메뉴 건너뛰기




Volumn 34, Issue 11, 2002, Pages 1372-1381

Mitochondrial function and dysfunction in the cell: Its relevance to aging and aging-related disease

Author keywords

Calcium; Glutathione; Membrane potential; Mitochondria; Reactive oxygen species

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM; GLUTATHIONE; PROTON; REACTIVE OXYGEN METABOLITE;

EID: 0036830474     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(02)00077-8     Document Type: Short Survey
Times cited : (196)

References (66)
  • 1
    • 0023895734 scopus 로고
    • Glutamate becomes neurotoxic via the N-methyl-D-aspartate receptor when intracellular energy levels are reduced
    • Novelli A., Reilly J.A., Lysko P.G., Henneberry R.C. Glutamate becomes neurotoxic via the N-methyl-D-aspartate receptor when intracellular energy levels are reduced. Brain Res. 451:1988;205-212.
    • (1988) Brain Res. , vol.451 , pp. 205-212
    • Novelli, A.1    Reilly, J.A.2    Lysko, P.G.3    Henneberry, R.C.4
  • 2
    • 0027477946 scopus 로고
    • Do defects in mitochondrial energy metabolism underlie the pathology of neurodegenerative diseases?
    • Beal M.F., Hyman B.T., Koroshetz W. Do defects in mitochondrial energy metabolism underlie the pathology of neurodegenerative diseases? Trends Neurosci. 16:1993;125-131.
    • (1993) Trends Neurosci. , vol.16 , pp. 125-131
    • Beal, M.F.1    Hyman, B.T.2    Koroshetz, W.3
  • 3
    • 0033971898 scopus 로고    scopus 로고
    • Mitochondria and neuronal survival
    • Nicholls D.G., Budd S.L. Mitochondria and neuronal survival. Physiol. Rev. 80:2000;315-360.
    • (2000) Physiol. Rev. , vol.80 , pp. 315-360
    • Nicholls, D.G.1    Budd, S.L.2
  • 4
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • Cadenas E., Davies K.J.A. Mitochondrial free radical generation, oxidative stress, and aging. Free Radic. Biol. Med. 29:2000;222-230.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.A.2
  • 6
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X., Kim C.N., Yang J., Jemmerson R., Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell. 86:1996;147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 8
    • 0023681148 scopus 로고
    • Physiological roles of nicotinamide nucleotide transhydrogenase
    • Hoek J.B., Rydstrom J. Physiological roles of nicotinamide nucleotide transhydrogenase. Biochem. J. 254:1988;1-10.
    • (1988) Biochem. J. , vol.254 , pp. 1-10
    • Hoek, J.B.1    Rydstrom, J.2
  • 9
    • 0035863011 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space
    • Han D., Williams E., Cadenas E. Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space. Biochem. J. 353:2001;411-416.
    • (2001) Biochem. J. , vol.353 , pp. 411-416
    • Han, D.1    Williams, E.2    Cadenas, E.3
  • 10
    • 0031721246 scopus 로고    scopus 로고
    • Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondria in the short-lived rat than in the longevous pigeon
    • Barja G., Herrero A. Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondria in the short-lived rat than in the longevous pigeon. J. Bioenerg. Biomembr. 30:1998;235-243.
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 235-243
    • Barja, G.1    Herrero, A.2
  • 11
    • 0032755436 scopus 로고    scopus 로고
    • Monoamine oxidase and mitochondrial respiration
    • Cohen G., Kesler N. Monoamine oxidase and mitochondrial respiration. J. Neurochem. 73:1999;2310-2315.
    • (1999) J. Neurochem. , vol.73 , pp. 2310-2315
    • Cohen, G.1    Kesler, N.2
  • 12
    • 0018864653 scopus 로고
    • Energy transduction in intact synaptosomes: Influence of plasma-membrane depolarization on the respiration and membrane potential of internal mitochondria determined in situ
    • Scott I.D., Nicholls D.G. Energy transduction in intact synaptosomes: influence of plasma-membrane depolarization on the respiration and membrane potential of internal mitochondria determined in situ. Biochem. J. 186:1980;21-33.
    • (1980) Biochem. J. , vol.186 , pp. 21-33
    • Scott, I.D.1    Nicholls, D.G.2
  • 14
    • 0025238864 scopus 로고
    • Analysis of the control of respiration rate, phosphorylation rate, proton leak rate and protonmotive force in isolated mitochondria using the 'top-down' approach of metabolic control theory
    • Hafner R.P., Brown G.C., Brand M.D. Analysis of the control of respiration rate, phosphorylation rate, proton leak rate and protonmotive force in isolated mitochondria using the 'top-down' approach of metabolic control theory. Eur. J. Biochem. 188:1990;313-319.
    • (1990) Eur. J. Biochem. , vol.188 , pp. 313-319
    • Hafner, R.P.1    Brown, G.C.2    Brand, M.D.3
  • 15
    • 0030707553 scopus 로고    scopus 로고
    • Threshold effects in synaptosomal and nonsynaptic mitochondria from hippocampal CA1 and paramedian neocortex brain regions
    • Davey G.P., Canevari L., Clark J.B. Threshold effects in synaptosomal and nonsynaptic mitochondria from hippocampal CA1 and paramedian neocortex brain regions. J. Neurochem. 69:1997;2564-2570.
    • (1997) J. Neurochem. , vol.69 , pp. 2564-2570
    • Davey, G.P.1    Canevari, L.2    Clark, J.B.3
  • 16
    • 0033963434 scopus 로고    scopus 로고
    • Calcium regulation of oxidative phosphorylation in rat skeletal muscle mitochondria
    • Kavanagh N.I., Ainscow E.K., Brand M.D. Calcium regulation of oxidative phosphorylation in rat skeletal muscle mitochondria. Biochim. Biophys. Acta Bioenerg. 1457:2000;57-70.
    • (2000) Biochim. Biophys. Acta Bioenerg. , vol.1457 , pp. 57-70
    • Kavanagh, N.I.1    Ainscow, E.K.2    Brand, M.D.3
  • 17
    • 0033522924 scopus 로고    scopus 로고
    • Titrating the effects of mitochondrial complex I impairment in the cell physiology
    • Barrientos A., Moraes C.T. Titrating the effects of mitochondrial complex I impairment in the cell physiology. J. Biol. Chem. 274:1999;16188-16197.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16188-16197
    • Barrientos, A.1    Moraes, C.T.2
  • 18
    • 0033369476 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical generation and leak: Sites of production in state 4 and 3, organ specificity, and relation to aging and longevity
    • Barja G. Mitochondrial oxygen radical generation and leak: sites of production in state 4 and 3, organ specificity, and relation to aging and longevity. J. Bioenerg. Biomembr. 31:1999;347-366.
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 347-366
    • Barja, G.1
  • 19
    • 0030803457 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegeneration
    • Cooper J.M., Schapira A.H.V. Mitochondrial dysfunction in neurodegeneration. J. Bioenerg. Biomembr. 29:1997;175-183.
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 175-183
    • Cooper, J.M.1    Schapira, A.H.V.2
  • 20
    • 0034079858 scopus 로고    scopus 로고
    • Oxidative stress, mitochondrial respiration, and Parkinson's disease
    • Cohen G. Oxidative stress, mitochondrial respiration, and Parkinson's disease. Ann. N. Y. Acad. Sci. 899:2000;112-120.
    • (2000) Ann. N. Y. Acad. Sci. , vol.899 , pp. 112-120
    • Cohen, G.1
  • 21
    • 0034714346 scopus 로고    scopus 로고
    • Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity - Implications for Parkinson's disease
    • Jha N., Jurma O., Lalli G., Liu Y., Pettus E.H., Greenamyre J.T., Liu R.M., Forman H.J., Andersen J.K. Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity - implications for Parkinson's disease. J. Biol. Chem. 275:2000;26096-26101.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26096-26101
    • Jha, N.1    Jurma, O.2    Lalli, G.3    Liu, Y.4    Pettus, E.H.5    Greenamyre, J.T.6    Liu, R.M.7    Forman, H.J.8    Andersen, J.K.9
  • 22
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov S.S., Skulachev V.P., Starkov A.A. High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 416:1997;15-18.
    • (1997) FEBS Lett. , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 23
    • 0017638174 scopus 로고
    • The effective proton conductances of the inner membrane of mitochondria from brown adipose tissue: Dependency on proton electrochemical gradient
    • Nicholls D.G. The effective proton conductances of the inner membrane of mitochondria from brown adipose tissue: dependency on proton electrochemical gradient. Eur. J. Biochem. 77:1977;349-356.
    • (1977) Eur. J. Biochem. , vol.77 , pp. 349-356
    • Nicholls, D.G.1
  • 24
    • 0035162338 scopus 로고    scopus 로고
    • Mitochondria deficient in complex I activity are depolarized by hydrogen peroxide in nerve terminals: Relevance to Parkinson's disease
    • Chinopoulos C., Adam-Vizi V. Mitochondria deficient in complex I activity are depolarized by hydrogen peroxide in nerve terminals: relevance to Parkinson's disease. J. Neurochem. 76:2001;302-306.
    • (2001) J. Neurochem. , vol.76 , pp. 302-306
    • Chinopoulos, C.1    Adam-Vizi, V.2
  • 26
    • 0035477926 scopus 로고    scopus 로고
    • Nitric oxide inhibits mitochondrial NADH: Ubiquinone reductase activity through peroxynitrite formation
    • Riobó N.A., Clementi E., Melani M., Boveris A., Cadenas E., Moncada S., Poderoso J.J. Nitric oxide inhibits mitochondrial NADH: ubiquinone reductase activity through peroxynitrite formation. Biochem. J. 359:2001;139-145.
    • (2001) Biochem. J. , vol.359 , pp. 139-145
    • Riobó, N.A.1    Clementi, E.2    Melani, M.3    Boveris, A.4    Cadenas, E.5    Moncada, S.6    Poderoso, J.J.7
  • 27
    • 0032535398 scopus 로고    scopus 로고
    • Thiol oxidation and loss of mitochondrial complex I precede excitatory amino acid-mediated neurodegeneration
    • Sriram K., Shankar S.K., Boyd M.R., Ravindranath V. Thiol oxidation and loss of mitochondrial complex I precede excitatory amino acid-mediated neurodegeneration. J. Neurosci. 18:1998;10287-10296.
    • (1998) J. Neurosci. , vol.18 , pp. 10287-10296
    • Sriram, K.1    Shankar, S.K.2    Boyd, M.R.3    Ravindranath, V.4
  • 28
    • 0032827391 scopus 로고    scopus 로고
    • Effect of thiol modification on brain mitochondrial complex I activity
    • Balijepalli S., Annepu J., Boyd M.R., Ravindranath V. Effect of thiol modification on brain mitochondrial complex I activity. Neurosci. Lett. 272:1999;203-206.
    • (1999) Neurosci. Lett. , vol.272 , pp. 203-206
    • Balijepalli, S.1    Annepu, J.2    Boyd, M.R.3    Ravindranath, V.4
  • 29
    • 0032557511 scopus 로고    scopus 로고
    • Energy thresholds in brain mitochondria - Potential involvement in neurodegeneration
    • Davey G.P., Peuchen S., Clark J.B. Energy thresholds in brain mitochondria - potential involvement in neurodegeneration. J. Biol. Chem. 273:1998;12753-12757.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12753-12757
    • Davey, G.P.1    Peuchen, S.2    Clark, J.B.3
  • 30
    • 0034678112 scopus 로고    scopus 로고
    • N-acetylcysteine elicited increase in complex I activity in synaptic mitochondria from aged mice: Implications for treatment of Parkinson's disease
    • Banaclocha M.M. N-acetylcysteine elicited increase in complex I activity in synaptic mitochondria from aged mice: implications for treatment of Parkinson's disease. Brain Res. 859:2000;173-175.
    • (2000) Brain Res. , vol.859 , pp. 173-175
    • Banaclocha, M.M.1
  • 32
    • 0020680904 scopus 로고
    • Chronic parkinsonism in humans due to a product of meperidine-analog synthesis
    • Langston J.W., Ballard P., Tetrud J.W., Irwin I. Chronic parkinsonism in humans due to a product of meperidine-analog synthesis. Science. 219:1983;979-980.
    • (1983) Science , vol.219 , pp. 979-980
    • Langston, J.W.1    Ballard, P.2    Tetrud, J.W.3    Irwin, I.4
  • 33
    • 0033286485 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Parkinson's disease
    • G.C. Brown, D.G. Nicholls, C. Cooper (Eds.), Portland Press, London
    • J.T. Greenamyre, G. MacKenzie, T.-I. Peng, S.E. Stephans, Mitochondrial dysfunction in Parkinson's disease, in: G.C. Brown, D.G. Nicholls, C. Cooper (Eds.), Mitochondria and Cell Death, Portland Press, London, 1999, pp. 85-98.
    • (1999) Mitochondria and Cell Death , pp. 85-98
    • Greenamyre, J.T.1    MacKenzie, G.2    Peng, T.-I.3    Stephans, S.E.4
  • 34
    • 0034704125 scopus 로고    scopus 로고
    • Functional analysis of lymphoblast and cybrid mitochondria containing the 3460, 11,778 or 14,484 Leber's hereditary optic neuropathy mitochondrial DNA mutation
    • Brown M.D., Trounce I.A., Jun A.S., Allen J.C., Wallace D.C. Functional analysis of lymphoblast and cybrid mitochondria containing the 3460, 11,778 or 14,484 Leber's hereditary optic neuropathy mitochondrial DNA mutation. J. Biol. Chem. 275:2000;39831-39836.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39831-39836
    • Brown, M.D.1    Trounce, I.A.2    Jun, A.S.3    Allen, J.C.4    Wallace, D.C.5
  • 35
    • 0032490091 scopus 로고    scopus 로고
    • Human complex I defects in neurodegenerative diseases
    • Schapira A.H.V. Human complex I defects in neurodegenerative diseases. Biochim. Biophys. Acta Bioenerg. 1364:1998;261-270.
    • (1998) Biochim. Biophys. Acta Bioenerg. , vol.1364 , pp. 261-270
    • Schapira, A.H.V.1
  • 36
    • 0030060823 scopus 로고    scopus 로고
    • Use of transmitochondrial cybrids to assign a complex I defect to the mitochondrial DNA-encoded NADH dehydrogenase subunit 6 gene mutation at nucleotide pair 14,459 that causes Leber hereditary optic neuropathy and dystonia
    • Jun A.S., Trounce I.A., Brown M.D., Shoffner J.M., Wallace D.C. Use of transmitochondrial cybrids to assign a complex I defect to the mitochondrial DNA-encoded NADH dehydrogenase subunit 6 gene mutation at nucleotide pair 14,459 that causes Leber hereditary optic neuropathy and dystonia. Mol. Cell. Biol. 16:1996;771-777.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 771-777
    • Jun, A.S.1    Trounce, I.A.2    Brown, M.D.3    Shoffner, J.M.4    Wallace, D.C.5
  • 37
    • 0030788483 scopus 로고    scopus 로고
    • Leber hereditary optic neuropathy: How do mitochondrial DNA mutations cause degeneration of the optic nerve?
    • Howell N. Leber hereditary optic neuropathy: how do mitochondrial DNA mutations cause degeneration of the optic nerve? J. Bioenerg. Biomembr. 29:1997;165-173.
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 165-173
    • Howell, N.1
  • 38
    • 0029049824 scopus 로고
    • Delayed excitotoxic neurodegeneration induced by excitatory amino acid agonists in isolated retina
    • Romano C., Price M.T., Olney J.W. Delayed excitotoxic neurodegeneration induced by excitatory amino acid agonists in isolated retina. J. Neurochem. 65:1995;59-67.
    • (1995) J. Neurochem. , vol.65 , pp. 59-67
    • Romano, C.1    Price, M.T.2    Olney, J.W.3
  • 39
    • 0030792543 scopus 로고    scopus 로고
    • Adenosine triphosphate degradation products after oxidative stress and metabolic dysfunction in cultured retinal cells
    • Rego A.C., Santos M.S., Oliveira C.R. Adenosine triphosphate degradation products after oxidative stress and metabolic dysfunction in cultured retinal cells. J. Neurochem. 69:1997;1228-1235.
    • (1997) J. Neurochem. , vol.69 , pp. 1228-1235
    • Rego, A.C.1    Santos, M.S.2    Oliveira, C.R.3
  • 40
    • 0030984429 scopus 로고    scopus 로고
    • Involvement of a caspase-3-like cysteine protease in 1-methyl-4-phenylpyridinium-mediated apoptosis of cultured cerebellar granule neurons
    • Du Y.S., Dodel R.C., Bales K.R., Jemmerson R., Hamilton-Byrd E., Paul S.M. Involvement of a caspase-3-like cysteine protease in 1-methyl-4-phenylpyridinium-mediated apoptosis of cultured cerebellar granule neurons. J. Neurochem. 69:1997;1382-1388.
    • (1997) J. Neurochem. , vol.69 , pp. 1382-1388
    • Du, Y.S.1    Dodel, R.C.2    Bales, K.R.3    Jemmerson, R.4    Hamilton-Byrd, E.5    Paul, S.M.6
  • 41
    • 0030881686 scopus 로고    scopus 로고
    • Oxidative damage during aging targets mitochondrial aconitase
    • Yan L.J., Levine R.L., Sohal R.S. Oxidative damage during aging targets mitochondrial aconitase. Proc. Natl. Acad. Sci. U.S.A. 94:1997;11168-11172.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 11168-11172
    • Yan, L.J.1    Levine, R.L.2    Sohal, R.S.3
  • 43
    • 0033535948 scopus 로고    scopus 로고
    • Declines in mitochondrial respiration during cardiac reperfusion: Age-dependent inactivation of α-ketoglutarate dehydrogenase
    • Lucas D.T., Szweda L.I. Declines in mitochondrial respiration during cardiac reperfusion: age-dependent inactivation of α-ketoglutarate dehydrogenase. Proc. Natl. Acad. Sci. U.S.A. 96:1999;6689-6693.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6689-6693
    • Lucas, D.T.1    Szweda, L.I.2
  • 44
    • 0034671429 scopus 로고    scopus 로고
    • Inhibition of Krebs cycle enzymes by hydrogen peroxide: A key role of α-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress
    • Tretter L., Adam-Vizi V. Inhibition of Krebs cycle enzymes by hydrogen peroxide: a key role of α-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress. J. Neurosci. 20:2000;8972-8979.
    • (2000) J. Neurosci. , vol.20 , pp. 8972-8979
    • Tretter, L.1    Adam-Vizi, V.2
  • 45
    • 0027204154 scopus 로고
    • Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate
    • Beal M.F., Brouillet E., Jenkins B., Henshaw R., Rosen B., Hyman B.T. Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate. J. Neurochem. 61:1993;1147-1150.
    • (1993) J. Neurochem. , vol.61 , pp. 1147-1150
    • Beal, M.F.1    Brouillet, E.2    Jenkins, B.3    Henshaw, R.4    Rosen, B.5    Hyman, B.T.6
  • 46
    • 0031912530 scopus 로고    scopus 로고
    • 3-Nitropropionic acid exacerbates N-methyl-D-aspartate toxicity in striatal culture by multiple mechanisms
    • Greene J.G., Sheu S.S., Gross R.A., Greenamyre J.T. 3-Nitropropionic acid exacerbates N-methyl-D-aspartate toxicity in striatal culture by multiple mechanisms. Neuroscience. 84:1998;503-510.
    • (1998) Neuroscience , vol.84 , pp. 503-510
    • Greene, J.G.1    Sheu, S.S.2    Gross, R.A.3    Greenamyre, J.T.4
  • 47
    • 0033286630 scopus 로고    scopus 로고
    • Secondary abnormalities of mitochondrial DNA associated with neurodegeneration
    • G.C. Brown, D.G. Nicholls, C. Cooper (Eds.), Portland Press, London
    • S.J. Tabrizi, A.H.V. Schapira, Secondary abnormalities of mitochondrial DNA associated with neurodegeneration, in: G.C. Brown, D.G. Nicholls, C. Cooper (Eds.), Mitochondria in the Life and Death of the Cell, Portland Press, London, 1999, pp. 99-110.
    • (1999) Mitochondria in the Life and Death of the Cell , pp. 99-110
    • Tabrizi, S.J.1    Schapira, A.H.V.2
  • 48
    • 0035834789 scopus 로고    scopus 로고
    • A defect in the cytochrome b large subunit in complex II causes both superoxide anion overproduction and abnormal energy metabolism in Caenorhabditis elegans
    • Senoo-Matsuda N., Yasuda K., Tsuda M., Ohkubo T., Yoshimura S., Nakazawa H., Hartman P.S., Ishii N. A defect in the cytochrome b large subunit in complex II causes both superoxide anion overproduction and abnormal energy metabolism in Caenorhabditis elegans. J. Biol. Chem. 276:2001;41553-41558.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41553-41558
    • Senoo-Matsuda, N.1    Yasuda, K.2    Tsuda, M.3    Ohkubo, T.4    Yoshimura, S.5    Nakazawa, H.6    Hartman, P.S.7    Ishii, N.8
  • 49
    • 0018837597 scopus 로고
    • Enhancement of hydrogen peroxide formation by protophores and ionophores in antimycin-supplemented mitochondria
    • Cadenas E., Boveris A. Enhancement of hydrogen peroxide formation by protophores and ionophores in antimycin-supplemented mitochondria. Biochem. J. 188:1980;31-37.
    • (1980) Biochem. J. , vol.188 , pp. 31-37
    • Cadenas, E.1    Boveris, A.2
  • 50
    • 0030775042 scopus 로고    scopus 로고
    • Decreased glutathione results in calcium-mediated cell death in PC12
    • Jurma O.P., Hom D.G., Andersen J.K. Decreased glutathione results in calcium-mediated cell death in PC12. Free Radic. Biol. Med. 23:1997;1055-1066.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 1055-1066
    • Jurma, O.P.1    Hom, D.G.2    Andersen, J.K.3
  • 51
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer F.Q., Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic. Biol. Med. 30:2001;1191-1212.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 52
    • 0016294206 scopus 로고
    • The influence of respiration and ATP hydrolysis on the proton electrochemical potential gradient across the inner membrane of rat liver mitochondria as determined by ion distribution
    • Nicholls D.G. The influence of respiration and ATP hydrolysis on the proton electrochemical potential gradient across the inner membrane of rat liver mitochondria as determined by ion distribution. Eur. J. Biochem. 50:1974;305-315.
    • (1974) Eur. J. Biochem. , vol.50 , pp. 305-315
    • Nicholls, D.G.1
  • 53
    • 0034668852 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins: From mitochondria to the regulation of energy balance
    • Ricquier D., Bouillaud F. Mitochondrial uncoupling proteins: from mitochondria to the regulation of energy balance. J. Physiol. (London). 529:2000;3-10.
    • (2000) J. Physiol. (London) , vol.529 , pp. 3-10
    • Ricquier, D.1    Bouillaud, F.2
  • 54
    • 0018269944 scopus 로고
    • The regulation of extra-mitochondrial free Ca by rat liver mitochondria
    • Nicholls D.G. The regulation of extra-mitochondrial free Ca by rat liver mitochondria. Biochem. J. 176:1978;463-474.
    • (1978) Biochem. J. , vol.176 , pp. 463-474
    • Nicholls, D.G.1
  • 55
    • 0019324973 scopus 로고
    • The regulation of brain mitochondrial calcium-ion transport: The role of ATP in the discrimination between kinetic and membrane-potential-dependent Ca efflux mechanisms
    • Nicholls D.G., Scott I.D. The regulation of brain mitochondrial calcium-ion transport: the role of ATP in the discrimination between kinetic and membrane-potential-dependent Ca efflux mechanisms. Biochem. J. 186:1980;833-839.
    • (1980) Biochem. J. , vol.186 , pp. 833-839
    • Nicholls, D.G.1    Scott, I.D.2
  • 56
    • 0025331705 scopus 로고
    • Regulation of the intracellular free calcium concentration in single rat dorsal root ganglion neurones in vitro
    • Thayer S.A., Miller R.J. Regulation of the intracellular free calcium concentration in single rat dorsal root ganglion neurones in vitro. J. Physiol. (London). 425:1990;85-115.
    • (1990) J. Physiol. (London) , vol.425 , pp. 85-115
    • Thayer, S.A.1    Miller, R.J.2
  • 57
    • 0034307759 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and glutamate excitotoxicity in cultured cerebellar granule cells
    • Ward M.W., Rego A.C., Frenguelli B.G., Nicholls D.G. Mitochondrial membrane potential and glutamate excitotoxicity in cultured cerebellar granule cells. J. Neurosci. 20:2000;7208-7219.
    • (2000) J. Neurosci. , vol.20 , pp. 7208-7219
    • Ward, M.W.1    Rego, A.C.2    Frenguelli, B.G.3    Nicholls, D.G.4
  • 58
    • 0029827804 scopus 로고    scopus 로고
    • Mitochondrial calcium regulation and acute glutamate excitotoxicity in cultured cerebellar granule cells
    • Budd S.L., Nicholls D.G. Mitochondrial calcium regulation and acute glutamate excitotoxicity in cultured cerebellar granule cells. J. Neurochem. 67:1996;2282-2291.
    • (1996) J. Neurochem. , vol.67 , pp. 2282-2291
    • Budd, S.L.1    Nicholls, D.G.2
  • 59
    • 0032535275 scopus 로고    scopus 로고
    • Mitochondrial control of acute glutamate excitotoxicity in cultured cerebellar granule cells
    • Castilho R.F., Hansson O., Ward M.W., Budd S.L., Nicholls D.G. Mitochondrial control of acute glutamate excitotoxicity in cultured cerebellar granule cells. J. Neurosci. 18:1998;10277-10286.
    • (1998) J. Neurosci. , vol.18 , pp. 10277-10286
    • Castilho, R.F.1    Hansson, O.2    Ward, M.W.3    Budd, S.L.4    Nicholls, D.G.5
  • 60
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem. J. 341:1999;233-249.
    • (1999) Biochem. J. , vol.341 , pp. 233-249
    • Crompton, M.1
  • 63
    • 0032538051 scopus 로고    scopus 로고
    • Quantitative assay by flow cytometry of the mitochondrial membrane potential in intact cells
    • Rottenberg H., Wu S.L. Quantitative assay by flow cytometry of the mitochondrial membrane potential in intact cells. Biochim. Biophys. Acta. 1404:1998;393-404.
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 393-404
    • Rottenberg, H.1    Wu, S.L.2
  • 64
    • 0033603889 scopus 로고    scopus 로고
    • Collapse of the inner mitochondrial transmembrane potential is not required for apoptosis of HL60 cells
    • Finucane D.M., Waterhouse N.J., Amarante-Mendes G.P., Cotter T.G., Green D.R. Collapse of the inner mitochondrial transmembrane potential is not required for apoptosis of HL60 cells. Exp. Cell Res. 251:1999;166-174.
    • (1999) Exp. Cell Res. , vol.251 , pp. 166-174
    • Finucane, D.M.1    Waterhouse, N.J.2    Amarante-Mendes, G.P.3    Cotter, T.G.4    Green, D.R.5
  • 65
    • 0033198273 scopus 로고    scopus 로고
    • Mitochondrial depolarization is not required for neuronal apoptosis
    • Krohn A.J., Wahlbrink T., Prehn J.H.M. Mitochondrial depolarization is not required for neuronal apoptosis. J. Neurosci. 19:1999;7394-7404.
    • (1999) J. Neurosci. , vol.19 , pp. 7394-7404
    • Krohn, A.J.1    Wahlbrink, T.2    Prehn, J.H.M.3
  • 66
    • 0035803568 scopus 로고    scopus 로고
    • Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2
    • Adrain C., Creagh E.M., Martin S.J. Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2. EMBO J. 20:2001;6627-6636.
    • (2001) EMBO J. , vol.20 , pp. 6627-6636
    • Adrain, C.1    Creagh, E.M.2    Martin, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.