메뉴 건너뛰기




Volumn 52, Issue 2, 2012, Pages 402-409

Disruption of alternative NAD(P)H dehydrogenases leads to decreased mitochondrial ROS in Neurospora crassa

Author keywords

Free radicals; Mitochondria; NAD(P)H dehydrogenase; Neurospora crassa; Paraquat; Reactive oxygen species; Respiratory mutant

Indexed keywords

OXIDOREDUCTASE; PARAQUAT; REACTIVE OXYGEN METABOLITE; SCAVENGER;

EID: 84855438617     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2011.10.492     Document Type: Article
Times cited : (12)

References (60)
  • 1
    • 0037056054 scopus 로고    scopus 로고
    • From NADH to ubiquinone in Neurospora mitochondria
    • DOI 10.1016/S0005-2728(02)00276-1, PII S0005272802002761
    • A. Videira, and M. Duarte From NADH to ubiquinone in Neurospora mitochondria Biochim. Biophys. Acta 1555 2002 187 191 (Pubitemid 35246026)
    • (2002) Biochimica et Biophysica Acta - Bioenergetics , vol.1555 , Issue.1-3 , pp. 187-191
    • Videira, A.1    Duarte, M.2
  • 3
    • 37249058385 scopus 로고    scopus 로고
    • The multiplicity of dehydrogenases in the electron transport chain of plant mitochondria
    • DOI 10.1016/j.mito.2007.10.004, PII S1567724907002504, Unique Aspects of Plant Motichondria
    • A.G. Rasmusson, D.A. Geisler, and I.M. Moller The multiplicity of dehydrogenases in the electron transport chain of plant mitochondria Mitochondrion 8 2008 47 60 (Pubitemid 350263739)
    • (2008) Mitochondrion , vol.8 , Issue.1 , pp. 47-60
    • Rasmusson, A.G.1    Geisler, D.A.2    Moller, I.M.3
  • 4
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • M.P. Murphy How mitochondria produce reactive oxygen species Biochem. J. 417 2009 1 13
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 6
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • M.L. Circu, and T.Y. Aw Reactive oxygen species, cellular redox systems, and apoptosis Free Radic. Biol. Med. 48 2010 749 762
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 7
    • 0029979744 scopus 로고    scopus 로고
    • Oxidants as stimulators of signal transduction
    • DOI 10.1016/S0891-5849(96)00275-4
    • Y.J. Suzuki, H.J. Forman, and A. Sevanian Oxidants as stimulators of signal transduction Free Radic. Biol. Med. 22 1997 269 285 (Pubitemid 26399334)
    • (1996) Free Radical Biology and Medicine , vol.22 , Issue.1-2 , pp. 269-285
    • Suzuki, Y.J.1    Forman, H.J.2    Sevanian, A.3
  • 8
    • 34548048824 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin-2/peroxiredoxin-3 system functions in parallel with mitochondrial GSH system in protection against oxidative stress
    • DOI 10.1016/j.abb.2007.05.001, PII S0003986107002421
    • H. Zhang, Y.M. Go, and D.P. Jones Mitochondrial thioredoxin-2/ peroxiredoxin-3 system functions in parallel with mitochondrial GSH system in protection against oxidative stress Arch. Biochem. Biophys. 465 2007 119 126 (Pubitemid 47283985)
    • (2007) Archives of Biochemistry and Biophysics , vol.465 , Issue.1 , pp. 119-126
    • Zhang, H.1    Go, Y.-M.2    Jones, D.P.3
  • 9
    • 77956250065 scopus 로고    scopus 로고
    • 2 removal in brain mitochondria via the thioredoxin/peroxiredoxin system
    • 2 removal in brain mitochondria via the thioredoxin/peroxiredoxin system J. Biol. Chem. 285 2010 27850 27858
    • (2010) J. Biol. Chem. , vol.285 , pp. 27850-27858
    • Drechsel, D.A.1    Patel, M.2
  • 11
    • 37849001800 scopus 로고    scopus 로고
    • Characterization of the transcriptional profile in primary astrocytes after oxidative stress induced by paraquat
    • B.T. Olesen, J. Clausen, and O. Vang Characterization of the transcriptional profile in primary astrocytes after oxidative stress induced by paraquat Neurotoxicology 29 2008 13 21
    • (2008) Neurotoxicology , vol.29 , pp. 13-21
    • Olesen, B.T.1    Clausen, J.2    Vang, O.3
  • 12
    • 77951432631 scopus 로고    scopus 로고
    • The causes of cancer revisited: "mitochondrial malignancy" and ROS-induced oncogenic transformation-why mitochondria are targets for cancer therapy
    • S.J. Ralph, S. Rodríguez-Enríquez, J. Neuzil, E. Saavedra, and R. Moreno-Sánchez The causes of cancer revisited: "mitochondrial malignancy" and ROS-induced oncogenic transformation-why mitochondria are targets for cancer therapy Mol. Aspects Med. 31 2010 145 170
    • (2010) Mol. Aspects Med. , vol.31 , pp. 145-170
    • Ralph, S.J.1    Rodríguez-Enríquez, S.2    Neuzil, J.3    Saavedra, E.4    Moreno-Sánchez, R.5
  • 13
    • 0025309791 scopus 로고
    • Mitochondrial mutations may increase oxidative stress: Implications for carcinogenesis and aging?
    • DOI 10.1016/0891-5849(90)90152-9
    • B. Bandy, and A.J. Davison Mitochondrial mutations may increase oxidative stress: implications for carcinogenesis and aging? Free Radic. Biol. Med. 8 1990 523 539 (Pubitemid 20204417)
    • (1990) Free Radical Biology and Medicine , vol.8 , Issue.6 , pp. 523-539
    • Bandy, B.1    Davison, A.J.2
  • 14
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants and aging
    • R.S. Balaban, S. Nemoto, and T. Finkel Mitochondria, oxidants and aging Cell 120 2005 483 495
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 15
    • 79952712223 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species drive proinflammatory cytokine production
    • E. Naik, and V.M. Dixit Mitochondrial reactive oxygen species drive proinflammatory cytokine production J. Exp. Med. 208 2011 417 420
    • (2011) J. Exp. Med. , vol.208 , pp. 417-420
    • Naik, E.1    Dixit, V.M.2
  • 16
    • 33751072935 scopus 로고    scopus 로고
    • Bioenergetics and the formation of mitochondrial reactive oxygen species
    • DOI 10.1016/j.tips.2006.10.005, PII S0165614706002495
    • V. Adam-Vizi, and C. Chinopoulos Bioenergetics and the formation of mitochondrial reactive oxygen species Trends Pharmacol. Sci. 27 2006 639 645 (Pubitemid 44767940)
    • (2006) Trends in Pharmacological Sciences , vol.27 , Issue.12 , pp. 639-645
    • Adam-Vizi, V.1    Chinopoulos, C.2
  • 18
    • 24144464489 scopus 로고    scopus 로고
    • Production of reactive oxygen species in brain mitochondria: Contribution by electron transport chain and non-electron transport chain sources
    • DOI 10.1089/ars.2005.7.1140
    • V. Adam-Vizi Production of reactive oxygen species in brain mitochondria: contribution by electron transport chain and non-electron transport chain sources Antioxid. Redox Signal. 7 2005 1140 1149 (Pubitemid 41232509)
    • (2005) Antioxidants and Redox Signaling , vol.7 , Issue.9-10 , pp. 1140-1149
    • Adam-Vizi, V.1
  • 19
    • 42749087763 scopus 로고    scopus 로고
    • The mitochondrial impairment, oxidative stress and neurodegeneration connection: Reality or just an attractive hypothesis?
    • H. Fukui, and C.T. Moraes The mitochondrial impairment, oxidative stress and neurodegeneration connection: reality or just an attractive hypothesis? Trends Neurosci. 31 2008 251 256
    • (2008) Trends Neurosci. , vol.31 , pp. 251-256
    • Fukui, H.1    Moraes, C.T.2
  • 20
    • 4544354262 scopus 로고    scopus 로고
    • Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • DOI 10.1074/jbc.M406576200
    • A.J. Lambert, and M.D. Brand Inhibitors of the quinine binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I) J. Biol. Chem. 279 2004 39414 39420 (Pubitemid 39258206)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.38 , pp. 39414-39420
    • Lambert, A.J.1    Brand, M.D.2
  • 21
    • 53849099653 scopus 로고    scopus 로고
    • The production of reactive oxygen species by complex i
    • J. Hirst, M.S. King, and K.R. Pryde The production of reactive oxygen species by complex I Biochem. Soc. Trans. 36 2008 976 980
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 976-980
    • Hirst, J.1    King, M.S.2    Pryde, K.R.3
  • 22
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria: Central role of complex III
    • DOI 10.1074/jbc.M304854200
    • Q. Chen, E.J. Vazquez, S. Moghaddas, C.L. Hoppel, and E.J. Lesnefsky Production of reactive oxygen species by mitochondria: central role of complex III J. Biol. Chem. 278 2003 36027 36031 (Pubitemid 37139922)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.38 , pp. 36027-36031
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 23
    • 52049104467 scopus 로고    scopus 로고
    • The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex
    • S. Dröse, and U. Brandt The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex J. Biol. Chem. 283 2008 21649 21654
    • (2008) J. Biol. Chem. , vol.283 , pp. 21649-21654
    • Dröse, S.1    Brandt, U.2
  • 25
    • 33750503465 scopus 로고    scopus 로고
    • The single subunit NADH dehydrogenase reduces generation of reactive oxygen species from complex I
    • DOI 10.1016/j.febslet.2006.10.008, PII S0014579306012087
    • B.B. Seo, M. Marella, T. Yagi, and A. Matsuno-Yagi The single subunit NADH dehydrogenase reduces generation of reactive oxygen species from complex I FEBS Lett. 580 2006 6105 6108 (Pubitemid 44666792)
    • (2006) FEBS Letters , vol.580 , Issue.26 , pp. 6105-6108
    • Seo, B.B.1    Marella, M.2    Yagi, T.3    Matsuno-Yagi, A.4
  • 27
    • 77953247010 scopus 로고    scopus 로고
    • Neuronal expression of a single-subunit yeast NADH-ubiquinone oxidoreductase (Ndi1) extends Drosophila lifespan
    • S. Bahadorani, J. Cho, T. Lo, H. Contreras, H.O. Lawal, D.E. Krantz, T.J. Bradley, and D.W. Walker Neuronal expression of a single-subunit yeast NADH-ubiquinone oxidoreductase (Ndi1) extends Drosophila lifespan Aging Cell 9 2010 191 202
    • (2010) Aging Cell , vol.9 , pp. 191-202
    • Bahadorani, S.1    Cho, J.2    Lo, T.3    Contreras, H.4    Lawal, H.O.5    Krantz, D.E.6    Bradley, T.J.7    Walker, D.W.8
  • 28
    • 0037441390 scopus 로고    scopus 로고
    • External alternative NADH dehydrogenase of Saccharomyces cerevisiae: A potential source of superoxide
    • DOI 10.1016/S0891-5849(02)01328-X
    • J. Fang, and D.S. Beattie External alternative NADH dehydrogenase of Saccharomyces cerevisiae: a potential source of superoxide Free Radic. Biol. Med. 34 2003 478 488 (Pubitemid 36140172)
    • (2003) Free Radical Biology and Medicine , vol.34 , Issue.4 , pp. 478-488
    • Fang, J.1    Beattie, D.S.2
  • 29
    • 63449114787 scopus 로고    scopus 로고
    • Paraquat-induced production of reactive oxygen species in brain mitochondria
    • D.A. Drechsel, and M. Patel Paraquat-induced production of reactive oxygen species in brain mitochondria Methods Enzymol. 456 2009 381 393
    • (2009) Methods Enzymol. , vol.456 , pp. 381-393
    • Drechsel, D.A.1    Patel, M.2
  • 30
    • 38349105900 scopus 로고    scopus 로고
    • Complex i is the major site of mitochondrial superoxide production by paraquat
    • H.M. Cochemé, and M.P. Murphy Complex I is the major site of mitochondrial superoxide production by paraquat J. Biol. Chem. 283 2008 1786 1798
    • (2008) J. Biol. Chem. , vol.283 , pp. 1786-1798
    • Cochemé, H.M.1    Murphy, M.P.2
  • 31
    • 0032791402 scopus 로고    scopus 로고
    • Primary structure and characterisation of a 64 kDa NADH dehydrogenase from the inner membrane of Neurospora crassa mitochondria
    • DOI 10.1016/S0005-2728(99)00072-9, PII S0005272899000729
    • A.M. Melo, M. Duarte, and A. Videira Primary structure and characterisation of a 64 kDa NADH dehydrogenase from the inner membrane of Neurospora crassa mitochondria Biochim. Biophys. Acta 1412 1999 282 287 (Pubitemid 29356108)
    • (1999) Biochimica et Biophysica Acta - Bioenergetics , vol.1412 , Issue.3 , pp. 282-287
    • Melo, A.M.P.1    Duarte, M.2    Videira, A.3
  • 32
    • 0038245247 scopus 로고    scopus 로고
    • The internal alternative NADH dehydrogenase of Neurospora crassa mitochondria
    • DOI 10.1042/BJ20021374
    • M. Duarte, M. Peters, U. Schulte, and A. Videira The internal alternative NADH dehydrogenase of Neurospora crassa mitochondria Biochem. J. 37 2003 1005 1011 (Pubitemid 36578900)
    • (2003) Biochemical Journal , vol.371 , Issue.3 , pp. 1005-1011
    • Duarte, M.1    Peters, M.2    Schulte, U.3    Videira, A.4
  • 33
    • 1642533556 scopus 로고    scopus 로고
    • The main external alternative NAD(P)H dehydrogenase of Neurospora crassa mitochondria
    • DOI 10.1016/j.bbabio.2003.10.004
    • P. Carneiro, M. Duarte, and A. Videira The main external alternative NAD(P)H dehydrogenase of Neurospora crassa mitochondria Biochim. Biophys. Acta 1608 2004 45 52 (Pubitemid 38115118)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1608 , Issue.1 , pp. 45-52
    • Carneiro, P.1    Duarte, M.2    Videira, A.3
  • 34
    • 34147171430 scopus 로고    scopus 로고
    • The External Alternative NAD(P)H Dehydrogenase NDE3 Is Localized both in the Mitochondria and in the Cytoplasm of Neurospora crassa
    • DOI 10.1016/j.jmb.2007.02.080, PII S0022283607002859
    • P. Carneiro, M. Duarte, and A. Videira The external alternative NAD(P)H dehydrogenase NDE3 is localized both in the mitochondria and in the cytoplasm of Neurospora crassa J. Mol. Biol. 368 2007 1114 1121 (Pubitemid 46574668)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.4 , pp. 1114-1121
    • Carneiro, P.1    Duarte, M.2    Videira, A.3
  • 36
    • 0041472360 scopus 로고    scopus 로고
    • The Fungal Genetics Stock Center: From molds to molecules
    • DOI 10.1016/S0065-2164(03)01010-4
    • K. McCluskey The Fungal Genetics Stock Center: from molds to molecules Adv. Appl. Microbiol. 52 2003 245 262 (Pubitemid 37012800)
    • (2003) Advances in Applied Microbiology , vol.52 , pp. 245-262
    • McCluskey, K.1
  • 38
    • 77956995235 scopus 로고
    • Genetic and microbiological research techniques for Neurospora crassa
    • R.H. Davis, and F.J. de Serres Genetic and microbiological research techniques for Neurospora crassa Methods Enzymol. 17A 1970 79 143
    • (1970) Methods Enzymol. , vol.17 A , pp. 79-143
    • Davis, R.H.1    De Serres, F.J.2
  • 39
    • 0036024976 scopus 로고    scopus 로고
    • Measuring mitochondrial reactive oxygen species
    • DOI 10.1016/S1046-2023(02)00039-7, PII S1046202302000397
    • M. Degli Esposti Measuring mitochondrial reactive oxygen species Methods 26 2002 335 340 (Pubitemid 34971573)
    • (2002) Methods , vol.26 , Issue.4 , pp. 335-340
    • Degli Esposti, M.1
  • 41
    • 0035222647 scopus 로고    scopus 로고
    • Blue-native gels to isolate protein complexes from mitochondria
    • H. Schägger Blue-native gels to isolate protein complexes from mitochondria Methods Cell Biol. 65 2001 231 244
    • (2001) Methods Cell Biol. , vol.65 , pp. 231-244
    • Schägger, H.1
  • 42
    • 0021288878 scopus 로고
    • Superoxide dismutase assays
    • L. Flohé, and F. Otting Superoxide dismutase assays Methods Enzymol. 105 1984 93 104 (Pubitemid 14165376)
    • (1984) Methods in Enzymology , vol.105 , pp. 93-104
    • Flohe, L.1    Otting, F.2
  • 43
    • 0037101885 scopus 로고    scopus 로고
    • Regulation and oxidation of two large monofunctional catalases
    • DOI 10.1016/S0891-5849(02)00909-7, PII S0891584902009097
    • S. Michán, F. Lledías, J.D. Baldwin, D.O. Natvig, and W. Hansberg Regulation and oxidation of two large monofunctional catalases Free Radic. Biol. Med. 33 2002 521 532 (Pubitemid 34874973)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.4 , pp. 521-532
    • Michan, S.1    Lledias, F.2    Baldwin, J.D.3    Natvig, D.O.4    Hansberg, W.5
  • 44
    • 0028314548 scopus 로고
    • Disruption of the gene encoding the NADH-binding subunit of NADH:ubiquinone oxidoreductase in Neurospora crassa - Formation of a partially assembled enzyme without FMN and the iron-sulphur cluster N-3
    • W. Fecke, V.D. Sled, T. Ohnishi, and H. Weiss Disruption of the gene encoding the NADH-binding subunit of NADH:ubiquinone oxidoreductase in Neurospora crassa: formation of a partially assembled enzyme without FMN and the iron-sulphur cluster N-3 Eur. J. Biochem. 220 1994 551 558 (Pubitemid 24092823)
    • (1994) European Journal of Biochemistry , vol.220 , Issue.2 , pp. 551-558
    • Fecke, W.1    Sled, V.D.2    Ohnishi, T.3    Weiss, H.4
  • 46
    • 34347242465 scopus 로고    scopus 로고
    • Mitochondria are a major source of paraquat-induced reactive oxygen species production in the brain
    • DOI 10.1074/jbc.M700827200
    • P.R. Castello, D.A. Drechsel, and M. Patel Mitochondria are a major source of paraquat-induced reactive oxygen species production in the brain J. Biol. Chem. 282 2007 14186 14193 (Pubitemid 47100444)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.19 , pp. 14186-14193
    • Castello, P.R.1    Drechsel, D.A.2    Patel, M.3
  • 47
    • 78649991374 scopus 로고    scopus 로고
    • Synergistic effects of environmental risk factors and gene mutations in Parkinson's disease accelerate age-related neurodegeneration
    • J. Peng, M.L. Oo, and J.K. Andersen Synergistic effects of environmental risk factors and gene mutations in Parkinson's disease accelerate age-related neurodegeneration J. Neurochem. 115 2010 1363 1373
    • (2010) J. Neurochem. , vol.115 , pp. 1363-1373
    • Peng, J.1    Oo, M.L.2    Andersen, J.K.3
  • 48
    • 70349305420 scopus 로고    scopus 로고
    • Decreased mitochondrial superoxide levels and enhanced protection against paraquat in Drosophila melanogaster supplemented with Rhodiola rósea
    • S.E. Schriner, A. Abrahamyan, A. Avanessian, I. Bussel, S. Maler, M. Gazarian, M.A. Holmbeck, and M. Jafari Decreased mitochondrial superoxide levels and enhanced protection against paraquat in Drosophila melanogaster supplemented with Rhodiola rósea Free Radic. Res. 43 2009 836 843
    • (2009) Free Radic. Res. , vol.43 , pp. 836-843
    • Schriner, S.E.1    Abrahamyan, A.2    Avanessian, A.3    Bussel, I.4    Maler, S.5    Gazarian, M.6    Holmbeck, M.A.7    Jafari, M.8
  • 49
  • 51
    • 2942724221 scopus 로고    scopus 로고
    • Dual targeting of yeast catalase A to peroxisomes and mitochondria
    • DOI 10.1042/BJ20040042
    • V.Y. Petrova, D. Drescher, A.V. Kujumdzieva, and M.J. Schmitt Dual targeting of yeast catalase A to peroxisomes and mitochondria Biochem. J. 380 2004 393 400 (Pubitemid 38788110)
    • (2004) Biochemical Journal , vol.380 , Issue.2 , pp. 393-400
    • Petrova, V.Y.1    Drescher, D.2    Kujumdzieva, A.V.3    Schmitt, M.J.4
  • 52
    • 0037438869 scopus 로고    scopus 로고
    • Ectopic expression of catalase in Drosophila mitochondria increases stress resistance but not longevity
    • DOI 10.1016/S0891-5849(02)01190-5, PII S0891584902011905
    • R.J. Mockett, A.C. Bayne, L.K. Kwong, W.C. Orr, and R.S. Sohal Ectopic expression of catalase in Drosophila mitochondria increases stress resistance but not longevity Free Radic. Biol. Med. 34 2003 207 217 (Pubitemid 36084324)
    • (2003) Free Radical Biology and Medicine , vol.34 , Issue.2 , pp. 207-217
    • Mockett, R.J.1    Bayne, A.-C.V.2    Kwong, L.K.3    Orr, W.C.4    Sohal, R.S.5
  • 54
    • 77949483956 scopus 로고    scopus 로고
    • Mitochondrial dysfunction confers resistance to multiple drugs in Caenorhabditis elegans
    • I.O. Zubovych, S. Straud, and M.G. Roth Mitochondrial dysfunction confers resistance to multiple drugs in Caenorhabditis elegans Mol. Biol. Cell 6 2010 956 969
    • (2010) Mol. Biol. Cell , vol.6 , pp. 956-969
    • Zubovych, I.O.1    Straud, S.2    Roth, M.G.3
  • 56
    • 0032873464 scopus 로고    scopus 로고
    • A transcriptional switch in the expression of yeast tricarboxylic acid cycle genes in response to a reduction or loss of respiratory function
    • Z. Liu, and R.A. Butow A transcriptional switch in the expression of yeast tricarboxylic acid cycle genes in response to a reduction or loss of respiratory function Mol. Cell. Biol. 19 1999 6720 6728 (Pubitemid 29441856)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.10 , pp. 6720-6728
    • Liu, Z.1    Butow, R.A.2
  • 57
    • 34247118250 scopus 로고    scopus 로고
    • Yeast NDI1 improves oxidative phosphorylation capacity and increases protection against oxidative stress and cell death in cells carrying a Leber's hereditary optic neuropathy mutation
    • DOI 10.1016/j.bbadis.2007.01.009, PII S0925443907000294
    • J.S. Park, Y. Li, and Y. Bai Yeast NDI1 improves oxidative phosphorylation capacity and increases protection against oxidative stress and cell death in cells carrying a Leber's hereditary optic neuropathy mutation Biochim. Biophys. Acta 1772 2007 533 542 (Pubitemid 46589981)
    • (2007) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1772 , Issue.5 , pp. 533-542
    • Park, J.S.1    Li, Y.-f.2    Bai, Y.3
  • 58
    • 33744924255 scopus 로고    scopus 로고
    • In vivo complementation of complex I by the yeast Ndi1 enzyme: Possible application for treatment of Parkinson disease
    • DOI 10.1074/jbc.M600922200
    • B.B. Seo, E. Nakamaru-Ogiso, T.R. Flotte, A. Matsuno-Yagi, and T. Yagi In vivo complementation of complex I by the yeast Ndi1 enzyme: possible application for treatment of Parkinson disease J. Biol. Chem. 281 2006 14250 14255 (Pubitemid 43848352)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.20 , pp. 14250-14255
    • Byoung, B.S.1    Nakamaru-Ogiso, E.2    Flotte, T.R.3    Matsuno-Yagi, A.4    Yagi, T.5
  • 59
    • 70350076154 scopus 로고    scopus 로고
    • Neuroprotective effect of long-term NDI1 gene expression in a chronic mouse model of Parkinson disorder
    • J. Barber-Singh, B.B. Seo, E. Nakamaru-Ogiso, Y.S. Lau, A. Matsuno-Yagi, and T. Yagi Neuroprotective effect of long-term NDI1 gene expression in a chronic mouse model of Parkinson disorder Rejuvenation Res. 12 2009 259 267
    • (2009) Rejuvenation Res. , vol.12 , pp. 259-267
    • Barber-Singh, J.1    Seo, B.B.2    Nakamaru-Ogiso, E.3    Lau, Y.S.4    Matsuno-Yagi, A.5    Yagi, T.6
  • 60
    • 77955368934 scopus 로고    scopus 로고
    • Successful amelioration of mitochondrial optic neuropathy using the yeast NDI1 gene in a rat animal model
    • M. Marella, B.B. Seo, B.B. Thomas, A. Matsuno-Yagi, and T. Yagi Successful amelioration of mitochondrial optic neuropathy using the yeast NDI1 gene in a rat animal model PLoS One 5 2010 e11472
    • (2010) PLoS One , vol.5 , pp. 11472
    • Marella, M.1    Seo, B.B.2    Thomas, B.B.3    Matsuno-Yagi, A.4    Yagi, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.