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Volumn 97, Issue 6, 2006, Pages 1659-1675

The role of mitochondria in inherited neurodegenerative diseases

Author keywords

Alzheimer's disease; Amyotrophic lateral sclerosis; Huntington's disease; Mitochondria; Neurodegeneration; Parkinson's disease

Indexed keywords

ALPHA SYNUCLEIN; GLUTATHIONE TRANSFERASE; MITOCHONDRIAL DNA; MITOCHONDRIAL PROTEIN; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE;

EID: 33745028132     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2006.03990.x     Document Type: Review
Times cited : (148)

References (199)
  • 1
    • 0033772264 scopus 로고    scopus 로고
    • OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28
    • Alexander C. Votruba M. Pesch U. E. et al. 2000 OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28. Nat. Genet. 26, 211 215.
    • (2000) Nat. Genet. , vol.26 , pp. 211-215
    • Alexander, C.1    Votruba, M.2    Pesch, U.E.3
  • 2
    • 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 H. K. Biswas G. Robin M. A. Avadhani N. G. 2003 Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells. J. Cell Biol. 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
  • 3
    • 0019423856 scopus 로고
    • Sequence and organization of the human mitochondrial genome
    • Anderson S. Bankier A. T. Barrell B. G. et al. 1981 Sequence and organization of the human mitochondrial genome. Nature 290, 457 465.
    • (1981) Nature , vol.290 , pp. 457-465
    • Anderson, S.1    Bankier, A.T.2    Barrell, B.G.3
  • 5
    • 0037009120 scopus 로고    scopus 로고
    • Membrane protein degradation by AAA proteases in mitochondria
    • Arnold I. Langer T. 2002 Membrane protein degradation by AAA proteases in mitochondria. Biochim. Biophys. Acta 1592, 89 96.
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 89-96
    • Arnold, I.1    Langer, T.2
  • 6
    • 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. Cassina L. Ballabio A. Marconi R. Langer T. Casari G. 2003 Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia. J. Cell Biol. 163, 777 787.
    • (2003) J. Cell Biol. , vol.163 , pp. 777-787
    • Atorino, L.1    Silvestri, L.2    Koppen, M.3    Cassina, L.4    Ballabio, A.5    Marconi, R.6    Langer, T.7    Casari, G.8
  • 9
    • 0037593949 scopus 로고    scopus 로고
    • Mitofusin-2 determines mitochondrial network architecture and mitochondrial metabolism. a novel regulatory mechanism altered in obesity
    • Bach D. Pich S. Soriano F. X. et al. 2003 Mitofusin-2 determines mitochondrial network architecture and mitochondrial metabolism. A novel regulatory mechanism altered in obesity. J. Biol. Chem. 278, 17 190 17 197.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17190-17197
    • Bach, D.1    Pich, S.2    Soriano, F.X.3
  • 10
    • 21544450545 scopus 로고    scopus 로고
    • P53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease
    • Bae B. I. Xu H. Igarashi S. et al. 2005 p53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease. Neuron 47, 29 41.
    • (2005) Neuron , vol.47 , pp. 29-41
    • Bae, B.I.1    Xu, H.2    Igarashi, S.3
  • 11
    • 0027204154 scopus 로고
    • Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate
    • Beal M. F. Brouillet E. Jenkins B. Henshaw R. Rosen B. Hyman B. T. 1993 Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate. J. Neurochem. 61, 1147 1150.
    • (1993) J. Neurochem. , vol.61 , pp. 1147-1150
    • Beal, M.F.1    Brouillet, E.2    Jenkins, B.3    Henshaw, R.4    Rosen, B.5    Hyman, B.T.6
  • 12
    • 33646375711 scopus 로고    scopus 로고
    • High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease
    • Bender A. Krishnan K. J. Morris C. M. et al. 2006 High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease. Nat. Genet. 38, 515 517.
    • (2006) Nat. Genet. , vol.38 , pp. 515-517
    • Bender, A.1    Krishnan, K.J.2    Morris, C.M.3
  • 14
    • 0042093555 scopus 로고    scopus 로고
    • Mitochondrial dysfunction due to mutant copper/zinc superoxide dismutase associated with amyotrophic lateral sclerosis is reversed by N-acetylcysteine
    • Beretta S. Sala G. Mattavelli L. Ceresa C. Casciati A. Ferri A. Carri M. T. Ferrarese C. 2003 Mitochondrial dysfunction due to mutant copper/zinc superoxide dismutase associated with amyotrophic lateral sclerosis is reversed by N-acetylcysteine. Neurobiol. Dis. 13, 213 221.
    • (2003) Neurobiol. Dis. , vol.13 , pp. 213-221
    • Beretta, S.1    Sala, G.2    Mattavelli, L.3    Ceresa, C.4    Casciati, A.5    Ferri, A.6    Carri, M.T.7    Ferrarese, C.8
  • 15
    • 11344262265 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system and Parkinson's diseases
    • Betarbet R. Sherer T. B. Greenamyre J. T. 2005 Ubiquitin-proteasome system and Parkinson's diseases. Exp Neurol. 191, S17 S27.
    • (2005) Exp Neurol. , vol.191
    • Betarbet, R.1    Sherer, T.B.2    Greenamyre, J.T.3
  • 17
    • 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. J. et al. 2003 Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 299, 256 259.
    • (2003) Science , vol.299 , pp. 256-259
    • Bonifati, V.1    Rizzu, P.2    Van Baren, M.J.3
  • 20
    • 18244390483 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in Alzheimer brain: Mechanistic implications
    • Bubber P. Haroutunian V. Fisch G. Blass J. P. Gibson G. E. 2005 Mitochondrial abnormalities in Alzheimer brain: mechanistic implications. Ann. Neurol. 57, 695 703.
    • (2005) Ann. Neurol. , vol.57 , pp. 695-703
    • Bubber, P.1    Haroutunian, V.2    Fisch, G.3    Blass, J.P.4    Gibson, G.E.5
  • 21
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • Bulteau A. L. O'Neill H. A. Kennedy M. C. Ikeda-Saito M. Isaya G. Szweda L. I. 2004 Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 305, 242 245.
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.L.1    O'Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 22
    • 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. Pigino G. Yuan M. Mori H. Yankner B. A. 2002 Altered metabolism of the amyloid beta precursor protein is associated with mitochondrial dysfunction in Down's syndrome. Neuron 33, 677 688.
    • (2002) Neuron , vol.33 , pp. 677-688
    • Busciglio, J.1    Pelsman, A.2    Wong, C.3    Pigino, G.4    Yuan, M.5    Mori, H.6    Yankner, B.A.7
  • 23
    • 9844222853 scopus 로고    scopus 로고
    • Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes
    • Campuzano V. Montermini L. Lutz Y. et al. 1997 Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes. Hum Mol Genet. 6, 1771 1780.
    • (1997) Hum Mol Genet. , vol.6 , pp. 1771-1780
    • Campuzano, V.1    Montermini, L.2    Lutz, Y.3
  • 24
    • 13344270899 scopus 로고    scopus 로고
    • Friedreich's ataxia: Autosomal recessive disease caused by an intronic GAA triplet repeat expansion
    • Campuzano V. Montermini L. Molto M. D. et al. 1996 Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion. Science 271, 1423 1427.
    • (1996) Science , vol.271 , pp. 1423-1427
    • Campuzano, V.1    Montermini, L.2    Molto, M.D.3
  • 26
    • 0037406049 scopus 로고    scopus 로고
    • Pathogenic expression of homoplasmic mtDNA mutations needs a complex nuclear-mitochondrial interaction
    • Carelli V. Giordano C. d'Amati G. 2003 Pathogenic expression of homoplasmic mtDNA mutations needs a complex nuclear-mitochondrial interaction. Trends Genet. 19, 257 262.
    • (2003) Trends Genet. , vol.19 , pp. 257-262
    • Carelli, V.1    Giordano, C.2    D'Amati, G.3
  • 28
    • 0031559896 scopus 로고    scopus 로고
    • Expression of a Cu,Zn superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca2+ concentration in transfected neuroblastoma SH-SY5Y cells
    • Carri M. T. Ferri A. Battistoni A. Famhy L. Gabbianelli R. Poccia F. Rotilio G. 1997 Expression of a Cu,Zn superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca2+ concentration in transfected neuroblastoma SH-SY5Y cells. FEBS Lett. 414, 365 368.
    • (1997) FEBS Lett. , vol.414 , pp. 365-368
    • Carri, M.T.1    Ferri, A.2    Battistoni, A.3    Famhy, L.4    Gabbianelli, R.5    Poccia, F.6    Rotilio, G.7
  • 29
    • 0032511186 scopus 로고    scopus 로고
    • Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease
    • Casari G. De Fusco M. Ciarmatori S. et al. 1998 Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease. Cell 93, 973 983.
    • (1998) Cell , vol.93 , pp. 973-983
    • Casari, G.1    De Fusco, M.2    Ciarmatori, S.3
  • 30
    • 0036272650 scopus 로고    scopus 로고
    • Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • Casley C. S. Canevari L. Land J. M. Clark J. B. Sharpe M. A. 2002 Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities. J. Neurochem. 80, 91 100.
    • (2002) J. Neurochem. , vol.80 , pp. 91-100
    • Casley, C.S.1    Canevari, L.2    Land, J.M.3    Clark, J.B.4    Sharpe, M.A.5
  • 32
    • 33646136884 scopus 로고    scopus 로고
    • Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons
    • Chang D. T. Rintoul G. L. Pandipati S. Reynolds I. J. 2006 Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons. Neurobiol. Dis. 22, 388 400.
    • (2006) Neurobiol. Dis. , vol.22 , pp. 388-400
    • Chang, D.T.1    Rintoul, G.L.2    Pandipati, S.3    Reynolds, I.J.4
  • 33
    • 27744491193 scopus 로고    scopus 로고
    • Emerging functions of mammalian mitochondrial fusion and fission
    • Chen H. Chan D. C. 2005 Emerging functions of mammalian mitochondrial fusion and fission. Hum. Mol. Genet. 14, Suppl. 2, R283 R289.
    • (2005) Hum. Mol. Genet. , vol.14 , Issue.2 SUPPL.
    • Chen, H.1    Chan, D.C.2
  • 35
    • 3543141113 scopus 로고    scopus 로고
    • Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release
    • Choo Y. S. Johnson G. V. MacDonald M. Detloff P. J. Lesort M. 2004 Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release. Hum. Mol. Genet. 13, 1407 1420.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1407-1420
    • Choo, Y.S.1    Johnson, G.V.2    MacDonald, M.3    Detloff, P.J.4    Lesort, M.5
  • 37
    • 7144253143 scopus 로고    scopus 로고
    • Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture
    • Cooper J. K. Schilling G. Peters M. F. et al. 1998 Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture. Hum. Mol. Genet. 7, 783 790.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 783-790
    • Cooper, J.K.1    Schilling, G.2    Peters, M.F.3
  • 39
    • 19944433571 scopus 로고    scopus 로고
    • Copper-dependent inhibition of human cytochrome c oxidase by a dimeric conformer of amyloid-beta1-42
    • Crouch P. J. Blake R. Duce J. A. et al. 2005 Copper-dependent inhibition of human cytochrome c oxidase by a dimeric conformer of amyloid-beta1-42. J. Neurosci. 25, 272 279.
    • (2005) J. Neurosci. , vol.25 , pp. 272-279
    • Crouch, P.J.1    Blake, R.2    Duce, J.A.3
  • 40
    • 0029433186 scopus 로고
    • Comparison of pathological alterations in ALS and a murine transgenic model: Pathogenetic implications
    • Dal Canto M. C. 1995 Comparison of pathological alterations in ALS and a murine transgenic model: pathogenetic implications. Clin. Neurosci. 3, 332 337.
    • (1995) Clin. Neurosci. , vol.3 , pp. 332-337
    • Dal Canto, M.C.1
  • 41
    • 0027946294 scopus 로고
    • Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis
    • Dal Canto M. C. Gurney M. E. 1994 Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis. Am. J. Pathol 145, 1271 1279.
    • (1994) Am. J. Pathol , vol.145 , pp. 1271-1279
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 42
    • 33645102302 scopus 로고    scopus 로고
    • Neural mitochondrial Ca2+ capacity impairment precedes the onset of motor symptoms in G93A Cu/Zn-superoxide dismutase mutant mice
    • Damiano M. Starkov A. A. Petri S. Kipiani K. Kiaei M. Mattiazzi M. Flint Beal M. Manfredi G. 2006 Neural mitochondrial Ca2+ capacity impairment precedes the onset of motor symptoms in G93A Cu/Zn-superoxide dismutase mutant mice. J. Neurochem. 96, 1349 1361.
    • (2006) J. Neurochem. , vol.96 , pp. 1349-1361
    • Damiano, M.1    Starkov, A.A.2    Petri, S.3    Kipiani, K.4    Kiaei, M.5    Mattiazzi, M.6    Flint Beal, M.7    Manfredi, G.8
  • 43
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • Danial N. N. Korsmeyer S. J. 2004 Cell death: critical control points. Cell 116, 205 219.
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 44
    • 0037338634 scopus 로고    scopus 로고
    • Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
    • Darios F. Corti O. Lucking C. B. et al. 2003 Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death. Hum. Mol. Genet. 12, 517 526.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 517-526
    • Darios, F.1    Corti, O.2    Lucking, C.B.3
  • 45
    • 0037195109 scopus 로고    scopus 로고
    • Resistance of alpha-synuclein null mice to the parkinsonian neurotoxin MPTP
    • Dauer W. Kholodilov N. Vila M. et al. 2002 Resistance of alpha-synuclein null mice to the parkinsonian neurotoxin MPTP. Proc. Natl. Acad. Sci. U.S.A. 99, 14 524 14 529.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 14524-14529
    • Dauer, W.1    Kholodilov, N.2    Vila, M.3
  • 46
    • 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 J. M. et al. 2000 Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy. Nat. Genet. 26, 207 210.
    • (2000) Nat. Genet. , vol.26 , pp. 207-210
    • Delettre, C.1    Lenaers, G.2    Griffoin, J.M.3
  • 47
    • 15944396616 scopus 로고    scopus 로고
    • Mitochondrial encephalomyopathies: An update
    • DiMauro S. Hirano M. 2005 Mitochondrial encephalomyopathies: an update. Neuromuscul. Disord. 15, 276 286.
    • (2005) Neuromuscul. Disord. , vol.15 , pp. 276-286
    • Dimauro, S.1    Hirano, M.2
  • 51
    • 0041522770 scopus 로고    scopus 로고
    • The hereditary spastic paraplegias: Nine genes and counting
    • Fink J. K. 2003 The hereditary spastic paraplegias: nine genes and counting. Arch. Neurol. 60, 1045 1049.
    • (2003) Arch. Neurol. , vol.60 , pp. 1045-1049
    • Fink, J.K.1
  • 53
    • 0031567601 scopus 로고    scopus 로고
    • Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria
    • Foury F. Cazzalini O. 1997 Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria. FEBS Lett. 411, 373 377.
    • (1997) FEBS Lett. , vol.411 , pp. 373-377
    • Foury, F.1    Cazzalini, O.2
  • 54
    • 31544445770 scopus 로고    scopus 로고
    • Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity
    • Gakh O. Park S. Liu G. Macomber L. Imlay J. A. Ferreira G. C. Isaya G. 2006 Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity. Hum. Mol. Genet. 15, 467 479.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 467-479
    • Gakh, O.1    Park, S.2    Liu, G.3    MacOmber, L.4    Imlay, J.A.5    Ferreira, G.C.6    Isaya, G.7
  • 55
    • 0030831352 scopus 로고    scopus 로고
    • Mutant superoxide dismutase-1-linked familial amyotrophic lateral sclerosis: Molecular mechanisms of neuronal death and protection
    • Ghadge G. D. Lee J. P. Bindokas V. P. Jordan J. Ma L. Miller R. J. Roos R. P. 1997 Mutant superoxide dismutase-1-linked familial amyotrophic lateral sclerosis: molecular mechanisms of neuronal death and protection. J. Neurosci. 17, 8756 8766.
    • (1997) J. Neurosci. , vol.17 , pp. 8756-8766
    • Ghadge, G.D.1    Lee, J.P.2    Bindokas, V.P.3    Jordan, J.4    Ma, L.5    Miller, R.J.6    Roos, R.P.7
  • 56
    • 0017839485 scopus 로고
    • Juvenile Huntington chorea: Clinical, ultrastructural, and biochemical studies
    • Goebel H. H. Heipertz R. Scholz W. Iqbal K. Tellez-Nagel I. 1978 Juvenile Huntington chorea: clinical, ultrastructural, and biochemical studies. Neurology 28, 23 31.
    • (1978) Neurology , vol.28 , pp. 23-31
    • Goebel, H.H.1    Heipertz, R.2    Scholz, W.3    Iqbal, K.4    Tellez-Nagel, I.5
  • 57
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • Goedert M. 2001 Alpha-synuclein and neurodegenerative diseases. Nat. Rev. Neurosci. 2, 492 501.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 492-501
    • Goedert, M.1
  • 58
    • 0034660695 scopus 로고    scopus 로고
    • The GAA*TTC triplet repeat expanded in Friedreich's ataxia impedes transcription elongation by T7 RNA polymerase in a length and supercoil dependent manner
    • Grabczyk E. Usdin K. 2000 The GAA*TTC triplet repeat expanded in Friedreich's ataxia impedes transcription elongation by T7 RNA polymerase in a length and supercoil dependent manner. Nucl. Acids Res. 28, 2815 2822.
    • (2000) Nucl. Acids Res. , vol.28 , pp. 2815-2822
    • Grabczyk, E.1    Usdin, K.2
  • 60
    • 15544380902 scopus 로고    scopus 로고
    • Genetic and genomic studies of Drosophila parkin mutants implicate oxidative stress and innate immune responses in pathogenesis
    • Greene J. C. Whitworth A. J. Andrews L. A. Parker T. J. Pallanck L. J. 2005 Genetic and genomic studies of Drosophila parkin mutants implicate oxidative stress and innate immune responses in pathogenesis. Hum. Mol. Genet. 14, 799 811.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 799-811
    • Greene, J.C.1    Whitworth, A.J.2    Andrews, L.A.3    Parker, T.J.4    Pallanck, L.J.5
  • 61
    • 0036241765 scopus 로고    scopus 로고
    • Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60
    • Hansen J. J. Durr A. Cournu-Rebeix I. et al. 2002 Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. Am. J. Hum. Genet. 70, 1328 1332.
    • (2002) Am. J. Hum. Genet. , vol.70 , pp. 1328-1332
    • Hansen, J.J.1    Durr, A.2    Cournu-Rebeix, I.3
  • 62
    • 19944373389 scopus 로고    scopus 로고
    • Nicastrin, presenilin, APH-1, and PEN-2 form active gamma-secretase complexes in mitochondria
    • Hansson C. A. Frykman S. Farmery M. R. et al. 2004 Nicastrin, presenilin, APH-1, and PEN-2 form active gamma-secretase complexes in mitochondria. J. Biol. Chem. 279, 51 654 51 660.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51654-51660
    • Hansson, C.A.1    Frykman, S.2    Farmery, M.R.3
  • 63
    • 0019782799 scopus 로고
    • Friedreich's ataxia: A clinical and genetic study of 90 families with an analysis of early diagnostic criteria and intrafamilial clustering of clinical features
    • Harding A. E. 1981 Friedreich's ataxia: a clinical and genetic study of 90 families with an analysis of early diagnostic criteria and intrafamilial clustering of clinical features. Brain 104, 589 620.
    • (1981) Brain , vol.104 , pp. 589-620
    • Harding, A.E.1
  • 64
    • 70449136625 scopus 로고
    • Prolongation of the normal life span by radiation protection chemicals
    • Harman D. 1957 Prolongation of the normal life span by radiation protection chemicals. J. Gerontol. 12, 257 263.
    • (1957) J. Gerontol. , vol.12 , pp. 257-263
    • Harman, D.1
  • 66
    • 0033574216 scopus 로고    scopus 로고
    • Rapid aggregate formation of the huntingtin N-terminal fragment carrying an expanded polyglutamine tract
    • Hazeki N. Nakamura K. Goto J. Kanazawa I. 1999 Rapid aggregate formation of the huntingtin N-terminal fragment carrying an expanded polyglutamine tract. Biochem. Biophys. Res. Commun. 256, 361 366.
    • (1999) Biochem. Biophys. Res. Commun. , vol.256 , pp. 361-366
    • Hazeki, N.1    Nakamura, K.2    Goto, J.3    Kanazawa, I.4
  • 68
    • 33645793947 scopus 로고    scopus 로고
    • UCHL-1 is not a Parkinson's disease susceptibility gene
    • Healy D. G. Abou-Sleiman P. M. Casas J. P. et al. 2006 UCHL-1 is not a Parkinson's disease susceptibility gene. Ann. Neurol. 59, 627 633.
    • (2006) Ann. Neurol. , vol.59 , pp. 627-633
    • Healy, D.G.1    Abou-Sleiman, P.M.2    Casas, J.P.3
  • 69
    • 0037088793 scopus 로고    scopus 로고
    • Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS
    • Higgins C. M. Jung C. Ding H. Xu Z. 2002 Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS. J Neurosci. 22, RC215.
    • (2002) J Neurosci. , vol.22
    • Higgins, C.M.1    Jung, C.2    Ding, H.3    Xu, Z.4
  • 70
    • 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 C. M. Jung C. Xu Z. 2003 ALS-associated mutant SOD1G93A causes mitochondrial vacuolation by expansion of the intermembrane space and by involvement of SOD1 aggregation and peroxisomes. BMC Neurosci. 4, 16.
    • (2003) BMC Neurosci. , vol.4 , pp. 16
    • Higgins, C.M.1    Jung, C.2    Xu, Z.3
  • 71
    • 0030813676 scopus 로고    scopus 로고
    • Population genetics and disease susceptibility: Characterization of central European haplogroups by mtDNA gene mutations, correlation with D loop variants and association with disease
    • Hofmann S. Jaksch M. Bezold R. Mertens S. Aholt S. Paprotta A. Gerbitz K. D. 1997 Population genetics and disease susceptibility: characterization of central European haplogroups by mtDNA gene mutations, correlation with D loop variants and association with disease. Hum. Mol. Genet. 6, 1835 1846.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1835-1846
    • Hofmann, S.1    Jaksch, M.2    Bezold, R.3    Mertens, S.4    Aholt, S.5    Paprotta, A.6    Gerbitz, K.D.7
  • 72
    • 0025267548 scopus 로고
    • A new mitochondrial disease associated with mitochondrial DNA heteroplasmy
    • Holt I. J. Harding A. E. Petty R. K. Morgan-Hughes J. A. 1990 A new mitochondrial disease associated with mitochondrial DNA heteroplasmy. Am. J. HumGenet. 46, 428 433.
    • (1990) Am. J. HumGenet. , vol.46 , pp. 428-433
    • Holt, I.J.1    Harding, A.E.2    Petty, R.K.3    Morgan-Hughes, J.A.4
  • 73
    • 23844545553 scopus 로고    scopus 로고
    • Mutational analysis of action of mitochondrial fusion factor mitofusin-2
    • Honda S. Aihara T. Hontani M. Okubo K. Hirose S. 2005 Mutational analysis of action of mitochondrial fusion factor mitofusin-2. J. Cell Sci. 118, 3153 3161.
    • (2005) J. Cell Sci. , vol.118 , pp. 3153-3161
    • Honda, S.1    Aihara, T.2    Hontani, M.3    Okubo, K.4    Hirose, S.5
  • 74
    • 0029006067 scopus 로고
    • Altered properties of mitochondrial ATP-synthase in patients with a T→G mutation in the ATPase 6 (subunit a) gene at position 8993 of mtDNA
    • Houstek J. Klement P. Hermanska J. Houstkova H. Hansikova H. Van den Bogert C. Zeman J. 1995 Altered properties of mitochondrial ATP-synthase in patients with a T→G mutation in the ATPase 6 (subunit a) gene at position 8993 of mtDNA. Biochim. Biophys. Acta 1271, 349 357.
    • (1995) Biochim. Biophys. Acta , vol.1271 , pp. 349-357
    • Houstek, J.1    Klement, P.2    Hermanska, J.3    Houstkova, H.4    Hansikova, H.5    Van Den Bogert, C.6    Zeman, J.7
  • 77
    • 0037454668 scopus 로고    scopus 로고
    • Inhibition of the alpha-ketoglutarate dehydrogenase complex alters mitochondrial function and cellular calcium regulation
    • Huang H. M. Zhang H. Xu H. Gibson G. E. 2003 Inhibition of the alpha-ketoglutarate dehydrogenase complex alters mitochondrial function and cellular calcium regulation. Biochim. Biophys. Acta 1637, 119 126.
    • (2003) Biochim. Biophys. Acta , vol.1637 , pp. 119-126
    • Huang, H.M.1    Zhang, H.2    Xu, H.3    Gibson, G.E.4
  • 78
    • 10744223086 scopus 로고    scopus 로고
    • The crucial role of caspase-9 in the disease progression of a transgenic ALS mouse model
    • Inoue H. Tsukita K. Iwasato T. et al. 2003 The crucial role of caspase-9 in the disease progression of a transgenic ALS mouse model. EMBO J. 22, 6665 6674.
    • (2003) EMBO J. , vol.22 , pp. 6665-6674
    • Inoue, H.1    Tsukita, K.2    Iwasato, T.3
  • 80
    • 0027741301 scopus 로고
    • Evidence for impairment of energy metabolism in vivo in Huntington's disease using localized 1H NMR spectroscopy
    • Jenkins B. G. Koroshetz W. J. Beal M. F. Rosen B. R. 1993 Evidence for impairment of energy metabolism in vivo in Huntington's disease using localized 1H NMR spectroscopy. Neurology 43, 2689 2695.
    • (1993) Neurology , vol.43 , pp. 2689-2695
    • Jenkins, B.G.1    Koroshetz, W.J.2    Beal, M.F.3    Rosen, B.R.4
  • 81
    • 0036830072 scopus 로고    scopus 로고
    • Mitochondrial electron transport chain complex dysfunction in a transgenic mouse model for amyotrophic lateral sclerosis
    • Jung C. Higgins C. M. Xu Z. 2002 Mitochondrial electron transport chain complex dysfunction in a transgenic mouse model for amyotrophic lateral sclerosis. J. Neurochem. 83, 535 545.
    • (2002) J. Neurochem. , vol.83 , pp. 535-545
    • Jung, C.1    Higgins, C.M.2    Xu, Z.3
  • 82
    • 1542373685 scopus 로고    scopus 로고
    • Transcriptional regulatory circuits controlling mitochondrial biogenesis and function
    • Kelly D. P. Scarpulla R. C. 2004 Transcriptional regulatory circuits controlling mitochondrial biogenesis and function. Genes Dev. 18, 357 368.
    • (2004) Genes Dev. , vol.18 , pp. 357-368
    • Kelly, D.P.1    Scarpulla, R.C.2
  • 83
    • 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. H. Smith P. D. Aleyasin H. et al. 2005 Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress. Proc. Natl. Acad. Sci. U.S.A. 102, 5215 5220.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 5215-5220
    • Kim, R.H.1    Smith, P.D.2    Aleyasin, H.3
  • 88
    • 0032079517 scopus 로고    scopus 로고
    • Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1
    • Kong J. Xu Z. 1998 Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1. J. Neurosci. 18, 3241 3250.
    • (1998) J. Neurosci. , vol.18 , pp. 3241-3250
    • Kong, J.1    Xu, Z.2
  • 89
    • 0031044805 scopus 로고    scopus 로고
    • Energy metabolism defects in Huntington's disease and effects of coenzyme Q10
    • Koroshetz W. J. Jenkins B. G. Rosen B. R. Beal M. F. 1997 Energy metabolism defects in Huntington's disease and effects of coenzyme Q10. Ann. Neurol. 41, 160 165.
    • (1997) Ann. Neurol. , vol.41 , pp. 160-165
    • Koroshetz, W.J.1    Jenkins, B.G.2    Rosen, B.R.3    Beal, M.F.4
  • 90
    • 0030756459 scopus 로고    scopus 로고
    • Bcl-2: Prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Kostic V. Jackson-Lewis V. de Bilbao F. Dubois-Dauphin M. Przedborski S. 1997 Bcl-2: prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis. Science 277, 559 562.
    • (1997) Science , vol.277 , pp. 559-562
    • Kostic, V.1    Jackson-Lewis, V.2    De Bilbao, F.3    Dubois-Dauphin, M.4    Przedborski, S.5
  • 91
    • 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. C. Geula C. Kowall N. W. Khrapko K. 2006 Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons. Nat Genet. 38, 518 520.
    • (2006) Nat Genet. , vol.38 , pp. 518-520
    • Kraytsberg, Y.1    Kudryavtseva, E.2    McKee, A.C.3    Geula, C.4    Kowall, N.W.5    Khrapko, K.6
  • 92
    • 0032731637 scopus 로고    scopus 로고
    • ALS-linked Cu/Zn-SOD mutation increases vulnerability of motor neurons to excitotoxicity by a mechanism involving increased oxidative stress and perturbed calcium homeostasis
    • Kruman I. I. Pedersen W. A. Springer J. E. Mattson M. P. 1999 ALS-linked Cu/Zn-SOD mutation increases vulnerability of motor neurons to excitotoxicity by a mechanism involving increased oxidative stress and perturbed calcium homeostasis. Exp. Neurol. 160, 28 39.
    • (1999) Exp. Neurol. , vol.160 , pp. 28-39
    • Kruman, I.I.1    Pedersen, W.A.2    Springer, J.E.3    Mattson, M.P.4
  • 95
    • 0020680904 scopus 로고
    • Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis
    • Langston J. W. Ballard P. Tetrud J. W. Irwin I. 1983 Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis. Science 219, 979 980.
    • (1983) Science , vol.219 , pp. 979-980
    • Langston, J.W.1    Ballard, P.2    Tetrud, J.W.3    Irwin, I.4
  • 96
    • 28844499005 scopus 로고    scopus 로고
    • Mitochondrial cyclic AMP response element-binding protein (CREB) mediates mitochondrial gene expression and neuronal survival
    • Lee J. Kim C. H. Simon D. K. et al. 2005 Mitochondrial cyclic AMP response element-binding protein (CREB) mediates mitochondrial gene expression and neuronal survival. J. Biol. Chem. 280, 40 398 40 401.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40398-40401
    • Lee, J.1    Kim, C.H.2    Simon, D.K.3
  • 97
    • 0000376151 scopus 로고
    • Subacute necrotizing encephalomyelopathy in an infant
    • Leigh D. 1951 Subacute necrotizing encephalomyelopathy in an infant. J. Neurol. Neurosurg Psychiatry 14, 216 221.
    • (1951) J. Neurol. Neurosurg Psychiatry , vol.14 , pp. 216-221
    • Leigh, D.1
  • 98
    • 0032190090 scopus 로고    scopus 로고
    • The ubiquitin pathway in Parkinson's disease
    • Leroy E. Boyer R. Auburger G. et al. 1998 The ubiquitin pathway in Parkinson's disease. Nature 395, 451 452.
    • (1998) Nature , vol.395 , pp. 451-452
    • Leroy, E.1    Boyer, R.2    Auburger, G.3
  • 99
    • 0036173896 scopus 로고    scopus 로고
    • Interaction of Huntington disease protein with transcriptional activator Sp1
    • Li S. H. Cheng A. L. Zhou H. Lam S. Rao M. Li H. Li X. J. 2002 Interaction of Huntington disease protein with transcriptional activator Sp1. Mol. Cell Biol. 22, 1277 1287.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 1277-1287
    • Li, S.H.1    Cheng, A.L.2    Zhou, H.3    Lam, S.4    Rao, M.5    Li, H.6    Li, X.J.7
  • 100
    • 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. 2004 The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses. Cell 119, 873 887.
    • (2004) Cell , vol.119 , pp. 873-887
    • Li, Z.1    Okamoto, K.2    Hayashi, Y.3    Sheng, M.4
  • 101
    • 0034647003 scopus 로고    scopus 로고
    • Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model
    • Li M. Ona V. O. Guegan C. et al. 2000 Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model. Science 288, 335 339.
    • (2000) Science , vol.288 , pp. 335-339
    • Li, M.1    Ona, V.O.2    Guegan, C.3
  • 102
    • 0037081814 scopus 로고    scopus 로고
    • High aggregate burden of somatic mtDNA point mutations in aging and Alzheimer's disease brain
    • Lin M. T. Simon D. K. Ahn C. H. Kim L. M. Beal M. F. 2002 High aggregate burden of somatic mtDNA point mutations in aging and Alzheimer's disease brain. Hum. Mol. Genet. 11, 133 145.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 133-145
    • Lin, M.T.1    Simon, D.K.2    Ahn, C.H.3    Kim, L.M.4    Beal, M.F.5
  • 103
    • 5344252327 scopus 로고    scopus 로고
    • Defects in adaptive energy metabolism with CNS-linked hyperactivity in PGC-1alpha null mice
    • Lin J. Wu P. H. Tarr P. T. et al. 2004 Defects in adaptive energy metabolism with CNS-linked hyperactivity in PGC-1alpha null mice. Cell 119, 121 135.
    • (2004) Cell , vol.119 , pp. 121-135
    • Lin, J.1    Wu, P.H.2    Tarr, P.T.3
  • 104
    • 3242701496 scopus 로고    scopus 로고
    • Toxicity of familial ALS-linked SOD1 mutants from selective recruitment to spinal mitochondria
    • Liu J. Lillo C. Jonsson P. A. et al. 2004 Toxicity of familial ALS-linked SOD1 mutants from selective recruitment to spinal mitochondria. Neuron 43, 5 17.
    • (2004) Neuron , vol.43 , pp. 5-17
    • Liu, J.1    Lillo, C.2    Jonsson, P.A.3
  • 106
    • 0026357457 scopus 로고
    • 3-Nitropropionic acid-exogenous animal neurotoxin and possible human striatal toxin
    • Ludolph A. C. He F. Spencer P. S. Hammerstad J. Sabri M. 1991 3-Nitropropionic acid-exogenous animal neurotoxin and possible human striatal toxin. Can. J. Neurol. Sci. 18, 492 498.
    • (1991) Can. J. Neurol. Sci. , vol.18 , pp. 492-498
    • Ludolph, A.C.1    He, F.2    Spencer, P.S.3    Hammerstad, J.4    Sabri, M.5
  • 107
    • 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. O. et al. 2004 Parkinsonism, premature menopause, and mitochondrial DNA polymerase gamma mutations: clinical and molecular genetic study. Lancet 364, 875 882.
    • (2004) Lancet , vol.364 , pp. 875-882
    • Luoma, P.1    Melberg, A.2    Rinne, J.O.3
  • 108
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease
    • Lustbader J. W. Cirilli M. Lin C. et al. 2004 ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science 304, 448 452.
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3
  • 109
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A{beta} accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • Manczak M. Anekonda T. S. Henson E. Park B. S. Quinn J. Reddy P. H. 2006 Mitochondria are a direct site of A{beta} accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression. Hum. Mol. Genet. 15, 1437 1449.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Reddy, P.H.6
  • 110
    • 0033515548 scopus 로고    scopus 로고
    • Oligomycin induces a decrease in the cellular content of a pathogenic mutation in the human mitochondrial ATPase 6 gene
    • Manfredi G. Gupta N. Vazquez-Memije M. E. Sadlock J. E. Spinazzola A. De Vivo D. C. Schon E. A. 1999 Oligomycin induces a decrease in the cellular content of a pathogenic mutation in the human mitochondrial ATPase 6 gene. J. Biol. Chem. 274, 9386 9391.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9386-9391
    • Manfredi, G.1    Gupta, N.2    Vazquez-Memije, M.E.3    Sadlock, J.E.4    Spinazzola, A.5    De Vivo, D.C.6    Schon, E.A.7
  • 112
    • 7644230386 scopus 로고    scopus 로고
    • Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice
    • Martins L. M. Morrison A. Klupsch K. et al. 2004 Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice. Mol. Cell Biol. 24, 9848 9862.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 9848-9862
    • Martins, L.M.1    Morrison, A.2    Klupsch, K.3
  • 114
    • 1942453308 scopus 로고    scopus 로고
    • The mtDNA T8993G (NARP) mutation results in an impairment of oxidative phosphorylation that can be improved by antioxidants
    • Mattiazzi M. Vijayvergiya C. Gajewski C. D. DeVivo D. C. Lenaz G. Wiedmann M. Manfredi G. 2004 The mtDNA T8993G (NARP) mutation results in an impairment of oxidative phosphorylation that can be improved by antioxidants. Hum. Mol. Genet. 13, 869 879.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 869-879
    • Mattiazzi, M.1    Vijayvergiya, C.2    Gajewski, C.D.3    Devivo, D.C.4    Lenaz, G.5    Wiedmann, M.6    Manfredi, G.7
  • 115
    • 0037194221 scopus 로고    scopus 로고
    • Cellular localization and development of neuronal intranuclear inclusions in striatal and cortical neurons in R6/2 transgenic mice
    • Meade C. A. Deng Y. P. Fusco F. R. Del Mar. N. Hersch S. Goldowitz D. Reiner A. 2002 Cellular localization and development of neuronal intranuclear inclusions in striatal and cortical neurons in R6/2 transgenic mice. J. Comp. Neurol. 449, 241 269.
    • (2002) J. Comp. Neurol. , vol.449 , pp. 241-269
    • Meade, C.A.1    Deng, Y.P.2    Fusco, F.R.3    Del Mar., N.4    Hersch, S.5    Goldowitz, D.6    Reiner, A.7
  • 116
    • 0030943110 scopus 로고    scopus 로고
    • Effects of wild-type and mutated copper/zinc superoxide dismutase on neuronal survival and L-DOPA-induced toxicity in postnatal midbrain culture
    • Mena M. A. Khan U. Togasaki D. M. Sulzer D. Epstein C. J. Przedborski S. 1997 Effects of wild-type and mutated copper/zinc superoxide dismutase on neuronal survival and L-DOPA-induced toxicity in postnatal midbrain culture. J. Neurochem. 69, 21 33.
    • (1997) J. Neurochem. , vol.69 , pp. 21-33
    • Mena, M.A.1    Khan, U.2    Togasaki, D.M.3    Sulzer, D.4    Epstein, C.J.5    Przedborski, S.6
  • 118
    • 0035692636 scopus 로고    scopus 로고
    • DJ-1 is an indicator for endogenous reactive oxygen species elicited by endotoxin
    • Mitsumoto A. Nakagawa Y. 2001 DJ-1 is an indicator for endogenous reactive oxygen species elicited by endotoxin. Free Radic. Res. 35, 885 893.
    • (2001) Free Radic. Res. , vol.35 , pp. 885-893
    • Mitsumoto, A.1    Nakagawa, Y.2
  • 120
    • 0023068586 scopus 로고
    • Motor neuron disease: Epidemiologic studies
    • Mulder D. W. Kurland L. T. 1987 Motor neuron disease: epidemiologic studies. Adv. Exp. Med. Biol. 209, 325 332.
    • (1987) Adv. Exp. Med. Biol. , vol.209 , pp. 325-332
    • Mulder, D.W.1    Kurland, L.T.2
  • 121
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • Mutisya E. M. Bowling A. C. Beal M. F. 1994 Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J. Neurochem. 63, 2179 2184.
    • (1994) J. Neurochem. , vol.63 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 122
    • 0042035647 scopus 로고    scopus 로고
    • Interactions between mitochondrial bioenergetics and cytoplasmic calcium in cultured cerebellar granule cells
    • Nicholls D. G. Vesce S. Kirk L. Chalmers S. 2003 Interactions between mitochondrial bioenergetics and cytoplasmic calcium in cultured cerebellar granule cells. Cell Calcium 34, 407 424.
    • (2003) Cell Calcium , vol.34 , pp. 407-424
    • Nicholls, D.G.1    Vesce, S.2    Kirk, L.3    Chalmers, S.4
  • 123
    • 0021810979 scopus 로고
    • Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1, 2,5,6-tetrahydropyridine
    • Nicklas W. J. Vyas I. Heikkila R. E. 1985 Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine. Life Sci. 36, 2503 2508.
    • (1985) Life Sci. , vol.36 , pp. 2503-2508
    • Nicklas, W.J.1    Vyas, I.2    Heikkila, R.E.3
  • 124
    • 26844484821 scopus 로고    scopus 로고
    • The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria
    • Nolden M. Ehses S. Koppen M. Bernacchia A. Rugarli E. I. Langer T. 2005 The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria. Cell 123, 277 289.
    • (2005) Cell , vol.123 , pp. 277-289
    • Nolden, M.1    Ehses, S.2    Koppen, M.3    Bernacchia, A.4    Rugarli, E.I.5    Langer, T.6
  • 125
    • 0034923434 scopus 로고    scopus 로고
    • Oxidative damage is the earliest event in Alzheimer disease
    • Nunomura A. Perry G. Aliev G. et al. 2001 Oxidative damage is the earliest event in Alzheimer disease. J. Neuropathol. Exp. Neurol. 60, 759 767.
    • (2001) J. Neuropathol. Exp. Neurol. , vol.60 , pp. 759-767
    • Nunomura, A.1    Perry, G.2    Aliev, G.3
  • 126
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
    • Okado-Matsumoto A. Fridovich I. 2001 Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria. J. Biol. Chem. 276, 38 388 38 393.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 128
    • 0037125183 scopus 로고    scopus 로고
    • The human dynamin-related protein OPA1 is anchored to the mitochondrial inner membrane facing the inter-membrane space
    • Olichon A. Emorine L. J. Descoins E. et al. 2002 The human dynamin-related protein OPA1 is anchored to the mitochondrial inner membrane facing the inter-membrane space. FEBS Lett. 523, 171 176.
    • (2002) FEBS Lett. , vol.523 , pp. 171-176
    • Olichon, A.1    Emorine, L.J.2    Descoins, E.3
  • 129
    • 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 I. G. Bennett J. P. Jr. Tuttle J. B. 2005 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. 19, 312 322.
    • (2005) Neurobiol. Dis. , vol.19 , pp. 312-322
    • Onyango, I.G.1    Bennett Jr., J.P.2    Tuttle, J.B.3
  • 133
    • 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 M. E. Lennon N. Bacskai B. J. Hyman B. T. Trotti D. Brown R. H. Jr. 2004 Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria. Neuron 43, 19 30.
    • (2004) Neuron , vol.43 , pp. 19-30
    • Pasinelli, P.1    Belford, M.E.2    Lennon, N.3    Bacskai, B.J.4    Hyman, B.T.5    Trotti, D.6    Brown Jr., R.H.7
  • 135
    • 26644440926 scopus 로고    scopus 로고
    • Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations
    • Petit A. Kawarai T. Paitel E. et al. 2005 Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations. J. Biol. Chem. 280, 34 025 34 032.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34025-34032
    • Petit, A.1    Kawarai, T.2    Paitel, E.3
  • 136
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos M. H. Lavedan C. Leroy E. et al. 1997 Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276, 2045 2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3
  • 137
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • Puccio H. Simon D. Cossee M. Criqui-Filipe P. Tiziano F. Melki J. Hindelang C. Matyas R. Rustin P. Koenig M. 2001 Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat. Genet. 27, 181 186.
    • (2001) Nat. Genet. , vol.27 , pp. 181-186
    • Puccio, H.1    Simon, D.2    Cossee, M.3    Criqui-Filipe, P.4    Tiziano, F.5    Melki, J.6    Hindelang, C.7    Matyas, R.8    Rustin, P.9    Koenig, M.10
  • 138
    • 0037326196 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma coactivator 1 alpha (PGC-1 alpha): Transcriptional coactivator and metabolic regulator
    • Puigserver P. Spiegelman B. M. 2003 Peroxisome proliferator-activated receptor-gamma coactivator 1 alpha (PGC-1 alpha): transcriptional coactivator and metabolic regulator. Endocr. Rev. 24, 78 90.
    • (2003) Endocr. Rev. , vol.24 , pp. 78-90
    • Puigserver, P.1    Spiegelman, B.M.2
  • 139
    • 20144389920 scopus 로고    scopus 로고
    • Mitochondrial DNA haplogroup cluster UKJT reduces the risk of PD
    • Pyle A. Foltynie T. Tiangyou W. et al. 2005 Mitochondrial DNA haplogroup cluster UKJT reduces the risk of PD. Ann. Neurol. 57, 564 567.
    • (2005) Ann. Neurol. , vol.57 , pp. 564-567
    • Pyle, A.1    Foltynie, T.2    Tiangyou, W.3
  • 140
  • 141
    • 85047690706 scopus 로고    scopus 로고
    • Frataxin deficiency in pancreatic islets causes diabetes due to loss of beta cell mass
    • Ristow M. Mulder H. Pomplun D. et al. 2003 Frataxin deficiency in pancreatic islets causes diabetes due to loss of beta cell mass. J. Clin. Invest. 112, 527 534.
    • (2003) J. Clin. Invest. , vol.112 , pp. 527-534
    • Ristow, M.1    Mulder, H.2    Pomplun, D.3
  • 143
    • 0029847118 scopus 로고    scopus 로고
    • Excitotoxicity hypothesis
    • discussion S26.
    • Rothstein J. D. 1996 Excitotoxicity hypothesis. Neurology 47, S19 S25 discussion S26.
    • (1996) Neurology , vol.47
    • Rothstein, J.D.1
  • 145
    • 0033120042 scopus 로고    scopus 로고
    • Sticky DNA: Self-Assocation properties of Long EAA. TCC repeats in R.R.Y triplex strutures from Friedreich's ataxia
    • Sakamoto N. Chastain P. D. Parniewski P. Ohshima K. Pandolfo M. Griffith J. D. Wells R. D. 1999 Sticky DNA: Self-Assocation properties of Long EAA. TCC repeats in R.R.Y triplex strutures from Friedreich's ataxia. Mol. Cell 4, 465 475.
    • (1999) Mol. Cell , vol.4 , pp. 465-475
    • Sakamoto, N.1    Chastain, P.D.2    Parniewski, P.3    Ohshima, K.4    Pandolfo, M.5    Griffith, J.D.6    Wells, R.D.7
  • 146
    • 0035057837 scopus 로고    scopus 로고
    • Control of mitochondrial morphology by a human mitofusin
    • Santel A. Fuller M. T. 2001 Control of mitochondrial morphology by a human mitofusin. J. Cell Sci. 114, 867 874.
    • (2001) J. Cell Sci. , vol.114 , pp. 867-874
    • Santel, A.1    Fuller, M.T.2
  • 147
    • 0034642203 scopus 로고    scopus 로고
    • Oxidative stress in patients with Friedreich ataxia
    • Schulz J. B. Dehmer T. Schols L. et al. 2000 Oxidative stress in patients with Friedreich ataxia. Neurology 55, 1719 1721.
    • (2000) Neurology , vol.55 , pp. 1719-1721
    • Schulz, J.B.1    Dehmer, T.2    Schols, L.3
  • 148
    • 26444441008 scopus 로고    scopus 로고
    • HD CAG repeat implicates a dominant property of huntingtin in mitochondrial energy metabolism
    • Seong I. S. Ivanova E. Lee J. M. et al. 2005 HD CAG repeat implicates a dominant property of huntingtin in mitochondrial energy metabolism. Hum. Mol. Genet. 14, 2871 2880.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2871-2880
    • Seong, I.S.1    Ivanova, E.2    Lee, J.M.3
  • 149
    • 14044273058 scopus 로고    scopus 로고
    • Friedreich ataxia: The oxidative stress paradox
    • Seznec H. Simon D. Bouton C. et al. 2005 Friedreich ataxia: the oxidative stress paradox. Hum. Mol. Genet. 14, 463 474.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 463-474
    • Seznec, H.1    Simon, D.2    Bouton, C.3
  • 150
    • 0033933048 scopus 로고    scopus 로고
    • Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
    • Shimura H. Hattori N. Kubo S. et al. 2000 Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat. Genet. 25, 302 305.
    • (2000) Nat. Genet. , vol.25 , pp. 302-305
    • Shimura, H.1    Hattori, N.2    Kubo, S.3
  • 151
    • 0035918258 scopus 로고    scopus 로고
    • Mutant Cu/Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis
    • Shinder G. A. Lacourse M. C. Minotti S. Durham H. D. 2001 Mutant Cu/Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis. J. Biol. Chem. 276, 12 791 12 796.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12791-12796
    • Shinder, G.A.1    Lacourse, M.C.2    Minotti, S.3    Durham, H.D.4
  • 152
    • 0037227946 scopus 로고    scopus 로고
    • Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis
    • Shirane M. Nakayama K. I. 2003 Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis. Nat. Cell Biol. 5, 28 37.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 28-37
    • Shirane, M.1    Nakayama, K.I.2
  • 154
    • 0033544323 scopus 로고    scopus 로고
    • Familial multisystem degeneration with parkinsonism associated with the 11778 mitochondrial DNA mutation
    • Simon D. K. Pulst S. M. Sutton J. P. Browne S. E. Beal M. F. Johns D. R. 1999 Familial multisystem degeneration with parkinsonism associated with the 11778 mitochondrial DNA mutation. Neurology 53, 1787 1793.
    • (1999) Neurology , vol.53 , pp. 1787-1793
    • Simon, D.K.1    Pulst, S.M.2    Sutton, J.P.3    Browne, S.E.4    Beal, M.F.5    Johns, D.R.6
  • 155
    • 0034620483 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations in complex I and tRNA genes in Parkinson's disease
    • Simon D. K. Mayeux R. Marder K. Kowall N. W. Beal M. F. Johns D. R. 2000 Mitochondrial DNA mutations in complex I and tRNA genes in Parkinson's disease. Neurology 54, 703 709.
    • (2000) Neurology , vol.54 , pp. 703-709
    • Simon, D.K.1    Mayeux, R.2    Marder, K.3    Kowall, N.W.4    Beal, M.F.5    Johns, D.R.6
  • 156
    • 1442324707 scopus 로고    scopus 로고
    • Friedreich ataxia mouse models with progressive cerebellar and sensory ataxia reveal autophagic neurodegeneration in dorsal root ganglia
    • Simon D. Seznec H. Gansmuller A. Carelle N. Weber P. Metzger D. Rustin P. Koenig M. Puccio H. 2004 Friedreich ataxia mouse models with progressive cerebellar and sensory ataxia reveal autophagic neurodegeneration in dorsal root ganglia. J. Neurosci. 24, 1987 1995.
    • (2004) J. Neurosci. , vol.24 , pp. 1987-1995
    • Simon, D.1    Seznec, H.2    Gansmuller, A.3    Carelle, N.4    Weber, P.5    Metzger, D.6    Rustin, P.7    Koenig, M.8    Puccio, H.9
  • 157
    • 0026471872 scopus 로고
    • Accumulation of deletions in human mitochondrial DNA during normal aging: Analysis by quantitative PCR
    • Simonetti S. Chen X. DiMauro S. Schon E. A. 1992 Accumulation of deletions in human mitochondrial DNA during normal aging: analysis by quantitative PCR. Biochim. Biophys. Acta 1180, 113 122.
    • (1992) Biochim. Biophys. Acta , vol.1180 , pp. 113-122
    • Simonetti, S.1    Chen, X.2    Dimauro, S.3    Schon, E.A.4
  • 159
    • 1542617769 scopus 로고    scopus 로고
    • Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP
    • Song D. D. Shults C. W. Sisk A. Rockenstein E. Masliah E. 2004 Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP. Exp. Neurol. 186, 158 172.
    • (2004) Exp. Neurol. , vol.186 , pp. 158-172
    • Song, D.D.1    Shults, C.W.2    Sisk, A.3    Rockenstein, E.4    Masliah, E.5
  • 160
    • 0027021442 scopus 로고
    • Mosaicism for a specific somatic mitochondrial DNA mutation in adult human brain
    • Soong N. W. Hinton D. R. Cortopassi G. Arnheim N. 1992 Mosaicism for a specific somatic mitochondrial DNA mutation in adult human brain. Nat. Genet. 2, 318 323.
    • (1992) Nat. Genet. , vol.2 , pp. 318-323
    • Soong, N.W.1    Hinton, D.R.2    Cortopassi, G.3    Arnheim, N.4
  • 161
    • 20044385920 scopus 로고    scopus 로고
    • Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease
    • Stokin G. B. Lillo C. Falzone T. L. et al. 2005 Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease. Science 307, 1282 1288.
    • (2005) Science , vol.307 , pp. 1282-1288
    • Stokin, G.B.1    Lillo, C.2    Falzone, T.L.3
  • 162
    • 25444498785 scopus 로고    scopus 로고
    • Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease
    • Strauss K. M. Martins L. M. Plun-Favreau H. et al. 2005 Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease. Hum. Mol. Genet. 14, 2099 2111.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2099-2111
    • Strauss, K.M.1    Martins, L.M.2    Plun-Favreau, H.3
  • 163
    • 0035851122 scopus 로고    scopus 로고
    • A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. a physiological role for SOD1 in guarding against mitochondrial oxidative damage
    • Sturtz L. A. Diekert K. Jensen L. T. Lill R. Culotta V. C. 2001 A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. J. Biol. Chem. 276, 38 084 38 089.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38084-38089
    • Sturtz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Culotta, V.C.5
  • 164
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki Y. Imai Y. Nakayama H. Takahashi K. Takio K. Takahashi R. 2001 A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol. Cell 8, 613 621.
    • (2001) Mol. Cell , vol.8 , pp. 613-621
    • Suzuki, Y.1    Imai, Y.2    Nakayama, H.3    Takahashi, K.4    Takio, K.5    Takahashi, R.6
  • 167
    • 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. Doyu M. Sobue G. 2002 Mitochondrial localization of mutant superoxide dismutase 1 triggers caspase-dependent cell death in a cellular model of familial amyotrophic lateral sclerosis. J. Biol. Chem. 277, 50 966 50 972.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50966-50972
    • Takeuchi, H.1    Kobayashi, Y.2    Ishigaki, S.3    Doyu, M.4    Sobue, G.5
  • 169
    • 0042232039 scopus 로고    scopus 로고
    • Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease
    • Tao X. Tong L. 2003 Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease. J. Biol. Chem. 278, 31 372 31 379.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31372-31379
    • Tao, X.1    Tong, L.2
  • 170
    • 0027244336 scopus 로고
    • The mitochondrial DNA mutation at 8993 associated with NARP slows the rate of ATP synthesis in isolated lymphoblast mitochondria
    • Tatuch Y. Robinson B. H. 1993 The mitochondrial DNA mutation at 8993 associated with NARP slows the rate of ATP synthesis in isolated lymphoblast mitochondria. Biochem. Biophys. Res. Commun. 192, 124 128.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 124-128
    • Tatuch, Y.1    Robinson, B.H.2
  • 172
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. the Huntington's Dis Collaborative Res. Group
    • The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group 1993 A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Dis Collaborative Res. Group. Cell 72, 971 983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 173
    • 29644448054 scopus 로고    scopus 로고
    • Targeted disruption of hepatic frataxin expression causes impaired mitochondrial function, decreased life span and tumor growth in mice
    • Thierbach R. Schulz T. J. Isken F. et al. 2005 Targeted disruption of hepatic frataxin expression causes impaired mitochondrial function, decreased life span and tumor growth in mice. Hum. Mol. Genet. 14, 3857 3864.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3857-3864
    • Thierbach, R.1    Schulz, T.J.2    Isken, F.3
  • 175
    • 16944363113 scopus 로고    scopus 로고
    • Haplotype and phylogenetic analyses suggest that one European-specific mtDNA background plays a role in the expression of Leber hereditary optic neuropathy by increasing the penetrance of the primary mutations 11778 and 14484
    • Torroni A. Petrozzi M. D'Urbano L. et al. 1997 Haplotype and phylogenetic analyses suggest that one European-specific mtDNA background plays a role in the expression of Leber hereditary optic neuropathy by increasing the penetrance of the primary mutations 11778 and 14484. Am. J. Hum. Genet. 60, 1107 1121.
    • (1997) Am. J. Hum. Genet. , vol.60 , pp. 1107-1121
    • Torroni, A.1    Petrozzi, M.2    D'Urbano, L.3
  • 176
    • 0027936218 scopus 로고
    • Cytoplasmic transfer of the mtDNA nt 8993 T→G (ATP6) point mutation associated with Leigh syndrome into mtDNA-less cells demonstrates cosegregation with a decrease in state III respiration and ADP/O ratio
    • Trounce I. Neill S. Wallace D. C. 1994 Cytoplasmic transfer of the mtDNA nt 8993 T→G (ATP6) point mutation associated with Leigh syndrome into mtDNA-less cells demonstrates cosegregation with a decrease in state III respiration and ADP/O ratio. Proc. Natl. Acad. Sci. U.S.A. 91, 8334 8338.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 8334-8338
    • Trounce, I.1    Neill, S.2    Wallace, D.C.3
  • 177
    • 0032927387 scopus 로고    scopus 로고
    • Smoking as an aetiological factor in a pedigree with Leber's hereditary optic neuropathy
    • Tsao K. Aitken P. A. Johns D. R. 1999 Smoking as an aetiological factor in a pedigree with Leber's hereditary optic neuropathy. Br. J. Ophthalmol. 83, 577 581.
    • (1999) Br. J. Ophthalmol. , vol.83 , pp. 577-581
    • Tsao, K.1    Aitken, P.A.2    Johns, D.R.3
  • 178
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • Valente E. M. Abou-Sleiman P. M. Caputo V. et al. 2004 Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304, 1158 1160.
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2    Caputo, V.3
  • 180
    • 14944385595 scopus 로고    scopus 로고
    • Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice
    • Vijayvergiya C. Beal M. F. Buck J. Manfredi G. 2005 Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice. J. Neurosci. 25, 2463 2470.
    • (2005) J. Neurosci. , vol.25 , pp. 2463-2470
    • Vijayvergiya, C.1    Beal, M.F.2    Buck, J.3    Manfredi, G.4
  • 182
    • 0037046163 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism
    • Volles M. J. Lansbury P. T. Jr. 2002 Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism. Biochemistry 41, 4595 4602.
    • (2002) Biochemistry , vol.41 , pp. 4595-4602
    • Volles, M.J.1    Lansbury Jr., P.T.2
  • 184
    • 0037385480 scopus 로고    scopus 로고
    • Mitochondrial polymorphisms significantly reduce the risk of Parkinson disease
    • van der Walt J. M. Nicodemus K. K. Martin E. R. et al. 2003 Mitochondrial polymorphisms significantly reduce the risk of Parkinson disease. Am. J. Hum. Genet. 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
  • 185
    • 0141755101 scopus 로고    scopus 로고
    • Altered distribution of mitochondria impairs calcium homeostasis in rat hippocampal neurons in culture
    • Wang G. J. Jackson J. G. Thayer S. A. 2003 Altered distribution of mitochondria impairs calcium homeostasis in rat hippocampal neurons in culture. J. Neurochem. 87, 85 94.
    • (2003) J. Neurochem. , vol.87 , pp. 85-94
    • Wang, G.J.1    Jackson, J.G.2    Thayer, S.A.3
  • 187
    • 0015848173 scopus 로고
    • Superoxide dismutase. Organelle specificity
    • Weisiger R. A. Fridovich I. 1973 Superoxide dismutase. Organelle specificity. J. Biol. Chem. 248, 3582 3592.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3582-3592
    • Weisiger, R.A.1    Fridovich, I.2
  • 189
    • 20344369560 scopus 로고    scopus 로고
    • Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease
    • Whitworth A. J. Theodore D. A. Greene J. C. Benes H. Wes P. D. Pallanck L. J. 2005 Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease. Proc. Natl. Acad. Sci. U.S.A. 102, 8024 8029.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 8024-8029
    • Whitworth, A.J.1    Theodore, D.A.2    Greene, J.C.3    Benes, H.4    Wes, P.D.5    Pallanck, L.J.6
  • 190
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong P. C. Pardo C. A. Borchelt D. R. Lee M. K. Copeland N. G. Jenkins N. A. Sisodia S. S. Cleveland D. W. Price D. L. 1995 An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14, 1105 1116.
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3    Lee, M.K.4    Copeland, N.G.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9
  • 191
    • 0033054177 scopus 로고    scopus 로고
    • The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
    • Wong A. Yang J. Cavadini P. Gellera C. Lonnerdal B. Taroni F. Cortopassi G. 1999 The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum. Mol. Genet. 8, 425 430.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 425-430
    • Wong, A.1    Yang, J.2    Cavadini, P.3    Gellera, C.4    Lonnerdal, B.5    Taroni, F.6    Cortopassi, G.7
  • 192
    • 0013079948 scopus 로고    scopus 로고
    • An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer's disease
    • Yan S. D. Fu J. Soto C. et al. 1997 An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer's disease. Nature 389, 689 695.
    • (1997) Nature , vol.389 , pp. 689-695
    • Yan, S.D.1    Fu, J.2    Soto, C.3
  • 193
    • 26444489693 scopus 로고    scopus 로고
    • Inactivation of Drosophila DJ-1 leads to impairments of oxidative stress response and phosphatidylinositol 3-kinase/Akt signaling
    • Yang Y. Gehrke S. Haque M. E. et al. 2005 Inactivation of Drosophila DJ-1 leads to impairments of oxidative stress response and phosphatidylinositol 3-kinase/Akt signaling. Proc. Natl. Acad. Sci. U.S.A. 102, 13 670 13 675.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 13670-13675
    • Yang, Y.1    Gehrke, S.2    Haque, M.E.3
  • 194
    • 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. 2005 Mitochondrial localization of the Parkinson's disease related protein DJ-1: implications for pathogenesis. Hum. Mol. Genet. 14, 2063 2073.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2063-2073
    • Zhang, L.1    Shimoji, M.2    Thomas, B.3
  • 195
    • 0037007645 scopus 로고    scopus 로고
    • Minocycline inhibits cytochrome c release and delays progression of amyotrophic lateral sclerosis in mice
    • Zhu S. Stavrovskaya I. G. Drozda M. et al. 2002 Minocycline inhibits cytochrome c release and delays progression of amyotrophic lateral sclerosis in mice. Nature 417, 74 78.
    • (2002) Nature , vol.417 , pp. 74-78
    • Zhu, S.1    Stavrovskaya, I.G.2    Drozda, M.3
  • 196
    • 8844233579 scopus 로고    scopus 로고
    • Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
    • Zimprich A. Biskup S. Leitner P. et al. 2004 Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology. Neuron 44, 601 607.
    • (2004) Neuron , vol.44 , pp. 601-607
    • Zimprich, A.1    Biskup, S.2    Leitner, P.3
  • 198
    • 2442589922 scopus 로고    scopus 로고
    • Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
    • Zuchner S. Mersiyanova I. V. Muglia M. et al. 2004 Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A. Nat Genet. 36, 449 451.
    • (2004) Nat Genet. , vol.36 , pp. 449-451
    • Zuchner, S.1    Mersiyanova, I.V.2    Muglia, M.3
  • 199
    • 32044474896 scopus 로고    scopus 로고
    • Axonal neuropathy with optic atrophy is caused by mutations in mitofusin 2
    • Zuchner S. De Jonghe P. Jordanova A. et al. 2006 Axonal neuropathy with optic atrophy is caused by mutations in mitofusin 2. Ann. Neurol. 59, 276 281.
    • (2006) Ann. Neurol. , vol.59 , pp. 276-281
    • Zuchner, S.1    De Jonghe, P.2    Jordanova, A.3


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