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Volumn 1807, Issue 12, 2011, Pages 1562-1572

Complex I and cytochrome c are molecular targets of flavonoids that inhibit hydrogen peroxide production by mitochondria

Author keywords

Complex I; Cytochrome c; Flavonoid; Hydrogen peroxide production; Mitochondria; Ubiquinone

Indexed keywords

ANTIMYCIN A1; APIGENIN; CYTOCHROME C; EPICATECHIN; FLAVONOID; HYDROGEN PEROXIDE; KAEMPFEROL; MITOCHONDRIAL ENZYME; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); ROTENONE; SUPEROXIDE DISMUTASE; UBIQUINONE;

EID: 81155128482     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.09.022     Document Type: Article
Times cited : (154)

References (86)
  • 2
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • DOI 10.1038/nature05292, PII NATURE05292
    • M.T. Lin, and M.F. Beal Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases Nature 443 2006 787 795 (Pubitemid 44622683)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 3
    • 84857190035 scopus 로고    scopus 로고
    • Reactive oxidants and diabetic vascular disease
    • C. Gutiérrez-Merino, C. Leeuwenburg, Research Signpost Kerala (India)
    • A. Vivekanandan-Giri, J. Byun, and S. Pennathur Reactive oxidants and diabetic vascular disease C. Gutiérrez-Merino, C. Leeuwenburg, Free Radicals in Biology and Medicine 2008 Research Signpost Kerala (India) 171 200
    • (2008) Free Radicals in Biology and Medicine , pp. 171-200
    • Vivekanandan-Giri, A.1    Byun, J.2    Pennathur, S.3
  • 4
    • 77956586695 scopus 로고    scopus 로고
    • Mitochondria in heart failure
    • M.G. Rosca, and C.L. Hoppel Mitochondria in heart failure Cardiovasc. Res. 88 2010 40 50
    • (2010) Cardiovasc. Res. , vol.88 , pp. 40-50
    • Rosca, M.G.1    Hoppel, C.L.2
  • 5
    • 77956804126 scopus 로고    scopus 로고
    • Endothelial mitochondria and heart disease
    • S.M. Davidson Endothelial mitochondria and heart disease Cardiovasc. Res. 88 2010 58 66
    • (2010) Cardiovasc. Res. , vol.88 , pp. 58-66
    • Davidson, S.M.1
  • 6
    • 45149107487 scopus 로고    scopus 로고
    • Mechanisms of neurodegeneration in Huntington's disease
    • DOI 10.1111/j.1460-9568.2008.06310.x
    • J.M. Gil, and A.C. Rego Mechanisms of neurodegeneration in Huntington's disease Eur. J. Neurosci. 27 2008 2803 2820 (Pubitemid 351832229)
    • (2008) European Journal of Neuroscience , vol.27 , Issue.11 , pp. 2803-2820
    • Gil, J.M.1    Rego, A.C.2
  • 7
    • 84857195783 scopus 로고    scopus 로고
    • Impact of nitric oxide on brain energy metabolism and antioxidant defense: Implications for neuroprotection and neurodegeneration
    • C. Gutierrez-Merino, C. Leeuwenburg, Research Signpost Kerala (India)
    • J. Bolaños, and A. Almeida Impact of nitric oxide on brain energy metabolism and antioxidant defense: implications for neuroprotection and neurodegeneration C. Gutierrez-Merino, C. Leeuwenburg, Free Radicals in Biology and Medicine 2008 Research Signpost Kerala (India) 151 169
    • (2008) Free Radicals in Biology and Medicine , pp. 151-169
    • Bolaños, J.1    Almeida, A.2
  • 8
    • 77956186783 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
    • R.B. Hamanaka, and N.S. Chandel Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes Trends Biochem. Sci. 35 2010 505 513
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 505-513
    • Hamanaka, R.B.1    Chandel, N.S.2
  • 9
    • 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
  • 10
    • 0031020172 scopus 로고    scopus 로고
    • Bright and dark sides of nitric oxide in ischemic brain injury
    • DOI 10.1016/S0166-2236(96)10074-6, PII S0166223696100746
    • C. Iadecola Bright and dark sides of nitric oxide in ischemic brain injury Trends Neurosci. 20 1997 132 139 (Pubitemid 27086729)
    • (1997) Trends in Neurosciences , vol.20 , Issue.3 , pp. 132-139
    • Iadecola, C.1
  • 11
    • 0037449409 scopus 로고    scopus 로고
    • Delayed effect of administration of COX-2 inhibitor in mice with acute cerebral ischemia
    • DOI 10.1016/S0006-8993(02)03805-2, PII S0006899302038052
    • K. Sugimoto, and C. Iadecola Delayed effect of administration of COX-2 inhibitor in mice with acute cerebral ischemia Brain Res. 960 2003 273 276 (Pubitemid 36044587)
    • (2003) Brain Research , vol.960 , Issue.1-2 , pp. 273-276
    • Sugimoto, K.1    Iadecola, C.2
  • 12
    • 0030787471 scopus 로고    scopus 로고
    • Extensive peroxynitrite activity during progressive stages of central nervous system inflammation
    • DOI 10.1016/S0165-5728(97)00013-1, PII S0165572897000131
    • R.C. Van der Veen, D.R. Hinton, F. Incardonna, and F.M. Hofman Extensive peroxynitrite activity during progressive stages of central nervous system inflammation J. Neuroimmunol. 77 1997 1 7 (Pubitemid 27286370)
    • (1997) Journal of Neuroimmunology , vol.77 , Issue.1 , pp. 1-7
    • Van Der Veen, R.C.1    Hinton, D.R.2    Incardonna, F.3    Hofman, F.M.4
  • 13
    • 0033793219 scopus 로고    scopus 로고
    • The role of reactive nitrogen species in secondary spinal cord injury: Formation of nitric oxide, peroxynitrite, and nitrated protein
    • D. Liu, X. Ling, J. Wen, and J. Liu The role of reactive nitrogen species in secondary spinal cord injury: formation of nitric oxide, peroxynitrite, and nitrated protein J. Neurochem. 75 2000 2144 2154
    • (2000) J. Neurochem. , vol.75 , pp. 2144-2154
    • Liu, D.1    Ling, X.2    Wen, J.3    Liu, J.4
  • 14
    • 2942657443 scopus 로고    scopus 로고
    • Hydroxyl radicals generated in the rat spinal cord at the level produced by impact injury induce cell death by necrosis and apoptosis: Protection by a metalloporphyrin
    • DOI 10.1016/j.neuroscience.2004.03.054, PII S0306452204002362
    • F. Bao, and D. Liu Hydroxyl radicals generated in the rat spinal cord at the level produced by impact injury induce cell death by necrosis and apoptosis: protection by a metalloporphyrin Neuroscience 126 2004 285 295 (Pubitemid 38780804)
    • (2004) Neuroscience , vol.126 , Issue.2 , pp. 285-295
    • Bao, F.1    Liu, D.2
  • 16
    • 29144468251 scopus 로고    scopus 로고
    • 3-Nitropropionic acid: A mitochondrial toxin to uncover physiopathological mechanisms underlying striatal degeneration in Huntington's disease
    • DOI 10.1111/j.1471-4159.2005.03515.x
    • E. Brouillet, C. Jacquard, N. Bizat, and D. Blum 3-Nitropropionic acid: a mitochondrial toxin to uncover physiopathological mechanisms underlying striatal degeneration in Huntington's disease J. Neurochem. 95 2005 1521 1540 (Pubitemid 41804051)
    • (2005) Journal of Neurochemistry , vol.95 , Issue.6 , pp. 1521-1540
    • Brouillet, E.1    Jacquard, C.2    Bizat, N.3    Blum, D.4
  • 17
    • 69549084529 scopus 로고    scopus 로고
    • Environmental toxins and Parkinson's disease: What have we learned from pesticide-induced animal models?
    • F. Cinchetti, J. Drouin-Ouellet, and R.E. Gross Environmental toxins and Parkinson's disease: what have we learned from pesticide-induced animal models? Trends Pharmacol. Sci. 30 2009 475 483
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 475-483
    • Cinchetti, F.1    Drouin-Ouellet, J.2    Gross, R.E.3
  • 19
    • 0027496238 scopus 로고
    • A radical hypothesis for neurodegeneration
    • DOI 10.1016/0166-2236(93)90070-3
    • C.W. Olanow A radical hypothesis for neurodegeneration Trends Neurosci. 16 1993 439 444 (Pubitemid 23313517)
    • (1993) Trends in Neurosciences , vol.16 , Issue.11 , pp. 439-444
    • Olanow, C.W.1
  • 20
    • 0031784348 scopus 로고    scopus 로고
    • Protein oxidative damage in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • P.K. Andrus, T.J. Fleck, M.E. Gurney, and E.D. Hall Protein oxidative damage in a transgenic mouse model of familial amyotrophic lateral sclerosis J. Neurochem. 71 1998 2041 2048 (Pubitemid 28491560)
    • (1998) Journal of Neurochemistry , vol.71 , Issue.5 , pp. 2041-2048
    • Andrus, P.K.1    Fleck, T.J.2    Gurney, M.E.3    Hall, E.D.4
  • 21
    • 0034237719 scopus 로고    scopus 로고
    • Energetics in the pathogenesis of neurodegenerative diseases
    • DOI 10.1016/S0166-2236(00)01584-8, PII S0166223600015848
    • M.F. Beal Energetics in the pathogenesis of neurodegenerative diseases Trends Neurosci. 23 2000 298 304 (Pubitemid 30387044)
    • (2000) Trends in Neurosciences , vol.23 , Issue.7 , pp. 298-304
    • Beal, M.F.1
  • 22
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • DOI 10.1016/S0891-5849(02)00780-3, PII S0891584902007803
    • M.F. Beal Oxidatively modified proteins in aging and disease Free Radic. Biol. Med. 32 2002 797 803 (Pubitemid 34439250)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.9 , pp. 797-803
    • Beal M.Flint1
  • 23
    • 0028153276 scopus 로고
    • Flavonoid antioxidants: Rate constants for reactions with oxygen radicals
    • W. Bors, C. Michel, and M. Saran Flavonoid antioxidants: rate constants for reactions with oxygen radicals Methods Enzymol. 234 1994 420 429
    • (1994) Methods Enzymol. , vol.234 , pp. 420-429
    • Bors, W.1    Michel, C.2    Saran, M.3
  • 26
    • 0033971898 scopus 로고    scopus 로고
    • Mitochondria and neuronal survival
    • D.G. Nicholls, and S.L. Budd Mitochondria and neuronal survival Physiol. Rev. 80 2000 315 360 (Pubitemid 30060567)
    • (2000) Physiological Reviews , vol.80 , Issue.1 , pp. 315-360
    • Nicholls, D.G.1    Budd, S.L.2
  • 27
    • 13844271387 scopus 로고    scopus 로고
    • Bioavailability and bioefficacy of polyphenols in humans. II. Review of 93 intervention studies
    • G. Williamson, and C. Manach Bioavailability and bioefficacy of polyphenols in humans. II. Review of 93 intervention studies Am. J. Clin. Nutr. 81 2005 243S 255S
    • (2005) Am. J. Clin. Nutr. , vol.81
    • Williamson, G.1    Manach, C.2
  • 28
    • 13844281685 scopus 로고    scopus 로고
    • Bioavailability and bioefficacy of polyphenols in humans. I. Review of 97 bioavailability studies
    • C. Manach, G. Williamson, C. Morand, A. Scalbert, and C. Rémésy Bioavailability and bioefficacy of polyphenols in humans. I. Review of 97 bioavailability studies Am. J. Clin. Nutr. 81 2005 230S 242S
    • (2005) Am. J. Clin. Nutr. , vol.81
    • Manach, C.1    Williamson, G.2    Morand, C.3    Scalbert, A.4    Rémésy, C.5
  • 29
    • 0031595920 scopus 로고    scopus 로고
    • 3H](-)-epigallocatechin gallate, a cancer preventive tea polyphenol, in mouse tissue
    • DOI 10.1093/carcin/19.10.1771
    • M. Suganuma, S. Okabe, M. Oniyama, Y. Tada, H. Ito, and H. Fujiki Wide distribution of [3H](-)-epigallocatechin gallate, a cancer preventive tea polyphenol, in mouse tissue Carcinogenesis 19 1998 1771 1776 (Pubitemid 28476352)
    • (1998) Carcinogenesis , vol.19 , Issue.10 , pp. 1771-1776
    • Suganuma, M.1    Okabe, S.2    Oniyama, M.3    Tada, Y.4    Ito, H.5    Fujiki, H.6
  • 34
    • 53249087817 scopus 로고    scopus 로고
    • Determination of baicalin in rat cerebrospinal fluid and blood using microdialysis coupled with ultra-performance liquid chromatography-tandem mass spectrometry
    • H. Huang, Y. Zhang, R. Yang, and X. Tang Determination of baicalin in rat cerebrospinal fluid and blood using microdialysis coupled with ultra-performance liquid chromatography-tandem mass spectrometry J. Chromatogr. B 874 2008 77 83
    • (2008) J. Chromatogr. B , vol.874 , pp. 77-83
    • Huang, H.1    Zhang, Y.2    Yang, R.3    Tang, X.4
  • 35
    • 0031840033 scopus 로고    scopus 로고
    • Determination of naringenin and its glucuronide conjugate in rat plasma and brain tissue by high-performance liquid chromatography
    • DOI 10.1016/S0378-4347(98)00204-7, PII S0378434798002047
    • H.W. Peng, F.C. Cheng, Y.T. Huang, C.F. Chen, and T.H. Tsai Determination of naringenin and its glucuronide conjugate in rat plasma and brain tissue by high-performance liquid chromatography J. Chromatogr. B: Biomed. Appl. 714 1998 369 374 (Pubitemid 28386860)
    • (1998) Journal of Chromatography B: Biomedical Applications , vol.714 , Issue.2 , pp. 369-374
    • Peng, H.W.1    Cheng, F.C.2    Huang, Y.T.3    Chen, C.F.4    Tsai, T.H.5
  • 36
    • 0034462079 scopus 로고    scopus 로고
    • Determination of unbound hesperetin in rat blood and brain by microdialysis coupled to microbore liquid chromatography
    • T.H. Tsai, and Y.F. Chen Determination of unbound hesperetin in rat blood and brain by microdialysis coupled to microbore liquid chromatography J. Food Drug Anal. 8 2000 331 336
    • (2000) J. Food Drug Anal. , vol.8 , pp. 331-336
    • Tsai, T.H.1    Chen, Y.F.2
  • 37
    • 0029056457 scopus 로고
    • In vivo and in vitro evidence for ATP-dependency of P-glycoprotein- mediated efflux of doxorubicin at the blood-brain barrier
    • T. Ohnishi, I. Tamai, K. Sakanaka, A. Sakata, T. Yamashima, J. Yamashita, and A. Tsuji In vivo and in vitro evidence for ATP-dependency of P-glycoprotein-mediated efflux of doxorubicin at the blood-brain barrier Biochem. Pharmacol. 49 1995 1541 1544
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 1541-1544
    • Ohnishi, T.1    Tamai, I.2    Sakanaka, K.3    Sakata, A.4    Yamashima, T.5    Yamashita, J.6    Tsuji, A.7
  • 38
    • 70449718818 scopus 로고    scopus 로고
    • The role of the blood-CNS barrier in CNS disorders and their treatment
    • A.M. Palmer The role of the blood-CNS barrier in CNS disorders and their treatment Neurobiol. Dis. 37 2010 3 12
    • (2010) Neurobiol. Dis. , vol.37 , pp. 3-12
    • Palmer, A.M.1
  • 40
    • 58849166492 scopus 로고    scopus 로고
    • Green tea epigallocatechin 3-gallate accumulates in mitochondria and displays a selective antiapoptotic effect against inducers of mitochondrial oxidative stress in neurons
    • E.K. Schroeder, N.A. Kelsey, J. Doyle, E. Breed, R.J. Bouchard, F.A. Loucks, R.A. Harbison, and D.A. Linseman Green tea epigallocatechin 3-gallate accumulates in mitochondria and displays a selective antiapoptotic effect against inducers of mitochondrial oxidative stress in neurons Antioxid. Redox Signal. 11 2009 469 480
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 469-480
    • Schroeder, E.K.1    Kelsey, N.A.2    Doyle, J.3    Breed, E.4    Bouchard, R.J.5    Loucks, F.A.6    Harbison, R.A.7    Linseman, D.A.8
  • 41
    • 77951498353 scopus 로고    scopus 로고
    • Mitochondria accumulate large amounts of quercetin: Prevention of mitochondrial damage and release upon oxidation of the extramitochondrial fraction of the flavonoid
    • M. Fiorani, A. Guidarelli, M. Blasa, C. Azzolini, M. Candiracci, E. Piatti, and O. Cantoni Mitochondria accumulate large amounts of quercetin: prevention of mitochondrial damage and release upon oxidation of the extramitochondrial fraction of the flavonoid J. Nutr. Biochem. 21 2010 397 404
    • (2010) J. Nutr. Biochem. , vol.21 , pp. 397-404
    • Fiorani, M.1    Guidarelli, A.2    Blasa, M.3    Azzolini, C.4    Candiracci, M.5    Piatti, E.6    Cantoni, O.7
  • 43
    • 0031839636 scopus 로고    scopus 로고
    • Effect of naturally occurring flavonoids on lipid peroxidation and membrane permeability transition in mitochondria
    • DOI 10.1016/S0891-5849(98)00003-3, PII S0891584998000033
    • A.C. Santos, S.A. Uyemura, J.L.C. Lopes, J.N. Bazon, F.E. Mingatto, and C. Curti Effect of naturally occurring flavonoids on lipid peroxidation and membrane permeability transition in mitochondria Free Radic. Biol. Med. 24 1998 1455 1461 (Pubitemid 28270347)
    • (1998) Free Radical Biology and Medicine , vol.24 , Issue.9 , pp. 1455-1461
    • Santos, A.C.1    Uyemura, S.A.2    Lopes, J.L.C.3    Bazon, J.N.4    Mingatto, F.E.5    Curti, C.6
  • 44
    • 0037010863 scopus 로고    scopus 로고
    • Interaction of genistein with the mitochondrial electron transport chain results in opening of the membrane transition pore
    • DOI 10.1016/S0005-2728(02)00361-4, PII S0005272802003614
    • M. Salvi, A.M. Brunati, G. Clari, and A. Toninello Interaction of genistein with the mitochondrial electron transport chain results in opening of the membrane transition pore Biochim. Biophys. Acta-Bioenergetics 1556 2002 187 196 (Pubitemid 35379677)
    • (2002) Biochimica et Biophysica Acta - Bioenergetics , vol.1556 , Issue.2-3 , pp. 187-196
    • Salvi, M.1    Brunati, A.M.2    Clari, G.3    Toninello, A.4
  • 45
    • 69249214137 scopus 로고    scopus 로고
    • Quercetin can act either as an inhibitor or an inducer of the mitochondrial permeability transition pore: A demonstration of the ambivalent redox character of polyphenols
    • U. De Marchi, L. Biasutto, S. Garbisa, A. Toninello, and M. Zoratti Quercetin can act either as an inhibitor or an inducer of the mitochondrial permeability transition pore: a demonstration of the ambivalent redox character of polyphenols Biochim. Biophys. Acta-Bioenergetics 1787 2009 1425 1432
    • (2009) Biochim. Biophys. Acta-Bioenergetics , vol.1787 , pp. 1425-1432
    • De Marchi, U.1    Biasutto, L.2    Garbisa, S.3    Toninello, A.4    Zoratti, M.5
  • 46
    • 63949084185 scopus 로고    scopus 로고
    • The flavonoid quercetin induces changes in mitochondrial permeability by inhibiting adenine nucleotide translocase
    • R. Ortega, and N. García The flavonoid quercetin induces changes in mitochondrial permeability by inhibiting adenine nucleotide translocase J. Bioenerg. Biomembr. 41 2009 41 47
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 41-47
    • Ortega, R.1    García, N.2
  • 47
    • 55249095521 scopus 로고    scopus 로고
    • Quercetin, kaempferol and biapigenin from hypericum perforatum are neuroprotective against excitotoxic insults
    • B. Silva, P.J. Oliveira, A. Dias, and J.O. Malva Quercetin, kaempferol and biapigenin from hypericum perforatum are neuroprotective against excitotoxic insults Neurotox. Res. 13 2008 265 279
    • (2008) Neurotox. Res. , vol.13 , pp. 265-279
    • Silva, B.1    Oliveira, P.J.2    Dias, A.3    Malva, J.O.4
  • 48
    • 0000514863 scopus 로고
    • Uncoupling activity of a series of flavones and flavonols on isolated plant mitochondria
    • P. Ravanel Uncoupling activity of a series of flavones and flavonols on isolated plant mitochondria Phytochemistry 25 1986 1015 1020
    • (1986) Phytochemistry , vol.25 , pp. 1015-1020
    • Ravanel, P.1
  • 49
    • 77953524436 scopus 로고    scopus 로고
    • Carcinoma cells activate AMP-activated protein kinase-dependent autophagy as survival response to kaempferol-mediated energetic impairment
    • G. Filomeni, E. Desideri, S. Cardaci, I. Graziani, S. Piccirillo, G. Rotilio, and M.R. Ciriolo Carcinoma cells activate AMP-activated protein kinase-dependent autophagy as survival response to kaempferol-mediated energetic impairment Autophagy 6 2010 202 216
    • (2010) Autophagy , vol.6 , pp. 202-216
    • Filomeni, G.1    Desideri, E.2    Cardaci, S.3    Graziani, I.4    Piccirillo, S.5    Rotilio, G.6    Ciriolo, M.R.7
  • 50
    • 0035884625 scopus 로고    scopus 로고
    • Flavonoids protect neurons from oxidized low-density-lipoprotein-induced apoptosis involving c-Jun N-terminal kinase (JNK), c-Jun and caspase-3
    • DOI 10.1042/0264-6021:3580547
    • H. Schroeter, J.P. Spencer, C. Rice-Evans, and R.J. Williams Flavonoids protect neurons from oxidized low-density-lipoprotein-induced apoptosis involving c-Jun N-terminal kinase (JNK), c-Jun and caspase-3 Biochem. J. 358 2001 547 557 (Pubitemid 32896942)
    • (2001) Biochemical Journal , vol.358 , Issue.3 , pp. 547-557
    • Schroeter, H.1    Spencer, J.P.E.2    Rice-Evans, C.3    Williams, R.J.4
  • 51
    • 0035865819 scopus 로고    scopus 로고
    • Flavonoids protect neuronal cells from oxidative stress by three distinct mechanisms
    • DOI 10.1016/S0891-5849(00)00498-6, PII S0891584900004986
    • K. Ishige, D. Schubert, and Y. Sagara Flavonoids protect neuronal cells from oxidative stress by three distinct mechanisms Free Radic. Biol. Med. 30 2001 433 446 (Pubitemid 32155542)
    • (2001) Free Radical Biology and Medicine , vol.30 , Issue.4 , pp. 433-446
    • Ishige, K.1    Schubert, D.2    Sagara, Y.3
  • 52
    • 2942596005 scopus 로고    scopus 로고
    • Kaempferol blocks oxidative stress in cerebellar granule cells and reveals a key role for reactive oxygen species production at the plasma membrane in the commitment to apoptosis
    • DOI 10.1016/j.freeradbiomed.2004.04.002, PII S0891584904003053
    • A.K. Samhan-Arias, F.J. Martin-Romero, and C. Gutierrez-Merino Kaempferol blocks oxidative stress in cerebellar granule cells and reveals a key role for reactive oxygen species production at the plasma membrane in the commitment to apoptosis Free Radic. Biol. Med. 37 2004 48 61 (Pubitemid 38746650)
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.1 , pp. 48-61
    • Samhan-Arias, A.K.1    Martin-Romero, F.J.2    Gutierrez-Merino, C.3
  • 53
    • 33747286388 scopus 로고    scopus 로고
    • Emerging role of polyphenolic compounds in the treatment of neurodegenerative diseases: A review of their intracellular targets
    • C. Ramassamy Emerging role of polyphenolic compounds in the treatment of neurodegenerative diseases: a review of their intracellular targets Eur. J. Pharmacol. 545 2006 51 64
    • (2006) Eur. J. Pharmacol. , vol.545 , pp. 51-64
    • Ramassamy, C.1
  • 54
    • 34548437268 scopus 로고    scopus 로고
    • Distinct mechanisms underlie distinct polyphenol-induced neuroprotection
    • DOI 10.1016/j.febslet.2006.11.011, PII S0014579306013275
    • K. Yazawa, T. Kihara, H. Shen, Y. Shimmyo, T. Niidome, and H. Sugimoto Distinct mechanisms underlie distinct polyphenol-induced neuroprotection FEBS Lett. 580 2006 6623 6628 (Pubitemid 44827019)
    • (2006) FEBS Letters , vol.580 , Issue.28-29 , pp. 6623-6628
    • Yazawa, K.1    Kihara, T.2    Shen, H.3    Shimmyo, Y.4    Niidome, T.5    Sugimoto, H.6
  • 56
    • 0031573401 scopus 로고    scopus 로고
    • A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: Applications in detecting the activity of phagocyte NADPH oxidase and other oxidases
    • DOI 10.1006/abio.1997.2391
    • M. Zhou, Z. Diwu, N. Panchuk-Voloshina, and R.P. Haugland A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases Anal. Biochem. 253 1997 162 168 (Pubitemid 27508167)
    • (1997) Analytical Biochemistry , vol.253 , Issue.2 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3    Haugland, R.P.4
  • 58
    • 0027484368 scopus 로고
    • Assay conditions for the mitochondrial NADH:coenzyme Q oxidoreductase
    • DOI 10.1016/0014-5793(93)80498-J
    • E. Estornell, R. Fato, F. Pallotti, and G. Lenaz Assay conditions for the mitochondrial NADH-Coenzyme-Q oxidoreductase FEBS Lett. 332 1993 127 131 (Pubitemid 23295913)
    • (1993) FEBS Letters , vol.332 , Issue.1-2 , pp. 127-131
    • Estornell, E.1    Fato, R.2    Pallotti, F.3    Lenaz, G.4
  • 59
    • 0029964226 scopus 로고    scopus 로고
    • Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines
    • I.A. Trounce, Y.L. Kim, A.S. Jun, and D.C. Wallace Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines Methods Enzymol. 264 1996 484 509
    • (1996) Methods Enzymol. , vol.264 , pp. 484-509
    • Trounce, I.A.1    Kim, Y.L.2    Jun, A.S.3    Wallace, D.C.4
  • 60
    • 0034740585 scopus 로고    scopus 로고
    • m-dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • DOI 10.1046/j.1471-4159.2001.00548.x
    • T.V. Votyakova, and I.J. Reynolds Delta psi(m)-dependent and -independent production of reactive oxygen species by rat brain mitochondria J. Neurochem. 79 2001 266 277 (Pubitemid 32988942)
    • (2001) Journal of Neurochemistry , vol.79 , Issue.2 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 61
    • 0042433242 scopus 로고    scopus 로고
    • 2 production by membrane potential and NAD(P)H redox state
    • 2 production by membrane potential and NAD(P)H redox state J. Neurochem. 86 2003 1101 1107 (Pubitemid 37022186)
    • (2003) Journal of Neurochemistry , vol.86 , Issue.5 , pp. 1101-1107
    • Starkov, A.A.1    Fiskum, G.2
  • 63
    • 63449131730 scopus 로고    scopus 로고
    • Quantification, localization, and tissue specificities of mouse mitochondrial reactive oxygen species production
    • A.M. Gusdon, J. Chen, T.V. Votyakova, and C.E. Mathews Quantification, localization, and tissue specificities of mouse mitochondrial reactive oxygen species production Methods Enzymol. 456 2009 439 457
    • (2009) Methods Enzymol. , vol.456 , pp. 439-457
    • Gusdon, A.M.1    Chen, J.2    Votyakova, T.V.3    Mathews, C.E.4
  • 64
    • 33845933196 scopus 로고    scopus 로고
    • Inhibition of horseradish peroxidase catalytic activity by new 3-phenylcoumarin derivatives: Synthesis and structure-activity relationships
    • DOI 10.1016/j.bmc.2006.10.068, PII S0968089606009114
    • L.M. Kabeya, A.A. de Marchi, A. Kanashiro, N.P. Lopes, C.H.T.P. da Silva, M.T. Pupo, and Y.M. Lucisano-Valim Inhibition of horseradish peroxidase catalytic activity by new 3-phenylcoumarin derivatives: synthesis and structure-activity relationships Bioorg. Med. Chem. 15 2007 1516 1524 (Pubitemid 46038124)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.3 , pp. 1516-1524
    • Kabeya, L.M.1    De Marchi, A.A.2    Kanashiro, A.3    Lopes, N.P.4    Da Silva, C.H.T.P.5    Pupo, M.T.6    Lucisano-Valim, Y.M.7
  • 65
    • 0019880605 scopus 로고
    • 2 generation in rat liver mitochondria by radical quenchers and phenolic compounds
    • 2 generation in rat liver mitochondria by radical quenchers and phenolic compounds Biochem. J. 194 1981 657 665
    • (1981) Biochem. J. , vol.194 , pp. 657-665
    • Swaroop, A.1    Ramasarma, T.2
  • 67
    • 0026095778 scopus 로고
    • Inhibition of mammalian 5-lipoxygenase and cyclo-oxygenase by flavonoids and phenolic dietary additives: Relationship to antioxidant activity and to iron ion-reducing ability
    • M.J. Laughton, P.J. Evans, M.A. Moroney, J.R.S. Hoult, and B. Halliwell Inhibition of mammalian 5-lipoxygenase and cyclo-oxygenase by flavonoids and phenolic dietary additives: relationship to antioxidant activity and to iron ion-reducing ability Biochem. Pharmacol. 42 1991 1673 1681
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 1673-1681
    • Laughton, M.J.1    Evans, P.J.2    Moroney, M.A.3    Hoult, J.R.S.4    Halliwell, B.5
  • 69
    • 37549011857 scopus 로고    scopus 로고
    • Mono-O-methylated flavanols and other flavonoids as inhibitors of endothelial NADPH oxidase
    • DOI 10.1016/j.abb.2007.10.012, PII S0003986107005139
    • Y. Steffen, C. Gruber, T. Schewe, and H. Sies Mono-O-methylated flavanols and other flavonoids as inhibitors of endothelial NADPH oxidase Arch. Biochem. Biophys. 469 2008 209 219 (Pubitemid 50008450)
    • (2008) Archives of Biochemistry and Biophysics , vol.469 , Issue.2 , pp. 209-219
    • Steffen, Y.1    Gruber, C.2    Schewe, T.3    Sies, H.4
  • 70
    • 67649378399 scopus 로고    scopus 로고
    • NAD(P)H- and superoxide-dependent nitric oxide degradation by rat liver mitochondria
    • H.C. Oliveira, E.E. Saviani, and I. Salgado NAD(P)H- and superoxide-dependent nitric oxide degradation by rat liver mitochondria FEBS Lett. 583 2009 2276 2280
    • (2009) FEBS Lett. , vol.583 , pp. 2276-2280
    • Oliveira, H.C.1    Saviani, E.E.2    Salgado, I.3
  • 71
    • 84856975752 scopus 로고    scopus 로고
    • Neuroprotection of kaempferol by autophagy in models of rotenone-mediated acute toxicity: Possible implications for Parkinson's disease
    • (in press), doi:10.1016/j.neurobiolaging.2010.05.021
    • G. Filomeni, I. Graziani, D. De Zio, L. Dini, D. Centonze, G. Rotilio, M.R. Ciriolo, Neuroprotection of kaempferol by autophagy in models of rotenone-mediated acute toxicity: possible implications for Parkinson's disease, Neurobiol. Aging (in press), doi:10.1016/j.neurobiolaging.2010.05.021.
    • Neurobiol. Aging
    • Filomeni, G.1    Graziani, I.2    De Zio, D.3    Dini, L.4    Centonze, D.5    Rotilio, G.6    Ciriolo, M.R.7
  • 72
    • 64549096768 scopus 로고    scopus 로고
    • Reduction of hydrophilic ubiquinones by the flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I) and production of reactive oxygen species
    • M.S. King, M.S. Sharpley, and J. Hirst Reduction of hydrophilic ubiquinones by the flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I) and production of reactive oxygen species Biochemistry 48 2009 2053 2062
    • (2009) Biochemistry , vol.48 , pp. 2053-2062
    • King, M.S.1    Sharpley, M.S.2    Hirst, J.3
  • 74
    • 0344820721 scopus 로고    scopus 로고
    • Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:Ubiquinone oxidoreductase)
    • DOI 10.1074/jbc.274.5.2625
    • J.G. Okun, P. Lümmen, and U. Brandt Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:Ubiquinone oxidoreductase) J. Biol. Chem. 274 1999 2625 2630 (Pubitemid 29075339)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.5 , pp. 2625-2630
    • Okun, J.G.1    Lummen, P.2    Brandt, U.3
  • 75
    • 60749121178 scopus 로고    scopus 로고
    • Characterization of the inhibitor binding site in mitochondrial NADH-ubiquinone oxidoreductase by photoaffinity labeling using a quinazoline-type inhibitor
    • M. Murai, K. Sekiguchi, T. Nishioka, and H. Miyoshi Characterization of the inhibitor binding site in mitochondrial NADH-ubiquinone oxidoreductase by photoaffinity labeling using a quinazoline-type inhibitor Biochemistry 48 2009 688 698
    • (2009) Biochemistry , vol.48 , pp. 688-698
    • Murai, M.1    Sekiguchi, K.2    Nishioka, T.3    Miyoshi, H.4
  • 76
    • 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 quinone-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
  • 79
    • 0034547969 scopus 로고    scopus 로고
    • Reactivity of semiquinones with ascorbate and the ascorbate radical as studied by pulse radiolysis
    • V. Roginsky, C. Michel, and W. Bors Reactivity of semiquinones with ascorbate and the ascorbate radical as studied by pulse radiolysis Arch. Biochem. Biophys. 384 2000 74 80
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 74-80
    • Roginsky, V.1    Michel, C.2    Bors, W.3
  • 80
    • 0031812255 scopus 로고    scopus 로고
    • Flavonoid deactivation of ferrylmyoglobin in relation to ease of oxidation as determined by cyclic voltammetry
    • L.V. Jørgensen, and L.H. Skibsted Flavonoid deactivation of ferrylmyoglobin in relation to ease of oxidation as determined by cyclic voltammetry Free. Radic. Res. 28 1998 335 351 (Pubitemid 28325580)
    • (1998) Free Radical Research , vol.28 , Issue.3 , pp. 335-351
    • Jorgensen, L.V.1    Skibsted, L.H.2
  • 82
    • 24644495344 scopus 로고    scopus 로고
    • Reduction potentials of flavonoid and model phenoxyl radicals. Which ring in flavonoids is responsible for antioxidant activity?
    • 6/01437B.
    • S.V. Jovanovic, S. Steenken, Y. Hara, and M.G. Simic Reduction potentials of flavonoid and model phenoxyl radicals. Which ring in flavonoids is responsible for antioxidant activity? J. Chem. Soc., Perkin Trans. 2 1996 2497 2504 (Pubitemid 126702005)
    • (1996) Journal of the Chemical Society. Perkin Transactions 2 , vol.0 , Issue.11 , pp. 2497-2504
    • Jovanovic, S.V.1    Steenken, S.2    Hara, Y.3    Simic, M.G.4
  • 84
    • 46349098382 scopus 로고    scopus 로고
    • Regulation of apoptosis by the redox state of cytochrome c
    • G.C. Brown, and V. Borutaite Regulation of apoptosis by the redox state of cytochrome c Biochim. Biophys. Acta-Bioenergetics 1777 2007 877 881
    • (2007) Biochim. Biophys. Acta-Bioenergetics , vol.1777 , pp. 877-881
    • Brown, G.C.1    Borutaite, V.2
  • 85
    • 36049033978 scopus 로고    scopus 로고
    • Blood micromolar concentrations of kaempferol afford protection against ischemia/reperfusion-induced damage in rat brain
    • DOI 10.1016/j.brainres.2007.08.087, PII S0006899307021336
    • C. López-Sánchez, F.J. Martín-Romero, F. Sun, L. Luis, A.K. Samhan-Arias, V. García-Martínez, and C. Gutierrez-Merino Blood micromolar concentrations of kaempferol afford protection against ischemia/reperfusion-induced damage in rat brain Brain Res. 1182 2007 123 137 (Pubitemid 350086989)
    • (2007) Brain Research , vol.1182 , Issue.1 , pp. 123-137
    • Lopez-Sanchez, C.1    Martin-Romero, F.J.2    Sun, F.3    Luis, L.4    Samhan-Arias, A.K.5    Garcia-Martinez, V.6    Gutierrez-Merino, C.7


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