메뉴 건너뛰기




Volumn 104, Issue 5, 2013, Pages 1127-1141

Synergy in free radical generation is blunted by high-fat diet induced alterations in skeletal muscle mitochondrial metabolism

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; HYDROGEN PEROXIDE; MITOCHONDRIAL PROTEIN; PYRUVIC ACID;

EID: 84874923241     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.01.025     Document Type: Article
Times cited : (6)

References (57)
  • 2
    • 0035936763 scopus 로고    scopus 로고
    • New perspectives into the molecular pathogenesis and treatment of type 2 diabetes
    • A.R. Saltiel New perspectives into the molecular pathogenesis and treatment of type 2 diabetes Cell 104 2001 517 529
    • (2001) Cell , vol.104 , pp. 517-529
    • Saltiel, A.R.1
  • 3
    • 34248140740 scopus 로고    scopus 로고
    • High-fat diet, muscular lipotoxicity and insulin resistance
    • P. Schrauwen High-fat diet, muscular lipotoxicity and insulin resistance Proc. Nutr. Soc. 66 2007 33 41
    • (2007) Proc. Nutr. Soc. , vol.66 , pp. 33-41
    • Schrauwen, P.1
  • 5
    • 33845881411 scopus 로고    scopus 로고
    • Mechanisms linking obesity to insulin resistance and type 2 diabetes
    • S.E. Kahn, R.L. Hull, and K.M. Utzschneider Mechanisms linking obesity to insulin resistance and type 2 diabetes Nature 444 2006 840 846
    • (2006) Nature , vol.444 , pp. 840-846
    • Kahn, S.E.1    Hull, R.L.2    Utzschneider, K.M.3
  • 6
    • 0033927667 scopus 로고    scopus 로고
    • Cellular mechanisms of insulin resistance
    • G.I. Shulman Cellular mechanisms of insulin resistance J. Clin. Invest. 106 2000 171 176
    • (2000) J. Clin. Invest. , vol.106 , pp. 171-176
    • Shulman, G.I.1
  • 7
    • 12144275294 scopus 로고    scopus 로고
    • Deficiency of subsarcolemmal mitochondria in obesity and type 2 diabetes
    • V.B. Ritov, and E.V. Menshikova D.E. Kelley Deficiency of subsarcolemmal mitochondria in obesity and type 2 diabetes Diabetes 54 2005 8 14
    • (2005) Diabetes , vol.54 , pp. 8-14
    • Ritov, V.B.1    Menshikova, E.V.2    Kelley, D.E.3
  • 8
    • 0036788293 scopus 로고    scopus 로고
    • Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes
    • D.E. Kelley, and J. He V.B. Ritov Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes Diabetes 51 2002 2944 2950
    • (2002) Diabetes , vol.51 , pp. 2944-2950
    • Kelley, D.E.1    He, J.2    Ritov, V.B.3
  • 9
    • 58149379936 scopus 로고    scopus 로고
    • Skeletal muscle "mitochondrial deficiency" does not mediate insulin resistance
    • J.O. Holloszy Skeletal muscle "mitochondrial deficiency" does not mediate insulin resistance Am. J. Clin. Nutr. 89 2009 463S 466S
    • (2009) Am. J. Clin. Nutr. , vol.89
    • Holloszy, J.O.1
  • 10
    • 76149131004 scopus 로고    scopus 로고
    • The role of mitochondria in the pathophysiology of skeletal muscle insulin resistance
    • I. Pagel-Langenickel, and J. Bao M.N. Sack The role of mitochondria in the pathophysiology of skeletal muscle insulin resistance Endocr. Rev. 31 2010 25 51
    • (2010) Endocr. Rev. , vol.31 , pp. 25-51
    • Pagel-Langenickel, I.1    Bao, J.2    Sack, M.N.3
  • 11
    • 67650815430 scopus 로고    scopus 로고
    • 2 emission and cellular redox state link excess fat intake to insulin resistance in both rodents and humans
    • 2 emission and cellular redox state link excess fat intake to insulin resistance in both rodents and humans J. Clin. Invest. 119 2009 573 581
    • (2009) J. Clin. Invest. , vol.119 , pp. 573-581
    • Anderson, E.J.1    Lustig, M.E.2    Neufer, P.D.3
  • 12
    • 33645860825 scopus 로고    scopus 로고
    • Reactive oxygen species have a causal role in multiple forms of insulin resistance
    • N. Houstis, E.D. Rosen, and E.S. Lander Reactive oxygen species have a causal role in multiple forms of insulin resistance Nature 440 2006 944 948
    • (2006) Nature , vol.440 , pp. 944-948
    • Houstis, N.1    Rosen, E.D.2    Lander, E.S.3
  • 13
    • 75149194772 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in diabetes: From molecular mechanisms to functional significance and therapeutic opportunities
    • W.I. Sivitz, and M.A. Yorek Mitochondrial dysfunction in diabetes: from molecular mechanisms to functional significance and therapeutic opportunities Antioxid. Redox Signal. 12 2010 537 577
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 537-577
    • Sivitz, W.I.1    Yorek, M.A.2
  • 14
    • 77954859197 scopus 로고    scopus 로고
    • The role of mitochondria in the pathogenesis of type 2 diabetes
    • M.-E. Patti, and S. Corvera The role of mitochondria in the pathogenesis of type 2 diabetes Endocr. Rev. 31 2010 364 395
    • (2010) Endocr. Rev. , vol.31 , pp. 364-395
    • Patti, M.-E.1    Corvera, S.2
  • 15
    • 0037376665 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease
    • S.J. Lin, and L. Guarente Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease Curr. Opin. Cell Biol. 15 2003 241 246
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 241-246
    • Lin, S.J.1    Guarente, L.2
  • 17
    • 50849098175 scopus 로고    scopus 로고
    • Mitochondrial signaling in mammalian cells activated by red and near-IR radiation
    • T.I. Karu Mitochondrial signaling in mammalian cells activated by red and near-IR radiation Photochem. Photobiol. 84 2008 1091 1099
    • (2008) Photochem. Photobiol. , vol.84 , pp. 1091-1099
    • Karu, T.I.1
  • 18
    • 0842328003 scopus 로고    scopus 로고
    • Prevention of mitochondrial oxidative damage as a therapeutic strategy in diabetes
    • K. Green, M.D. Brand, and M.P. Murphy Prevention of mitochondrial oxidative damage as a therapeutic strategy in diabetes Diabetes 53 Suppl 1 2004 S110 S118
    • (2004) Diabetes , vol.53 , Issue.SUPPL. 1
    • Green, K.1    Brand, M.D.2    Murphy, M.P.3
  • 19
    • 61449147889 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species generation in obese non-diabetic and type 2 diabetic participants
    • M.A. Abdul-Ghani, and R. Jani R.A. Defronzo Mitochondrial reactive oxygen species generation in obese non-diabetic and type 2 diabetic participants Diabetologia 52 2009 574 582
    • (2009) Diabetologia , vol.52 , pp. 574-582
    • Abdul-Ghani, M.A.1    Jani, R.2    Defronzo, R.A.3
  • 20
    • 77957269940 scopus 로고    scopus 로고
    • Virtual mitochondrion: Towards an integrated model of oxidative phosphorylation complexes and beyond
    • J.P. Mazat, and J. Fromentin S. Ransac Virtual mitochondrion: towards an integrated model of oxidative phosphorylation complexes and beyond Biochem. Soc. Trans. 38 2010 1215 1219
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 1215-1219
    • Mazat, J.P.1    Fromentin, J.2    Ransac, S.3
  • 21
    • 84555178541 scopus 로고    scopus 로고
    • Computational modeling of mitochondrial energy transduction
    • J.P. Schmitz, and J. Vanlier J.A. Jeneson Computational modeling of mitochondrial energy transduction Crit. Rev. Biomed. Eng. 39 2011 363 377
    • (2011) Crit. Rev. Biomed. Eng. , vol.39 , pp. 363-377
    • Schmitz, J.P.1    Vanlier, J.2    Jeneson, J.A.3
  • 22
    • 79953667930 scopus 로고    scopus 로고
    • Reactive oxygen species production by forward and reverse electron fluxes in the mitochondrial respiratory chain
    • V.A. Selivanov, and T.V. Votyakova M. Cascante Reactive oxygen species production by forward and reverse electron fluxes in the mitochondrial respiratory chain PLOS Comput. Biol. 7 2011 e1001115
    • (2011) PLOS Comput. Biol. , vol.7 , pp. 1001115
    • Selivanov, V.A.1    Votyakova, T.V.2    Cascante, M.3
  • 23
    • 77049113232 scopus 로고    scopus 로고
    • Autoregulation of free radicals via uncoupling protein control in pancreatic β-cell mitochondria
    • W.J. Heuett, and V. Periwal Autoregulation of free radicals via uncoupling protein control in pancreatic β-cell mitochondria Biophys. J. 98 2010 207 217
    • (2010) Biophys. J. , vol.98 , pp. 207-217
    • Heuett, W.J.1    Periwal, V.2
  • 24
    • 34548297895 scopus 로고    scopus 로고
    • Computer modeling of mitochondrial tricarboxylic acid cycle, oxidative phosphorylation, metabolite transport, and electrophysiology
    • F. Wu, and F. Yang D.A. Beard Computer modeling of mitochondrial tricarboxylic acid cycle, oxidative phosphorylation, metabolite transport, and electrophysiology J. Biol. Chem. 282 2007 24525 24537
    • (2007) J. Biol. Chem. , vol.282 , pp. 24525-24537
    • Wu, F.1    Yang, F.2    Beard, D.A.3
  • 25
    • 78149455629 scopus 로고    scopus 로고
    • The electron transfer flavoprotein: Ubiquinone oxidoreductases
    • N.J. Watmough, and F.E. Frerman The electron transfer flavoprotein: ubiquinone oxidoreductases Biochim. Biophys. Acta 1797 2010 1910 1916
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1910-1916
    • Watmough, N.J.1    Frerman, F.E.2
  • 27
    • 60649106368 scopus 로고    scopus 로고
    • Dynamic simulations on the mitochondrial fatty acid β-oxidation network
    • R. Modre-Osprian, and I. Osprian A. Graber Dynamic simulations on the mitochondrial fatty acid β-oxidation network BMC Syst. Biol. 3 2009 2 15
    • (2009) BMC Syst. Biol. , vol.3 , pp. 2-15
    • Modre-Osprian, R.1    Osprian, I.2    Graber, A.3
  • 28
    • 4444332930 scopus 로고    scopus 로고
    • A general computational model of mitochondrial metabolism in a whole organelle scale
    • K. Yugi, and M. Tomita A general computational model of mitochondrial metabolism in a whole organelle scale Bioinformatics 20 2004 1795 1796
    • (2004) Bioinformatics , vol.20 , pp. 1795-1796
    • Yugi, K.1    Tomita, M.2
  • 29
    • 79953762174 scopus 로고    scopus 로고
    • Unraveling the biological roles of reactive oxygen species
    • M.P. Murphy, and A. Holmgren C.C. Winterbourn Unraveling the biological roles of reactive oxygen species Cell Metab. 13 2011 361 366
    • (2011) Cell Metab. , vol.13 , pp. 361-366
    • Murphy, M.P.1    Holmgren, A.2    Winterbourn, C.C.3
  • 30
    • 74449091635 scopus 로고    scopus 로고
    • Superoxide dismutases - A review of the metal-associated mechanistic variations
    • I.A. Abreu, and D.E. Cabelli Superoxide dismutases - a review of the metal-associated mechanistic variations Biochim. Biophys. Acta 1804 2010 263 274
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 263-274
    • Abreu, I.A.1    Cabelli, D.E.2
  • 31
    • 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
  • 32
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • J.F. Turrens Mitochondrial formation of reactive oxygen species J. Physiol. 552 2003 335 344
    • (2003) J. Physiol. , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 34
    • 0034177951 scopus 로고    scopus 로고
    • Tissue variation in the control of oxidative phosphorylation: Implication for mitochondrial diseases
    • R. Rossignol, and T. Letellier J.P. Mazat Tissue variation in the control of oxidative phosphorylation: implication for mitochondrial diseases Biochem. J. 347 2000 45 53
    • (2000) Biochem. J. , vol.347 , pp. 45-53
    • Rossignol, R.1    Letellier, T.2    Mazat, J.P.3
  • 35
    • 45549089279 scopus 로고    scopus 로고
    • High-fat diets cause insulin resistance despite an increase in muscle mitochondria
    • C.R. Hancock, and D.-H. Han J.O. Holloszy High-fat diets cause insulin resistance despite an increase in muscle mitochondria Proc. Natl. Acad. Sci. USA 105 2008 7815 7820
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7815-7820
    • Hancock, C.R.1    Han, D.-H.2    Holloszy, J.O.3
  • 36
    • 82155192472 scopus 로고    scopus 로고
    • High fat diet-induced changes in mouse muscle mitochondrial phospholipids do not impair mitochondrial respiration despite insulin resistance
    • J. Hoeks, and J. Wilde E.C. Mariman High fat diet-induced changes in mouse muscle mitochondrial phospholipids do not impair mitochondrial respiration despite insulin resistance PLoS ONE 6 2011 e27274
    • (2011) PLoS ONE , vol.6 , pp. 27274
    • Hoeks, J.1    Wilde, J.2    Mariman, E.C.3
  • 37
    • 0026519290 scopus 로고
    • Metabolic response to a high-fat diet in neonatal and adult rat muscle
    • P.M. Nemeth, and B.W. Rosser K.M. Baker Metabolic response to a high-fat diet in neonatal and adult rat muscle Am. J. Physiol. 262 1992 C282 C286
    • (1992) Am. J. Physiol. , vol.262
    • Nemeth, P.M.1    Rosser, B.W.2    Baker, K.M.3
  • 38
    • 79551510868 scopus 로고    scopus 로고
    • Interactions between the consumption of a high-fat diet and fasting in the regulation of fatty acid oxidation enzyme gene expression: An evaluation of potential mechanisms
    • B.C. Frier, R.L. Jacobs, and D.C. Wright Interactions between the consumption of a high-fat diet and fasting in the regulation of fatty acid oxidation enzyme gene expression: an evaluation of potential mechanisms Am. J. Physiol. Regul. Integr. Comp. Physiol. 300 2011 R212 R221
    • (2011) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.300
    • Frier, B.C.1    Jacobs, R.L.2    Wright, D.C.3
  • 39
    • 77952650736 scopus 로고    scopus 로고
    • Computational model of cellular metabolic dynamics: Effect of insulin on glucose disposal in human skeletal muscle
    • Y. Li, and T.P. Solomon J.P. Kirwan Computational model of cellular metabolic dynamics: effect of insulin on glucose disposal in human skeletal muscle Am. J. Physiol. Endocrinol. Metab. 298 2010 E1198 E1209
    • (2010) Am. J. Physiol. Endocrinol. Metab. , vol.298
    • Li, Y.1    Solomon, T.P.2    Kirwan, J.P.3
  • 40
    • 77951665882 scopus 로고    scopus 로고
    • PPARγ expression after a high-fat meal is associated with plasma superoxide dismutase activity in morbidly obese persons
    • E. Garcia-Fuentes, and M. Murri M. Macias-Gonzalez PPARγ expression after a high-fat meal is associated with plasma superoxide dismutase activity in morbidly obese persons Obesity (Silver Spring) 18 2010 952 958
    • (2010) Obesity (Silver Spring) , vol.18 , pp. 952-958
    • Garcia-Fuentes, E.1    Murri, M.2    MacIas-Gonzalez, M.3
  • 41
    • 0032452225 scopus 로고    scopus 로고
    • Regulatory interactions between lipids and carbohydrates: The glucose fatty acid cycle after 35 years
    • P.J. Randle Regulatory interactions between lipids and carbohydrates: the glucose fatty acid cycle after 35 years Diabetes Metab. Rev. 14 1998 263 283
    • (1998) Diabetes Metab. Rev. , vol.14 , pp. 263-283
    • Randle, P.J.1
  • 42
    • 84857788916 scopus 로고    scopus 로고
    • Glycerolipid/free fatty acid cycle and islet β-cell function in health, obesity and diabetes
    • M. Prentki, and S.R. Madiraju Glycerolipid/free fatty acid cycle and islet β-cell function in health, obesity and diabetes Mol. Cell. Endocrinol. 353 2012 88 100
    • (2012) Mol. Cell. Endocrinol. , vol.353 , pp. 88-100
    • Prentki, M.1    Madiraju, S.R.2
  • 43
    • 34948890528 scopus 로고    scopus 로고
    • β-Cell mitochondria exhibit membrane potential heterogeneity that can be altered by stimulatory or toxic fuel levels
    • J.D. Wikstrom, and S.M. Katzman O.S. Shirihai β-Cell mitochondria exhibit membrane potential heterogeneity that can be altered by stimulatory or toxic fuel levels Diabetes 56 2007 2569 2578
    • (2007) Diabetes , vol.56 , pp. 2569-2578
    • Wikstrom, J.D.1    Katzman, S.M.2    Shirihai, O.S.3
  • 44
    • 80054051101 scopus 로고    scopus 로고
    • The regulation and physiology of mitochondrial proton leak
    • A.S. Divakaruni, and M.D. Brand The regulation and physiology of mitochondrial proton leak Physiology (Bethesda) 26 2011 192 205
    • (2011) Physiology (Bethesda) , vol.26 , pp. 192-205
    • Divakaruni, A.S.1    Brand, M.D.2
  • 45
    • 63349087445 scopus 로고    scopus 로고
    • Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation
    • E.B. Tahara, F.D. Navarete, and A.J. Kowaltowski Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation Free Radic. Biol. Med. 46 2009 1283 1297
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 1283-1297
    • Tahara, E.B.1    Navarete, F.D.2    Kowaltowski, A.J.3
  • 46
    • 33646846683 scopus 로고    scopus 로고
    • 3-Nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme
    • L.S. Huang, and G. Sun E.A. Berry 3-Nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme J. Biol. Chem. 281 2006 5965 5972
    • (2006) J. Biol. Chem. , vol.281 , pp. 5965-5972
    • Huang, L.S.1    Sun, G.2    Berry, E.A.3
  • 47
    • 0038389439 scopus 로고    scopus 로고
    • 3-Nitropropionic acid inhibition of succinate dehydrogenase (complex II) activity in cultured Chinese hamster ovary cells: Antagonism by L-carnitine
    • A.C. Scallet, and R.L. Haley Z.K. Binienda 3-Nitropropionic acid inhibition of succinate dehydrogenase (complex II) activity in cultured Chinese hamster ovary cells: antagonism by L-carnitine Ann. N. Y. Acad. Sci. 993 2003 305 3129
    • (2003) Ann. N. Y. Acad. Sci. , vol.993 , pp. 305-3129
    • Scallet, A.C.1    Haley, R.L.2    Binienda, Z.K.3
  • 48
    • 0036801419 scopus 로고    scopus 로고
    • Inhibition of the α-ketoglutarate dehydrogenase and pyruvate dehydrogenase complexes by a putative aberrant metabolite of serotonin, tryptamine-4,5-dione
    • X.R. Jiang, and G. Dryhurst Inhibition of the α-ketoglutarate dehydrogenase and pyruvate dehydrogenase complexes by a putative aberrant metabolite of serotonin, tryptamine-4,5-dione Chem. Res. Toxicol. 15 2002 1242 1247
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 1242-1247
    • Jiang, X.R.1    Dryhurst, G.2
  • 49
    • 77449110345 scopus 로고    scopus 로고
    • Biapigenin modulates the activity of the adenine nucleotide translocator in isolated rat brain mitochondria
    • B.A. Silva, and P.J. Oliveira J.O. Malva Biapigenin modulates the activity of the adenine nucleotide translocator in isolated rat brain mitochondria Neurotox. Res. 17 2010 75 90
    • (2010) Neurotox. Res. , vol.17 , pp. 75-90
    • Silva, B.A.1    Oliveira, P.J.2    Malva, J.O.3
  • 50
    • 80051783174 scopus 로고    scopus 로고
    • Uncoupling proteins and the control of mitochondrial reactive oxygen species production
    • R.J. Mailloux, and M.E. Harper Uncoupling proteins and the control of mitochondrial reactive oxygen species production Free Radic. Biol. Med. 51 2011 1106 1115
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 1106-1115
    • Mailloux, R.J.1    Harper, M.E.2
  • 51
    • 79958735550 scopus 로고    scopus 로고
    • Glutathionylation acts as a control switch for uncoupling proteins UCP2 and UCP3
    • R.J. Mailloux, and E.L. Seifert M.E. Harper Glutathionylation acts as a control switch for uncoupling proteins UCP2 and UCP3 J. Biol. Chem. 286 2011 21865 21875
    • (2011) J. Biol. Chem. , vol.286 , pp. 21865-21875
    • Mailloux, R.J.1    Seifert, E.L.2    Harper, M.E.3
  • 52
    • 84864022828 scopus 로고    scopus 로고
    • Glutathione/thioredoxin systems modulate mitochondrial H2O2 emission: An experimental-computational study
    • M.A. Aon, and B.A. Stanley S. Cortassa Glutathione/thioredoxin systems modulate mitochondrial H2O2 emission: an experimental-computational study J. Gen. Physiol. 139 2012 479 491
    • (2012) J. Gen. Physiol. , vol.139 , pp. 479-491
    • Aon, M.A.1    Stanley, B.A.2    Cortassa, S.3
  • 53
    • 33745635338 scopus 로고    scopus 로고
    • Mitochondrial NADPH, transhydrogenase and disease
    • J. Rydström Mitochondrial NADPH, transhydrogenase and disease Biochim. Biophys. Acta 1757 2006 721 726
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 721-726
    • Rydström, J.1
  • 54
    • 63549114784 scopus 로고    scopus 로고
    • Hypertrophy and/or hyperplasia: Dynamics of adipose tissue growth
    • J. Jo, and O. Gavrilova V. Periwal Hypertrophy and/or hyperplasia: dynamics of adipose tissue growth PLOS Comput. Biol. 5 2009 e1000324
    • (2009) PLOS Comput. Biol. , vol.5 , pp. 1000324
    • Jo, J.1    Gavrilova, O.2    Periwal, V.3
  • 55
    • 65349123514 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function
    • D.F. Stowe, and A.K. Camara Mitochondrial reactive oxygen species production in excitable cells: modulators of mitochondrial and cell function Antioxid. Redox Signal. 11 2009 1373 1414
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 1373-1414
    • Stowe, D.F.1    Camara, A.K.2
  • 57
    • 4444240180 scopus 로고    scopus 로고
    • A mitochondrial oscillator dependent on reactive oxygen species
    • S. Cortassa, and M.A. Aon B. O'Rourke A mitochondrial oscillator dependent on reactive oxygen species Biophys. J. 87 2004 2060 2073
    • (2004) Biophys. J. , vol.87 , pp. 2060-2073
    • Cortassa, S.1    Aon, M.A.2    O'Rourke, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.