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Volumn 33, Issue 11, 2002, Pages 1440-1450

Nitric oxide inhibition of mitochondrial respiration and its role in cell death

Author keywords

Apoptosis; Cell death; Free radicals; Mitochondria; Necrosis; Nitric oxide; Permeability transition; Respiration

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYTOCHROME C OXIDASE; FREE RADICAL; GLUTAMATE RECEPTOR; GLUTAMIC ACID; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NITRIC OXIDE; OXYGEN; REACTIVE NITROGEN SPECIES;

EID: 0036889794     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(02)01112-7     Document Type: Article
Times cited : (338)

References (125)
  • 1
    • 0032947296 scopus 로고    scopus 로고
    • Nitric oxide and mitochondrial respiration
    • Brown G.C. Nitric oxide and mitochondrial respiration. Biochim. Biophys. Acta. 1411:1999;351-369.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 351-369
    • Brown, G.C.1
  • 2
    • 0035282782 scopus 로고    scopus 로고
    • Regulation of mitochondrial respiration by nitric oxide inhibition of cytochrome c oxidase
    • Brown G.C. Regulation of mitochondrial respiration by nitric oxide inhibition of cytochrome c oxidase. Biochim. Biophys. Acta. 1504:2001;46-57.
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 46-57
    • Brown, G.C.1
  • 3
    • 0036162636 scopus 로고    scopus 로고
    • Nitric oxide and cytochrome oxidase: Substrate, inhibitor, or effector?
    • Cooper C.E. Nitric oxide and cytochrome oxidase substrate, inhibitor, or effector? Trends Biochem. Sci. 27:2002;33-39.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 33-39
    • Cooper, C.E.1
  • 5
  • 7
    • 0033004242 scopus 로고    scopus 로고
    • Mechanisms of nitric oxide-dependent apoptosis: Involvement of mitochondrial mediators
    • Bosca L., Hortelano S. Mechanisms of nitric oxide-dependent apoptosis involvement of mitochondrial mediators . Cell. Signal. 11:1999;239-244.
    • (1999) Cell. Signal. , vol.11 , pp. 239-244
    • Bosca, L.1    Hortelano, S.2
  • 10
    • 0032898838 scopus 로고    scopus 로고
    • Nitric oxide and cell death
    • Murphy M.P. Nitric oxide and cell death. Biochim. Biophys. Acta. 1411:1999;401-414.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 401-414
    • Murphy, M.P.1
  • 11
    • 0036137771 scopus 로고    scopus 로고
    • Nitric oxide, mitochondria, and cell death
    • Brown G.C., Borutaite V. Nitric oxide, mitochondria, and cell death. IUBMB Life. 52:2001;189-195.
    • (2001) IUBMB Life , vol.52 , pp. 189-195
    • Brown, G.C.1    Borutaite, V.2
  • 13
    • 0033615544 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide synthase stimulation causes cytochrome c release from isolated mitochondria. Evidence for intramitochondrial peroxynitrite formation
    • Ghafourifar P., Schenk U., Klein S.D., Richter C. Mitochondrial nitric oxide synthase stimulation causes cytochrome c release from isolated mitochondria. Evidence for intramitochondrial peroxynitrite formation. J. Biol. Chem. 274:1999;31185-31188.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31185-31188
    • Ghafourifar, P.1    Schenk, U.2    Klein, S.D.3    Richter, C.4
  • 14
    • 0032923492 scopus 로고    scopus 로고
    • Nonenzymatic nitric oxide synthesis in biological systems
    • Zweier J.L., Samouilov A., Kuppusamy P. Nonenzymatic nitric oxide synthesis in biological systems. Biochim. Biophys. Acta. 1411:1999;250-262.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 250-262
    • Zweier, J.L.1    Samouilov, A.2    Kuppusamy, P.3
  • 15
    • 0029998238 scopus 로고    scopus 로고
    • Different inhibitory actions of NO and peroxynitrite on mitochondrial electron transport
    • Cassina A., Radi R. Different inhibitory actions of NO and peroxynitrite on mitochondrial electron transport. Arch. Biophys. Biochem. 328:1996;309-316.
    • (1996) Arch. Biophys. Biochem. , vol.328 , pp. 309-316
    • Cassina, A.1    Radi, R.2
  • 16
    • 28044464985 scopus 로고
    • Reversible inhibition of cytochrome oxidase, the terminal enzyme of the mitochondrial respiratory chain by NO
    • Cleeter M.W.J., Cooper J.M., Darley-Usmar V.M., Moncada S., Schapira A.H.V. Reversible inhibition of cytochrome oxidase, the terminal enzyme of the mitochondrial respiratory chain by NO. FEBS Lett. 345:1994;50-54.
    • (1994) FEBS Lett , vol.345 , pp. 50-54
    • Cleeter, M.W.J.1    Cooper, J.M.2    Darley-Usmar, V.M.3    Moncada, S.4    Schapira, A.H.V.5
  • 17
    • 0027945838 scopus 로고
    • NO potently and reversibly deenergizes mitochondria at low oxygen tension
    • Schweizer M., Richter C. NO potently and reversibly deenergizes mitochondria at low oxygen tension. Biochem. Biophys. Res. Commun. 204:1994;169-175.
    • (1994) Biochem. Biophys. Res. Commun , vol.204 , pp. 169-175
    • Schweizer, M.1    Richter, C.2
  • 18
    • 0028134892 scopus 로고
    • Nanomolar concentrations of NO reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown G.C., Cooper C.E. Nanomolar concentrations of NO 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
  • 19
    • 0029161636 scopus 로고
    • NO regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase
    • Brown G.C. NO regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase. FEBS Lett. 368:1995;136-139.
    • (1995) FEBS Lett , vol.368 , pp. 136-139
    • Brown, G.C.1
  • 20
    • 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
  • 22
    • 0028865420 scopus 로고
    • NO: An important signalling mechanism between vascular endothelium and parenchymal cells in the regulation of oxygen consumption
    • Shen W., Hintze T.H., Wolin M.S. NO an important signalling mechanism between vascular endothelium and parenchymal cells in the regulation of oxygen consumption . Circulation. 92:1995;3505-3512.
    • (1995) Circulation , vol.92 , pp. 3505-3512
    • Shen, W.1    Hintze, T.H.2    Wolin, M.S.3
  • 23
    • 0028885796 scopus 로고
    • Inhibition of cytochrome c oxidase in turnover by NO: Mechanisms and implications for control of respiration
    • Torres J., Darley-Usmar V., Wilson M.T. Inhibition of cytochrome c oxidase in turnover by NO mechanisms and implications for control of respiration . Biochem. J. 312:1995;169-173.
    • (1995) Biochem. J. , vol.312 , pp. 169-173
    • Torres, J.1    Darley-Usmar, V.2    Wilson, M.T.3
  • 25
    • 0032951871 scopus 로고    scopus 로고
    • Modulation of mitochondrial respiration by NO: Investigation by single cell fluorescence microscopy
    • Sarti P., Lendaro E., Ippoliti R., Bellelli A., Benedetti P.A., Brunori M. Modulation of mitochondrial respiration by NO investigation by single cell fluorescence microscopy . FASEB J. 13:1999;191-197.
    • (1999) FASEB J , vol.13 , pp. 191-197
    • Sarti, P.1    Lendaro, E.2    Ippoliti, R.3    Bellelli, A.4    Benedetti, P.A.5    Brunori, M.6
  • 26
    • 0033573981 scopus 로고    scopus 로고
    • On the mechanism by which vascular endothelial cells regulate their oxygen consumption
    • Clementi E., Brown G.C., Foxwell N., Moncada S. On the mechanism by which vascular endothelial cells regulate their oxygen consumption. Proc. Natl. Acad. Sci. USA. 96:1999;1559-1562.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1559-1562
    • Clementi, E.1    Brown, G.C.2    Foxwell, N.3    Moncada, S.4
  • 28
    • 0032502730 scopus 로고    scopus 로고
    • A common mechanism for the interaction of nitric oxide with the oxidized binuclear center and oxygen intermediates of cytochrome c oxidase
    • Torres J., Cooper C.E., Wilson M.T. A common mechanism for the interaction of nitric oxide with the oxidized binuclear center and oxygen intermediates of cytochrome c oxidase. J. Biol. Chem. 273:1998;8756-8766.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8756-8766
    • Torres, J.1    Cooper, C.E.2    Wilson, M.T.3
  • 29
  • 30
    • 0031730661 scopus 로고    scopus 로고
    • Transcellular regulation of cell respiration by NO generated by activated macrophages
    • Brown G.C., Foxwell N., Moncada S. Transcellular regulation of cell respiration by NO generated by activated macrophages. FEBS Lett. 439:1998;321-324.
    • (1998) FEBS Lett , vol.439 , pp. 321-324
    • Brown, G.C.1    Foxwell, N.2    Moncada, S.3
  • 31
    • 0035665482 scopus 로고    scopus 로고
    • Reversible inhibition of cellular respiration by nitric oxide in vascular inflammation
    • Borutaite V., Matthias A., Harris H., Moncada S., Brown G.C. Reversible inhibition of cellular respiration by nitric oxide in vascular inflammation. Am. J. Physiol. 281:2001;H2256-H2260.
    • (2001) Am. J. Physiol. , vol.281
    • Borutaite, V.1    Matthias, A.2    Harris, H.3    Moncada, S.4    Brown, G.C.5
  • 32
    • 0034663637 scopus 로고    scopus 로고
    • Reversal of nitric oxide-, peroxynitrite-, and S-nitrosothiol-induced inhibition of mitochondrial respiration or complex I activity by light and thiols
    • Borutaite V., Budriunaite A., Brown G.C. Reversal of nitric oxide-, peroxynitrite-, and S-nitrosothiol-induced inhibition of mitochondrial respiration or complex I activity by light and thiols. Biochim. Biophys. Acta. 1459:2000;405-412.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 405-412
    • Borutaite, V.1    Budriunaite, A.2    Brown, G.C.3
  • 34
    • 0035449358 scopus 로고    scopus 로고
    • Inflammatory neurodegeneration mediated by nitric oxide from activated glia-inhibiting neuronal respiration, causing glutamate release and excitotoxicity
    • Bal-Price A., Brown G.C. Inflammatory neurodegeneration mediated by nitric oxide from activated glia-inhibiting neuronal respiration, causing glutamate release and excitotoxicity. J. Neurosci. 21:2001;6480-6491.
    • (2001) J. Neurosci. , vol.21 , pp. 6480-6491
    • Bal-Price, A.1    Brown, G.C.2
  • 37
    • 0035312317 scopus 로고    scopus 로고
    • Nitric oxide moves myoglobin center stage
    • Brunori M. Nitric oxide moves myoglobin center stage. Trends Biochem. Sci. 26:2001;209-210.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 209-210
    • Brunori, M.1
  • 38
    • 0037200070 scopus 로고    scopus 로고
    • Differential sensitivity of guanylyl cyclase and mitochondrial respiration to nitric oxide measured using clamped concentrations
    • Bellamy T.C., Griffiths C., Garthwaite J. Differential sensitivity of guanylyl cyclase and mitochondrial respiration to nitric oxide measured using clamped concentrations. J. Biol. Chem. 277:2002;31801-31807.
    • (2002) J. Biol. Chem , vol.277 , pp. 31801-31807
    • Bellamy, T.C.1    Griffiths, C.2    Garthwaite, J.3
  • 39
    • 0028061310 scopus 로고
    • Role of NO in the regulation of oxygen consumption in conscious dogs
    • Shen W., Xu X., Ochoa M., Zhao G., Wolin M.S., Hintze T.H. Role of NO in the regulation of oxygen consumption in conscious dogs. Circ. Res. 75:1994;1086-1095.
    • (1994) Circ. Res , vol.75 , pp. 1086-1095
    • Shen, W.1    Xu, X.2    Ochoa, M.3    Zhao, G.4    Wolin, M.S.5    Hintze, T.H.6
  • 40
    • 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. 359:2001;139-145.
    • (2001) 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
  • 41
    • 0020460870 scopus 로고
    • Sites of inhibition of mitochondrial electron transport in macrophage-injured neoplastic cells
    • Granger D.L., Lehninger A.L. Sites of inhibition of mitochondrial electron transport in macrophage-injured neoplastic cells. J. Cell Biol. 95:1982;527-535.
    • (1982) J. Cell Biol. , vol.95 , pp. 527-535
    • Granger, D.L.1    Lehninger, A.L.2
  • 42
    • 0023940538 scopus 로고
    • Differentiation of murine macrophages to express nonspecific cytotoxicity for tumor cells results in L-arginine-dependent inhibition of mitochondrial iron-sulphur in the macrophage effector cells
    • Drapier J.C., Hibbs J.B. Jr. Differentiation of murine macrophages to express nonspecific cytotoxicity for tumor cells results in L-arginine-dependent inhibition of mitochondrial iron-sulphur in the macrophage effector cells. J. Immunol. 140:1988;2829-2838.
    • (1988) J. Immunol. , vol.140 , pp. 2829-2838
    • Drapier, J.C.1    Hibbs J.B., Jr.2
  • 43
    • 0024584020 scopus 로고
    • NO: A macrophage product responsible for cytostasis and respiratory inhibition in tumor target cells
    • Stuehr D.J., Nathan C.F. NO a macrophage product responsible for cytostasis and respiratory inhibition in tumor target cells . J. Exp. Med. 169:1989;1543-1555.
    • (1989) J. Exp. Med. , vol.169 , pp. 1543-1555
    • Stuehr, D.J.1    Nathan, C.F.2
  • 44
    • 0032533622 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite-dependent aconitase inactivation and iron-regulatory protein-1 activation in mammalian fibroblasts
    • Castro L.A., Robalinho R.L., Cayota A., Meneghini R., Radi R. Nitric oxide and peroxynitrite-dependent aconitase inactivation and iron-regulatory protein-1 activation in mammalian fibroblasts. Arch. Biochem. Biophys. 359:1998;215-224.
    • (1998) Arch. Biochem. Biophys. , vol.359 , pp. 215-224
    • Castro, L.A.1    Robalinho, R.L.2    Cayota, A.3    Meneghini, R.4    Radi, R.5
  • 45
    • 0028952832 scopus 로고
    • Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary culture
    • Bolanos 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 culture . J. Neurochem. 64:1995;1965-1972.
    • (1995) J. Neurochem. , vol.64 , pp. 1965-1972
    • Bolanos, J.P.1    Heales, S.J.R.2    Land, J.M.3    Clark, J.B.4
  • 46
    • 0031571757 scopus 로고    scopus 로고
    • Calcium-independent permeabilization of the inner mitochondrial membrane by peroxynitrite is mediated by membrane protein thiol cross-linking and lipid peroxidation
    • Gadelha F.R., Thomson L., Fagian M.M., Costa A.D.T., Radi R., Vercesi A.E. Calcium-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
  • 47
    • 0036169830 scopus 로고    scopus 로고
    • Selective nitration of mitochondrial complex I by peroxynitrite: Involvement in mitochondria dysfunction and cell death of dopaminergic SH-SY5Y cells
    • Yamamoto T., Maruyama W., Kato Y., Yi H., Shamoto-Nagai M., Tanaka M., Sato Y., Naoi M. Selective nitration of mitochondrial complex I by peroxynitrite involvement in mitochondria dysfunction and cell death of dopaminergic SH-SY5Y cells . J. Neural Transm. 109:2002;1-13.
    • (2002) J. Neural Transm. , vol.109 , pp. 1-13
    • Yamamoto, T.1    Maruyama, W.2    Kato, Y.3    Yi, H.4    Shamoto-Nagai, M.5    Tanaka, M.6    Sato, Y.7    Naoi, M.8
  • 48
    • 0027282347 scopus 로고
    • EPR characterization of molecular targets for NO in mammalian cells and organelles
    • Henry Y., Lepoivre M., Drapier J.C., Ducrocq C., Boucher J.L., Guissani A. EPR characterization of molecular targets for NO in mammalian cells and organelles. FASEB J. 7:1993;1124-1134.
    • (1993) FASEB J , vol.7 , pp. 1124-1134
    • Henry, Y.1    Lepoivre, M.2    Drapier, J.C.3    Ducrocq, C.4    Boucher, J.L.5    Guissani, A.6
  • 49
    • 0030200037 scopus 로고    scopus 로고
    • The effects of NO on electron transport complexes
    • Welter R., Yu L., Yu C.A. The effects of NO on electron transport complexes. Arch. Biophys. Biochem. 331:1996;9-14.
    • (1996) Arch. Biophys. Biochem. , vol.331 , pp. 9-14
    • Welter, R.1    Yu, L.2    Yu, C.A.3
  • 50
    • 0035708661 scopus 로고    scopus 로고
    • Identification of respiratory complexes I and II as mitochondrial sites of damage following exposure to ionizing radiation and nitric oxide
    • Pearce L.L., Epperly M.W., Greenberger J.S., Pitt B.R., Peterson J. Identification of respiratory complexes I and II as mitochondrial sites of damage following exposure to ionizing radiation and nitric oxide. Nitric Oxide. 5:2001;128-136.
    • (2001) Nitric Oxide , vol.5 , pp. 128-136
    • Pearce, L.L.1    Epperly, M.W.2    Greenberger, J.S.3    Pitt, B.R.4    Peterson, J.5
  • 51
    • 0032553302 scopus 로고    scopus 로고
    • Interaction of peroxynitrite with mitochondrial cytochrome oxidase: Catalytic production of nitric oxide and irreversible inhibition of enzyme activity
    • Sharpe M.A., Cooper C.E. Interaction of peroxynitrite with mitochondrial cytochrome oxidase catalytic production of nitric oxide and irreversible inhibition of enzyme activity . J. Biol. Chem. 273:1998;30961-30972.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30961-30972
    • Sharpe, M.A.1    Cooper, C.E.2
  • 52
    • 0034663539 scopus 로고    scopus 로고
    • Effects of nitric oxide on the cytochrome oxidase Km for oxygen: Implications for mitochondrial pathology
    • Cooper C.E., Davies N.A. Effects of nitric oxide on the cytochrome oxidase Km for oxygen implications for mitochondrial pathology . Biochim. Biophys. Acta. 1459:2000;390-396.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 390-396
    • Cooper, C.E.1    Davies, N.A.2
  • 55
    • 0032479147 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase is a prime target of peroxynitrite-induced modification and inactivation
    • Stachowiak O., Dolder M., Wallimann T., Richter C. Mitochondrial creatine kinase is a prime target of peroxynitrite-induced modification and inactivation. J. Biol. Chem. 273:1998;16694-16699.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16694-16699
    • Stachowiak, O.1    Dolder, M.2    Wallimann, T.3    Richter, C.4
  • 56
    • 0032966627 scopus 로고    scopus 로고
    • Nitric oxide inhibits cardiac energy production via inhibition of mitochondrial creatine kinase
    • Kaasik A., Minajeva A., De Sousa E., Ventura-Clapier R., Veksler V. Nitric oxide inhibits cardiac energy production via inhibition of mitochondrial creatine kinase. FEBS Lett. 444:1999;75-77.
    • (1999) FEBS Lett , vol.444 , pp. 75-77
    • Kaasik, A.1    Minajeva, A.2    De Sousa, E.3    Ventura-Clapier, R.4    Veksler, V.5
  • 57
    • 0029986691 scopus 로고    scopus 로고
    • NO inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles
    • Poderoso J.J., Carreras M.C., Lisdero C., Riobo N., Schopfer F., Boveris A. NO inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles. Arch. Biophys. Biochem. 328:1996;85-92.
    • (1996) Arch. Biophys. Biochem. , vol.328 , pp. 85-92
    • Poderoso, J.J.1    Carreras, M.C.2    Lisdero, C.3    Riobo, N.4    Schopfer, F.5    Boveris, A.6
  • 59
    • 0035912784 scopus 로고    scopus 로고
    • Nitric oxide partitioning into mitochondrial membranes and the control of respiration at cytochrome c oxidase
    • Shiva S., Brookes P.S., Patel R.P., Anderson P.G., Darley-Usmar V.M. Nitric oxide partitioning into mitochondrial membranes and the control of respiration at cytochrome c oxidase. Proc. Natl. Acad. Sci. USA. 98:2001;7212-7217.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7212-7217
    • Shiva, S.1    Brookes, P.S.2    Patel, R.P.3    Anderson, P.G.4    Darley-Usmar, V.M.5
  • 60
    • 0029963244 scopus 로고    scopus 로고
    • Mitochondria rapidly reduce nitric oxide, and nitric oxide reversibly inhibits mitochondrial respiration
    • Borutaite V., Brown G.C. Mitochondria rapidly reduce nitric oxide, and nitric oxide reversibly inhibits mitochondrial respiration. Biochem. J. 315:1996;295-299.
    • (1996) Biochem. J. , vol.315 , pp. 295-299
    • Borutaite, V.1    Brown, G.C.2
  • 61
    • 0029132167 scopus 로고
    • Reversible binding and inhibition of catalase by nitric oxide
    • Brown G.C. Reversible binding and inhibition of catalase by nitric oxide. Eur. J. Biochem. 232:1995;188-191.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 188-191
    • Brown, G.C.1
  • 62
    • 0032803509 scopus 로고    scopus 로고
    • Superoxide dismutase and hydrogen peroxide cause rapid nitric oxide breakdown, peroxynitrite production, and subsequent cell death
    • McBride A.G., Borutaite V., Brown G.C. Superoxide dismutase and hydrogen peroxide cause rapid nitric oxide breakdown, peroxynitrite production, and subsequent cell death. Biochim. Biophys. Acta. 1454:1999;275-288.
    • (1999) Biochim. Biophys. Acta , vol.1454 , pp. 275-288
    • McBride, A.G.1    Borutaite, V.2    Brown, G.C.3
  • 63
    • 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
  • 64
    • 0032929052 scopus 로고    scopus 로고
    • Release of cytochrome c from heart mitochondria is induced by high calcium and peroxynitrite and is responsible for calcium-induced inhibition of substrate oxidation
    • Borutaite V., Morkuniene R., Brown G.C. Release of cytochrome c from heart mitochondria is induced by high calcium and peroxynitrite and is responsible for calcium-induced inhibition of substrate oxidation. Biochim. Biophys. Acta. 1453:1999;41-48.
    • (1999) Biochim. Biophys. Acta , vol.1453 , pp. 41-48
    • Borutaite, V.1    Morkuniene, R.2    Brown, G.C.3
  • 65
    • 0033980876 scopus 로고    scopus 로고
    • Nitric oxide donors, nitrosothiols, and mitochondrial respiration inhibitors induce caspase activation by different mechanisms
    • Borutaite V., Morkuniene R., Brown G.C. Nitric oxide donors, nitrosothiols, and mitochondrial respiration inhibitors induce caspase activation by different mechanisms. FEBS Lett. 467:2000;155-159.
    • (2000) FEBS Lett , vol.467 , pp. 155-159
    • Borutaite, V.1    Morkuniene, R.2    Brown, G.C.3
  • 66
    • 84920049699 scopus 로고    scopus 로고
    • The permeability transition pore. Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death
    • Bernardi P. The permeability transition pore. Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death. Biochim. Biophys. Acta. 238:1996;623-630.
    • (1996) Biochim. Biophys. Acta , vol.238 , pp. 623-630
    • Bernardi, P.1
  • 68
    • 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
  • 69
    • 0033290850 scopus 로고    scopus 로고
    • The mitochondrial permeability transition: Its molecular mechanism and role in reperfusion injury
    • Halestrap A.P. The mitochondrial permeability transition its molecular mechanism and role in reperfusion injury . Biochem. Soc. Sym. 66:1999;181-203.
    • (1999) Biochem. Soc. Sym. , vol.66 , pp. 181-203
    • Halestrap, A.P.1
  • 71
    • 0035930505 scopus 로고    scopus 로고
    • Anti-apoptotic effect of cGMP in cultured astrocytes: Inhibition by cGMP-dependent protein kinase of mitochondrial permeable transition pore
    • Takuma K., Phuagphong P., Lee E., Mori K., Baba A., Matsuda T. Anti-apoptotic effect of cGMP in cultured astrocytes inhibition by cGMP-dependent protein kinase of mitochondrial permeable transition pore . J. Biol. Chem. 276:2001;48093-48099.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48093-48099
    • Takuma, K.1    Phuagphong, P.2    Lee, E.3    Mori, K.4    Baba, A.5    Matsuda, T.6
  • 72
    • 0025739622 scopus 로고
    • Phenylarsine oxide induces the cyclosporin A-sensitive membrane permeability transition in rat liver mitochondria
    • Lenartowicz E., Bernardi P., Azzone G.F. Phenylarsine oxide induces the cyclosporin A-sensitive membrane permeability transition in rat liver mitochondria. J. Bioenerg. Biomembr. 4:1991;679-688.
    • (1991) J. Bioenerg. Biomembr. , vol.4 , pp. 679-688
    • Lenartowicz, E.1    Bernardi, P.2    Azzone, G.F.3
  • 73
    • 0031573552 scopus 로고    scopus 로고
    • 2+ acting at the external side of the inner mitochondrial membrane can stimulate mitochondrial permeability transition induced by phenylarsine oxide
    • 2+ acting at the external side of the inner mitochondrial membrane can stimulate mitochondrial permeability transition induced by phenylarsine oxide. Biochim. Biophys. Acta. 1322:1997;221-229.
    • (1997) Biochim. Biophys. Acta , vol.1322 , pp. 221-229
    • Kowaltowski, A.J.1    Castilho, R.F.2
  • 75
    • 0036330255 scopus 로고    scopus 로고
    • Nitric oxide and differential effects of ATP on mitochondrial permeability transition
    • Piantadosi C.A., Tatro C.A., Whorton A.R. Nitric oxide and differential effects of ATP on mitochondrial permeability transition. Nitric Oxide. 6:2002;45-60.
    • (2002) Nitric Oxide , vol.6 , pp. 45-60
    • Piantadosi, C.A.1    Tatro, C.A.2    Whorton, A.R.3
  • 76
    • 0034617449 scopus 로고    scopus 로고
    • Apoptosis-inducing factor (AIF): A ubiquitous mitochondrial oxidoreductase involved in apoptosis
    • Daugas E., Nochy D., Ravagnan L., Loeffler M., Susin S.A., Zamzami N., Kroemer G. Apoptosis-inducing factor (AIF) a ubiquitous mitochondrial oxidoreductase involved in apoptosis . FEBS Lett. 476:2000;118-123.
    • (2000) FEBS Lett , vol.476 , pp. 118-123
    • Daugas, E.1    Nochy, D.2    Ravagnan, L.3    Loeffler, M.4    Susin, S.A.5    Zamzami, N.6    Kroemer, G.7
  • 77
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/Diablo
    • Chai J., Du C., Wu J.W., Kyin S., Wang X., Shi Y. Structural and biochemical basis of apoptotic activation by Smac/Diablo. Nature. 406:2000;855-862.
    • (2000) Nature , vol.406 , pp. 855-862
    • Chai, J.1    Du, C.2    Wu, J.W.3    Kyin, S.4    Wang, X.5    Shi, Y.6
  • 78
    • 0033021780 scopus 로고    scopus 로고
    • Transient and long-lasting openings of the mitochondrial permeability transition pore can be monitored directly in intact cells by changes in mitochondrial calcein fluorescence
    • Petronilli V., Miotto G., Canton M., Brini M., Colonna R., Bernardi P., Di Lisa F. Transient and long-lasting openings of the mitochondrial permeability transition pore can be monitored directly in intact cells by changes in mitochondrial calcein fluorescence. Biophys. J. 76:1999;725-734.
    • (1999) Biophys. J. , vol.76 , pp. 725-734
    • Petronilli, V.1    Miotto, G.2    Canton, M.3    Brini, M.4    Colonna, R.5    Bernardi, P.6    Di Lisa, F.7
  • 79
    • 0035853721 scopus 로고    scopus 로고
    • The mitochondrial permeability transition, release of cytochrome c, and cell death. Correlation with the duration of pore openings in situ
    • Petronilli V., Penzo D., Scorrano L., Bernardi P., Di Lisa F. The mitochondrial permeability transition, release of cytochrome c, and cell death. Correlation with the duration of pore openings in situ. J. Biol. Chem. 276:2001;12030-12034.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12030-12034
    • Petronilli, V.1    Penzo, D.2    Scorrano, L.3    Bernardi, P.4    Di Lisa, F.5
  • 80
    • 0032535514 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase inactivation by peroxynitrite
    • Souza J.M., Radi R. Glyceraldehyde-3-phosphate dehydrogenase inactivation by peroxynitrite. Arch. Biochem. Biophys. 360:1998;187-194.
    • (1998) Arch. Biochem. Biophys. , vol.360 , pp. 187-194
    • Souza, J.M.1    Radi, R.2
  • 81
    • 0028794890 scopus 로고
    • Protein thiol modification and apoptotic cell death as cGMP-independent nitric oxide (NO) signalling pathways
    • Brune B., Mohr S., Messmer U.K. Protein thiol modification and apoptotic cell death as cGMP-independent nitric oxide (NO) signalling pathways. Rev. Physiol. Biochem. Pharmacol. 127:1995;1-30.
    • (1995) Rev. Physiol. Biochem. Pharmacol. , vol.127 , pp. 1-30
    • Brune, B.1    Mohr, S.2    Messmer, U.K.3
  • 82
    • 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
  • 83
    • 0033165935 scopus 로고    scopus 로고
    • Acyl phosphatase activity of NO-inhibited glyceraldehyde-3-phosphate dehydrogenase (GAPDH): A potential mechanism for uncoupling glycolysis from ATP generation in NO-producing cells
    • Albina J.E., Mastrofrancesco B., Reichner J.S. Acyl phosphatase activity of NO-inhibited glyceraldehyde-3-phosphate dehydrogenase (GAPDH) a potential mechanism for uncoupling glycolysis from ATP generation in NO-producing cells . Biochem. J. 341:1999;5-9.
    • (1999) Biochem. J. , vol.341 , pp. 5-9
    • Albina, J.E.1    Mastrofrancesco, B.2    Reichner, J.S.3
  • 84
    • 0029135454 scopus 로고
    • Impact of nitric oxide on macrophage glucose metabolism and glyceraldehyde-3-phosphate dehydrogenase activity
    • Mateo R.B., Reichner J.S., Mastrofrancesco B., Kraft-Stolar D., Albina J.E. Impact of nitric oxide on macrophage glucose metabolism and glyceraldehyde-3-phosphate dehydrogenase activity. Am. J. Physiol. 268:1995;C669-C675.
    • (1995) Am. J. Physiol. , vol.268
    • Mateo, R.B.1    Reichner, J.S.2    Mastrofrancesco, B.3    Kraft-Stolar, D.4    Albina, J.E.5
  • 85
    • 0029980062 scopus 로고    scopus 로고
    • Modification of macrophage glyceraldehyde-3-phosphate dehydrogenase in response to nitric oxide
    • Messmer U.K., Brune B. Modification of macrophage glyceraldehyde-3-phosphate dehydrogenase in response to nitric oxide. Eur. J. Pharmacol. 302:1996;171-182.
    • (1996) Eur. J. Pharmacol. , vol.302 , pp. 171-182
    • Messmer, U.K.1    Brune, B.2
  • 86
    • 0033563776 scopus 로고    scopus 로고
    • Inhibition of mitochondrial ATP generation by nitric oxide switches apoptosis to necrosis
    • Leist M., Single B., Naumann H., Fava E., Simon B., Kuhnle S., Nicotera P. Inhibition of mitochondrial ATP generation by nitric oxide switches apoptosis to necrosis. Exp. Cell Res. 249:1999;396-403.
    • (1999) Exp. Cell Res. , vol.249 , pp. 396-403
    • Leist, M.1    Single, B.2    Naumann, H.3    Fava, E.4    Simon, B.5    Kuhnle, S.6    Nicotera, P.7
  • 87
    • 0033822197 scopus 로고    scopus 로고
    • Nitric oxide induced necrosis and apoptosis in PC12 cells mediated by mitochondria
    • Bal-Price A., Brown G.C. Nitric oxide induced necrosis and apoptosis in PC12 cells mediated by mitochondria. J. Neurochem. 75:2000;1455-1464.
    • (2000) J. Neurochem. , vol.75 , pp. 1455-1464
    • Bal-Price, A.1    Brown, G.C.2
  • 89
    • 0034987439 scopus 로고    scopus 로고
    • Factors directly affecting impulse transmission in inflammatory demyelinating disease: Recent advances in our understanding
    • Smith K.J., Hall S.M. Factors directly affecting impulse transmission in inflammatory demyelinating disease recent advances in our understanding . Curr. Opin. Neurol. 14:2001;289-298.
    • (2001) Curr. Opin. Neurol. , vol.14 , pp. 289-298
    • Smith, K.J.1    Hall, S.M.2
  • 90
    • 0032577469 scopus 로고    scopus 로고
    • Role of poly(ADP ribose) synthetase in inflammation
    • Szabo C. Role of poly(ADP ribose) synthetase in inflammation. Eur. J. Pharmacol. 350:1998;1-19.
    • (1998) Eur. J. Pharmacol. , vol.350 , pp. 1-19
    • Szabo, C.1
  • 91
    • 0028294246 scopus 로고
    • Nitric oxide activation of poly(ADP-ribose) synthetase in neurotoxicity
    • Zhang J., Dawson V., Dawson T., Snyder S. Nitric oxide activation of poly(ADP-ribose) synthetase in neurotoxicity. Science. 263:1994;687-689.
    • (1994) Science , vol.263 , pp. 687-689
    • Zhang, J.1    Dawson, V.2    Dawson, T.3    Snyder, S.4
  • 92
    • 0032403857 scopus 로고    scopus 로고
    • Crucial role of apopain in the peroxynitrite-induced apoptotic DNA fragmentation
    • Virag L., Marmer D.J., Szabo C. Crucial role of apopain in the peroxynitrite-induced apoptotic DNA fragmentation. Free Radic. Biol. Med. 25:1998;1075-1082.
    • (1998) Free Radic. Biol. Med. , vol.25 , pp. 1075-1082
    • Virag, L.1    Marmer, D.J.2    Szabo, C.3
  • 94
    • 0034634441 scopus 로고    scopus 로고
    • Mechanism of nitric oxide-induced apoptosis in human neuroblastoma SH-SY5Y cells
    • Moriya R., Uehara T., Momura Y. Mechanism of nitric oxide-induced apoptosis in human neuroblastoma SH-SY5Y cells. FEBS Lett. 484:2000;253-260.
    • (2000) FEBS Lett , vol.484 , pp. 253-260
    • Moriya, R.1    Uehara, T.2    Momura, Y.3
  • 95
    • 0034012313 scopus 로고    scopus 로고
    • Caspase activation and cytochrome c release during HL-60 cell apoptosis induced by a nitric oxide donor
    • Yabuki M., Tsusui K., Horton A.A., Yoshioka T., Utsumi K. Caspase activation and cytochrome c release during HL-60 cell apoptosis induced by a nitric oxide donor. Free Radic. Res. 32:2000;507-514.
    • (2000) Free Radic. Res , vol.32 , pp. 507-514
    • Yabuki, M.1    Tsusui, K.2    Horton, A.A.3    Yoshioka, T.4    Utsumi, K.5
  • 96
    • 0032955601 scopus 로고    scopus 로고
    • Caspase activation accompanying cytochrome c release from mitochondria is possibly involved in nitric oxide-induced neuronal apoptosis in SH-SY5Y cells
    • Uehara T., Kikuchi Y., Nomura Y. Caspase activation accompanying cytochrome c release from mitochondria is possibly involved in nitric oxide-induced neuronal apoptosis in SH-SY5Y cells. J. Neurochem. 72:1999;196-205.
    • (1999) J. Neurochem. , vol.72 , pp. 196-205
    • Uehara, T.1    Kikuchi, Y.2    Nomura, Y.3
  • 98
    • 0033120803 scopus 로고    scopus 로고
    • Nitric oxide-induced apoptosis in human leukemic lines requires mitochondrial lipid degradation and cytochrome c release
    • Ushmorov A., Ratter F., Lehman V., Droge W., Schirrmacher V., Umansky V. Nitric oxide-induced apoptosis in human leukemic lines requires mitochondrial lipid degradation and cytochrome c release. Blood. 93:1999;2342-2352.
    • (1999) Blood , vol.93 , pp. 2342-2352
    • Ushmorov, A.1    Ratter, F.2    Lehman, V.3    Droge, W.4    Schirrmacher, V.5    Umansky, V.6
  • 99
    • 0033595780 scopus 로고    scopus 로고
    • Loss of molecular interaction between cytochrome c and cardiolipin due to peroxidation
    • Shidoji Y., Hayashi K., Komura S., Ohishi N., Yagi K. Loss of molecular interaction between cytochrome c and cardiolipin due to peroxidation. Biochem. Biophys. Res. Commun. 264:1999;343-347.
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 343-347
    • Shidoji, Y.1    Hayashi, K.2    Komura, S.3    Ohishi, N.4    Yagi, K.5
  • 100
    • 0029812216 scopus 로고    scopus 로고
    • Nitric oxide-induced apoptosis: P53-dependent and p53-independent signalling pathways
    • Messmer U.K., Brune B. Nitric oxide-induced apoptosis p53-dependent and p53-independent signalling pathways . Biochem. J. 319:1996;299-305.
    • (1996) Biochem. J. , vol.319 , pp. 299-305
    • Messmer, U.K.1    Brune, B.2
  • 102
    • 0031666555 scopus 로고    scopus 로고
    • Involvement of Bcl-2 family and caspase-3-like protease in NO-mediated neuronal apoptosis
    • Tamatani M., Ogawa S., Niitsu Y., Tohyama M. Involvement of Bcl-2 family and caspase-3-like protease in NO-mediated neuronal apoptosis. J. Neurochem. 71:1998;1588-1596.
    • (1998) J. Neurochem. , vol.71 , pp. 1588-1596
    • Tamatani, M.1    Ogawa, S.2    Niitsu, Y.3    Tohyama, M.4
  • 104
    • 0035812912 scopus 로고    scopus 로고
    • Induction of CHOP and apoptosis by nitric oxide in p53-deficient microglial cells
    • Kawahara K., Oyadomari S., Gotoh T., Kohsaka S., Nakayama H., Mori M. Induction of CHOP and apoptosis by nitric oxide in p53-deficient microglial cells. FEBS Lett. 506:2001;135-139.
    • (2001) FEBS Lett , vol.506 , pp. 135-139
    • Kawahara, K.1    Oyadomari, S.2    Gotoh, T.3    Kohsaka, S.4    Nakayama, H.5    Mori, M.6
  • 106
    • 0032924755 scopus 로고    scopus 로고
    • Resistance to nitric oxide-mediated apoptosis in HL-60 variant cells is associated with increased activities of Cu,Zn-superoxide dismutase and catalase
    • Yabuli M., Kariya S., Ishisaka R., Yasuda T., Yoshioka T., Horton A.A., Utsumi K. Resistance to nitric oxide-mediated apoptosis in HL-60 variant cells is associated with increased activities of Cu,Zn-superoxide dismutase and catalase. Free Radic. Biol. Med. 26:1999;325-332.
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 325-332
    • Yabuli, M.1    Kariya, S.2    Ishisaka, R.3    Yasuda, T.4    Yoshioka, T.5    Horton, A.A.6    Utsumi, K.7
  • 107
    • 0032855506 scopus 로고    scopus 로고
    • Mitochondrial phospholipid hydroperoxide glutathione peroxidase suppresses apoptosis mediated by a mitochondrial death pathway
    • Nomura K., Imai H., Koumura T., Arai M., Nakagawa Y. Mitochondrial phospholipid hydroperoxide glutathione peroxidase suppresses apoptosis mediated by a mitochondrial death pathway. J. Biol. Chem. 274:1999;29294-29302.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29294-29302
    • Nomura, K.1    Imai, H.2    Koumura, T.3    Arai, M.4    Nakagawa, Y.5
  • 108
    • 0034866507 scopus 로고    scopus 로고
    • Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential
    • Smaili S.S., Hsu Y.T., Sanders K.M., Russell J.T., Youle R.J. Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential. Cell Death Differ. 8:2001;909-920.
    • (2001) Cell Death Differ , vol.8 , pp. 909-920
    • Smaili, S.S.1    Hsu, Y.T.2    Sanders, K.M.3    Russell, J.T.4    Youle, R.J.5
  • 109
    • 0035947596 scopus 로고    scopus 로고
    • Bcl-2 prevents Bax oligomeriztion in the mitochondrial outer membrane
    • Mikhailov V., Mikhailova M., Pulkrabek D.J., Dong Z. Bcl-2 prevents Bax oligomeriztion in the mitochondrial outer membrane. J. Biol. Chem. 276:2001;18361-18374.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18361-18374
    • Mikhailov, V.1    Mikhailova, M.2    Pulkrabek, D.J.3    Dong, Z.4
  • 112
    • 0034687662 scopus 로고    scopus 로고
    • The effect of nitric oxide on cell respiration: A key to understanding its role in cell survival or death
    • Beltran B., Mathur A., Duchen M.R., Erusalimsky J.D., Moncada S. The effect of nitric oxide on cell respiration a key to understanding its role in cell survival or death . Proc. Natl. Acad. Sci. USA. 97:2000;14602-14607.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14602-14607
    • Beltran, B.1    Mathur, A.2    Duchen, M.R.3    Erusalimsky, J.D.4    Moncada, S.5
  • 113
    • 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., Bolanos 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    Bolanos, J.P.3    Moncada, S.4
  • 114
    • 0032808057 scopus 로고    scopus 로고
    • Nitric oxide induces tyrosine nitration and release of cytochrome c preceding an increase of mitochondrial transmembrane potential in macrophages
    • Hortelano S., Alvarez A.M., Bosca L. Nitric oxide induces tyrosine nitration and release of cytochrome c preceding an increase of mitochondrial transmembrane potential in macrophages. FASEB J. 13:1999;2311-2317.
    • (1999) FASEB J , vol.13 , pp. 2311-2317
    • Hortelano, S.1    Alvarez, A.M.2    Bosca, L.3
  • 117
    • 0031882897 scopus 로고    scopus 로고
    • Nitric oxide causes glutamate release from brain synaptosomes following inhibition of mitochondrial function
    • McNaught K.S., Brown G.C. Nitric oxide causes glutamate release from brain synaptosomes following inhibition of mitochondrial function. J. Neurochem. 70:1998;1541-1546.
    • (1998) J. Neurochem. , vol.70 , pp. 1541-1546
    • McNaught, K.S.1    Brown, G.C.2
  • 118
    • 0032421139 scopus 로고    scopus 로고
    • Neuronal excitotoxicity: The role of mitochondria
    • Nicholls D.G., Budd S.L. Neuronal excitotoxicity the role of mitochondria . Biofactors. 8:1998;287-299.
    • (1998) Biofactors , vol.8 , pp. 287-299
    • Nicholls, D.G.1    Budd, S.L.2
  • 119
    • 0033986453 scopus 로고    scopus 로고
    • Production of nitric oxide by glial cells
    • Murphy S. Production of nitric oxide by glial cells. Glia. 29:2000;1-14.
    • (2000) Glia , vol.29 , pp. 1-14
    • Murphy, S.1
  • 120
    • 0029033427 scopus 로고
    • Nitric oxide produced by activated astrocytes rapidly and reversibly inhibits cellular respiration
    • Brown G.C., Bolanos J.P., Heales S.J.R., Clark J.B. Nitric oxide produced by activated astrocytes rapidly and reversibly inhibits cellular respiration. Neurosci. Lett. 193:1995;201-204.
    • (1995) Neurosci. Lett. , vol.193 , pp. 201-204
    • Brown, G.C.1    Bolanos, J.P.2    Heales, S.J.R.3    Clark, J.B.4
  • 121
    • 0036062517 scopus 로고    scopus 로고
    • Different pathways for iNOS-mediated toxicity in vitro dependent on neuronal maturation and NMDA receptor expression
    • Golde S., Chandran S., Brown G.C., Compston A. Different pathways for iNOS-mediated toxicity in vitro dependent on neuronal maturation and NMDA receptor expression. J. Neurochem. 82:2002;269-282.
    • (2002) J. Neurochem. , vol.82 , pp. 269-282
    • Golde, S.1    Chandran, S.2    Brown, G.C.3    Compston, A.4
  • 122
    • 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. (Lond.). 520:1999;797-813.
    • (1999) J. Physiol. (Lond.) , vol.520 , pp. 797-813
    • Keelan, J.1    Vergun, O.2    Duchen, M.R.3
  • 123
    • 0029737355 scopus 로고    scopus 로고
    • + channels, glutamate release, and NMDA receptors mediates delayed neurodegeneration through nitric oxide formation
    • + channels, glutamate release, and NMDA receptors mediates delayed neurodegeneration through nitric oxide formation. J. Neurosci. 16:1996;5004-5013.
    • (1996) J. Neurosci. , vol.16 , pp. 5004-5013
    • Strijbos, P.L.M.1    Leach, M.J.2    Garthwaite, J.3
  • 124
    • 0035048454 scopus 로고    scopus 로고
    • A transient inhibition of mitochondrial ATP synthesis by nitric oxide synthase activation triggered apoptosis in primary cortical neurons
    • Almeida A., Bolanos J.P. A transient inhibition of mitochondrial ATP synthesis by nitric oxide synthase activation triggered apoptosis in primary cortical neurons. J. Neurochem. 77:2001;676-690.
    • (2001) J. Neurochem. , vol.77 , pp. 676-690
    • Almeida, A.1    Bolanos, J.P.2


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