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Volumn 58, Issue 4, 2005, Pages 495-505

Mitochondria take center stage in aging and neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS DNA; COPPER ZINC SUPEROXIDE DISMUTASE; HEAT SHOCK PROTEIN 60; MITOCHONDRIAL DNA; REACTIVE OXYGEN METABOLITE;

EID: 25444474703     PISSN: 03645134     EISSN: None     Source Type: Journal    
DOI: 10.1002/ana.20624     Document Type: Review
Times cited : (816)

References (97)
  • 1
    • 13844281067 scopus 로고    scopus 로고
    • The powerhouse takes control of the cell: Is the mitochondrial permeability transition a viable therapeutic target against neuronal dysfunction and death?
    • Stavrovskaya IG, Kristal BS. The powerhouse takes control of the cell: is the mitochondrial permeability transition a viable therapeutic target against neuronal dysfunction and death? Free Radic Biol Med 2005;38:687-697.
    • (2005) Free Radic Biol Med , vol.38 , pp. 687-697
    • Stavrovskaya, I.G.1    Kristal, B.S.2
  • 2
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines CP, Kaiser RA, Purcell NH, et al. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 2005;434:658-662.
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1    Kaiser, R.A.2    Purcell, N.H.3
  • 3
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa T, Shimizu S, Watanabe T, et al. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 2005;434:652-658.
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3
  • 4
    • 33644840693 scopus 로고    scopus 로고
    • Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury
    • Degterev A, Huang Z, Boyce M, et al. Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury. Nat Chem Biol 2005;1:112-119.
    • (2005) Nat Chem Biol , vol.1 , pp. 112-119
    • Degterev, A.1    Huang, Z.2    Boyce, M.3
  • 5
    • 0033595684 scopus 로고    scopus 로고
    • Aging-dependent large accumulation of point mutations in the human mtDNA control region for replication
    • Michikawa Y, Mazzucchelli F, Bresolin N, et al. Aging-dependent large accumulation of point mutations in the human mtDNA control region for replication. Science 1999;286:774-779.
    • (1999) Science , vol.286 , pp. 774-779
    • Michikawa, Y.1    Mazzucchelli, F.2    Bresolin, N.3
  • 6
    • 0034327572 scopus 로고    scopus 로고
    • The age-related accumulation of a mitochondrial DNA control region mutation in muscle, but not brain, detected by a sensitive PNA-directed PCR clamping based method
    • Murdock DG, Christacos NC, Wallace DC. The age-related accumulation of a mitochondrial DNA control region mutation in muscle, but not brain, detected by a sensitive PNA-directed PCR clamping based method. Nucleic Acids Res 2000;28:4350-4355.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4350-4355
    • Murdock, D.G.1    Christacos, N.C.2    Wallace, D.C.3
  • 7
    • 0034620483 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations in complex I and tRNA genes in Parkinson's disease
    • Simon DK, Mayeux R, Marder K, et al. Mitochondrial DNA mutations in complex I and tRNA genes in Parkinson's disease. Neurology 2000;54:703-709.
    • (2000) Neurology , vol.54 , pp. 703-709
    • Simon, D.K.1    Mayeux, R.2    Marder, K.3
  • 8
    • 0035957323 scopus 로고    scopus 로고
    • Muscle-specific mutations accumulate with aging in critical human mtDNA control sites for replication
    • Wang Y, Michikawa Y, Mallidis C, et al. Muscle-specific mutations accumulate with aging in critical human mtDNA control sites for replication. Proc Natl Acad Sci USA 2001;98:4022-4027.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4022-4027
    • Wang, Y.1    Michikawa, Y.2    Mallidis, C.3
  • 9
    • 0037417898 scopus 로고    scopus 로고
    • Strikingly higher frequency in centenarians and twins of mtDNA mutation causing remodeling of replication origin in leukocytes
    • Zhang J, Asin-Cayuela J, Fish J, et al. Strikingly higher frequency in centenarians and twins of mtDNA mutation causing remodeling of replication origin in leukocytes. Proc Natl Acad Sci USA 2003;100:1116-1121.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1116-1121
    • Zhang, J.1    Asin-Cayuela, J.2    Fish, J.3
  • 10
    • 0037081814 scopus 로고    scopus 로고
    • High aggregate burden of somatic mtDNA point mutations in aging and Alzheimer's disease brain
    • Lin MT, Simon DK, Ahn CH, et al. High aggregate burden of somatic mtDNA point mutations in aging and Alzheimer's disease brain. Hum Mol Genet 2002;11:133-145.
    • (2002) Hum Mol Genet , vol.11 , pp. 133-145
    • Lin, M.T.1    Simon, D.K.2    Ahn, C.H.3
  • 11
    • 2642580016 scopus 로고    scopus 로고
    • Premature ageing in mice expressing defective mitochondrial DNA polymerase
    • Trifunovic A, Wredenberg A, Falkenberg M, et al. Premature ageing in mice expressing defective mitochondrial DNA polymerase. Nature 2004;429:417-423.
    • (2004) Nature , vol.429 , pp. 417-423
    • Trifunovic, A.1    Wredenberg, A.2    Falkenberg, M.3
  • 12
    • 22344456832 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging
    • Kujoth GC, Hiona A, Pugh TD, et al. Mitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging. Science 2005;309:481-484.
    • (2005) Science , vol.309 , pp. 481-484
    • Kujoth, G.C.1    Hiona, A.2    Pugh, T.D.3
  • 13
    • 3042631024 scopus 로고    scopus 로고
    • Gene regulation and DNA damage in the ageing human brain
    • Lu T, Pan Y, Kao SY, et al. Gene regulation and DNA damage in the ageing human brain. Nature 2004;429:883-891.
    • (2004) Nature , vol.429 , pp. 883-891
    • Lu, T.1    Pan, Y.2    Kao, S.Y.3
  • 14
    • 0037022556 scopus 로고    scopus 로고
    • High-quality life extension by the enzyme peptide methionine sulfoxide reductase
    • Ruan H, Tang XD, Chen ML, et al. High-quality life extension by the enzyme peptide methionine sulfoxide reductase. Proc Natl Acad Sci USA 2002;99:2748-2753.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2748-2753
    • Ruan, H.1    Tang, X.D.2    Chen, M.L.3
  • 15
    • 21144434217 scopus 로고    scopus 로고
    • Extension of murine lifespan by overexpression of catalase targeted to mitochondria
    • Schriner SE, Linford NJ, Martin GM, et al. Extension of murine lifespan by overexpression of catalase targeted to mitochondria. Science 2005;308:1909-1911.
    • (2005) Science , vol.308 , pp. 1909-1911
    • Schriner, S.E.1    Linford, N.J.2    Martin, G.M.3
  • 16
    • 0034923434 scopus 로고    scopus 로고
    • Oxidative damage is the earliest event in Alzheimer disease
    • Nunomura A, Perry G, Aliev G, et al. Oxidative damage is the earliest event in Alzheimer disease. J Neuropathol Exp Neurol 2001;60:759-767.
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 759-767
    • Nunomura, A.1    Perry, G.2    Aliev, G.3
  • 17
    • 0344838535 scopus 로고    scopus 로고
    • Deficits in a tricarboxylic acid cycle enzyme in brains from patients with Parkinson's disease
    • Gibson GE, Kingsbury AE, Xu H, et al. Deficits in a tricarboxylic acid cycle enzyme in brains from patients with Parkinson's disease. Neurochem Int 2003;43:129-135.
    • (2003) Neurochem Int , vol.43 , pp. 129-135
    • Gibson, G.E.1    Kingsbury, A.E.2    Xu, H.3
  • 18
    • 17544378704 scopus 로고    scopus 로고
    • Endogenous oxidative stress in sporadic Alzheimer's disease neuronal cybrids reduces viability by increasing apoptosis through pro-death signaling pathways and is mimicked by oxidant exposure of control cybrids
    • Onyango IG, Bennett JP Jr, Turtle JB. Endogenous oxidative stress in sporadic Alzheimer's disease neuronal cybrids reduces viability by increasing apoptosis through pro-death signaling pathways and is mimicked by oxidant exposure of control cybrids. Neurobiol Dis 2005;19:312-322.
    • (2005) Neurobiol Dis , vol.19 , pp. 312-322
    • Onyango, I.G.1    Bennett Jr., J.P.2    Turtle, J.B.3
  • 19
    • 0033515075 scopus 로고    scopus 로고
    • Functional integrity of mitochondrial genomes in human platelets and autopsied brain tissues from elderly patients with Alzheimer's disease
    • Ito S, Ohta S, Nishimaki K, et al. Functional integrity of mitochondrial genomes in human platelets and autopsied brain tissues from elderly patients with Alzheimer's disease. Proc Natl Acad Sci USA 1999;96:2099-2103.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2099-2103
    • Ito, S.1    Ohta, S.2    Nishimaki, K.3
  • 20
    • 0344625398 scopus 로고    scopus 로고
    • No mitochondrial haplotype was found to increase risk for Alzheimer's disease
    • Zsurka G, Kalman J, Csaszar A, et al. No mitochondrial haplotype was found to increase risk for Alzheimer's disease. Biol Psychiatry 1998;44:371-373.
    • (1998) Biol Psychiatry , vol.44 , pp. 371-373
    • Zsurka, G.1    Kalman, J.2    Csaszar, A.3
  • 21
    • 3242668604 scopus 로고    scopus 로고
    • Alzheimer's brains harbor somatic mtDNA control-region mutations that suppress mitochondrial transcription and eplication
    • Coskun PE, Beal MF, Wallace DC. Alzheimer's brains harbor somatic mtDNA control-region mutations that suppress mitochondrial transcription and eplication. Proc Natl Acad Sci USA 2004;101:10726-10731.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10726-10731
    • Coskun, P.E.1    Beal, M.F.2    Wallace, D.C.3
  • 22
    • 20044385920 scopus 로고    scopus 로고
    • Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease
    • Stokin GB, Lillo C, Falzone TL, et al. Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease. Science 2005;307:1282-1288.
    • (2005) Science , vol.307 , pp. 1282-1288
    • Stokin, G.B.1    Lillo, C.2    Falzone, T.L.3
  • 23
    • 10944269186 scopus 로고    scopus 로고
    • The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
    • Li Z, Okamoto K, Hayashi Y, Sheng M. The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses. Cell 2004;119:873-887.
    • (2004) Cell , vol.119 , pp. 873-887
    • Li, Z.1    Okamoto, K.2    Hayashi, Y.3    Sheng, M.4
  • 24
    • 0037186074 scopus 로고    scopus 로고
    • Altered metabolism of the amyloid beta precursor protein is associated with mitochondrial dysfunction in Down's syndrome
    • Busciglio J, Pelsman A, Wong C, et al. Altered metabolism of the amyloid beta precursor protein is associated with mitochondrial dysfunction in Down's syndrome. Neuron 2002;33:677-688.
    • (2002) Neuron , vol.33 , pp. 677-688
    • Busciglio, J.1    Pelsman, A.2    Wong, C.3
  • 25
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease
    • Lustbader JW, Cirilli M, Lin C, et al. ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science 2004;304:448-452.
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3
  • 26
    • 19944433571 scopus 로고    scopus 로고
    • Copper-dependent inhibition of human cytochrome c oxidase by a dimeric conformer of amyloid-beta1-42
    • Crouch PJ, Blake R, Duce JA, et al. Copper-dependent inhibition of human cytochrome c oxidase by a dimeric conformer of amyloid-beta1-42. J Neurosci 2005;25:672-679.
    • (2005) J Neurosci , vol.25 , pp. 672-679
    • Crouch, P.J.1    Blake, R.2    Duce, J.A.3
  • 27
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
    • Anandatheerthavarada HK, Biswas G, Robin MA, Avadhani NG. Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells. J Cell Biol 2003;161:41-54.
    • (2003) J Cell Biol , vol.161 , pp. 41-54
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Robin, M.A.3    Avadhani, N.G.4
  • 28
    • 9144260111 scopus 로고    scopus 로고
    • Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria
    • Leissring MA, Farris W, Wu X, et al. Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria. Biochem J 2004;383:439-446.
    • (2004) Biochem J , vol.383 , pp. 439-446
    • Leissring, M.A.1    Farris, W.2    Wu, X.3
  • 29
    • 19944373389 scopus 로고    scopus 로고
    • Nicastrin, presenilin, APH-1, and PEN-2 form active gamma-secretase complexes in mitochondria
    • Hansson CA, Frykman S, Farmery MR, et al. Nicastrin, presenilin, APH-1, and PEN-2 form active gamma-secretase complexes in mitochondria. J Biol Chem 2004;279:51654-51660.
    • (2004) J Biol Chem , vol.279 , pp. 51654-51660
    • Hansson, C.A.1    Frykman, S.2    Farmery, M.R.3
  • 30
    • 2642544767 scopus 로고    scopus 로고
    • Increased plaque burden in brains of APP mutant MnSOD heterozygous knockout mice
    • Li F, Calingasan NY, Yu F, et al. Increased plaque burden in brains of APP mutant MnSOD heterozygous knockout mice. J Neurochem 2004;89:1308-1312.
    • (2004) J Neurochem , vol.89 , pp. 1308-1312
    • Li, F.1    Calingasan, N.Y.2    Yu, F.3
  • 31
    • 0036403838 scopus 로고    scopus 로고
    • Oxidative stress increases expression and activity of BACE in NT2 neurons
    • Tamagno E, Bardini P, Obbili A, et al. Oxidative stress increases expression and activity of BACE in NT2 neurons. Neurobiol Dis 2002;10:279-288.
    • (2002) Neurobiol Dis , vol.10 , pp. 279-288
    • Tamagno, E.1    Bardini, P.2    Obbili, A.3
  • 32
    • 19944433845 scopus 로고    scopus 로고
    • Beta-site APP cleaving enzyme up-regulation induced by 4-hydroxynonenal is mediated by stress-activated protein kinases pathways
    • Tamagno E, Parola M, Bardini P, et al. Beta-site APP cleaving enzyme up-regulation induced by 4-hydroxynonenal is mediated by stress-activated protein kinases pathways. J Neurochem 2005;92:628-636.
    • (2005) J Neurochem , vol.92 , pp. 628-636
    • Tamagno, E.1    Parola, M.2    Bardini, P.3
  • 33
    • 0035875690 scopus 로고    scopus 로고
    • Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis
    • Pratico D, Uryu K, Leight S, et al. Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis. J Neurosci 2001;21:4183-4187.
    • (2001) J Neurosci , vol.21 , pp. 4183-4187
    • Pratico, D.1    Uryu, K.2    Leight, S.3
  • 34
    • 1442314722 scopus 로고    scopus 로고
    • Early vitamin e supplementation in young but not aged mice reduces Abeta levels and amyloid deposition in a transgenic model of Alzheimer's disease
    • Sung S, Yao Y, Uryu K, et al. Early vitamin E supplementation in young but not aged mice reduces Abeta levels and amyloid deposition in a transgenic model of Alzheimer's disease. FASEB J 2004;18:323-325.
    • (2004) FASEB J , vol.18 , pp. 323-325
    • Sung, S.1    Yao, Y.2    Uryu, K.3
  • 35
    • 0035503597 scopus 로고    scopus 로고
    • The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse
    • Lim GP, Chu T, Yang F, et al. The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse. J Neurosci 2001;21:8370-8377.
    • (2001) J Neurosci , vol.21 , pp. 8370-8377
    • Lim, G.P.1    Chu, T.2    Yang, F.3
  • 36
    • 0033681149 scopus 로고    scopus 로고
    • Chronic systemic pesticide exposure reproduces features of Parkinson's disease
    • Betarbet R, Sherer TB, MacKenzie G, et al. Chronic systemic pesticide exposure reproduces features of Parkinson's disease. Nat Neurosci 2000;3:1301-1306.
    • (2000) Nat Neurosci , vol.3 , pp. 1301-1306
    • Betarbet, R.1    Sherer, T.B.2    MacKenzie, G.3
  • 37
    • 0344198025 scopus 로고    scopus 로고
    • Mechanism of toxicity in rotenone models of Parkinson's disease
    • Sherer TB, Betarbet R, Testa CM, et al. Mechanism of toxicity in rotenone models of Parkinson's disease. J Neurosci 2003;23:10756-10764.
    • (2003) J Neurosci , vol.23 , pp. 10756-10764
    • Sherer, T.B.1    Betarbet, R.2    Testa, C.M.3
  • 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 2000;48:730-736.
    • (2000) Ann Neurol , vol.48 , pp. 730-736
    • Thyagarajan, D.1    Bressman, S.2    Bruno, C.3
  • 39
    • 0036297660 scopus 로고    scopus 로고
    • Sequence analysis of the entire mitochondrial genome in Parkinson's disease
    • Vives-Bauza C, Andreu AL, Manfredi G, et al. Sequence analysis of the entire mitochondrial genome in Parkinson's disease. Biochem Biophys Res Commun 2002;290:1593-1601.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 1593-1601
    • Vives-Bauza, C.1    Andreu, A.L.2    Manfredi, G.3
  • 40
    • 10444243239 scopus 로고    scopus 로고
    • Mitochondrial ND5 mutations in idiopathic Parkinson's disease
    • Parker WD Jr, Parks JK. Mitochondrial ND5 mutations in idiopathic Parkinson's disease. Biochem Biophys Res Commun 2005;326:667-669.
    • (2005) Biochem Biophys Res Commun , vol.326 , pp. 667-669
    • Parker Jr., W.D.1    Parks, J.K.2
  • 41
    • 0347356538 scopus 로고    scopus 로고
    • Effects of purifying and adaptive selection on regional variation in human mtDNA
    • Ruiz-Pesini E, Mishmar D, Brandon M, et al. Effects of purifying and adaptive selection on regional variation in human mtDNA. Science 2004;303:223-226.
    • (2004) Science , vol.303 , pp. 223-226
    • Ruiz-Pesini, E.1    Mishmar, D.2    Brandon, M.3
  • 42
    • 0037385480 scopus 로고    scopus 로고
    • Mitochondrial polymorphisms significantly reduce the risk of Parkinson's disease
    • van der Walt JM, Nicodemus KK, Martin ER, et al. Mitochondrial polymorphisms significantly reduce the risk of Parkinson's disease. Am J Hum Genet 2003;72:804-811.
    • (2003) Am J Hum Genet , vol.72 , pp. 804-811
    • Van Der Walt, J.M.1    Nicodemus, K.K.2    Martin, E.R.3
  • 43
    • 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 2005;57:564-567.
    • (2005) Ann Neurol , vol.57 , pp. 564-567
    • Pyle, A.1    Foltynie, T.2    Tiangyou, W.3
  • 44
    • 2942750228 scopus 로고    scopus 로고
    • Mitochondrial DNA polymorphisms as risk factors for Parkinson's disease and Parkinson's disease dementia
    • Autere J, Moilanen JS, Finnila S, et al. Mitochondrial DNA polymorphisms as risk factors for Parkinson's disease and Parkinson's disease dementia. Hum Genet 2004;115:29-35.
    • (2004) Hum Genet , vol.115 , pp. 29-35
    • Autere, J.1    Moilanen, J.S.2    Finnila, S.3
  • 45
    • 1542617769 scopus 로고    scopus 로고
    • Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP
    • Song DD, Shults CW, Sisk A, et al. Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP. Exp Neurol 2004;186:158-172.
    • (2004) Exp Neurol , vol.186 , pp. 158-172
    • Song, D.D.1    Shults, C.W.2    Sisk, A.3
  • 46
    • 0033890821 scopus 로고    scopus 로고
    • alpha-synuclein promotes mitochondrial deficit and oxidative stress
    • Hsu LJ, Sagara Y, Arroyo A, et al. alpha-synuclein promotes mitochondrial deficit and oxidative stress. Am J Pathol 2000;157:401-410.
    • (2000) Am J Pathol , vol.157 , pp. 401-410
    • Hsu, L.J.1    Sagara, Y.2    Arroyo, A.3
  • 47
    • 20044385568 scopus 로고    scopus 로고
    • Parkinson-like syndrome induced by continuous MPTP infusion: Convergent roles of the ubiquitin-proteasome system and alpha-synuclein
    • Fornai F, Schluter OM, Lenzi P, et al. Parkinson-like syndrome induced by continuous MPTP infusion: convergent roles of the ubiquitin-proteasome system and alpha-synuclein. Proc Natl Acad Sci USA 2005;102:3413-3418.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3413-3418
    • Fornai, F.1    Schluter, O.M.2    Lenzi, P.3
  • 48
    • 0037386532 scopus 로고    scopus 로고
    • Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants
    • Greene JC, Whirworth AJ, Kuo I, et al. Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants. Proc Natl Acad Sci USA 2003;100:4078-4083.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4078-4083
    • Greene, J.C.1    Whirworth, A.J.2    Kuo, I.3
  • 49
    • 2542560342 scopus 로고    scopus 로고
    • Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress
    • Pesah Y, Pham T, Burgess H, et al. Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress. Development 2004;131:2183-2219.
    • (2004) Development , vol.131 , pp. 2183-2219
    • Pesah, Y.1    Pham, T.2    Burgess, H.3
  • 50
    • 20344369560 scopus 로고    scopus 로고
    • Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease
    • Whirworth AJ, Theodore DA, Green JC, et al. Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease. Proc Natl Acad Sci USA 2005;102:8024-8029.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8024-8029
    • Whirworth, A.J.1    Theodore, D.A.2    Green, J.C.3
  • 51
    • 0037338634 scopus 로고    scopus 로고
    • Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
    • Darios F, Corti O, Lucking CB, et al. Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death. Hum Mol Genet 2003;12:517-526.
    • (2003) Hum Mol Genet , vol.12 , pp. 517-526
    • Darios, F.1    Corti, O.2    Lucking, C.B.3
  • 52
    • 2442481789 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative damage in parkin-deficient mice
    • Palacino JJ, Sagi D, Goldberg MS, et al. Mitochondrial dysfunction and oxidative damage in parkin-deficient mice. J Biol Chem 2004;279:18614-18622.
    • (2004) J Biol Chem , vol.279 , pp. 18614-18622
    • Palacino, J.J.1    Sagi, D.2    Goldberg, M.S.3
  • 53
    • 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 2004;19:544-548.
    • (2004) Mov Disord , vol.19 , pp. 544-548
    • Muftuoglu, M.1    Elibol, B.2    Dalmizrak, O.3
  • 54
    • 2542534741 scopus 로고    scopus 로고
    • S-nitrosylation of parkin regulates ubiquitin and compromises parkin's proctective function
    • Chung, KK, Thomas B, Li X, Pletnikova O, et al. S-nitrosylation of parkin regulates ubiquitin and compromises parkin's proctective function. Science 2004;304:1328-1321.
    • (2004) Science , vol.304 , pp. 1328-11321
    • Chung, K.K.1    Thomas, B.2    Li, X.3    Pletnikova, O.4
  • 55
    • 0037428241 scopus 로고    scopus 로고
    • Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism
    • Bonifati V, Rizzu P, van Baren MJ, et al. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 2003;299:256-259.
    • (2003) Science , vol.299 , pp. 256-259
    • Bonifati, V.1    Rizzu, P.2    Van Baren, M.J.3
  • 56
    • 13944279784 scopus 로고    scopus 로고
    • Sensitivity to oxidative stress in DJ-1-deficient dopamine neurons: An ES-derived cell model of primary parkinsonism
    • Martinat C, Shendelman S, Jonason A, et al. Sensitivity to oxidative stress in DJ-1-deficient dopamine neurons: an ES-derived cell model of primary parkinsonism. PLoS Biol 2004;2:e327.
    • (2004) PLoS Biol , vol.2
    • Martinat, C.1    Shendelman, S.2    Jonason, A.3
  • 57
    • 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 2004;5:213-218.
    • (2004) EMBO Rep , vol.5 , pp. 213-218
    • Taira, T.1    Saito, Y.2    Niki, T.3
  • 58
    • 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 2003;312:1342-1348.
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 1342-1348
    • Yokota, T.1    Sugawara, K.2    Ito, K.3
  • 59
    • 2942684871 scopus 로고    scopus 로고
    • The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization
    • Canet-Aviles RM, Wilson MA, Miller DW, et al. The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization. Proc Natl Acad Sci USA 2004;101:9103-9108.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9103-9108
    • Canet-Aviles, R.M.1    Wilson, M.A.2    Miller, D.W.3
  • 60
    • 20144389422 scopus 로고    scopus 로고
    • Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6- tetrahydropyridine (MPTP) and oxidative stress
    • Kim RH, Smith PD, Aleyasin H, et al. Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and oxidative stress. Proc Natl Acad Sci USA 2005;102:5215-5220.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5215-5220
    • Kim, R.H.1    Smith, P.D.2    Aleyasin, H.3
  • 61
    • 25444472004 scopus 로고    scopus 로고
    • Role of Drosophila DJ-1 in oxidative stress response and survival signaling through the P13K/Akt pathway
    • in press
    • Yang Y, Gehrke S, Haque E, et al. Role of Drosophila DJ-1 in oxidative stress response and survival signaling through the P13K/Akt pathway. Proc Natl Acad Sci USA (in press).
    • Proc Natl Acad Sci USA
    • Yang, Y.1    Gehrke, S.2    Haque, E.3
  • 62
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • Valente EM, Abou-Sleiman PM, Caputo V, et al. Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 2004;304:1158-1160.
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2    Caputo, V.3
  • 63
    • 0036310142 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in a cell culture model of familial amyotrophic lateral sclerosis
    • Menzies FM, Cookson MR, Taylor RW, et al. Mitochondrial dysfunction in a cell culture model of familial amyotrophic lateral sclerosis. Brain 2002;125:1522-1533.
    • (2002) Brain , vol.125 , pp. 1522-1533
    • Menzies, F.M.1    Cookson, M.R.2    Taylor, R.W.3
  • 64
    • 0034669552 scopus 로고    scopus 로고
    • Measuring the quantity and activity of mitochondrial electron transport chain complexes in tissues of central nervous system using blue native polyacrylamide gel electrophoresis
    • Jung C, Higgins CM, Xu Z. Measuring the quantity and activity of mitochondrial electron transport chain complexes in tissues of central nervous system using blue native polyacrylamide gel electrophoresis. Anal Biochem 2000;286:214-223.
    • (2000) Anal Biochem , vol.286 , pp. 214-223
    • Jung, C.1    Higgins, C.M.2    Xu, Z.3
  • 65
    • 0037119407 scopus 로고    scopus 로고
    • Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice
    • Mattiazzi M, D'Aurelio M, Gajewski CD, et al. Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice. J Biol Chem 2002;277:29626-29633.
    • (2002) J Biol Chem , vol.277 , pp. 29626-29633
    • Mattiazzi, M.1    D'Aurelio, M.2    Gajewski, C.D.3
  • 66
    • 0344240348 scopus 로고    scopus 로고
    • ALS-associated mutant SOD1G93A causes mitochondrial vacuolation by expansion of the intermembrane space and by involvement of SOD1 aggregation and peroxisomes
    • Higgins CM, Jung C, Xu Z. ALS-associated mutant SOD1G93A causes mitochondrial vacuolation by expansion of the intermembrane space and by involvement of SOD1 aggregation and peroxisomes. BMC Neurosci 2003;4:16.
    • (2003) BMC Neurosci , vol.4 , pp. 16
    • Higgins, C.M.1    Jung, C.2    Xu, Z.3
  • 67
    • 0034821922 scopus 로고    scopus 로고
    • CuZn superoxide dismutase (SOD1) accumulates in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis-linked SOD1 mutations
    • Jaarsma D, Rognoni F, van Duijn W, et al. CuZn superoxide dismutase (SOD1) accumulates in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis-linked SOD1 mutations. Acta Neuropathol (Berl) 2001;102:293-305.
    • (2001) Acta Neuropathol (Berl) , vol.102 , pp. 293-305
    • Jaarsma, D.1    Rognoni, F.2    Van Duijn, W.3
  • 68
    • 0037173038 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: A proposed mechanism
    • Okado-Matsumoto A, Fridovich I. Amyotrophic lateral sclerosis: a proposed mechanism. Proc Natl Acad Sci USA 2002;99:9010-9014.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9010-9014
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 70
    • 5644301010 scopus 로고    scopus 로고
    • Expression of a familial amyotrophic lateral sclerosis-associated mutant human superoxide dismutase in yeast leads to decreased mitochondrial electron transport
    • Gunther MR, Vangilder R, Fang J, Beattie DS. Expression of a familial amyotrophic lateral sclerosis-associated mutant human superoxide dismutase in yeast leads to decreased mitochondrial electron transport. Arch Biochem Biophys 2004;431:207-214.
    • (2004) Arch Biochem Biophys , vol.431 , pp. 207-214
    • Gunther, M.R.1    Vangilder, R.2    Fang, J.3    Beattie, D.S.4
  • 71
    • 3242701496 scopus 로고    scopus 로고
    • Toxicity of familial ALS-linked SOD1 mutants from selective recruitment to spinal mitochondria
    • Liu J, Lillo C, Jonsson PA, et al. Toxicity of familial ALS-linked SOD1 mutants from selective recruitment to spinal mitochondria. Neuron 2004;43:5-17.
    • (2004) Neuron , vol.43 , pp. 5-17
    • Liu, J.1    Lillo, C.2    Jonsson, P.A.3
  • 72
    • 3242703300 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria
    • Pasinelli P, Belford ME, Lennon N, et al. Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria. Neuron 2004;43:19-30.
    • (2004) Neuron , vol.43 , pp. 19-30
    • Pasinelli, P.1    Belford, M.E.2    Lennon, N.3
  • 73
    • 14944385595 scopus 로고    scopus 로고
    • Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice
    • Vijayvergiya C, Beal MF, Buck J, et al. Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice. J Neurosci 2005;25:2463-2470.
    • (2005) J Neurosci , vol.25 , pp. 2463-2470
    • Vijayvergiya, C.1    Beal, M.F.2    Buck, J.3
  • 74
    • 0037184999 scopus 로고    scopus 로고
    • Mitochondrial localization of mutant superoxide dismutase 1 triggers caspase-dependent cell death in a cellular model of familial amyotrophic lateral sclerosis
    • Takeuchi H, Kobayashi Y, Ishigaki S, et al. Mitochondrial localization of mutant superoxide dismutase 1 triggers caspase-dependent cell death in a cellular model of familial amyotrophic lateral sclerosis. J Biol Chem 2002;277:50966-50972.
    • (2002) J Biol Chem , vol.277 , pp. 50966-50972
    • Takeuchi, H.1    Kobayashi, Y.2    Ishigaki, S.3
  • 75
    • 1542348209 scopus 로고    scopus 로고
    • The energetics of Huntington's disease
    • Browne SE, Beal MF. The energetics of Huntington's disease. Neurochem Res 2004;29:531-546.
    • (2004) Neurochem Res , vol.29 , pp. 531-546
    • Browne, S.E.1    Beal, M.F.2
  • 76
    • 0036327065 scopus 로고    scopus 로고
    • Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines
    • Panov AV, Gutekunst CA, Leavitt BR, et al. Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines. Nat Neurosci 2002;5:731-736.
    • (2002) Nat Neurosci , vol.5 , pp. 731-736
    • Panov, A.V.1    Gutekunst, C.A.2    Leavitt, B.R.3
  • 77
    • 3543141113 scopus 로고    scopus 로고
    • Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release
    • Choo YS, Johnson GV, MacDonald M, et al. Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release. Hum Mol Genet 2004;13:1407-1420.
    • (2004) Hum Mol Genet , vol.13 , pp. 1407-1420
    • Choo, Y.S.1    Johnson, G.V.2    MacDonald, M.3
  • 78
    • 0037335074 scopus 로고    scopus 로고
    • Specific progressive cAMP reduction implicates energy deficit in presymptomatic Huntington's disease knock-in mice
    • Gines S, Seong IS, Fossale E, et al. Specific progressive cAMP reduction implicates energy deficit in presymptomatic Huntington's disease knock-in mice. Hum Mol Genet 2003;12:497-508.
    • (2003) Hum Mol Genet , vol.12 , pp. 497-508
    • Gines, S.1    Seong, I.S.2    Fossale, E.3
  • 79
    • 5344252327 scopus 로고    scopus 로고
    • Defects in adaptive energy metabolism with CNS-linked hyperactivity in PGC-1alpha null mice
    • Lin J, Wu PH, Tarr PT, et al. Defects in adaptive energy metabolism with CNS-linked hyperactivity in PGC-1alpha null mice. Cell 2004;119:121-135.
    • (2004) Cell , vol.119 , pp. 121-135
    • Lin, J.1    Wu, P.H.2    Tarr, P.T.3
  • 80
    • 21544450545 scopus 로고    scopus 로고
    • p53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease
    • Bae BI, Xu Hong, Igarashi S, et al. p53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease. Neuron 2005;47:29-41.
    • (2005) Neuron , vol.47 , pp. 29-41
    • Bae, B.I.1    Hong, X.2    Igarashi, S.3
  • 81
    • 0036245217 scopus 로고    scopus 로고
    • Progressive loss of striatal neurons causes motor dysfunction in MND2 mutant mice and is not prevented by Bcl-2
    • Rathke-Hartlieb S, Schlomann U, Heimann P, et al. Progressive loss of striatal neurons causes motor dysfunction in MND2 mutant mice and is not prevented by Bcl-2. Exp Neurol 2002;175:87-97.
    • (2002) Exp Neurol , vol.175 , pp. 87-97
    • Rathke-Hartlieb, S.1    Schlomann, U.2    Heimann, P.3
  • 82
    • 25444498785 scopus 로고    scopus 로고
    • Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease
    • Strauss KM, Martins LM, Plun-Favreau H, et al. Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease. Hum Mol Genet 2005;14:2099-2111.
    • (2005) Hum Mol Genet , vol.14 , pp. 2099-2111
    • Strauss, K.M.1    Martins, L.M.2    Plun-Favreau, H.3
  • 83
    • 0142246441 scopus 로고    scopus 로고
    • Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice
    • Jones JM, Datta P, Srinivasula SM, et al. Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice. Nature 2003;425:721-727.
    • (2003) Nature , vol.425 , pp. 721-727
    • Jones, J.M.1    Datta, P.2    Srinivasula, S.M.3
  • 84
    • 0344736798 scopus 로고    scopus 로고
    • Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia
    • Atorino L, Silvestri L, Koppen M, et al. Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia. J Cell Biol 2003;163:777-787.
    • (2003) J Cell Biol , vol.163 , pp. 777-787
    • Atorino, L.1    Silvestri, L.2    Koppen, M.3
  • 85
    • 1342310772 scopus 로고    scopus 로고
    • Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport
    • Ferreirinha F, Quattrini A, Pirozzi M, et al. Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport. J Clin Invest 2004;113:231-242.
    • (2004) J Clin Invest , vol.113 , pp. 231-242
    • Ferreirinha, F.1    Quattrini, A.2    Pirozzi, M.3
  • 86
    • 0036241765 scopus 로고    scopus 로고
    • Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60
    • Hansen JJ, Durr A, Cournu-Rebeix I, et al. Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. Am J Hum Genet 2002;70:1328-1332.
    • (2002) Am J Hum Genet , vol.70 , pp. 1328-1332
    • Hansen, J.J.1    Durr, A.2    Cournu-Rebeix, I.3
  • 87
    • 0036176614 scopus 로고    scopus 로고
    • Spinocerebellar ataxias due to mitochondrial defects
    • Kaplan J. Spinocerebellar ataxias due to mitochondrial defects. Neurochem Int 2002;40:553-557.
    • (2002) Neurochem Int , vol.40 , pp. 553-557
    • Kaplan, J.1
  • 88
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • Bulteau AL, O'Neill HA, Kennedy MC, et al. Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 2004;305:242-245.
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.L.1    O'Neill, H.A.2    Kennedy, M.C.3
  • 89
    • 14044273058 scopus 로고    scopus 로고
    • Friedreich ataxia: The oxidative stress paradox
    • Seznec H, Simon D, Bouton C, et al. Friedreich ataxia: the oxidative stress paradox. Hum Mol Genet 2005;14:463-474.
    • (2005) Hum Mol Genet , vol.14 , pp. 463-474
    • Seznec, H.1    Simon, D.2    Bouton, C.3
  • 90
    • 12744280679 scopus 로고    scopus 로고
    • Altered neuronal mitochondrial coenzyme a synthesis in neurodegeneration with brain iron accumulation caused by abnormal processing, stability, and catalytic activity of mutant pantothenate kinase 2
    • Kotzbauer PT, Truax AC, Trojanowski JQ, Lee VM. Altered neuronal mitochondrial coenzyme a synthesis in neurodegeneration with brain iron accumulation caused by abnormal processing, stability, and catalytic activity of mutant pantothenate kinase 2. J Neurosci 2005;25:689-698.
    • (2005) J Neurosci , vol.25 , pp. 689-698
    • Kotzbauer, P.T.1    Truax, A.C.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 91
    • 20244381365 scopus 로고    scopus 로고
    • Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy
    • Delettre C, Lenaers G, Griffoin JM, et al. Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy. Nat Genet 2000;26:207-210.
    • (2000) Nat Genet , vol.26 , pp. 207-210
    • Delettre, C.1    Lenaers, G.2    Griffoin, J.M.3
  • 92
    • 0037424239 scopus 로고    scopus 로고
    • Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis
    • Olichon A, Baricault L, Gas N, et al. Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis. J Biol Chem 2003;278:7743-7746.
    • (2003) J Biol Chem , vol.278 , pp. 7743-7746
    • Olichon, A.1    Baricault, L.2    Gas, N.3
  • 93
    • 9144238312 scopus 로고    scopus 로고
    • Deficit of in vivo mitochondrial ATP production in OPA1-related dominant optic atrophy
    • Lodi R, Tonon C, Valentino ML, et al. Deficit of in vivo mitochondrial ATP production in OPA1-related dominant optic atrophy. Ann Neurol 2004;56:719-723.
    • (2004) Ann Neurol , vol.56 , pp. 719-723
    • Lodi, R.1    Tonon, C.2    Valentino, M.L.3
  • 94
    • 3042794162 scopus 로고    scopus 로고
    • Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease
    • McNaught KS, Perl DP, Brownell AL, Olanow CW. Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease. Ann Neurol 2004;56:149-162.
    • (2004) Ann Neurol , vol.56 , pp. 149-162
    • McNaught, K.S.1    Perl, D.P.2    Brownell, A.L.3    Olanow, C.W.4
  • 95
    • 2442645048 scopus 로고    scopus 로고
    • Proteasome inhibition alters neural mitochondrial homeostasis and mitochondria turnover
    • Sullivan PG, Dragicevic NB, Deng JH, et al. Proteasome inhibition alters neural mitochondrial homeostasis and mitochondria turnover. J Biol Chem 2004;279:20699-20707.
    • (2004) J Biol Chem , vol.279 , pp. 20699-20707
    • Sullivan, P.G.1    Dragicevic, N.B.2    Deng, J.H.3
  • 96
    • 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 GU, Carrard G, Michel PP, 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 2003;86:1297-1307.
    • (2003) J Neurochem , vol.86 , pp. 1297-1307
    • Hoglinger, G.U.1    Carrard, G.2    Michel, P.P.3
  • 97
    • 15744384860 scopus 로고    scopus 로고
    • Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death
    • Bota DA, Ngo JK, Davies KJ. Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death. Free Radic Biol Med 2005;38:665-677.
    • (2005) Free Radic Biol Med , vol.38 , pp. 665-677
    • Bota, D.A.1    Ngo, J.K.2    Davies, K.J.3


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