메뉴 건너뛰기




Volumn 13, Issue 2, 2014, Pages 135-143

Genetic variability of respiratory complex abundance, organization and activity in mouse brain

Author keywords

Brain; C57BL 6J; Complex I (NADH dehydrogenase); Complex III (cytochrome c reductase cytochrome bc1 complex); Complex IV (cytochrome c oxidase); DBA 2J; Genetic; Mitochondrial supercomplexes; Mouse; Respiratory chain

Indexed keywords

CYTOCHROME C OXIDASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUCCINATE DEHYDROGENASE (UBIQUINONE); UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 84892986978     PISSN: 16011848     EISSN: 1601183X     Source Type: Journal    
DOI: 10.1111/gbb.12101     Document Type: Article
Times cited : (13)

References (79)
  • 3
    • 81255210901 scopus 로고    scopus 로고
    • Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1
    • Althoff, T., Mills, D.J., Popot, J.L. & Kuhlbrandt, W. (2011) Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1. EMBO J 30, 4652-4664.
    • (2011) EMBO J , vol.30 , pp. 4652-4664
    • Althoff, T.1    Mills, D.J.2    Popot, J.L.3    Kuhlbrandt, W.4
  • 4
    • 63849247206 scopus 로고    scopus 로고
    • Redox sensitive signaling pathways in cardiac remodeling, hypertrophy and failure
    • Anilkumar, N., Sirker, A. & Shah, A.M. (2009) Redox sensitive signaling pathways in cardiac remodeling, hypertrophy and failure. Front Biosci 14, 3168-3187.
    • (2009) Front Biosci , vol.14 , pp. 3168-3187
    • Anilkumar, N.1    Sirker, A.2    Shah, A.M.3
  • 5
    • 84872081577 scopus 로고    scopus 로고
    • Cardiolipin-dependent reconstitution of respiratory supercomplexes from purified Saccharomyces cerevisiae complexes III and IV
    • Bazan, S., Mileykovskaya, E., Mallampalli, V.K., Heacock, P., Sparagna, G.C. & Dowhan, W. (2013) Cardiolipin-dependent reconstitution of respiratory supercomplexes from purified Saccharomyces cerevisiae complexes III and IV. J Biol Chem 288, 401-411.
    • (2013) J Biol Chem , vol.288 , pp. 401-411
    • Bazan, S.1    Mileykovskaya, E.2    Mallampalli, V.K.3    Heacock, P.4    Sparagna, G.C.5    Dowhan, W.6
  • 8
    • 44349165818 scopus 로고    scopus 로고
    • Shotgun lipidomics reveals the temporally dependent, highly diversified cardiolipin profile in the mammalian brain: temporally coordinated postnatal diversification of cardiolipin molecular species with neuronal remodeling
    • Cheng, H., Mancuso, D.J., Jiang, X., Guan, S., Yang, J., Yang, K., Sun, G., Gross, R.W. & Han, X. (2008) Shotgun lipidomics reveals the temporally dependent, highly diversified cardiolipin profile in the mammalian brain: temporally coordinated postnatal diversification of cardiolipin molecular species with neuronal remodeling. Biochemistry 47, 5869-5880.
    • (2008) Biochemistry , vol.47 , pp. 5869-5880
    • Cheng, H.1    Mancuso, D.J.2    Jiang, X.3    Guan, S.4    Yang, J.5    Yang, K.6    Sun, G.7    Gross, R.W.8    Han, X.9
  • 10
    • 0034674060 scopus 로고    scopus 로고
    • The cytochrome bc1 and cytochrome c oxidase complexes associate to form a single supracomplex in yeast mitochondria
    • Cruciat, C.M., Brunner, S., Baumann, F., Neupert, W. & Stuart, R.A. (2000) The cytochrome bc1 and cytochrome c oxidase complexes associate to form a single supracomplex in yeast mitochondria. J Biol Chem 275, 18093-18098.
    • (2000) J Biol Chem , vol.275 , pp. 18093-18098
    • Cruciat, C.M.1    Brunner, S.2    Baumann, F.3    Neupert, W.4    Stuart, R.A.5
  • 11
    • 33745242989 scopus 로고    scopus 로고
    • Respiratory chain supercomplexes set the threshold for respiration defects in human mtDNA mutant cybrids
    • D'Aurelio, M., Gajewski, C.D., Lenaz, G. & Manfredi, G. (2006) Respiratory chain supercomplexes set the threshold for respiration defects in human mtDNA mutant cybrids. Hum Mol Genet 15, 2157-2169.
    • (2006) Hum Mol Genet , vol.15 , pp. 2157-2169
    • D'Aurelio, M.1    Gajewski, C.D.2    Lenaz, G.3    Manfredi, G.4
  • 12
    • 47249097894 scopus 로고    scopus 로고
    • Molecular analyses and identification of promising candidate genes for loci on mouse chromosome 1 affecting alcohol physical dependence and associated withdrawal
    • Denmark, D.L. & Buck, K.J. (2008) Molecular analyses and identification of promising candidate genes for loci on mouse chromosome 1 affecting alcohol physical dependence and associated withdrawal. Genes Brain Behav 7, 599-608.
    • (2008) Genes Brain Behav , vol.7 , pp. 599-608
    • Denmark, D.L.1    Buck, K.J.2
  • 13
    • 33745478725 scopus 로고    scopus 로고
    • Cytochrome c oxidase is required for the assembly/stability of respiratory complex I in mouse fibroblasts
    • Diaz, F., Fukui, H., Garcia, S. & Moraes, C.T. (2006) Cytochrome c oxidase is required for the assembly/stability of respiratory complex I in mouse fibroblasts. Mol Cell Biol 26, 4872-4881.
    • (2006) Mol Cell Biol , vol.26 , pp. 4872-4881
    • Diaz, F.1    Fukui, H.2    Garcia, S.3    Moraes, C.T.4
  • 14
    • 75749152961 scopus 로고    scopus 로고
    • Evaluation of the mitochondrial respiratory chain and oxidative phosphorylation system using blue native gel electrophoresis
    • Chapter 19, Unit194
    • Diaz, F., Barrientos, A. & Fontanesi, F. (2009) Evaluation of the mitochondrial respiratory chain and oxidative phosphorylation system using blue native gel electrophoresis. Curr Protoc Hum Genet Chapter 19, Unit19.4.
    • (2009) Curr Protoc Hum Genet
    • Diaz, F.1    Barrientos, A.2    Fontanesi, F.3
  • 15
    • 84856787016 scopus 로고    scopus 로고
    • Cells lacking Rieske iron-sulfur protein have a reactive oxygen species-associated decrease in respiratory complexes I and IV
    • Diaz, F., Enriquez, J.A. & Moraes, C.T. (2012) Cells lacking Rieske iron-sulfur protein have a reactive oxygen species-associated decrease in respiratory complexes I and IV. Mol Cell Biol 32, 415-429.
    • (2012) Mol Cell Biol , vol.32 , pp. 415-429
    • Diaz, F.1    Enriquez, J.A.2    Moraes, C.T.3
  • 16
    • 67649814648 scopus 로고    scopus 로고
    • Heterogeneity of nervous system mitochondria: location, location, location!
    • Dubinsky, J.M. (2009) Heterogeneity of nervous system mitochondria: location, location, location!. Exp Neurol 218, 293-307.
    • (2009) Exp Neurol , vol.218 , pp. 293-307
    • Dubinsky, J.M.1
  • 17
    • 80053073046 scopus 로고    scopus 로고
    • Interaction of complexes I, III, and IV within the bovine respirasome by single particle cryoelectron tomography
    • Dudkina, N.V., Kudryashev, M., Stahlberg, H. & Boekema, E.J. (2011) Interaction of complexes I, III, and IV within the bovine respirasome by single particle cryoelectron tomography. Proc Natl Acad Sci U S A 108, 15196-15200.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 15196-15200
    • Dudkina, N.V.1    Kudryashev, M.2    Stahlberg, H.3    Boekema, E.J.4
  • 18
    • 33748377123 scopus 로고    scopus 로고
    • Central nervous system manifestations of mitochondrial disorders
    • Finsterer, J. (2006) Central nervous system manifestations of mitochondrial disorders. Acta Neurol Scand 114, 217-238.
    • (2006) Acta Neurol Scand , vol.114 , pp. 217-238
    • Finsterer, J.1
  • 19
    • 0038066355 scopus 로고    scopus 로고
    • Rapid reduction of ATP synthesis and lack of free radical formation by MPP+in rat brain synaptosomes and mitochondria
    • Fonck, C. & Baudry, M. (2003) Rapid reduction of ATP synthesis and lack of free radical formation by MPP+in rat brain synaptosomes and mitochondria. Brain Res 975, 214-221.
    • (2003) Brain Res , vol.975 , pp. 214-221
    • Fonck, C.1    Baudry, M.2
  • 20
    • 77953357281 scopus 로고    scopus 로고
    • Ageing alters the supramolecular architecture of OxPhos complexes in rat brain cortex
    • Frenzel, M., Rommelspacher, H., Sugawa, M.D. & Dencher, N.A. (2010) Ageing alters the supramolecular architecture of OxPhos complexes in rat brain cortex. Exp Gerontol 45, 563-572.
    • (2010) Exp Gerontol , vol.45 , pp. 563-572
    • Frenzel, M.1    Rommelspacher, H.2    Sugawa, M.D.3    Dencher, N.A.4
  • 21
    • 84855809495 scopus 로고    scopus 로고
    • Damage to mitochondrial complex I during cardiac ischemia reperfusion injury is reduced indirectly by anti-anginal drug ranolazine
    • Gadicherla, A.K., Stowe, D.F., Antholine, W.E., Yang, M. & Camara, A.K. (2012) Damage to mitochondrial complex I during cardiac ischemia reperfusion injury is reduced indirectly by anti-anginal drug ranolazine. Biochim Biophys Acta 1817, 419-429.
    • (2012) Biochim Biophys Acta , vol.1817 , pp. 419-429
    • Gadicherla, A.K.1    Stowe, D.F.2    Antholine, W.E.3    Yang, M.4    Camara, A.K.5
  • 23
    • 0030499311 scopus 로고    scopus 로고
    • The neurotoxin MPTP causes degeneration of specific nucleus A8, A9 and A10 dopaminergic neurons in the mouse
    • German, D.C., Nelson, E.L., Liang, C.L., Speciale, S.G., Sinton, C.M. & Sonsalla, P.K. (1996) The neurotoxin MPTP causes degeneration of specific nucleus A8, A9 and A10 dopaminergic neurons in the mouse. Neurodegeneration 5, 299-312.
    • (1996) Neurodegeneration , vol.5 , pp. 299-312
    • German, D.C.1    Nelson, E.L.2    Liang, C.L.3    Speciale, S.G.4    Sinton, C.M.5    Sonsalla, P.K.6
  • 24
    • 70349446460 scopus 로고    scopus 로고
    • Supercomplexes of the mitochondrial electron transport chain decline in the aging rat heart
    • Gomez, L.A., Monette, J.S., Chavez, J.D., Maier, C.S. & Hagen, T.M. (2009) Supercomplexes of the mitochondrial electron transport chain decline in the aging rat heart. Arch Biochem Biophys 490, 30-35.
    • (2009) Arch Biochem Biophys , vol.490 , pp. 30-35
    • Gomez, L.A.1    Monette, J.S.2    Chavez, J.D.3    Maier, C.S.4    Hagen, T.M.5
  • 25
    • 84856321622 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain: biochemical analysis and criterion for deficiency in diagnosis
    • Grazina, M.M. (2012) Mitochondrial respiratory chain: biochemical analysis and criterion for deficiency in diagnosis. Methods Mol Biol 837, 73-91.
    • (2012) Methods Mol Biol , vol.837 , pp. 73-91
    • Grazina, M.M.1
  • 26
    • 0033562891 scopus 로고    scopus 로고
    • Differential strain susceptibility following 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) administration acts in an autosomal dominant fashion: quantitative analysis in seven strains of Mus musculus
    • Hamre, K., Tharp, R., Poon, K., Xiong, X. & Smeyne, R.J. (1999) Differential strain susceptibility following 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine (MPTP) administration acts in an autosomal dominant fashion: quantitative analysis in seven strains of Mus musculus. Brain Res 828, 91-103.
    • (1999) Brain Res , vol.828 , pp. 91-103
    • Hamre, K.1    Tharp, R.2    Poon, K.3    Xiong, X.4    Smeyne, R.J.5
  • 32
    • 0034669552 scopus 로고    scopus 로고
    • Measuring the quantity and activity of mitochondrial electron transport chain complexes in tissues of central nervous system using blue native polyacrylamide gel electrophoresis
    • Jung, C., Higgins, C.M. & Xu, Z. (2000) Measuring the quantity and activity of mitochondrial electron transport chain complexes in tissues of central nervous system using blue native polyacrylamide gel electrophoresis. Anal Biochem 286, 214-223.
    • (2000) Anal Biochem , vol.286 , pp. 214-223
    • Jung, C.1    Higgins, C.M.2    Xu, Z.3
  • 33
    • 80052851950 scopus 로고    scopus 로고
    • Mouse genomic variation and its effect on phenotypes and gene regulation
    • Keane, T.M., Goodstadt, L., Danecek, P. et al. (2011) Mouse genomic variation and its effect on phenotypes and gene regulation. Nature 477, 289-294.
    • (2011) Nature , vol.477 , pp. 289-294
    • Keane, T.M.1    Goodstadt, L.2    Danecek, P.3
  • 34
    • 0021247811 scopus 로고
    • Ethanol sensitivity and membrane lipid composition in three strains of mouse
    • La Droitte, P., Lamboeuf, Y. & de Saint Blanquat, G. (1984) Ethanol sensitivity and membrane lipid composition in three strains of mouse. Comp Biochem Physiol C 77, 351-356.
    • (1984) Comp Biochem Physiol C , vol.77 , pp. 351-356
    • La Droitte, P.1    Lamboeuf, Y.2    de Saint Blanquat, G.3
  • 36
    • 84856353116 scopus 로고    scopus 로고
    • Blue native polyacrylamide gel electrophoresis: a powerful diagnostic tool for the detection of assembly defects in the enzyme complexes of oxidative phosphorylation
    • Leary, S.C. (2012) Blue native polyacrylamide gel electrophoresis: a powerful diagnostic tool for the detection of assembly defects in the enzyme complexes of oxidative phosphorylation. Methods Mol Biol 837, 195-206.
    • (2012) Methods Mol Biol , vol.837 , pp. 195-206
    • Leary, S.C.1
  • 37
    • 68949107623 scopus 로고    scopus 로고
    • Structural and functional organization of the mitochondrial respiratory chain: a dynamic super-assembly
    • Lenaz, G. & Genova, M.L. (2009) Structural and functional organization of the mitochondrial respiratory chain: a dynamic super-assembly. Int J Biochem Cell Biol 41, 1750-1772.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 1750-1772
    • Lenaz, G.1    Genova, M.L.2
  • 38
    • 84863754137 scopus 로고    scopus 로고
    • Supramolecular organisation of the mitochondrial respiratory chain: a new challenge for the mechanism and control of oxidative phosphorylation
    • Lenaz, G. & Genova, M.L. (2012) Supramolecular organisation of the mitochondrial respiratory chain: a new challenge for the mechanism and control of oxidative phosphorylation. Adv Exp Med Biol 748, 107-144.
    • (2012) Adv Exp Med Biol , vol.748 , pp. 107-144
    • Lenaz, G.1    Genova, M.L.2
  • 39
    • 67349251869 scopus 로고    scopus 로고
    • Maintaining the brain: insight into human neurodegeneration from Drosophila melanogaster mutants
    • Lessing, D. & Bonini, N.M. (2009) Maintaining the brain: insight into human neurodegeneration from Drosophila melanogaster mutants. Nat Rev Genet 10, 359-370.
    • (2009) Nat Rev Genet , vol.10 , pp. 359-370
    • Lessing, D.1    Bonini, N.M.2
  • 41
    • 84886246212 scopus 로고    scopus 로고
    • Mitochondrial respiratory supercomplex association limits production of reactive oxygen species from complex I
    • Maranzana, E., Barbero, G., Falasca, A.I., Lenaz, G. & Genova, M.L. (2013) Mitochondrial respiratory supercomplex association limits production of reactive oxygen species from complex I. Antioxid Redox Signal 19, 1469-1480.
    • (2013) Antioxid Redox Signal , vol.19 , pp. 1469-1480
    • Maranzana, E.1    Barbero, G.2    Falasca, A.I.3    Lenaz, G.4    Genova, M.L.5
  • 42
    • 33746327466 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain supercomplexes are destabilized in Barth Syndrome patients
    • McKenzie, M., Lazarou, M., Thorburn, D.R. & Ryan, M.T. (2006) Mitochondrial respiratory chain supercomplexes are destabilized in Barth Syndrome patients. J Mol Biol 361, 462-469.
    • (2006) J Mol Biol , vol.361 , pp. 462-469
    • McKenzie, M.1    Lazarou, M.2    Thorburn, D.R.3    Ryan, M.T.4
  • 43
    • 57849102015 scopus 로고    scopus 로고
    • Inbred C57BL/6J and DBA/2J mouse strains exhibit constitutive differences in regional brain fatty acid composition
    • McNamara, R.K., Able, J., Jandacek, R., Rider, T. & Tso, P. (2009) Inbred C57BL/6J and DBA/2J mouse strains exhibit constitutive differences in regional brain fatty acid composition. Lipids 44, 1-8.
    • (2009) Lipids , vol.44 , pp. 1-8
    • McNamara, R.K.1    Able, J.2    Jandacek, R.3    Rider, T.4    Tso, P.5
  • 44
    • 70349523247 scopus 로고    scopus 로고
    • Cardiolipin membrane domains in prokaryotes and eukaryotes
    • Mileykovskaya, E. & Dowhan, W. (2009) Cardiolipin membrane domains in prokaryotes and eukaryotes. Biochim Biophys Acta 1788, 2084-2091.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 2084-2091
    • Mileykovskaya, E.1    Dowhan, W.2
  • 47
    • 0036053197 scopus 로고    scopus 로고
    • Dopamine efflux by MPTP and hydroxyl radical generation
    • Obata, T. (2002) Dopamine efflux by MPTP and hydroxyl radical generation. J Neural Transm 109, 1159-1180.
    • (2002) J Neural Transm , vol.109 , pp. 1159-1180
    • Obata, T.1
  • 48
    • 0036182026 scopus 로고    scopus 로고
    • Mitochondrial involvement in Parkinson's disease
    • Orth, M. & Schapira, A.H. (2002) Mitochondrial involvement in Parkinson's disease. Neurochem Int 40, 533-541.
    • (2002) Neurochem Int , vol.40 , pp. 533-541
    • Orth, M.1    Schapira, A.H.2
  • 49
    • 44349150953 scopus 로고    scopus 로고
    • Mitochondrial membrane potential in human neutrophils is maintained by complex III activity in the absence of supercomplex organisation
    • van Raam, B.J., Sluiter, W., de Wit, E., Roos, D., Verhoeven, A.J. & Kuijpers, T.W. (2008) Mitochondrial membrane potential in human neutrophils is maintained by complex III activity in the absence of supercomplex organisation. PLoS One 3, e2013.
    • (2008) PLoS One , vol.3
    • van Raam, B.J.1    Sluiter, W.2    de Wit, E.3    Roos, D.4    Verhoeven, A.J.5    Kuijpers, T.W.6
  • 51
    • 84857116578 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
    • Ray, P.D., Huang, B.W. & Tsuji, Y. (2012) Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling. Cell Signal 24, 981-990.
    • (2012) Cell Signal , vol.24 , pp. 981-990
    • Ray, P.D.1    Huang, B.W.2    Tsuji, Y.3
  • 52
    • 33845197506 scopus 로고    scopus 로고
    • Effects of age and caloric intake on glutathione redox state in different brain regions of C57BL/6 and DBA/2 mice
    • Rebrin, I., Forster, M.J. & Sohal, R.S. (2007) Effects of age and caloric intake on glutathione redox state in different brain regions of C57BL/6 and DBA/2 mice. Brain Res 1127, 10-18.
    • (2007) Brain Res , vol.1127 , pp. 10-18
    • Rebrin, I.1    Forster, M.J.2    Sohal, R.S.3
  • 53
    • 79957967864 scopus 로고    scopus 로고
    • Association between life-span extension by caloric restriction and thiol redox state in two different strains of mice
    • Rebrin, I., Forster, M.J. & Sohal, R.S. (2011) Association between life-span extension by caloric restriction and thiol redox state in two different strains of mice. Free Radic Biol Med 51, 225-233.
    • (2011) Free Radic Biol Med , vol.51 , pp. 225-233
    • Rebrin, I.1    Forster, M.J.2    Sohal, R.S.3
  • 54
    • 33646586344 scopus 로고    scopus 로고
    • Defining the mitochondrial proteomes from five rat organs in a physiologically significant context using 2D blue-native/SDS-PAGE
    • Reifschneider, N.H., Goto, S., Nakamoto, H., Takahashi, R., Sugawa, M., Dencher, N.A. & Krause, F. (2006) Defining the mitochondrial proteomes from five rat organs in a physiologically significant context using 2D blue-native/SDS-PAGE. J Proteome Res 5, 1117-1132.
    • (2006) J Proteome Res , vol.5 , pp. 1117-1132
    • Reifschneider, N.H.1    Goto, S.2    Nakamoto, H.3    Takahashi, R.4    Sugawa, M.5    Dencher, N.A.6    Krause, F.7
  • 56
    • 33644839474 scopus 로고    scopus 로고
    • Histochemical staining and quantification of plant mitochondrial respiratory chain complexes using blue-native polyacrylamide gel electrophoresis
    • Sabar, M., Balk, J. & Leaver, C.J. (2005) Histochemical staining and quantification of plant mitochondrial respiratory chain complexes using blue-native polyacrylamide gel electrophoresis. Plant J 44, 893-901.
    • (2005) Plant J , vol.44 , pp. 893-901
    • Sabar, M.1    Balk, J.2    Leaver, C.J.3
  • 59
    • 0035222647 scopus 로고    scopus 로고
    • Blue-native gels to isolate protein complexes from mitochondria
    • Schagger, H. (2001) Blue-native gels to isolate protein complexes from mitochondria. Methods Cell Biol 65, 231-244.
    • (2001) Methods Cell Biol , vol.65 , pp. 231-244
    • Schagger, H.1
  • 60
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schagger, H. & Pfeiffer, K. (2000) Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J 19, 1777-1783.
    • (2000) EMBO J , vol.19 , pp. 1777-1783
    • Schagger, H.1    Pfeiffer, K.2
  • 61
    • 0035851099 scopus 로고    scopus 로고
    • The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes
    • Schagger, H. & Pfeiffer, K. (2001) The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes. J Biol Chem 276, 37861-37867.
    • (2001) J Biol Chem , vol.276 , pp. 37861-37867
    • Schagger, H.1    Pfeiffer, K.2
  • 62
    • 4344630010 scopus 로고    scopus 로고
    • Significance of respirasomes for the assembly/stability of human respiratory chain complex I
    • Schagger, H., de Coo, R., Bauer, M.F., Hofmann, S., Godinot, C. & Brandt, U. (2004) Significance of respirasomes for the assembly/stability of human respiratory chain complex I. J Biol Chem 279, 36349-36353.
    • (2004) J Biol Chem , vol.279 , pp. 36349-36353
    • Schagger, H.1    de Coo, R.2    Bauer, M.F.3    Hofmann, S.4    Godinot, C.5    Brandt, U.6
  • 63
    • 0029743756 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial dysfunction in neurodegeneration
    • Schapira, A.H. (1996) Oxidative stress and mitochondrial dysfunction in neurodegeneration. Curr Opin Neurol 9, 260-264.
    • (1996) Curr Opin Neurol , vol.9 , pp. 260-264
    • Schapira, A.H.1
  • 64
    • 0025128703 scopus 로고
    • Relationship between lipid saturation and lipid-protein interaction in liver mitochondria modified by catalytic hydrogenation with reference to cardiolipin molecular species
    • Schlame, M., Horvath, L. & Vigh, L. (1990) Relationship between lipid saturation and lipid-protein interaction in liver mitochondria modified by catalytic hydrogenation with reference to cardiolipin molecular species. Biochem J 265, 79-85.
    • (1990) Biochem J , vol.265 , pp. 79-85
    • Schlame, M.1    Horvath, L.2    Vigh, L.3
  • 66
    • 0033751421 scopus 로고    scopus 로고
    • Metabolic, metallic, and mitotic sources of oxidative stress in Alzheimer disease
    • Smith, M.A., Nunomura, A., Zhu, X., Takeda, A. & Perry, G. (2000) Metabolic, metallic, and mitotic sources of oxidative stress in Alzheimer disease. Antioxid Redox Signal 2, 413-420.
    • (2000) Antioxid Redox Signal , vol.2 , pp. 413-420
    • Smith, M.A.1    Nunomura, A.2    Zhu, X.3    Takeda, A.4    Perry, G.5
  • 67
    • 82755189501 scopus 로고    scopus 로고
    • Optimization of respiratory chain enzymatic assays in muscle for the diagnosis of mitochondrial disorders
    • Spinazzi, M., Casarin, A., Pertegato, V., Ermani, M., Salviati, L. & Angelini, C. (2011) Optimization of respiratory chain enzymatic assays in muscle for the diagnosis of mitochondrial disorders. Mitochondrion 11, 893-904.
    • (2011) Mitochondrion , vol.11 , pp. 893-904
    • Spinazzi, M.1    Casarin, A.2    Pertegato, V.3    Ermani, M.4    Salviati, L.5    Angelini, C.6
  • 68
    • 1042278126 scopus 로고    scopus 로고
    • Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans
    • Stroh, A., Anderka, O., Pfeiffer, K., Yagi, T., Finel, M., Ludwig, B. & Schagger, H. (2004) Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans. J Biol Chem 279, 5000-5007.
    • (2004) J Biol Chem , vol.279 , pp. 5000-5007
    • Stroh, A.1    Anderka, O.2    Pfeiffer, K.3    Yagi, T.4    Finel, M.5    Ludwig, B.6    Schagger, H.7
  • 69
    • 57049106773 scopus 로고    scopus 로고
    • Supercomplex organization of the oxidative phosphorylation enzymes in yeast mitochondria
    • Stuart, R.A. (2008) Supercomplex organization of the oxidative phosphorylation enzymes in yeast mitochondria. J Bioenerg Biomembr 40, 411-417.
    • (2008) J Bioenerg Biomembr , vol.40 , pp. 411-417
    • Stuart, R.A.1
  • 70
    • 78650339863 scopus 로고    scopus 로고
    • Mutations in mitochondrial complex III uniquely affect complex I in Caenorhabditis elegans
    • Suthammarak, W., Morgan, P.G. & Sedensky, M.M. (2010) Mutations in mitochondrial complex III uniquely affect complex I in Caenorhabditis elegans. J Biol Chem 285, 40724-40731.
    • (2010) J Biol Chem , vol.285 , pp. 40724-40731
    • Suthammarak, W.1    Morgan, P.G.2    Sedensky, M.M.3
  • 71
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace, D.C. (1999) Mitochondrial diseases in man and mouse. Science 283, 1482-1488.
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 72
    • 84864024064 scopus 로고    scopus 로고
    • Sealing the mitochondrial respirasome
    • Winge, D.R. (2012) Sealing the mitochondrial respirasome. Mol Cell Biol 32, 2647-2652.
    • (2012) Mol Cell Biol , vol.32 , pp. 2647-2652
    • Winge, D.R.1
  • 73
    • 28444497467 scopus 로고    scopus 로고
    • Advantages and limitations of clear-native PAGE
    • Wittig, I. & Schagger, H. (2005) Advantages and limitations of clear-native PAGE. Proteomics 5, 4338-4346.
    • (2005) Proteomics , vol.5 , pp. 4338-4346
    • Wittig, I.1    Schagger, H.2
  • 74
    • 34147218109 scopus 로고    scopus 로고
    • Electrophoretic methods to isolate protein complexes from mitochondria
    • Wittig, I. & Schagger, H. (2007) Electrophoretic methods to isolate protein complexes from mitochondria. Methods Cell Biol 80, 723-741.
    • (2007) Methods Cell Biol , vol.80 , pp. 723-741
    • Wittig, I.1    Schagger, H.2
  • 75
    • 67349200007 scopus 로고    scopus 로고
    • Supramolecular organization of ATP synthase and respiratory chain in mitochondrial membranes
    • Wittig, I. & Schagger, H. (2009) Supramolecular organization of ATP synthase and respiratory chain in mitochondrial membranes. Biochim Biophys Acta 1787, 672-680.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 672-680
    • Wittig, I.1    Schagger, H.2
  • 77
    • 36348941768 scopus 로고    scopus 로고
    • Functional assays in high-resolution clear native gels to quantify mitochondrial complexes in human biopsies and cell lines
    • Wittig, I., Carrozzo, R., Santorelli, F.M. & Schagger, H. (2007) Functional assays in high-resolution clear native gels to quantify mitochondrial complexes in human biopsies and cell lines. Electrophoresis 28, 3811-3820.
    • (2007) Electrophoresis , vol.28 , pp. 3811-3820
    • Wittig, I.1    Carrozzo, R.2    Santorelli, F.M.3    Schagger, H.4
  • 79


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.