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Volumn 34, Issue 3, 2003, Pages 287-303

Nitric oxide-induced mitochondrial dysfunction: Implications for neurodegeneration

Author keywords

Electron transport chain; Free radicals; Glia; Mitochondria; Neurodegeneration; Neuron; Nitric oxide

Indexed keywords

3,4 METHYLENEDIOXYMETHAMPHETAMINE; ACETYLCYSTEINE; AMPHETAMINE; ANTIOXIDANT; BETA INTERFERON; CANNABINOID DERIVATIVE; COCAINE; CYTOCHROME C OXIDASE; CYTOKINE; GLUTAMIC ACID; GLUTATHIONE; MANGANESE SUPEROXIDE DISMUTASE; MELATONIN; MESSENGER RNA; N METHYL DEXTRO ASPARTIC ACID; N METHYL DEXTRO ASPARTIC ACID RECEPTOR BLOCKING AGENT; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; NITRIC OXIDE SYNTHASE INHIBITOR; PARACETAMOL; PEROXYNITRITE; PSYCHOSTIMULANT AGENT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUCCINATE DEHYDROGENASE (UBIQUINONE); SUPEROXIDE DISMUTASE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 0037303479     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(02)01327-8     Document Type: Review
Times cited : (177)

References (197)
  • 2
    • 0028349156 scopus 로고
    • Nitric oxide synthases in mammals
    • Knowles R.G., Moncada S. Nitric oxide synthases in mammals. Biochem. J. 298:1994;249-258.
    • (1994) Biochem. J. , vol.298 , pp. 249-258
    • Knowles, R.G.1    Moncada, S.2
  • 3
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology, and pharmacology
    • Moncada S., Palmer R.M.J., Higgs E.A. Nitric oxide physiology, pathophysiology, and pharmacology . Pharmacol. Rev. 43:1991;109-142.
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.J.2    Higgs, E.A.3
  • 4
    • 0027975453 scopus 로고
    • Nitric oxide: A physiologic messenger molecule
    • Bredt D.S., Snyder S.H. Nitric oxide a physiologic messenger molecule . Annu. Rev. Biochem. 63:1994;175-195.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 175-195
    • Bredt, D.S.1    Snyder, S.H.2
  • 6
    • 0035893981 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide synthase is constitutively active and is functionally upregulated in hypoxia
    • Lacza Z., Puskar M., Figueroa J.P., Zhang J., Rajapakse N., Busija D.W. Mitochondrial nitric oxide synthase is constitutively active and is functionally upregulated in hypoxia. Free Radic. Biol. Med. 31:2001;1609-1615.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1609-1615
    • Lacza, Z.1    Puskar, M.2    Figueroa, J.P.3    Zhang, J.4    Rajapakse, N.5    Busija, D.W.6
  • 8
    • 0029924622 scopus 로고    scopus 로고
    • In vivo expression of inducible nitric oxide synthase in cerebellar neurons
    • Minc-Golomb D., Yadid G., Tsarfaty I., Resau J.H., Schwartz J.P. In vivo expression of inducible nitric oxide synthase in cerebellar neurons. J. Neurochem. 66:1996;1504-1509.
    • (1996) J. Neurochem. , vol.66 , pp. 1504-1509
    • Minc-Golomb, D.1    Yadid, G.2    Tsarfaty, I.3    Resau, J.H.4    Schwartz, J.P.5
  • 11
    • 0030083086 scopus 로고    scopus 로고
    • Astrocytes and Bergmann glia as an important site of nitric oxide synthase 1
    • Kugler P., Drenckhahn D. Astrocytes and Bergmann glia as an important site of nitric oxide synthase 1. Glia. 16:1996;165-173.
    • (1996) Glia , vol.16 , pp. 165-173
    • Kugler, P.1    Drenckhahn, D.2
  • 12
    • 0030636128 scopus 로고    scopus 로고
    • Immunocytochemical characterization of the expression of inducible and consitutive isoforms of nitric oxide synthase in demyelinating multiple sclerosis lesions
    • DeGroot C.J.A., Ruuls S., Theeuwes J.W.M., Dijkstra C.D., Van der Walk P. Immunocytochemical characterization of the expression of inducible and consitutive isoforms of nitric oxide synthase in demyelinating multiple sclerosis lesions. J. Neuropathol. Exp. Neurol. 56:1997;10-20.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 10-20
    • DeGroot, C.J.A.1    Ruuls, S.2    Theeuwes, J.W.M.3    Dijkstra, C.D.4    Van der Walk, P.5
  • 13
    • 0030587864 scopus 로고    scopus 로고
    • Expression of type II nitric oxide synthase in primary human astrocytes and microglia: Role of IL-1 β and Il-1 receptor antagonists
    • Liu J., Zhao M.L., Brosnan C.F., Lee S.C. Expression of type II nitric oxide synthase in primary human astrocytes and microglia role of IL-1 β and Il-1 receptor antagonists . J. Immunol. 157:1996;3569-3576.
    • (1996) J. Immunol. , vol.157 , pp. 3569-3576
    • Liu, J.1    Zhao, M.L.2    Brosnan, C.F.3    Lee, S.C.4
  • 15
    • 0031759128 scopus 로고    scopus 로고
    • Absence of nitric oxide synthase in rat oligodendrocytes: A light and electron microscopic study
    • Keilhoff G., Seidel B., Wolf G. Absence of nitric oxide synthase in rat oligodendrocytes a light and electron microscopic study . Acta Histochem. 100:1998;409-417.
    • (1998) Acta Histochem , vol.100 , pp. 409-417
    • Keilhoff, G.1    Seidel, B.2    Wolf, G.3
  • 16
    • 0033135875 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase expression in cultures enriched for mature oligodendrocytes is due to microglia
    • Hewett J.A., Hewett S.J., Winkler S., Pfeiffer S.E. Inducible nitric oxide synthase expression in cultures enriched for mature oligodendrocytes is due to microglia. J. Neurosci. Res. 56:1999;189-198.
    • (1999) J. Neurosci. Res. , vol.56 , pp. 189-198
    • Hewett, J.A.1    Hewett, S.J.2    Winkler, S.3    Pfeiffer, S.E.4
  • 17
    • 0027194540 scopus 로고
    • A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds
    • Lipton S.A., Choi Y.B., Pan Z.H., Lei S.Z., Chen H.S.V., Sucher N.J., Loscalzo J., Singel D.J., Stamler J.S. A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds. Nature. 364:1993;626-632.
    • (1993) Nature , vol.364 , pp. 626-632
    • Lipton, S.A.1    Choi, Y.B.2    Pan, Z.H.3    Lei, S.Z.4    Chen, H.S.V.5    Sucher, N.J.6    Loscalzo, J.7    Singel, D.J.8    Stamler, J.S.9
  • 18
    • 0028675513 scopus 로고
    • The machine that makes ATP
    • Pedersen P.L. The machine that makes ATP. Curr. Biol. 4:1994;1138-1141.
    • (1994) Curr. Biol. , vol.4 , pp. 1138-1141
    • Pedersen, P.L.1
  • 19
    • 0029873904 scopus 로고    scopus 로고
    • Threshold effects and control of oxidative phosphorylation in nonsynaptic rat brain mitochondria
    • Davey G.P., Clark J.B. Threshold effects and control of oxidative phosphorylation in nonsynaptic rat brain mitochondria. J. Neurochem. 66:1996;1617-1624.
    • (1996) J. Neurochem. , vol.66 , pp. 1617-1624
    • Davey, G.P.1    Clark, J.B.2
  • 20
    • 0017154414 scopus 로고
    • Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
    • Boveris A., Cadenas E., Stoppani A.O. Role of ubiquinone in the mitochondrial generation of hydrogen peroxide. Biochem. J. 156:1976;435-444.
    • (1976) Biochem. J. , vol.156 , pp. 435-444
    • Boveris, A.1    Cadenas, E.2    Stoppani, A.O.3
  • 21
    • 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
  • 22
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens J.F., Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191:1980;421-427.
    • (1980) Biochem. J. , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 23
  • 24
  • 25
    • 0033358590 scopus 로고    scopus 로고
    • Human mitochondrial complex I in health and disease
    • Smeitink J., van den Heuvel L. Human mitochondrial complex I in health and disease. Am. J. Hum. Genet. 64:1999;1505-1510.
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 1505-1510
    • Smeitink, J.1    Van den Heuvel, L.2
  • 26
    • 0023940538 scopus 로고
    • Differentiation of murine macrophages to express nonspecific cytotoxicity for tumor cells results in L-arginine-dependent inhibition of mitochondrial iron-sulfur enzymes in the macrophage effector cells
    • Drapier J., Hibbs J.B. Jr. Differentiation of murine macrophages to express nonspecific cytotoxicity for tumor cells results in L-arginine-dependent inhibition of mitochondrial iron-sulfur enzymes in the macrophage effector cells. J. Immunol. 140:1988;2829-2838.
    • (1988) J. Immunol. , vol.140 , pp. 2829-2838
    • Drapier, J.1    Hibbs J.B., Jr.2
  • 27
    • 0029146981 scopus 로고
    • The interactions between nitric oxide and brain nerve terminals as studied by electron paramagnetic resonance
    • Cooper C.E., Brown G.C. The interactions between nitric oxide and brain nerve terminals as studied by electron paramagnetic resonance. Biochem. Biophys. Res. Commun. 212:1995;404-412.
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 404-412
    • Cooper, C.E.1    Brown, G.C.2
  • 28
    • 0026655617 scopus 로고
    • Interferon-γ and tumor necrosis factor synergize to induce nitric oxide production and inhibit mitochondrial respiration in vascular smooth muscle cells
    • Geng Y., Hansson G.K., Holme E. Interferon-γ and tumor necrosis factor synergize to induce nitric oxide production and inhibit mitochondrial respiration in vascular smooth muscle cells. Circ. Res. 71:1992;1268-1276.
    • (1992) Circ. Res. , vol.71 , pp. 1268-1276
    • Geng, Y.1    Hansson, G.K.2    Holme, E.3
  • 30
    • 0029998238 scopus 로고    scopus 로고
    • Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport
    • Cassina A., Radi R. Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport. Arch. Biochem. Biophys. 328:1996;309-316.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 309-316
    • Cassina, A.1    Radi, R.2
  • 31
    • 0035477926 scopus 로고    scopus 로고
    • Nitric oxide inhibits mitochondrial NADH: Ubiquinone reductase activity through peroxynitrite formation
    • Riobo 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. 359:2000;139-145.
    • (2000) Biochem. J. , vol.359 , pp. 139-145
    • Riobo, N.A.1    Clementi, E.2    Melani, M.3    Boveris, A.4    Cadenas, E.5    Moncada, S.6    Poderoso, J.J.7
  • 32
    • 0028145462 scopus 로고
    • Nitric oxide-mediated inhibition of the mitochondrial respiratory chain in cultured astrocytes
    • Bolaos J.P., Peuchen S., Heales S.J.R., Land J.M., Clark J.B. Nitric oxide-mediated inhibition of the mitochondrial respiratory chain in cultured astrocytes. J. Neurochem. 63:1994;910-916.
    • (1994) J. Neurochem. , vol.63 , pp. 910-916
    • Bolaos, J.P.1    Peuchen, S.2    Heales, S.J.R.3    Land, J.M.4    Clark, J.B.5
  • 33
    • 0028952832 scopus 로고
    • Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary cultures
    • Bolaos J.P., Heales S.J.R., Land J.M., Clark J.B. Effect of peroxynitrite on the mitochondrial respiratory chain differential susceptibility of neurones and astrocytes in primary cultures . J. Neurochem. 64:1995;1965-1972.
    • (1995) J. Neurochem. , vol.64 , pp. 1965-1972
    • Bolaos, J.P.1    Heales, S.J.R.2    Land, J.M.3    Clark, J.B.4
  • 34
    • 0030921516 scopus 로고    scopus 로고
    • Pretreatment of astrocytes with interferon-α/β impairs interferon-γ induction of nitric oxide synthase
    • Stewart V.C., Giovannoni G., Land J.M., McDonald W.I., Clark J.B., Heales S.J.R. Pretreatment of astrocytes with interferon-α/β impairs interferon-γ induction of nitric oxide synthase. J. Neurochem. 68:1997;2547-2551.
    • (1997) J. Neurochem. , vol.68 , pp. 2547-2551
    • Stewart, V.C.1    Giovannoni, G.2    Land, J.M.3    McDonald, W.I.4    Clark, J.B.5    Heales, S.J.R.6
  • 35
    • 0031970112 scopus 로고    scopus 로고
    • Peroxynitrite and brain mitochondria: Evidence for increased proton leak
    • Brookes P.S., Land J.M., Clark J.B., Heales S.J.R. Peroxynitrite and brain mitochondria evidence for increased proton leak . J. Neurochem. 70:1998;2195-2202.
    • (1998) J. Neurochem. , vol.70 , pp. 2195-2202
    • Brookes, P.S.1    Land, J.M.2    Clark, J.B.3    Heales, S.J.R.4
  • 36
    • 0029962693 scopus 로고    scopus 로고
    • Glutathione protects astrocytes from peroxynitrite-mediated mitochondrial damage: Implications for neuronal/astrocytic trafficking and neurodegeneration
    • Barker J.E., Bolaos J.P., Land J.M., Clark J.B., Heales S.J.R. Glutathione protects astrocytes from peroxynitrite-mediated mitochondrial damage implications for neuronal/astrocytic trafficking and neurodegeneration . Dev. Neurosci. 18:1996;391-396.
    • (1996) Dev. Neurosci. , vol.18 , pp. 391-396
    • Barker, J.E.1    Bolaos, J.P.2    Land, J.M.3    Clark, J.B.4    Heales, S.J.R.5
  • 37
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: Crucial role of S-nitrosylation of mitochondrial complex I and protective role of glutathione
    • Clementi E., Brown G.C., Feelisch M., Moncada S. Persistent inhibition of cell respiration by nitric oxide crucial role of S-nitrosylation of mitochondrial complex I and protective role of glutathione . Proc. Natl. Acad. Sci. USA. 95:1998;7631-7636.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 38
    • 0034057120 scopus 로고    scopus 로고
    • Oxidative stress and S-nitrosylation of proteins in cells
    • Beltran B., Orsi A., Clementi E., Moncada S. Oxidative stress and S-nitrosylation of proteins in cells. Br. J. Pharmacol. 129:2000;953-960.
    • (2000) Br. J. Pharmacol. , vol.129 , pp. 953-960
    • Beltran, B.1    Orsi, A.2    Clementi, E.3    Moncada, S.4
  • 40
    • 0035097462 scopus 로고    scopus 로고
    • Depletion of glutathione upregulates mitochondrial complex I expression in glial cells
    • Vasquez O.L., Almeida A., Bolaos J.P. Depletion of glutathione upregulates mitochondrial complex I expression in glial cells. J. Neurochem. 76:2001;1593-1596.
    • (2001) J. Neurochem. , vol.76 , pp. 1593-1596
    • Vasquez, O.L.1    Almeida, A.2    Bolaos, J.P.3
  • 41
    • 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
  • 42
    • 0032764173 scopus 로고    scopus 로고
    • Characterization of the human SDHD gene encoding the small subunit of cytochrome b (cybS) in mitochondrial succinate-ubiquinone oxidoreductase
    • Hirawake H., Taniwaki M., Tamura A., Amino H., Tomitsuka E., Kita K. Characterization of the human SDHD gene encoding the small subunit of cytochrome b (cybS) in mitochondrial succinate-ubiquinone oxidoreductase. Biochim. Biophys. Acta. 1412:1999;295-300.
    • (1999) Biochim. Biophys. Acta , vol.1412 , pp. 295-300
    • Hirawake, H.1    Taniwaki, M.2    Tamura, A.3    Amino, H.4    Tomitsuka, E.5    Kita, K.6
  • 43
    • 77957014831 scopus 로고
    • 1 particle, and reconstitution of succinate cytochrome c reductase
    • 1 particle, and reconstitution of succinate cytochrome c reductase. Methods Enzymol. 10:1967;216-225.
    • (1967) Methods Enzymol , vol.10 , pp. 216-225
    • King, T.E.1
  • 46
    • 0028061167 scopus 로고
    • Nitric oxide as a potential pathological mechanism in demyelination: Its differential effects on primary glial cells in vitro
    • Mitrovic B., Ignarro L.J., Montestruque S., Smoll A., Merrill J.E. Nitric oxide as a potential pathological mechanism in demyelination its differential effects on primary glial cells in vitro . Neuroscience. 61:1994;575-585.
    • (1994) Neuroscience , vol.61 , pp. 575-585
    • Mitrovic, B.1    Ignarro, L.J.2    Montestruque, S.3    Smoll, A.4    Merrill, J.E.5
  • 48
    • 0033984710 scopus 로고    scopus 로고
    • The effect of reactive oxygen species generated from mitochondrial electron transport chain on the cytochrome c oxidase and on the cardiolipin content in bovine heart submitochondrial particles
    • Paradies G., Petrosillo G., Pistolese M., Ruggiero F.M. The effect of reactive oxygen species generated from mitochondrial electron transport chain on the cytochrome c oxidase and on the cardiolipin content in bovine heart submitochondrial particles. FEBS Lett. 466:2000;323-326.
    • (2000) FEBS Lett , vol.466 , pp. 323-326
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 50
    • 0019322671 scopus 로고
    • Reactions of nitric oxide with cytochrome c oxidase
    • Brudvig G.W., Stevens T.H., Chan S.I. Reactions of nitric oxide with cytochrome c oxidase. Biochemistry. 19:1980;5275-5285.
    • (1980) Biochemistry , vol.19 , pp. 5275-5285
    • Brudvig, G.W.1    Stevens, T.H.2    Chan, S.I.3
  • 51
    • 0029682487 scopus 로고    scopus 로고
    • Reactions of nitric oxide with metalloproteins
    • Radi R. Reactions of nitric oxide with metalloproteins. Chem. Res. Toxicol. 9:1996;828-835.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 828-835
    • Radi, R.1
  • 52
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown G.C., Cooper C.E. Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase. FEBS Lett. 356:1994;295-298.
    • (1994) FEBS Lett , vol.356 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 53
    • 0029161636 scopus 로고
    • Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase
    • Brown G.C. Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase. FEBS Lett. 369:1995;136-139.
    • (1995) FEBS Lett , vol.369 , pp. 136-139
    • Brown, G.C.1
  • 54
    • 0029122402 scopus 로고
    • Cytochrome c oxidase catalysis of the reduction of nitric oxide to nitrous oxide
    • Zhao X.J., Sampath V., Caughey W.S. Cytochrome c oxidase catalysis of the reduction of nitric oxide to nitrous oxide. Biochem. Biophys. Res. Commun. 212:1995;1054-1060.
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 1054-1060
    • Zhao, X.J.1    Sampath, V.2    Caughey, W.S.3
  • 55
    • 0029986691 scopus 로고    scopus 로고
    • Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles
    • Poderoso J.J., Carreras M.C., Lisdero C.L., Riobo N.A., Schopfer F., Boveris A.D. Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles. Arch. Biochem. Biophys. 328:1996;85-92.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 85-92
    • Poderoso, J.J.1    Carreras, M.C.2    Lisdero, C.L.3    Riobo, N.A.4    Schopfer, F.5    Boveris, A.D.6
  • 57
    • 0029857135 scopus 로고    scopus 로고
    • Superoxide production by mitochondria in the presence of nitric oxide forms peroxynitrite
    • Packer M.A., Porteous C.M., Murphy M.P. Superoxide production by mitochondria in the presence of nitric oxide forms peroxynitrite. Biochem. Mol. Biol. Int. 40:1996;527-534.
    • (1996) Biochem. Mol. Biol. Int. , vol.40 , pp. 527-534
    • Packer, M.A.1    Porteous, C.M.2    Murphy, M.P.3
  • 58
    • 0032553302 scopus 로고    scopus 로고
    • Interaction of peroxynitrite with mitochondrial cytochrome oxidase
    • Sharpe M.A., Cooper C.E. Interaction of peroxynitrite with mitochondrial cytochrome oxidase. J. Biol. Chem. 273:1998;30961-30972.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30961-30972
    • Sharpe, M.A.1    Cooper, C.E.2
  • 59
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide
    • Radi R., Beckman J.S., Bush K.M., Freeman B.A. Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. J. Biol. Chem. 266:1991;4244-4250.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 60
    • 0001363220 scopus 로고
    • The phospholipid composition of mammalian tissues
    • G.B. Ansell, J.N. Hawthorne, Dawson R.M.C. Amsterdam: Elsevier Science Ltd
    • White D.A. The phospholipid composition of mammalian tissues. Ansell G.B., Hawthorne J.N., Dawson R.M.C. Form and function of phospholipids. vol. 3:1973;441-482 Elsevier Science Ltd, Amsterdam.
    • (1973) Form and function of phospholipids , vol.3 , pp. 441-482
    • White, D.A.1
  • 61
    • 0028604337 scopus 로고
    • Trolox protects mitochondrial complex IV from nitric oxide-mediated damage in astrocytes
    • Heales S.J.R., Bolaos J.P., Land J.M., Clark J.B. Trolox protects mitochondrial complex IV from nitric oxide-mediated damage in astrocytes. Brain Res. 668:1994;243-245.
    • (1994) Brain Res , vol.668 , pp. 243-245
    • Heales, S.J.R.1    Bolaos, J.P.2    Land, J.M.3    Clark, J.B.4
  • 62
    • 0028172263 scopus 로고
    • The oxidation of α-tocopherol and Trolox by peroxynitrite
    • Hogg N., Joseph J., Kalyanaraman B. The oxidation of α-tocopherol and Trolox by peroxynitrite. Arch. Biochem. Biophys. 314:1994;153-158.
    • (1994) Arch. Biochem. Biophys. , vol.314 , pp. 153-158
    • Hogg, N.1    Joseph, J.2    Kalyanaraman, B.3
  • 63
    • 0034648103 scopus 로고    scopus 로고
    • Nitric oxide-mediated induction of cytochrome c oxidase mRNA and protein in a mouse macrophage cell line
    • Lehrer-Graiwer J.E., Firestein B.L., Bredt D.S. Nitric oxide-mediated induction of cytochrome c oxidase mRNA and protein in a mouse macrophage cell line. Neurosci. Lett. 288:2000;107-110.
    • (2000) Neurosci. Lett. , vol.288 , pp. 107-110
    • Lehrer-Graiwer, J.E.1    Firestein, B.L.2    Bredt, D.S.3
  • 64
    • 0024561501 scopus 로고
    • Cytochrome oxidase: An endogenous metabolic marker for neuronal activity
    • Wong-Riley M.T.T. Cytochrome oxidase an endogenous metabolic marker for neuronal activity . Trends Neurosci. 12:1989;94-101.
    • (1989) Trends Neurosci , vol.12 , pp. 94-101
    • Wong-Riley, M.T.T.1
  • 65
    • 0030581279 scopus 로고    scopus 로고
    • Do nitric oxide synthase, NMDA receptor subunit R1, and cytochrome oxidase colocalize in the rat central nervous system?
    • Zhang C., Wong-Riley M.T.T. Do nitric oxide synthase, NMDA receptor subunit R1, and cytochrome oxidase colocalize in the rat central nervous system? Brain Res. 729:1996;205-215.
    • (1996) Brain Res , vol.729 , pp. 205-215
    • Zhang, C.1    Wong-Riley, M.T.T.2
  • 66
    • 0035909948 scopus 로고    scopus 로고
    • Different responses of astrocytes and neurons to nitric oxide: The role of glycolytically generated ATP in astrocyte protection
    • Almeida A., Almeida J., Bolaos J.P., Moncada S. Different responses of astrocytes and neurons to nitric oxide the role of glycolytically generated ATP in astrocyte protection . Proc. Natl. Acad. Sci. USA. 98:2001;15294-15299.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15294-15299
    • Almeida, A.1    Almeida, J.2    Bolaos, J.P.3    Moncada, S.4
  • 67
    • 0012642534 scopus 로고    scopus 로고
    • Impairment of brain mitochondrial function by reactive nitrogen species: The role of glutathione in dictating susceptibility
    • Heales S.J.R., Bolaos J.P. Impairment of brain mitochondrial function by reactive nitrogen species the role of glutathione in dictating susceptibility . Neurochem. Int. 1157:2001;1-6.
    • (2001) Neurochem. Int. , vol.1157 , pp. 1-6
    • Heales, S.J.R.1    Bolaos, J.P.2
  • 68
    • 0029981670 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite exert distinct effects on mitochondrial respiration which are differentially blocked by glutathione or glucose
    • Lizasoain I., Moro M.A., Knowles R.G., Darley-Usmar V., Moncada S. Nitric oxide and peroxynitrite exert distinct effects on mitochondrial respiration which are differentially blocked by glutathione or glucose. Biochem. J. 314:1996;877-880.
    • (1996) Biochem. J. , vol.314 , pp. 877-880
    • Lizasoain, I.1    Moro, M.A.2    Knowles, R.G.3    Darley-Usmar, V.4    Moncada, S.5
  • 69
    • 0033555806 scopus 로고    scopus 로고
    • Synthesis of the antioxidant glutathione in neurons: Supply by astrocytes of cys-gly as precursor for neuronal glutathione
    • Dringen R., Pfeiffer B., Hamprecht B. Synthesis of the antioxidant glutathione in neurons supply by astrocytes of cys-gly as precursor for neuronal glutathione . J. Neurosci. 19:1999;562-569.
    • (1999) J. Neurosci. , vol.19 , pp. 562-569
    • Dringen, R.1    Pfeiffer, B.2    Hamprecht, B.3
  • 70
    • 0031004608 scopus 로고    scopus 로고
    • The γ-glutamyltranspeptidase inhibitor acivicin preserves glutathione released by astroclial cells in culture
    • Dringen R., Kranich O., Hamprecht B. The γ-glutamyltranspeptidase inhibitor acivicin preserves glutathione released by astroclial cells in culture. Neurochem. Res. 22:1997;727-733.
    • (1997) Neurochem. Res. , vol.22 , pp. 727-733
    • Dringen, R.1    Kranich, O.2    Hamprecht, B.3
  • 71
    • 0033378590 scopus 로고    scopus 로고
    • Astrocyte nitric oxide causes neuronal mitochondrial damage but antioxidant release limits neuronal cell death
    • Stone R., Stewart V.C., Hurst R.D., Clark J.B., Heales S.J.R. Astrocyte nitric oxide causes neuronal mitochondrial damage but antioxidant release limits neuronal cell death. Ann. NY Acad. Sci. 893:1999;400-403.
    • (1999) Ann. NY Acad. Sci. , vol.893 , pp. 400-403
    • Stone, R.1    Stewart, V.C.2    Hurst, R.D.3    Clark, J.B.4    Heales, S.J.R.5
  • 72
    • 0036826902 scopus 로고    scopus 로고
    • Preservation of extracellular glutathione by an astrocyte-derived factor with properties comparable to superoxide dismutase
    • Stewart V.C., Stone R., Gegg M.E., Sharpe M.A., Hurst R.D., Clark J.B., Heales S.J.R. Preservation of extracellular glutathione by an astrocyte-derived factor with properties comparable to superoxide dismutase. J. Neurochem. 83:2002;984-991.
    • (2002) J. Neurochem. , vol.83 , pp. 984-991
    • Stewart, V.C.1    Stone, R.2    Gegg, M.E.3    Sharpe, M.A.4    Hurst, R.D.5    Clark, J.B.6    Heales, S.J.R.7
  • 73
    • 0033914409 scopus 로고    scopus 로고
    • Astrocyte-derived nitric oxide causes both reversible and irreversible damage to the neuronal mitochondrial respiratory chain
    • Stewart V.C., Sharpe M.A., Clark J.B., Heales S.J.R. Astrocyte-derived nitric oxide causes both reversible and irreversible damage to the neuronal mitochondrial respiratory chain. J. Neurochem. 75:2000;694-700.
    • (2000) J. Neurochem. , vol.75 , pp. 694-700
    • Stewart, V.C.1    Sharpe, M.A.2    Clark, J.B.3    Heales, S.J.R.4
  • 74
    • 0027976087 scopus 로고
    • Vitamin E, ascorbate, glutathione, glutathione disulfide, and enzymes of glutathione metabolism in cultures of chick astrocytes and neurones: Evidence that astrocytes play an important role in antioxidative processes in the brain
    • Makar T.K., Nedergraard M., Preuss A., Gelbard A.S., Perumal A.S., Cooper A.J.L. Vitamin E, ascorbate, glutathione, glutathione disulfide, and enzymes of glutathione metabolism in cultures of chick astrocytes and neurones evidence that astrocytes play an important role in antioxidative processes in the brain . J. Neurochem. 62:1994;45-53.
    • (1994) J. Neurochem. , vol.62 , pp. 45-53
    • Makar, T.K.1    Nedergraard, M.2    Preuss, A.3    Gelbard, A.S.4    Perumal, A.S.5    Cooper, A.J.L.6
  • 75
    • 0031972780 scopus 로고    scopus 로고
    • Pretreatment of astrocytes with interferon-α/β prevents neuronal mitochondrial respiratory chain damage
    • Stewart V.C., Land J.M., Clark J.B., Heales S.J.R. Pretreatment of astrocytes with interferon-α/β prevents neuronal mitochondrial respiratory chain damage. J. Neurochem. 70:1998;432-434.
    • (1998) J. Neurochem. , vol.70 , pp. 432-434
    • Stewart, V.C.1    Land, J.M.2    Clark, J.B.3    Heales, S.J.R.4
  • 76
    • 0027221653 scopus 로고
    • Nitric oxide synthase induction in glial cells: Effect on neuronal survival
    • Demerl-Pallardy C., Lonchampt M.O., Chabrier P.E., Braquet P. Nitric oxide synthase induction in glial cells effect on neuronal survival . Life Sci. 52:1993;1883-1890.
    • (1993) Life Sci , vol.52 , pp. 1883-1890
    • Demerl-Pallardy, C.1    Lonchampt, M.O.2    Chabrier, P.E.3    Braquet, P.4
  • 77
    • 0027932457 scopus 로고
    • Selective potentiation of NMDA-induced neuronal injury following induction of astrocytic iNOS
    • Hewett S.J., Csernansky C.A., Choi D.W. Selective potentiation of NMDA-induced neuronal injury following induction of astrocytic iNOS. Neuron. 13:1994;487-494.
    • (1994) Neuron , vol.13 , pp. 487-494
    • Hewett, S.J.1    Csernansky, C.A.2    Choi, D.W.3
  • 78
    • 0028089896 scopus 로고
    • Expression of inducible nitric oxide synthase causes delayed neurotoxicity in primary mixed neuronal-glial cortical cultures
    • Dawson V.L., Brahmbhatt H.P., Mong J.A., Dawson T.M. Expression of inducible nitric oxide synthase causes delayed neurotoxicity in primary mixed neuronal-glial cortical cultures. Neuropharmacology. 33:1994;1425-1430.
    • (1994) Neuropharmacology , vol.33 , pp. 1425-1430
    • Dawson, V.L.1    Brahmbhatt, H.P.2    Mong, J.A.3    Dawson, T.M.4
  • 80
    • 0026702955 scopus 로고
    • Microglial-produced nitric oxide and reactive nitrogen oxides mediate neuronal cell death
    • Boje K.M., Arora P.K. Microglial-produced nitric oxide and reactive nitrogen oxides mediate neuronal cell death. Brain Res. 587:1992;250-256.
    • (1992) Brain Res , vol.587 , pp. 250-256
    • Boje, K.M.1    Arora, P.K.2
  • 81
    • 85031235978 scopus 로고    scopus 로고
    • Comparing the effects of astrocytes and microglia on neurons in coculture
    • Stewart V.C., Clark J.B., Heales S.J.R. Comparing the effects of astrocytes and microglia on neurons in coculture. Eur. J. Neurosci. 2:(Suppl. 11):2000;354.
    • (2000) Eur. J. Neurosci. , vol.2 , Issue.SUPPL. 11 , pp. 354
    • Stewart, V.C.1    Clark, J.B.2    Heales, S.J.R.3
  • 82
    • 0027161216 scopus 로고
    • Microglial cell cytotoxicity of oligodendrocytes is mediated through nitric oxide
    • Merrill J., Ignarro L.J., Sherman M.P., Melinek J., Lane T.E. Microglial cell cytotoxicity of oligodendrocytes is mediated through nitric oxide. J. Immunol. 151:1993;2132-2141.
    • (1993) J. Immunol. , vol.151 , pp. 2132-2141
    • Merrill, J.1    Ignarro, L.J.2    Sherman, M.P.3    Melinek, J.4    Lane, T.E.5
  • 84
    • 0030108525 scopus 로고    scopus 로고
    • Cytokine-stimulated astrocytes damage human neurons via a nitric oxide mechanism
    • Chao C.C., Hu S., Sheng W.S., Bu D., Bukrinsky M.I., Peterson P. Cytokine-stimulated astrocytes damage human neurons via a nitric oxide mechanism. Glia. 16:1996;276-284.
    • (1996) Glia , vol.16 , pp. 276-284
    • Chao, C.C.1    Hu, S.2    Sheng, W.S.3    Bu, D.4    Bukrinsky, M.I.5    Peterson, P.6
  • 85
    • 0032495195 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase expression is selectively induced in astrocytes isolated from adult human brain
    • Zhao M.L., Liu J.S.H., He D., Dickson D.W., Lee S.C. Inducible nitric oxide synthase expression is selectively induced in astrocytes isolated from adult human brain. Brain Res. 813:1998;402-405.
    • (1998) Brain Res , vol.813 , pp. 402-405
    • Zhao, M.L.1    Liu, J.S.H.2    He, D.3    Dickson, D.W.4    Lee, S.C.5
  • 86
    • 0031882897 scopus 로고    scopus 로고
    • Nitric oxide causes glutamate release from brain synaptosomes
    • McNaught K.S., Brown G.C. Nitric oxide causes glutamate release from brain synaptosomes. J. Neurochem. 70:1998;1541-1546.
    • (1998) J. Neurochem. , vol.70 , pp. 1541-1546
    • McNaught, K.S.1    Brown, G.C.2
  • 87
    • 0035449358 scopus 로고    scopus 로고
    • Inflammatory neurodegeneration mediated by nitric oxide from activated glia-inhibiting neuronal respiration, causing glutamate release and excitoxicity
    • Bal-Price A., Brown G.C. Inflammatory neurodegeneration mediated by nitric oxide from activated glia-inhibiting neuronal respiration, causing glutamate release and excitoxicity. J. Neurosci. 21:2001;6480-6491.
    • (2001) J. Neurosci. , vol.21 , pp. 6480-6491
    • Bal-Price, A.1    Brown, G.C.2
  • 88
    • 0033230821 scopus 로고    scopus 로고
    • Excitotoxic mitochondrial depolarization requires both calcium and nitric oxide in rat hippocampal neurons
    • Keelan J., Vergun O., Duchen M.R. Excitotoxic mitochondrial depolarization requires both calcium and nitric oxide in rat hippocampal neurons. J. Physiol. 520:1999;797-813.
    • (1999) J. Physiol. , vol.520 , pp. 797-813
    • Keelan, J.1    Vergun, O.2    Duchen, M.R.3
  • 90
    • 0032550199 scopus 로고    scopus 로고
    • Glutamate neurotoxicity is associated with nitric oxide-mediated mitochondrial dysfunction and glutathione depletion
    • Almeida A., Heales S.J.R., Bolaos J.P., Medina J.M. Glutamate neurotoxicity is associated with nitric oxide-mediated mitochondrial dysfunction and glutathione depletion. Brain Res. 790:1998;209-216.
    • (1998) Brain Res , vol.790 , pp. 209-216
    • Almeida, A.1    Heales, S.J.R.2    Bolaos, J.P.3    Medina, J.M.4
  • 92
    • 0025456905 scopus 로고
    • Structure-activity relationships for amino acid transmitter candidates acting at N-methyl-D-aspartate and quisqualate receptors
    • Patneau D.K., Mayer M.L. Structure-activity relationships for amino acid transmitter candidates acting at N-methyl-D-aspartate and quisqualate receptors. J. Neurosci. 10:1990;2385-2399.
    • (1990) J. Neurosci. , vol.10 , pp. 2385-2399
    • Patneau, D.K.1    Mayer, M.L.2
  • 93
    • 0028872674 scopus 로고
    • Excitotoxicity and the NMDA receptor: Still lethal after eight years
    • Rothman S.M., Olney J.W. Excitotoxicity and the NMDA receptor still lethal after eight years . Trends Neurosci. 18:1995;57-58.
    • (1995) Trends Neurosci , vol.18 , pp. 57-58
    • Rothman, S.M.1    Olney, J.W.2
  • 94
    • 0031816414 scopus 로고    scopus 로고
    • Apoptosis, excitotoxicity, and neuropathology
    • Leist M., Nicotera P. Apoptosis, excitotoxicity, and neuropathology. Exp. Cell Res. 239:1998;183-201.
    • (1998) Exp. Cell Res. , vol.239 , pp. 183-201
    • Leist, M.1    Nicotera, P.2
  • 95
    • 0029064518 scopus 로고
    • Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation
    • Reynolds I.J., Hastings T.G. Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation. J. Neurosci. 15:1995;3318-3327.
    • (1995) J. Neurosci. , vol.15 , pp. 3318-3327
    • Reynolds, I.J.1    Hastings, T.G.2
  • 96
    • 0026775370 scopus 로고
    • Blockade of nitric oxide formation does not prevent glutamate-induced neurotoxicity in neuronal cultures from rat hippocampus
    • Pauwels P.J., Leysen J.E. Blockade of nitric oxide formation does not prevent glutamate-induced neurotoxicity in neuronal cultures from rat hippocampus. Neurosci. Lett. 143:1992;27-30.
    • (1992) Neurosci. Lett. , vol.143 , pp. 27-30
    • Pauwels, P.J.1    Leysen, J.E.2
  • 97
    • 0028126477 scopus 로고
    • Nitric oxide does not mediate acute glutamate neurotoxicity, nor is it neuroprotective, in rat brain slices
    • Garthwaite G., Garthwaite J. Nitric oxide does not mediate acute glutamate neurotoxicity, nor is it neuroprotective, in rat brain slices. Neuropharmacology. 33:1994;1431-1438.
    • (1994) Neuropharmacology , vol.33 , pp. 1431-1438
    • Garthwaite, G.1    Garthwaite, J.2
  • 98
    • 0023877523 scopus 로고
    • Vulnerability of cultured cortical neurons to damage by excitotoxins: Differential susceptibility of neurons containing NADPH-diaphorase
    • Koh J.Y., Choi D.W. Vulnerability of cultured cortical neurons to damage by excitotoxins differential susceptibility of neurons containing NADPH-diaphorase . J. Neurosci. 8:1988;2153-2163.
    • (1988) J. Neurosci. , vol.8 , pp. 2153-2163
    • Koh, J.Y.1    Choi, D.W.2
  • 99
    • 0027178135 scopus 로고
    • Mechanisms of nitric oxide-mediated neurotoxicity in primary brain cultures
    • Dawson V.L., Dawson T.M., Bartley D.A., Uhl G.R., Snyder S.H. Mechanisms of nitric oxide-mediated neurotoxicity in primary brain cultures. J. Neurosci. 13:1993;2651-2661.
    • (1993) J. Neurosci. , vol.13 , pp. 2651-2661
    • Dawson, V.L.1    Dawson, T.M.2    Bartley, D.A.3    Uhl, G.R.4    Snyder, S.H.5
  • 100
    • 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
  • 101
    • 0032557511 scopus 로고    scopus 로고
    • Energy thresholds in brain mitochondria
    • Davey G.P., Peuchen S., Clark J.B. Energy thresholds in brain mitochondria. 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
  • 102
    • 0028793257 scopus 로고
    • Glutamate-induced neuronal death: A succession of necrosis or apoptosis depending on mitochondrial function
    • Ankarcrona M., Dypbukt J.M., Bonfoco E., Zhivotovsky B., Orrenius S., Lipton S.A., Nicotera P. Glutamate-induced neuronal death a succession of necrosis or apoptosis depending on mitochondrial function . Neuron. 15:1995;961-973.
    • (1995) Neuron , vol.15 , pp. 961-973
    • Ankarcrona, M.1    Dypbukt, J.M.2    Bonfoco, E.3    Zhivotovsky, B.4    Orrenius, S.5    Lipton, S.A.6    Nicotera, P.7
  • 103
    • 84975751684 scopus 로고
    • Complex I inhibitors induce dose-dependent apoptosis in PC12 cells: Relevance to Parkinson's disease
    • Hartley A., Stone J.M., Heron C., Cooper J.M., Schapira A.H.V. Complex I inhibitors induce dose-dependent apoptosis in PC12 cells relevance to Parkinson's disease . J. Neurochem. 63:1994;1987-1990.
    • (1994) J. Neurochem. , vol.63 , pp. 1987-1990
    • Hartley, A.1    Stone, J.M.2    Heron, C.3    Cooper, J.M.4    Schapira, A.H.V.5
  • 105
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M., Szabo I. The mitochondrial permeability transition. Biochim. Biophys. Acta. 1241:1995;139-176.
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 106
    • 0030580287 scopus 로고    scopus 로고
    • Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell
    • Skulachev V.P. Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell. FEBS Lett. 397:1996;7-10.
    • (1996) FEBS Lett , vol.397 , pp. 7-10
    • Skulachev, V.P.1
  • 108
    • 0028306269 scopus 로고
    • Peroxynitrite causes calcium efflux from mitochondria which is prevented by cyclosporin A
    • Packer M.A., Murphy M.P. Peroxynitrite causes calcium efflux from mitochondria which is prevented by cyclosporin A. FEBS Lett. 345:1994;237-240.
    • (1994) FEBS Lett , vol.345 , pp. 237-240
    • Packer, M.A.1    Murphy, M.P.2
  • 110
    • 0030800033 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in the central nervous system: Induction by calcium cycling-dependent and -independent pathways
    • Kristal B.S., Dubinsky J.M. Mitochondrial permeability transition in the central nervous system induction by calcium cycling-dependent and -independent pathways . J. Neurochem. 69:1997;524-538.
    • (1997) J. Neurochem. , vol.69 , pp. 524-538
    • Kristal, B.S.1    Dubinsky, J.M.2
  • 111
    • 0030298459 scopus 로고    scopus 로고
    • Cyclosporin A delays mitochondrial depolarization induced by N-methyl-D-aspartate in cortical neurons: Evidence of the mitochondrial permeability transition
    • Nieminen A.L., Petrie T.G., LeMasters J.J., Selman W.R. Cyclosporin A delays mitochondrial depolarization induced by N-methyl-D-aspartate in cortical neurons evidence of the mitochondrial permeability transition . Neuroscience. 75:1996;993-997.
    • (1996) Neuroscience , vol.75 , pp. 993-997
    • Nieminen, A.L.1    Petrie, T.G.2    LeMasters, J.J.3    Selman, W.R.4
  • 112
    • 0031571757 scopus 로고    scopus 로고
    • 2+-independent permeabilization of the inner mitochondrial membrane by peroxynitrite is mediated by membrane protein thiol cross-linking and lipid peroxidation
    • 2+-independent permeabilization of the inner mitochondrial membrane by peroxynitrite is mediated by membrane protein thiol cross-linking and lipid peroxidation. Arch. Biochem. Biophys. 345:1997;243-250.
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 243-250
    • Gadelha, F.R.1    Thomson, L.2    Fagian, M.M.3    Costa, A.D.T.4    Radi, R.5    Vercesi, A.E.6
  • 113
    • 0030941354 scopus 로고    scopus 로고
    • Modulation of the mitochondrial permeability transition by nitric oxide
    • Balakirev M.Y., Khramtsov V.V., Zimmer G. Modulation of the mitochondrial permeability transition by nitric oxide. Eur. J. Biochem. 246:1997;710-718.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 710-718
    • Balakirev, M.Y.1    Khramtsov, V.V.2    Zimmer, G.3
  • 114
    • 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
  • 116
    • 0028364696 scopus 로고
    • Immunocytochemical analysis of tumor necrosis factor and its receptors in Parkinson's disease
    • Boka G., Anglade P., Wallach D., Javoy-Agid F., Agid Y. Immunocytochemical analysis of tumor necrosis factor and its receptors in Parkinson's disease. Neurosci. Lett. 172:1994;151-154.
    • (1994) Neurosci. Lett. , vol.172 , pp. 151-154
    • Boka, G.1    Anglade, P.2    Wallach, D.3    Javoy-Agid, F.4    Agid, Y.5
  • 122
    • 0030682431 scopus 로고    scopus 로고
    • Neurotoxicity and possible roles of aspartic acid, glutamic acid, and GABA in some neurological disorders
    • Qureshi G.A., Baia S.M., Parvez S. Neurotoxicity and possible roles of aspartic acid, glutamic acid, and GABA in some neurological disorders. Biogenic Amines. 13:1998;565-578.
    • (1998) Biogenic Amines , vol.13 , pp. 565-578
    • Qureshi, G.A.1    Baia, S.M.2    Parvez, S.3
  • 124
    • 0026598930 scopus 로고
    • Irreversible inhibition of mitochondrial complex I by 1-methyl-4-phenylpyridinium: Evidence for free radical involvement
    • Cleeter M.J.W., Cooper J.M., Schapira A.H.V. Irreversible inhibition of mitochondrial complex I by 1-methyl-4-phenylpyridinium evidence for free radical involvement . J. Neurochem. 58:1992;786-789.
    • (1992) J. Neurochem. , vol.58 , pp. 786-789
    • Cleeter, M.J.W.1    Cooper, J.M.2    Schapira, A.H.V.3
  • 125
    • 0029969350 scopus 로고    scopus 로고
    • Nature of inhibition of mitochondrial respiratory complex I by 6-hydroxydopamine
    • Glinka Y., Tipton K.F., Youdim M.B.H. Nature of inhibition of mitochondrial respiratory complex I by 6-hydroxydopamine. J. Neurochem. 66:1996;2004-2010.
    • (1996) J. Neurochem. , vol.66 , pp. 2004-2010
    • Glinka, Y.1    Tipton, K.F.2    Youdim, M.B.H.3
  • 126
    • 0026635461 scopus 로고
    • Oxidative stress as a cause of nigral cell death in Parkinson's disease and incidental Lewy body disease
    • Jenner P., Dexter D.T., Sian J., Schapira A.H.V., Marsden C.D. Oxidative stress as a cause of nigral cell death in Parkinson's disease and incidental Lewy body disease. Ann. Neurol. 32:1992;S82-S87.
    • (1992) Ann. Neurol. , vol.32
    • Jenner, P.1    Dexter, D.T.2    Sian, J.3    Schapira, A.H.V.4    Marsden, C.D.5
  • 127
    • 0032169935 scopus 로고    scopus 로고
    • Mitochondrial impairment as an early event in the process of apoptosis induced by glutathione depletion in neuronal cells: Relevance to Parkinson's Disease
    • Merad-Boudia M., Nicole A., Santiard-Baron D., Saille C., Ceballos-Picot I. Mitochondrial impairment as an early event in the process of apoptosis induced by glutathione depletion in neuronal cells relevance to Parkinson's Disease . Biochem. Pharmacol. 56:1998;645-655.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 645-655
    • Merad-Boudia, M.1    Nicole, A.2    Santiard-Baron, D.3    Saille, C.4    Ceballos-Picot, I.5
  • 128
    • 0028799706 scopus 로고
    • Clark, J. B. Depletion of brain glutathione is accompanied by impaired mitochondrial function and decreased N-acetyl aspartate concentration
    • Heales S.J.R., Davies S.E.C., Bates T.E. Clark, J. B. Depletion of brain glutathione is accompanied by impaired mitochondrial function and decreased N-acetyl aspartate concentration. Neurochem. Res. 20:1995;31-38.
    • (1995) Neurochem. Res. , vol.20 , pp. 31-38
    • Heales, S.J.R.1    Davies, S.E.C.2    Bates, T.E.3
  • 129
    • 0021813419 scopus 로고
    • An immunochemical study of the pyruvate dehydrogenase deficit in Alzheimer's disease brain
    • Sheu K.F.R., Kim Y.T., Blass J.P., Weksler M.E. An immunochemical study of the pyruvate dehydrogenase deficit in Alzheimer's disease brain. Ann. Neurol. 17:1985;444-449.
    • (1985) Ann. Neurol. , vol.17 , pp. 444-449
    • Sheu, K.F.R.1    Kim, Y.T.2    Blass, J.P.3    Weksler, M.E.4
  • 130
    • 0028387219 scopus 로고
    • Abnormality of the α-ketoglutarate dehydrogenase complex in fibroblasts from familial Alzheimer's disease
    • Sheu K.F.R., Cooper A.J.L., Koike K., Koike M., Lindsay J.G., Blass J.P. Abnormality of the α-ketoglutarate dehydrogenase complex in fibroblasts from familial Alzheimer's disease. Ann. Neurol. 35:1994;312-318.
    • (1994) Ann. Neurol. , vol.35 , pp. 312-318
    • Sheu, K.F.R.1    Cooper, A.J.L.2    Koike, K.3    Koike, M.4    Lindsay, J.G.5    Blass, J.P.6
  • 132
    • 0028124916 scopus 로고
    • Nitric oxide synthase activation is elevated in brain microvessels in Alzheimer's disease
    • Dorheim M.A., Tracey W.R., Pollock J.S., Grammas P. Nitric oxide synthase activation is elevated in brain microvessels in Alzheimer's disease. Biochem. Biophys. Res. Commun. 205:1994;659-665.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 659-665
    • Dorheim, M.A.1    Tracey, W.R.2    Pollock, J.S.3    Grammas, P.4
  • 133
    • 0028893441 scopus 로고
    • Increased number of NADPH-D-positive neurons within the substantia innominata in Alzheimer's disease
    • Benzing W.C., Mufson E.J. Increased number of NADPH-D-positive neurons within the substantia innominata in Alzheimer's disease. Brain. 670:1995;351-355.
    • (1995) Brain , vol.670 , pp. 351-355
    • Benzing, W.C.1    Mufson, E.J.2
  • 136
    • 0028173033 scopus 로고
    • S100β protein expression in Alzheimer's disease: Potential role in the pathogenesis of neuritic plaques
    • Sheng J.G., Mrak R.E., Griffin W.S.T. S100β protein expression in Alzheimer's disease potential role in the pathogenesis of neuritic plaques . J. Neurosci. Res. 39:1994;398-404.
    • (1994) J. Neurosci. Res. , vol.39 , pp. 398-404
    • Sheng, J.G.1    Mrak, R.E.2    Griffin, W.S.T.3
  • 137
    • 0029671449 scopus 로고    scopus 로고
    • S100β stimulates inducible nitric oxide synthase activity and mRNA levels in rat cortical astrocytes
    • Hu J., Castets F., Guevara J.L., Van Eldik L.J. S100β stimulates inducible nitric oxide synthase activity and mRNA levels in rat cortical astrocytes. J. Biol. Chem. 271:1996;2543-2547.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2543-2547
    • Hu, J.1    Castets, F.2    Guevara, J.L.3    Van Eldik, L.J.4
  • 138
    • 0030583248 scopus 로고    scopus 로고
    • Synergistic induction of nitric oxide by β-amyloid and cytokines in astrocytes
    • Rossi F., Bianchini E. Synergistic induction of nitric oxide by β-amyloid and cytokines in astrocytes. Biochem. Biophys. Res. Commun. 225:1996;474-478.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 474-478
    • Rossi, F.1    Bianchini, E.2
  • 139
    • 0031127418 scopus 로고    scopus 로고
    • Nitric oxide synthase in reactive astrocytes adjacent to β-amyloid plaques
    • Wallace M.N., Geddes J.G., Farquhar D.A., Mason M.R. Nitric oxide synthase in reactive astrocytes adjacent to β-amyloid plaques. Exp. Neurol. 144:1997;266-272.
    • (1997) Exp. Neurol. , vol.144 , pp. 266-272
    • Wallace, M.N.1    Geddes, J.G.2    Farquhar, D.A.3    Mason, M.R.4
  • 140
    • 0032510692 scopus 로고    scopus 로고
    • Amyloid β peptide stimulates nitric oxide production in astrocytes through an NF-κB-dependent mechanism
    • Akama K.T., Albanese C., Pestell R.G., Van Eldik L.J. Amyloid β peptide stimulates nitric oxide production in astrocytes through an NF-κB-dependent mechanism. Proc. Natl. Acad. Sci. USA. 95:1998;5795-5800.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5795-5800
    • Akama, K.T.1    Albanese, C.2    Pestell, R.G.3    Van Eldik, L.J.4
  • 141
    • 0012701946 scopus 로고    scopus 로고
    • Amyloid β peptide inhibits mitochondrial enzymes and function
    • Canevari L., Casley C.S., Sharpe M.A., Land J.M. Amyloid β peptide inhibits mitochondrial enzymes and function. J. Neurochem. 76:(Suppl. 1):2001;30.
    • (2001) J. Neurochem. , vol.76 , Issue.SUPPL. 1 , pp. 30
    • Canevari, L.1    Casley, C.S.2    Sharpe, M.A.3    Land, J.M.4
  • 142
    • 0032810909 scopus 로고    scopus 로고
    • Beta-amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria
    • Canevari L., Clark J.B., Bates T.E. Beta-amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria. FEBS Lett. 457:1999;131-134.
    • (1999) FEBS Lett , vol.457 , pp. 131-134
    • Canevari, L.1    Clark, J.B.2    Bates, T.E.3
  • 143
    • 0036272650 scopus 로고    scopus 로고
    • Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • Casley C.S., Canevari L., Land J.M., Clark J.B., Sharpe M.A. Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities. J. Neurochem. 80:2002;91-100.
    • (2002) J. Neurochem. , vol.80 , pp. 91-100
    • Casley, C.S.1    Canevari, L.2    Land, J.M.3    Clark, J.B.4    Sharpe, M.A.5
  • 148
    • 0028868821 scopus 로고
    • Expression of the inducible isoform of nitric oxide synthase in the central nervous system of mice correlates with the severity of actively induced experimental allergic encephalitis
    • Okuda Y., Nakatsuji Y., Fujimura H., Esumi H., Ogura T., Yanagihara T., Sakada S. Expression of the inducible isoform of nitric oxide synthase in the central nervous system of mice correlates with the severity of actively induced experimental allergic encephalitis. J. Neuroimmunol. 62:1995;103-112.
    • (1995) J. Neuroimmunol. , vol.62 , pp. 103-112
    • Okuda, Y.1    Nakatsuji, Y.2    Fujimura, H.3    Esumi, H.4    Ogura, T.5    Yanagihara, T.6    Sakada, S.7
  • 149
    • 0031059091 scopus 로고    scopus 로고
    • Nitric oxide synthase type II expression by different cell types in MHV-JHM encephalitis suggests distinct roles for nitric oxide in acute vs. persistent virus infection
    • Grzybicki D., Kwack K.B., Perlman S., Murphy S. Nitric oxide synthase type II expression by different cell types in MHV-JHM encephalitis suggests distinct roles for nitric oxide in acute vs. persistent virus infection. J. Neuroimmunol. 73:1997;15-27.
    • (1997) J. Neuroimmunol. , vol.73 , pp. 15-27
    • Grzybicki, D.1    Kwack, K.B.2    Perlman, S.3    Murphy, S.4
  • 151
    • 0029933293 scopus 로고    scopus 로고
    • Nitric oxide induced perturbation in a cell culture model of the blood brain barrier
    • Hurst R.D., Fritz I.B. Nitric oxide induced perturbation in a cell culture model of the blood brain barrier. J. Cell Physiol. 167:1996;89-94.
    • (1996) J. Cell Physiol. , vol.167 , pp. 89-94
    • Hurst, R.D.1    Fritz, I.B.2
  • 152
    • 0031439343 scopus 로고    scopus 로고
    • Nitric oxide donors reversibly block axonal conduction: Demyelinated axons are especially susceptible
    • Redford E.J., Kapoor R., Smith K.J. Nitric oxide donors reversibly block axonal conduction demyelinated axons are especially susceptible . Brain. 120:1997;2149-2157.
    • (1997) Brain , vol.120 , pp. 2149-2157
    • Redford, E.J.1    Kapoor, R.2    Smith, K.J.3
  • 153
    • 0034662806 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial DNA and activity of mitochondrial enzymes in chronic active lesions of multiple sclerosis
    • Lu F., Selak M., O'Connor J., Croul S., Lorenzana C., Butunoi C., Kalman B. Oxidative damage to mitochondrial DNA and activity of mitochondrial enzymes in chronic active lesions of multiple sclerosis. J. Neurol. Sci. 177:2000;95-103.
    • (2000) J. Neurol. Sci. , vol.177 , pp. 95-103
    • Lu, F.1    Selak, M.2    O'Connor, J.3    Croul, S.4    Lorenzana, C.5    Butunoi, C.6    Kalman, B.7
  • 154
    • 0028874051 scopus 로고
    • Inhibition of brain microglial respiratory chain enzyme activity in experimental autoimmune encephalomyelitis of the Lewis rat
    • Zielasek J., Reichmann H., Kunzig H., Jung S., Hartung H.P., Toyka K.V. Inhibition of brain microglial respiratory chain enzyme activity in experimental autoimmune encephalomyelitis of the Lewis rat. Neurosci. Lett. 184:1995;129-132.
    • (1995) Neurosci. Lett. , vol.184 , pp. 129-132
    • Zielasek, J.1    Reichmann, H.2    Kunzig, H.3    Jung, S.4    Hartung, H.P.5    Toyka, K.V.6
  • 157
    • 0028792005 scopus 로고
    • Reversible decreases in N-acetyl aspartate after acute brain injury
    • DeStefano N., Matthews P.M., Arnold D.L. Reversible decreases in N-acetyl aspartate after acute brain injury. Magn. Res. Med. 34:1995;721-727.
    • (1995) Magn. Res. Med. , vol.34 , pp. 721-727
    • DeStefano, N.1    Matthews, P.M.2    Arnold, D.L.3
  • 158
    • 0015289197 scopus 로고
    • N-acetyl-L-aspartic acid content in human neural tumors and bovine peripheral nervous tissues
    • Nadier J.V., Cooper J.R. N-acetyl-L-aspartic acid content in human neural tumors and bovine peripheral nervous tissues. J. Neurochem. 19:1972;313-319.
    • (1972) J. Neurochem. , vol.19 , pp. 313-319
    • Nadier, J.V.1    Cooper, J.R.2
  • 159
    • 0027450301 scopus 로고
    • Proton nuclear magnetic resonance spectroscopy unambiguously identifies different neural cell types
    • Urenjak J., Williams S.R., Gadian D.G., Noble M. Proton nuclear magnetic resonance spectroscopy unambiguously identifies different neural cell types. J. Neurosci. 13:1993;981-989.
    • (1993) J. Neurosci. , vol.13 , pp. 981-989
    • Urenjak, J.1    Williams, S.R.2    Gadian, D.G.3    Noble, M.4
  • 160
    • 0033961818 scopus 로고    scopus 로고
    • In vitro expression of N-acetyl aspartate by oligodendrocytes: Implications for proton magnetic resonance spectroscopy signal in vivo
    • Bhakoo K.K., Pearce D. In vitro expression of N-acetyl aspartate by oligodendrocytes implications for proton magnetic resonance spectroscopy signal in vivo . J. Neurochem. 74:2000;254-262.
    • (2000) J. Neurochem. , vol.74 , pp. 254-262
    • Bhakoo, K.K.1    Pearce, D.2
  • 161
    • 0018622817 scopus 로고
    • Synthesis of N-acetyl-L-aspartate by rat mitochondria and its involvement in mitochondrial/cytosolic carbon transport
    • Patel T.B., Clark J.B. Synthesis of N-acetyl-L-aspartate by rat mitochondria and its involvement in mitochondrial/cytosolic carbon transport. Biochem. J. 184:1979;539-546.
    • (1979) Biochem. J. , vol.184 , pp. 539-546
    • Patel, T.B.1    Clark, J.B.2
  • 165
    • 0033018506 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase upregulation in a transgenic mouse model of familial ALS
    • Almer G., Vukovasic S., Romero N., Prezedborski S. Inducible nitric oxide synthase upregulation in a transgenic mouse model of familial ALS. J. Neurochem. 72:1999;2415-2425.
    • (1999) J. Neurochem. , vol.72 , pp. 2415-2425
    • Almer, G.1    Vukovasic, S.2    Romero, N.3    Prezedborski, S.4
  • 166
    • 0035826750 scopus 로고    scopus 로고
    • Nitrotyrosination contributes minimally to toxicity of mutant SOD1 associated with ALS
    • Doroudchi M.M., Minotti S., Figlewicz D.A., Durham H.D. Nitrotyrosination contributes minimally to toxicity of mutant SOD1 associated with ALS. Neuroreport. 12:2001;1239-1243.
    • (2001) Neuroreport , vol.12 , pp. 1239-1243
    • Doroudchi, M.M.1    Minotti, S.2    Figlewicz, D.A.3    Durham, H.D.4
  • 167
    • 0029004898 scopus 로고
    • Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis
    • Collard J.F., Cote F., Julien J.P. Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis. Nature. 375:1995;61-64.
    • (1995) Nature , vol.375 , pp. 61-64
    • Collard, J.F.1    Cote, F.2    Julien, J.P.3
  • 168
    • 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., Yamaucji M., Shibayama K., Ando M., Honda M., Nagata Y. 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. 45:1996;276-281.
    • (1996) J. Neurosci. Res. , vol.45 , pp. 276-281
    • Fujita, K.1    Yamaucji, M.2    Shibayama, K.3    Ando, M.4    Honda, M.5    Nagata, Y.6
  • 169
    • 0032496695 scopus 로고    scopus 로고
    • Role of brain nitric oxide in 3,4-methylenedioxymethamphetamine- (MDMA-) induced neurotoxicity in rats
    • Zhen Y.W., Laverty R. Role of brain nitric oxide in 3,4-methylenedioxymethamphetamine- (MDMA-) induced neurotoxicity in rats. Brain Res. 795:1998;257-263.
    • (1998) Brain Res , vol.795 , pp. 257-263
    • Zhen, Y.W.1    Laverty, R.2
  • 170
    • 0035679302 scopus 로고    scopus 로고
    • A study of the mechanisms inolved in the neurotoxic action of 3,4-methylenedioxymethamphetamine (MDMA, ecstasy) on dopamine neurones in mouse brain
    • Colado M.I., Camarero J., Meehan A.O., Sanchez V., Esteban B., Elliott J.M., Green A.R. A study of the mechanisms inolved in the neurotoxic action of 3,4-methylenedioxymethamphetamine (MDMA, ecstasy) on dopamine neurones in mouse brain. Br. J. Pharmacol. 134:2001;1711-1723.
    • (2001) Br. J. Pharmacol. , vol.134 , pp. 1711-1723
    • Colado, M.I.1    Camarero, J.2    Meehan, A.O.3    Sanchez, V.4    Esteban, B.5    Elliott, J.M.6    Green, A.R.7
  • 171
    • 0032696491 scopus 로고    scopus 로고
    • Systemic adminstration of D-amphetamine induced a delayed production of nitric oxide in the striatum of rats
    • Lin H.C., Kang B.H., Wong C.S., Mao S.P., Wan F.J. Systemic adminstration of D-amphetamine induced a delayed production of nitric oxide in the striatum of rats. Neurosci. Lett. 276:1999;141-144.
    • (1999) Neurosci. Lett. , vol.276 , pp. 141-144
    • Lin, H.C.1    Kang, B.H.2    Wong, C.S.3    Mao, S.P.4    Wan, F.J.5
  • 172
    • 0034625498 scopus 로고    scopus 로고
    • Rapid and transient inhibition of mitochondrial function following methamphetamine or 3,4-methylenedioxymethamphetamine administration
    • Burrows K.B., Gudelsky G., Yamamoto B.K. Rapid and transient inhibition of mitochondrial function following methamphetamine or 3,4-methylenedioxymethamphetamine administration. Eur. J. Pharmacol. 398:2000;11-18.
    • (2000) Eur. J. Pharmacol. , vol.398 , pp. 11-18
    • Burrows, K.B.1    Gudelsky, G.2    Yamamoto, B.K.3
  • 173
    • 0031557098 scopus 로고    scopus 로고
    • Impairment of mitochondrial respiration and electron transport chain enzymes during cocaine-induced hepatic injury
    • Devi B.G., Chan A.W.K. Impairment of mitochondrial respiration and electron transport chain enzymes during cocaine-induced hepatic injury. Life Sci. 60:1997;849-855.
    • (1997) Life Sci , vol.60 , pp. 849-855
    • Devi, B.G.1    Chan, A.W.K.2
  • 174
    • 0034069847 scopus 로고    scopus 로고
    • Effect of cocaine on mitochondrial electron transport chain evaluated in primary cultures of neonatal rat myocardial cells and in isolated mitochondrial preparations
    • Yuan C., Acosta D. Effect of cocaine on mitochondrial electron transport chain evaluated in primary cultures of neonatal rat myocardial cells and in isolated mitochondrial preparations. Drug Chem. Toxicol. 23:2000;339-348.
    • (2000) Drug Chem. Toxicol. , vol.23 , pp. 339-348
    • Yuan, C.1    Acosta, D.2
  • 175
    • 0026501020 scopus 로고
    • Global ischemia induces biphasic response of the mitochondrial respiratory chain
    • Veitch K., Hombroeck A., Caucheteux D., Pouleur H., Hue L. Global ischemia induces biphasic response of the mitochondrial respiratory chain. Biochem. J. 281:1992;709-715.
    • (1992) Biochem. J. , vol.281 , pp. 709-715
    • Veitch, K.1    Hombroeck, A.2    Caucheteux, D.3    Pouleur, H.4    Hue, L.5
  • 176
  • 178
    • 0032031586 scopus 로고    scopus 로고
    • Intrastriatal mesencephalic grafts affect neuronal activity in basal ganglia nuclei and their target structures in a rat model of Parkinson's disease
    • Nakao N., Ogura M., Nakai K., Itakura T. Intrastriatal mesencephalic grafts affect neuronal activity in basal ganglia nuclei and their target structures in a rat model of Parkinson's disease. J. Neurosci. 18:1998;1806-1817.
    • (1998) J. Neurosci. , vol.18 , pp. 1806-1817
    • Nakao, N.1    Ogura, M.2    Nakai, K.3    Itakura, T.4
  • 180
    • 0027359334 scopus 로고
    • Superoxide dismutase activity, oxidative damage, and mtochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis
    • Bowling A.A., Schulz J.B., Brown R.H., Beal M.F. Superoxide dismutase activity, oxidative damage, and mtochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J. Neurochem. 61:1993;2322-2325.
    • (1993) J. Neurochem. , vol.61 , pp. 2322-2325
    • Bowling, A.A.1    Schulz, J.B.2    Brown, R.H.3    Beal, M.F.4
  • 182
  • 183
    • 0035155763 scopus 로고    scopus 로고
    • Peroxynitrite plays a role in methamphetamine-induced dopaminergic neurotoxicity: Evidence from mice lacking neuronal nitric oxide synthase gene or overexpressing copper-zinc superoxide dismutase
    • Imam S.Z., Newport G.D., Itzhak Y., Cadet J.L., Islam F., Slikker W. Jr, Ali S.F. Peroxynitrite plays a role in methamphetamine-induced dopaminergic neurotoxicity evidence from mice lacking neuronal nitric oxide synthase gene or overexpressing copper-zinc superoxide dismutase . J. Neurochem. 76:2001;745-749.
    • (2001) J. Neurochem. , vol.76 , pp. 745-749
    • Imam, S.Z.1    Newport, G.D.2    Itzhak, Y.3    Cadet, J.L.4    Islam, F.5    Slikker W., Jr.6    Ali, S.F.7
  • 185
    • 0028936221 scopus 로고
    • The interferons: Biological effects, mechanisms of action, and use in multiple sclerosis
    • Weinstock-Guttman B., Ransohoff R.M., Kinkel R.P., Rudick R.A. The interferons biological effects, mechanisms of action, and use in multiple sclerosis . Ann. Neurol. 36:1995;7-15.
    • (1995) Ann. Neurol. , vol.36 , pp. 7-15
    • Weinstock-Guttman, B.1    Ransohoff, R.M.2    Kinkel, R.P.3    Rudick, R.A.4
  • 186
    • 0031952988 scopus 로고    scopus 로고
    • Selective inhibition of human glial inducible nitric oxide synthase by interferon-β: Implications for multiple sclerosis
    • Hua L.L., Liu S.J.H., Brosnan C.F., Lee S.C. Selective inhibition of human glial inducible nitric oxide synthase by interferon-β implications for multiple sclerosis . Ann. Neurol. 43:1998;384-387.
    • (1998) Ann. Neurol. , vol.43 , pp. 384-387
    • Hua, L.L.1    Liu, S.J.H.2    Brosnan, C.F.3    Lee, S.C.4
  • 188
    • 0028937241 scopus 로고
    • N-acetylcysteine protects against age-related decline of oxidative phosphorylation in liver mitochondria
    • Miquel J., Ferrandiz M.L., De Juan E., Sevila I., Martinez M. N-acetylcysteine protects against age-related decline of oxidative phosphorylation in liver mitochondria. Eur. J. Pharmacol. 292:1995;333-335.
    • (1995) Eur. J. Pharmacol. , vol.292 , pp. 333-335
    • Miquel, J.1    Ferrandiz, M.L.2    De Juan, E.3    Sevila, I.4    Martinez, M.5
  • 189
    • 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
  • 192
    • 0034930671 scopus 로고    scopus 로고
    • Free radical-mediated molecular damage. Mechanisms for the protective actions of melatonin in the central nervous system
    • Reiter R.J., Acuna-Castroviejo D., Tan D.X., Burkhardt S. Free radical-mediated molecular damage. Mechanisms for the protective actions of melatonin in the central nervous system. Ann. NY Acad. Sci. 939:2001;200-215.
    • (2001) Ann. NY Acad. Sci. , vol.939 , pp. 200-215
    • Reiter, R.J.1    Acuna-Castroviejo, D.2    Tan, D.X.3    Burkhardt, S.4
  • 193
    • 0035170284 scopus 로고    scopus 로고
    • Melatonin protects against 6-OHDA-induced neurotoxicity in rats: A role for mitochondrial complex I activity
    • Dabbeni-Sala F., Di Santo S., Franceschini D., Skaper S.D., Giusti P. Melatonin protects against 6-OHDA-induced neurotoxicity in rats a role for mitochondrial complex I activity . FASEB J. 15:2001;164-170.
    • (2001) FASEB J , vol.15 , pp. 164-170
    • Dabbeni-Sala, F.1    Di Santo, S.2    Franceschini, D.3    Skaper, S.D.4    Giusti, P.5
  • 194
    • 0030795910 scopus 로고    scopus 로고
    • Anandamide suppresses nitric oxide and TNF-α responses to Theiler's virus or endotoxin in astrocytes
    • Molina-Holgado F., Lledo A., Guaza C. Anandamide suppresses nitric oxide and TNF-α responses to Theiler's virus or endotoxin in astrocytes. Neuroreport. 8:1997;1929-1933.
    • (1997) Neuroreport , vol.8 , pp. 1929-1933
    • Molina-Holgado, F.1    Lledo, A.2    Guaza, C.3
  • 195
    • 0032982520 scopus 로고    scopus 로고
    • The central cannabinoid receptor (CB1) mediates inhibition of nitric oxide production by rat microglial cells
    • Waksman Y., Olson J., Carlisle S.J., Cabral G.A. The central cannabinoid receptor (CB1) mediates inhibition of nitric oxide production by rat microglial cells. J. Pharmacol. Exp. Ther. 288:1999;1357-1366.
    • (1999) J. Pharmacol. Exp. Ther. , vol.288 , pp. 1357-1366
    • Waksman, Y.1    Olson, J.2    Carlisle, S.J.3    Cabral, G.A.4
  • 196
    • 0034888225 scopus 로고    scopus 로고
    • Selective cannabinoid CB1 receptor-mediated inhibition of inducible nitric oxide synthase protein expression in C6 rat glioma cells
    • Esposito G., Izzo A.A., DiRosa M., Iuvone T. Selective cannabinoid CB1 receptor-mediated inhibition of inducible nitric oxide synthase protein expression in C6 rat glioma cells. J. Neurochem. 78:2001;835-841.
    • (2001) J. Neurochem. , vol.78 , pp. 835-841
    • Esposito, G.1    Izzo, A.A.2    DiRosa, M.3    Iuvone, T.4
  • 197
    • 0036488182 scopus 로고    scopus 로고
    • Neuroprotective properties of cannabinoids against oxidative stress: Role of the cannabinoid receptor CB1
    • Marsicano G., Moosmann B., Hermann H., Lutz B., Behl C. Neuroprotective properties of cannabinoids against oxidative stress role of the cannabinoid receptor CB1 . J. Neurochem. 80:2002;448-456.
    • (2002) J. Neurochem. , vol.80 , pp. 448-456
    • Marsicano, G.1    Moosmann, B.2    Hermann, H.3    Lutz, B.4    Behl, C.5


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