메뉴 건너뛰기




Volumn 748, Issue , 2012, Pages 305-339

Cytochrome c oxidase and its role in neurodegeneration and neuroprotection

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE NUCLEOTIDE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALPHA TOCOPHEROL; ANTIOXIDANT; ASCORBIC ACID; BILOBALIDE; CYTOCHROME C OXIDASE; CYTOCHROME C OXIDASE IV 1; CYTOCHROME C OXIDASE IV 2; GINKGO BILOBA EXTRACT; GLUTATHIONE; HERBACEOUS AGENT; ISOENZYME; OXYGEN; REACTIVE OXYGEN METABOLITE; STEROID; TOXIN; UNCLASSIFIED DRUG;

EID: 84863751490     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4614-3573-0_13     Document Type: Article
Times cited : (62)

References (241)
  • 2
    • 0028871222 scopus 로고
    • Isoforms of yeast cytochrome c oxidase subunit v affect the binuclear reaction center and alter the kinetics of interaction with the isoforms of cytochrome c
    • Allen LA, Zhao XJ, Caughey W, Poyton RO (1995) Isoforms of yeast cytochrome c oxidase subunit V affect the binuclear reaction center and alter the kinetics of interaction with the isoforms of cytochrome c. J Biol Chem 270:110-118
    • (1995) J Biol Chem , vol.270 , pp. 110-118
    • Allen, L.A.1    Zhao, X.J.2    Caughey, W.3    Poyton, R.O.4
  • 3
    • 0024264842 scopus 로고
    • ATP-induced spectral changes in cytochrome c oxidase. A kinetic investigation
    • Antonini G, Malatesta F, Sarti P, Vallone B, Brunori M (1988) ATP-induced spectral changes in cytochrome c oxidase. A kinetic investigation. Biochem J 256:835-840
    • (1988) Biochem J , vol.256 , pp. 835-840
    • Antonini, G.1    Malatesta, F.2    Sarti, P.3    Vallone, B.4    Brunori, M.5
  • 4
    • 45549091568 scopus 로고    scopus 로고
    • Oestrogen influences on mitochondrial gene expression and respiratory chain activity in cortical and mesencephalic astrocytes
    • Araujo GW, Beyer C, Arnold S (2008) Oestrogen in fluences on mitochondrial gene expression and respiratory chain activity in cortical and mesencephalic astrocytes. J Neuroendocrinol 20:930-941
    • (2008) J Neuroendocrinol , vol.20 , pp. 930-941
    • Araujo, G.W.1    Beyer, C.2    Arnold, S.3
  • 5
    • 84856553941 scopus 로고    scopus 로고
    • The power of life - Cytochrome c oxidase takes center stage in metabolic control, cell signalling and survival
    • Arnold S (2012) The power of life - cytochrome c oxidase takes center stage in metabolic control, cell signalling and survival. Mitochondrion 12:46-56
    • (2012) Mitochondrion , vol.12 , pp. 46-56
    • Arnold, S.1
  • 6
    • 67449116583 scopus 로고    scopus 로고
    • Neuroprotection by estrogen in the brain: The mitochondrial compartment as presumed therapeutic target
    • Arnold S, Beyer C (2009) Neuroprotection by estrogen in the brain: the mitochondrial compartment as presumed therapeutic target. J Neurochem 110:1-11
    • (2009) J Neurochem , vol.110 , pp. 1-11
    • Arnold, S.1    Beyer, C.2
  • 7
    • 0030848050 scopus 로고    scopus 로고
    • Cell respiration is controlled by ATP, an allosteric inhibitor of cytochrome c oxidase
    • Arnold S, Kadenbach B (1997) Cell respiration is controlled by ATP, an allosteric inhibitor of cytochrome c oxidase. Eur J Biochem 249:350-354
    • (1997) Eur J Biochem , vol.249 , pp. 350-354
    • Arnold, S.1    Kadenbach, B.2
  • 8
    • 0033033002 scopus 로고    scopus 로고
    • The intramitochondrial ATP/ADP ratio controls cytochrome c oxidase activity allosterically
    • Arnold S, Kadenbach B (1999) The intramitochondrial ATP/ADP ratio controls cytochrome c oxidase activity allosterically. FEBS Lett 443:105-108
    • (1999) FEBS Lett , vol.443 , pp. 105-108
    • Arnold, S.1    Kadenbach, B.2
  • 9
    • 0032031485 scopus 로고    scopus 로고
    • 3,5-Diiodothyronine binds to subunit Va of cytochrome c oxidase and abolishes the allosteric inhibition of respiration by ATP
    • Arnold S, Goglia F, Kadenbach B (1998) 3,5-Diiodothyronine binds to subunit Va of cytochrome c oxidase and abolishes the allosteric inhibition of respiration by ATP. Eur J Biochem 252:325-330
    • (1998) Eur J Biochem , vol.252 , pp. 325-330
    • Arnold, S.1    Goglia, F.2    Kadenbach, B.3
  • 10
    • 57749118636 scopus 로고    scopus 로고
    • Gender-specific regulation of mitochondrial fusion and fission gene transcription and viability of cortical astrocytes by steroid hormones
    • Arnold S, de Ara'jo GW, Beyer C (2008) Gender-specific regulation of mitochondrial fusion and fission gene transcription and viability of cortical astrocytes by steroid hormones. J Mol Endocrinol 41:289-300
    • (2008) J Mol Endocrinol , vol.41 , pp. 289-300
    • Arnold, S.1    De Ara'Jo, G.W.2    Beyer, C.3
  • 11
    • 84859247743 scopus 로고    scopus 로고
    • Estrogen and the regulation of mitochondrial structure and function in the brain
    • in press
    • Arnold S, Victor MB, Beyer C (2012) Estrogen and the regulation of mitochondrial structure and function in the brain. J Steroid Biochem Mol Biol (in press)
    • (2012) J Steroid Biochem Mol Biol
    • Arnold, S.1    Victor, M.B.2    Beyer, C.3
  • 12
    • 33751103136 scopus 로고    scopus 로고
    • Heme binding to amyloid- b peptide: Mechanistic role in Alzheimer's disease
    • Atamna H (2006) Heme binding to amyloid- b peptide: mechanistic role in Alzheimer's disease. J Alzheimers Dis 10:255-266
    • (2006) J Alzheimers Dis , vol.10 , pp. 255-266
    • Atamna, H.1
  • 13
    • 70449449751 scopus 로고    scopus 로고
    • Amino acids variations in amyloid-beta peptides, mitochondrial dysfunction, and new therapies for Alzheimer's disease
    • Atamna H (2009) Amino acids variations in amyloid-beta peptides, mitochondrial dysfunction, and new therapies for Alzheimer's disease. J Bioenerg Biomembr 41:457-464
    • (2009) J Bioenerg Biomembr , vol.41 , pp. 457-464
    • Atamna, H.1
  • 14
    • 3342880690 scopus 로고    scopus 로고
    • A role for heme in Alzheimer's disease: Heme binds amyloid b and has altered metabolism
    • Atamna H, Frey WH II (2004) A role for heme in Alzheimer's disease: heme binds amyloid b and has altered metabolism. Proc Natl Acad Sci USA 101:11153-11158
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11153-11158
    • Atamna, H.1    Frey, W.H.I.I.2
  • 15
    • 52949119162 scopus 로고    scopus 로고
    • A peptide containing residues 26-44 of tau protein impairs mitochondrial oxidative phosphorylation acting at the level of the adenine nucleotide translocator
    • Atlante A, Amadoro G, Bobba A, de Bari L, Corsetti V, Pappalardo G, Marra E, Calissano P, Passarella S (2008) A peptide containing residues 26-44 of tau protein impairs mitochondrial oxidative phosphorylation acting at the level of the adenine nucleotide translocator. Biochim Biophys Acta 1777:1289-1300
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1289-1300
    • Atlante, A.1    Amadoro, G.2    Bobba, A.3    De Bari, L.4    Corsetti, V.5    Pappalardo, G.6    Marra, E.7    Calissano, P.8    Passarella, S.9
  • 16
    • 34249811232 scopus 로고    scopus 로고
    • Mitochondrial toxins and neurodegenerative diseases
    • Ayala A, Venero JL, Cano J, Machado A (2007) Mitochondrial toxins and neurodegenerative diseases. Front Biosci 12:986-1007
    • (2007) Front Biosci , vol.12 , pp. 986-1007
    • Ayala, A.1    Venero, J.L.2    Cano, J.3    MacHado, A.4
  • 17
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock GT, Wikstrom M (1992) Oxygen activation and the conservation of energy in cell respiration. Nature 356:301-309
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikstrom, M.2
  • 18
    • 34447498400 scopus 로고    scopus 로고
    • Tau aggregation and toxicity in a cell culture model of tauopathy
    • Bandyopadhyay B, Li G, Yin H, Kuret J (2007) Tau aggregation and toxicity in a cell culture model of tauopathy. J Biol Chem 282:16454-16464
    • (2007) J Biol Chem , vol.282 , pp. 16454-16464
    • Bandyopadhyay, B.1    Li, G.2    Yin, H.3    Kuret, J.4
  • 19
    • 68649108355 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in the limelight of Parkinson's disease pathogenesis
    • Banerjee R, Starkov AA, Beal MF, Thomas B (2009) Mitochondrial dysfunction in the limelight of Parkinson's disease pathogenesis. Biochim Biophys Acta 1792:651-663
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 651-663
    • Banerjee, R.1    Starkov, A.A.2    Beal, M.F.3    Thomas, B.4
  • 20
    • 0029125857 scopus 로고
    • Aging, energy, and oxidative stress in neurodegenerative diseases
    • Beal MF (1995) Aging, energy, and oxidative stress in neurodegenerative diseases. Ann Neurol 38:357-366
    • (1995) Ann Neurol , vol.38 , pp. 357-366
    • Beal, M.F.1
  • 21
    • 25444474703 scopus 로고    scopus 로고
    • Mitochondria take center stage in aging and neurodegeneration
    • Beal MF (2005) Mitochondria take center stage in aging and neurodegeneration. Ann Neurol 58:495-505
    • (2005) Ann Neurol , vol.58 , pp. 495-505
    • Beal, M.F.1
  • 22
    • 0035504324 scopus 로고    scopus 로고
    • Cytochrome c oxidase subunit Vb interacts with human androgen receptor: A potential mechanism for neurotoxicity in spinobulbar muscular atrophy
    • Beauchemin AMJ, Gottlieb B, Beitel LK, Elhaji YA, Pinsky L, Tri firo MA (2001) Cytochrome c oxidase subunit Vb interacts with human androgen receptor: a potential mechanism for neurotoxicity in spinobulbar muscular atrophy. Brain Res Bull 56:285-297
    • (2001) Brain Res Bull , vol.56 , pp. 285-297
    • Beauchemin, A.M.J.1    Gottlieb, B.2    Beitel, L.K.3    Elhaji, Y.A.4    Pinsky, L.5    Trifiro, M.A.6
  • 23
    • 0036137785 scopus 로고    scopus 로고
    • Regulation of cytochrome c oxidase by adenylic nucleotides. Is oxidative phosphorylation feedback regulated by its end-products?
    • Beauvoit B, Rigoulet M (2001) Regulation of cytochrome c oxidase by adenylic nucleotides. Is oxidative phosphorylation feedback regulated by its end-products? IUBMB Life 52:143-152
    • (2001) IUBMB Life , vol.52 , pp. 143-152
    • Beauvoit, B.1    Rigoulet, M.2
  • 24
    • 0026600596 scopus 로고
    • The mitochondrial electron transfer alteration as a factor involved in the brain aging
    • Benzi G, Pastoris O, Marzatico F, Villa RF, Dagani F, Curti D (1992) The mitochondrial electron transfer alteration as a factor involved in the brain aging. Neurobiol Aging 13:361-368
    • (1992) Neurobiol Aging , vol.13 , pp. 361-368
    • Benzi, G.1    Pastoris, O.2    Marzatico, F.3    Villa, R.F.4    Dagani, F.5    Curti, D.6
  • 25
    • 0015745743 scopus 로고
    • Brain dopamine and the syndromes of Parkinson and Huntington. Clinical, morphological and neurochemical correlations
    • Bernheimer H, Birkmayer W, Hornykiewicz O, Jellinger K, Seitelberger F (1973) Brain dopamine and the syndromes of Parkinson and Huntington. Clinical, morphological and neurochemical correlations. J Neurol Sci 20:415-455
    • (1973) J Neurol Sci , vol.20 , pp. 415-455
    • Bernheimer, H.1    Birkmayer, W.2    Hornykiewicz, O.3    Jellinger, K.4    Seitelberger, F.5
  • 26
  • 27
    • 0026666952 scopus 로고
    • Estrogen induction of cytochrome c oxidase subunit III in rat hippocampus
    • Bettini E, Maggi A (1992) Estrogen induction of cytochrome c oxidase subunit III in rat hippocampus. J Neurochem 58:1923-1929
    • (1992) J Neurochem , vol.58 , pp. 1923-1929
    • Bettini, E.1    Maggi, A.2
  • 28
    • 0023644754 scopus 로고
    • ATP induces conformational changes in mitochondrial cytochrome c oxidase. Effect on the cytochrome c binding site
    • Bisson R, Schiavo G, Montecucco C (1987) ATP induces conformational changes in mitochondrial cytochrome c oxidase. Effect on the cytochrome c binding site. J Biol Chem 262:5992-5998
    • (1987) J Biol Chem , vol.262 , pp. 5992-5998
    • Bisson, R.1    Schiavo, G.2    Montecucco, C.3
  • 29
    • 0028952832 scopus 로고
    • Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary culture
    • Bolanos JP, Heales SJR, Land JM, Clark JB (1995) Effect of peroxynitrite on the mitochondrial respiratory chain: differential susceptibility of neurones and astrocytes in primary culture. J Neurochem 64:1965-1972
    • (1995) J Neurochem , vol.64 , pp. 1965-1972
    • Bolanos, J.P.1    Heales, S.J.R.2    Land, J.M.3    Clark, J.B.4
  • 33
    • 0036231792 scopus 로고    scopus 로고
    • Cytochrome c oxidase and mitochondrial F1F0-ATPase (ATP synthase) activities in platelets and brain from patients with Alzheimer's disease
    • Bosetti F, Brizzi F, Barogi S, Mancuso M, Siciliano G, Tendi EA, Murri L, Rapoport SI, Solaini G (2002) Cytochrome c oxidase and mitochondrial F1F0-ATPase (ATP synthase) activities in platelets and brain from patients with Alzheimer's disease. Neurobiol Aging 23:371-376
    • (2002) Neurobiol Aging , vol.23 , pp. 371-376
    • Bosetti, F.1    Brizzi, F.2    Barogi, S.3    Mancuso, M.4    Siciliano, G.5    Tendi, E.A.6    Murri, L.7    Rapoport, S.I.8    Solaini, G.9
  • 34
    • 33947722245 scopus 로고    scopus 로고
    • Waiting to inhale: HIF-1 modulates aerobic respiration
    • Boutin AT, Johnson RS (2007) Waiting to inhale: HIF-1 modulates aerobic respiration. Cell 129:29-30
    • (2007) Cell , vol.129 , pp. 29-30
    • Boutin, A.T.1    Johnson, R.S.2
  • 35
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • Boveris A, Chance B (1973) The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem J 134:707-716
    • (1973) Biochem J , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 37
    • 80053632127 scopus 로고    scopus 로고
    • Gender- and brain region-specific role of cytochrome c oxidase in 1-methyl-4-phenylpyridinium-mediated astrocyte vulnerability
    • Boyalla SS, Victor MB, Roemgens A, Beyer C, Arnold S (2011) Gender- and brain region-specific role of cytochrome c oxidase in 1-methyl-4- phenylpyridinium-mediated astrocyte vulnerability. J Neurosci Res 89:2068-2082
    • (2011) J Neurosci Res , vol.89 , pp. 2068-2082
    • Boyalla, S.S.1    Victor, M.B.2    Roemgens, A.3    Beyer, C.4    Arnold, S.5
  • 38
    • 0021883670 scopus 로고
    • Regional mitochondrial respiratory activity in Huntington's disease brain
    • Brennan WA, Bird ED, Aprille JR (1985) Regional mitochondrial respiratory activity in Huntington's disease brain. J Neurochem 44:1948-1950
    • (1985) J Neurochem , vol.44 , pp. 1948-1950
    • Brennan, W.A.1    Bird, E.D.2    Aprille, J.R.3
  • 39
    • 52049083656 scopus 로고    scopus 로고
    • The healthy cell bias of estrogen action: Mitochondrial bioenergetics and neurological implications
    • Brinton RD (2008) The healthy cell bias of estrogen action: mitochondrial bioenergetics and neurological implications. Trends Neurosci 31:529-537
    • (2008) Trends Neurosci , vol.31 , pp. 529-537
    • Brinton, R.D.1
  • 41
    • 0032052215 scopus 로고    scopus 로고
    • Structure/function of oxygen-regulated isoforms in cytochrome c oxidase
    • Burke PV, Poyton RO (1998) Structure/function of oxygen-regulated isoforms in cytochrome c oxidase. J Exp Biol 201:1177-1195
    • (1998) J Exp Biol , vol.201 , pp. 1177-1195
    • Burke, P.V.1    Poyton, R.O.2
  • 42
    • 0017406503 scopus 로고
    • Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
    • Cadenas E, Boveris A, Ragan CI, Stoppani AO (1977) Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria. Arch Biochem Biophys 180:248-257
    • (1977) Arch Biochem Biophys , vol.180 , pp. 248-257
    • Cadenas, E.1    Boveris, A.2    Ragan, C.I.3    Stoppani, A.O.4
  • 43
    • 0032810909 scopus 로고    scopus 로고
    • Beta-Amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria
    • Canevari L, Clark JB, Bates TE (1999) Beta-Amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria. FEBS Lett 457:131-134
    • (1999) FEBS Lett , vol.457 , pp. 131-134
    • Canevari, L.1    Clark, J.B.2    Bates, T.E.3
  • 44
    • 0025322981 scopus 로고
    • Structure and function of cytochrome c oxidase
    • Capaldi RA (1990) Structure and function of cytochrome c oxidase. Annu Rev Biochem 59:569-596
    • (1990) Annu Rev Biochem , vol.59 , pp. 569-596
    • Capaldi, R.A.1
  • 46
    • 0031559896 scopus 로고    scopus 로고
    • Expression of a Cu, Zn superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca 2+ concentration in transfected neuroblastoma SH-SY5Y cells
    • Carri MT, Ferri A, Battistoni A, Famhy L, Gabbianelli R, Poccia F, Rotilio G (1997) Expression of a Cu, Zn superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca 2+ concentration in transfected neuroblastoma SH-SY5Y cells. FEBS Lett 414:365-368
    • (1997) FEBS Lett , vol.414 , pp. 365-368
    • Carri, M.T.1    Ferri, A.2    Battistoni, A.3    Famhy, L.4    Gabbianelli, R.5    Poccia, F.6    Rotilio, G.7
  • 47
    • 0028948660 scopus 로고
    • Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases
    • Chagnon P, Betard C, Robitaille Y, Cholette A, Gauvreau D (1995) Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases. Neuroreport 6:711-715
    • (1995) Neuroreport , vol.6 , pp. 711-715
    • Chagnon, P.1    Betard, C.2    Robitaille, Y.3    Cholette, A.4    Gauvreau, D.5
  • 48
    • 77049249588 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. III. The steady state
    • Chance B, Williams CR (1955) Respiratory enzymes in oxidative phosphorylation. III. The steady state. J Biol Chem 217:409-427
    • (1955) J Biol Chem , vol.217 , pp. 409-427
    • Chance, B.1    Williams, C.R.2
  • 49
    • 0032525344 scopus 로고    scopus 로고
    • Downregulation of oxidative phosphorylation in Alzheimer disease: Loss of cytochrome oxidase subunit mRNA in the hippocampus and entorhinal cortex
    • Chandrasekaran K, Hatanpaa K, Brady DR, Stoll J, Rapoport SI (1998) Downregulation of oxidative phosphorylation in Alzheimer disease: loss of cytochrome oxidase subunit mRNA in the hippocampus and entorhinal cortex. Brain Res 796:13-19
    • (1998) Brain Res , vol.796 , pp. 13-19
    • Chandrasekaran, K.1    Hatanpaa, K.2    Brady, D.R.3    Stoll, J.4    Rapoport, S.I.5
  • 50
    • 0034709545 scopus 로고    scopus 로고
    • Possible role of calpain in normal processing of betaamyloid precursor protein in human platelets
    • Chen M, Durr J, Fernandez HL (2000) Possible role of calpain in normal processing of betaamyloid precursor protein in human platelets. Biochem Biophys Res Commun 273:170-175
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 170-175
    • Chen, M.1    Durr, J.2    Fernandez, H.L.3
  • 51
    • 26944439050 scopus 로고    scopus 로고
    • Regulation of mitochondrial respiratory chain structure and function by estrogens/estrogen receptors and potential physiological/pathophysiological implications
    • Chen JQ, Yager JD, Russo J (2005) Regulation of mitochondrial respiratory chain structure and function by estrogens/estrogen receptors and potential physiological/pathophysiological implications. Biochim Biophys Acta 1746:1-17
    • (2005) Biochim Biophys Acta , vol.1746 , pp. 1-17
    • Chen, J.Q.1    Yager, J.D.2    Russo, J.3
  • 52
    • 69949092670 scopus 로고    scopus 로고
    • Regulation of mitochondrial respiratory chain biogenesis by estrogens/estrogen receptors and physiological, pathological and pharmacological implications
    • Chen JQ, Cammarata PR, Baines CP, Yager JD (2009) Regulation of mitochondrial respiratory chain biogenesis by estrogens/estrogen receptors and physiological, pathological and pharmacological implications. Biochim Biophys Acta 1793:1540-1570
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 1540-1570
    • Chen, J.Q.1    Cammarata, P.R.2    Baines, C.P.3    Yager, J.D.4
  • 53
    • 0032788739 scopus 로고    scopus 로고
    • Mitochondrial DNA and disease
    • Chinnery PF, Turnbull DM (1999) Mitochondrial DNA and disease. Lancet 354:17-21
    • (1999) Lancet , vol.354 , pp. 17-21
    • Chinnery, P.F.1    Turnbull, D.M.2
  • 55
    • 76049087222 scopus 로고    scopus 로고
    • Using a functional enzyme model to understand the chemistry behind hydrogen sul fide induced hibernation
    • Collman JP, Ghosh S, Dey A, Decreau RA (2009) Using a functional enzyme model to understand the chemistry behind hydrogen sul fide induced hibernation. Proc Natl Acad Sci USA 106:22090-22095
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 22090-22095
    • Collman, J.P.1    Ghosh, S.2    Dey, A.3    Decreau, R.A.4
  • 56
    • 0034663539 scopus 로고    scopus 로고
    • Effects of nitric oxide and peroxynitrite on the cytochrome oxidase Km for oxygen: Implications for mitochondrial pathology
    • Cooper CE, Davies NA (2000) Effects of nitric oxide and peroxynitrite on the cytochrome oxidase Km for oxygen: implications for mitochondrial pathology. Biochim Biophys Acta 1459:390-396
    • (2000) Biochim Biophys Acta , vol.1459 , pp. 390-396
    • Cooper, C.E.1    Davies, N.A.2
  • 59
    • 70450225376 scopus 로고    scopus 로고
    • Control of respiration by cytochrome c oxidase in intact cells: Role of the membrane potential
    • Dalmonte ME, Forte E, Genova ML, Giuffre A, Sarti P, Lenaz G (2009) Control of respiration by cytochrome c oxidase in intact cells: role of the membrane potential. J Biol Chem 284:32331-32335
    • (2009) J Biol Chem , vol.284 , pp. 32331-32335
    • Dalmonte, M.E.1    Forte, E.2    Genova, M.L.3    Giuffre, A.4    Sarti, P.5    Lenaz, G.6
  • 60
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer W, Przedborski S (2003) Parkinson's disease: mechanisms and models. Neuron 39:889-909
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 63
    • 0036451982 scopus 로고    scopus 로고
    • Bilobalide and neuroprotection
    • Defeudis FV (2002) Bilobalide and neuroprotection. Pharmacol Res 46:565-568
    • (2002) Pharmacol Res , vol.46 , pp. 565-568
    • Defeudis, F.V.1
  • 64
    • 0028841899 scopus 로고
    • The mitochondrion as a primary site of action of glucocorticoids: The interaction of the glucocorticoid receptor with mitochondrial DNA sequences showing partial similarity to the nuclear glucocorticoid responsive elements
    • Demonacos C, Djordjevic-Markovic R, Tsawdaroglou N, Sekeris CE (1995) The mitochondrion as a primary site of action of glucocorticoids: the interaction of the glucocorticoid receptor with mitochondrial DNA sequences showing partial similarity to the nuclear glucocorticoid responsive elements. J Steroid Biochem Mol Biol 55:43-55
    • (1995) J Steroid Biochem Mol Biol , vol.55 , pp. 43-55
    • Demonacos, C.1    Djordjevic-Markovic, R.2    Tsawdaroglou, N.3    Sekeris, C.E.4
  • 66
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction
    • Devi L, Prabhu BM, Galati DF, Avadhani NG, Anandatheerthavarada HK (2006) Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction. J Neurosci 26:9057-9068
    • (2006) J Neurosci , vol.26 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 67
    • 41249086496 scopus 로고    scopus 로고
    • Nuclear respiratory factor 1 regulates all ten nuclear encoded subunits of cytochrome c oxidase in neurons
    • Dhar SS, Ongwijitwat S, Wong-Riley MT (2008) Nuclear respiratory factor 1 regulates all ten nuclear encoded subunits of cytochrome c oxidase in neurons. J Biol Chem 283:3120-3129
    • (2008) J Biol Chem , vol.283 , pp. 3120-3129
    • Dhar, S.S.1    Ongwijitwat, S.2    Wong-Riley, M.T.3
  • 70
    • 0034278428 scopus 로고    scopus 로고
    • Gender differences in neurotoxicity of the nigrostriatal dopaminergic system: Implications for Parkinson's disease
    • Dluzen DE, McDermott JL (2000) Gender differences in neurotoxicity of the nigrostriatal dopaminergic system: implications for Parkinson's disease. J Gend Specif Med 3:36-42
    • (2000) J Gend Specif Med , vol.3 , pp. 36-42
    • Dluzen, D.E.1    McDermott, J.L.2
  • 71
    • 34249937901 scopus 로고    scopus 로고
    • Pink1, Parkin, DJ-1 and mitochondrial dysfunction in Parkinson's disease
    • Dodson MW, Guo M (2007) Pink1, Parkin, DJ-1 and mitochondrial dysfunction in Parkinson's disease. Curr Opin Neurobiol 17:331-337
    • (2007) Curr Opin Neurobiol , vol.17 , pp. 331-337
    • Dodson, M.W.1    Guo, M.2
  • 72
    • 52049104467 scopus 로고    scopus 로고
    • The mechanism of mitochondrial superoxide production by cytochrome bc1 complex
    • Drose S, Brandt U (2008) The mechanism of mitochondrial superoxide production by cytochrome bc1 complex. J Biol Chem 283:21649-21654
    • (2008) J Biol Chem , vol.283 , pp. 21649-21654
    • Drose, S.1    Brandt, U.2
  • 73
    • 25144513902 scopus 로고    scopus 로고
    • Development of 17alpha-estradiol as a neuroprotective therapeutic agent: Rationale and results from a phase i clinical study
    • Dykens JA, Moos WH, Howell N (2005) Development of 17alpha-estradiol as a neuroprotective therapeutic agent: rationale and results from a phase I clinical study. Ann N Y Acad Sci 1052:116-135
    • (2005) Ann N y Acad Sci , vol.1052 , pp. 116-135
    • Dykens, J.A.1    Moos, W.H.2    Howell, N.3
  • 75
    • 3543056130 scopus 로고    scopus 로고
    • Neurodegeneration and neuroprotection in Parkinson disease
    • Fahn S, Sulzer D (2004) Neurodegeneration and neuroprotection in Parkinson disease. NeuroRx 1:139-154
    • (2004) NeuroRx , vol.1 , pp. 139-154
    • Fahn, S.1    Sulzer, D.2
  • 76
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • Ferguson-Miller S, Babcock GT (1996) Heme/copper terminal oxidases. Chem Rev 96:2889-2908
    • (1996) Chem Rev , vol.96 , pp. 2889-2908
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 77
    • 77049108173 scopus 로고    scopus 로고
    • Sustained deficiency of mitochondrial complex i activity during long periods of survival after seizures induced in immature rats by homocysteic acid
    • Folbergrova J, Jesina P, Haugvicova R, Lisy V, Houst KJ (2010) Sustained deficiency of mitochondrial complex I activity during long periods of survival after seizures induced in immature rats by homocysteic acid. Neurochem Int 56:394-403
    • (2010) Neurochem Int , vol.56 , pp. 394-403
    • Folbergrova, J.1    Jesina, P.2    Haugvicova, R.3    Lisy, V.4    Houst, K.J.5
  • 78
    • 50949103793 scopus 로고    scopus 로고
    • The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal
    • Forman HJ, Fukuto JM, Miller T, Zhang H, Rinna A, Levy S (2008) The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal. Arch Biochem Biophys 477:183-195
    • (2008) Arch Biochem Biophys , vol.477 , pp. 183-195
    • Forman, H.J.1    Fukuto, J.M.2    Miller, T.3    Zhang, H.4    Rinna, A.5    Levy, S.6
  • 79
    • 0029670481 scopus 로고    scopus 로고
    • Regulation of the H + /e - -stoichiometry of cytochrome c oxidase from bovine heart by intraliposomal ATP/ADP ratios
    • Frank V, Kadenbach B (1996) Regulation of the H + /e - -stoichiometry of cytochrome c oxidase from bovine heart by intraliposomal ATP/ADP ratios. FEBS Lett 382:121-124
    • (1996) FEBS Lett , vol.382 , pp. 121-124
    • Frank, V.1    Kadenbach, B.2
  • 80
    • 77953357281 scopus 로고    scopus 로고
    • Ageing alters the supramolecular architecture of OxPhos complexes in rat brain cortex
    • Frenzel M, Rommelspacher H, Sugawa MD, Dencher NA (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
  • 81
    • 0029744863 scopus 로고    scopus 로고
    • Decreased cytochrome c oxidase activity but unchanged superoxide dismutase and glutathione peroxidase activities in the spinal cords of patients with amyotrophic lateral sclerosis
    • Fujita K, Yamauchi M, Shibayama K, Ando M, Honda M, Nagata Y (1996) Decreased cytochrome c oxidase activity but unchanged superoxide dismutase and glutathione peroxidase activities in the spinal cords of patients with amyotrophic lateral sclerosis. J Neurosci Res 45:276-281
    • (1996) J Neurosci Res , vol.45 , pp. 276-281
    • Fujita, K.1    Yamauchi, M.2    Shibayama, K.3    Ando, M.4    Honda, M.5    Nagata, Y.6
  • 82
    • 12744268421 scopus 로고    scopus 로고
    • Mitochondrial proteomic analysis of a cell line model of familial amyotrophic lateral sclerosis
    • Fukada K, Zhang F, Vien A, Cashman NR, Zhu H (2004) Mitochondrial proteomic analysis of a cell line model of familial amyotrophic lateral sclerosis. Mol Cell Proteomics 3:1211-1223
    • (2004) Mol Cell Proteomics , vol.3 , pp. 1211-1223
    • Fukada, K.1    Zhang, F.2    Vien, A.3    Cashman, N.R.4    Zhu, H.5
  • 83
    • 33947724515 scopus 로고    scopus 로고
    • HIF-1 regulates cytochrome c oxidase subunits to optimize efficiency of respiration in hypoxic cells
    • Fukuda R, Zhang H, Kim JW, Shimoda L, Dang CV, Semenza GL (2007) HIF-1 regulates cytochrome c oxidase subunits to optimize ef ficiency of respiration in hypoxic cells. Cell 129:111-122
    • (2007) Cell , vol.129 , pp. 111-122
    • Fukuda, R.1    Zhang, H.2    Kim, J.W.3    Shimoda, L.4    Dang, C.V.5    Semenza, G.L.6
  • 84
    • 42749087763 scopus 로고    scopus 로고
    • The mitochondrial impairment, oxidative stress and neurodegeneration connection: Reality or just an attractive hypothesis?
    • Fukui H, Moraes CT (2008) The mitochondrial impairment, oxidative stress and neurodegeneration connection: reality or just an attractive hypothesis? Trends Neurosci 31:251-256
    • (2008) Trends Neurosci , vol.31 , pp. 251-256
    • Fukui, H.1    Moraes, C.T.2
  • 86
    • 0036488133 scopus 로고    scopus 로고
    • Metabolic changes in the basal ganglia of patients with Huntington's disease: An in situ hybridization study of cytochrome oxidase subunit i mRNA
    • Gour finkel-An I, Vila M, Faucheux B, Duyckaerts C, Viallet F, Hauw JJ, Brice A, Agid Y, Hirsch EC (2002) Metabolic changes in the basal ganglia of patients with Huntington's disease: an in situ hybridization study of cytochrome oxidase subunit I mRNA. J Neurochem 80:466-476
    • (2002) J Neurochem , vol.80 , pp. 466-476
    • Gour Finkel-An, I.1    Vila, M.2    Faucheux, B.3    Duyckaerts, C.4    Viallet, F.5    Hauw, J.J.6    Brice, A.7    Agid, Y.8    Hirsch, E.C.9
  • 87
    • 0027198567 scopus 로고
    • Inhibition of succinate dehydrogenase by malonic acid produces an excitotoxic lesion in rat striatum
    • Greene JG, Porter RH, Eller RV, Greenamyre JT (1993) Inhibition of succinate dehydrogenase by malonic acid produces an excitotoxic lesion in rat striatum. J Neurochem 61:1151-1154
    • (1993) J Neurochem , vol.61 , pp. 1151-1154
    • Greene, J.G.1    Porter, R.H.2    Eller, R.V.3    Greenamyre, J.T.4
  • 88
    • 0020490497 scopus 로고
    • Quantification of the contribution of various steps to the control of mitochondrial respiration
    • Groen AK, Wanders RJA, Westerhoff HV, van der Meer R, Tager JM (1982) Quantification of the contribution of various steps to the control of mitochondrial respiration. J Biol Chem 257:2754-2757
    • (1982) J Biol Chem , vol.257 , pp. 2754-2757
    • Groen, A.K.1    Wanders, R.J.A.2    Westerhoff, H.V.3    Van Der Meer, R.4    Tager, J.M.5
  • 89
    • 0031004868 scopus 로고    scopus 로고
    • Nuclear genes for cytochrome c oxidase
    • Grossman LI, Lomax MI (1997) Nuclear genes for cytochrome c oxidase. Biochim Biophys Acta 1352:174-192
    • (1997) Biochim Biophys Acta , vol.1352 , pp. 174-192
    • Grossman, L.I.1    Lomax, M.I.2
  • 92
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell B (1992) Reactive oxygen species and the central nervous system. J Neurochem 59:1609-1623
    • (1992) J Neurochem , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 93
    • 0015319592 scopus 로고
    • The biologic clock: The mitochondria?
    • Harman D (1972) The biologic clock: the mitochondria? J Am Geriatr Soc 20:145-147
    • (1972) J Am Geriatr Soc , vol.20 , pp. 145-147
    • Harman, D.1
  • 94
    • 0031557163 scopus 로고    scopus 로고
    • The detection of nucleotide sequences with strong similarity to hormone responsive elements in the genome of eubacteria and archaebacteria and their possible relation to similar sequences present in the mitochondrial genome
    • Hatzoglou E, Sekeris CE (1997) The detection of nucleotide sequences with strong similarity to hormone responsive elements in the genome of eubacteria and archaebacteria and their possible relation to similar sequences present in the mitochondrial genome. J Theor Biol 184:339-344
    • (1997) J Theor Biol , vol.184 , pp. 339-344
    • Hatzoglou, E.1    Sekeris, C.E.2
  • 97
    • 55849122639 scopus 로고    scopus 로고
    • Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis
    • Henchcliffe C, Beal MF (2008) Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis. Nat Clin Pract Neurol 4:600-609
    • (2008) Nat Clin Pract Neurol , vol.4 , pp. 600-609
    • Henchcliffe, C.1    Beal, M.F.2
  • 98
    • 0025784931 scopus 로고
    • Comparison of energy-transducing capabilities of the two- and three-subunit cytochromes aa3 from Paracoccus denitrificans and the 13-subunit beef heart enzyme
    • Hendler RW, Pardhasaradhi K, Reynafarje B, Ludwig B (1991) Comparison of energy-transducing capabilities of the two- and three-subunit cytochromes aa3 from Paracoccus denitrificans and the 13-subunit beef heart enzyme. Biophys J 60:415-423
    • (1991) Biophys J , vol.60 , pp. 415-423
    • Hendler, R.W.1    Pardhasaradhi, K.2    Reynafarje, B.3    Ludwig, B.4
  • 99
    • 0024355783 scopus 로고
    • Brain cytochrome oxidase: Puri fication, antibody production, and immunohistochemical/histochemical correlations in the CNS
    • Hevner RF, Wong-Riley MTT (1989) Brain cytochrome oxidase: puri fication, antibody production, and immunohistochemical/histochemical correlations in the CNS. J Neurosci 9:3884-3898
    • (1989) J Neurosci , vol.9 , pp. 3884-3898
    • Hevner, R.F.1    Wong-Riley, M.T.T.2
  • 100
    • 0028883121 scopus 로고
    • A metabolic map of cytochrome oxidase in the rat brain: Histochemical, densitometric and biochemical studies
    • Hevner RF, Liu S, Wong-Riley MT (1995) A metabolic map of cytochrome oxidase in the rat brain: histochemical, densitometric and biochemical studies. Neuroscience 65:313-342
    • (1995) Neuroscience , vol.65 , pp. 313-342
    • Hevner, R.F.1    Liu, S.2    Wong-Riley, M.T.3
  • 103
    • 33750070935 scopus 로고    scopus 로고
    • Effect of hypoxia on the transcription pattern of subunit isoforms and the kinetics of cytochrome c oxidase in cortical astrocytes and cerebellar neurons
    • Horvat S, Beyer C, Arnold S (2006) Effect of hypoxia on the transcription pattern of subunit isoforms and the kinetics of cytochrome c oxidase in cortical astrocytes and cerebellar neurons. J Neurochem 99:937-951
    • (2006) J Neurochem , vol.99 , pp. 937-951
    • Horvat, S.1    Beyer, C.2    Arnold, S.3
  • 104
    • 33748422042 scopus 로고    scopus 로고
    • Upregulation of mitochondrial respiratory complex IV by estrogen receptor-beta is critical for inhibiting mitochondrial apoptotic signaling and restoring cardiac functions following traumahemorrhage
    • Hsieh YC, Yu HP, Suzuki T, Choudhry MA, Schwacha MG, Bland KI, Chaudry IH (2006) Upregulation of mitochondrial respiratory complex IV by estrogen receptor-beta is critical for inhibiting mitochondrial apoptotic signaling and restoring cardiac functions following traumahemorrhage. J Mol Cell Cardiol 41:511-521
    • (2006) J Mol Cell Cardiol , vol.41 , pp. 511-521
    • Hsieh, Y.C.1    Yu, H.P.2    Suzuki, T.3    Choudhry, M.A.4    Schwacha, M.G.5    Bland, K.I.6    Chaudry, I.H.7
  • 105
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • Huntington's Disease Collaborative Research Group
    • Huntington's Disease Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72:971-983
    • (1993) Cell , vol.72 , pp. 971-983
  • 106
    • 0035804655 scopus 로고    scopus 로고
    • Mammalian subunit IV isoforms of cytochrome c oxidase
    • Huttemann M, Kadenbach B, Grossman LI (2001) Mammalian subunit IV isoforms of cytochrome c oxidase. Gene 267:111-123
    • (2001) Gene , vol.267 , pp. 111-123
    • Huttemann, M.1    Kadenbach, B.2    Grossman, L.I.3
  • 107
    • 0042768716 scopus 로고    scopus 로고
    • Cytochrome c oxidase of mammals contains a testes-specific isoform of subunit VIb - The counterpart to testes-specific cytochrome c?
    • Huttemann M, Jaradat S, Grossman LI (2003a) Cytochrome c oxidase of mammals contains a testes-specific isoform of subunit VIb - the counterpart to testes-specific cytochrome c? Mol Reprod Dev 66:8-16
    • (2003) Mol Reprod Dev , vol.66 , pp. 8-16
    • Huttemann, M.1    Jaradat, S.2    Grossman, L.I.3
  • 108
    • 0141541807 scopus 로고    scopus 로고
    • A third isoform of cytochrome c oxidase subunit VIII is present in mammals
    • Huttemann M, Schmidt TR, Grossman LI (2003b) A third isoform of cytochrome c oxidase subunit VIII is present in mammals. Gene 312:95-102
    • (2003) Gene , vol.312 , pp. 95-102
    • Huttemann, M.1    Schmidt, T.R.2    Grossman, L.I.3
  • 109
    • 35448995703 scopus 로고    scopus 로고
    • Transcription of mammalian cytochrome c oxidase subunit IV-2 is controlled by a novel conserved oxygen responsive element
    • Huttemann M, Lee I, Liu J, Grossman LI (2007) Transcription of mammalian cytochrome c oxidase subunit IV-2 is controlled by a novel conserved oxygen responsive element. FEBS J 274:5737-5748
    • (2007) FEBS J , vol.274 , pp. 5737-5748
    • Huttemann, M.1    Lee, I.2    Liu, J.3    Grossman, L.I.4
  • 112
    • 0030294728 scopus 로고    scopus 로고
    • Cytochrome c oxidase defects of the human substantia nigra in normal aging
    • Itoh K, Weis S, Mehraein P, Muller-Hocker J (1996) Cytochrome c oxidase defects of the human substantia nigra in normal aging. Neurobiol Aging 17:843-848
    • (1996) Neurobiol Aging , vol.17 , pp. 843-848
    • Itoh, K.1    Weis, S.2    Mehraein, P.3    Muller-Hocker, J.4
  • 113
    • 0030780350 scopus 로고    scopus 로고
    • Copper/zinc superoxide dismutase 1 and sporadic amyotrophic lateral sclerosis: Analysis of 155 cases and Identification of an ovelinsertion mutation
    • Jackson M, Al-Chalabi A, Enayat ZE, Chioza B, Leigh PN, Morrison KE (1997) Copper/zinc superoxide dismutase 1 and sporadic amyotrophic lateral sclerosis: analysis of 155 cases and Identification of an ovelinsertion mutation. Ann Neurol 42:803-807
    • (1997) Ann Neurol , vol.42 , pp. 803-807
    • Jackson, M.1    Al-Chalabi, A.2    Enayat, Z.E.3    Chioza, B.4    Leigh, P.N.5    Morrison, K.E.6
  • 114
    • 77954697219 scopus 로고    scopus 로고
    • Oestrogen regulates mitochondrial respiratory chain enzyme transcription in the mouse spinal cord
    • Johann S, Dahm M, Kipp M, Beyer C, Arnold S (2010) Oestrogen regulates mitochondrial respiratory chain enzyme transcription in the mouse spinal cord. J Neuroendocrinol 22:926-935
    • (2010) J Neuroendocrinol , vol.22 , pp. 926-935
    • Johann, S.1    Dahm, M.2    Kipp, M.3    Beyer, C.4    Arnold, S.5
  • 115
    • 0022621176 scopus 로고
    • Regulation of respiration and ATP synthesis in higher organisms: Hypothesis
    • Kadenbach B (1986) Regulation of respiration and ATP synthesis in higher organisms: hypothesis. J Bioenerg Biomembr 18:39-54
    • (1986) J Bioenerg Biomembr , vol.18 , pp. 39-54
    • Kadenbach, B.1
  • 116
    • 0032970653 scopus 로고    scopus 로고
    • A second mechanism of respiratory control
    • Kadenbach B, Arnold S (1999) A second mechanism of respiratory control. FEBS Lett 447:131-134
    • (1999) FEBS Lett , vol.447 , pp. 131-134
    • Kadenbach, B.1    Arnold, S.2
  • 117
    • 7144231774 scopus 로고
    • Cytochrome c oxidase: Tissue-specific expression of isoforms and regulation of activity
    • Ernster L (ed) Elsevier, Amsterdam
    • Kadenbach B, Reimann A (1992) Cytochrome c oxidase: tissue-specific expression of isoforms and regulation of activity. In: Ernster L (ed) Molecular mechanisms in bioenergetics. Elsevier, Amsterdam, pp 241-263
    • (1992) Molecular Mechanisms in Bioenergetics , pp. 241-263
    • Kadenbach, B.1    Reimann, A.2
  • 118
    • 0020724790 scopus 로고
    • Separation of mammalian cytochrome c oxidase into 13 polypeptides by a sodium dodecyl sulfate-gel electrophoretic procedure
    • Kadenbach B, Jarausch J, Hartmann R, Merle P (1983) Separation of mammalian cytochrome c oxidase into 13 polypeptides by a sodium dodecyl sulfate-gel electrophoretic procedure. Anal Biochem 129:517-521
    • (1983) Anal Biochem , vol.129 , pp. 517-521
    • Kadenbach, B.1    Jarausch, J.2    Hartmann, R.3    Merle, P.4
  • 119
    • 0031799482 scopus 로고    scopus 로고
    • Regulation of energy transduction and electron transfer in cytochrome c oxidase by adenine nucleotides
    • Kadenbach B, Napiwotzki J, Frank V, Arnold S, Exner S, Huttemann M (1998) Regulation of energy transduction and electron transfer in cytochrome c oxidase by adenine nucleotides. J Bioenerg Biomembr 30:25-33
    • (1998) J Bioenerg Biomembr , vol.30 , pp. 25-33
    • Kadenbach, B.1    Napiwotzki, J.2    Frank, V.3    Arnold, S.4    Exner, S.5    Huttemann, M.6
  • 120
    • 0343714594 scopus 로고    scopus 로고
    • Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase
    • Kadenbach B, Huttemann M, Arnold S, Lee I, Bender E (2000) Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase. Free Radic Biol Med 29:211-221
    • (2000) Free Radic Biol Med , vol.29 , pp. 211-221
    • Kadenbach, B.1    Huttemann, M.2    Arnold, S.3    Lee, I.4    Bender, E.5
  • 121
    • 1942536167 scopus 로고    scopus 로고
    • The possible role of cytochrome c oxidase in stress- induced apoptosis and degenerative diseases
    • Kadenbach B, Arnold S, Lee I, Huttemann M (2004) The possible role of cytochrome c oxidase in stress- induced apoptosis and degenerative diseases. Biochim Biophys Acta 1655:400-408
    • (2004) Biochim Biophys Acta , vol.1655 , pp. 400-408
    • Kadenbach, B.1    Arnold, S.2    Lee, I.3    Huttemann, M.4
  • 122
    • 63449139296 scopus 로고    scopus 로고
    • Degenerative diseases, oxidative stress and cytochrome c oxidase function
    • Kadenbach B, Ramzan R, Vogt S (2009) Degenerative diseases, oxidative stress and cytochrome c oxidase function. Trends Mol Med 15:139-147
    • (2009) Trends Mol Med , vol.15 , pp. 139-147
    • Kadenbach, B.1    Ramzan, R.2    Vogt, S.3
  • 123
    • 76749091531 scopus 로고    scopus 로고
    • New extension of the Mitchell Theory for oxidative phosphorylation in mitochondria of living organisms
    • Kadenbach B, Ramzan R, Wen L, Vogt S (2010) New extension of the Mitchell Theory for oxidative phosphorylation in mitochondria of living organisms. Biochim Biophys Acta 1800:205-212
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 205-212
    • Kadenbach, B.1    Ramzan, R.2    Wen, L.3    Vogt, S.4
  • 124
    • 0033517144 scopus 로고    scopus 로고
    • ATP synthesis by F-type ATP synthase is obligatorily dependent on the transmembrane voltage
    • Kaim G, Dimroth P (1999) ATP synthesis by F-type ATP synthase is obligatorily dependent on the transmembrane voltage. EMBO J 18:4118-4127
    • (1999) EMBO J , vol.18 , pp. 4118-4127
    • Kaim, G.1    Dimroth, P.2
  • 125
    • 0028850087 scopus 로고
    • Suppression of mitochondrial succinate dehydrogenase, a primary target of beta-amyloid, and its derivative racemized at ser residue
    • Kaneko I, Yamada N, Sakuraba Y, Kamenosono M, Tutumi S (1995) Suppression of mitochondrial succinate dehydrogenase, a primary target of beta-amyloid, and its derivative racemized at Ser residue. J Neurochem 65:2585-2593
    • (1995) J Neurochem , vol.65 , pp. 2585-2593
    • Kaneko, I.1    Yamada, N.2    Sakuraba, Y.3    Kamenosono, M.4    Tutumi, S.5
  • 127
    • 0030962492 scopus 로고    scopus 로고
    • Nanomolar amyloid beta protein-induced inhibition of cellular redox activity in cultured astrocytes
    • Kato M, Saito H, Abe K (1997) Nanomolar amyloid beta protein-induced inhibition of cellular redox activity in cultured astrocytes. J Neurochem 68:1889-1895
    • (1997) J Neurochem , vol.68 , pp. 1889-1895
    • Kato, M.1    Saito, H.2    Abe, K.3
  • 128
    • 0022616654 scopus 로고
    • Alzheimer's disease
    • Katzman R (1986) Alzheimer's disease. N Engl J Med 314:964-973
    • (1986) N Engl J Med , vol.314 , pp. 964-973
    • Katzman, R.1
  • 131
    • 57349115353 scopus 로고    scopus 로고
    • Estrogenic control of mitochondrial function and biogenesis
    • Klinge CM (2008) Estrogenic control of mitochondrial function and biogenesis. J Cell Biochem 105:1342-1351
    • (2008) J Cell Biochem , vol.105 , pp. 1342-1351
    • Klinge, C.M.1
  • 132
    • 33646351299 scopus 로고    scopus 로고
    • Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons
    • Kraytsberg Y, Kudryavtseva E, McKee AC, Geula C, Kowall NW, Khrapko K (2006) Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons. Nat Genet 38:518-520
    • (2006) Nat Genet , vol.38 , pp. 518-520
    • Kraytsberg, Y.1    Kudryavtseva, E.2    McKee, A.C.3    Geula, C.4    Kowall, N.W.5    Khrapko, K.6
  • 133
    • 0032731637 scopus 로고    scopus 로고
    • ALS-linked Cu/Zn-SOD mutation increases vulnerability of motor neurons to excitotoxicity by a mechanism involving increased oxidative stress and perturbed calcium homeostasis
    • Kruman II, Pedersen WA, Springer JE, Mattson MP (1999) ALS-linked Cu/Zn-SOD mutation increases vulnerability of motor neurons to excitotoxicity by a mechanism involving increased oxidative stress and perturbed calcium homeostasis. Exp Neurol 160:28-39
    • (1999) Exp Neurol , vol.160 , pp. 28-39
    • Kruman, I.I.1    Pedersen, W.A.2    Springer, J.E.3    Mattson, M.P.4
  • 135
    • 0032052761 scopus 로고    scopus 로고
    • Oxygen sensing and transcriptional regulation of oxygenresponsive genes in yeast
    • Kwast KE, Burke PV, Poyton RO (1998) Oxygen sensing and transcriptional regulation of oxygenresponsive genes in yeast. J Exp Biol 201:1177-1195
    • (1998) J Exp Biol , vol.201 , pp. 1177-1195
    • Kwast, K.E.1    Burke, P.V.2    Poyton, R.O.3
  • 136
    • 0033545977 scopus 로고    scopus 로고
    • Oxygen sensing in yeast: Evidence for the involvement of the respiratory chain in regulating the transcription of a subset of hypoxic genes
    • Kwast KE, Burke PV, Staahl BT, Poyton RO (1999) Oxygen sensing in yeast: evidence for the involvement of the respiratory chain in regulating the transcription of a subset of hypoxic genes. Proc Natl Acad Sci USA 96:5446-5451
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5446-5451
    • Kwast, K.E.1    Burke, P.V.2    Staahl, B.T.3    Poyton, R.O.4
  • 137
    • 0000379911 scopus 로고
    • Oxidative phosphorylations; Role of inorganic phosphate and acceptor systems in control of metabolic rates
    • Lardy HA, Wellman H (1952) Oxidative phosphorylations; role of inorganic phosphate and acceptor systems in control of metabolic rates. J Biol Chem 195:215-224
    • (1952) J Biol Chem , vol.195 , pp. 215-224
    • Lardy, H.A.1    Wellman, H.2
  • 138
    • 0025800526 scopus 로고
    • Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy
    • LaSpada AR, Wilson EM, Lubahn DB, Harding AE, Fischbeck KH (1991) Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature 352:77-79
    • (1991) Nature , vol.352 , pp. 77-79
    • Laspada, A.R.1    Wilson, E.M.2    Lubahn, D.B.3    Harding, A.E.4    Fischbeck, K.H.5
  • 139
    • 0028349234 scopus 로고
    • Differential accumulations of 4,977 bp deletion in mitochondrial DNA of various tissues in human ageing
    • Lee HC, Pang CY, Hsu HS, Wei YH (1994) Differential accumulations of 4,977 bp deletion in mitochondrial DNA of various tissues in human ageing. Biochim Biophys Acta 1226:37-43
    • (1994) Biochim Biophys Acta , vol.1226 , pp. 37-43
    • Lee, H.C.1    Pang, C.Y.2    Hsu, H.S.3    Wei, Y.H.4
  • 140
    • 0035702819 scopus 로고    scopus 로고
    • New control of mitochondrial membrane potential and ROS formation - A hypothesis
    • Lee I, Bender E, Arnold S, Kadenbach B (2001) New control of mitochondrial membrane potential and ROS formation - a hypothesis. Biol Chem 382:1629-1636
    • (2001) Biol Chem , vol.382 , pp. 1629-1636
    • Lee, I.1    Bender, E.2    Arnold, S.3    Kadenbach, B.4
  • 142
    • 0027467531 scopus 로고
    • Control of oxidative phosphorylation in rat muscle mitochondria: Implications for mitochondrial myopathies
    • Letellier T, Malgat M, Mazat JP (1993) Control of oxidative phosphorylation in rat muscle mitochondria: implications for mitochondrial myopathies. Biochim Biophys Acta 1141:58-64
    • (1993) Biochim Biophys Acta , vol.1141 , pp. 58-64
    • Letellier, T.1    Malgat, M.2    Mazat, J.P.3
  • 143
    • 33845667921 scopus 로고    scopus 로고
    • Cytochrome c oxidase subunit IV is essential for assembly and respiratory function of the enzyme complex
    • Li Y, Park JS, Deng JH, Bai Y (2006) Cytochrome c oxidase subunit IV is essential for assembly and respiratory function of the enzyme complex. J Bioenerg Biomembr 38:283-291
    • (2006) J Bioenerg Biomembr , vol.38 , pp. 283-291
    • Li, Y.1    Park, J.S.2    Deng, J.H.3    Bai, Y.4
  • 145
    • 0024541837 scopus 로고
    • Mitochondrial DNA mutations as an important contributor to aging and degenerative diseases
    • Linnane AW, Marzuki S, Ozawa T, Tanaka M (1989) Mitochondrial DNA mutations as an important contributor to aging and degenerative diseases. Lancet 1:642-645
    • (1989) Lancet , vol.1 , pp. 642-645
    • Linnane, A.W.1    Marzuki, S.2    Ozawa, T.3    Tanaka, M.4
  • 149
    • 0023656624 scopus 로고
    • Modulation of cytochrome oxidase activity by inorganic and organic phosphate
    • Malatesta F, Antonini G, Sarti P, Brunori M (1987) Modulation of cytochrome oxidase activity by inorganic and organic phosphate. Biochem J 248:161-165
    • (1987) Biochem J , vol.248 , pp. 161-165
    • Malatesta, F.1    Antonini, G.2    Sarti, P.3    Brunori, M.4
  • 150
    • 2342628596 scopus 로고    scopus 로고
    • Differential expression of oxidative phosphorylation genes in patients with Alzheimer's disease: Implications for early mitochondrial dysfunction and oxidative damage
    • Manczak M, Park BS, Jung Y, Reddy PH (2004) Differential expression of oxidative phosphorylation genes in patients with Alzheimer's disease: implications for early mitochondrial dysfunction and oxidative damage. Neuromolecular Med 5:147-162
    • (2004) Neuromolecular Med , vol.5 , pp. 147-162
    • Manczak, M.1    Park, B.S.2    Jung, Y.3    Reddy, P.H.4
  • 151
    • 13244292394 scopus 로고    scopus 로고
    • Time-course of mitochondrial gene expressions in mice brains: Implications for mitochondrial dysfunction, oxidative damage, and cytochrome c in aging
    • Manczak M, Jung Y, Park BS, Partovi D, Reddy PH (2005) Time-course of mitochondrial gene expressions in mice brains: implications for mitochondrial dysfunction, oxidative damage, and cytochrome c in aging. J Neurochem 92:494-504
    • (2005) J Neurochem , vol.92 , pp. 494-504
    • Manczak, M.1    Jung, Y.2    Park, B.S.3    Partovi, D.4    Reddy, P.H.5
  • 153
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery WR (1997) Oxidative stress hypothesis in Alzheimer's disease. Free Radic Biol Med 23:134-147
    • (1997) Free Radic Biol Med , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 154
    • 0025232430 scopus 로고
    • Parkinson's disease
    • Marsden CD (1990) Parkinson's disease. Lancet 335:948-952
    • (1990) Lancet , vol.335 , pp. 948-952
    • Marsden, C.D.1
  • 157
    • 0034612075 scopus 로고    scopus 로고
    • A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients
    • Maurer I, Zierz S, Moller HJ (2000) A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients. Neurobiol Aging 21:455-462
    • (2000) Neurobiol Aging , vol.21 , pp. 455-462
    • Maurer, I.1    Zierz, S.2    Moller, H.J.3
  • 158
    • 47349104402 scopus 로고    scopus 로고
    • Glial reactions in Parkinson's disease
    • McGeer PL, McGeer EG (2008) Glial reactions in Parkinson's disease. Mov Disord 23:474-483
    • (2008) Mov Disord , vol.23 , pp. 474-483
    • McGeer, P.L.1    McGeer, E.G.2
  • 160
    • 77953872839 scopus 로고    scopus 로고
    • Gender-specific role of mitochondria in the vulnerability of 6-hydroxydopamine-treated mesencephalic neurons
    • Misiak M, Beyer C, Arnold S (2010a) Gender-specific role of mitochondria in the vulnerability of 6-hydroxydopamine-treated mesencephalic neurons. Biochim Biophys Acta 1797:1178-1188
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1178-1188
    • Misiak, M.1    Beyer, C.2    Arnold, S.3
  • 161
    • 77954353778 scopus 로고    scopus 로고
    • Brain region-specific vulnerability of astrocytes in response to 3-nitropropionic acid is mediated by cytochrome c oxidase isoform expression
    • Misiak M, Singh S, Drewlo S, Beyer C, Arnold S (2010b) Brain region-specific vulnerability of astrocytes in response to 3-nitropropionic acid is mediated by cytochrome c oxidase isoform expression. Cell Tissue Res 341:83-93
    • (2010) Cell Tissue Res , vol.341 , pp. 83-93
    • Misiak, M.1    Singh, S.2    Drewlo, S.3    Beyer, C.4    Arnold, S.5
  • 162
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism
    • Mitchell P (1961) Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism. Nature 191:144-148
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 165
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP (2009) How mitochondria produce reactive oxygen species. Biochem J 417:1-13
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 166
    • 0023221581 scopus 로고
    • Variable stoichiometry of proton pumping by the mitochondrial respiratory chain
    • Murphy MP, Brand MD (1987) Variable stoichiometry of proton pumping by the mitochondrial respiratory chain. Nature 329:170-172
    • (1987) Nature , vol.329 , pp. 170-172
    • Murphy, M.P.1    Brand, M.D.2
  • 167
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • Mutisya EM, Bowling AC, Beal MF (1994) Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J Neurochem 63:2179-2184
    • (1994) J Neurochem , vol.63 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 168
    • 0031924141 scopus 로고    scopus 로고
    • Extramitochondrial ATP/ADP-ratios regulate cytochrome c oxidase activity via binding to the cytosolic domain of subunit IV
    • Napiwotzki J, Kadenbach B (1998) Extramitochondrial ATP/ADP-ratios regulate cytochrome c oxidase activity via binding to the cytosolic domain of subunit IV. Biol Chem 379:335-339
    • (1998) Biol Chem , vol.379 , pp. 335-339
    • Napiwotzki, J.1    Kadenbach, B.2
  • 169
    • 0030770323 scopus 로고    scopus 로고
    • ATP and ADP bind to cytochrome c oxidase and regulate its activity
    • Napiwotzki J, Shinzawa-Itoh K, Yoshikawa S, Kadenbach B (1997) ATP and ADP bind to cytochrome c oxidase and regulate its activity. Biol Chem 378:1013-1021
    • (1997) Biol Chem , vol.378 , pp. 1013-1021
    • Napiwotzki, J.1    Shinzawa-Itoh, K.2    Yoshikawa, S.3    Kadenbach, B.4
  • 170
    • 6344289360 scopus 로고    scopus 로고
    • Rat brain and liver mitochondria develop oxidative stress and lose enzymatic activities on aging
    • Navarro A, Boveris A (2004) Rat brain and liver mitochondria develop oxidative stress and lose enzymatic activities on aging. Am J Physiol Regul Integr Comp Physiol 287:R1244-R1249
    • (2004) Am J Physiol Regul Integr Comp Physiol , vol.287
    • Navarro, A.1    Boveris, A.2
  • 171
    • 33847059997 scopus 로고    scopus 로고
    • The mitochondrial energy transduction system and the aging process
    • Navarro A, Boveris A (2007) The mitochondrial energy transduction system and the aging process. Am J Physiol Cell Physiol 292:670-686
    • (2007) Am J Physiol Cell Physiol , vol.292 , pp. 670-686
    • Navarro, A.1    Boveris, A.2
  • 173
    • 51649127553 scopus 로고    scopus 로고
    • Estradiol and neurodegenerative oxidative stress
    • Nilsen J (2008) Estradiol and neurodegenerative oxidative stress. Front Neuroendocrinol 29:463-475
    • (2008) Front Neuroendocrinol , vol.29 , pp. 463-475
    • Nilsen, J.1
  • 174
    • 38449089795 scopus 로고    scopus 로고
    • Estradiol in vivo regulation of brain mitochondrial proteome
    • Nilsen J, Irwin RW, Gallaher TK, Brinton RD (2007) Estradiol in vivo regulation of brain mitochondrial proteome. J Neurosci 27:14069-14077
    • (2007) J Neurosci , vol.27 , pp. 14069-14077
    • Nilsen, J.1    Irwin, R.W.2    Gallaher, T.K.3    Brinton, R.D.4
  • 175
    • 26444545461 scopus 로고    scopus 로고
    • Is nuclear respiratory factor 2 a master transcriptional coordinator for all ten nuclear-encoded cytochrome c oxidase subunits in neurons?
    • Ongwijitwat S, Wong-Riley MT (2005) Is nuclear respiratory factor 2 a master transcriptional coordinator for all ten nuclear-encoded cytochrome c oxidase subunits in neurons? Gene 360:65-77
    • (2005) Gene , vol.360 , pp. 65-77
    • Ongwijitwat, S.1    Wong-Riley, M.T.2
  • 176
    • 33646690296 scopus 로고    scopus 로고
    • Nuclear respiratory factor 2 senses changing cellular energy demands and its silencing down-regulates cytochrome oxidase and other target gene mRNAs
    • Ongwijitwat S, Liang HL, Graboyes EM, Wong-Riley MT (2006) Nuclear respiratory factor 2 senses changing cellular energy demands and its silencing down-regulates cytochrome oxidase and other target gene mRNAs. Gene 374:39-49
    • (2006) Gene , vol.374 , pp. 39-49
    • Ongwijitwat, S.1    Liang, H.L.2    Graboyes, E.M.3    Wong-Riley, M.T.4
  • 177
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment
    • Ostermeier C, Harrenga A, Ermler U, Michel H (1997) Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment. Proc Natl Acad Sci USA 94:10547-10553
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2    Ermler, U.3    Michel, H.4
  • 178
    • 0025910477 scopus 로고
    • The cytochrome chain of mitochondria exhibits variable H+/e - Stoichiometry
    • Papa S, Capitanio N, Capitanio G, De Nitto E, Minuto M (1991) The cytochrome chain of mitochondria exhibits variable H+/e - stoichiometry. FEBS Lett 288:183-186
    • (1991) FEBS Lett , vol.288 , pp. 183-186
    • Papa, S.1    Capitanio, N.2    Capitanio, G.3    De Nitto, E.4    Minuto, M.5
  • 179
    • 0025087726 scopus 로고
    • Evidence for a defect in NADH: Ubiquinone oxidoreductase (complex I) in Huntington's disease
    • Parker WD Jr, Boyson SJ, Luder AS, Parks JK (1990a) Evidence for a defect in NADH: ubiquinone oxidoreductase (complex I) in Huntington's disease. Neurology 40:1231-1234
    • (1990) Neurology , vol.40 , pp. 1231-1234
    • Parker Jr., W.D.1    Boyson, S.J.2    Luder, A.S.3    Parks, J.K.4
  • 180
    • 0025024024 scopus 로고
    • Cytochrome oxidase deficiency in Alzheimer's disease
    • Parker WD, Filley CM, Parks JK (1990b) Cytochrome oxidase deficiency in Alzheimer's disease. Neurology 40:1302-1303
    • (1990) Neurology , vol.40 , pp. 1302-1303
    • Parker, W.D.1    Filley, C.M.2    Parks, J.K.3
  • 182
    • 1642457265 scopus 로고    scopus 로고
    • Neuroenergetics: Calling upon astrocytes to satisfy hungry neurons
    • Pellerin L, Magistretti PJ (2004) Neuroenergetics: calling upon astrocytes to satisfy hungry neurons. Neuroscientist 10:53-62
    • (2004) Neuroscientist , vol.10 , pp. 53-62
    • Pellerin, L.1    Magistretti, P.J.2
  • 185
    • 77954760554 scopus 로고    scopus 로고
    • Mitochondrial respiration and membrane potential are regulated by the allosteric ATP-inhibition of cytochrome c oxidase
    • Ramzan R, Staniek K, Kadenbach B, Vogt S (2010) Mitochondrial respiration and membrane potential are regulated by the allosteric ATP-inhibition of cytochrome c oxidase. Biochim Biophys Acta 1797:1672-1680
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1672-1680
    • Ramzan, R.1    Staniek, K.2    Kadenbach, B.3    Vogt, S.4
  • 186
    • 39149122810 scopus 로고    scopus 로고
    • Amyloid beta, mitochondrial dysfunction and synaptic damage: Implication for cognitive decline in aging and Alzheimer's disease
    • Reddy PH, Beal MF (2008) Amyloid beta, mitochondrial dysfunction and synaptic damage: implication for cognitive decline in aging and Alzheimer's disease. Trends Mol Med 14:45-53
    • (2008) Trends Mol Med , vol.14 , pp. 45-53
    • Reddy, P.H.1    Beal, M.F.2
  • 188
    • 0023802001 scopus 로고
    • Anions induce conformational changes and in fluence the activity and photoaf finity labeling by 8-azido-ATP of isolated cytochrome c oxidase
    • Reimann A, Huther FJ, Berden JA, Kadenbach B (1988) Anions induce conformational changes and in fluence the activity and photoaf finity labeling by 8-azido-ATP of isolated cytochrome c oxidase. Biochem J 254:835-840
    • (1988) Biochem J , vol.254 , pp. 835-840
    • Reimann, A.1    Huther, F.J.2    Berden, J.A.3    Kadenbach, B.4
  • 189
    • 77952548782 scopus 로고    scopus 로고
    • How increase oxidative stress promotes longevity and metabolic health: The concept of mitochondrial hormesis (mitohormesis)
    • Ristow M, Zarse K (2010) How increase oxidative stress promotes longevity and metabolic health: the concept of mitochondrial hormesis (mitohormesis). Exp Gerontol 45:410-418
    • (2010) Exp Gerontol , vol.45 , pp. 410-418
    • Ristow, M.1    Zarse, K.2
  • 191
    • 79958081676 scopus 로고    scopus 로고
    • Inducers of chemical hypoxia act in a genderand brain region-specific manner on primary astrocyte viability and cytochrome c oxidase
    • Roemgens A, Singh S, Beyer C, Arnold S (2010) Inducers of chemical hypoxia act in a genderand brain region-specific manner on primary astrocyte viability and cytochrome c oxidase. Neurotox Res 20:1-14
    • (2010) Neurotox Res , vol.20 , pp. 1-14
    • Roemgens, A.1    Singh, S.2    Beyer, C.3    Arnold, S.4
  • 193
    • 0030019414 scopus 로고    scopus 로고
    • Ultrastructural study of synapses in the anterior horn neurons of patients with amyotrophic lateral sclerosis
    • Sasaki S, Iwata M (1996) Ultrastructural study of synapses in the anterior horn neurons of patients with amyotrophic lateral sclerosis. Neurosci Lett 204:53-56
    • (1996) Neurosci Lett , vol.204 , pp. 53-56
    • Sasaki, S.1    Iwata, M.2
  • 194
    • 33846087291 scopus 로고    scopus 로고
    • Mitochondrial alterations in the spinal cord of patients with sporadic amyotrophic lateral sclerosis
    • Sasaki S, Iwata M (2007) Mitochondrial alterations in the spinal cord of patients with sporadic amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 66:10-16
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 10-16
    • Sasaki, S.1    Iwata, M.2
  • 195
    • 0028869597 scopus 로고
    • Human diseases with defects in oxidative phosphorylation. 2. F1F0- ATP synthase defects in Alzheimer disease revealed by blue native polyacrylamide gel electrophoresis (PAGE)
    • Schagger H, Ohm TG (1995) Human diseases with defects in oxidative phosphorylation. 2. F1F0- ATP synthase defects in Alzheimer disease revealed by blue native polyacrylamide gel electrophoresis (PAGE). Eur J Biochem 227:916-921
    • (1995) Eur J Biochem , vol.227 , pp. 916-921
    • Schagger, H.1    Ohm, T.G.2
  • 196
    • 0029743756 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial dysfunction in neurodegeneration
    • Schapira AH (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
  • 197
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval R, Shvets E, Fass E, Shorer H, Gil L, Elazar Z (2007) Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J 26:1749-1760
    • (2007) EMBO J , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5    Elazar, Z.6
  • 198
    • 0025639020 scopus 로고
    • The mitochondrial genome: A possible primary site of action of steroid hormones
    • Sekeris CE (1990) The mitochondrial genome: a possible primary site of action of steroid hormones. In Vivo 4:317-320
    • (1990) In Vivo , vol.4 , pp. 317-320
    • Sekeris, C.E.1
  • 199
    • 0029040824 scopus 로고
    • The intracellular component of cellular 3-(4,5-dimethylthiazol- 2-yl)-2, 5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by beta-amyloid peptides
    • Shearman MS, Hawtin SR, Tailor VJ (1995) The intracellular component of cellular 3-(4,5-dimethylthiazol- 2-yl)-2, 5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by beta-amyloid peptides. J Neurochem 65:218-227
    • (1995) J Neurochem , vol.65 , pp. 218-227
    • Shearman, M.S.1    Hawtin, S.R.2    Tailor, V.J.3
  • 200
    • 60849096071 scopus 로고    scopus 로고
    • Increased vulnerability of brain to estrogen withdrawal-induced mitochondrial dysfunction with aging
    • Shi C, Xu J (2008) Increased vulnerability of brain to estrogen withdrawal-induced mitochondrial dysfunction with aging. J Bioenerg Biomembr 40:625-630
    • (2008) J Bioenerg Biomembr , vol.40 , pp. 625-630
    • Shi, C.1    Xu, J.2
  • 201
    • 40649107161 scopus 로고    scopus 로고
    • Possible role of mitochondrial dysfunction in central neurodegeneration of ovariectomized rats
    • Shi C, Xu XW, Forster EL, Tang LF, Ge Z, Yew DT, Xu J (2008) Possible role of mitochondrial dysfunction in central neurodegeneration of ovariectomized rats. Cell Biochem Funct 26:172-178
    • (2008) Cell Biochem Funct , vol.26 , pp. 172-178
    • Shi, C.1    Xu, X.W.2    Forster, E.L.3    Tang, L.F.4    Ge, Z.5    Yew, D.T.6    Xu, J.7
  • 203
    • 34250378592 scopus 로고    scopus 로고
    • Gender differences in Parkinson's disease
    • Shulman LM (2007) Gender differences in Parkinson's disease. Gend Med 4:8-18
    • (2007) Gend Med , vol.4 , pp. 8-18
    • Shulman, L.M.1
  • 204
    • 0030026832 scopus 로고    scopus 로고
    • Ultrastructural evidence for altered calcium in motor nerve terminals in amyotropic lateral sclerosis
    • Siklos L, Engelhardt J, Harati Y, Smith RG, Joo F, Appel SH (1996) Ultrastructural evidence for altered calcium in motor nerve terminals in amyotropic lateral sclerosis. Ann Neurol 39:203-216
    • (1996) Ann Neurol , vol.39 , pp. 203-216
    • Siklos, L.1    Engelhardt, J.2    Harati, Y.3    Smith, R.G.4    Joo, F.5    Appel, S.H.6
  • 205
    • 0026471872 scopus 로고
    • Accumulation of deletions in human mitochondrial DNA during normal aging: Analysis by quantitative PCR
    • Simonetti S, Chen X, DiMauro S, Schon EA (1992) Accumulation of deletions in human mitochondrial DNA during normal aging: analysis by quantitative PCR. Biochim Biophys Acta 1180:113-122
    • (1992) Biochim Biophys Acta , vol.1180 , pp. 113-122
    • Simonetti, S.1    Chen, X.2    Dimauro, S.3    Schon, E.A.4
  • 206
    • 0028023533 scopus 로고
    • Functional alterations in Alzheimer's disease: Selective loss of mitochondrial-encoded cytochrome oxidase mRNA in the hippocampal formation
    • Simonian NA, Hyman BT (1994) Functional alterations in Alzheimer's disease: selective loss of mitochondrial-encoded cytochrome oxidase mRNA in the hippocampal formation. J Neuropathol Exp Neurol 53:508-512
    • (1994) J Neuropathol Exp Neurol , vol.53 , pp. 508-512
    • Simonian, N.A.1    Hyman, B.T.2
  • 207
    • 40749118030 scopus 로고    scopus 로고
    • Mitochondrial mechanisms of estrogen neuroprotection
    • Simpkins JW, Dykens JA (2008) Mitochondrial mechanisms of estrogen neuroprotection. Brain Res Rev 57:421-430
    • (2008) Brain Res Rev , vol.57 , pp. 421-430
    • Simpkins, J.W.1    Dykens, J.A.2
  • 210
    • 70450220248 scopus 로고    scopus 로고
    • Cytochrome c oxidase isoform IV-2 is involved in 3-nitropropionic acid-induced toxicity in striatal astrocytes
    • Singh S, Misiak M, Beyer C, Arnold S (2009) Cytochrome c oxidase isoform IV-2 is involved in 3-nitropropionic acid-induced toxicity in striatal astrocytes. Glia 57:1480-1491
    • (2009) Glia , vol.57 , pp. 1480-1491
    • Singh, S.1    Misiak, M.2    Beyer, C.3    Arnold, S.4
  • 211
    • 77955093673 scopus 로고    scopus 로고
    • Brain region specificity of 3-nitropropionic acidinduced vulnerability of neurons involves cytochrome c oxidase
    • Singh S, Misiak M, Beyer C, Arnold S (2010) Brain region specificity of 3-nitropropionic acidinduced vulnerability of neurons involves cytochrome c oxidase. Neurochem Int 57:297-305
    • (2010) Neurochem Int , vol.57 , pp. 297-305
    • Singh, S.1    Misiak, M.2    Beyer, C.3    Arnold, S.4
  • 212
    • 0027021442 scopus 로고
    • Mosaicism for a specific somatic mitochondrial DNA mutation in adult human brain
    • Soong NW, Hinton DR, Cortopassi G, Arnheim N (1992) Mosaicism for a specific somatic mitochondrial DNA mutation in adult human brain. Nat Genet 2:318-323
    • (1992) Nat Genet , vol.2 , pp. 318-323
    • Soong, N.W.1    Hinton, D.R.2    Cortopassi, G.3    Arnheim, N.4
  • 213
    • 25144524774 scopus 로고    scopus 로고
    • Estrogen increases mitochondrial ef ficiency and reduces oxidative stress in cerebral blood vessels
    • Stirone C, Duckles SP, Krause DN, Procaccio V (2005) Estrogen increases mitochondrial ef ficiency and reduces oxidative stress in cerebral blood vessels. Mol Pharmacol 68:959-965
    • (2005) Mol Pharmacol , vol.68 , pp. 959-965
    • Stirone, C.1    Duckles, S.P.2    Krause, D.N.3    Procaccio, V.4
  • 218
    • 77950890499 scopus 로고    scopus 로고
    • Nitric oxide, cytochrome C oxidase, and the cellular response to hypoxia
    • Taylor CT, Moncada S (2010) Nitric oxide, cytochrome C oxidase, and the cellular response to hypoxia. Arterioscler Thromb Vasc Biol 30:643-647
    • (2010) Arterioscler Thromb Vasc Biol , vol.30 , pp. 643-647
    • Taylor, C.T.1    Moncada, S.2
  • 222
    • 0031029962 scopus 로고    scopus 로고
    • In vivo control of respiration by cytochrome c oxidase in wild-type and mitochondrial DNA mutation-carrying human cells
    • Villani G, Attardi G (1997) In vivo control of respiration by cytochrome c oxidase in wild-type and mitochondrial DNA mutation-carrying human cells. Proc Natl Acad Sci USA 94:1166-1171
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1166-1171
    • Villani, G.1    Attardi, G.2
  • 223
    • 0033795824 scopus 로고    scopus 로고
    • In vivo control of respiration by cytochrome c oxidase in human cells
    • Villani G, Attardi G (2000) In vivo control of respiration by cytochrome c oxidase in human cells. Free Radic Biol Med 29:202-210
    • (2000) Free Radic Biol Med , vol.29 , pp. 202-210
    • Villani, G.1    Attardi, G.2
  • 224
    • 0033610865 scopus 로고    scopus 로고
    • Low reserve of cytochrome c oxidase capacity in vivo in the respiratory chain of a variety of human cell types
    • Villani G, Greco M, Papa S, Attardi G (1998) Low reserve of cytochrome c oxidase capacity in vivo in the respiratory chain of a variety of human cell types. J Biol Chem 273:31829-31836
    • (1998) J Biol Chem , vol.273 , pp. 31829-31836
    • Villani, G.1    Greco, M.2    Papa, S.3    Attardi, G.4
  • 225
    • 0028011017 scopus 로고
    • Activation of the human mitochondrial transcription factor A gene by nuclear respiratory factors: A potential regulatory link between nuclear and mitochondrial gene expression in organelle biogenesis
    • Virbasius JV, Scarpulla RC (1994) Activation of the human mitochondrial transcription factor A gene by nuclear respiratory factors: a potential regulatory link between nuclear and mitochondrial gene expression in organelle biogenesis. Proc Natl Acad Sci USA 91:1309-1313
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1309-1313
    • Virbasius, J.V.1    Scarpulla, R.C.2
  • 226
  • 228
    • 0027164617 scopus 로고
    • Regionally specific loss of neurons in the aging human hippocampus
    • West MJ (1993) Regionally specific loss of neurons in the aging human hippocampus. Neurobiol Aging 14:287-293
    • (1993) Neurobiol Aging , vol.14 , pp. 287-293
    • West, M.J.1
  • 229
    • 0028122463 scopus 로고
    • Differences in the pattern of hippocampal neuronal loss in normal ageing and Alzheimer's disease
    • West M, Coleman P, Flood D, Tronsco J (1994) Differences in the pattern of hippocampal neuronal loss in normal ageing and Alzheimer's disease. Lancet 344:769-772
    • (1994) Lancet , vol.344 , pp. 769-772
    • West, M.1    Coleman, P.2    Flood, D.3    Tronsco, J.4
  • 231
    • 0028030571 scopus 로고
    • The primary oxygen sensor of the cat carotoid body is cytochrome a3 of the mitochondrial respiratory chain
    • Wilson DF, Mokashi A, Chugh D, Vinogradov S, Osanai S, Lahiri S (1994) The primary oxygen sensor of the cat carotoid body is cytochrome a3 of the mitochondrial respiratory chain. FEBS Lett 351:370-374
    • (1994) FEBS Lett , vol.351 , pp. 370-374
    • Wilson, D.F.1    Mokashi, A.2    Chugh, D.3    Vinogradov, S.4    Osanai, S.5    Lahiri, S.6
  • 232
    • 0024561501 scopus 로고
    • Cytochrome oxidase: An endogenous metabolic marker for neuronal activity
    • Wong-Riley MTT (1989) Cytochrome oxidase: an endogenous metabolic marker for neuronal activity. Trends Neurosci 12:94-101
    • (1989) Trends Neurosci , vol.12 , pp. 94-101
    • Wong-Riley, M.T.T.1
  • 233
    • 0030830677 scopus 로고    scopus 로고
    • Cytochrome oxidase in Alzheimer's disease: Biochemical, histochemical, and immunohistochemical analyses of the visual and other systems
    • Wong-Riley M, Antuono P, Ho KC, Egan R, Hevner R, Liebl W, Huang Z, Rachel R, Jones J (1997) Cytochrome oxidase in Alzheimer's disease: biochemical, histochemical, and immunohistochemical analyses of the visual and other systems. Vision Res 37:3593-3608
    • (1997) Vision Res , vol.37 , pp. 3593-3608
    • Wong-Riley, M.1    Antuono, P.2    Ho, K.C.3    Egan, R.4    Hevner, R.5    Liebl, W.6    Huang, Z.7    Rachel, R.8    Jones, J.9
  • 236
    • 0031745229 scopus 로고    scopus 로고
    • Crystal structure of bovine heart cytochrome c oxidase at 2.8 A resolution
    • Yoshikawa S, Shinzawa-Itoh K, Tsukihara T (1998) Crystal structure of bovine heart cytochrome c oxidase at 2.8 A resolution. J Bioenerg Biomembr 30:7-14
    • (1998) J Bioenerg Biomembr , vol.30 , pp. 7-14
    • Yoshikawa, S.1    Shinzawa-Itoh, K.2    Tsukihara, T.3
  • 237
    • 1642464725 scopus 로고    scopus 로고
    • Genistein ameliorates beta-amyloid peptide (25-35)-induced hippocampal neuronal apoptosis
    • Zeng H, Chen Q, Zhao B (2004) Genistein ameliorates beta-amyloid peptide (25-35)-induced hippocampal neuronal apoptosis. Free Radic Biol Med 36:180-188
    • (2004) Free Radic Biol Med , vol.36 , pp. 180-188
    • Zeng, H.1    Chen, Q.2    Zhao, B.3
  • 238
    • 2342630011 scopus 로고    scopus 로고
    • Estrogen receptor subtypes alpha and beta contribute to neuroprotection and increased Bcl-2 expression in primary hippocampal neurons
    • Zhao L, Wu TW, Brinton RD (2004) Estrogen receptor subtypes alpha and beta contribute to neuroprotection and increased Bcl-2 expression in primary hippocampal neurons. Brain Res 1010:22-34
    • (2004) Brain Res , vol.1010 , pp. 22-34
    • Zhao, L.1    Wu, T.W.2    Brinton, R.D.3
  • 239
    • 34548507935 scopus 로고    scopus 로고
    • Design, synthesis, and estrogenic activity of a novel estrogen receptor modulator - A hybrid structure of 17beta-estradiol and vitamin e in hippocampal neurons
    • Zhao L, Jin C, Mao Z, Gopinathan MB, Rehder K, Brinton RD (2007) Design, synthesis, and estrogenic activity of a novel estrogen receptor modulator-a hybrid structure of 17beta-estradiol and vitamin E in hippocampal neurons. J Med Chem 50:4471-4481
    • (2007) J Med Chem , vol.50 , pp. 4471-4481
    • Zhao, L.1    Jin, C.2    Mao, Z.3    Gopinathan, M.B.4    Rehder, K.5    Brinton, R.D.6
  • 240
    • 59649094237 scopus 로고    scopus 로고
    • A select combination of clinically relevant phytoestrogens enhances estrogen receptor {beta}-binding selectivity and neuroprotective activities in vitro and in vivo
    • Zhao L, Mao Z, Brinton RD (2009) A select combination of clinically relevant phytoestrogens enhances estrogen receptor {beta}-binding selectivity and neuroprotective activities in vitro and in vivo. Endocrinology 150:770-783
    • (2009) Endocrinology , vol.150 , pp. 770-783
    • Zhao, L.1    Mao, Z.2    Brinton, R.D.3
  • 241
    • 79954724910 scopus 로고    scopus 로고
    • Paeonol increases levels of cortical cytochrome oxidase and vascular actin and improves behavior in a rat model of Alzheimer's disease
    • Zhou J, Zhou L, Hou D, Tang J, Sun J, Bondy SC (2011) Paeonol increases levels of cortical cytochrome oxidase and vascular actin and improves behavior in a rat model of Alzheimer's disease. Brain Res 1388:141-147
    • (2011) Brain Res , vol.1388 , pp. 141-147
    • Zhou, J.1    Zhou, L.2    Hou, D.3    Tang, J.4    Sun, J.5    Bondy, S.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.