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Volumn 1777, Issue 7-8, 2008, Pages 853-859

Corrigendum to “Mitigation of NADH:ubiquinone oxidoreductase deficiency by chronic Trolox treatment” (BBA - Bioenergetics (2008) 1777(7–8) (853–859), (S0005272808000686) (10.1016/j.bbabio.2008.03.028));Mitigation of NADH: Ubiquinone oxidoreductase deficiency by chronic Trolox treatment

Author keywords

Complex I deficiency; Mitochondria; Reactive oxygen species; Vitamin E

Indexed keywords

REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); TROLOX C;

EID: 46349094407     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2018.06.003     Document Type: Erratum
Times cited : (51)

References (48)
  • 1
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: channels, exchangers, and permeability transition
    • Bernardi P. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol. Rev. 79 (1999) 1127-1155
    • (1999) Physiol. Rev. , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 3
    • 4544378532 scopus 로고    scopus 로고
    • Mitochondrial fusion intermediates revealed in vitro
    • Meeusen S., McCaffery J.M., and Nunnari J. Mitochondrial fusion intermediates revealed in vitro. Science 305 (2004) 1747-1752
    • (2004) Science , vol.305 , pp. 1747-1752
    • Meeusen, S.1    McCaffery, J.M.2    Nunnari, J.3
  • 4
    • 0035474099 scopus 로고    scopus 로고
    • Nuclear genetic defects of oxidative phosphorylation
    • Shoubridge E.A. Nuclear genetic defects of oxidative phosphorylation. Hum. Mol. Genet. 10 (2001) 2277-2284
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2277-2284
    • Shoubridge, E.A.1
  • 6
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine
    • Wallace D.C. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu. Rev. Genet. 39 (2005) 359-407
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 12
    • 26444488636 scopus 로고    scopus 로고
    • A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy
    • Ogilvie I., Kennaway N.G., and Shoubridge E.A. A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy. J. Clin. Invest. 115 (2005) 2784-2792
    • (2005) J. Clin. Invest. , vol.115 , pp. 2784-2792
    • Ogilvie, I.1    Kennaway, N.G.2    Shoubridge, E.A.3
  • 13
    • 1642382090 scopus 로고    scopus 로고
    • Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency
    • Ugalde C., Janssen R.J., van den Heuvel L.W., Smeitink J.A.M., and Nijtmans L.G. Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency. Hum. Mol. Genet. 13 (2004) 659-667
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 659-667
    • Ugalde, C.1    Janssen, R.J.2    van den Heuvel, L.W.3    Smeitink, J.A.M.4    Nijtmans, L.G.5
  • 15
    • 9644283053 scopus 로고    scopus 로고
    • Application of the yeast Yarrowia lipolytica as a model to analyse human pathogenic mutations in mitochondrial complex I (NADH:ubiquinone oxidoreductase)
    • Kerscher S., Grgic L., Garofano A., and Brandt U. Application of the yeast Yarrowia lipolytica as a model to analyse human pathogenic mutations in mitochondrial complex I (NADH:ubiquinone oxidoreductase). Biochim. Biophys. Acta 1659 (2004) 197-205
    • (2004) Biochim. Biophys. Acta , vol.1659 , pp. 197-205
    • Kerscher, S.1    Grgic, L.2    Garofano, A.3    Brandt, U.4
  • 18
    • 29644439802 scopus 로고    scopus 로고
    • Decreased agonist-stimulated mitochondrial ATP production caused by a pathological reduction in endoplasmic reticulum calcium content in human complex I deficiency
    • Visch H.J., Koopman W.J.H., Leusink A., van Emst-de Vries S.E., van den Heuvel L.W., Willems P.H.G.M., and Smeitink J.A.M. Decreased agonist-stimulated mitochondrial ATP production caused by a pathological reduction in endoplasmic reticulum calcium content in human complex I deficiency. Biochim. Biophys. Acta 1762 (2005) 115-123
    • (2005) Biochim. Biophys. Acta , vol.1762 , pp. 115-123
    • Visch, H.J.1    Koopman, W.J.H.2    Leusink, A.3    van Emst-de Vries, S.E.4    van den Heuvel, L.W.5    Willems, P.H.G.M.6    Smeitink, J.A.M.7
  • 19
    • 1842338036 scopus 로고    scopus 로고
    • Excessive formation of hydroxyl radicals and aldehydic lipid peroxidation products in cultured skin fibroblasts from patients with complex I deficiency
    • Luo X., Pitkänen S., Kassovska-Bratinova S., Robinson B.H., and Lehotay D.C. Excessive formation of hydroxyl radicals and aldehydic lipid peroxidation products in cultured skin fibroblasts from patients with complex I deficiency. J. Clin. Invest. 99 (1997) 2877-2882
    • (1997) J. Clin. Invest. , vol.99 , pp. 2877-2882
    • Luo, X.1    Pitkänen, S.2    Kassovska-Bratinova, S.3    Robinson, B.H.4    Lehotay, D.C.5
  • 20
    • 0030056515 scopus 로고    scopus 로고
    • Mitochondrial complex I deficiency leads to increased production of superoxide radicals and induction of superoxide dismutase
    • Pitkänen S., and Robinson B.H. Mitochondrial complex I deficiency leads to increased production of superoxide radicals and induction of superoxide dismutase. J. Clin. Invest. 98 (1996) 345-351
    • (1996) J. Clin. Invest. , vol.98 , pp. 345-351
    • Pitkänen, S.1    Robinson, B.H.2
  • 22
    • 33845950116 scopus 로고    scopus 로고
    • Simultaneous quantification of oxidative stress and cell spreading using 5-(and -6)-chloromethyl-2′,7′-dichlorofluorescein
    • Koopman W.J.H., Verkaart S., van Emst-de Vries S.E., Grefte S., Smeitink J.A.M., and Willems P.H.G.M. Simultaneous quantification of oxidative stress and cell spreading using 5-(and -6)-chloromethyl-2′,7′-dichlorofluorescein. Cytometry A 69 (2006) 1184-1192
    • (2006) Cytometry A , vol.69 , pp. 1184-1192
    • Koopman, W.J.H.1    Verkaart, S.2    van Emst-de Vries, S.E.3    Grefte, S.4    Smeitink, J.A.M.5    Willems, P.H.G.M.6
  • 26
    • 27844605495 scopus 로고    scopus 로고
    • Superoxide generation from mitochondrial NADH dehydrogenase induces self inactivation with specific protein radical formation
    • Chen Y.R., Chen C.W., Zhang L., Green-church K.B., and Zweier J.L. Superoxide generation from mitochondrial NADH dehydrogenase induces self inactivation with specific protein radical formation. J. Biol. Chem. 280 (2005) 37339-37348
    • (2005) J. Biol. Chem. , vol.280 , pp. 37339-37348
    • Chen, Y.R.1    Chen, C.W.2    Zhang, L.3    Green-church, K.B.4    Zweier, J.L.5
  • 27
    • 27744508427 scopus 로고    scopus 로고
    • Rapid rates of newly synthesized mitochondrial protein degradation are significantly effected by the generation of mitochondrial free radicals
    • Basoah A., Matthews P.M., and Morten K.J. Rapid rates of newly synthesized mitochondrial protein degradation are significantly effected by the generation of mitochondrial free radicals. FEBS Lett. 579 (2005) 6511-6517
    • (2005) FEBS Lett. , vol.579 , pp. 6511-6517
    • Basoah, A.1    Matthews, P.M.2    Morten, K.J.3
  • 28
    • 0942298545 scopus 로고    scopus 로고
    • Endogenous mitochondrial oxidative stress: neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice
    • Hinerfeld D., Traini M.D., Weinberger R.P., Cochran B., Doctrow S.R., Harry J., and Melov S. Endogenous mitochondrial oxidative stress: neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice. J. Neurochem. 88 (2004) 657-667
    • (2004) J. Neurochem. , vol.88 , pp. 657-667
    • Hinerfeld, D.1    Traini, M.D.2    Weinberger, R.P.3    Cochran, B.4    Doctrow, S.R.5    Harry, J.6    Melov, S.7
  • 29
    • 1942453308 scopus 로고    scopus 로고
    • The mtDNA T8993G (NARP) mutation results in an impairment of oxidative phosphorylation that can be improved by antioxidants
    • Mattiazzi M., Vijayvergiya C., Gajewski C.D., DeVivo D.C., Lenaz G., Wiedmann M., and Manfredi G. The mtDNA T8993G (NARP) mutation results in an impairment of oxidative phosphorylation that can be improved by antioxidants. Hum. Mol. Genet. 13 (2004) 869-879
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 869-879
    • Mattiazzi, M.1    Vijayvergiya, C.2    Gajewski, C.D.3    DeVivo, D.C.4    Lenaz, G.5    Wiedmann, M.6    Manfredi, G.7
  • 31
    • 4344575973 scopus 로고    scopus 로고
    • Effect of high-dose vitamins, coenzyme Q and high-fat diet in paediatric patients with mitochondrial diseases
    • Panetta J., Smith L.J., and Boneh A. Effect of high-dose vitamins, coenzyme Q and high-fat diet in paediatric patients with mitochondrial diseases. J. Inherit. Metab. Dis. 27 (2004) 487-498
    • (2004) J. Inherit. Metab. Dis. , vol.27 , pp. 487-498
    • Panetta, J.1    Smith, L.J.2    Boneh, A.3
  • 33
    • 0036024975 scopus 로고    scopus 로고
    • Blue Native electrophoresis to study mitochondrial and other protein complexes
    • Nijtmans L.G., Henderson N.S., and Holt I.J. Blue Native electrophoresis to study mitochondrial and other protein complexes. Methods 26 (2002) 327-334
    • (2002) Methods , vol.26 , pp. 327-334
    • Nijtmans, L.G.1    Henderson, N.S.2    Holt, I.J.3
  • 34
    • 19544369483 scopus 로고    scopus 로고
    • Human mitochondrial complex I assembles through the combination of evolutionary conserved modules: a framework to interpret complex I deficiencies
    • Ugalde C., Vogel R., Huijbens R., van den Heuvel L.W., Smeitink J.A.M., and Nijtmans L.G. Human mitochondrial complex I assembles through the combination of evolutionary conserved modules: a framework to interpret complex I deficiencies. Hum. Mol. Genet. 13 (2004) 2461-2472
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2461-2472
    • Ugalde, C.1    Vogel, R.2    Huijbens, R.3    van den Heuvel, L.W.4    Smeitink, J.A.M.5    Nijtmans, L.G.6
  • 37
    • 0034663704 scopus 로고    scopus 로고
    • Application of the obligate aerobic yeast Yarrowia lipolytica as a eucaryotic model to analyse Leigh Syndrome mutations in the complex I core subunits PSST and TYKY
    • Ahlers P., Garofano A., Kerscher S., and Brandt U. Application of the obligate aerobic yeast Yarrowia lipolytica as a eucaryotic model to analyse Leigh Syndrome mutations in the complex I core subunits PSST and TYKY. Biochim. Biophys. Acta 1459 (2000) 258-265
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 258-265
    • Ahlers, P.1    Garofano, A.2    Kerscher, S.3    Brandt, U.4
  • 38
    • 22444434735 scopus 로고    scopus 로고
    • Neurospora strains harboring mitochondrial disease-associated mutations in iron-sulfur subunits of complex I
    • Duarte M., Schulte U., Ushakova A.V., and Videira A. Neurospora strains harboring mitochondrial disease-associated mutations in iron-sulfur subunits of complex I. Genetics 171 (2005) 91-99
    • (2005) Genetics , vol.171 , pp. 91-99
    • Duarte, M.1    Schulte, U.2    Ushakova, A.V.3    Videira, A.4
  • 39
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH:quinone oxidoreductase (complex I)
    • Brandt U. Energy converting NADH:quinone oxidoreductase (complex I). Annu. Rev. Biochem. 75 (2006) 69-92
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 69-92
    • Brandt, U.1
  • 40
    • 33751072935 scopus 로고    scopus 로고
    • Bioenergetics and the formation of mitochondrial reactive oxygen species
    • Adam-Vizi V., and Chinopoulos C. Bioenergetics and the formation of mitochondrial reactive oxygen species. Trends Pharmacol. Sci. 27 (2006) 639-645
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 639-645
    • Adam-Vizi, V.1    Chinopoulos, C.2
  • 41
    • 27144537231 scopus 로고    scopus 로고
    • Prooxidant and antioxidant activity of vitamin E analogues and troglitazone
    • Tafazoli S., Wright J.S., and O'Brien P.J. Prooxidant and antioxidant activity of vitamin E analogues and troglitazone. Chem. Res. Toxicol. 18 (2005) 1567-1574
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 1567-1574
    • Tafazoli, S.1    Wright, J.S.2    O'Brien, P.J.3
  • 43
    • 0037029129 scopus 로고    scopus 로고
    • Reactive oxygen species affect mitochondrial electron transport complex I activity through oxidative cardiolipin damage
    • Paradies G., Petrosillo G., Pistolese M., and Ruggiero F.M. Reactive oxygen species affect mitochondrial electron transport complex I activity through oxidative cardiolipin damage. Gene 286 (2002) 135-141
    • (2002) Gene , vol.286 , pp. 135-141
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 44
    • 33644850965 scopus 로고    scopus 로고
    • Depletion of cardiolipin and cytochrome c during ischemia increases hydrogen peroxide production from the electron transport chain
    • Chen Q., and Lesnefsky E.J. Depletion of cardiolipin and cytochrome c during ischemia increases hydrogen peroxide production from the electron transport chain. Free Rad. Biol. Med. 40 (2006) 976-982
    • (2006) Free Rad. Biol. Med. , vol.40 , pp. 976-982
    • Chen, Q.1    Lesnefsky, E.J.2
  • 45
    • 20444461625 scopus 로고    scopus 로고
    • The Charcot-Marie-Tooth type 2A gene product, Mfn2, up-regulates fuel oxidation through expression of OXPHOS system
    • Pich S., Bach D., Briones P., Liesa M., Camps M., Testar X., Palacin M., and Zorzano A. The Charcot-Marie-Tooth type 2A gene product, Mfn2, up-regulates fuel oxidation through expression of OXPHOS system. Hum. Mol. Genet. 14 (2005) 1405-1415
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1405-1415
    • Pich, S.1    Bach, D.2    Briones, P.3    Liesa, M.4    Camps, M.5    Testar, X.6    Palacin, M.7    Zorzano, A.8


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