메뉴 건너뛰기




Volumn 31, Issue , 2008, Pages 91-123

Mitochondrial disorders in the nervous system

Author keywords

Aging; Apoptosis; Maternal inheritance; Mitochondrial DNA; Oxidative phosphorylation; Oxidative stress

Indexed keywords

MITOCHONDRIAL DNA; MITOCHONDRIAL PROTEIN;

EID: 48249156188     PISSN: 0147006X     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.neuro.30.051606.094302     Document Type: Review
Times cited : (465)

References (176)
  • 1
    • 0028101282 scopus 로고
    • cDNA cloning and characterization of mitochondrial import stimulation factor (MSF) purified from rat liver cytosol
    • Alam R, Hachiya N, Sakaguchi M, Kawabata S, Iwanaga S, et al. 1994. cDNA cloning and characterization of mitochondrial import stimulation factor (MSF) purified from rat liver cytosol. J. Biochem. 116:416-25
    • (1994) J. Biochem , vol.116 , pp. 416-425
    • Alam, R.1    Hachiya, N.2    Sakaguchi, M.3    Kawabata, S.4    Iwanaga, S.5
  • 2
    • 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 UEA, Thiselton DL, Mayer S, et al. 2000. OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28. Nat. Genet. 26:211-15
    • (2000) Nat. Genet , vol.26 , pp. 211-215
    • Alexander, C.1    Votruba, M.2    Pesch, U.E.A.3    Thiselton, D.L.4    Mayer, S.5
  • 3
    • 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. 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
  • 6
    • 0032720496 scopus 로고    scopus 로고
    • Presenilin 1 controls γ-secretase processing of amyloid precursor protein in pre-Golgi compartments of hippocampal neurons
    • Annaert WG, Levesque L, Craessaerts K, Dierinck I, Snellings G, et al. 1999. Presenilin 1 controls γ-secretase processing of amyloid precursor protein in pre-Golgi compartments of hippocampal neurons. J. Cell Biol. 147:277-94
    • (1999) J. Cell Biol , vol.147 , pp. 277-294
    • Annaert, W.G.1    Levesque, L.2    Craessaerts, K.3    Dierinck, I.4    Snellings, G.5
  • 7
    • 0027253399 scopus 로고
    • Early detection of Alzheimer's disease: A statistical approach using positron emission tomographic data
    • Azari NP, Pettigrew KD, Schapiro MB, Haxby JV, Grady CL, et al. 1993. Early detection of Alzheimer's disease: a statistical approach using positron emission tomographic data. J. Cereb. Blood Flow Metab. 13:438-47
    • (1993) J. Cereb. Blood Flow Metab , vol.13 , pp. 438-447
    • Azari, N.P.1    Pettigrew, K.D.2    Schapiro, M.B.3    Haxby, J.V.4    Grady, C.L.5
  • 8
    • 25444474703 scopus 로고    scopus 로고
    • Mitochondria take center stage in aging and neurodegeneration
    • Beal MF. 2005. Mitochondria take center stage in aging and neurodegeneration. Ann. Neurol. 58:495-505
    • (2005) Ann. Neurol , vol.58 , pp. 495-505
    • Beal, M.F.1
  • 9
    • 33646375711 scopus 로고    scopus 로고
    • High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease
    • Bender A, Krishnan KJ, Morris CM, Taylor GA, Reeve AK, et al. 2006. High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease. Nat. Genet. 38:515-17
    • (2006) Nat. Genet , vol.38 , pp. 515-517
    • Bender, A.1    Krishnan, K.J.2    Morris, C.M.3    Taylor, G.A.4    Reeve, A.K.5
  • 10
    • 33745740660 scopus 로고    scopus 로고
    • Molecular neuropathology of MELAS: Level of heteroplasmy in individual neurones and evidence of extensive vascular involvement
    • Betts J, Jaros E, Perry RH, Schaefer AM, Taylor RW, et al. 2006. Molecular neuropathology of MELAS: level of heteroplasmy in individual neurones and evidence of extensive vascular involvement. Neuropath. Appl. Neurobiol. 32:359-73
    • (2006) Neuropath. Appl. Neurobiol , vol.32 , pp. 359-373
    • Betts, J.1    Jaros, E.2    Perry, R.H.3    Schaefer, A.M.4    Taylor, R.W.5
  • 12
    • 0032745071 scopus 로고    scopus 로고
    • Mitochondrial enzyme activity in amyotrophic lateral sclerosis: Implications for the role of mitochondria in neuronal cell death
    • Borthwick GM, Johnson MA, Ince PG, Shaw PJ, Turnbull DM. 1999. Mitochondrial enzyme activity in amyotrophic lateral sclerosis: implications for the role of mitochondria in neuronal cell death. Ann. Neurol. 46:787-90
    • (1999) Ann. Neurol , vol.46 , pp. 787-790
    • Borthwick, G.M.1    Johnson, M.A.2    Ince, P.G.3    Shaw, P.J.4    Turnbull, D.M.5
  • 14
    • 34249811206 scopus 로고    scopus 로고
    • Mutation of RRM2B, encoding p53-controlled ribonucleotide reductase (p53R2), causes severe mitochondrial DNA depletion
    • Bourdon A, Minai L, Serre V, Jais J-P, Sarzi E, et al. 2007. Mutation of RRM2B, encoding p53-controlled ribonucleotide reductase (p53R2), causes severe mitochondrial DNA depletion. Nat. Genet. 39:776-80
    • (2007) Nat. Genet , vol.39 , pp. 776-780
    • Bourdon, A.1    Minai, L.2    Serre, V.3    Jais, J.-P.4    Sarzi, E.5
  • 15
  • 16
    • 2442691791 scopus 로고    scopus 로고
    • Missense mutation in pseudouridine synthase 1 (PUS1) causes mitochondrial myopathy and sideroblastic anemia (MLASA)
    • Bykhovskaya Y, Casas KA, Mengesha E, Inbal A, Fischel-Ghodsian N. 2004. Missense mutation in pseudouridine synthase 1 (PUS1) causes mitochondrial myopathy and sideroblastic anemia (MLASA). Am. J. Hum. Genet. 74:1303-8
    • (2004) Am. J. Hum. Genet , vol.74 , pp. 1303-1308
    • Bykhovskaya, Y.1    Casas, K.A.2    Mengesha, E.3    Inbal, A.4    Fischel-Ghodsian, N.5
  • 17
    • 2942684871 scopus 로고    scopus 로고
    • The Parkinsons disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization
    • Canet-Aviles RM, Wilson MA, Miller DW, Ahmad R, McLendon C, et al. 2004. The Parkinsons disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization. Proc. Natl. Acad. Sci. USA 101:9103-8
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9103-9108
    • Canet-Aviles, R.M.1    Wilson, M.A.2    Miller, D.W.3    Ahmad, R.4    McLendon, C.5
  • 18
    • 33645344999 scopus 로고    scopus 로고
    • Haplogroup effects and recombination of mitochondrial DNA: Novel clues from the analysis of Leber hereditary optic neuropathy pedigrees
    • Carelli V, Achilli A, Valentino ML, Rengo C, Semino O, et al. 2006. Haplogroup effects and recombination of mitochondrial DNA: novel clues from the analysis of Leber hereditary optic neuropathy pedigrees. Am. J. Hum. Genet. 78:564-74
    • (2006) Am. J. Hum. Genet , vol.78 , pp. 564-574
    • Carelli, V.1    Achilli, A.2    Valentino, M.L.3    Rengo, C.4    Semino, O.5
  • 19
    • 34250630964 scopus 로고    scopus 로고
    • Mitochondrial optic neuropathies: How two genomes may kill the same cell type?
    • Carelli V, La Morgia C, Iommarini L, Carroccia R, Mattiazzi M, et al. 2007. Mitochondrial optic neuropathies: how two genomes may kill the same cell type? Biosci. Rep. 27:173-84
    • (2007) Biosci. Rep , vol.27 , pp. 173-184
    • Carelli, V.1    La Morgia, C.2    Iommarini, L.3    Carroccia, R.4    Mattiazzi, M.5
  • 20
    • 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, Zeviani M, Mora M, et al. 1998. Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease. Cell 93:973-83
    • (1998) Cell , vol.93 , pp. 973-983
    • Casari, G.1    De Fusco, M.2    Ciarmatori, S.3    Zeviani, M.4    Mora, M.5
  • 21
    • 0036272650 scopus 로고    scopus 로고
    • β-amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • Casley CS, Canevari L, Land JM, Clark JB, Sharpe MA. 2002. β-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
  • 22
    • 8744219628 scopus 로고    scopus 로고
    • Moving proteins from the cytosol into mitochondria
    • Chacinska A, Rehling P. 2004. Moving proteins from the cytosol into mitochondria. Biochem. Soc. Trans. 32:774-76
    • (2004) Biochem. Soc. Trans , vol.32 , pp. 774-776
    • Chacinska, A.1    Rehling, P.2
  • 23
    • 33745274726 scopus 로고    scopus 로고
    • Mitochondria: Dynamic organelles in disease, aging, and development
    • Chan DC. 2006. Mitochondria: dynamic organelles in disease, aging, and development. Cell 125:1241-52
    • (2006) Cell , vol.125 , pp. 1241-1252
    • Chan, D.C.1
  • 25
    • 0037449905 scopus 로고    scopus 로고
    • Mammalian and yeast 14-3-3 isoforms form distinct patterns of dimers in vivo
    • Chaudhri M, Scarabel M, Aitken A. 2003. Mammalian and yeast 14-3-3 isoforms form distinct patterns of dimers in vivo. Biochem. Biophys. Res. Commun. 300:679-85
    • (2003) Biochem. Biophys. Res. Commun , vol.300 , pp. 679-685
    • Chaudhri, M.1    Scarabel, M.2    Aitken, A.3
  • 26
    • 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, Detloff PJ, Lesort M. 2004. Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release. Hum. Mol. Genet. 13:1407-20
    • (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
  • 27
    • 33747872317 scopus 로고    scopus 로고
    • Early onset severe and late-onset mild Charcot-Marie-Tooth disease with mitofusin 2 (MFN2) mutations
    • Chung KW, Kim SB, Park KD, Choi KG, Lee JH, et al. 2006. Early onset severe and late-onset mild Charcot-Marie-Tooth disease with mitofusin 2 (MFN2) mutations. Brain 129:2103-18
    • (2006) Brain , vol.129 , pp. 2103-2118
    • Chung, K.W.1    Kim, S.B.2    Park, K.D.3    Choi, K.G.4    Lee, J.H.5
  • 29
    • 33745685054 scopus 로고    scopus 로고
    • Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling
    • Cipolat S, Rudka T, Hartmann D, Costa V, Serneels L, et al. 2006. Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling. Cell 126:163-75
    • (2006) Cell , vol.126 , pp. 163-175
    • Cipolat, S.1    Rudka, T.2    Hartmann, D.3    Costa, V.4    Serneels, L.5
  • 30
    • 33746606474 scopus 로고    scopus 로고
    • Mitochondrial mislocalization and altered assembly of cluster of Barth syndrome mutant tafazzins
    • Claypool SM, McCaffrey JM, Koehler CM. 2006. Mitochondrial mislocalization and altered assembly of cluster of Barth syndrome mutant tafazzins. J. Cell Biol. 174:379-90
    • (2006) J. Cell Biol , vol.174 , pp. 379-390
    • Claypool, S.M.1    McCaffrey, J.M.2    Koehler, C.M.3
  • 31
    • 8344259033 scopus 로고    scopus 로고
    • Mutant mitochondrial elongation factor G1 and combined oxidative phosphorylation deficiency
    • Coenen MJH, Antonicka H, Ugalde C, Sasarman F, Rossi P, et al. 2004. Mutant mitochondrial elongation factor G1 and combined oxidative phosphorylation deficiency. New Engl. J. Med. 351:2080-86
    • (2004) New Engl. J. Med , vol.351 , pp. 2080-2086
    • Coenen, M.J.H.1    Antonicka, H.2    Ugalde, C.3    Sasarman, F.4    Rossi, P.5
  • 32
    • 0031915174 scopus 로고    scopus 로고
    • Cytochrome c oxidase subunit I microdeletion in a patient with motor neuron disease
    • Comi GP, Bordoni A, Salani S, Franceschina L, Sciacco M, et al. 1998. Cytochrome c oxidase subunit I microdeletion in a patient with motor neuron disease. Ann. Neurol. 43:110-16
    • (1998) Ann. Neurol , vol.43 , pp. 110-116
    • Comi, G.P.1    Bordoni, A.2    Salani, S.3    Franceschina, L.4    Sciacco, M.5
  • 33
    • 0027194791 scopus 로고
    • Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families
    • Corder EH, Saunders AM, Strittmatter WJ, Schmechel DE, Gaskell PC, et al. 1993. Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families. Science 261:921-23
    • (1993) Science , vol.261 , pp. 921-923
    • Corder, E.H.1    Saunders, A.M.2    Strittmatter, W.J.3    Schmechel, D.E.4    Gaskell, P.C.5
  • 34
    • 0037338634 scopus 로고    scopus 로고
    • Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
    • Darios F, Corti O, Lucking CB, Hampe C, Muriel M-P, et al. 2003. Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death. Hum. Mol. Genet. 12:517-26
    • (2003) Hum. Mol. Genet , vol.12 , pp. 517-526
    • Darios, F.1    Corti, O.2    Lucking, C.B.3    Hampe, C.4    Muriel, M.-P.5
  • 36
    • 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, Gigarel N, Lorenzo C, et al. 2000. Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy. Nat. Genet. 26:207-10
    • (2000) Nat. Genet , vol.26 , pp. 207-210
    • Delettre, C.1    Lenaers, G.2    Griffoin, J.-M.3    Gigarel, N.4    Lorenzo, C.5
  • 37
    • 1242269834 scopus 로고    scopus 로고
    • Respiratory chain complex V deficiency due to a mutation in the assembly gene ATP12
    • De Meirleir L, Seneca S, Lissens W, De Clercq I, Eyskens F, et al. 2004. Respiratory chain complex V deficiency due to a mutation in the assembly gene ATP12. J. Med. Genet. 41:120-24
    • (2004) J. Med. Genet , vol.41 , pp. 120-124
    • De Meirleir, L.1    Seneca, S.2    Lissens, W.3    De Clercq, I.4    Eyskens, F.5
  • 38
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and nicastrin with presenilin generate an active γ-secretase complex
    • De Strooper B. 2003. Aph-1, Pen-2, and nicastrin with presenilin generate an active γ-secretase complex. Neuron 38:9-12
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 39
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction
    • Devi L, Prabhu BM, Galati DF, Avadhani NG, Anandatheerthavarada HK. 2006. Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction. J. Neurosci. 26:9057-68
    • (2006) J. Neurosci , vol.26 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 40
    • 20344366079 scopus 로고    scopus 로고
    • Mitochondrial DNA and disease
    • DiMauro S, Davidzon G. 2005. Mitochondrial DNA and disease. Ann. Med. 37:222-32
    • (2005) Ann. Med , vol.37 , pp. 222-232
    • DiMauro, S.1    Davidzon, G.2
  • 41
    • 33745727824 scopus 로고    scopus 로고
    • A polymorphic polymerase
    • DiMauro S, Davidzon G, Hirano M. 2006a. A polymorphic polymerase. Brain 126:1637-39
    • (2006) Brain , vol.126 , pp. 1637-1639
    • DiMauro, S.1    Davidzon, G.2    Hirano, M.3
  • 42
    • 15944396616 scopus 로고    scopus 로고
    • Mitochondrial encephalomyopathies: An update
    • DiMauro S, Hirano M. 2005. Mitochondrial encephalomyopathies: an update. Neuromusc. Disord. 15:276-86
    • (2005) Neuromusc. Disord , vol.15 , pp. 276-286
    • DiMauro, S.1    Hirano, M.2
  • 43
    • 33748090036 scopus 로고    scopus 로고
    • Mitochondrial psychiatry
    • ed. S DiMauro, M Hirano, EA Schon, pp, London: Informa Healthcare
    • DiMauro S, Hirano M, Kaufmann P, Mann JJ. 2006b. Mitochondrial psychiatry. In Mitochondrial Medicine, ed. S DiMauro, M Hirano, EA Schon, pp. 261-77. London: Informa Healthcare
    • (2006) Mitochondrial Medicine , pp. 261-277
    • DiMauro, S.1    Hirano, M.2    Kaufmann, P.3    Mann, J.J.4
  • 44
    • 33748089976 scopus 로고    scopus 로고
    • Approaches to the treatment of mitochondrial diseases
    • DiMauro S, Hirano M, Schon EA. 2006c. Approaches to the treatment of mitochondrial diseases. Muscle Nerve 34:265-83
    • (2006) Muscle Nerve , vol.34 , pp. 265-283
    • DiMauro, S.1    Hirano, M.2    Schon, E.A.3
  • 45
    • 33847404036 scopus 로고    scopus 로고
    • Mutations in coenzyme Q10 biosynthetic genes
    • DiMauro S, Quinzii C, Hirano M. 2007. Mutations in coenzyme Q10 biosynthetic genes. J. Clin. Invest. 117:587-89
    • (2007) J. Clin. Invest , vol.117 , pp. 587-589
    • DiMauro, S.1    Quinzii, C.2    Hirano, M.3
  • 46
    • 0037972522 scopus 로고    scopus 로고
    • Mitochondrial respiratory-chain diseases
    • DiMauro S, Schon EA. 2003. Mitochondrial respiratory-chain diseases. New Engl. J. Med. 348:2656-68
    • (2003) New Engl. J. Med , vol.348 , pp. 2656-2668
    • DiMauro, S.1    Schon, E.A.2
  • 47
    • 18944390365 scopus 로고    scopus 로고
    • Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomy-opathy and mitochondrial DNA depletion
    • Elpeleg O, Miller C, Hershkovitz E, Bitner-Glindzicz M, Bondi-Rubinstein G, et al. 2005. Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomy-opathy and mitochondrial DNA depletion. Am. J. Hum. Genet. 76:1081-86
    • (2005) Am. J. Hum. Genet , vol.76 , pp. 1081-1086
    • Elpeleg, O.1    Miller, C.2    Hershkovitz, E.3    Bitner-Glindzicz, M.4    Bondi-Rubinstein, G.5
  • 48
    • 0030726894 scopus 로고    scopus 로고
    • Huntingtin-associated protein 1 (HAP1) interacts with the p150Glued subunit of dynactin
    • Engelender S, Sharp AH, Colomer V, Tokito MK, Lanahan A, et al. 1997. Huntingtin-associated protein 1 (HAP1) interacts with the p150Glued subunit of dynactin. Hum. Mol. Genet. 6:2205-12
    • (1997) Hum. Mol. Genet , vol.6 , pp. 2205-2212
    • Engelender, S.1    Sharp, A.H.2    Colomer, V.3    Tokito, M.K.4    Lanahan, A.5
  • 49
    • 0029075554 scopus 로고
    • Mitochondrial protein transport: A system in search of mutations
    • Fenton WA. 1995. Mitochondrial protein transport: a system in search of mutations. Am. J. Hum. Genet. 57:235-38
    • (1995) Am. J. Hum. Genet , vol.57 , pp. 235-238
    • Fenton, W.A.1
  • 50
    • 34147144142 scopus 로고    scopus 로고
    • Nonsense mutation in pseudouridylate synthase 1 (PUS1) in two brothers affected by myopathy, lactic acidosis and sideroblastic anemia (MLASA)
    • Fernandez-Vizarra E, Berardinelli A, Valente L, Tiranti V, Zeviani M. 2006. Nonsense mutation in pseudouridylate synthase 1 (PUS1) in two brothers affected by myopathy, lactic acidosis and sideroblastic anemia (MLASA). J. Med. Genet. 44:173-80
    • (2006) J. Med. Genet , vol.44 , pp. 173-180
    • Fernandez-Vizarra, E.1    Berardinelli, A.2    Valente, L.3    Tiranti, V.4    Zeviani, M.5
  • 51
    • 4644258352 scopus 로고    scopus 로고
    • Evidence of kinesin heavy chain (KIF5A) involvement in pure hereditary spastic paraplegia
    • Fichera M, Lo Giudice M, Falco M, Sturnio M, Amata A, et al. 2004. Evidence of kinesin heavy chain (KIF5A) involvement in pure hereditary spastic paraplegia. Neurology 63:1108-10
    • (2004) Neurology , vol.63 , pp. 1108-1110
    • Fichera, M.1    Lo Giudice, M.2    Falco, M.3    Sturnio, M.4    Amata, A.5
  • 52
    • 33845630817 scopus 로고    scopus 로고
    • Novel mitochondrial intermembrane space proteins as substrates of the MIA import pathway
    • Gabriel K, Milenkovic D, Chacinska A, Muller J, Guiard B, et al. 2006. Novel mitochondrial intermembrane space proteins as substrates of the MIA import pathway. J. Mol. Biol. 365:612-20
    • (2006) J. Mol. Biol , vol.365 , pp. 612-620
    • Gabriel, K.1    Milenkovic, D.2    Chacinska, A.3    Muller, J.4    Guiard, B.5
  • 53
    • 34248171499 scopus 로고    scopus 로고
    • The myopathic form of coenzyme Q10 deficiency is caused by mutations in the electron-transferring-flavoprotein dehydrogenase (ETFDH) gene
    • Gempel K, Topaloglu H, Talim B, Schneiderat P, Schoser BGH, et al. 2007. The myopathic form of coenzyme Q10 deficiency is caused by mutations in the electron-transferring-flavoprotein dehydrogenase (ETFDH) gene. Brain 130:2037-44
    • (2007) Brain , vol.130 , pp. 2037-2044
    • Gempel, K.1    Topaloglu, H.2    Talim, B.3    Schneiderat, P.4    Schoser, B.G.H.5
  • 54
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimer's disease
    • Goedert M, Spillantini MG. 2006. A century of Alzheimer's disease. Science 314:777-81
    • (2006) Science , vol.314 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 55
  • 56
    • 33846654677 scopus 로고    scopus 로고
    • Huntington's Disease - making connections
    • Greenamyre JT. 2007. Huntington's Disease - making connections. New Engl. J. Med. 356:518-20
    • (2007) New Engl. J. Med , vol.356 , pp. 518-520
    • Greenamyre, J.T.1
  • 57
    • 0032190391 scopus 로고    scopus 로고
    • The cellular and subcellular localization of huntingtin-associated protein 1 (HAP1): Comparison with huntingtin in rat and human
    • Gutekunst CA, Li SH, Yi H, Ferrante RJ, Li XJ, Hersch SM. 1998. The cellular and subcellular localization of huntingtin-associated protein 1 (HAP1): comparison with huntingtin in rat and human. J. Neurosci. 18:7674-86
    • (1998) J. Neurosci , vol.18 , pp. 7674-7686
    • Gutekunst, C.A.1    Li, S.H.2    Yi, H.3    Ferrante, R.J.4    Li, X.J.5    Hersch, S.M.6
  • 58
    • 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, Georgopoulos C, Ang D, et al. 2002. Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. Am. J. Hum. Genet. 70:1328-32
    • (2002) Am. J. Hum. Genet , vol.70 , pp. 1328-1332
    • Hansen, J.J.1    Durr, A.2    Cournu-Rebeix, I.3    Georgopoulos, C.4    Ang, D.5
  • 59
    • 19944373389 scopus 로고    scopus 로고
    • Nicastrin, presenilin, APH-1, and PEN-2 form active γ-secretase complexes in mitochondria
    • Hansson CA, Frykman S, Farmery MR, Tjernberg LO, Nilsberth C, et al. 2004. Nicastrin, presenilin, APH-1, and PEN-2 form active γ-secretase complexes in mitochondria. J. Biol. Chem. 279:51654-60
    • (2004) J. Biol. Chem , vol.279 , pp. 51654-51660
    • Hansson, C.A.1    Frykman, S.2    Farmery, M.R.3    Tjernberg, L.O.4    Nilsberth, C.5
  • 60
    • 0027016008 scopus 로고
    • Growing old: The most common mitochondrial disease of all?
    • Harding AE. 1992. Growing old: the most common mitochondrial disease of all? Nat. Genet. 2:251-52
    • (1992) Nat. Genet , vol.2 , pp. 251-252
    • Harding, A.E.1
  • 62
    • 0015319592 scopus 로고
    • The biologic clock: The mitochondria?
    • Harman D. 1972. The biologic clock: the mitochondria? J. Am. Geriat. Soc. 20:145-47
    • (1972) J. Am. Geriat. Soc , vol.20 , pp. 145-147
    • Harman, D.1
  • 63
    • 0037897337 scopus 로고    scopus 로고
    • A deletion in the human QP-C gene causes a complex III deficiency resulting in hypoglycaemia and lactic acidosis
    • Haut S, Brivet M, Touati G, Rustin P, Lebon S, et al. 2003. A deletion in the human QP-C gene causes a complex III deficiency resulting in hypoglycaemia and lactic acidosis. Hum. Genet. 113:118-22
    • (2003) Hum. Genet , vol.113 , pp. 118-122
    • Haut, S.1    Brivet, M.2    Touati, G.3    Rustin, P.4    Lebon, S.5
  • 64
    • 33748091467 scopus 로고    scopus 로고
    • Mitochondrial neurology II: Myopathies and peripheral neuropathies
    • ed. S DiMauro, M Hirano, EA Schon, pp, London: Informa Healthcare
    • Hays AP, Oskoui M, Tanji K, Kaufmann P, Bonilla E. 2006. Mitochondrial neurology II: myopathies and peripheral neuropathies. In Mitochondrial Medicine, ed. S DiMauro, M Hirano, EA Schon, pp. 45-74. London: Informa Healthcare
    • (2006) Mitochondrial Medicine , pp. 45-74
    • Hays, A.P.1    Oskoui, M.2    Tanji, K.3    Kaufmann, P.4    Bonilla, E.5
  • 65
    • 33748054049 scopus 로고    scopus 로고
    • Mitochondrial neurology I: Encephalopathies
    • ed. S DiMauro, M Hirano, EA Schon, pp, London: Informa Healthcare
    • Hirano M, Kaufmann P, De Vivo DC, Tanji K. 2006a. Mitochondrial neurology I: Encephalopathies. In Mitochondrial Medicine, ed. S DiMauro, M Hirano, EA Schon, pp. 27-44. London: Informa Healthcare
    • (2006) Mitochondrial Medicine , pp. 27-44
    • Hirano, M.1    Kaufmann, P.2    De Vivo, D.C.3    Tanji, K.4
  • 66
    • 23644432014 scopus 로고    scopus 로고
    • Thymidine phosphorylase mutations cause instability of mitochondrial DNA
    • Hirano M, Lagier-Tourenne C, Valentino ML, Marti R, Nishigaki Y. 2005. Thymidine phosphorylase mutations cause instability of mitochondrial DNA. Gene 354:152-56
    • (2005) Gene , vol.354 , pp. 152-156
    • Hirano, M.1    Lagier-Tourenne, C.2    Valentino, M.L.3    Marti, R.4    Nishigaki, Y.5
  • 67
    • 33750306390 scopus 로고    scopus 로고
    • Allogeneic stem cell transplantation corrects biochemical derangements in MNGIE
    • Hirano M, Marti R, Casali C, Tadesse BS, Uldrick T, et al. 2006b. Allogeneic stem cell transplantation corrects biochemical derangements in MNGIE. Neurology 67:1458-60
    • (2006) Neurology , vol.67 , pp. 1458-1460
    • Hirano, M.1    Marti, R.2    Casali, C.3    Tadesse, B.S.4    Uldrick, T.5
  • 68
    • 0023883150 scopus 로고
    • Deletions of muscle mitochondrial DNA in patients with mitochondrial myopathies
    • Holt IJ, Harding AE, Morgan Hughes JA. 1988. Deletions of muscle mitochondrial DNA in patients with mitochondrial myopathies. Nature 331:717-19
    • (1988) Nature , vol.331 , pp. 717-719
    • Holt, I.J.1    Harding, A.E.2    Morgan Hughes, J.A.3
  • 69
    • 0034212576 scopus 로고    scopus 로고
    • Familial Alzheimer's disease-associated mutations block translocation of full-length presenilin 1 to the nuclear envelope
    • Honda T, Nihonmatsu N, Yasutake K, Ohtake A, Sato K, et al. 2000. Familial Alzheimer's disease-associated mutations block translocation of full-length presenilin 1 to the nuclear envelope. Neurosci. Res. 37:101-11
    • (2000) Neurosci. Res , vol.37 , pp. 101-111
    • Honda, T.1    Nihonmatsu, N.2    Yasutake, K.3    Ohtake, A.4    Sato, K.5
  • 70
    • 28144454984 scopus 로고    scopus 로고
    • Identification of an X-chromosomal locus and haplotype modulating the phenotype of a mitochondrial DNA disorder
    • Hudson G, Keers S, Yu Wai Man P, Griffiths P, Huoponen K, et al. 2005. Identification of an X-chromosomal locus and haplotype modulating the phenotype of a mitochondrial DNA disorder. Am. J. Hum. Genet. 77:1086-91
    • (2005) Am. J. Hum. Genet , vol.77 , pp. 1086-1091
    • Hudson, G.1    Keers, S.2    Yu3    Wai Man, P.4    Griffiths, P.5    Huoponen, K.6
  • 71
    • 33845665844 scopus 로고    scopus 로고
    • Fasciculation and elongation protein zeta-1 (FEZ1) participates in the polarization of hippocampal neuron by controlling the mitochondrial motility
    • Ikuta J, Maturana A, Fujita T, Okajima T, Tatematsu K, et al. 2007. Fasciculation and elongation protein zeta-1 (FEZ1) participates in the polarization of hippocampal neuron by controlling the mitochondrial motility. Biochem. Biophys. Res. Commun. 353:127-32
    • (2007) Biochem. Biophys. Res. Commun , vol.353 , pp. 127-132
    • Ikuta, J.1    Maturana, A.2    Fujita, T.3    Okajima, T.4    Tatematsu, K.5
  • 72
    • 2342539835 scopus 로고    scopus 로고
    • Disrupted in schizophrenia 1 (DISC1) is a multicompartmentalized protein that predominantly localizes to mitochondria
    • James R, Adams RR, Christie S, Buchanan SR, Porteous DJ, Millar JK. 2004. Disrupted in schizophrenia 1 (DISC1) is a multicompartmentalized protein that predominantly localizes to mitochondria. Mol. Cell. Neurosci. 26:112-22
    • (2004) Mol. Cell. Neurosci , vol.26 , pp. 112-122
    • James, R.1    Adams, R.R.2    Christie, S.3    Buchanan, S.R.4    Porteous, D.J.5    Millar, J.K.6
  • 73
    • 25844454917 scopus 로고    scopus 로고
    • Quantitative analysis of mitochondrial DNA deletions in the brains of patients with bipolar disorder and schizophrenia
    • Kakiuchi C, Ishiwata M, Kametani M, Nelson C, Iwamoto K, Kato T. 2005. Quantitative analysis of mitochondrial DNA deletions in the brains of patients with bipolar disorder and schizophrenia. Int. J. Neuropharmacol. 8:1-8
    • (2005) Int. J. Neuropharmacol , vol.8 , pp. 1-8
    • Kakiuchi, C.1    Ishiwata, M.2    Kametani, M.3    Nelson, C.4    Iwamoto, K.5    Kato, T.6
  • 74
    • 0141730405 scopus 로고    scopus 로고
    • Impaired feedback regulation of XBP1 as a genetic risk factor for bipolar disorder
    • Kakiuchi C, Iwamoto K, Ishiwata M, Bundo M, Kasahara T, et al. 2003. Impaired feedback regulation of XBP1 as a genetic risk factor for bipolar disorder. Nat. Genet. 35:171-75
    • (2003) Nat. Genet , vol.35 , pp. 171-175
    • Kakiuchi, C.1    Iwamoto, K.2    Ishiwata, M.3    Bundo, M.4    Kasahara, T.5
  • 76
    • 0742288280 scopus 로고    scopus 로고
    • Mechanisms of altered calcium signalling in transformed lymphoblastoid cells from patients with bipolar disorder
    • Kato T, Ishiwata M, Mori K, Washizuka S, Tajima O, et al. 2002. Mechanisms of altered calcium signalling in transformed lymphoblastoid cells from patients with bipolar disorder. Int. J. Neuropharmacol. 6:379-89
    • (2002) Int. J. Neuropharmacol , vol.6 , pp. 379-389
    • Kato, T.1    Ishiwata, M.2    Mori, K.3    Washizuka, S.4    Tajima, O.5
  • 77
    • 0346166189 scopus 로고    scopus 로고
    • Psychiatric symptoms are common features of clinical syndromes associated with mitochondrial DNA point mutations
    • Abstract
    • Kaufmann P, Sano MC, Jhung S, Engelstadt K, De Vivo DC. 2002. Psychiatric symptoms are common features of clinical syndromes associated with mitochondrial DNA point mutations. Neurology 58:A315 (Abstract)
    • (2002) Neurology , vol.58
    • Kaufmann, P.1    Sano, M.C.2    Jhung, S.3    Engelstadt, K.4    De Vivo, D.C.5
  • 78
    • 11144355448 scopus 로고    scopus 로고
    • Cerebral lactic acidosis correlates with neurological impairment in MELAS
    • Kaufmann P, Shungu D, Sano MC, Jhung S, Engelstad K, et al. 2004. Cerebral lactic acidosis correlates with neurological impairment in MELAS. Neurology 62:1297-302
    • (2004) Neurology , vol.62 , pp. 1297-1302
    • Kaufmann, P.1    Shungu, D.2    Sano, M.C.3    Jhung, S.4    Engelstad, K.5
  • 79
    • 33744458966 scopus 로고    scopus 로고
    • Does premature aging of the mtDNA mutator mouse prove that mtDNA mutations are involved in natural aging?
    • Khrapko K, Kraytsberg Y, de Grey ADNJ, Vijg J, Schon EA. 2006. Does premature aging of the mtDNA mutator mouse prove that mtDNA mutations are involved in natural aging? Aging Cell 5:279-82
    • (2006) Aging Cell , vol.5 , pp. 279-282
    • Khrapko, K.1    Kraytsberg, Y.2    de Grey, A.D.N.J.3    Vijg, J.4    Schon, E.A.5
  • 80
    • 33750151421 scopus 로고    scopus 로고
    • Subcellular trafficking of the amyloid precursor protein gene family and its pathogenic role in Alzheimer's disease
    • Kins S, Lauther N, Szodorai A, Beyreuther K. 2006. Subcellular trafficking of the amyloid precursor protein gene family and its pathogenic role in Alzheimer's disease. Neurodegen. Dis. 3:218-26
    • (2006) Neurodegen. Dis , vol.3 , pp. 218-226
    • Kins, S.1    Lauther, N.2    Szodorai, A.3    Beyreuther, K.4
  • 81
    • 0141535366 scopus 로고    scopus 로고
    • Low mutant load of mitochondrial DNA G13513A mutation can cause Leigh's disease
    • Kirby DM, Boneh A, Chow CW, Ohtake A, Ryan MT, et al. 2003. Low mutant load of mitochondrial DNA G13513A mutation can cause Leigh's disease. Ann. Neurol. 54:473-78
    • (2003) Ann. Neurol , vol.54 , pp. 473-478
    • Kirby, D.M.1    Boneh, A.2    Chow, C.W.3    Ohtake, A.4    Ryan, M.T.5
  • 82
    • 0033358084 scopus 로고    scopus 로고
    • Mitochondrial genetic analyses suggest selection against maternal lineages in bipolar affective disorder
    • Kirk R, Furlong RA, Amos W, Cooper G, Rubinsztein JS, et al. 1999. Mitochondrial genetic analyses suggest selection against maternal lineages in bipolar affective disorder. Am. J. Hum. Genet. 65:508-18
    • (1999) Am. J. Hum. Genet , vol.65 , pp. 508-518
    • Kirk, R.1    Furlong, R.A.2    Amos, W.3    Cooper, G.4    Rubinsztein, J.S.5
  • 85
    • 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 AC, Geula C, Kowall NW, Khrapko K. 2006. Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons. Nat. Genet. 38:518-20
    • (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
  • 86
    • 22344456832 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging
    • Kujoth GC, Hiona A, Pugh TD, Someya S, Panzer K, et al. 2005. Mitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging. Science 309:481-84
    • (2005) Science , vol.309 , pp. 481-484
    • Kujoth, G.C.1    Hiona, A.2    Pugh, T.D.3    Someya, S.4    Panzer, K.5
  • 87
    • 22544465572 scopus 로고    scopus 로고
    • Clinical and electrophysiologic features of CMT2A with mutations in the mitofusin 2 gene
    • Lawson VH, Graham BV, Flanigan KM. 2005. Clinical and electrophysiologic features of CMT2A with mutations in the mitofusin 2 gene. Neurology 65:197-204
    • (2005) Neurology , vol.65 , pp. 197-204
    • Lawson, V.H.1    Graham, B.V.2    Flanigan, K.M.3
  • 88
    • 0025211899 scopus 로고
    • Mutation eliminating mitochondrial leader sequence of methylmalonyl-CoA mutase causes mut° methylmalonic acidemia
    • Ledley FD, Jansen R, Nham SU, Fenton WA, Rosenberg LE. 1990. Mutation eliminating mitochondrial leader sequence of methylmalonyl-CoA mutase causes mut° methylmalonic acidemia. Proc. Natl. Acad. Sci. USA 87:3147-50
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3147-3150
    • Ledley, F.D.1    Jansen, R.2    Nham, S.U.3    Fenton, W.A.4    Rosenberg, L.E.5
  • 89
    • 22144491144 scopus 로고    scopus 로고
    • NudEL targets dynein to microtubule ends through LIS1
    • Li J, Lee WL, Cooper JA. 2005. NudEL targets dynein to microtubule ends through LIS1. Nat. Cell Biol. 7:686-90
    • (2005) Nat. Cell Biol , vol.7 , pp. 686-690
    • Li, J.1    Lee, W.L.2    Cooper, J.A.3
  • 90
    • 0032519646 scopus 로고    scopus 로고
    • Interaction of huntingtin-associated protein with dynactin P150Glued
    • Li SH, Gutekunst CA, Hersch SM, Li XJ. 1998. Interaction of huntingtin-associated protein with dynactin P150Glued. J. Neurosci. 18:1261-69
    • (1998) J. Neurosci , vol.18 , pp. 1261-1269
    • Li, S.H.1    Gutekunst, C.A.2    Hersch, S.M.3    Li, X.J.4
  • 91
    • 3242701496 scopus 로고    scopus 로고
    • Toxicity of familial ALS-linked SOD1 mutants from selective recruitment to spinal mitochondria
    • Liu JK, Lillo C, Jonsson PA, Velde CV, Ward CM, 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.K.1    Lillo, C.2    Jonsson, P.A.3    Velde, C.V.4    Ward, C.M.5
  • 92
    • 33646859687 scopus 로고    scopus 로고
    • Mutant POLG2 disrupts DNA polymerase gamma subunits and causes progressive external ophthalmoplegia
    • Longley MJ, Clark S, Man CYW, Hudson G, Durham SE, et al. 2006. Mutant POLG2 disrupts DNA polymerase gamma subunits and causes progressive external ophthalmoplegia. Am. J. Hum. Genet. 78:1026-34
    • (2006) Am. J. Hum. Genet , vol.78 , pp. 1026-1034
    • Longley, M.J.1    Clark, S.2    Man, C.Y.W.3    Hudson, G.4    Durham, S.E.5
  • 93
    • 33845232634 scopus 로고    scopus 로고
    • Leigh syndrome with nephropathy and CoQ10 deficiency due to decaprenyl diphosphate synthase subunit 2 (PDSS2) mutations
    • López LC, Quinzii C, Schuelke M, Kanki T, Naini A, et al. 2006. Leigh syndrome with nephropathy and CoQ10 deficiency due to decaprenyl diphosphate synthase subunit 2 (PDSS2) mutations. Am. J. Hum. Genet. 79:1125-29
    • (2006) Am. J. Hum. Genet , vol.79 , pp. 1125-1129
    • López, L.C.1    Quinzii, C.2    Schuelke, M.3    Kanki, T.4    Naini, A.5
  • 94
    • 33748043331 scopus 로고    scopus 로고
    • The hereditary spastic paraplegia protein spartin localises to mitochondria
    • Lu J, Rashid F, Byrne PC. 2006. The hereditary spastic paraplegia protein spartin localises to mitochondria. J. Neurochem. 98:1908-19
    • (2006) J. Neurochem , vol.98 , pp. 1908-1919
    • Lu, J.1    Rashid, F.2    Byrne, P.C.3
  • 95
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Aβ to mitochondrial toxicity in Alzheimer's disease
    • Lustbader JW, Cirilli M, Lin C, Xu HW, Takuma K, et al. 2004. ABAD directly links Aβ to mitochondrial toxicity in Alzheimer's disease. Science 304:448-52
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3    Xu, H.W.4    Takuma, K.5
  • 96
    • 33750058844 scopus 로고    scopus 로고
    • Differential expression of disrupted-in-schizophrenia (DISC1) in bipolar disorder
    • Maeda K, Nwulia E, Chang J, Balkissoon R, Ishizuka K, et al. 2006. Differential expression of disrupted-in-schizophrenia (DISC1) in bipolar disorder. Biol. Psych. 60:929-35
    • (2006) Biol. Psych , vol.60 , pp. 929-935
    • Maeda, K.1    Nwulia, E.2    Chang, J.3    Balkissoon, R.4    Ishizuka, K.5
  • 97
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • Manczak M, Anekonda TS, Henson E, Park BS, Quinn J, Reddy PH. 2006. Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum. Mol. Genet. 15:1437-49
    • (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
  • 98
    • 18344380083 scopus 로고    scopus 로고
    • A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions
    • Marambaud P, Shioi J, Serban G, Georgakopoulos A, Sarner S, et al. 2002. A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. EMBO J. 21:1948-56
    • (2002) EMBO J , vol.21 , pp. 1948-1956
    • Marambaud, P.1    Shioi, J.2    Serban, G.3    Georgakopoulos, A.4    Sarner, S.5
  • 99
    • 0027332651 scopus 로고
    • Brain α-ketoglutarate dehydrogenase complex activity in Alzheimer's disease
    • Mastrogiacomo F, Bergeron C, Kish SJ. 1993. Brain α-ketoglutarate dehydrogenase complex activity in Alzheimer's disease. J. Neurochem. 61:2007-14
    • (1993) J. Neurochem , vol.61 , pp. 2007-2014
    • Mastrogiacomo, F.1    Bergeron, C.2    Kish, S.J.3
  • 100
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson MP. 2004. Pathways towards and away from Alzheimer's disease. Nature 430:631-39
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 101
    • 0344664376 scopus 로고    scopus 로고
    • Hereditary spastic paraparesis: Disrupted intracellular transport associated with spastin mutation
    • McDermott CJ, Grierson AJ, Wood JD, Bingley M, Wharton SB, et al. 2003. Hereditary spastic paraparesis: disrupted intracellular transport associated with spastin mutation. Ann. Neurol. 54:748-59
    • (2003) Ann. Neurol , vol.54 , pp. 748-759
    • McDermott, C.J.1    Grierson, A.J.2    Wood, J.D.3    Bingley, M.4    Wharton, S.B.5
  • 102
    • 28344457312 scopus 로고    scopus 로고
    • Disrupted in schizophrenia 1 (DISC1): Subcellular targeting and induction of ring mitochondria
    • Millar JK, James R, Christie S, Porteous DJ. 2005. Disrupted in schizophrenia 1 (DISC1): subcellular targeting and induction of ring mitochondria. Mol. Cell. Neurosci. 30:477-84
    • (2005) Mol. Cell. Neurosci , vol.30 , pp. 477-484
    • Millar, J.K.1    James, R.2    Christie, S.3    Porteous, D.J.4
  • 103
    • 9144268494 scopus 로고    scopus 로고
    • Defective mitochondrial translation caused by a ribosomal protein (MRPS16) mutation
    • Miller C, Saada A, Shaul N, Shabtai N, Ben-Shalom E, et al. 2004. Defective mitochondrial translation caused by a ribosomal protein (MRPS16) mutation. Ann. Neurol. 56:734-38
    • (2004) Ann. Neurol , vol.56 , pp. 734-738
    • Miller, C.1    Saada, A.2    Shaul, N.3    Shabtai, N.4    Ben-Shalom, E.5
  • 104
    • 33847347629 scopus 로고    scopus 로고
    • Prenyldiphosphate synthase (PDSS1) and OH-benzoate prenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders
    • Mollet J, Giurgea I, Schlemmer D, Dallner G, Chretien D, et al. 2007. Prenyldiphosphate synthase (PDSS1) and OH-benzoate prenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders. J. Clin. Invest. 117:765-72
    • (2007) J. Clin. Invest , vol.117 , pp. 765-772
    • Mollet, J.1    Giurgea, I.2    Schlemmer, D.3    Dallner, G.4    Chretien, D.5
  • 105
    • 0037458031 scopus 로고    scopus 로고
    • Identification of a gene causing human cytochrome c oxidase deficiency by integrative genomics
    • Mootha VK, Lepage P, Miller K, Bunkenborg J, Reich M, et al. 2003. Identification of a gene causing human cytochrome c oxidase deficiency by integrative genomics. Proc. Natl. Acad. Sci. USA 100:605-10
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 605-610
    • Mootha, V.K.1    Lepage, P.2    Miller, K.3    Bunkenborg, J.4    Reich, M.5
  • 106
    • 0027379869 scopus 로고
    • Clinical, metabolic, and genetic aspects of cytochrome c oxidase deficiency in Saguenay-Lac-Saint-Jean
    • Morin C, Mitchell G, Larochelle J, Lambert M, Ogier H, et al. 1993. Clinical, metabolic, and genetic aspects of cytochrome c oxidase deficiency in Saguenay-Lac-Saint-Jean. Am. J. Hum. Genet. 53:488-96
    • (1993) Am. J. Hum. Genet , vol.53 , pp. 488-496
    • Morin, C.1    Mitchell, G.2    Larochelle, J.3    Lambert, M.4    Ogier, H.5
  • 107
    • 4544326057 scopus 로고    scopus 로고
    • Mitochondrial complex I and IV activities in leukocytes from patients with parkin mutations
    • Muftuoglu M, Elibol B, Dalmizrak O, Ercan A, Kulaksiz G, et al. 2003. Mitochondrial complex I and IV activities in leukocytes from patients with parkin mutations. Mov. Disord. 19:544-48
    • (2003) Mov. Disord , vol.19 , pp. 544-548
    • Muftuoglu, M.1    Elibol, B.2    Dalmizrak, O.3    Ercan, A.4    Kulaksiz, G.5
  • 108
    • 2142705756 scopus 로고    scopus 로고
    • POLG mutations associated with Alpers' syndrome and mitochondrial DNA depletion
    • Naviaux RK, Nguyen KV. 2004. POLG mutations associated with Alpers' syndrome and mitochondrial DNA depletion. Ann. Neurol. 55:706-12
    • (2004) Ann. Neurol , vol.55 , pp. 706-712
    • Naviaux, R.K.1    Nguyen, K.V.2
  • 109
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machinery of death
    • Newmeyer DD, Ferguson-Miller S. 2003. Mitochondria: releasing power for life and unleashing the machinery of death. Cell 112:481-90
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 110
    • 25444514731 scopus 로고    scopus 로고
    • Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network: New implications for Charcot-Marie-Tooth disease
    • Niemann A, Ruegg M, La Padula V, Schenone A, Suter U. 2005. Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network: new implications for Charcot-Marie-Tooth disease. J. Cell Biol. 170:1067-78
    • (2005) J. Cell Biol , vol.170 , pp. 1067-1078
    • Niemann, A.1    Ruegg, M.2    La Padula, V.3    Schenone, A.4    Suter, U.5
  • 111
    • 0033613865 scopus 로고    scopus 로고
    • Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial disorder
    • Nishino I, Spinazzola A, Hirano M. 1999. Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial disorder. Science 283:689-92
    • (1999) Science , vol.283 , pp. 689-692
    • Nishino, I.1    Spinazzola, A.2    Hirano, M.3
  • 112
    • 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 EI, Langer T. 2005. The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria. Cell 123:277-89
    • (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
  • 113
    • 26444488636 scopus 로고    scopus 로고
    • A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy
    • Ogilvie I, Kennaway NG, Shoubridge EA. 2005. A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy. J. Clin. Invest. 115:2784-92
    • (2005) J. Clin. Invest , vol.115 , pp. 2784-2792
    • Ogilvie, I.1    Kennaway, N.G.2    Shoubridge, E.A.3
  • 114
    • 0029741431 scopus 로고    scopus 로고
    • Evidence that specific mtDNA point mutations may not accumulate in skeletal muscle during normal human aging
    • Pallotti F, Chen X, Bonilla E, Schon EA. 1996. Evidence that specific mtDNA point mutations may not accumulate in skeletal muscle during normal human aging. Am. J. Hum. Genet. 59:591-602
    • (1996) Am. J. Hum. Genet , vol.59 , pp. 591-602
    • Pallotti, F.1    Chen, X.2    Bonilla, E.3    Schon, E.A.4
  • 115
    • 17744376804 scopus 로고    scopus 로고
    • GDAP1, the protein causing Charcot-Marie-Tooth disease type 4A, is expressed in neurons and is associated with mitochondria
    • Pedrola L, Espert A, Wu X, Claramunt R, Shy ME, Palau F. 2005. GDAP1, the protein causing Charcot-Marie-Tooth disease type 4A, is expressed in neurons and is associated with mitochondria. Hum. Mol. Genet. 14:1087-94
    • (2005) Hum. Mol. Genet , vol.14 , pp. 1087-1094
    • Pedrola, L.1    Espert, A.2    Wu, X.3    Claramunt, R.4    Shy, M.E.5    Palau, F.6
  • 116
    • 34250768073 scopus 로고    scopus 로고
    • A cut short to death: Parl and Opa1 in the regulation of mitochondrial morphology and apoptosis
    • Pellegrini L, Scorrano L. 2007. A cut short to death: Parl and Opa1 in the regulation of mitochondrial morphology and apoptosis. Cell Death Differ. 14:1275-84
    • (2007) Cell Death Differ , vol.14 , pp. 1275-1284
    • Pellegrini, L.1    Scorrano, L.2
  • 117
    • 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, Sanjo N, Maj M, et al. 2005. Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations. J. Biol. Chem. 280:34025-32
    • (2005) J. Biol. Chem , vol.280 , pp. 34025-34032
    • Petit, A.1    Kawarai, T.2    Paitel, E.3    Sanjo, N.4    Maj, M.5
  • 119
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, et al. 1997. Mutation in the α-synuclein gene identified in families with Parkinson's disease. Science 276:2045-47
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5
  • 120
    • 13244277454 scopus 로고    scopus 로고
    • Coenzyme Q deficiency and cerebellar ataxia associated with an aprataxin mutation
    • Quinzii C, Kattah AG, Naini A, Akman HO, Mootha VK, et al. 2005. Coenzyme Q deficiency and cerebellar ataxia associated with an aprataxin mutation. Neurology 64:539-41
    • (2005) Neurology , vol.64 , pp. 539-541
    • Quinzii, C.1    Kattah, A.G.2    Naini, A.3    Akman, H.O.4    Mootha, V.K.5
  • 121
    • 31544480133 scopus 로고    scopus 로고
    • A mutation in parahydoxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency
    • Quinzii C, Naini A, Salviati L, Trevisson E, Navas P, et al. 2006. A mutation in parahydoxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency. Am. J. Hum. Genet. 78:345-49
    • (2006) Am. J. Hum. Genet , vol.78 , pp. 345-349
    • Quinzii, C.1    Naini, A.2    Salviati, L.3    Trevisson, E.4    Navas, P.5
  • 122
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid β-induced deficits in an Alzheimer's disease mouse model
    • Roberson ED, Scearce-Levie K, Palop JJ, Yan F, Cheng IH, et al. 2007. Reducing endogenous tau ameliorates amyloid β-induced deficits in an Alzheimer's disease mouse model. Science 316:750-54
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5
  • 123
    • 33845866359 scopus 로고    scopus 로고
    • Schizophrenia in translation: Disrupted in schizophrenia (DISC1I): integrating clinical and basic findings
    • Roberts RC. 2007. Schizophrenia in translation: disrupted in schizophrenia (DISC1I): integrating clinical and basic findings. Schizophr. Bull. 33:11-15
    • (2007) Schizophr. Bull , vol.33 , pp. 11-15
    • Roberts, R.C.1
  • 124
    • 0036501592 scopus 로고    scopus 로고
    • Human deafness dystonia syndrome is caused by a defect in assembly of the DDP1/TIMM8a-TIMM13 complex
    • Roesch K, Curran SP, Tranebjaerg L, Koehler CM. 2002. Human deafness dystonia syndrome is caused by a defect in assembly of the DDP1/TIMM8a-TIMM13 complex. Hum. Mol. Genet. 11:477-86
    • (2002) Hum. Mol. Genet , vol.11 , pp. 477-486
    • Roesch, K.1    Curran, S.P.2    Tranebjaerg, L.3    Koehler, C.M.4
  • 125
    • 33846613222 scopus 로고    scopus 로고
    • The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease
    • Rogaeva E, Meng Y, Lee JH, Gu Y, Kawarai T, et al. 2007. The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease. Nat. Genet. 39:168-77
    • (2007) Nat. Genet , vol.39 , pp. 168-177
    • Rogaeva, E.1    Meng, Y.2    Lee, J.H.3    Gu, Y.4    Kawarai, T.5
  • 126
    • 0001157467 scopus 로고
    • Mitochondrial encephalomyopathies: Lumping, splitting, and melding
    • ed. AHV Schapira, S DiMauro, pp, Oxford: Butterworth-Heinemann
    • Rowland LP. 1994. Mitochondrial encephalomyopathies: lumping, splitting, and melding. In Mitochondrial Disorders in Neurology, ed. AHV Schapira, S DiMauro, pp. 116-29. Oxford: Butterworth-Heinemann
    • (1994) Mitochondrial Disorders in Neurology , pp. 116-129
    • Rowland, L.P.1
  • 127
    • 0036523031 scopus 로고    scopus 로고
    • Inhibition of intracellular cholesterol transport alters presenilin localization and amyloid precursor protein processing in neuronal cells
    • Runz H, Rietdorf J, Tomic I, de Bernard M, Beyreuther K, et al. 2002. Inhibition of intracellular cholesterol transport alters presenilin localization and amyloid precursor protein processing in neuronal cells. J. Neurosci. 22:1679-89
    • (2002) J. Neurosci , vol.22 , pp. 1679-1689
    • Runz, H.1    Rietdorf, J.2    Tomic, I.3    de Bernard, M.4    Beyreuther, K.5
  • 128
    • 31144453436 scopus 로고    scopus 로고
    • Spastin and atlastin, two proteins mutated in autosomal-dominant hereditary spastic paraplegia, are binding partners
    • Sanderson CM, Connell JW, Edwards TL, Bright NA, Duley S, et al. 2006. Spastin and atlastin, two proteins mutated in autosomal-dominant hereditary spastic paraplegia, are binding partners. Hum. Mol. Genet. 15:307-18
    • (2006) Hum. Mol. Genet , vol.15 , pp. 307-318
    • Sanderson, C.M.1    Connell, J.W.2    Edwards, T.L.3    Bright, N.A.4    Duley, S.5
  • 129
    • 33846008430 scopus 로고    scopus 로고
    • A novel mitochondrial DNA mutation in ND3 gene is associated with isolated complex I deficiency causing Leigh syndrome and dystonia
    • Sarzi E, Brown MD, Lebon S, Chretien D, Munnich A, et al. 2007. A novel mitochondrial DNA mutation in ND3 gene is associated with isolated complex I deficiency causing Leigh syndrome and dystonia. Am. J. Med. Genet. 143A:33-41
    • (2007) Am. J. Med. Genet , vol.143 A , pp. 33-41
    • Sarzi, E.1    Brown, M.D.2    Lebon, S.3    Chretien, D.4    Munnich, A.5
  • 130
    • 33749162349 scopus 로고    scopus 로고
    • Isoform- and subcellular fraction-specific differences in hippocampal 14-3-3 levels following experimentally evoked seizures and in human temporal lobe epilepsy
    • Schindler CK, Heverin M, Henshall DC. 2006. Isoform- and subcellular fraction-specific differences in hippocampal 14-3-3 levels following experimentally evoked seizures and in human temporal lobe epilepsy. J. Neurochem. 99:561-69
    • (2006) J. Neurochem , vol.99 , pp. 561-569
    • Schindler, C.K.1    Heverin, M.2    Henshall, D.C.3
  • 131
    • 33749061065 scopus 로고    scopus 로고
    • Barth syndrome, a human disorder of cardiolipin metabolism
    • Schlame M, Ren M. 2006. Barth syndrome, a human disorder of cardiolipin metabolism. FEBS Lett. 580:5450-55
    • (2006) FEBS Lett , vol.580 , pp. 5450-5455
    • Schlame, M.1    Ren, M.2
  • 132
    • 34147124830 scopus 로고    scopus 로고
    • Appendix 5. Gene products present in mitochondria of yeast and animal cells
    • Schon EA. 2007. Appendix 5. Gene products present in mitochondria of yeast and animal cells. Meth. Cell Biol. 80:835-76
    • (2007) Meth. Cell Biol , vol.80 , pp. 835-876
    • Schon, E.A.1
  • 133
    • 0024596946 scopus 로고
    • A direct repeat is a hotspot for large-scale deletions of human mitochondrial DNA
    • Schon EA, Rizzuto R, Moraes CT, Nakase H, Zeviani M, DiMauro S. 1989. A direct repeat is a hotspot for large-scale deletions of human mitochondrial DNA. Science 244:346-49
    • (1989) Science , vol.244 , pp. 346-349
    • Schon, E.A.1    Rizzuto, R.2    Moraes, C.T.3    Nakase, H.4    Zeviani, M.5    DiMauro, S.6
  • 135
    • 0033529331 scopus 로고    scopus 로고
    • Endogenous presenilin 1 redistributes to the surface of lamellipodia upon adhesion of Jurkat cells to a collagen matrix
    • Schwarzman AL, Singh N, Tsiper M, Gregori L, Dranovsky A, et al. 1999. Endogenous presenilin 1 redistributes to the surface of lamellipodia upon adhesion of Jurkat cells to a collagen matrix. Proc. Natl. Acad. Sci. USA 96:7932-37
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7932-7937
    • Schwarzman, A.L.1    Singh, N.2    Tsiper, M.3    Gregori, L.4    Dranovsky, A.5
  • 136
    • 31044445705 scopus 로고    scopus 로고
    • Photolabeling of cardiolipin binding subunits within bovine heart cytochrome c oxidase
    • Sedlak E, Panda M, Dale MP, Weintraub ST, Robinson NC. 2006. Photolabeling of cardiolipin binding subunits within bovine heart cytochrome c oxidase. Biochemistry 45:746-54
    • (2006) Biochemistry , vol.45 , pp. 746-754
    • Sedlak, E.1    Panda, M.2    Dale, M.P.3    Weintraub, S.T.4    Robinson, N.C.5
  • 138
    • 0017346294 scopus 로고
    • Mitochondrial encephalomyopathies: A group of neuromuscular disorders with defects in oxidative metabolism
    • Shapira Y, Harel S, Russell A. 1977. Mitochondrial encephalomyopathies: a group of neuromuscular disorders with defects in oxidative metabolism. Isr. J. Med. Sci. 13:161-64
    • (1977) Isr. J. Med. Sci , vol.13 , pp. 161-164
    • Shapira, Y.1    Harel, S.2    Russell, A.3
  • 139
    • 0021813419 scopus 로고
    • An immunochemical study of the pyruvate dehydrogenase deficit in Alzheimer's disease brain
    • Sheu KF, Kim YT, Blass JP, Weksler ME. 1985. An immunochemical study of the pyruvate dehydrogenase deficit in Alzheimer's disease brain. Ann. Neurol. 17:444-49
    • (1985) Ann. Neurol , vol.17 , pp. 444-449
    • Sheu, K.F.1    Kim, Y.T.2    Blass, J.P.3    Weksler, M.E.4
  • 141
    • 27944444154 scopus 로고    scopus 로고
    • Mitochondrial import and enzymatic activity of PINK1 mutants associated with recessive parkinsonism
    • Silvestri L, Caputo V, Bellacchio E, Atorino L, Dallapiccola B, et al. 2005. Mitochondrial import and enzymatic activity of PINK1 mutants associated with recessive parkinsonism. Hum. Mol. Genet. 14:3477-92
    • (2005) Hum. Mol. Genet , vol.14 , pp. 3477-3492
    • Silvestri, L.1    Caputo, V.2    Bellacchio, E.3    Atorino, L.4    Dallapiccola, B.5
  • 142
    • 0037339735 scopus 로고    scopus 로고
    • Localization of presenilin-nicastrin complexes and γ-secretase activity to the trans-Golgi network
    • Siman R, Velji J. 2003. Localization of presenilin-nicastrin complexes and γ-secretase activity to the trans-Golgi network. J. Neurochem. 84:1143-53
    • (2003) J. Neurochem , vol.84 , pp. 1143-1153
    • Siman, R.1    Velji, J.2
  • 143
    • 33751085653 scopus 로고    scopus 로고
    • Distinct clinical phenotypes associated with a mutation in the mitochondrial translation elongation factor EFTs
    • Smeitink JAM, Elpeleg O, Antonicka H, Diepstra H, Saada A, et al. 2006. Distinct clinical phenotypes associated with a mutation in the mitochondrial translation elongation factor EFTs. Am. J. Hum. Genet. 79:869-77
    • (2006) Am. J. Hum. Genet , vol.79 , pp. 869-877
    • Smeitink, J.A.M.1    Elpeleg, O.2    Antonicka, H.3    Diepstra, H.4    Saada, A.5
  • 144
    • 0027021442 scopus 로고
    • Mosaicism for a specific mitochondrial DNA mutation in adult human brain
    • Soong NW, Hinton DR, Cortopassi G, Arnheim N. 1992. Mosaicism for a specific mitochondrial DNA mutation in adult human brain. Nat. Genet. 2:318-23
    • (1992) Nat. Genet , vol.2 , pp. 318-323
    • Soong, N.W.1    Hinton, D.R.2    Cortopassi, G.3    Arnheim, N.4
  • 145
    • 33646376465 scopus 로고    scopus 로고
    • MPV17 encodes an inner mitochondrial membrane protein and is mutated in infantile hepatic mitochondrial DNA depletion
    • Spinazzola A, Viscomi C, Fernandez-Vizarra E, Carrara F, D'Adamo P, et al. 2006. MPV17 encodes an inner mitochondrial membrane protein and is mutated in infantile hepatic mitochondrial DNA depletion. Nat. Genet. 38:570-75
    • (2006) Nat. Genet , vol.38 , pp. 570-575
    • Spinazzola, A.1    Viscomi, C.2    Fernandez-Vizarra, E.3    Carrara, F.4    D'Adamo, P.5
  • 146
    • 23644436319 scopus 로고    scopus 로고
    • Disorders of nuclear-mitochondrial intergenomic signaling
    • Spinazzola A, Zeviani M. 2005. Disorders of nuclear-mitochondrial intergenomic signaling. Gene 354:162-68
    • (2005) Gene , vol.354 , pp. 162-168
    • Spinazzola, A.1    Zeviani, M.2
  • 147
    • 0025277392 scopus 로고
    • Association within a family of a balanced autosomal translocation with major mental illness
    • St Clair D, Blackwood D, Muir W, Carothers A, Walker M, et al. 1990. Association within a family of a balanced autosomal translocation with major mental illness. Lancet 336:13-16
    • (1990) Lancet , vol.336 , pp. 13-16
    • St Clair, D.1    Blackwood, D.2    Muir, W.3    Carothers, A.4    Walker, M.5
  • 148
    • 20044385920 scopus 로고    scopus 로고
    • Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease
    • Stokin GB, Lillo C, Falzone TL, Brusch RG, Rockenstein E, et al. 2005. Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease. Science 307:1282-88
    • (2005) Science , vol.307 , pp. 1282-1288
    • Stokin, G.B.1    Lillo, C.2    Falzone, T.L.3    Brusch, R.G.4    Rockenstein, E.5
  • 150
    • 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 LA, Diekert K, Jensen LT, Lill R, Culotta VC. 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. 276:38084-89
    • (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
  • 151
    • 0029162897 scopus 로고
    • An amino acid substitution in the pyruvate dehydrogenase E1αa gene, affecting mitochondrial import of the precursor protein
    • Takakubo F, Cartwright P, Hoogenraad N, Thorburn DR, Collins F, et al. 1995. An amino acid substitution in the pyruvate dehydrogenase E1αa gene, affecting mitochondrial import of the precursor protein. Am. J. Hum. Genet. 57:772-80
    • (1995) Am. J. Hum. Genet , vol.57 , pp. 772-780
    • Takakubo, F.1    Cartwright, P.2    Hoogenraad, N.3    Thorburn, D.R.4    Collins, F.5
  • 152
    • 0035782896 scopus 로고    scopus 로고
    • Neuropathological features of mitochondrial disorders
    • Tanji K, Kunimatsu T, Vu TH, Bonilla E. 2001. Neuropathological features of mitochondrial disorders. Cell Dev. Biol. 12:429-39
    • (2001) Cell Dev. Biol , vol.12 , pp. 429-439
    • Tanji, K.1    Kunimatsu, T.2    Vu, T.H.3    Bonilla, E.4
  • 153
    • 0034283541 scopus 로고    scopus 로고
    • Kearns-Sayre syndrome: Oncocytic transformation of choroid plexus epithelium
    • Tanji K, Schon EA, DiMauro S, Bonilla E. 2000. Kearns-Sayre syndrome: oncocytic transformation of choroid plexus epithelium. J. Neurol. Sci. 178:29-36
    • (2000) J. Neurol. Sci , vol.178 , pp. 29-36
    • Tanji, K.1    Schon, E.A.2    DiMauro, S.3    Bonilla, E.4
  • 154
    • 0026566850 scopus 로고
    • Heteroplasmic mtDNA mutation (T > G) at 8993 can cause Leigh disease when the percentage of abnormal mtDNA is high
    • Tatuch Y, Christodoulou J, Feigenbaum A, Clarke J, Wherret J, et al. 1992. Heteroplasmic mtDNA mutation (T > G) at 8993 can cause Leigh disease when the percentage of abnormal mtDNA is high. Am. J. Hum. Genet. 50:852-58
    • (1992) Am. J. Hum. Genet , vol.50 , pp. 852-858
    • Tatuch, Y.1    Christodoulou, J.2    Feigenbaum, A.3    Clarke, J.4    Wherret, J.5
  • 156
    • 33748054875 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and neurodegenerative disorders
    • ed. S DiMauro, M Hirano, EA Schon, pp, London: Informa Healthcare
    • Tieu K, Przedborski S. 2006. Mitochondrial dysfunction and neurodegenerative disorders. In Mitochondrial Medicine, ed. S DiMauro, M Hirano, EA Schon, pp. 279-307. London: Informa Healthcare
    • (2006) Mitochondrial Medicine , pp. 279-307
    • Tieu, K.1    Przedborski, S.2
  • 157
    • 0032470811 scopus 로고    scopus 로고
    • Mutations of SURF-1 in Leigh disease associated with cytochrome c oxidase deficiency
    • Tiranti V, Hoertnagel K, Carrozzo R, Galimberti C, Munaro M, et al. 1998. Mutations of SURF-1 in Leigh disease associated with cytochrome c oxidase deficiency. Am. J. Hum. Genet. 63:1609-21
    • (1998) Am. J. Hum. Genet , vol.63 , pp. 1609-1621
    • Tiranti, V.1    Hoertnagel, K.2    Carrozzo, R.3    Galimberti, C.4    Munaro, M.5
  • 158
    • 0038757833 scopus 로고    scopus 로고
    • 14-3-3ε is important for neuronal migration by binding to NUDEL: A molecular explanation for Miller-Dieker syndrome
    • Toyo-oka K, Shionoya A, Gambello MJ, Cardoso C, Leventer R, et al. 2003. 14-3-3ε is important for neuronal migration by binding to NUDEL: a molecular explanation for Miller-Dieker syndrome. Nat. Genet. 34:274-85
    • (2003) Nat. Genet , vol.34 , pp. 274-285
    • Toyo-oka, K.1    Shionoya, A.2    Gambello, M.J.3    Cardoso, C.4    Leventer, R.5
  • 159
  • 160
    • 4444316194 scopus 로고    scopus 로고
    • Mutant huntingtin impairs axonal trafficking in mammalian neurons in vivo and in vitro
    • Trushina E, Dyer RB, Badger JD 2nd, Ure D, Eide L, et al. 2004. Mutant huntingtin impairs axonal trafficking in mammalian neurons in vivo and in vitro. Mol. Cell. Biol. 24:8195-209
    • (2004) Mol. Cell. Biol , vol.24 , pp. 8195-8209
    • Trushina, E.1    Dyer, R.B.2    Badger 2nd, J.D.3    Ure, D.4    Eide, L.5
  • 161
    • 0142123112 scopus 로고    scopus 로고
    • Microtubule destabilization and nuclear entry are sequential steps leading to toxicity in Huntington's disease
    • Trushina E, Heldebrant MP, Perez-Terzic CM, Bortolon R, Kovtun IV, et al. 2003. Microtubule destabilization and nuclear entry are sequential steps leading to toxicity in Huntington's disease. Proc. Natl. Acad. Sci. USA 100:12171-76
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12171-12176
    • Trushina, E.1    Heldebrant, M.P.2    Perez-Terzic, C.M.3    Bortolon, R.4    Kovtun, I.V.5
  • 162
    • 33846006253 scopus 로고    scopus 로고
    • Infantile encephalopathy and defective mitochondrial DNA translation in patients with mutations of mitochondrial elongation factors EGF1 and EFTu
    • Valente L, Tiranti V, Marsano RM, Malfatti E, Fernandez-Vizarra E, et al. 2007. Infantile encephalopathy and defective mitochondrial DNA translation in patients with mutations of mitochondrial elongation factors EGF1 and EFTu. Am. J. Hum. Genet. 80:44-58
    • (2007) Am. J. Hum. Genet , vol.80 , pp. 44-58
    • Valente, L.1    Tiranti, V.2    Marsano, R.M.3    Malfatti, E.4    Fernandez-Vizarra, E.5
  • 163
    • 7244258941 scopus 로고    scopus 로고
    • Association of γ-secretase with lipid rafts in post-Golgi and endosome membranes
    • Vetrivel KS, Cheng H, Lin W, Sakurai T, Li T, et al. 2004. Association of γ-secretase with lipid rafts in post-Golgi and endosome membranes. J. Biol. Chem. 279:44945-54
    • (2004) J. Biol. Chem , vol.279 , pp. 44945-44954
    • Vetrivel, K.S.1    Cheng, H.2    Lin, W.3    Sakurai, T.4    Li, T.5
  • 164
    • 19044365959 scopus 로고    scopus 로고
    • GRACILE syndrome, a lethal metabolic disorder with iron overload, is caused by a point mutation in BCS1L
    • Visapaa I, Fellman V, Vesa J, Dasvarma A, Hutton JL, et al. 2002. GRACILE syndrome, a lethal metabolic disorder with iron overload, is caused by a point mutation in BCS1L. Am. J. Hum. Genet. 71:863-76
    • (2002) Am. J. Hum. Genet , vol.71 , pp. 863-876
    • Visapaa, I.1    Fellman, V.2    Vesa, J.3    Dasvarma, A.4    Hutton, J.L.5
  • 165
    • 0024242545 scopus 로고
    • Mitochondrial DNA mutation associated with Leber's hereditary optic neuropathy
    • Wallace DC, Singh G, Lott MT, Hodge JA, Shurr TG, et al. 1988. Mitochondrial DNA mutation associated with Leber's hereditary optic neuropathy. Science 242:1427-30
    • (1988) Science , vol.242 , pp. 1427-1430
    • Wallace, D.C.1    Singh, G.2    Lott, M.T.3    Hodge, J.A.4    Shurr, T.G.5
  • 166
    • 0032833421 scopus 로고    scopus 로고
    • Mitochondrial DNA variation in human evolution and disease
    • Wallace DC, Brown MD, Lott MT. 1999. Mitochondrial DNA variation in human evolution and disease. Gene 238:211-30
    • (1999) Gene , vol.238 , pp. 211-230
    • Wallace, D.C.1    Brown, M.D.2    Lott, M.T.3
  • 167
    • 8044231311 scopus 로고    scopus 로고
    • The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum
    • Walter J, Capell A, Grunberg J, Pesold B, Schindzielorz A, et al. 1996. The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum. Mol. Med. 2:673-91
    • (1996) Mol. Med , vol.2 , pp. 673-691
    • Walter, J.1    Capell, A.2    Grunberg, J.3    Pesold, B.4    Schindzielorz, A.5
  • 169
    • 0036321382 scopus 로고    scopus 로고
    • Mitochondrial DNA and respiratory chain function in spinal cords of ALS patients
    • Wiedemann FR, Manfredi G, Mawrin C, Beal MF, Schon EA. 2002. Mitochondrial DNA and respiratory chain function in spinal cords of ALS patients. J. Neurochem. 80:616-25
    • (2002) J. Neurochem , vol.80 , pp. 616-625
    • Wiedemann, F.R.1    Manfredi, G.2    Mawrin, C.3    Beal, M.F.4    Schon, E.A.5
  • 171
    • 24944534660 scopus 로고    scopus 로고
    • Mitochondrial localization of Parkinson's disease related protein DJ-1: Implications for pathogenesis
    • Zhang LS, Shimoji M, Thomas B, Moore D, Yu S-W, et al. 2005a. Mitochondrial localization of Parkinson's disease related protein DJ-1: implications for pathogenesis. Hum. Mol. Genet. 14:2063-73
    • (2005) Hum. Mol. Genet , vol.14 , pp. 2063-2073
    • Zhang, L.S.1    Shimoji, M.2    Thomas, B.3    Moore, D.4    Yu, S.-W.5
  • 172
    • 23844540312 scopus 로고    scopus 로고
    • Cardiolipin is essential for organization of complexes III and IV into a supercomplex in intact yeast mitochondria
    • Zhang M, Mileykovskaya E, Dowhan W. 2005b. Cardiolipin is essential for organization of complexes III and IV into a supercomplex in intact yeast mitochondria. J. Biol. Chem. 280:29403-8
    • (2005) J. Biol. Chem , vol.280 , pp. 29403-29408
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3
  • 173
    • 17344362021 scopus 로고    scopus 로고
    • SURF1, encoding a factor involved in the biogenesis of cytochrome c oxidase, is mutated in Leigh syndrome
    • Zhu Z, Yao J, Johns T, Fu K, De Bie I, et al. 1998. SURF1, encoding a factor involved in the biogenesis of cytochrome c oxidase, is mutated in Leigh syndrome. Nat. Genet. 20:337-43
    • (1998) Nat. Genet , vol.20 , pp. 337-343
    • Zhu, Z.1    Yao, J.2    Johns, T.3    Fu, K.4    De Bie, I.5
  • 175
    • 2442589922 scopus 로고    scopus 로고
    • Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
    • Zuchner S, Mersiyanova IV, Muglia M, Bissar-Tadmouri N, Rochelle J, et al. 2004. Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A. Nat. Genet. 36:449-51
    • (2004) Nat. Genet , vol.36 , pp. 449-451
    • Zuchner, S.1    Mersiyanova, I.V.2    Muglia, M.3    Bissar-Tadmouri, N.4    Rochelle, J.5
  • 176
    • 33746554263 scopus 로고    scopus 로고
    • Mutations in the novel mitochondrial protein REEP1 cause hereditary spastic paraplegia type 31
    • Zuchner S, Wang G, Tran-Viet KN, Nance MA, Gaskell PC, et al. 2006b. Mutations in the novel mitochondrial protein REEP1 cause hereditary spastic paraplegia type 31. Am. J. Hum. Genet. 79:365-69
    • (2006) Am. J. Hum. Genet , vol.79 , pp. 365-369
    • Zuchner, S.1    Wang, G.2    Tran-Viet, K.N.3    Nance, M.A.4    Gaskell, P.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.