
    • Petersen, K.1    Olesen, O.F.2    Mikkelsen, J.D.3
  • 142
    • 0033966487 scopus 로고    scopus 로고
    • α-synuclein up-regulation in substantia nigra dopaminergic neurons following administration of the parkinsonian toxin MPTP
    • DOI 10.1046/j.1471-4159.2000.740721.x
    • Vila M, S Vukosavic, V Jackson-Lewis, M Neystat, M Jakowec, S Przedborski: Alpha-synuclein up-regulation in substantia nigra dopaminergic neurons following administration of the parkinsonian toxin MPTP. J Neurochem 74, 721-729 (2000) (Pubitemid 30053745)
    • (2000) Journal of Neurochemistry , vol.74 , Issue.2 , pp. 721-729
    • Vila, M.1    Vukosavic, S.2    Jackson-Lewis, V.3    Neystat, M.4    Jakowec, M.5    Przedborski, S.6
  • 144
    • 34247139885 scopus 로고    scopus 로고
    • Over-expression of alpha-synuclein in human neural progenitors leads to specific changes in fate and differentiation
    • DOI 10.1093/hmg/ddm008
    • Schneider BL, CR Seehus, EE Capowski, P Aebischer, SC Zhang, CN Svendsen: Over-expression of alpha-synuclein in human neural progenitors leads to specific changes in fate and differentiation. Hum Mol Genet 16, 651-666 (2007) (Pubitemid 46591118)
    • (2007) Human Molecular Genetics , vol.16 , Issue.6 , pp. 651-666
    • Schneider, B.L.1    Seehus, C.R.2    Capowski, E.E.3    Aebischer, P.4    Zhang, S.-C.5    Svendsen, C.N.6
  • 145
    • 0037150773 scopus 로고    scopus 로고
    • Immunohistochemical comparison of α- and β-synuclein in adult rat central nervous system
    • DOI 10.1016/S0006-8993(02)02643-4, PII S0006899302026434
    • Mori F, K Tanji, M Yoshimoto, H Takahashi, K Wakabayashi: Immunohistochemical comparison of alphaand beta-synuclein in adult rat central nervous system. Brain Res 941, 118-126 (2002) (Pubitemid 34603290)
    • (2002) Brain Research , vol.941 , Issue.1-2 , pp. 118-126
    • Mori, F.1    Tanji, K.2    Yoshimoto, M.3    Takahashi, H.4    Wakabayashi, K.5
  • 147
    • 4043107784 scopus 로고    scopus 로고
    • Inhibition of tyrosine hydroxylase expression in α-synuclein- transfected dopaminergic neuronal cells
    • DOI 10.1016/j.neulet.2004.05.118, PII S0304394004006755
    • Yu S, X Zuo, Y Li, C Zhang, M Zhou, YA Zhang, K Ueda, P Chan: Inhibition of tyrosine hydroxylase expression in alpha-synuclein-transfected dopaminergic neuronal cells. Neurosci Lett 367, 34-39 (2004) (Pubitemid 39078779)
    • (2004) Neuroscience Letters , vol.367 , Issue.1 , pp. 34-39
    • Yu, S.1    Zuo, X.2    Li, Y.3    Zhang, C.4    Zhou, M.5    Zhang, Y.A.6    Ueda, K.7    Chan, P.8
  • 148
    • 33847649977 scopus 로고    scopus 로고
    • Extensive nuclear localization of α-synuclein in normal rat brain neurons revealed by a novel monoclonal antibody
    • DOI 10.1016/j.neuroscience.2006.12.028, PII S0306452206016915
    • Yu S, X Li, G Liu, J Han, C Zhang, Y Li, S Xu, C Liu, Y Gao, H Yang, K Ueda, P Chan: Extensive nuclear localization of alpha-synuclein in normal rat brain neurons revealed by a novel monoclonal antibody. Neuroscience 145, 539-555 (2007) (Pubitemid 46350815)
    • (2007) Neuroscience , vol.145 , Issue.2 , pp. 539-555
    • Yu, S.1    Li, X.2    Liu, G.3    Han, J.4    Zhang, C.5    Li, Y.6    Xu, S.7    Liu, C.8    Gao, Y.9    Yang, H.10    Ueda, K.11    Chan, P.12
  • 149
    • 0023315049 scopus 로고
    • Free diffusion to and from the inner nuclear membrane of newly synthesized plasma membrane glycoproteins
    • Torrisi MR, LV Lotti, A Pavan, G Migliaccio, S Bonatti: Free diffusion to and from the inner nuclear membrane of newly synthesized plasma membrane glycoproteins. J Cell Biol 104, 733-737 (1987)
    • (1987) J Cell Biol , vol.104 , pp. 733-737
    • Torrisi, M.R.1    Lotti, L.V.2    Pavan, A.3    Migliaccio, G.4    Bonatti, S.5
  • 151
    • 33749583553 scopus 로고    scopus 로고
    • α-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity
    • DOI 10.1093/hmg/ddl243
    • Kontopoulos E, JD Parvin, MB Feany: Alphasynuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity. Hum Mol Genet 15, 3012-3023 (2006) (Pubitemid 44530705)
    • (2006) Human Molecular Genetics , vol.15 , Issue.20 , pp. 3012-3023
    • Kontopoulos, E.1    Parvin, J.D.2    Feany, M.B.3
  • 153
    • 0036591852 scopus 로고    scopus 로고
    • Formation of hydrogen peroxide and hydroxyl radicals from Aβ and α-synuclein as a possible mechanism of cell death in Alzheimer's disease and Parkinson's disease
    • DOI 10.1016/S0891-5849(02)00801-8, PII S0891584902008018
    • Tabner BJ, S Turnbull, OM El-Agnaf, D Allsop: Formation of hydrogen peroxide and hydroxyl radicals from A (beta) and alpha-synuclein as a possible mechanism of cell death in Alzheimer's disease and Parkinson's disease. Free Radic Biol Med 32, 1076-1083 (2002) (Pubitemid 34603345)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.11 , pp. 1076-1083
    • Tabner, B.J.1    Turnbull, S.2    El-Agnaf, O.M.A.3    Allsop, D.4
  • 154
    • 0142241356 scopus 로고    scopus 로고
    • Fe(II)-induced DNA damage in α-synuclein-transfected human dopaminergic BE(2)-M17 neuroblastoma cells: Detection by the Comet assay
    • DOI 10.1046/j.1471-4159.2003.02013.x
    • Martin FL, SJ Williamson, KE Paleologou, R Hewitt, OM El-Agnaf, D Allsop: Fe (II)-induced DNA damage in alpha-synuclein-transfected human dopaminergic BE (2)- M17 neuroblastoma cells: detection by the Comet assay. J Neurochem 87,
    • (2003) Journal of Neurochemistry , vol.87 , Issue.3 , pp. 620-630
    • Martin, F.L.1    Williamson, S.J.M.2    Paleologou, K.E.3    Hewitt, R.4    El-Agnaf, O.M.A.5    Allsop, D.6
  • 155
    • 3042743587 scopus 로고    scopus 로고
    • First evidence for helical transitions in supercoiled DNA by amyloid β peptide (1-42) and aluminum: A new insight in understanding Alzheimer's disease
    • DOI 10.1385/JMN:22:1-2:19
    • Hegde ML, S Anitha, KS Latha, MS Mustak, R Stein, R Ravid, KS Rao: First evidence for helical transitions in supercoiled DNA by amyloid Beta Peptide (1-42) and aluminum: a new insight in understanding Alzheimer's disease. J Mol Neurosci 22, 19-31 (2004) (Pubitemid 41359012)
    • (2004) Journal of Molecular Neuroscience , vol.22 , Issue.1-2 , pp. 19-31
    • Hegde, M.L.1    Anitha, S.2    Latha, K.S.3    Mustak, M.S.4    Stein, R.5    Ravid, R.6    Rao, K.S.J.7
  • 156
    • 34447096496 scopus 로고    scopus 로고
    • A new evidence for DNA nicking property of amyloid β-peptide (1-42): Relevance to Alzheimer's disease
    • DOI 10.1016/j.abb.2007.03.015, PII S0003986107001476
    • Suram A, ML Hegde, KS Rao: A new evidence for DNA nicking property of amyloid beta-peptide (1-42): relevance to Alzheimer's disease. Arch Biochem Biophys 463, 245-252 (2007) (Pubitemid 47030340)
    • (2007) Archives of Biochemistry and Biophysics , vol.463 , Issue.2 , pp. 245-252
    • Suram, A.1    Hegde, M.L.2    Rao, K.S.J.3
  • 157
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure
    • Uversky VN, J Li, AL Fink: Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure. J Biol Chem 276, 44284-44296 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 159
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
    • DOI 10.1074/jbc.M010907200
    • Uversky VN, J Li, AL Fink: Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J Biol Chem 276, 10737-10744 (2001) (Pubitemid 38089246)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 160
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • Fink AL: Compact intermediate states in protein folding. Annu Rev Biophys Biomol Struct 24, 495-522 (1995)
    • (1995) Annu Rev Biophys Biomol Struct , vol.24 , pp. 495-522
    • Fink, A.L.1
  • 161
    • 0030572683 scopus 로고    scopus 로고
    • For protein misassembly, it's the "i" decade
    • Wetzel R: For protein misassembly, it's the "I" decade. Cell, 86, 699-702 (1996)
    • (1996) Cell , vol.86 , pp. 699-702
    • Wetzel, R.1
  • 162
    • 0035976814 scopus 로고    scopus 로고
    • Trimethylamine-N-oxideinduced folding of alpha-synuclein
    • Uversky VN, J Li, AL Fink: Trimethylamine-N-oxideinduced folding of alpha-synuclein. FEBS Lett 509, 31-35 (2001)
    • (2001) FEBS Lett , vol.509 , pp. 31-35
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 168
    • 0031875169 scopus 로고    scopus 로고
    • Polymerization of human prion peptide HuPrP 106-126 to amyloid in nucleic acid solution
    • DOI 10.1007/s007050050373
    • Nandi PK: Polymerization of human prion peptide HuPrP 106-126 to amyloid in nucleic acid solution. Arch Virol 143, 1251-1263 (1998) (Pubitemid 28371590)
    • (1998) Archives of Virology , vol.143 , Issue.7 , pp. 1251-1263
    • Nandi, P.K.1
  • 170
    • 0036959437 scopus 로고    scopus 로고
    • Beta-Amyloid induces oxidative DNA damage and cell death through activation of c-Jun N terminal kinase
    • Jang JH, YJ Surh: beta-Amyloid induces oxidative DNA damage and cell death through activation of c-Jun N terminal kinase. Ann N Y Acad Sci 973, 228-236 (2002)
    • (2002) Ann N y Acad Sci , vol.973 , pp. 228-236
    • Jang, J.H.1    Surh, Y.J.2
  • 171
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
    • DOI 10.1016/S0014-5793(96)01386-5, PII S0014579396013865
    • Kampers T, P Friedhoff, J Biernat, EM Mandelkow, E Mandelkow: RNA stimulates aggregation of microtubuleassociated protein tau into Alzheimer-like paired helical filaments. FEBS Lett 399, 344-349 (1996) (Pubitemid 26426879)
    • (1996) FEBS Letters , vol.399 , Issue.3 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 172
    • 0036970469 scopus 로고    scopus 로고
    • DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid
    • DOI 10.1016/S0022-2836(02)00750-7
    • Nandi PK, E Leclerc, JC Nicole, M Takahashi: DNAinduced partial unfolding of prion protein leads to its polymerisation to amyloid. J Mol Biol 322, 153-161 (2002) (Pubitemid 36132675)
    • (2002) Journal of Molecular Biology , vol.322 , Issue.1 , pp. 153-161
    • Nandi, P.K.1    Leclerc, E.2    Nicole, J.-C.3    Takahashi, M.4
  • 173
    • 0032880060 scopus 로고    scopus 로고
    • Polymerization of murine recombinant prion protein in nucleic acid solution
    • DOI 10.1007/s007050050702
    • Nandi PK, E Leclerc: Polymerization of murine recombinant prion protein in nucleic acid solution. Arch Virol 144, 1751-1763 (1999) (Pubitemid 29490035)
    • (1999) Archives of Virology , vol.144 , Issue.9 , pp. 1751-1763
    • Nandi, P.K.1    Leclerc, E.2
  • 174
    • 0035966046 scopus 로고    scopus 로고
    • DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation
    • Cordeiro Y, F Machado, L Juliano, MA Juliano, RR Brentani, D Foguel, JL Silva: DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation. J Biol Chem 276, 49400-49409 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 49400-49409
    • Cordeiro, Y.1    MacHado, F.2    Juliano, L.3    Juliano, M.4    Brentani, R.R.5    Foguel, D.6    Silva, J.L.7
  • 176
    • 33748441164 scopus 로고    scopus 로고
    • Role of protein conformational dynamics and DNA integrity in relevance to neuronal cell death in neurodegeneration
    • DOI 10.2174/156720506778249452
    • Gupta VB, ML Hegde, KS Rao: Role of protein conformational dynamics and DNA integrity in relevance to neuronal cell death in neurodegeneration. Curr Alzheimer Res 3, 297-309 (2006) (Pubitemid 44351474)
    • (2006) Current Alzheimer Research , vol.3 , Issue.4 , pp. 297-309
    • Gupta, V.B.1    Hegde, M.L.2    Jagnnathan Rao, K.S.3
  • 177
    • 33744940785 scopus 로고    scopus 로고
    • Amyloid β and neuromelanin-Toxic or protective molecules?. The cellular context makes the difference
    • DOI 10.1016/j.pneurobio.2006.03.004, PII S0301008206000281
    • Rao KS, ML Hegde, S Anitha, M Musicco, FA Zucca, NJ Turro, L Zecca: Amyloid beta and neuromelanin-toxic or protective molecules? The cellular context makes the difference. Prog Neurobiol 78, 364-373 (2006) (Pubitemid 43850101)
    • (2006) Progress in Neurobiology , vol.78 , Issue.6 , pp. 364-373
    • Rao, K.S.J.1    Hegde, M.L.2    Anitha, S.3    Musicco, M.4    Zucca, F.A.5    Turro, N.J.6    Zecca, L.7
  • 178
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • DOI 10.1021/bi961799n
    • Weinreb PH, W Zhen, AW Poon, KA Conway, PT Lansbury Jr,.: NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35, 13709-13715 (1996) (Pubitemid 26363912)
    • (1996) Biochemistry , vol.35 , Issue.43 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury Jr., P.T.5
  • 179
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • DOI 10.1110/ps.4210102
    • Uversky VN: Natively unfolded proteins: a point where biology waits for physics. Protein Sci 11, 739-756 (2002) (Pubitemid 34241284)
    • (2002) Protein Science , vol.11 , Issue.4 , pp. 739-756
    • Uversky, V.N.1
  • 180
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky VN, JR Gillespie, AL Fink: Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 41, 415-427 (2000)
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 181
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • DOI 10.1046/j.0014-2956.2001.02649.x
    • Uversky VN: What does it mean to be natively unfolded? Eur J Biochem 269, 2-12 (2002) (Pubitemid 34107333)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.1 , pp. 2-12
    • Uversky, V.N.1
  • 182
    • 0031728689 scopus 로고    scopus 로고
    • Synthetic filaments assembled from C-terminally truncated α-synuclein
    • DOI 10.1016/S0014-5793(98)01146-6, PII S0014579398011466
    • Crowther RA, R Jakes, MG Spillantini, M.Goedert: Synthetic filaments assembled from C-terminally truncated alpha-synuclein. FEBS Lett 436, 309-312 (1998) (Pubitemid 28482951)
    • (1998) FEBS Letters , vol.436 , Issue.3 , pp. 309-312
    • Crowther, R.A.1    Jakes, R.2    Spillantini, M.G.3    Goedert, M.4
  • 183
    • 0033538541 scopus 로고    scopus 로고
    • Alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease
    • Wood SJ, J Wypych, S Steavenson, JC Louis, M Citron, AL Biere: alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease. J Biol Chem 274, 19509-19512 (1999)
    • (1999) J Biol Chem , vol.274 , pp. 19509-19512
    • Wood, S.J.1    Wypych, J.2    Steavenson, S.3    Louis, J.C.4    Citron, M.5    Biere, A.L.6
  • 184
    • 0033583215 scopus 로고    scopus 로고
    • Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro
    • Giasson BI, K Uryu, JQ Trojanowski, VM Lee: Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro. J Biol Chem 274, 7619-7622 (1999)
    • (1999) J Biol Chem , vol.274 , pp. 7619-7622
    • Giasson, B.I.1    Uryu, K.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 187
    • 0035949542 scopus 로고    scopus 로고
    • Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human α-synuclein
    • DOI 10.1021/bi010616g
    • Li J, VN Uversky, AL Fink: Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein. Biochemistry 40, 11604-11613 (2001) (Pubitemid 32911305)
    • (2001) Biochemistry , vol.40 , Issue.38 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 188
  • 189
    • 33746064033 scopus 로고    scopus 로고
    • Emerging evidence for the neuroprotective role of α-synuclein
    • DOI 10.1016/j.expneurol.2006.04.024, PII S0014488606002780
    • Lee HG, X Zhu, A Takeda, G Perry, MA Smith: Emerging evidence for the neuroprotective role of alphasynuclein. Exp Neurol 200, 1-7 (2006) (Pubitemid 44080768)
    • (2006) Experimental Neurology , vol.200 , Issue.1 , pp. 1-7
    • Lee, H.-g.1    Zhu, X.2    Takeda, A.3    Perry, G.4    Smith, M.A.5
  • 190
    • 0242499460 scopus 로고    scopus 로고
    • Will Preventing Protein Aggregates Live Up to its Promise as Prophylaxis Against Neurodegenerative Diseases?
    • Lee HG, RB Petersen, X Zhu, K Honda, G Aliev, MA Smith, G Perry: Will preventing protein aggregates live up to its promise as prophylaxis against neurodegenerative diseases? Brain Pathol 13, 630-8 (2003) (Pubitemid 37420705)
    • (2003) Brain Pathology , vol.13 , Issue.4 , pp. 630-638
    • Lee, H.-G.1    Petersen, R.B.2    Zhu, X.3    Honda, K.4    Aliev, G.5    Smith, M.A.6    Perry, G.7
  • 191
    • 0037192865 scopus 로고    scopus 로고
    • α-synuclein protects against oxidative stress via inactivation of the c-Jun N-terminal kinase stress-signaling pathway in neuronal cells
    • DOI 10.1074/jbc.M111428200
    • Hashimoto M, LJ Hsu, E Rockenstein, T Takenouchi, M Mallory, E Masliah: alpha-Synuclein protects against oxidative stress via inactivation of the c-Jun N-terminal kinase stress-signaling pathway in neuronal cells. J Biol Chem 277, 11465-11472 (2002) (Pubitemid 34952915)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.13 , pp. 11465-11472
    • Hashimoto, M.1    Hsu, L.J.2    Rockenstein, E.3    Takenouchi, T.4    Mallory, M.5    Masliah, E.6
  • 192
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in α-synuclein mice: Implications for neurodegenerative disorders
    • DOI 10.1126/science.287.5456.1265
    • Masliah E, E Rockenstein, I Veinbergs, M Mallory, M Hashimoto, A Takeda, Y Sagara, A Sisk, L Mucke: Dopaminergic loss and inclusion body formation in alphasynuclein mice: implications for neurodegenerative disorders. Science 287, 1265-1269 (2000) (Pubitemid 30112148)
    • (2000) Science , vol.287 , Issue.5456 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5    Takeda, A.6    Sagara, Y.7    Sisk, A.8    Mucke, L.9
  • 196
    • 2942615527 scopus 로고    scopus 로고
    • Accelerated α-synuclein aggregation after differentiation of SH-SY5Y neuroblastoma cells
    • DOI 10.1016/j.brainres.2004.04.018, PII S000689930400544X
    • Hasegawa T, M Matsuzaki, A Takeda, A Kikuchi, H Akita, G Perry, MA Smith & Y. Itoyama: Accelerated alpha-synuclein aggregation after differentiation of SHSY5Y neuroblastoma cells. Brain Res, 1013, 51-59 (2004) (Pubitemid 38757408)
    • (2004) Brain Research , vol.1013 , Issue.1 , pp. 51-59
    • Hasegawa, T.1    Matsuzaki, M.2    Takeda, A.3    Kikuchi, A.4    Akita, H.5    Perry, G.6    Smith, M.A.7    Itoyama, Y.8
  • 197
    • 1642293184 scopus 로고    scopus 로고
    • Histochemical features of stress-induced aggregates in α-synuclein overexpressing cells
    • DOI 10.1016/j.brainres.2004.01.017, PII S0006899304000885
    • Matsuzaki M, T Hasegawa, A Takeda, A Kikuchi, K Furukawa, Y Kato, Y Itoyama: Histochemical features of stress-induced aggregates in alpha-synuclein overexpressing cells. Brain Res 1004, 83-90 (2004) (Pubitemid 38368064)
    • (2004) Brain Research , vol.1004 , Issue.1-2 , pp. 83-90
    • Matsuzaki, M.1    Hasegawa, T.2    Takeda, A.3    Kikuchi, A.4    Furukawa, K.5    Kato, Y.6    Itoyama, Y.7
  • 198
    • 0035017068 scopus 로고    scopus 로고
    • Sensitivity to MPTP is not increased in Parkinson' s disease-associated mutant α-synuclein transgenic mice
    • DOI 10.1046/j.1471-4159.2001.00366.x
    • Rathke-Hartlieb S, PJ Kahle, M Neumann, L Ozmen, S Haid, M Okochi, C Haass, JB Schulz: Sensitivity to MPTP is not increased in Parkinson's disease-associated mutant alpha-synuclein transgenic mice. J Neurochem 77, 1181-1184 (2001) (Pubitemid 32467072)
    • (2001) Journal of Neurochemistry , vol.77 , Issue.4 , pp. 1181-1184
    • Rathke-Hartlieb, S.1    Kahle, P.J.2    Neumann, M.3    Ozmen, L.4    Haid, S.5    Okochi, M.6    Haass, C.7    Schulz, J.B.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.