메뉴 건너뛰기




Volumn 7, Issue 1, 2008, Pages 97-109

Mitochondria in the aetiology and pathogenesis of Parkinson's disease

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; CREATINE; DJ 1 PROTEIN; DNA DIRECTED DNA POLYMERASE BETA; DNA DIRECTED DNA POLYMERASE GAMMA; DNA POLYMERASE GAMMA 1; FREE RADICAL; LEUCINE RICH REPEAT KINASE 2; LEVODOPA; MITOCHONDRIAL DNA; MITOCHONDRIAL PROTEIN; PARKIN; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PLACEBO; PTEN INDUCED PUTATIVE KINASE 1; SERINE PROTEINASE OMI; TOXIN; UBIDECARENONE; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 37049004489     PISSN: 14744422     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1474-4422(07)70327-7     Document Type: Review
Times cited : (719)

References (164)
  • 1
    • 33745919520 scopus 로고    scopus 로고
    • Epidemiology of Parkinson's disease
    • de Lau L., and Breteler M. Epidemiology of Parkinson's disease. Lancet Neurol 5 (2006) 525-535
    • (2006) Lancet Neurol , vol.5 , pp. 525-535
    • de Lau, L.1    Breteler, M.2
  • 2
    • 0036209085 scopus 로고    scopus 로고
    • The accuracy of diagnosis of parkinsonian syndromes in a specialist movement disorder service
    • Hughes A., Daniel S., Ben Shlomo Y., and Lees A. The accuracy of diagnosis of parkinsonian syndromes in a specialist movement disorder service. Brain 125 (2002) 861-870
    • (2002) Brain , vol.125 , pp. 861-870
    • Hughes, A.1    Daniel, S.2    Ben Shlomo, Y.3    Lees, A.4
  • 3
    • 0037379324 scopus 로고    scopus 로고
    • Genetic and environmental factors in the cause of Parkinson's disease
    • Warner T., and Schapira A. Genetic and environmental factors in the cause of Parkinson's disease. Ann Neurol 53 suppl 3 (2003) S16-S23
    • (2003) Ann Neurol , vol.53 , Issue.SUPPL. 3
    • Warner, T.1    Schapira, A.2
  • 4
    • 0033032999 scopus 로고    scopus 로고
    • Mitochondrial involvement in Parkinson's disease, Huntington's disease, hereditary spastic paraplegia and Friedreich's ataxia
    • Schapira A. Mitochondrial involvement in Parkinson's disease, Huntington's disease, hereditary spastic paraplegia and Friedreich's ataxia. Biochim Biophys Acta 1410 (1999) 159-170
    • (1999) Biochim Biophys Acta , vol.1410 , pp. 159-170
    • Schapira, A.1
  • 5
    • 0024390719 scopus 로고
    • Mitochondrial complex I deficiency in Parkinson's disease
    • Schapira A., Cooper J., Dexter D., et al. Mitochondrial complex I deficiency in Parkinson's disease. Lancet 1 (1989) 1269
    • (1989) Lancet , vol.1 , pp. 1269
    • Schapira, A.1    Cooper, J.2    Dexter, D.3
  • 6
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G., Galluzzi L., and Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev 87 (2007) 99-163
    • (2007) Physiol Rev , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 8
    • 0024848034 scopus 로고
    • Abnormalities of the electron transport chain in idiopathic Parkinson's disease
    • Parker Jr. W., Boyson S., and Parks J. Abnormalities of the electron transport chain in idiopathic Parkinson's disease. Ann Neurol 26 (1989) 719-723
    • (1989) Ann Neurol , vol.26 , pp. 719-723
    • Parker Jr., W.1    Boyson, S.2    Parks, J.3
  • 9
    • 0024330311 scopus 로고
    • Deficiencies in complex I subunits of the respiratory chain in Parkinson's disease
    • Mizuno Y., Ohta S., Tanaka M., et al. Deficiencies in complex I subunits of the respiratory chain in Parkinson's disease. Biochem Biophys Res Commun 163 (1989) 1450-1455
    • (1989) Biochem Biophys Res Commun , vol.163 , pp. 1450-1455
    • Mizuno, Y.1    Ohta, S.2    Tanaka, M.3
  • 10
    • 0025640845 scopus 로고
    • Anatomic and disease specificity of NADH CoQ1 reductase (complex I) deficiency in Parkinson's disease
    • Schapira A., Mann V., Cooper J., et al. Anatomic and disease specificity of NADH CoQ1 reductase (complex I) deficiency in Parkinson's disease. J Neurochem 55 (1990) 2142-2145
    • (1990) J Neurochem , vol.55 , pp. 2142-2145
    • Schapira, A.1    Mann, V.2    Cooper, J.3
  • 11
    • 0027995435 scopus 로고
    • Complex I, iron, and ferritin in Parkinson's disease substantia nigra
    • Mann V., Cooper J., Daniel S., et al. Complex I, iron, and ferritin in Parkinson's disease substantia nigra. Ann Neurol 36 (1994) 876-881
    • (1994) Ann Neurol , vol.36 , pp. 876-881
    • Mann, V.1    Cooper, J.2    Daniel, S.3
  • 12
    • 0028316759 scopus 로고
    • Unaltered aconitase activity, but decreased complex I activity in substantia nigra pars compacta of patients with Parkinson's disease
    • Janetzky B., Hauck S., Youdim M., et al. Unaltered aconitase activity, but decreased complex I activity in substantia nigra pars compacta of patients with Parkinson's disease. Neurosci Lett 169 (1994) 126-128
    • (1994) Neurosci Lett , vol.169 , pp. 126-128
    • Janetzky, B.1    Hauck, S.2    Youdim, M.3
  • 13
    • 0026484964 scopus 로고
    • Platelet mitochondrial function in Parkinson's disease. The Royal Kings and Queens Parkinson Disease Research Group
    • Krige D., Carroll M., Cooper J., Marsden C., and Schapira A. Platelet mitochondrial function in Parkinson's disease. The Royal Kings and Queens Parkinson Disease Research Group. Ann Neurol 32 (1992) 782-788
    • (1992) Ann Neurol , vol.32 , pp. 782-788
    • Krige, D.1    Carroll, M.2    Cooper, J.3    Marsden, C.4    Schapira, A.5
  • 14
    • 0029050583 scopus 로고
    • Low platelet mitochondrial complex I and complex II/III activity in early untreated Parkinson's disease
    • Haas R., Nasirian F., Nakano K., et al. Low platelet mitochondrial complex I and complex II/III activity in early untreated Parkinson's disease. Ann Neurol 37 (1995) 714-722
    • (1995) Ann Neurol , vol.37 , pp. 714-722
    • Haas, R.1    Nasirian, F.2    Nakano, K.3
  • 15
    • 0026718086 scopus 로고
    • Brain, skeletal muscle and platelet homogenate mitochondrial function in Parkinson's disease
    • Mann V., Cooper J., Krige D., et al. Brain, skeletal muscle and platelet homogenate mitochondrial function in Parkinson's disease. Brain 115 (1992) 333-342
    • (1992) Brain , vol.115 , pp. 333-342
    • Mann, V.1    Cooper, J.2    Krige, D.3
  • 16
    • 0028170328 scopus 로고
    • 31P magnetic resonance spectroscopy study of mitochondrial function in skeletal muscle of patients with Parkinson's disease
    • 31P magnetic resonance spectroscopy study of mitochondrial function in skeletal muscle of patients with Parkinson's disease. J Neurol Sci 125 (1994) 77-81
    • (1994) J Neurol Sci , vol.125 , pp. 77-81
    • Taylor, D.1    Krige, D.2    Barnes, P.3
  • 17
    • 0029396976 scopus 로고
    • Generalized mitochondrial dysfunction in Parkinson's disease detected by magnetic resonance spectroscopy of muscle
    • Penn A., Roberts T., Hodder J., et al. Generalized mitochondrial dysfunction in Parkinson's disease detected by magnetic resonance spectroscopy of muscle. Neurology 45 (1995) 2097-2099
    • (1995) Neurology , vol.45 , pp. 2097-2099
    • Penn, A.1    Roberts, T.2    Hodder, J.3
  • 18
    • 33646948530 scopus 로고    scopus 로고
    • Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled
    • Keeney P., Xie J., Capaldi R., and Bennett Jr. J. Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. J Neurosci 26 (2006) 5256-5264
    • (2006) J Neurosci , vol.26 , pp. 5256-5264
    • Keeney, P.1    Xie, J.2    Capaldi, R.3    Bennett Jr., J.4
  • 19
    • 30044442094 scopus 로고    scopus 로고
    • Complex I deficiency primes Bax-dependent neuronal apoptosis through mitochondrial oxidative damage
    • Perier C., Tieu K., Guegan C., et al. Complex I deficiency primes Bax-dependent neuronal apoptosis through mitochondrial oxidative damage. Proc Natl Acad Sci USA 102 (2005) 19126-19131
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 19126-19131
    • Perier, C.1    Tieu, K.2    Guegan, C.3
  • 20
    • 0025113789 scopus 로고
    • Increase of deleted mitochondrial DNA in the striatum in Parkinson's disease and senescence
    • Ikebe S., Tanaka M., Ohno K., et al. Increase of deleted mitochondrial DNA in the striatum in Parkinson's disease and senescence. Biochem Biophys Res Commun 170 (1990) 1044-1048
    • (1990) Biochem Biophys Res Commun , vol.170 , pp. 1044-1048
    • Ikebe, S.1    Tanaka, M.2    Ohno, K.3
  • 21
    • 0025010120 scopus 로고
    • Mitochondrial DNA analysis in Parkinson's disease
    • Schapira A., Holt I., Sweeney M., et al. Mitochondrial DNA analysis in Parkinson's disease. Mov Disord 5 (1990) 294-347
    • (1990) Mov Disord , vol.5 , pp. 294-347
    • Schapira, A.1    Holt, I.2    Sweeney, M.3
  • 22
    • 0025793685 scopus 로고
    • Mitochondrial DNA in postmortem brain from patients with Parkinson's disease
    • Lestienne P., Nelson I., Riederer P., Reichmann H., and Jellinger K. Mitochondrial DNA in postmortem brain from patients with Parkinson's disease. J Neurochem 56 (1991) 1819
    • (1991) J Neurochem , vol.56 , pp. 1819
    • Lestienne, P.1    Nelson, I.2    Riederer, P.3    Reichmann, H.4    Jellinger, K.5
  • 23
    • 33646351299 scopus 로고    scopus 로고
    • Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons
    • Kraytsberg Y., Kudryavtseva E., McKee A., et al. Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons. Nat Genet 38 (2006) 518-520
    • (2006) Nat Genet , vol.38 , pp. 518-520
    • Kraytsberg, Y.1    Kudryavtseva, E.2    McKee, A.3
  • 24
    • 33646375711 scopus 로고    scopus 로고
    • High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease
    • Bender A., Krishnan K., Morris C., et al. High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease. Nat Genet 38 (2006) 515-517
    • (2006) Nat Genet , vol.38 , pp. 515-517
    • Bender, A.1    Krishnan, K.2    Morris, C.3
  • 25
    • 0025863393 scopus 로고
    • Distinct clustering of point mutations in mitochondrial DNA among patients with mitochondrial encephalomyopathies and with Parkinson's disease
    • Ozawa T., Tanaka M., Ino H., et al. Distinct clustering of point mutations in mitochondrial DNA among patients with mitochondrial encephalomyopathies and with Parkinson's disease. Biochem Biophys Res Commun 176 (1991) 938-946
    • (1991) Biochem Biophys Res Commun , vol.176 , pp. 938-946
    • Ozawa, T.1    Tanaka, M.2    Ino, H.3
  • 26
    • 0028854722 scopus 로고
    • Point mutations of mitochondrial genome in Parkinson's disease
    • Ikebe S., Tanaka M., and Ozawa T. Point mutations of mitochondrial genome in Parkinson's disease. Brain Res Mol Brain Res 28 (1995) 281-295
    • (1995) Brain Res Mol Brain Res , vol.28 , pp. 281-295
    • Ikebe, S.1    Tanaka, M.2    Ozawa, T.3
  • 27
    • 0027200741 scopus 로고
    • Mitochondrial DNA variants observed in Alzheimer disease and Parkinson disease patients
    • Shoffner J., Brown M., Torroni A., et al. Mitochondrial DNA variants observed in Alzheimer disease and Parkinson disease patients. Genomics 17 (1993) 171-184
    • (1993) Genomics , vol.17 , pp. 171-184
    • Shoffner, J.1    Brown, M.2    Torroni, A.3
  • 28
  • 31
    • 0036297660 scopus 로고    scopus 로고
    • Sequence analysis of the entire mitochondrial genome in Parkinson's disease
    • Vives-Bauza C., Andreu A., Manfredi G., et al. Sequence analysis of the entire mitochondrial genome in Parkinson's disease. Biochem Biophys Res Commun 290 (2002) 1593-1601
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 1593-1601
    • Vives-Bauza, C.1    Andreu, A.2    Manfredi, G.3
  • 32
    • 0037385480 scopus 로고    scopus 로고
    • Mitochondrial polymorphisms significantly reduce the risk of Parkinson disease
    • van der Walt J., Nicodemus K., Martin E., et al. Mitochondrial polymorphisms significantly reduce the risk of Parkinson disease. Am J Hum Genet 72 (2003) 804-811
    • (2003) Am J Hum Genet , vol.72 , pp. 804-811
    • van der Walt, J.1    Nicodemus, K.2    Martin, E.3
  • 33
    • 20144389920 scopus 로고    scopus 로고
    • Mitochondrial DNA haplogroup cluster UKJT reduces the risk of PD
    • Pyle A., Foltynie T., Tiangyou W., et al. Mitochondrial DNA haplogroup cluster UKJT reduces the risk of PD. Ann Neurol 57 (2005) 564-567
    • (2005) Ann Neurol , vol.57 , pp. 564-567
    • Pyle, A.1    Foltynie, T.2    Tiangyou, W.3
  • 34
    • 0037380725 scopus 로고    scopus 로고
    • mt4216C variant in linkage with the mtDNA TJ cluster may confer a susceptibility to mitochondrial dysfunction resulting in an increased risk of Parkinson's disease in the Irish
    • Ross O., McCormack R., Maxwell L., et al. mt4216C variant in linkage with the mtDNA TJ cluster may confer a susceptibility to mitochondrial dysfunction resulting in an increased risk of Parkinson's disease in the Irish. Exp Gerontol 38 (2003) 397-405
    • (2003) Exp Gerontol , vol.38 , pp. 397-405
    • Ross, O.1    McCormack, R.2    Maxwell, L.3
  • 35
    • 33748087125 scopus 로고    scopus 로고
    • Identification of mitochondrial DNA polymorphisms that alter mitochondrial matrix pH and intracellular calcium dynamics
    • Kazuno A., Munakata K., Nagai T., et al. Identification of mitochondrial DNA polymorphisms that alter mitochondrial matrix pH and intracellular calcium dynamics. PLoS Genet 2 (2006) e128
    • (2006) PLoS Genet , vol.2
    • Kazuno, A.1    Munakata, K.2    Nagai, T.3
  • 36
    • 0029908226 scopus 로고    scopus 로고
    • Origin and functional consequences of the complex I defect in Parkinson's disease
    • Swerdlow R., Parks J., Miller S., et al. Origin and functional consequences of the complex I defect in Parkinson's disease. Ann Neurol 40 (1996) 663-671
    • (1996) Ann Neurol , vol.40 , pp. 663-671
    • Swerdlow, R.1    Parks, J.2    Miller, S.3
  • 37
    • 0031859395 scopus 로고    scopus 로고
    • Mitochondrial DNA transmission of the mitochondrial defect in Parkinson's disease
    • Gu M., Cooper J., Taanman J., and Schapira A. Mitochondrial DNA transmission of the mitochondrial defect in Parkinson's disease. Ann Neurol 44 (1998) 177-186
    • (1998) Ann Neurol , vol.44 , pp. 177-186
    • Gu, M.1    Cooper, J.2    Taanman, J.3    Schapira, A.4
  • 38
    • 0033768121 scopus 로고    scopus 로고
    • A novel mitochondrial 12SrRNA point mutation in parkinsonism, deafness, and neuropathy
    • Thyagarajan D., Bressman S., Bruno C., et al. A novel mitochondrial 12SrRNA point mutation in parkinsonism, deafness, and neuropathy. Ann Neurol 48 (2000) 730-736
    • (2000) Ann Neurol , vol.48 , pp. 730-736
    • Thyagarajan, D.1    Bressman, S.2    Bruno, C.3
  • 39
    • 0033767317 scopus 로고    scopus 로고
    • An out-of-frame cytochrome b gene deletion from a patient with parkinsonism is associated with impaired complex III assembly and an increase in free radical production
    • Rana M., de C., Diaz F., Smeets H., and Moraes C. An out-of-frame cytochrome b gene deletion from a patient with parkinsonism is associated with impaired complex III assembly and an increase in free radical production. Ann Neurol 48 (2000) 774-781
    • (2000) Ann Neurol , vol.48 , pp. 774-781
    • Rana, M.1    de, C.2    Diaz, F.3    Smeets, H.4    Moraes, C.5
  • 40
    • 10444243239 scopus 로고    scopus 로고
    • Mitochondrial ND5 mutations in idiopathic Parkinson's disease
    • Parker Jr. W., and Parks J. Mitochondrial ND5 mutations in idiopathic Parkinson's disease. Biochem Biophys Res Commun 326 (2005) 667-669
    • (2005) Biochem Biophys Res Commun , vol.326 , pp. 667-669
    • Parker Jr., W.1    Parks, J.2
  • 41
    • 33846636481 scopus 로고    scopus 로고
    • Progressive parkinsonism in mice with respiratory-chain-deficient dopamine neurons
    • Ekstrand M., Terzioglu M., Galter D., et al. Progressive parkinsonism in mice with respiratory-chain-deficient dopamine neurons. Proc Natl Acad Sci USA 104 (2007) 1325-1330
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1325-1330
    • Ekstrand, M.1    Terzioglu, M.2    Galter, D.3
  • 42
    • 0034943022 scopus 로고    scopus 로고
    • Parkin is associated with cellular vesicles
    • Kubo S., Kitami T., Noda S., et al. Parkin is associated with cellular vesicles. J Neurochem 78 (2001) 42-54
    • (2001) J Neurochem , vol.78 , pp. 42-54
    • Kubo, S.1    Kitami, T.2    Noda, S.3
  • 43
    • 0032957883 scopus 로고    scopus 로고
    • Immunohistochemical and subcellular localization of parkin protein: absence of protein in autosomal recessive juvenile parkinsonism patients
    • Shimura H., Hattori N., Kubo S., et al. Immunohistochemical and subcellular localization of parkin protein: absence of protein in autosomal recessive juvenile parkinsonism patients. Ann Neurol 45 (1999) 668-672
    • (1999) Ann Neurol , vol.45 , pp. 668-672
    • Shimura, H.1    Hattori, N.2    Kubo, S.3
  • 44
    • 0034515773 scopus 로고    scopus 로고
    • Parkin expression in the adult mouse brain
    • Stichel C., Augustin M., Kuhn K., et al. Parkin expression in the adult mouse brain. Eur J Neurosci 12 (2000) 4181-4194
    • (2000) Eur J Neurosci , vol.12 , pp. 4181-4194
    • Stichel, C.1    Augustin, M.2    Kuhn, K.3
  • 45
    • 0033933048 scopus 로고    scopus 로고
    • Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
    • Shimura H., Hattori N., Kubo S., et al. Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet 25 (2000) 302-305
    • (2000) Nat Genet , vol.25 , pp. 302-305
    • Shimura, H.1    Hattori, N.2    Kubo, S.3
  • 46
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • Zhang Y., Gao J., Chung K., et al. Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc Natl Acad Sci USA 97 (2000) 13354-13359
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.3
  • 47
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai Y., Soda M., Inoue H., et al. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105 (2001) 891-902
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3
  • 48
    • 13544266179 scopus 로고    scopus 로고
    • Parkin phosphorylation and modulation of its E3 ubiquitin ligase activity
    • Yamamoto A., Friedlein A., Imai Y., et al. Parkin phosphorylation and modulation of its E3 ubiquitin ligase activity. J Biol Chem 280 (2005) 3390-3399
    • (2005) J Biol Chem , vol.280 , pp. 3390-3399
    • Yamamoto, A.1    Friedlein, A.2    Imai, Y.3
  • 49
    • 2542534741 scopus 로고    scopus 로고
    • S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function
    • Chung K., Thomas B., Li X., et al. S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science 304 (2004) 1328-1331
    • (2004) Science , vol.304 , pp. 1328-1331
    • Chung, K.1    Thomas, B.2    Li, X.3
  • 50
    • 33644778845 scopus 로고    scopus 로고
    • Parkin enhances mitochondrial biogenesis in proliferating cells
    • Kuroda Y., Mitsui T., Kunishige M., et al. Parkin enhances mitochondrial biogenesis in proliferating cells. Hum Mol Genet 15 (2006) 883-895
    • (2006) Hum Mol Genet , vol.15 , pp. 883-895
    • Kuroda, Y.1    Mitsui, T.2    Kunishige, M.3
  • 51
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T., Asakawa S., Hattori N., et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392 (1998) 605-608
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3
  • 52
    • 0342368772 scopus 로고    scopus 로고
    • Association between early-onset Parkinson's disease and mutations in the parkin gene
    • Lucking C., Durr A., Bonifati V., et al. Association between early-onset Parkinson's disease and mutations in the parkin gene. N Engl J Med 342 (2000) 1560-1567
    • (2000) N Engl J Med , vol.342 , pp. 1560-1567
    • Lucking, C.1    Durr, A.2    Bonifati, V.3
  • 53
    • 0034848395 scopus 로고    scopus 로고
    • Lewy bodies and parkinsonism in families with parkin mutations
    • Farrer M., Chan P., Chen R., et al. Lewy bodies and parkinsonism in families with parkin mutations. Ann Neurol 50 (2001) 293-300
    • (2001) Ann Neurol , vol.50 , pp. 293-300
    • Farrer, M.1    Chan, P.2    Chen, R.3
  • 54
    • 0042415580 scopus 로고    scopus 로고
    • How much phenotypic variation can be attributed to parkin genotype?
    • for the French Parkinson's Disease Genetics Study Group. European Consortium on Genetic Susceptibility in Parkinson's Disease
    • Lohmann E., Periquet M., Bonifati V., et al., for the French Parkinson's Disease Genetics Study Group, European Consortium on Genetic Susceptibility in Parkinson's Disease. How much phenotypic variation can be attributed to parkin genotype?. Ann Neurol 54 (2003) 176-185
    • (2003) Ann Neurol , vol.54 , pp. 176-185
    • Lohmann, E.1    Periquet, M.2    Bonifati, V.3
  • 55
    • 24644462201 scopus 로고    scopus 로고
    • Lewy body Parkinson's disease in a large pedigree with 77 Parkin mutation carriers
    • Pramstaller P., Schlossmacher M., Jacques T., et al. Lewy body Parkinson's disease in a large pedigree with 77 Parkin mutation carriers. Ann Neurol 58 (2005) 411-422
    • (2005) Ann Neurol , vol.58 , pp. 411-422
    • Pramstaller, P.1    Schlossmacher, M.2    Jacques, T.3
  • 56
    • 0033814671 scopus 로고    scopus 로고
    • An autopsy case of autosomal-recessive juvenile parkinsonism with a homozygous exon 4 deletion in the parkin gene
    • Hayashi S., Wakabayashi K., Ishikawa A., et al. An autopsy case of autosomal-recessive juvenile parkinsonism with a homozygous exon 4 deletion in the parkin gene. Mov Disord 15 (2000) 884-888
    • (2000) Mov Disord , vol.15 , pp. 884-888
    • Hayashi, S.1    Wakabayashi, K.2    Ishikawa, A.3
  • 57
    • 0141891953 scopus 로고    scopus 로고
    • Parkin-deficient mice exhibit nigrostriatal deficits but not loss of dopaminergic neurons
    • Goldberg M., Fleming S., Palacino J., et al. Parkin-deficient mice exhibit nigrostriatal deficits but not loss of dopaminergic neurons. J Biol Chem 278 (2003) 43628-43635
    • (2003) J Biol Chem , vol.278 , pp. 43628-43635
    • Goldberg, M.1    Fleming, S.2    Palacino, J.3
  • 58
    • 2442481789 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative damage in parkin-deficient mice
    • Palacino J., Sagi D., Goldberg M., et al. Mitochondrial dysfunction and oxidative damage in parkin-deficient mice. J Biol Chem 279 (2004) 18614-18622
    • (2004) J Biol Chem , vol.279 , pp. 18614-18622
    • Palacino, J.1    Sagi, D.2    Goldberg, M.3
  • 59
    • 33646114508 scopus 로고    scopus 로고
    • Susceptibility to rotenone is increased in neurons from parkin null mice and is reduced by minocycline
    • Casarejos M., Menendez J., Solano R., et al. Susceptibility to rotenone is increased in neurons from parkin null mice and is reduced by minocycline. J Neurochem 97 (2006) 934-946
    • (2006) J Neurochem , vol.97 , pp. 934-946
    • Casarejos, M.1    Menendez, J.2    Solano, R.3
  • 60
    • 0037386532 scopus 로고    scopus 로고
    • Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants
    • Greene J., Whitworth A., Kuo I., et al. Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants. Proc Natl Acad Sci USA 100 (2003) 4078-4083
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4078-4083
    • Greene, J.1    Whitworth, A.2    Kuo, I.3
  • 61
    • 4544326057 scopus 로고    scopus 로고
    • Mitochondrial complex I and IV activities in leukocytes from patients with parkin mutations
    • Muftuoglu M., Elibol B., Dalmizrak O., et al. Mitochondrial complex I and IV activities in leukocytes from patients with parkin mutations. Mov Disord 19 (2004) 544-548
    • (2004) Mov Disord , vol.19 , pp. 544-548
    • Muftuoglu, M.1    Elibol, B.2    Dalmizrak, O.3
  • 62
    • 27944444154 scopus 로고    scopus 로고
    • Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism
    • Silvestri L., Caputo V., Bellacchio E., et al. Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism. Hum Mol Genet 14 (2005) 3477-3492
    • (2005) Hum Mol Genet , vol.14 , pp. 3477-3492
    • Silvestri, L.1    Caputo, V.2    Bellacchio, E.3
  • 63
    • 0035958558 scopus 로고    scopus 로고
    • Growth-suppressive effects of BPOZ and EGR2, two genes involved in the PTEN signaling pathway
    • Unoki M., and Nakamura Y. Growth-suppressive effects of BPOZ and EGR2, two genes involved in the PTEN signaling pathway. Oncogene 20 (2001) 4457-4465
    • (2001) Oncogene , vol.20 , pp. 4457-4465
    • Unoki, M.1    Nakamura, Y.2
  • 64
    • 0242321145 scopus 로고    scopus 로고
    • BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential
    • Nakajima A., Kataoka K., Hong M., Sakaguchi M., and Huh N. BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential. Cancer Lett 201 (2003) 195-201
    • (2003) Cancer Lett , vol.201 , pp. 195-201
    • Nakajima, A.1    Kataoka, K.2    Hong, M.3    Sakaguchi, M.4    Huh, N.5
  • 65
    • 33847019962 scopus 로고    scopus 로고
    • Mitochondrial translation initiation factor 3 gene polymorphism associated with Parkinson's disease
    • Abahuni N., Gispert S., Bauer P., et al. Mitochondrial translation initiation factor 3 gene polymorphism associated with Parkinson's disease. Neurosci Lett 414 (2007) 126-129
    • (2007) Neurosci Lett , vol.414 , pp. 126-129
    • Abahuni, N.1    Gispert, S.2    Bauer, P.3
  • 66
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • Valente E., Abou-Sleiman P., Caputo V., et al. Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304 (2004) 1158-1160
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.1    Abou-Sleiman, P.2    Caputo, V.3
  • 67
    • 4444274910 scopus 로고    scopus 로고
    • PINK1 mutations are associated with sporadic early-onset parkinsonism
    • Valente E., Salvi S., Ialongo T., et al. PINK1 mutations are associated with sporadic early-onset parkinsonism. Ann Neurol 56 (2004) 336-341
    • (2004) Ann Neurol , vol.56 , pp. 336-341
    • Valente, E.1    Salvi, S.2    Ialongo, T.3
  • 68
    • 4444237208 scopus 로고    scopus 로고
    • Novel PINK1 mutations in early-onset parkinsonism
    • Hatano Y., Li Y., Sato K., et al. Novel PINK1 mutations in early-onset parkinsonism. Ann Neurol 56 (2004) 424-427
    • (2004) Ann Neurol , vol.56 , pp. 424-427
    • Hatano, Y.1    Li, Y.2    Sato, K.3
  • 69
    • 4444269012 scopus 로고    scopus 로고
    • Homozygous PINK1 C-terminus mutation causing early-onset parkinsonism
    • Rohe C., Montagna P., Breedveld G., et al. Homozygous PINK1 C-terminus mutation causing early-onset parkinsonism. Ann Neurol 56 (2004) 427-431
    • (2004) Ann Neurol , vol.56 , pp. 427-431
    • Rohe, C.1    Montagna, P.2    Breedveld, G.3
  • 70
    • 17644365438 scopus 로고    scopus 로고
    • Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
    • Beilina A., Van Der B., Ahmad R., et al. Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc Natl Acad Sci USA 102 (2005) 5703-5708
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5703-5708
    • Beilina, A.1    Van Der, B.2    Ahmad, R.3
  • 71
    • 33745087689 scopus 로고    scopus 로고
    • PINK1 protein in normal human brain and Parkinson's disease
    • Gandhi S., Muqit M., Stanyer L., et al. PINK1 protein in normal human brain and Parkinson's disease. Brain 129 (2006) 1720-1731
    • (2006) Brain , vol.129 , pp. 1720-1731
    • Gandhi, S.1    Muqit, M.2    Stanyer, L.3
  • 72
    • 33745068109 scopus 로고    scopus 로고
    • Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress
    • Muqit M., Abou-Sleiman P., Saurin A., et al. Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress. J Neurochem 98 (2006) 156-169
    • (2006) J Neurochem , vol.98 , pp. 156-169
    • Muqit, M.1    Abou-Sleiman, P.2    Saurin, A.3
  • 73
    • 4444375576 scopus 로고    scopus 로고
    • The gene responsible for PARK6 Parkinson's disease, PINK1, does not influence common forms of parkinsonism
    • Healy D., Abou-Sleiman P., Ahmadi K., et al. The gene responsible for PARK6 Parkinson's disease, PINK1, does not influence common forms of parkinsonism. Ann Neurol 56 (2004) 329-335
    • (2004) Ann Neurol , vol.56 , pp. 329-335
    • Healy, D.1    Abou-Sleiman, P.2    Ahmadi, K.3
  • 74
    • 7944221966 scopus 로고    scopus 로고
    • Genetic association study of PINK1 coding polymorphisms in Parkinson's disease
    • Groen J., Kawarai T., Toulina A., et al. Genetic association study of PINK1 coding polymorphisms in Parkinson's disease. Neurosci Lett 372 (2004) 226-229
    • (2004) Neurosci Lett , vol.372 , pp. 226-229
    • Groen, J.1    Kawarai, T.2    Toulina, A.3
  • 75
    • 33745099053 scopus 로고    scopus 로고
    • Clinical spectrum of homozygous and heterozygous PINK1 mutations in a large German family with Parkinson disease: role of a single hit?
    • Hedrich K., Hagenah J., Djarmati A., et al. Clinical spectrum of homozygous and heterozygous PINK1 mutations in a large German family with Parkinson disease: role of a single hit?. Arch Neurol 63 (2006) 833-838
    • (2006) Arch Neurol , vol.63 , pp. 833-838
    • Hedrich, K.1    Hagenah, J.2    Djarmati, A.3
  • 76
    • 22044432781 scopus 로고    scopus 로고
    • Early-onset parkinsonism associated with PINK1 mutations: frequency, genotypes, and phenotypes
    • Bonifati V., Rohe C., Breedveld G., et al. Early-onset parkinsonism associated with PINK1 mutations: frequency, genotypes, and phenotypes. Neurology 65 (2005) 87-95
    • (2005) Neurology , vol.65 , pp. 87-95
    • Bonifati, V.1    Rohe, C.2    Breedveld, G.3
  • 77
    • 10044275502 scopus 로고    scopus 로고
    • Analysis of the PINK1 gene in a large cohort of cases with Parkinson disease
    • Rogaeva E., Johnson J., Lang A., et al. Analysis of the PINK1 gene in a large cohort of cases with Parkinson disease. Arch Neurol 61 (2004) 1898-1904
    • (2004) Arch Neurol , vol.61 , pp. 1898-1904
    • Rogaeva, E.1    Johnson, J.2    Lang, A.3
  • 78
    • 33847622175 scopus 로고    scopus 로고
    • Biological effects of the PINK1 c.1366C>T mutation: implications in Parkinson disease pathogenesis
    • Grunewald A., Breedveld G., Lohmann-Hedrich K., et al. Biological effects of the PINK1 c.1366C>T mutation: implications in Parkinson disease pathogenesis. Neurogenetics 8 (2007) 103-109
    • (2007) Neurogenetics , vol.8 , pp. 103-109
    • Grunewald, A.1    Breedveld, G.2    Lohmann-Hedrich, K.3
  • 79
    • 33745845523 scopus 로고    scopus 로고
    • PINK1 mutations in sporadic early-onset Parkinson's disease
    • Tan E., Yew K., Chua E., et al. PINK1 mutations in sporadic early-onset Parkinson's disease. Mov Disord 21 (2006) 789-793
    • (2006) Mov Disord , vol.21 , pp. 789-793
    • Tan, E.1    Yew, K.2    Chua, E.3
  • 80
    • 33750598457 scopus 로고    scopus 로고
    • A heterozygous effect for PINK1 mutations in Parkinson's disease?
    • Abou-Sleiman P., Muqit M., McDonald N., et al. A heterozygous effect for PINK1 mutations in Parkinson's disease?. Ann Neurol 60 (2006) 414-419
    • (2006) Ann Neurol , vol.60 , pp. 414-419
    • Abou-Sleiman, P.1    Muqit, M.2    McDonald, N.3
  • 82
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • Park J., Lee S., Lee S., et al. Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441 (2006) 1157-1161
    • (2006) Nature , vol.441 , pp. 1157-1161
    • Park, J.1    Lee, S.2    Lee, S.3
  • 83
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • Clark I., Dodson M., Jiang C., et al. Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441 (2006) 1162-1166
    • (2006) Nature , vol.441 , pp. 1162-1166
    • Clark, I.1    Dodson, M.2    Jiang, C.3
  • 84
    • 24944534660 scopus 로고    scopus 로고
    • Mitochondrial localization of the Parkinson's disease related protein DJ-1: implications for pathogenesis
    • Zhang L., Shimoji M., Thomas B., et al. Mitochondrial localization of the Parkinson's disease related protein DJ-1: implications for pathogenesis. Hum Mol Genet 14 (2005) 2063-2073
    • (2005) Hum Mol Genet , vol.14 , pp. 2063-2073
    • Zhang, L.1    Shimoji, M.2    Thomas, B.3
  • 85
    • 0031566231 scopus 로고    scopus 로고
    • DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras
    • Nagakubo D., Taira T., Kitaura H., et al. DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras. Biochem Biophys Res Commun 231 (1997) 509-513
    • (1997) Biochem Biophys Res Commun , vol.231 , pp. 509-513
    • Nagakubo, D.1    Taira, T.2    Kitaura, H.3
  • 86
    • 0035813135 scopus 로고    scopus 로고
    • DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor
    • Takahashi K., Taira T., Niki T., et al. DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor. J Biol Chem 276 (2001) 37556-37563
    • (2001) J Biol Chem , vol.276 , pp. 37556-37563
    • Takahashi, K.1    Taira, T.2    Niki, T.3
  • 87
    • 1642527499 scopus 로고    scopus 로고
    • DJ-1 has a role in antioxidative stress to prevent cell death
    • Taira T., Saito Y., Niki T., et al. DJ-1 has a role in antioxidative stress to prevent cell death. EMBO Rep 5 (2004) 213-218
    • (2004) EMBO Rep , vol.5 , pp. 213-218
    • Taira, T.1    Saito, Y.2    Niki, T.3
  • 88
    • 2942684871 scopus 로고    scopus 로고
    • The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization
    • Canet-Aviles R., Wilson M., Miller D., et al. The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization. Proc Natl Acad Sci USA 101 (2004) 9103-9108
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9103-9108
    • Canet-Aviles, R.1    Wilson, M.2    Miller, D.3
  • 89
    • 10744224738 scopus 로고    scopus 로고
    • The expression of DJ-1 (PARK7) in normal human CNS and idiopathic Parkinson's disease
    • Bandopadhyay R., Kingsbury A., Cookson M., et al. The expression of DJ-1 (PARK7) in normal human CNS and idiopathic Parkinson's disease. Brain 127 (2004) 420-430
    • (2004) Brain , vol.127 , pp. 420-430
    • Bandopadhyay, R.1    Kingsbury, A.2    Cookson, M.3
  • 90
    • 0345357664 scopus 로고    scopus 로고
    • Down regulation of DJ-1 enhances cell death by oxidative stress, ER stress, and proteasome inhibition
    • Yokota T., Sugawara K., Ito K., et al. Down regulation of DJ-1 enhances cell death by oxidative stress, ER stress, and proteasome inhibition. Biochem Biophys Res Commun 312 (2003) 1342-1348
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 1342-1348
    • Yokota, T.1    Sugawara, K.2    Ito, K.3
  • 91
    • 0037428241 scopus 로고    scopus 로고
    • Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism
    • Bonifati V., Rizzu P., van Baren M., et al. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 299 (2003) 256-259
    • (2003) Science , vol.299 , pp. 256-259
    • Bonifati, V.1    Rizzu, P.2    van Baren, M.3
  • 92
    • 20944437573 scopus 로고    scopus 로고
    • The Parkinson's disease-associated DJ-1 protein is a transcriptional co-activator that protects against neuronal apoptosis
    • Xu J., Zhong N., Wang H., et al. The Parkinson's disease-associated DJ-1 protein is a transcriptional co-activator that protects against neuronal apoptosis. Hum Mol Genet 14 (2005) 1231-1241
    • (2005) Hum Mol Genet , vol.14 , pp. 1231-1241
    • Xu, J.1    Zhong, N.2    Wang, H.3
  • 93
    • 13944267769 scopus 로고    scopus 로고
    • DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation
    • Shendelman S., Jonason A., Martinat C., Leete T., and Abeliovich A. DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation. PLoS Biol 2 (2004) e362
    • (2004) PLoS Biol , vol.2
    • Shendelman, S.1    Jonason, A.2    Martinat, C.3    Leete, T.4    Abeliovich, A.5
  • 94
    • 33744760852 scopus 로고    scopus 로고
    • Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease
    • Tang B., Xiong H., Sun P., et al. Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease. Hum Mol Genet 15 (2006) 1816-1825
    • (2006) Hum Mol Genet , vol.15 , pp. 1816-1825
    • Tang, B.1    Xiong, H.2    Sun, P.3
  • 95
    • 13844253723 scopus 로고    scopus 로고
    • Nigrostriatal dopaminergic deficits and hypokinesia caused by inactivation of the familial Parkinsonism-linked gene DJ-1
    • Goldberg M., Pisani A., Haburcak M., et al. Nigrostriatal dopaminergic deficits and hypokinesia caused by inactivation of the familial Parkinsonism-linked gene DJ-1. Neuron 45 (2005) 489-496
    • (2005) Neuron , vol.45 , pp. 489-496
    • Goldberg, M.1    Pisani, A.2    Haburcak, M.3
  • 96
    • 33745163261 scopus 로고    scopus 로고
    • Enhanced sensitivity of DJ-1-deficient dopaminergic neurons to energy metabolism impairment: role of Na+/K+ ATPase
    • Pisani A., Martella G., Tscherter A., et al. Enhanced sensitivity of DJ-1-deficient dopaminergic neurons to energy metabolism impairment: role of Na+/K+ ATPase. Neurobiol Dis 23 (2006) 54-60
    • (2006) Neurobiol Dis , vol.23 , pp. 54-60
    • Pisani, A.1    Martella, G.2    Tscherter, A.3
  • 97
    • 20144389422 scopus 로고    scopus 로고
    • Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6- tetrahydropyrindine (MPTP) and oxidative stress
    • Kim R., Smith P., Aleyasin H., et al. Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6- tetrahydropyrindine (MPTP) and oxidative stress. Proc Natl Acad Sci USA 102 (2005) 5215-5220
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5215-5220
    • Kim, R.1    Smith, P.2    Aleyasin, H.3
  • 98
    • 0042922454 scopus 로고    scopus 로고
    • Clinical and genetic heterogeneity in progressive external ophthalmoplegia due to mutations in polymerase gamma
    • Filosto M., Mancuso M., Nishigaki Y., et al. Clinical and genetic heterogeneity in progressive external ophthalmoplegia due to mutations in polymerase gamma. Arch Neurol 60 (2003) 1279-1284
    • (2003) Arch Neurol , vol.60 , pp. 1279-1284
    • Filosto, M.1    Mancuso, M.2    Nishigaki, Y.3
  • 99
    • 33745410626 scopus 로고    scopus 로고
    • Mitochondrial disease
    • Schapira A. Mitochondrial disease. Lancet 368 (2006) 70-82
    • (2006) Lancet , vol.368 , pp. 70-82
    • Schapira, A.1
  • 100
    • 4544273256 scopus 로고    scopus 로고
    • Parkinsonism, premature menopause, and mitochondrial DNA polymerase gamma mutations: clinical and molecular genetic study
    • Luoma P., Melberg A., Rinne J., et al. Parkinsonism, premature menopause, and mitochondrial DNA polymerase gamma mutations: clinical and molecular genetic study. Lancet 364 (2004) 875-882
    • (2004) Lancet , vol.364 , pp. 875-882
    • Luoma, P.1    Melberg, A.2    Rinne, J.3
  • 101
    • 33646358693 scopus 로고    scopus 로고
    • Early-onset familial parkinsonism due to POLG mutations
    • Davidzon G., Greene P., Mancuso M., et al. Early-onset familial parkinsonism due to POLG mutations. Ann Neurol 59 (2006) 859-862
    • (2006) Ann Neurol , vol.59 , pp. 859-862
    • Davidzon, G.1    Greene, P.2    Mancuso, M.3
  • 102
    • 3543017697 scopus 로고    scopus 로고
    • A novel polymerase gamma mutation in a family with ophthalmoplegia, neuropathy, and Parkinsonism
    • Mancuso M., Filosto M., Oh S., and DiMauro S. A novel polymerase gamma mutation in a family with ophthalmoplegia, neuropathy, and Parkinsonism. Arch Neurol 61 (2004) 1777-1779
    • (2004) Arch Neurol , vol.61 , pp. 1777-1779
    • Mancuso, M.1    Filosto, M.2    Oh, S.3    DiMauro, S.4
  • 103
    • 13444270783 scopus 로고    scopus 로고
    • Analysis of the trinucleotide CAG repeat from the DNA polymerase gamma gene (POLG) in patients with Parkinson's disease
    • Taanman J., and Schapira A. Analysis of the trinucleotide CAG repeat from the DNA polymerase gamma gene (POLG) in patients with Parkinson's disease. Neurosci Lett 376 (2005) 56-59
    • (2005) Neurosci Lett , vol.376 , pp. 56-59
    • Taanman, J.1    Schapira, A.2
  • 104
    • 34247122280 scopus 로고    scopus 로고
    • Mutation of the linker region of the polymerase gamma-1 (POLG1) gene associated with progressive external ophthalmoplegia and Parkinsonism
    • Hudson G., Schaefer A., Taylor R., et al. Mutation of the linker region of the polymerase gamma-1 (POLG1) gene associated with progressive external ophthalmoplegia and Parkinsonism. Arch Neurol 64 (2007) 553-557
    • (2007) Arch Neurol , vol.64 , pp. 553-557
    • Hudson, G.1    Schaefer, A.2    Taylor, R.3
  • 105
    • 7644230386 scopus 로고    scopus 로고
    • Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice
    • Martins L., Morrison A., Klupsch K., et al. Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice. Mol Cell Biol 24 (2004) 9848-9862
    • (2004) Mol Cell Biol , vol.24 , pp. 9848-9862
    • Martins, L.1    Morrison, A.2    Klupsch, K.3
  • 106
    • 25444498785 scopus 로고    scopus 로고
    • Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease
    • Strauss K., Martins L., Plun-Favreau H., et al. Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease. Hum Mol Genet 14 (2005) 2099-2111
    • (2005) Hum Mol Genet , vol.14 , pp. 2099-2111
    • Strauss, K.1    Martins, L.2    Plun-Favreau, H.3
  • 107
    • 35748935851 scopus 로고    scopus 로고
    • The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1
    • Plun-Favreau H., Klupsch K., Moisoi N., et al. The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1. Nat Cell Biol 9 (2007) 1243-1252
    • (2007) Nat Cell Biol , vol.9 , pp. 1243-1252
    • Plun-Favreau, H.1    Klupsch, K.2    Moisoi, N.3
  • 108
    • 17844406856 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
    • Chen L., and Feany M. Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease. Nat Neurosci 8 (2005) 657-663
    • (2005) Nat Neurosci , vol.8 , pp. 657-663
    • Chen, L.1    Feany, M.2
  • 109
    • 0033890821 scopus 로고    scopus 로고
    • Alpha-synuclein promotes mitochondrial deficit and oxidative stress
    • Hsu L., Sagara Y., Arroyo A., et al. Alpha-synuclein promotes mitochondrial deficit and oxidative stress. Am J Pathol 157 (2000) 401-410
    • (2000) Am J Pathol , vol.157 , pp. 401-410
    • Hsu, L.1    Sagara, Y.2    Arroyo, A.3
  • 110
    • 0034326816 scopus 로고    scopus 로고
    • Expression of mutant alpha-synuclein causes increased susceptibility to dopamine toxicity
    • Tabrizi S., Orth M., Wilkinson J., et al. Expression of mutant alpha-synuclein causes increased susceptibility to dopamine toxicity. Hum Mol Genet 9 (2000) 2683-2689
    • (2000) Hum Mol Genet , vol.9 , pp. 2683-2689
    • Tabrizi, S.1    Orth, M.2    Wilkinson, J.3
  • 111
    • 0034077041 scopus 로고    scopus 로고
    • Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system
    • Abeliovich A., Schmitz Y., Farinas I., et al. Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system. Neuron 25 (2000) 239-252
    • (2000) Neuron , vol.25 , pp. 239-252
    • Abeliovich, A.1    Schmitz, Y.2    Farinas, I.3
  • 112
    • 3042541863 scopus 로고    scopus 로고
    • G209A mutant alpha synuclein expression specifically enhances dopamine induced oxidative damage
    • Orth M., Tabrizi S., Tomlinson C., et al. G209A mutant alpha synuclein expression specifically enhances dopamine induced oxidative damage. Neurochem Int 45 (2004) 669-676
    • (2004) Neurochem Int , vol.45 , pp. 669-676
    • Orth, M.1    Tabrizi, S.2    Tomlinson, C.3
  • 113
    • 0037173006 scopus 로고    scopus 로고
    • Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala-53→Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice
    • Lee M., Stirling W., Xu Y., et al. Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala-53→Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice. Proc Natl Acad Sci USA 99 (2002) 8968-8973
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8968-8973
    • Lee, M.1    Stirling, W.2    Xu, Y.3
  • 114
    • 30644471051 scopus 로고    scopus 로고
    • Parkinson's disease alpha-synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death
    • Martin L., Pan Y., Price A., et al. Parkinson's disease alpha-synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death. J Neurosci 26 (2006) 41-50
    • (2006) J Neurosci , vol.26 , pp. 41-50
    • Martin, L.1    Pan, Y.2    Price, A.3
  • 115
    • 33244460534 scopus 로고    scopus 로고
    • Mice lacking alpha-synuclein are resistant to mitochondrial toxins
    • Klivenyi P., Siwek D., Gardian G., et al. Mice lacking alpha-synuclein are resistant to mitochondrial toxins. Neurobiol Dis 21 (2006) 541-548
    • (2006) Neurobiol Dis , vol.21 , pp. 541-548
    • Klivenyi, P.1    Siwek, D.2    Gardian, G.3
  • 116
    • 0037195109 scopus 로고    scopus 로고
    • Resistance of alpha-synuclein null mice to the parkinsonian neurotoxin MPTP
    • Dauer W., Kholodilov N., Vila M., et al. Resistance of alpha-synuclein null mice to the parkinsonian neurotoxin MPTP. Proc Natl Acad Sci USA 99 (2002) 14524-14529
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14524-14529
    • Dauer, W.1    Kholodilov, N.2    Vila, M.3
  • 117
    • 33947513592 scopus 로고    scopus 로고
    • Pesticide exposure exacerbates alpha-synucleinopathy in an A53T transgenic mouse model
    • Norris E., Uryu K., Leight S., et al. Pesticide exposure exacerbates alpha-synucleinopathy in an A53T transgenic mouse model. Am J Pathol 170 (2007) 658-666
    • (2007) Am J Pathol , vol.170 , pp. 658-666
    • Norris, E.1    Uryu, K.2    Leight, S.3
  • 118
    • 24644497562 scopus 로고    scopus 로고
    • LRRK2 mutations in Parkinson disease
    • Farrer M., Stone J., Mata I., et al. LRRK2 mutations in Parkinson disease. Neurology 65 (2005) 738-740
    • (2005) Neurology , vol.65 , pp. 738-740
    • Farrer, M.1    Stone, J.2    Mata, I.3
  • 119
    • 19944432921 scopus 로고    scopus 로고
    • A common LRRK2 mutation in idiopathic Parkinson's disease
    • Gilks W., Abou-Sleiman P., Gandhi S., et al. A common LRRK2 mutation in idiopathic Parkinson's disease. Lancet 365 (2005) 415-416
    • (2005) Lancet , vol.365 , pp. 415-416
    • Gilks, W.1    Abou-Sleiman, P.2    Gandhi, S.3
  • 120
    • 24644486896 scopus 로고    scopus 로고
    • A clinic-based study of the LRRK2 gene in Parkinson disease yields new mutations
    • Zabetian C., Samii A., Mosley A., et al. A clinic-based study of the LRRK2 gene in Parkinson disease yields new mutations. Neurology 65 (2005) 741-744
    • (2005) Neurology , vol.65 , pp. 741-744
    • Zabetian, C.1    Samii, A.2    Mosley, A.3
  • 121
    • 20444414834 scopus 로고    scopus 로고
    • Genetic and clinical identification of Parkinson's disease patients with LRRK2 G2019S mutation
    • Deng H., Le W., Guo Y., et al. Genetic and clinical identification of Parkinson's disease patients with LRRK2 G2019S mutation. Ann Neurol 57 (2005) 933-934
    • (2005) Ann Neurol , vol.57 , pp. 933-934
    • Deng, H.1    Le, W.2    Guo, Y.3
  • 122
    • 19944431081 scopus 로고    scopus 로고
    • A frequent LRRK2 gene mutation associated with autosomal dominant Parkinson's disease
    • Di Fonzo A., Rohe C., Ferreira J., et al. A frequent LRRK2 gene mutation associated with autosomal dominant Parkinson's disease. Lancet 365 (2005) 412-415
    • (2005) Lancet , vol.365 , pp. 412-415
    • Di Fonzo, A.1    Rohe, C.2    Ferreira, J.3
  • 123
    • 20144387207 scopus 로고    scopus 로고
    • Identification of a novel LRRK2 mutation linked to autosomal dominant parkinsonism: evidence of a common founder across European populations
    • Kachergus J., Mata I., Hulihan M., et al. Identification of a novel LRRK2 mutation linked to autosomal dominant parkinsonism: evidence of a common founder across European populations. Am J Hum Genet 76 (2005) 672-680
    • (2005) Am J Hum Genet , vol.76 , pp. 672-680
    • Kachergus, J.1    Mata, I.2    Hulihan, M.3
  • 124
    • 24644474856 scopus 로고    scopus 로고
    • The dardarin G 2019 S mutation is a common cause of Parkinson's disease but not other neurodegenerative diseases
    • Hernandez D., Paisan R., Crawley A., et al. The dardarin G 2019 S mutation is a common cause of Parkinson's disease but not other neurodegenerative diseases. Neurosci Lett 389 (2005) 137-139
    • (2005) Neurosci Lett , vol.389 , pp. 137-139
    • Hernandez, D.1    Paisan, R.2    Crawley, A.3
  • 125
    • 19944432606 scopus 로고    scopus 로고
    • Genetic screening for a single common LRRK2 mutation in familial Parkinson's disease
    • Nichols W., Pankratz N., Hernandez D., et al. Genetic screening for a single common LRRK2 mutation in familial Parkinson's disease. Lancet 365 (2005) 410-412
    • (2005) Lancet , vol.365 , pp. 410-412
    • Nichols, W.1    Pankratz, N.2    Hernandez, D.3
  • 126
    • 18244394793 scopus 로고    scopus 로고
    • Clinical features of LRRK2-associated Parkinson's disease in central Norway
    • Aasly J., Toft M., Fernandez-Mata I., et al. Clinical features of LRRK2-associated Parkinson's disease in central Norway. Ann Neurol 57 (2005) 762-765
    • (2005) Ann Neurol , vol.57 , pp. 762-765
    • Aasly, J.1    Toft, M.2    Fernandez-Mata, I.3
  • 127
    • 33645139675 scopus 로고    scopus 로고
    • Comprehensive analysis of the LRRK2 gene in sixty families with Parkinson's disease
    • Di Fonzo A., Tassorelli C., De Mari M., et al. Comprehensive analysis of the LRRK2 gene in sixty families with Parkinson's disease. Eur J Hum Genet 14 (2006) 322-331
    • (2006) Eur J Hum Genet , vol.14 , pp. 322-331
    • Di Fonzo, A.1    Tassorelli, C.2    De Mari, M.3
  • 128
    • 32044432395 scopus 로고    scopus 로고
    • Biochemical and pathological characterization of Lrrk2
    • Giasson B., Covy J., Bonini N., et al. Biochemical and pathological characterization of Lrrk2. Ann Neurol 59 (2006) 315-322
    • (2006) Ann Neurol , vol.59 , pp. 315-322
    • Giasson, B.1    Covy, J.2    Bonini, N.3
  • 129
    • 31144443248 scopus 로고    scopus 로고
    • The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity
    • Gloeckner C., Kinkl N., Schumacher A., et al. The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity. Hum Mol Genet 15 (2006) 223-232
    • (2006) Hum Mol Genet , vol.15 , pp. 223-232
    • Gloeckner, C.1    Kinkl, N.2    Schumacher, A.3
  • 130
    • 29444437871 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration
    • Smith W., Pei Z., Jiang H., et al. Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration. Proc Natl Acad Sci USA 102 (2005) 18676-18681
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18676-18681
    • Smith, W.1    Pei, Z.2    Jiang, H.3
  • 131
    • 28044460070 scopus 로고    scopus 로고
    • Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity
    • West A., Moore D., Biskup S., et al. Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity. Proc Natl Acad Sci USA 102 (2005) 1684247
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1684247
    • West, A.1    Moore, D.2    Biskup, S.3
  • 132
    • 33748619215 scopus 로고    scopus 로고
    • The importance of LRRK2 mutations in Parkinson disease
    • Schapira A. The importance of LRRK2 mutations in Parkinson disease. Arch Neurol 63 (2006) 1225-1228
    • (2006) Arch Neurol , vol.63 , pp. 1225-1228
    • Schapira, A.1
  • 133
    • 0022516397 scopus 로고
    • Interactions of the neurotoxic amine 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine with monoamine oxidases
    • Singer T., Salach J., Castagnoli Jr. N., and Trevor A. Interactions of the neurotoxic amine 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine with monoamine oxidases. Biochem J 235 (1986) 785-789
    • (1986) Biochem J , vol.235 , pp. 785-789
    • Singer, T.1    Salach, J.2    Castagnoli Jr., N.3    Trevor, A.4
  • 134
    • 0029844003 scopus 로고    scopus 로고
    • Inhibition of neuronal nitric oxide synthase prevents MPTP-induced parkinsonism in baboons
    • Hantraye P., Brouillet E., Ferrante R., et al. Inhibition of neuronal nitric oxide synthase prevents MPTP-induced parkinsonism in baboons. Nature Med 2 (1996) 1017-1021
    • (1996) Nature Med , vol.2 , pp. 1017-1021
    • Hantraye, P.1    Brouillet, E.2    Ferrante, R.3
  • 135
    • 0033681149 scopus 로고    scopus 로고
    • Chronic systemic pesticide exposure reproduces features of Parkinson's disease
    • Betarbet R., Sherer T., MacKenzie G., et al. Chronic systemic pesticide exposure reproduces features of Parkinson's disease. Nat Neurosci 3 (2000) 1301-1306
    • (2000) Nat Neurosci , vol.3 , pp. 1301-1306
    • Betarbet, R.1    Sherer, T.2    MacKenzie, G.3
  • 136
    • 0037314540 scopus 로고    scopus 로고
    • Chronic systemic complex I inhibition induces a hypokinetic multisystem degeneration in rats
    • Hoglinger G., Feger J., Prigent A., et al. Chronic systemic complex I inhibition induces a hypokinetic multisystem degeneration in rats. J Neurochem 84 (2003) 491-502
    • (2003) J Neurochem , vol.84 , pp. 491-502
    • Hoglinger, G.1    Feger, J.2    Prigent, A.3
  • 137
    • 33745612296 scopus 로고    scopus 로고
    • Intersecting pathways to neurodegeneration in Parkinson's disease: effects of the pesticide rotenone on DJ-1, alpha-synuclein, and the ubiquitin-proteasome system
    • Betarbet R., Canet-Aviles R., Sherer T., et al. Intersecting pathways to neurodegeneration in Parkinson's disease: effects of the pesticide rotenone on DJ-1, alpha-synuclein, and the ubiquitin-proteasome system. Neurobiol Dis 22 (2006) 404-420
    • (2006) Neurobiol Dis , vol.22 , pp. 404-420
    • Betarbet, R.1    Canet-Aviles, R.2    Sherer, T.3
  • 138
    • 0037104723 scopus 로고    scopus 로고
    • An in vitro model of Parkinson's disease: linking mitochondrial impairment to altered alpha-synuclein metabolism and oxidative damage
    • Sherer T., Betarbet R., Stout A., et al. An in vitro model of Parkinson's disease: linking mitochondrial impairment to altered alpha-synuclein metabolism and oxidative damage. J Neurosci 22 (2002) 7006-7015
    • (2002) J Neurosci , vol.22 , pp. 7006-7015
    • Sherer, T.1    Betarbet, R.2    Stout, A.3
  • 139
    • 33745143950 scopus 로고    scopus 로고
    • Inhibitory effects of pesticides on proteasome activity: implication in Parkinson's disease
    • Wang X., Li S., Chou A., and Bronstein J. Inhibitory effects of pesticides on proteasome activity: implication in Parkinson's disease. Neurobiol Dis 23 (2006) 198-205
    • (2006) Neurobiol Dis , vol.23 , pp. 198-205
    • Wang, X.1    Li, S.2    Chou, A.3    Bronstein, J.4
  • 140
    • 0032569676 scopus 로고    scopus 로고
    • Cyclosporin inhibition of apoptosis induced by mitochondrial complex I toxin
    • Seaton T., Cooper J., and Schapira A. Cyclosporin inhibition of apoptosis induced by mitochondrial complex I toxin. Brain Res 809 (1998) 12-17
    • (1998) Brain Res , vol.809 , pp. 12-17
    • Seaton, T.1    Cooper, J.2    Schapira, A.3
  • 141
    • 9144275011 scopus 로고    scopus 로고
    • Annonacin, a lipophilic inhibitor of mitochondrial complex I, induces nigral and striatal neurodegeneration in rats: possible relevance for atypical parkinsonism in Guadeloupe
    • Champy P., Hoglinger G., Feger J., et al. Annonacin, a lipophilic inhibitor of mitochondrial complex I, induces nigral and striatal neurodegeneration in rats: possible relevance for atypical parkinsonism in Guadeloupe. J Neurochem 88 (2004) 63-69
    • (2004) J Neurochem , vol.88 , pp. 63-69
    • Champy, P.1    Hoglinger, G.2    Feger, J.3
  • 142
    • 0027495547 scopus 로고
    • Smoking and mitochondrial function: a model for environmental toxins
    • Smith P., Cooper J., Govan G., Harding A., and Schapira A. Smoking and mitochondrial function: a model for environmental toxins. Q J Med 86 (1993) 657-660
    • (1993) Q J Med , vol.86 , pp. 657-660
    • Smith, P.1    Cooper, J.2    Govan, G.3    Harding, A.4    Schapira, A.5
  • 143
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • Jenner P. Oxidative stress in Parkinson's disease. Ann Neurol 53 suppl 3 (2003) S26-S36
    • (2003) Ann Neurol , vol.53 , Issue.SUPPL. 3
    • Jenner, P.1
  • 144
    • 0027739829 scopus 로고
    • Myopathy in vitamin E deficient rats: muscle fibre necrosis associated with disturbances of mitochondrial function
    • Thomas P., Cooper J., King R., et al. Myopathy in vitamin E deficient rats: muscle fibre necrosis associated with disturbances of mitochondrial function. J Anat 183 (1993) 451-461
    • (1993) J Anat , vol.183 , pp. 451-461
    • Thomas, P.1    Cooper, J.2    King, R.3
  • 145
    • 0028924168 scopus 로고
    • Oxidative stress in Parkinson's disease
    • Schapira A. Oxidative stress in Parkinson's disease. Neuropathol Appl Neurobiol 21 (1995) 3-9
    • (1995) Neuropathol Appl Neurobiol , vol.21 , pp. 3-9
    • Schapira, A.1
  • 146
    • 34347359673 scopus 로고    scopus 로고
    • 'Rejuvenation' protects neurons in mouse models of Parkinson's disease
    • Chan C., Guzman J., Ilijic E., et al. 'Rejuvenation' protects neurons in mouse models of Parkinson's disease. Nature 447 (2007) 1081-1086
    • (2007) Nature , vol.447 , pp. 1081-1086
    • Chan, C.1    Guzman, J.2    Ilijic, E.3
  • 148
    • 3042794162 scopus 로고    scopus 로고
    • Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease
    • McNaught K., Perl D., Brownell A., and Olanow C. Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease. Ann Neurol 56 (2004) 149-162
    • (2004) Ann Neurol , vol.56 , pp. 149-162
    • McNaught, K.1    Perl, D.2    Brownell, A.3    Olanow, C.4
  • 149
    • 33746823308 scopus 로고    scopus 로고
    • Proteasomal inhibition causes loss of nigral tyrosine hydroxylase neurons
    • Schapira A., Cleeter M., Muddle J., et al. Proteasomal inhibition causes loss of nigral tyrosine hydroxylase neurons. Ann Neurol 60 (2006) 253-255
    • (2006) Ann Neurol , vol.60 , pp. 253-255
    • Schapira, A.1    Cleeter, M.2    Muddle, J.3
  • 150
    • 33746851548 scopus 로고    scopus 로고
    • Reproducible nigral cell loss after systemic proteasomal inhibitor administration to rats
    • Zeng B., Bukhatwa S., Hikima A., Rose S., and Jenner P. Reproducible nigral cell loss after systemic proteasomal inhibitor administration to rats. Ann Neurol 60 (2006) 248-252
    • (2006) Ann Neurol , vol.60 , pp. 248-252
    • Zeng, B.1    Bukhatwa, S.2    Hikima, A.3    Rose, S.4    Jenner, P.5
  • 151
    • 33746791044 scopus 로고    scopus 로고
    • Lack of nigrostriatal pathology in a rat model of proteasome inhibition
    • Manning-Bog A., Reaney S., Chou V., et al. Lack of nigrostriatal pathology in a rat model of proteasome inhibition. Ann Neurol 60 (2006) 256-260
    • (2006) Ann Neurol , vol.60 , pp. 256-260
    • Manning-Bog, A.1    Reaney, S.2    Chou, V.3
  • 152
    • 33746850545 scopus 로고    scopus 로고
    • Proteasome inhibition and Parkinson's disease modeling
    • Bove J., Zhou C., Jackson-Lewis V., et al. Proteasome inhibition and Parkinson's disease modeling. Ann Neurol 60 (2006) 260-264
    • (2006) Ann Neurol , vol.60 , pp. 260-264
    • Bove, J.1    Zhou, C.2    Jackson-Lewis, V.3
  • 153
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: a molecular machine designed for controlled proteolysis
    • Voges D., Zwickl P., and Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 68 (1999) 1015-1068
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 154
    • 0041430614 scopus 로고    scopus 로고
    • Dysfunction of mitochondrial complex I and the proteasome: interactions between two biochemical deficits in a cellular model of Parkinson's disease
    • Hoglinger G., Carrard G., Michel P., et al. Dysfunction of mitochondrial complex I and the proteasome: interactions between two biochemical deficits in a cellular model of Parkinson's disease. J Neurochem 86 (2003) 1297-1307
    • (2003) J Neurochem , vol.86 , pp. 1297-1307
    • Hoglinger, G.1    Carrard, G.2    Michel, P.3
  • 155
    • 0036771852 scopus 로고    scopus 로고
    • Effects of coenzyme Q10 in early Parkinson disease: evidence of slowing of the functional decline
    • Shults C., Oakes D., Kieburtz K., et al. Effects of coenzyme Q10 in early Parkinson disease: evidence of slowing of the functional decline. Arch Neurol 59 (2002) 1541-1550
    • (2002) Arch Neurol , vol.59 , pp. 1541-1550
    • Shults, C.1    Oakes, D.2    Kieburtz, K.3
  • 156
    • 33846115045 scopus 로고    scopus 로고
    • A randomized clinical trial of coenzyme Q10 and GPI-1485 in early Parkinson disease
    • The NINDS NET-PD Investigators
    • The NINDS NET-PD Investigators. A randomized clinical trial of coenzyme Q10 and GPI-1485 in early Parkinson disease. Neurology 68 (2007) 20-28
    • (2007) Neurology , vol.68 , pp. 20-28
  • 157
    • 0037426566 scopus 로고    scopus 로고
    • Coenzyme Q10 supplementation provides mild symptomatic benefit in patients with Parkinson's disease
    • Muller T., Buttner T., Gholipour A., and Kuhn W. Coenzyme Q10 supplementation provides mild symptomatic benefit in patients with Parkinson's disease. Neurosci Lett 341 (2003) 201-204
    • (2003) Neurosci Lett , vol.341 , pp. 201-204
    • Muller, T.1    Buttner, T.2    Gholipour, A.3    Kuhn, W.4
  • 158
    • 34447252358 scopus 로고    scopus 로고
    • Randomized, double-blind, placebo-controlled trial on symptomatic effects of coenzyme Q10 in Parkinson's disease
    • Storch A., Jost W., Vieregge P., et al. Randomized, double-blind, placebo-controlled trial on symptomatic effects of coenzyme Q10 in Parkinson's disease. Arch Neurol 64 (2007) 938-944
    • (2007) Arch Neurol , vol.64 , pp. 938-944
    • Storch, A.1    Jost, W.2    Vieregge, P.3
  • 159
    • 0032914740 scopus 로고    scopus 로고
    • Creatine and cyclocreatine attenuate MPTP neurotoxicity
    • Matthews R., Ferrante R., Klivenyi P., et al. Creatine and cyclocreatine attenuate MPTP neurotoxicity. Exp Neurol 157 (1999) 142-149
    • (1999) Exp Neurol , vol.157 , pp. 142-149
    • Matthews, R.1    Ferrante, R.2    Klivenyi, P.3
  • 160
    • 33645894705 scopus 로고    scopus 로고
    • A randomized, double-blind, futility clinical trial of creatine and minocycline in early Parkinson disease
    • The NINDS NET-PD Investigators
    • The NINDS NET-PD Investigators. A randomized, double-blind, futility clinical trial of creatine and minocycline in early Parkinson disease. Neurology 66 (2006) 664-671
    • (2006) Neurology , vol.66 , pp. 664-671
  • 161
    • 33749835508 scopus 로고    scopus 로고
    • Creatine supplementation in Parkinson disease: a placebo-controlled randomized pilot trial
    • Bender A., Koch W., Elstner M., et al. Creatine supplementation in Parkinson disease: a placebo-controlled randomized pilot trial. Neurology 67 (2006) 1262-1264
    • (2006) Neurology , vol.67 , pp. 1262-1264
    • Bender, A.1    Koch, W.2    Elstner, M.3
  • 162
    • 33750719088 scopus 로고    scopus 로고
    • TCH346 as a neuroprotective drug in Parkinson's disease: a double-blind, randomised, controlled trial
    • Olanow C., Schapira A., LeWitt P., et al. TCH346 as a neuroprotective drug in Parkinson's disease: a double-blind, randomised, controlled trial. Lancet Neurol 5 (2006) 1013-1020
    • (2006) Lancet Neurol , vol.5 , pp. 1013-1020
    • Olanow, C.1    Schapira, A.2    LeWitt, P.3
  • 163
    • 33749247103 scopus 로고    scopus 로고
    • Novel pharmacological targets for the treatment of Parkinson's disease
    • Schapira A., Bezard E., Brotchie J., et al. Novel pharmacological targets for the treatment of Parkinson's disease. Nat Rev Drug Discov 5 (2006) 845-854
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 845-854
    • Schapira, A.1    Bezard, E.2    Brotchie, J.3
  • 164
    • 34547916390 scopus 로고    scopus 로고
    • Treatment options in the modern management of Parkinson disease
    • Schapira A. Treatment options in the modern management of Parkinson disease. Arch Neurol 64 (2007) 108:3-108:8
    • (2007) Arch Neurol , vol.64
    • Schapira, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.