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Volumn 38, Issue 3, 2015, Pages 405-415

Mitochondrial disease associated with complex I (NADH-CoQ oxidoreductase) deficiency

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS DNA; IRON SULFUR PROTEIN; MITOCHONDRIAL DNA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); STRUCTURAL PROTEIN;

EID: 84929146466     PISSN: 01418955     EISSN: 15732665     Source Type: Journal    
DOI: 10.1007/s10545-014-9768-6     Document Type: Article
Times cited : (54)

References (81)
  • 1
    • 3543015013 scopus 로고    scopus 로고
    • Subunit composition of mitochondrial complex I from the yeast Yarrowia lipolytica
    • COI: 1:CAS:528:DC%2BD2cXmt1WktLw%3D, PID: 15282186
    • Abdrakhmanova A, Zickermann V, Bostina M et al (2004) Subunit composition of mitochondrial complex I from the yeast Yarrowia lipolytica. Biochim Biophys Acta 1658:148–156
    • (2004) Biochim Biophys Acta , vol.1658 , pp. 148-156
    • Abdrakhmanova, A.1    Zickermann, V.2    Bostina, M.3
  • 2
    • 79959714122 scopus 로고    scopus 로고
    • A scaffold of accessory subunits links the peripheral arm and the distal proton-pumping module of mitochondrial complex I
    • COI: 1:CAS:528:DC%2BC3MXotFSmu7s%3D, PID: 21545356
    • Angerer H, Zwicker K, Wumaier Z et al (2011) A scaffold of accessory subunits links the peripheral arm and the distal proton-pumping module of mitochondrial complex I. Biochem J 437:279–288
    • (2011) Biochem J , vol.437 , pp. 279-288
    • Angerer, H.1    Zwicker, K.2    Wumaier, Z.3
  • 3
    • 84874352529 scopus 로고    scopus 로고
    • Crystal structure of the entire respiratory complex I
    • COI: 1:CAS:528:DC%2BC3sXjtFWiu70%3D, PID: 23417064
    • Baradaran R, Berrisford JM, Minhas GS, Sazanov LA (2013) Crystal structure of the entire respiratory complex I. Nature 494:443–448
    • (2013) Nature , vol.494 , pp. 443-448
    • Baradaran, R.1    Berrisford, J.M.2    Minhas, G.S.3    Sazanov, L.A.4
  • 4
    • 0035888637 scopus 로고    scopus 로고
    • Selection of a mtDNA sequence variant in hepatocytes of heteroplasmic mice is not due to differences in respiratory chain function or efficiency of replication
    • COI: 1:CAS:528:DC%2BD3MXptVarurs%3D, PID: 11709534
    • Battersby BJ, Shoubridge EA (2001) Selection of a mtDNA sequence variant in hepatocytes of heteroplasmic mice is not due to differences in respiratory chain function or efficiency of replication. Hum Mol Genet 10:2469–2479
    • (2001) Hum Mol Genet , vol.10 , pp. 2469-2479
    • Battersby, B.J.1    Shoubridge, E.A.2
  • 5
    • 0018427128 scopus 로고
    • Respiration-deficient Chinese hamster cell mutants: biochemical characterization
    • COI: 1:CAS:528:DyaE1MXlsFCqsLo%3D, PID: 494059
    • Breen GAM, Scheffler IE (1979) Respiration-deficient Chinese hamster cell mutants: biochemical characterization. Somat Cell Genet 5:441–451
    • (1979) Somat Cell Genet , vol.5 , pp. 441-451
    • Breen, G.A.M.1    Scheffler, I.E.2
  • 6
    • 0019724812 scopus 로고
    • Integrity of mitochondria in a mammalian cell mutant defective in mitochondrial protein synthesis
    • COI: 1:CAS:528:DyaL3MXksF2nsLs%3D, PID: 6265473
    • Burnett KG, Scheffler IE (1981) Integrity of mitochondria in a mammalian cell mutant defective in mitochondrial protein synthesis. J Cell Biol 90:108–115
    • (1981) J Cell Biol , vol.90 , pp. 108-115
    • Burnett, K.G.1    Scheffler, I.E.2
  • 7
    • 77957606541 scopus 로고    scopus 로고
    • High-throughput, pooled sequencing identifies mutations in NUBPL and FOXRED1 in human complex I deficiency
    • COI: 1:CAS:528:DC%2BC3cXhtFWksrbF, PID: 20818383
    • Calvo SE, Tucker EJ, Compton AG et al (2010) High-throughput, pooled sequencing identifies mutations in NUBPL and FOXRED1 in human complex I deficiency. Nat Genet 42:851–858
    • (2010) Nat Genet , vol.42 , pp. 851-858
    • Calvo, S.E.1    Tucker, E.J.2    Compton, A.G.3
  • 8
    • 74249105479 scopus 로고    scopus 로고
    • New evidence confirms that the mitochondrial bottleneck is generated without reduction of mitochondrial DNA content in early primordial germ cells of mice
    • Cao L, Shitara H, Sugimoto M, Hayashi J, Abe K, Yonekawa H (2009) New evidence confirms that the mitochondrial bottleneck is generated without reduction of mitochondrial DNA content in early primordial germ cells of mice. PLoSGenet 5:e1000756
    • (2009) PLoSGenet , vol.5 , pp. 1000756
    • Cao, L.1    Shitara, H.2    Sugimoto, M.3    Hayashi, J.4    Abe, K.5    Yonekawa, H.6
  • 9
    • 0038160473 scopus 로고    scopus 로고
    • Analysis of the subunit composition of complex I from bovine heart mitochondria. Mol
    • COI: 1:CAS:528:DC%2BD3sXivFWnt70%3D
    • Carroll J, Fearnley IM, Shannon RJ, Hirst J, Walker JE (2003) Analysis of the subunit composition of complex I from bovine heart mitochondria. Mol. Cell Proteomics 2:117–126
    • (2003) Cell Proteomics , vol.2 , pp. 117-126
    • Carroll, J.1    Fearnley, I.M.2    Shannon, R.J.3    Hirst, J.4    Walker, J.E.5
  • 10
    • 0020463725 scopus 로고
    • Mapping of the genes for some components of complex I of the electron transport chain on the X chromosome of mammals
    • COI: 1:CAS:528:DyaL2cXktVCmtbs%3D, PID: 6819642
    • Day C, Scheffler IE (1982) Mapping of the genes for some components of complex I of the electron transport chain on the X chromosome of mammals. Somat Cell Genet 8:691–707
    • (1982) Somat Cell Genet , vol.8 , pp. 691-707
    • Day, C.1    Scheffler, I.E.2
  • 11
    • 39849104755 scopus 로고    scopus 로고
    • cAMP-dependent protein kinase regulates the mitochondrial import of the nuclear encoded NDUFS4 subunit of complex I
    • De RD, Panelli D, Sardanelli AM, Papa S (2008) cAMP-dependent protein kinase regulates the mitochondrial import of the nuclear encoded NDUFS4 subunit of complex I. Cell Signal 20:989–997
    • (2008) Cell Signal , vol.20 , pp. 989-997
    • De, R.D.1    Panelli, D.2    Sardanelli, A.M.3    Papa, S.4
  • 12
    • 0017303538 scopus 로고
    • A respiration-deficient Chinese hamster cell line with a defect in NADH-Coenzyme Q reductase
    • COI: 1:CAS:528:DyaE28Xlt1Smur8%3D, PID: 947896
    • DeFrancesco L, Scheffler IE, Bissell MJ (1976) A respiration-deficient Chinese hamster cell line with a defect in NADH-Coenzyme Q reductase. J Biol Chem 251:4588–4595
    • (1976) J Biol Chem , vol.251 , pp. 4588-4595
    • DeFrancesco, L.1    Scheffler, I.E.2    Bissell, M.J.3
  • 13
    • 0016975851 scopus 로고
    • The selection of Chinese hamster cells deficient in oxidative energy metabolism
    • COI: 1:CAS:528:DyaE1cXhtFymsr4%3D, PID: 1027147
    • Ditta GS, Soderberg K, Scheffler IE (1976) The selection of Chinese hamster cells deficient in oxidative energy metabolism. Somat Cell Genet 2:331–344
    • (1976) Somat Cell Genet , vol.2 , pp. 331-344
    • Ditta, G.S.1    Soderberg, K.2    Scheffler, I.E.3
  • 14
    • 0017390038 scopus 로고
    • Chinese hamster cell mutant with defective mitochondrial protein synthesis
    • COI: 1:CAS:528:DyaE2sXlsVOhsrk%3D, PID: 196202
    • Ditta GS, Soderberg K, Scheffler IE (1977) Chinese hamster cell mutant with defective mitochondrial protein synthesis. Nature 268:64–67
    • (1977) Nature , vol.268 , pp. 64-67
    • Ditta, G.S.1    Soderberg, K.2    Scheffler, I.E.3
  • 15
    • 39349105943 scopus 로고    scopus 로고
    • A mouse model of mitochondrial disease reveals germline selection against severe mtDNA mutations
    • COI: 1:CAS:528:DC%2BD1cXhslOmt70%3D, PID: 18276892
    • Fan W, Waymire KG, Narula N et al (2008) A mouse model of mitochondrial disease reveals germline selection against severe mtDNA mutations. Science 319:958–962
    • (2008) Science , vol.319 , pp. 958-962
    • Fan, W.1    Waymire, K.G.2    Narula, N.3
  • 16
    • 78649454768 scopus 로고    scopus 로고
    • FOXRED1, encoding an FAD-dependent oxidoreductase complex-I-specific molecular chaperone, is mutated in infantile-onset mitochondrial encephalopathy
    • COI: 1:CAS:528:DC%2BC3cXhsVyhsrzI, PID: 20858599
    • Fassone E, Duncan AJ, Taanman JW et al (2010) FOXRED1, encoding an FAD-dependent oxidoreductase complex-I-specific molecular chaperone, is mutated in infantile-onset mitochondrial encephalopathy. Hum Mol Genet 19(24):4837–4847
    • (2010) Hum Mol Genet , vol.19 , Issue.24 , pp. 4837-4847
    • Fassone, E.1    Duncan, A.J.2    Taanman, J.W.3
  • 17
    • 33846846449 scopus 로고    scopus 로고
    • X-linked NDUFA1 gene mutations associated with mitochondrial encephalomyopathy
    • COI: 1:CAS:528:DC%2BD2sXitlyjtLs%3D, PID: 17262856
    • Fernandez-Moreira D, Ugalde C, Smeets R et al (2007) X-linked NDUFA1 gene mutations associated with mitochondrial encephalomyopathy. Ann Neurol 61:73–83
    • (2007) Ann Neurol , vol.61 , pp. 73-83
    • Fernandez-Moreira, D.1    Ugalde, C.2    Smeets, R.3
  • 18
    • 77950326171 scopus 로고    scopus 로고
    • Severe X-linked mitochondrial encephalomyopathy associated with a mutation in apoptosis-inducing factor
    • COI: 1:CAS:528:DC%2BC3cXlsFWmtro%3D, PID: 20362274
    • Ghezzi D, Sevrioukova I, Invernizzi F et al (2010) Severe X-linked mitochondrial encephalomyopathy associated with a mutation in apoptosis-inducing factor. Am J Hum Genet 86:639–649
    • (2010) Am J Hum Genet , vol.86 , pp. 639-649
    • Ghezzi, D.1    Sevrioukova, I.2    Invernizzi, F.3
  • 19
    • 79251600222 scopus 로고    scopus 로고
    • Mitochondrial 12S rRNA mutations associated with aminoglycoside ototoxicity
    • COI: 1:CAS:528:DC%2BC3MXhtlGlt7Y%3D, PID: 21047563
    • Guan MX (2011) Mitochondrial 12S rRNA mutations associated with aminoglycoside ototoxicity. Mitochondrion 11:237–245
    • (2011) Mitochondrion , vol.11 , pp. 237-245
    • Guan, M.X.1
  • 20
    • 0021891869 scopus 로고
    • The mitochondrial electron transport and oxidative phosphorylation system
    • COI: 1:STN:280:DyaL2M3nsl2rsg%3D%3D, PID: 2862839
    • Hatefi Y (1985) The mitochondrial electron transport and oxidative phosphorylation system. Ann Rev Biochem 54:1015–1069
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 1015-1069
    • Hatefi, Y.1
  • 21
    • 0018337615 scopus 로고
    • Proteins, polypeptides, prosthetic groups and enzymic properties of complexes I, II, III, IV, and V of the mitochondrial oxidative phosphorylation system
    • COI: 1:CAS:528:DyaE1MXkvVKjsbg%3D, PID: 459885
    • Hatefi Y, Galante YM, Stiggal DL, Ragan CI (1979) Proteins, polypeptides, prosthetic groups and enzymic properties of complexes I, II, III, IV, and V of the mitochondrial oxidative phosphorylation system. Methods Enzymol 56:577–602
    • (1979) Methods Enzymol , vol.56 , pp. 577-602
    • Hatefi, Y.1    Galante, Y.M.2    Stiggal, D.L.3    Ragan, C.I.4
  • 22
    • 84867101923 scopus 로고    scopus 로고
    • Complexome profiling identifies TMEM126B as a component of the mitochondrial complex I assembly complex
    • COI: 1:CAS:528:DC%2BC38XhtlGqu7vM, PID: 22982022
    • Heide H, Bleier L, Steger M et al (2012) Complexome profiling identifies TMEM126B as a component of the mitochondrial complex I assembly complex. Cell Metab 16:538–549
    • (2012) Cell Metab , vol.16 , pp. 538-549
    • Heide, H.1    Bleier, L.2    Steger, M.3
  • 23
    • 73849114263 scopus 로고    scopus 로고
    • Towards the molecular mechanism of respiratory complex I
    • PID: 20025615
    • Hirst J (2009) Towards the molecular mechanism of respiratory complex I. Biochem J 425:327–339
    • (2009) Biochem J , vol.425 , pp. 327-339
    • Hirst, J.1
  • 24
    • 79959731297 scopus 로고    scopus 로고
    • Why does mitochondrial complex I have so many subunits?
    • COI: 1:CAS:528:DC%2BC3MXotFSls78%3D, PID: 21711245
    • Hirst J (2011) Why does mitochondrial complex I have so many subunits? Biochem J 437:e1–e3
    • (2011) Biochem J , vol.437 , pp. 1-3
    • Hirst, J.1
  • 25
    • 84864567425 scopus 로고    scopus 로고
    • Molecular base of biochemical complex I deficiency
    • COI: 1:CAS:528:DC%2BC38XhtlWksLjO, PID: 22820119, %20
    • Hoefs SJ, Rodenburg RJ, Smeitink JA, Van den Heuvel LP (2012) Molecular base of biochemical complex I deficiency. Mitochondrion 12(5):520–532, %20
    • (2012) Mitochondrion , vol.12 , Issue.5 , pp. 520-532
    • Hoefs, S.J.1    Rodenburg, R.J.2    Smeitink, J.A.3    Van den Heuvel, L.P.4
  • 26
    • 0023883150 scopus 로고
    • Deletions of muscle mitochondrial DNA in patients with mitochondrial myopathies
    • COI: 1:STN:280:DyaL1c7ktlWmtQ%3D%3D, PID: 2830540
    • Holt IJ, Harding AE, Morgan Hughes JA (1988a) Deletions of muscle mitochondrial DNA in patients with mitochondrial myopathies. Nature 331:717–719
    • (1988) Nature , vol.331 , pp. 717-719
    • Holt, I.J.1    Harding, A.E.2    Morgan Hughes, J.A.3
  • 27
    • 0023936944 scopus 로고
    • Mitochondrial DNA polymorphism in mitochondrial myopathy
    • COI: 1:STN:280:DyaL1c3ht1Chsw%3D%3D, PID: 2896621
    • Holt IJ, Harding AE, Morgan-Hughes JA (1988b) Mitochondrial DNA polymorphism in mitochondrial myopathy. Hum Genet 79:53–57
    • (1988) Hum Genet , vol.79 , pp. 53-57
    • Holt, I.J.1    Harding, A.E.2    Morgan-Hughes, J.A.3
  • 28
    • 0036024979 scopus 로고    scopus 로고
    • Production of mitochondrial DNA transgenic mice using zygotes
    • COI: 1:CAS:528:DC%2BD38Xks1Ghu7w%3D, PID: 12054927
    • Inoue K, Ogura A, Hayashi J (2002) Production of mitochondrial DNA transgenic mice using zygotes. Methods 26:358–363
    • (2002) Methods , vol.26 , pp. 358-363
    • Inoue, K.1    Ogura, A.2    Hayashi, J.3
  • 29
    • 69149109036 scopus 로고    scopus 로고
    • AIF: not just an apoptosis-inducing factor
    • COI: 1:CAS:528:DC%2BD1MXht1SntbzE
    • Joza N, Pospisilik JA, Hangen E et al (2009) AIF: not just an apoptosis-inducing factor. AnnNYAcadSci 1171:2–11
    • (2009) AnnNYAcadSci , vol.1171 , pp. 2-11
    • Joza, N.1    Pospisilik, J.A.2    Hangen, E.3
  • 30
    • 84929172899 scopus 로고    scopus 로고
    • A novel mouse model for nuclear-encoded partial respiratory chain complex I deficiency
    • Kim C, Potluri P, Gout D, Minter LM, Wallace DC, Yadava N (2012) A novel mouse model for nuclear-encoded partial respiratory chain complex I deficiency. Mitochondrion 12:571
    • (2012) Mitochondrion , vol.12 , pp. 571
    • Kim, C.1    Potluri, P.2    Gout, D.3    Minter, L.M.4    Wallace, D.C.5    Yadava, N.6
  • 31
    • 0032561134 scopus 로고    scopus 로고
    • Involvement of two novel chaperones in the assembly of mitochondrial NADH:Ubiquinone oxidoreductase (complex I)cAMP-dependent phosphorylation of the nuclear encoded 18-kDa (IP) subunit of respiratory complex I and activation of the complex in serum-starved mouse fibroblast cultures
    • COI: 1:CAS:528:DyaK1cXntFWhsb8%3D
    • Kuffner R, Rohr A, Schmiede A et al (1998) Involvement of two novel chaperones in the assembly of mitochondrial NADH:Ubiquinone oxidoreductase (complex I)cAMP-dependent phosphorylation of the nuclear encoded 18-kDa (IP) subunit of respiratory complex I and activation of the complex in serum-starved mouse fibroblast cultures. J Biol Chem 283:409–417
    • (1998) J Biol Chem , vol.283 , pp. 409-417
    • Kuffner, R.1    Rohr, A.2    Schmiede, A.3
  • 32
    • 4043089861 scopus 로고    scopus 로고
    • Molecular analysis of the mitochondrial 12S rRNA and tRNASer(UCN) genes in paediatric subjects with non-syndromic hearing loss
    • COI: 1:CAS:528:DC%2BD2cXnsFCku7c%3D, PID: 15286157
    • Li R, Greinwald JH Jr, Yang L, Choo DI, Wenstrup RJ, Guan MX (2004) Molecular analysis of the mitochondrial 12S rRNA and tRNASer(UCN) genes in paediatric subjects with non-syndromic hearing loss. J Med Genet 41:615–620
    • (2004) J Med Genet , vol.41 , pp. 615-620
    • Li, R.1    Greinwald, J.H.2    Yang, L.3    Choo, D.I.4    Wenstrup, R.J.5    Guan, M.X.6
  • 33
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases
    • COI: 1:CAS:528:DC%2BD1cXos1eku70%3D, PID: 18366324
    • Lill R, Muhlenhoff U (2008) Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu Rev Biochem 77:669–700
    • (2008) Annu Rev Biochem , vol.77 , pp. 669-700
    • Lill, R.1    Muhlenhoff, U.2
  • 34
    • 30044434360 scopus 로고    scopus 로고
    • The mitochondrial theory of aging and its relationship to reactive oxygen species damage and somatic mtDNA mutations
    • COI: 1:CAS:528:DC%2BD28XivVyktw%3D%3D, PID: 16365283
    • Loeb LA, Wallace DC, Martin GM (2005) The mitochondrial theory of aging and its relationship to reactive oxygen species damage and somatic mtDNA mutations. Proc Natl Acad Sci U S A 102:18769–18770
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 18769-18770
    • Loeb, L.A.1    Wallace, D.C.2    Martin, G.M.3
  • 35
    • 39049085707 scopus 로고    scopus 로고
    • Protection by the NDI1 gene against neurodegeneration in a rotenone rat model of Parkinson’s disease
    • Marella M, Seo BB, Nakamaru-Ogiso E, Greenamyre JT, Matsuno-Yagi A, Yagi T (2008) Protection by the NDI1 gene against neurodegeneration in a rotenone rat model of Parkinson’s disease. PLoSONE 3:e1433
    • (2008) PLoSONE , vol.3 , pp. 1433
    • Marella, M.1    Seo, B.B.2    Nakamaru-Ogiso, E.3    Greenamyre, J.T.4    Matsuno-Yagi, A.5    Yagi, T.6
  • 36
    • 77955368934 scopus 로고    scopus 로고
    • Successful amelioration of mitochondrial optic neuropathy using the yeast NDI1 gene in a rat animal model
    • Marella M, Seo BB, Thomas BB, Matsuno-Yagi A, Yagi T (2010) Successful amelioration of mitochondrial optic neuropathy using the yeast NDI1 gene in a rat animal model. PLoSONE 5(7):e11472
    • (2010) PLoSONE , vol.5 , Issue.7 , pp. 11472
    • Marella, M.1    Seo, B.B.2    Thomas, B.B.3    Matsuno-Yagi, A.4    Yagi, T.5
  • 38
    • 84858057118 scopus 로고    scopus 로고
    • Mitochondrial complex I plays an essential role in human respirasome assembly
    • COI: 1:CAS:528:DC%2BC38XisFKgurc%3D, PID: 22342700
    • Moreno-Lastres D, Fontanesi F, Garcaa-Consuegra I et al (2012) Mitochondrial complex I plays an essential role in human respirasome assembly. Cell Metab 15:324–335
    • (2012) Cell Metab , vol.15 , pp. 324-335
    • Moreno-Lastres, D.1    Fontanesi, F.2    Garcaa-Consuegra, I.3
  • 39
    • 77956318447 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenase 9is required for the biogenesis of oxidative phosphorylation complex I
    • COI: 1:CAS:528:DC%2BC3cXhtFamsbnE, PID: 20816094
    • Nouws J, Nijtmans L, Houten SM et al (2010) Acyl-CoA dehydrogenase 9is required for the biogenesis of oxidative phosphorylation complex I. Cell Metab 12:283–294
    • (2010) Cell Metab , vol.12 , pp. 283-294
    • Nouws, J.1    Nijtmans, L.2    Houten, S.M.3
  • 40
    • 84856734831 scopus 로고    scopus 로고
    • Assembly factors as a new class of disease genes for mitochondrial complex I deficiency: cause, pathology and treatment options
    • PID: 22036961
    • Nouws J, Nijtmans LG, Smeitink JA, Vogel RO (2012) Assembly factors as a new class of disease genes for mitochondrial complex I deficiency: cause, pathology and treatment options. Brain 135(Pt 1):12–22
    • (2012) Brain , vol.135 , pp. 12-22
    • Nouws, J.1    Nijtmans, L.G.2    Smeitink, J.A.3    Vogel, R.O.4
  • 41
    • 26444488636 scopus 로고    scopus 로고
    • A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy
    • COI: 1:CAS:528:DC%2BD2MXhtVygt7nE, PID: 16200211
    • Ogilvie I, Kennaway NG, Shoubridge EA (2005) A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy. J Clin Invest 115:2784–2792
    • (2005) J Clin Invest , vol.115 , pp. 2784-2792
    • Ogilvie, I.1    Kennaway, N.G.2    Shoubridge, E.A.3
  • 42
    • 0028785471 scopus 로고
    • A Chinese hamster mutant cell line with a defect in the integral membrane protein CII-3 of complex II of the mitochondrial electron transport chain
    • Oostveen FG, Au HC, Meijer P-J, Scheffler IE (1995) A Chinese hamster mutant cell line with a defect in the integral membrane protein CII-3 of complex II of the mitochondrial electron transport chain. J Biol Chem 270:26104–26108
    • (1995) J Biol Chem , vol.270 , pp. 26104-26108
    • Oostveen, F.G.1    Au, H.C.2    Meijer, P.-J.3    Scheffler, I.E.4
  • 43
    • 46349103594 scopus 로고    scopus 로고
    • A mitochondrial protein compendium elucidates complex I disease biology
    • COI: 1:CAS:528:DC%2BD1cXoslyjtLY%3D, PID: 18614015
    • Pagliarini DJ, Calvo SE, Chang B et al (2008) A mitochondrial protein compendium elucidates complex I disease biology. Cell 134:112–123
    • (2008) Cell , vol.134 , pp. 112-123
    • Pagliarini, D.J.1    Calvo, S.E.2    Chang, B.3
  • 45
    • 84856120776 scopus 로고    scopus 로고
    • Mitochondrial complex I deficiency of nuclear origin II. Non-structural genes
    • COI: 1:CAS:528:DC%2BC38XhtFKru74%3D, PID: 22099533
    • Pagniez-Mammeri H, Rak M, Legrand A, Benit P, Rustin P, Slama A (2012b) Mitochondrial complex I deficiency of nuclear origin II. Non-structural genes. Mol Genet Metab 105:173–179
    • (2012) Mol Genet Metab , vol.105 , pp. 173-179
    • Pagniez-Mammeri, H.1    Rak, M.2    Legrand, A.3    Benit, P.4    Rustin, P.5    Slama, A.6
  • 46
    • 0035793474 scopus 로고    scopus 로고
    • Mutation in the NDUFS4 gene of complex I abolishes cAMP-dependent activation of the complex in a child with fatal neurological syndrome
    • COI: 1:CAS:528:DC%2BD3MXpsF2mug%3D%3D, PID: 11165261
    • Papa S, Scacco S, Sardanelli AM et al (2001) Mutation in the NDUFS4 gene of complex I abolishes cAMP-dependent activation of the complex in a child with fatal neurological syndrome. FEBS Lett 489:259–262
    • (2001) FEBS Lett , vol.489 , pp. 259-262
    • Papa, S.1    Scacco, S.2    Sardanelli, A.M.3
  • 47
    • 3242883875 scopus 로고    scopus 로고
    • The role of the ESSS protein in the assembly of a functional and stable mammalian mitochondrial complex I (NADH-ubiquinone oxidoreductase)
    • COI: 1:CAS:528:DC%2BD2cXmsFCit7g%3D, PID: 15265046
    • Potluri P, Yadava N, Scheffler IE (2004) The role of the ESSS protein in the assembly of a functional and stable mammalian mitochondrial complex I (NADH-ubiquinone oxidoreductase). Eur J Biochem 271:3265–3273
    • (2004) Eur J Biochem , vol.271 , pp. 3265-3273
    • Potluri, P.1    Yadava, N.2    Scheffler, I.E.3
  • 48
    • 62149099561 scopus 로고    scopus 로고
    • A novel NDUFA1 mutation leads to a progressive mitochondrial complex I-specific neurodegenerative disease
    • COI: 1:CAS:528:DC%2BD1MXjt1agtbc%3D, PID: 19185523
    • Potluri P, Davila A, Ruiz-Pesini E et al (2009) A novel NDUFA1 mutation leads to a progressive mitochondrial complex I-specific neurodegenerative disease. Mol Genet Metab 96:189–195
    • (2009) Mol Genet Metab , vol.96 , pp. 189-195
    • Potluri, P.1    Davila, A.2    Ruiz-Pesini, E.3
  • 49
    • 38749144436 scopus 로고    scopus 로고
    • C6ORF66 is an assembly factor of mitochondrial complex I
    • COI: 1:CAS:528:DC%2BD1cXhsFOks74%3D, PID: 18179882
    • Saada A, Edvardson S, Rapoport M et al (2008) C6ORF66 is an assembly factor of mitochondrial complex I. Am J Hum Genet 82:32–38
    • (2008) Am J Hum Genet , vol.82 , pp. 32-38
    • Saada, A.1    Edvardson, S.2    Rapoport, M.3
  • 50
    • 77952689461 scopus 로고    scopus 로고
    • Expression of the yeast NADH dehydrogenase Ndi1 in Drosophila confers increased lifespan independently of dietary restriction
    • COI: 1:CAS:528:DC%2BC3cXmslGrtrw%3D, PID: 20435911
    • Sanz A, Soikkeli M, Portero-Otin M et al (2010) Expression of the yeast NADH dehydrogenase Ndi1 in Drosophila confers increased lifespan independently of dietary restriction. Proc Natl Acad Sci U S A 107(20):9105–9110
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.20 , pp. 9105-9110
    • Sanz, A.1    Soikkeli, M.2    Portero-Otin, M.3
  • 51
    • 0028848239 scopus 로고
    • Native electrophoresis for isolation of mitochondrial oxidative phosphorylation protein complexes
    • COI: 1:STN:280:DyaK287jtVOjtQ%3D%3D, PID: 8592444
    • Schagger H (1995) Native electrophoresis for isolation of mitochondrial oxidative phosphorylation protein complexes. Methods Enzymol 260:190–202
    • (1995) Methods Enzymol , vol.260 , pp. 190-202
    • Schagger, H.1
  • 53
    • 9644268262 scopus 로고    scopus 로고
    • Molecular genetics of complex I-deficient Chinese hamster cell lines
    • COI: 1:CAS:528:DC%2BD2cXhtVCktb%2FN, PID: 15576048
    • Scheffler IE, Yadava N, Potluri P (2004) Molecular genetics of complex I-deficient Chinese hamster cell lines. Biochim Biophys Acta 1659:160–171
    • (2004) Biochim Biophys Acta , vol.1659 , pp. 160-171
    • Scheffler, I.E.1    Yadava, N.2    Potluri, P.3
  • 54
    • 0032483007 scopus 로고    scopus 로고
    • Molecular remedy of complex I defects: rotenone insensitive internal NADH-quinone oxidoreductase of Saccharomyces cerevisiae mitochondria restores NADH oxidase activity of complex I-deficient mammalian cells
    • COI: 1:CAS:528:DyaK1cXltlCmtLw%3D, PID: 9689052
    • Seo BB, Kitajima-Ihara T, Chan EKL, Scheffler IE, Matsuno-Yagi A, Yagi T (1998) Molecular remedy of complex I defects: rotenone insensitive internal NADH-quinone oxidoreductase of Saccharomyces cerevisiae mitochondria restores NADH oxidase activity of complex I-deficient mammalian cells. Proc Natl Acad Sci U S A 95:9167–9171
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 9167-9171
    • Seo, B.B.1    Kitajima-Ihara, T.2    Chan, E.K.L.3    Scheffler, I.E.4    Matsuno-Yagi, A.5    Yagi, T.6
  • 55
    • 84867522393 scopus 로고    scopus 로고
    • Heteroplasmy of mouse mtDNA is genetically unstable and results in altered behavior and cognition
    • COI: 1:CAS:528:DC%2BC38XhsV2qtLjK, PID: 23063123
    • Sharpley M, Marciniak C, Eckel-Mahan K et al (2012) Heteroplasmy of mouse mtDNA is genetically unstable and results in altered behavior and cognition. Cell 151:333–343
    • (2012) Cell , vol.151 , pp. 333-343
    • Sharpley, M.1    Marciniak, C.2    Eckel-Mahan, K.3
  • 56
    • 71949116823 scopus 로고    scopus 로고
    • Human ind1, an iron-sulfur cluster assembly factor for respiratory complex I
    • COI: 1:CAS:528:DC%2BD1MXhsValtLzM, PID: 19752196
    • Sheftel AD, Stehling O, Pierik AJ et al (2009) Human ind1, an iron-sulfur cluster assembly factor for respiratory complex I. Mol Cell Biol 29:6059–6073
    • (2009) Mol Cell Biol , vol.29 , pp. 6059-6073
    • Sheftel, A.D.1    Stehling, O.2    Pierik, A.J.3
  • 57
    • 77952472876 scopus 로고    scopus 로고
    • Iron-sulfur proteins in health and disease
    • COI: 1:CAS:528:DC%2BC3cXlsFaltbY%3D, PID: 20060739
    • Sheftel A, Stehling O, Lill R (2010) Iron-sulfur proteins in health and disease. Trends Endocrinol Metab 21(5):302–314
    • (2010) Trends Endocrinol Metab , vol.21 , Issue.5 , pp. 302-314
    • Sheftel, A.1    Stehling, O.2    Lill, R.3
  • 58
    • 33846032681 scopus 로고    scopus 로고
    • Mitochondrial DNA and the mammalian oocyte
    • COI: 1:CAS:528:DC%2BD2sXmt1Gltbo%3D, PID: 17222701
    • Shoubridge EA, Wai T (2007) Mitochondrial DNA and the mammalian oocyte. Curr Top Dev Biol 77:87–111
    • (2007) Curr Top Dev Biol , vol.77 , pp. 87-111
    • Shoubridge, E.A.1    Wai, T.2
  • 59
    • 39349108878 scopus 로고    scopus 로고
    • Sidestepping mutational meltdown
    • COI: 1:CAS:528:DC%2BD1cXisFamtbY%3D, PID: 18276880
    • Shoubridge EA, Wai T (2008) Sidestepping mutational meltdown. Science 319:914–915
    • (2008) Science , vol.319 , pp. 914-915
    • Shoubridge, E.A.1    Wai, T.2
  • 60
    • 0034687797 scopus 로고    scopus 로고
    • Maternal germ-line transmission of mutant mtDNAs from embryonic stem cell-derived chimeric mice
    • COI: 1:CAS:528:DC%2BD3MXitVCqsg%3D%3D, PID: 11106380
    • Sligh JE, Levy SE, Waymire KG et al (2000) Maternal germ-line transmission of mutant mtDNAs from embryonic stem cell-derived chimeric mice. Proc Natl Acad Sci U S A 97:14461–14466
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 14461-14466
    • Sligh, J.E.1    Levy, S.E.2    Waymire, K.G.3
  • 61
    • 0038380689 scopus 로고    scopus 로고
    • Mitochondrial disorders: clinical presentation and diagnostic dilemmas
    • COI: 1:CAS:528:DC%2BD3sXkvVCku7Y%3D, PID: 12889661
    • Smeitink JA (2003) Mitochondrial disorders: clinical presentation and diagnostic dilemmas. J Inherit Metab Dis 26:199–207
    • (2003) J Inherit Metab Dis , vol.26 , pp. 199-207
    • Smeitink, J.A.1
  • 63
    • 0017638189 scopus 로고
    • Mammalian cells with defective mitochondrial functions: a Chinese hamster mutant cell line lacking succinate dehydrogenase activity
    • COI: 1:CAS:528:DyaE2sXktVemtrg%3D, PID: 558831
    • Soderberg K, Ditta GS, Scheffler IE (1977) Mammalian cells with defective mitochondrial functions: a Chinese hamster mutant cell line lacking succinate dehydrogenase activity. Cell 10:697–702
    • (1977) Cell , vol.10 , pp. 697-702
    • Soderberg, K.1    Ditta, G.S.2    Scheffler, I.E.3
  • 64
    • 0018343079 scopus 로고
    • Respiration-deficient Chinese hamster cell mutants: genetic characterization
    • COI: 1:CAS:528:DyaE1MXhs1Gqu7o%3D, PID: 483122
    • Soderberg K, Mascarello JT, Breen GAM, Scheffler IE (1979) Respiration-deficient Chinese hamster cell mutants: genetic characterization. Somat Cell Genet 5:225–240
    • (1979) Somat Cell Genet , vol.5 , pp. 225-240
    • Soderberg, K.1    Mascarello, J.T.2    Breen, G.A.M.3    Scheffler, I.E.4
  • 65
    • 53049098744 scopus 로고    scopus 로고
    • Mutation of C20orf7 disrupts complex I assembly and causes lethal neonatal mitochondrial disease
    • COI: 1:CAS:528:DC%2BD1cXht1Omtb3I, PID: 18940309
    • Sugiana C, Pagliarini DJ, McKenzie M et al (2008) Mutation of C20orf7 disrupts complex I assembly and causes lethal neonatal mitochondrial disease. Am J Hum Genet 83:468–478
    • (2008) Am J Hum Genet , vol.83 , pp. 468-478
    • Sugiana, C.1    Pagliarini, D.J.2    McKenzie, M.3
  • 66
    • 79959218252 scopus 로고    scopus 로고
    • Respiratory chain complex I deficiency caused by mitochondrial DNA mutations
    • COI: 1:CAS:528:DC%2BC3MXnsFKqsrc%3D, PID: 21364701
    • Swalwell H, Kirby DM, Blakely EL et al (2011) Respiratory chain complex I deficiency caused by mitochondrial DNA mutations. Eur J Hum Genet 19:769–775
    • (2011) Eur J Hum Genet , vol.19 , pp. 769-775
    • Swalwell, H.1    Kirby, D.M.2    Blakely, E.L.3
  • 67
    • 10644244369 scopus 로고    scopus 로고
    • AIF deficiency compromises oxidative phosphorylation
    • COI: 1:CAS:528:DC%2BD2cXhtVWisr3N, PID: 15526035
    • Vahsen N, Cande C, Briere JJ et al (2004) AIF deficiency compromises oxidative phosphorylation. EMBO J 23:4679–4689
    • (2004) EMBO J , vol.23 , pp. 4679-4689
    • Vahsen, N.1    Cande, C.2    Briere, J.J.3
  • 68
    • 27144528747 scopus 로고    scopus 로고
    • Human mitochondrial complex I assembly is mediated by NDUFAF1
    • COI: 1:CAS:528:DC%2BD2MXhtFGqtbnK, PID: 16218961
    • Vogel RO, Janssen RJ, Ugalde C et al (2005) Human mitochondrial complex I assembly is mediated by NDUFAF1. FEBS J 272:5317–5326
    • (2005) FEBS J , vol.272 , pp. 5317-5326
    • Vogel, R.O.1    Janssen, R.J.2    Ugalde, C.3
  • 69
    • 33947129099 scopus 로고    scopus 로고
    • Cytosolic signaling protein Ecsit also localizes to mitochondria where it interacts with chaperone NDUFAF1 and functions in complex I assembly
    • COI: 1:CAS:528:DC%2BD2sXjsVSqtbY%3D, PID: 17344420
    • Vogel RO, Janssen RJ, van den Brand MA et al (2007) Cytosolic signaling protein Ecsit also localizes to mitochondria where it interacts with chaperone NDUFAF1 and functions in complex I assembly. Genes Dev 21:615–624
    • (2007) Genes Dev , vol.21 , pp. 615-624
    • Vogel, R.O.1    Janssen, R.J.2    van den Brand, M.A.3
  • 70
    • 56749180593 scopus 로고    scopus 로고
    • The mitochondrial DNA genetic bottleneck results from replication of a subpopulation of genomes
    • Wai T, Teoli D, Shoubridge EA (2010) The mitochondrial DNA genetic bottleneck results from replication of a subpopulation of genomes. Nat Genet 40:1484–1488
    • (2010) Nat Genet , vol.40 , pp. 1484-1488
    • Wai, T.1    Teoli, D.2    Shoubridge, E.A.3
  • 71
    • 0031205455 scopus 로고    scopus 로고
    • Mitochondrial DNA in aging and disease
    • COI: 1:STN:280:DyaK2szovVKjtA%3D%3D, PID: 9245840
    • Wallace DC (1997) Mitochondrial DNA in aging and disease. Sci Am 277:40–47
    • (1997) Sci Am , vol.277 , pp. 40-47
    • Wallace, D.C.1
  • 72
    • 0035234813 scopus 로고    scopus 로고
    • A mitochondrial paradigm for degenerative diseases and ageing
    • COI: 1:CAS:528:DC%2BD38Xlt1Oksbs%3D, PID: 11280029
    • Wallace DC (2001) A mitochondrial paradigm for degenerative diseases and ageing. Novartis Found Symp 235:247–263
    • (2001) Novartis Found Symp , vol.235 , pp. 247-263
    • Wallace, D.C.1
  • 73
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine
    • COI: 1:CAS:528:DC%2BD28Xlt1Wrtw%3D%3D, PID: 16285865
    • Wallace DC (2005) A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu Rev Genet 39:359–407
    • (2005) Annu Rev Genet , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 74
    • 0024242545 scopus 로고
    • Mitochondrial DNA mutation associated with Leber’s hereditary optic neuropathy
    • COI: 1:CAS:528:DyaL1MXntVentQ%3D%3D, PID: 3201231
    • Wallace DC, Singh G, Lott MT et al (1988a) Mitochondrial DNA mutation associated with Leber’s hereditary optic neuropathy. Science 242:1427–1431
    • (1988) Science , vol.242 , pp. 1427-1431
    • Wallace, D.C.1    Singh, G.2    Lott, M.T.3
  • 75
    • 0024163051 scopus 로고
    • Familial mitochondrial encephalomyopathy (MERRF): genetic, pathophysiological, and biochemical characterization of a mitochondrial DNA disease
    • COI: 1:CAS:528:DyaL1MXitFyrug%3D%3D, PID: 3180221
    • Wallace DC, Zheng X, Lott MT et al (1988b) Familial mitochondrial encephalomyopathy (MERRF): genetic, pathophysiological, and biochemical characterization of a mitochondrial DNA disease. Cell 55:601–610
    • (1988) Cell , vol.55 , pp. 601-610
    • Wallace, D.C.1    Zheng, X.2    Lott, M.T.3
  • 76
    • 77949882290 scopus 로고    scopus 로고
    • Mitochondrial energetics and therapeutics
    • COI: 1:CAS:528:DC%2BC3cXivFektL4%3D
    • Wallace DC, Fan W, Procaccio V (2010) Mitochondrial energetics and therapeutics. AnnuRev Pathol 5:297–348
    • (2010) AnnuRev Pathol , vol.5 , pp. 297-348
    • Wallace, D.C.1    Fan, W.2    Procaccio, V.3
  • 77
    • 9644260854 scopus 로고    scopus 로고
    • Import and orientation of the MWFE protein in mitochondrial NADH-ubiquinone oxidoreductase
    • COI: 1:CAS:528:DC%2BD2cXmt1Kjsrs%3D, PID: 16120368
    • Yadava N, Scheffler IE (2004) Import and orientation of the MWFE protein in mitochondrial NADH-ubiquinone oxidoreductase. Mitochondrion 4:1–12
    • (2004) Mitochondrion , vol.4
    • Yadava, N.1    Scheffler, I.E.2
  • 78
    • 1842582613 scopus 로고    scopus 로고
    • Development and characterization of a conditional mitochondrial complex I assembly system
    • COI: 1:CAS:528:DC%2BD2cXitl2gs7Y%3D, PID: 14722084
    • Yadava N, Houchens T, Potluri P, Scheffler IE (2004) Development and characterization of a conditional mitochondrial complex I assembly system. J Biol Chem 279:12406–12413
    • (2004) J Biol Chem , vol.279 , pp. 12406-12413
    • Yadava, N.1    Houchens, T.2    Potluri, P.3    Scheffler, I.E.4
  • 79
    • 39049110244 scopus 로고    scopus 로고
    • Investigations of the potential effects of phosphorylation of the MWFE and ESSS subunits on complex I activity and assembly
    • COI: 1:CAS:528:DC%2BD1cXitVent78%3D, PID: 17931954
    • Yadava N, Potluri P, Scheffler IE (2008) Investigations of the potential effects of phosphorylation of the MWFE and ESSS subunits on complex I activity and assembly. Int J Biochem Cell Biol 40:447–460
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 447-460
    • Yadava, N.1    Potluri, P.2    Scheffler, I.E.3
  • 80
    • 33744955549 scopus 로고    scopus 로고
    • Can a single subunit yeast NADH dehydrogenase (Ndi1) remedy diseases caused by respiratory complex I defects?
    • COI: 1:CAS:528:DC%2BD28Xks1ajt74%3D, PID: 16706641
    • Yagi T, Seo BB, Nakamaru-Ogiso E et al (2006) Can a single subunit yeast NADH dehydrogenase (Ndi1) remedy diseases caused by respiratory complex I defects? Rejuvenation Res 9:191–197
    • (2006) Rejuvenation Res , vol.9 , pp. 191-197
    • Yagi, T.1    Seo, B.B.2    Nakamaru-Ogiso, E.3
  • 81
    • 84860807146 scopus 로고    scopus 로고
    • Mitochondrial tRNA mutations associated with deafness
    • COI: 1:CAS:528:DC%2BC38XnsVCrt7w%3D, PID: 22538251
    • Zheng J, Ji Y, Guan MX (2012) Mitochondrial tRNA mutations associated with deafness. Mitochondrion 12:406–413
    • (2012) Mitochondrion , vol.12 , pp. 406-413
    • Zheng, J.1    Ji, Y.2    Guan, M.X.3


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