메뉴 건너뛰기




Volumn 273, Issue 3, 2006, Pages 433-450

Calcium, mitochondria and oxidative stress in neuronal pathology: Novel aspects of an enduring theme

Author keywords

Alpha ketoglutarate dehydrogenase; Oxidative stress; Permeability transition pore; Store operated Ca2+ entry; Transient receptor potential; TRPM2; TRPM7

Indexed keywords

CALCIUM; CALCIUM CHANNEL; CALCIUM ION; CATION CHANNEL; CYCLOSPORIN A; CYCLOSPORIN DERIVATIVE; GLUTAMIC ACID; N METHYL VALINE 4 CYCLOSPORIN; OXOGLUTARATE DEHYDROGENASE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 33644953299     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.05103.x     Document Type: Review
Times cited : (208)

References (265)
  • 1
    • 0029064518 scopus 로고
    • Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation
    • Reynolds IJ Hastings TG 1995 Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation J Neurosci 15 3318 3327
    • (1995) J Neurosci , vol.15 , pp. 3318-3327
    • Reynolds, I.J.1    Hastings, T.G.2
  • 5
    • 0031869004 scopus 로고    scopus 로고
    • NMDA-induced superoxide production and neurotoxicity in cultured rat hippocampal neurons: Role of mitochondria
    • Sengpiel B Preis E Krieglstein J Prehn JH 1998 NMDA-induced superoxide production and neurotoxicity in cultured rat hippocampal neurons: role of mitochondria Eur J Neurosci 10 1903 1910
    • (1998) Eur J Neurosci , vol.10 , pp. 1903-1910
    • Sengpiel, B.1    Preis, E.2    Krieglstein, J.3    Prehn, J.H.4
  • 6
    • 0028856368 scopus 로고
    • NMDA receptor activation produces concurrent generation of nitric oxide and reactive oxygen species: Implication for cell death
    • Gunasekar PG Kanthasamy AG Borowitz JL Isom GE 1995 NMDA receptor activation produces concurrent generation of nitric oxide and reactive oxygen species: implication for cell death J Neurochem 65 2016 2021
    • (1995) J Neurochem , vol.65 , pp. 2016-2021
    • Gunasekar, P.G.1    Kanthasamy, A.G.2    Borowitz, J.L.3    Isom, G.E.4
  • 7
    • 0027933701 scopus 로고
    • +: Implications for neurodegeneration
    • +: implications for neurodegeneration J Neurochem 63 584 591
    • (1994) J Neurochem , vol.63 , pp. 584-591
    • Dykens, J.A.1
  • 8
    • 0032557424 scopus 로고    scopus 로고
    • The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Evidence for the participation of reactive oxygen species in this mechanism
    • Kowaltowski AJ Netto LE Vercesi AE 1998 The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Evidence for the participation of reactive oxygen species in this mechanism J Biol Chem 273 12766 12769
    • (1998) J Biol Chem , vol.273 , pp. 12766-12769
    • Kowaltowski, A.J.1    Netto, L.E.2    Vercesi, A.E.3
  • 12
    • 0035667431 scopus 로고    scopus 로고
    • 2+ -induced membrane permeability transition in brain mitochondria
    • 2+ -induced membrane permeability transition in brain mitochondria J Neurochem 79 1237 1245
    • (2001) J Neurochem , vol.79 , pp. 1237-1245
    • MacIel, E.N.1    Vercesi, A.E.2    Castilho, R.F.3
  • 13
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov SS Skulachev VP Starkov AA 1997 High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria FEBS Lett 416 15 18
    • (1997) FEBS Lett , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 14
    • 0036788941 scopus 로고    scopus 로고
    • Regulation of hydrogen peroxide production by brain mitochondria by calcium and Bax
    • Starkov AA Polster BM Fiskum G 2002 Regulation of hydrogen peroxide production by brain mitochondria by calcium and Bax J Neurochem 83 220 228
    • (2002) J Neurochem , vol.83 , pp. 220-228
    • Starkov, A.A.1    Polster, B.M.2    Fiskum, G.3
  • 15
    • 0042433242 scopus 로고    scopus 로고
    • 2 production by membrane potential and NAD(P) H redox state
    • 2 production by membrane potential and NAD(P) H redox state J Neurochem 86 1101 1107
    • (2003) J Neurochem , vol.86 , pp. 1101-1107
    • Starkov, A.A.1    Fiskum, G.2
  • 16
    • 3342910554 scopus 로고    scopus 로고
    • Mitochondrial calcium and oxidative stress as mediators of ischemic brain injury
    • Starkov AA Chinopoulos C Fiskum G 2004 Mitochondrial calcium and oxidative stress as mediators of ischemic brain injury Cell Calcium 36 257 264
    • (2004) Cell Calcium , vol.36 , pp. 257-264
    • Starkov, A.A.1    Chinopoulos, C.2    Fiskum, G.3
  • 18
    • 0034740585 scopus 로고    scopus 로고
    • DeltaPsi (m)-dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • Votyakova TV Reynolds IJ 2001 DeltaPsi (m)-dependent and -independent production of reactive oxygen species by rat brain mitochondria J Neurochem 79 266 277
    • (2001) J Neurochem , vol.79 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 19
    • 0141482026 scopus 로고    scopus 로고
    • The production of reactive oxygen species in intact isolated nerve terminals is independent of the mitochondrial membrane potential
    • Sipos I Tretter L Adam-Vizi V 2003 The production of reactive oxygen species in intact isolated nerve terminals is independent of the mitochondrial membrane potential Neurochem Res 28 1575 1581
    • (2003) Neurochem Res , vol.28 , pp. 1575-1581
    • Sipos, I.1    Tretter, L.2    Adam-Vizi, V.3
  • 20
    • 24144464489 scopus 로고    scopus 로고
    • Production of reactive oxygen species in brain mitochondria: Contribution by electron transport chain and non-electron transport chain sources
    • Adam-Vizi V 2005 Production of reactive oxygen species in brain mitochondria: contribution by electron transport chain and non-electron transport chain sources Antioxid Redox Signal 7 1140 1149
    • (2005) Antioxid Redox Signal , vol.7 , pp. 1140-1149
    • Adam-Vizi, V.1
  • 21
    • 0036313070 scopus 로고    scopus 로고
    • The effects of focal ischemia and reperfusion on the glutathione content of mitochondria from rat brain subregions
    • Anderson MF Sims NR 2002 The effects of focal ischemia and reperfusion on the glutathione content of mitochondria from rat brain subregions J Neurochem 81 541 549
    • (2002) J Neurochem , vol.81 , pp. 541-549
    • Anderson, M.F.1    Sims, N.R.2
  • 22
    • 0032496143 scopus 로고    scopus 로고
    • Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss
    • Cai J Jones DP 1998 Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss J Biol Chem 273 11401 11404
    • (1998) J Biol Chem , vol.273 , pp. 11401-11404
    • Cai, J.1    Jones, D.P.2
  • 23
    • 4544226082 scopus 로고    scopus 로고
    • Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase
    • Tretter L Adam-Vizi V 2004 Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase J Neurosci 24 7771 7778
    • (2004) J Neurosci , vol.24 , pp. 7771-7778
    • Tretter, L.1    Adam-Vizi, V.2
  • 25
    • 0014010888 scopus 로고
    • Antimycin-insensitive oxidation of succinate and reduced nicotinamide-adenine dinucleotide in electron-transport particles. I. pH dependency and hydrogen peroxide formation
    • Jensen PK 1966 Antimycin-insensitive oxidation of succinate and reduced nicotinamide-adenine dinucleotide in electron-transport particles. I. pH dependency and hydrogen peroxide formation Biochim Biophys Acta 122 157 166
    • (1966) Biochim Biophys Acta , vol.122 , pp. 157-166
    • Jensen, P.K.1
  • 27
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • Boveris A Chance B 1973 The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen Biochem J 134 707 716
    • (1973) Biochem J , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 28
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens JF 2003 Mitochondrial formation of reactive oxygen species J Physiol 552 335 344
    • (2003) J Physiol , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 29
    • 0036139856 scopus 로고    scopus 로고
    • The mitochondrial production of reactive oxygen species: Mechanisms and implications in human pathology
    • Lenaz G 2001 The mitochondrial production of reactive oxygen species: mechanisms and implications in human pathology IUBMB Life 52 159 164
    • (2001) IUBMB Life , vol.52 , pp. 159-164
    • Lenaz, G.1
  • 30
    • 0033369476 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical generation and leak: Sites of production in states 4 and 3, organ specificity, and relation to aging and longevity
    • Barja G 1999 Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity, and relation to aging and longevity J Bioenerg Biomembr 31 347 366
    • (1999) J Bioenerg Biomembr , vol.31 , pp. 347-366
    • Barja, G.1
  • 31
    • 0034467677 scopus 로고    scopus 로고
    • Localization of the site of oxygen radical generation inside the Complex I of heart and nonsynaptic brain mammalian mitochondria
    • Herrero A Barja G 2000 Localization of the site of oxygen radical generation inside the Complex I of heart and nonsynaptic brain mammalian mitochondria J Bioenerg Biomembr 32 609 615
    • (2000) J Bioenerg Biomembr , vol.32 , pp. 609-615
    • Herrero, A.1    Barja, G.2
  • 32
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens JF Boveris A 1980 Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria Biochem J 191 421 427
    • (1980) Biochem J , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 33
    • 0016148483 scopus 로고
    • Superoxide radicals as precursors of mitochondrial hydrogen peroxide
    • Loschen G Azzi A Richter C Flohe L 1974 Superoxide radicals as precursors of mitochondrial hydrogen peroxide FEBS Lett 42 68 72
    • (1974) FEBS Lett , vol.42 , pp. 68-72
    • Loschen, G.1    Azzi, A.2    Richter, C.3    Flohe, L.4
  • 34
    • 0016701593 scopus 로고
    • Superoxide radicals and hydrogen peroxide formation in mitochondria from normal and neoplastic tissues
    • Dionisi O Galeotti T Terranova T Azzi A 1975 Superoxide radicals and hydrogen peroxide formation in mitochondria from normal and neoplastic tissues Biochim Biophys Acta 403 292 300
    • (1975) Biochim Biophys Acta , vol.403 , pp. 292-300
    • Dionisi, O.1    Galeotti, T.2    Terranova, T.3    Azzi, A.4
  • 35
    • 0017154414 scopus 로고
    • Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
    • Boveris A Cadenas E Stoppani AO 1976 Role of ubiquinone in the mitochondrial generation of hydrogen peroxide Biochem J 156 435 444
    • (1976) Biochem J , vol.156 , pp. 435-444
    • Boveris, A.1    Cadenas, E.2    Stoppani, A.O.3
  • 36
    • 0030969868 scopus 로고    scopus 로고
    • Superoxide production by the mitochondrial respiratory chain
    • Turrens JF 1997 Superoxide production by the mitochondrial respiratory chain Biosci Report 17 3 8
    • (1997) Biosci Report , vol.17 , pp. 3-8
    • Turrens, J.F.1
  • 37
    • 0033386202 scopus 로고    scopus 로고
    • Mitochondria in neurodegeneration: Bioenergetic function in cell life and death
    • Murphy AN Fiskum G Beal MF 1999 Mitochondria in neurodegeneration: bioenergetic function in cell life and death J Cereb Blood Flow Metab 19 231 245
    • (1999) J Cereb Blood Flow Metab , vol.19 , pp. 231-245
    • Murphy, A.N.1    Fiskum, G.2    Beal, M.F.3
  • 38
    • 0014217470 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome beta region of the respiratory chain of beef heart submitochondrial particles
    • Hinkle PC Butow RA Racker E Chance B 1967 Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome beta region of the respiratory chain of beef heart submitochondrial particles J Biol Chem 242 5169 5173
    • (1967) J Biol Chem , vol.242 , pp. 5169-5173
    • Hinkle, P.C.1    Butow, R.A.2    Racker, E.3    Chance, B.4
  • 39
    • 0037269343 scopus 로고    scopus 로고
    • Quantitative relationship between inhibition of respiratory complexes and formation of reactive oxygen species in isolated nerve terminals
    • Sipos I Tretter L Adam-Vizi V 2003 Quantitative relationship between inhibition of respiratory complexes and formation of reactive oxygen species in isolated nerve terminals J Neurochem 84 112 118
    • (2003) J Neurochem , vol.84 , pp. 112-118
    • Sipos, I.1    Tretter, L.2    Adam-Vizi, V.3
  • 40
    • 0037352050 scopus 로고    scopus 로고
    • 2-Oxo acid dehydrogenase complexes in redox regulation
    • Bunik VI 2003 2-Oxo acid dehydrogenase complexes in redox regulation Eur J Biochem 270 1036 1042
    • (2003) Eur J Biochem , vol.270 , pp. 1036-1042
    • Bunik, V.I.1
  • 41
    • 0025689355 scopus 로고
    • Localization of the alpha-oxoacid dehydrogenase multienzyme complexes within the mitochondrion
    • Maas E Bisswanger H 1990 Localization of the alpha-oxoacid dehydrogenase multienzyme complexes within the mitochondrion FEBS Lett 277 189 190
    • (1990) FEBS Lett , vol.277 , pp. 189-190
    • Maas, E.1    Bisswanger, H.2
  • 42
    • 0021744544 scopus 로고
    • Complex I binds several mitochondrial NAD-coupled dehydrogenases
    • Sumegi B Srere PA 1984 Complex I binds several mitochondrial NAD-coupled dehydrogenases J Biol Chem 259 15040 15045
    • (1984) J Biol Chem , vol.259 , pp. 15040-15045
    • Sumegi, B.1    Srere, P.A.2
  • 43
    • 0024586535 scopus 로고
    • Supramolecular organization of tricarboxylic acid cycle enzymes
    • Lyubarev AE Kurganov BI 1989 Supramolecular organization of tricarboxylic acid cycle enzymes Biosystems 22 91 102
    • (1989) Biosystems , vol.22 , pp. 91-102
    • Lyubarev, A.E.1    Kurganov, B.I.2
  • 44
    • 0016254851 scopus 로고
    • Properties and subunit composition of the pig heart 2-oxoglutarate dehydrogenase
    • Koike K Hamada M Tanaka N Otsuka KI Ogasahara K Koike M 1974 Properties and subunit composition of the pig heart 2-oxoglutarate dehydrogenase J Biol Chem 249 3836 3842
    • (1974) J Biol Chem , vol.249 , pp. 3836-3842
    • Koike, K.1    Hamada, M.2    Tanaka, N.3    Otsuka, K.I.4    Ogasahara, K.5    Koike, M.6
  • 45
    • 0025221771 scopus 로고
    • Molecular biology and biochemistry of pyruvate dehydrogenase complexes
    • Patel MS Roche TE 1990 Molecular biology and biochemistry of pyruvate dehydrogenase complexes FASEB J 4 3224 3233
    • (1990) FASEB J , vol.4 , pp. 3224-3233
    • Patel, M.S.1    Roche, T.E.2
  • 46
    • 0025370816 scopus 로고
    • Structure-function relationships in dihydrolipoamide acyltransferases
    • Reed LJ Hackert ML 1990 Structure-function relationships in dihydrolipoamide acyltransferases J Biol Chem 265 8971 8974
    • (1990) J Biol Chem , vol.265 , pp. 8971-8974
    • Reed, L.J.1    Hackert, M.L.2
  • 47
    • 0022483367 scopus 로고
    • Inhibition of glycine oxidation by pyruvate, alpha-ketoglutarate, and branched-chain alpha-keto acids in rat liver mitochondria: Presence of interaction between the glycine cleavage system and alpha-keto acid dehydrogenase complexes
    • Kochi H Seino H Ono K 1986 Inhibition of glycine oxidation by pyruvate, alpha-ketoglutarate, and branched-chain alpha-keto acids in rat liver mitochondria: presence of interaction between the glycine cleavage system and alpha-keto acid dehydrogenase complexes Arch Biochem Biophys 249 263 272
    • (1986) Arch Biochem Biophys , vol.249 , pp. 263-272
    • Kochi, H.1    Seino, H.2    Ono, K.3
  • 48
    • 2142782325 scopus 로고
    • An oxidase for reduced diphosphopyridine nucleotide
    • Huennekens FM Basford RE Gabrio BW 1955 An oxidase for reduced diphosphopyridine nucleotide J Biol Chem 213 951 967
    • (1955) J Biol Chem , vol.213 , pp. 951-967
    • Huennekens, F.M.1    Basford, R.E.2    Gabrio, B.W.3
  • 49
    • 0037155880 scopus 로고    scopus 로고
    • Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase
    • Gazaryan IG Krasnikov BF Ashby GA Thorneley RN Kristal BS Brown AM 2002 Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase J Biol Chem 277 10064 10072
    • (2002) J Biol Chem , vol.277 , pp. 10064-10072
    • Gazaryan, I.G.1    Krasnikov, B.F.2    Ashby, G.A.3    Thorneley, R.N.4    Kristal, B.S.5    Brown, A.M.6
  • 50
    • 0027267866 scopus 로고
    • Quantification of the content of fluorescent flavoproteins in mitochondria from liver, kidney cortex, skeletal muscle, and brain
    • Kunz WS Gellerich FN 1993 Quantification of the content of fluorescent flavoproteins in mitochondria from liver, kidney cortex, skeletal muscle, and brain Biochem Med Metab Biol 50 103 110
    • (1993) Biochem Med Metab Biol , vol.50 , pp. 103-110
    • Kunz, W.S.1    Gellerich, F.N.2
  • 51
    • 0022412317 scopus 로고
    • Contribution of different enzymes to flavoprotein fluorescence of isolated rat liver mitochondria
    • Kunz WS Kunz W 1985 Contribution of different enzymes to flavoprotein fluorescence of isolated rat liver mitochondria Biochim Biophys Acta 841 237 246
    • (1985) Biochim Biophys Acta , vol.841 , pp. 237-246
    • Kunz, W.S.1    Kunz, W.2
  • 52
    • 0036408866 scopus 로고    scopus 로고
    • Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species
    • Bunik VI Sievers C 2002 Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species Eur J Biochem 269 5004 5015
    • (2002) Eur J Biochem , vol.269 , pp. 5004-5015
    • Bunik, V.I.1    Sievers, C.2
  • 53
    • 0016499611 scopus 로고
    • A kinetic study of the alpha-keto acid dehydrogenase complexes from pig heart mitochondria
    • Hamada M Koike K Nakaula Y Hiraoka T Koike M 1975 A kinetic study of the alpha-keto acid dehydrogenase complexes from pig heart mitochondria J Biochem (Tokyo) 77 1047 1056
    • (1975) J Biochem (Tokyo) , vol.77 , pp. 1047-1056
    • Hamada, M.1    Koike, K.2    Nakaula, Y.3    Hiraoka, T.4    Koike, M.5
  • 54
    • 0017342257 scopus 로고
    • Studies on the mechanism and kinetics of the 2-oxoglutarate dehydrogenase system from pig heart
    • Mcminn CL Ottaway JH 1977 Studies on the mechanism and kinetics of the 2-oxoglutarate dehydrogenase system from pig heart Biochem J 161 569 581
    • (1977) Biochem J , vol.161 , pp. 569-581
    • McMinn, C.L.1    Ottaway, J.H.2
  • 56
    • 0025104580 scopus 로고
    • Kinetic characterization of the pyruvate and oxoglutarate dehydrogenase complexes from human heart
    • Kiselevsky YV Ostrovtsova SA Strumilo SA 1990 Kinetic characterization of the pyruvate and oxoglutarate dehydrogenase complexes from human heart Acta Biochim Pol 37 135 139
    • (1990) Acta Biochim Pol , vol.37 , pp. 135-139
    • Kiselevsky, Y.V.1    Ostrovtsova, S.A.2    Strumilo, S.A.3
  • 57
    • 0034671429 scopus 로고    scopus 로고
    • Inhibition of Krebs cycle enzymes by hydrogen peroxide: A key role of [alpha]-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress
    • Tretter L Adam-Vizi V 2000 Inhibition of Krebs cycle enzymes by hydrogen peroxide: a key role of [alpha]-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress J Neurosci 20 8972 8979
    • (2000) J Neurosci , vol.20 , pp. 8972-8979
    • Tretter, L.1    Adam-Vizi, V.2
  • 58
    • 0344443765 scopus 로고    scopus 로고
    • Oxidative a-ketoglutarate dehydrogenase inhibition via subtle elevations in monoamine oxidase B levels results in loss of spare respiratory capacity: Implications for Parkinson's disease
    • Kumar MJ Nicholls DG Andersen JK 2003 Oxidative a-ketoglutarate dehydrogenase inhibition via subtle elevations in monoamine oxidase B levels results in loss of spare respiratory capacity: Implications for Parkinson's disease J Biol Chem 278 46432 46439
    • (2003) J Biol Chem , vol.278 , pp. 46432-46439
    • Kumar, M.J.1    Nicholls, D.G.2    Andersen, J.K.3
  • 59
    • 0033000269 scopus 로고    scopus 로고
    • Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: Inhibition of alpha-ketoglutarate dehydrogenase
    • Chinopoulos C Tretter L Adam-Vizi V 1999 Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: inhibition of alpha-ketoglutarate dehydrogenase J Neurochem 73 220 228
    • (1999) J Neurochem , vol.73 , pp. 220-228
    • Chinopoulos, C.1    Tretter, L.2    Adam-Vizi, V.3
  • 60
    • 0033975305 scopus 로고    scopus 로고
    • Reversible depolarization of in situ mitochondria by oxidative stress parallels a decrease in NAD(P)H level in nerve terminals
    • Chinopoulos C Tretter L Adam-Vizi V 2000 Reversible depolarization of in situ mitochondria by oxidative stress parallels a decrease in NAD(P)H level in nerve terminals Neurochem Int 36 483 488
    • (2000) Neurochem Int , vol.36 , pp. 483-488
    • Chinopoulos, C.1    Tretter, L.2    Adam-Vizi, V.3
  • 61
    • 0033382252 scopus 로고    scopus 로고
    • Depolarization of in situ mitochondria by hydrogen peroxide in nerve terminals
    • Chinopoulos C Adam-Vizi V 1999 Depolarization of in situ mitochondria by hydrogen peroxide in nerve terminals Ann NY Acad Sci 893 269 272
    • (1999) Ann NY Acad Sci , vol.893 , pp. 269-272
    • Chinopoulos, C.1    Adam-Vizi, V.2
  • 62
    • 0030273295 scopus 로고    scopus 로고
    • Mitochondria, free radicals, and neurodegeneration
    • Beal MF 1996 Mitochondria, free radicals, and neurodegeneration Curr Opin Neurobiol 6 661 666
    • (1996) Curr Opin Neurobiol , vol.6 , pp. 661-666
    • Beal, M.F.1
  • 63
    • 23244435445 scopus 로고    scopus 로고
    • The alpha-ketoglutarate-dehydrogenase complex: A mediator between mitochondria and oxidative stress in neurodegeneration
    • Gibson GE Blass JP Beal MF Bunik V 2005 The alpha-ketoglutarate- dehydrogenase complex: a mediator between mitochondria and oxidative stress in neurodegeneration Mol Neurobiol 31 43 64
    • (2005) Mol Neurobiol , vol.31 , pp. 43-64
    • Gibson, G.E.1    Blass, J.P.2    Beal, M.F.3    Bunik, V.4
  • 64
    • 0023732664 scopus 로고
    • Reduced activities of thiamine-dependent enzymes in the brains and peripheral tissues of patients with Alzheimer's disease
    • Gibson GE Sheu KF Blass JP Baker A Carlson KC Harding B Perrino P 1988 Reduced activities of thiamine-dependent enzymes in the brains and peripheral tissues of patients with Alzheimer's disease Arch Neurol 45 836 840
    • (1988) Arch Neurol , vol.45 , pp. 836-840
    • Gibson, G.E.1    Sheu, K.F.2    Blass, J.P.3    Baker, A.4    Carlson, K.C.5    Harding, B.6    Perrino, P.7
  • 65
    • 0025650037 scopus 로고
    • Thiamine-dependent enzyme changes in temporal cortex of patients with Alzheimer's disease
    • Butterworth RF Besnard AM 1990 Thiamine-dependent enzyme changes in temporal cortex of patients with Alzheimer's disease Metab Brain Dis 5 179 184
    • (1990) Metab Brain Dis , vol.5 , pp. 179-184
    • Butterworth, R.F.1    Besnard, A.M.2
  • 66
    • 0027332651 scopus 로고
    • Brain alpha-ketoglutarate dehydrogenase complex activity in Alzheimer's disease
    • Mastrogiacomo F Bergeron C Kish SJ 1993 Brain alpha-ketoglutarate dehydrogenase complex activity in Alzheimer's disease J Neurochem 61 2007 2014
    • (1993) J Neurochem , vol.61 , pp. 2007-2014
    • Mastrogiacomo, F.1    Bergeron, C.2    Kish, S.J.3
  • 67
    • 0032569826 scopus 로고    scopus 로고
    • Affected enzyme activities in Alzheimer's disease are sensitive to antemortem hypoxia
    • Terwel D Bothmer J Wolf E Meng F Jolles J 1998 Affected enzyme activities in Alzheimer's disease are sensitive to antemortem hypoxia J Neurol Sci 161 47 56
    • (1998) J Neurol Sci , vol.161 , pp. 47-56
    • Terwel, D.1    Bothmer, J.2    Wolf, E.3    Meng, F.4    Jolles, J.5
  • 68
    • 0028176592 scopus 로고
    • An immunohistochemical study on alpha-ketoglutarate dehydrogenase complex in Parkinson's disease
    • Mizuno Y Matuda S Yoshino H Mori H Hattori N Ikebe S 1994 An immunohistochemical study on alpha-ketoglutarate dehydrogenase complex in Parkinson's disease Ann Neurol 35 204 210
    • (1994) Ann Neurol , vol.35 , pp. 204-210
    • Mizuno, Y.1    Matuda, S.2    Yoshino, H.3    Mori, H.4    Hattori, N.5    Ikebe, S.6
  • 73
    • 0035576822 scopus 로고    scopus 로고
    • Mitochondrial impairment in the cerebellum of the patients with progressive supranuclear palsy
    • Park LC Albers DS Xu H Lindsay JG Beal MF Gibson GE 2001 Mitochondrial impairment in the cerebellum of the patients with progressive supranuclear palsy J Neurosci Res 66 1028 1034
    • (2001) J Neurosci Res , vol.66 , pp. 1028-1034
    • Park, L.C.1    Albers, D.S.2    Xu, H.3    Lindsay, J.G.4    Beal, M.F.5    Gibson, G.E.6
  • 74
    • 0027131501 scopus 로고
    • Thiamine-dependent enzyme changes in the brains of alcoholics: Relationship to the Wernicke-Korsakoff syndrome
    • Butterworth RF Kril JJ Harper CG 1993 Thiamine-dependent enzyme changes in the brains of alcoholics: relationship to the Wernicke-Korsakoff syndrome Alcohol Clin Exp Res 17 1084 1088
    • (1993) Alcohol Clin Exp Res , vol.17 , pp. 1084-1088
    • Butterworth, R.F.1    Kril, J.J.2    Harper, C.G.3
  • 78
    • 0031891606 scopus 로고    scopus 로고
    • Immunochemical characterization of the deficiency of the alpha-ketoglutarate dehydrogenase complex in thiamine-deficient rat brain
    • Sheu KF Calingasan NY Lindsay JG Gibson GE 1998 Immunochemical characterization of the deficiency of the alpha-ketoglutarate dehydrogenase complex in thiamine-deficient rat brain J Neurochem 70 1143 1150
    • (1998) J Neurochem , vol.70 , pp. 1143-1150
    • Sheu, K.F.1    Calingasan, N.Y.2    Lindsay, J.G.3    Gibson, G.E.4
  • 79
    • 15744369433 scopus 로고    scopus 로고
    • Reduction in the E2k subunit of the alpha-ketoglutarate dehydrogenase complex has effects independent of complex activity
    • Shi Q Chen HL Xu H Gibson GE 2005 Reduction in the E2k subunit of the alpha-ketoglutarate dehydrogenase complex has effects independent of complex activity J Biol Chem 280 10888 10896
    • (2005) J Biol Chem , vol.280 , pp. 10888-10896
    • Shi, Q.1    Chen, H.L.2    Xu, H.3    Gibson, G.E.4
  • 80
    • 0033545874 scopus 로고    scopus 로고
    • The crystal structure of a multifunctional protein: Phosphoglucose isomerase/autocrine motility factor/neuroleukin
    • Sun YJ Chou CC Chen WS Wu RT Meng M Hsiao CD 1999 The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin Proc Natl Acad Sci USA 96 5412 5417
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5412-5417
    • Sun, Y.J.1    Chou, C.C.2    Chen, W.S.3    Wu, R.T.4    Meng, M.5    Hsiao, C.D.6
  • 81
    • 0027081042 scopus 로고
    • Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein
    • Kennedy MC Mende-Mueller L Blondin GA Beinert H 1992 Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein Proc Natl Acad Sci USA 89 11730 11734
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11730-11734
    • Kennedy, M.C.1    Mende-Mueller, L.2    Blondin, G.A.3    Beinert, H.4
  • 82
    • 0027440290 scopus 로고
    • Yeast mitochondrial NAD(+)-dependent isocitrate dehydrogenase is an RNA-binding protein
    • Elzinga SD van Bednarz ALOK Dekker PJ Grivell LA 1993 Yeast mitochondrial NAD(+)-dependent isocitrate dehydrogenase is an RNA-binding protein Nucl Acids Res 21 5328 5331
    • (1993) Nucl Acids Res , vol.21 , pp. 5328-5331
    • Elzinga, S.D.1    Bednarz Alok, V.2    Dekker, P.J.3    Grivell, L.A.4
  • 85
    • 0028169899 scopus 로고
    • Distribution of the alpha-ketoglutarate dehydrogenase complex in rat brain
    • Calingasan NY Baker H Sheu KF Gibson GE 1994 Distribution of the alpha-ketoglutarate dehydrogenase complex in rat brain J Comp Neurol 346 461 479
    • (1994) J Comp Neurol , vol.346 , pp. 461-479
    • Calingasan, N.Y.1    Baker, H.2    Sheu, K.F.3    Gibson, G.E.4
  • 86
    • 0033989334 scopus 로고    scopus 로고
    • Quantitative alpha-ketoglutarate dehydrogenase activity staining in brain sections and in cultured cells
    • Park LC Calingasan NY Sheu KF Gibson GE 2000 Quantitative alpha-ketoglutarate dehydrogenase activity staining in brain sections and in cultured cells Anal Biochem 277 86 93
    • (2000) Anal Biochem , vol.277 , pp. 86-93
    • Park, L.C.1    Calingasan, N.Y.2    Sheu, K.F.3    Gibson, G.E.4
  • 87
    • 0141481850 scopus 로고    scopus 로고
    • Inhibition of alpha-ketoglutarate dehydrogenase complex promotes cytochrome c release from mitochondria, caspase-3 activation, and necrotic cell death
    • Huang HM Ou HC Xu H Chen HL Fowler C Gibson GE 2003 Inhibition of alpha-ketoglutarate dehydrogenase complex promotes cytochrome c release from mitochondria, caspase-3 activation, and necrotic cell death J Neurosci Res 74 309 317
    • (2003) J Neurosci Res , vol.74 , pp. 309-317
    • Huang, H.M.1    Ou, H.C.2    Xu, H.3    Chen, H.L.4    Fowler, C.5    Gibson, G.E.6
  • 88
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M Szabo I 1995 The mitochondrial permeability transition Biochim Biophys Acta 1241 139 176
    • (1995) Biochim Biophys Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 89
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: Channels, exchangers, and permeability transition
    • Bernardi P 1999 Mitochondrial transport of cations: channels, exchangers, and permeability transition Physiol Rev 79 1127 1155
    • (1999) Physiol Rev , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 90
    • 0034518449 scopus 로고    scopus 로고
    • 2+ in cell physiology and pathophysiology
    • 2+ in cell physiology and pathophysiology Cell Calcium 28 339 348
    • (2000) Cell Calcium , vol.28 , pp. 339-348
    • Duchen, M.R.1
  • 91
    • 0033971898 scopus 로고    scopus 로고
    • Mitochondria and neuronal survival
    • Nicholls DG Budd SL 2000 Mitochondria and neuronal survival Physiol Rev 80 315 360
    • (2000) Physiol Rev , vol.80 , pp. 315-360
    • Nicholls, D.G.1    Budd, S.L.2
  • 92
    • 0033199019 scopus 로고    scopus 로고
    • Glutamate-induced mitochondrial depolarisation and perturbation of calcium homeostasis in cultured rat hippocampal neurones
    • Vergun O Keelan J Khodorov BI Duchen MR 1999 Glutamate-induced mitochondrial depolarisation and perturbation of calcium homeostasis in cultured rat hippocampal neurones J Physiol 519 Part 2 451 466
    • (1999) J Physiol , vol.5192 , pp. 451-466
    • Vergun, O.1    Keelan, J.2    Khodorov, B.I.3    Duchen, M.R.4
  • 94
    • 0032535275 scopus 로고    scopus 로고
    • Mitochondrial control of acute glutamate excitotoxicity in cultured cerebellar granule cells
    • Castilho RF Hansson O Ward MW Budd SL Nicholls DG 1998 Mitochondrial control of acute glutamate excitotoxicity in cultured cerebellar granule cells J Neurosci 18 10277 10286
    • (1998) J Neurosci , vol.18 , pp. 10277-10286
    • Castilho, R.F.1    Hansson, O.2    Ward, M.W.3    Budd, S.L.4    Nicholls, D.G.5
  • 95
    • 0032530326 scopus 로고    scopus 로고
    • Calcium-induced activation of the mitochondrial permeability transition in hippocampal neurons
    • Dubinsky JM Levi Y 1998 Calcium-induced activation of the mitochondrial permeability transition in hippocampal neurons J Neurosci Res 53 728 741
    • (1998) J Neurosci Res , vol.53 , pp. 728-741
    • Dubinsky, J.M.1    Levi, Y.2
  • 96
    • 0034057293 scopus 로고    scopus 로고
    • Inhibition of glutamate-induced mitochondrial depolarization by tamoxifen in cultured neurons
    • Hoyt KR Mclaughlin BA Higgins DS Jr. Reynolds IJ 2000 Inhibition of glutamate-induced mitochondrial depolarization by tamoxifen in cultured neurons J Pharmacol Exp Ther 293 480 486
    • (2000) J Pharmacol Exp Ther , vol.293 , pp. 480-486
    • Hoyt, K.R.1    McLaughlin, B.A.2    Higgins Jr., D.S.3    Reynolds, I.J.4
  • 97
    • 0031797319 scopus 로고    scopus 로고
    • Effects of oxidants and glutamate receptor activation on mitochondrial membrane potential in rat forebrain neurons
    • Scanlon JM Reynolds IJ 1998 Effects of oxidants and glutamate receptor activation on mitochondrial membrane potential in rat forebrain neurons J Neurochem 71 2392 2400
    • (1998) J Neurochem , vol.71 , pp. 2392-2400
    • Scanlon, J.M.1    Reynolds, I.J.2
  • 98
    • 0030729437 scopus 로고    scopus 로고
    • Trifluoperazine and dibucaine-induced inhibition of glutamate-induced mitochondrial depolarization in rat cultured forebrain neurones
    • Hoyt KR Sharma TA Reynolds IJ 1997 Trifluoperazine and dibucaine-induced inhibition of glutamate-induced mitochondrial depolarization in rat cultured forebrain neurones Br J Pharmacol 122 803 808
    • (1997) Br J Pharmacol , vol.122 , pp. 803-808
    • Hoyt, K.R.1    Sharma, T.A.2    Reynolds, I.J.3
  • 99
    • 0023263612 scopus 로고
    • Action of cyclosporine on mitochondrial calcium fluxes
    • Fournier N Ducet G Crevat A 1987 Action of cyclosporine on mitochondrial calcium fluxes J Bioenerg Biomembr 19 297 303
    • (1987) J Bioenerg Biomembr , vol.19 , pp. 297-303
    • Fournier, N.1    Ducet, G.2    Crevat, A.3
  • 101
    • 4344614641 scopus 로고    scopus 로고
    • Desensitization of the permeability transition pore by cyclosporin a prevents activation of the mitochondrial apoptotic pathway and liver damage by tumor necrosis factor-alpha
    • Soriano ME Nicolosi L Bernardi P 2004 Desensitization of the permeability transition pore by cyclosporin a prevents activation of the mitochondrial apoptotic pathway and liver damage by tumor necrosis factor-alpha J Biol Chem 279 36803 36808
    • (2004) J Biol Chem , vol.279 , pp. 36803-36808
    • Soriano, M.E.1    Nicolosi, L.2    Bernardi, P.3
  • 102
    • 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 2001 The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ J Biol Chem 276 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
  • 103
    • 0035951823 scopus 로고    scopus 로고
    • Opening of the mitochondrial permeability transition pore causes depletion of mitochondrial and cytosolic NAD+ and is a causative event in the death of myocytes in postischemic reperfusion of the heart
    • Di Lisa F Menabo R Canton M Barile M Bernardi P 2001 Opening of the mitochondrial permeability transition pore causes depletion of mitochondrial and cytosolic NAD+ and is a causative event in the death of myocytes in postischemic reperfusion of the heart J Biol Chem 276 2571 2575
    • (2001) J Biol Chem , vol.276 , pp. 2571-2575
    • Di Lisa, F.1    Menabo, R.2    Canton, M.3    Barile, M.4    Bernardi, P.5
  • 104
    • 0037891050 scopus 로고    scopus 로고
    • Cyclosporin A-insensitive permeability transition in brain mitochondria: Inhibition by 2-aminoethoxydiphenyl borate
    • Chinopoulos C Starkov AA Fiskum G 2003 Cyclosporin A-insensitive permeability transition in brain mitochondria: inhibition by 2-aminoethoxydiphenyl borate J Biol Chem 278 27382 27389
    • (2003) J Biol Chem , vol.278 , pp. 27382-27389
    • Chinopoulos, C.1    Starkov, A.A.2    Fiskum, G.3
  • 105
    • 0242684750 scopus 로고    scopus 로고
    • Heterogeneity of the calcium-induced permeability transition in isolated non-synaptic brain mitochondria
    • Kristian T Weatherby TM Bates TE Fiskum G 2002 Heterogeneity of the calcium-induced permeability transition in isolated non-synaptic brain mitochondria J Neurochem 83 1297 1308
    • (2002) J Neurochem , vol.83 , pp. 1297-1308
    • Kristian, T.1    Weatherby, T.M.2    Bates, T.E.3    Fiskum, G.4
  • 106
    • 0038143180 scopus 로고    scopus 로고
    • The relationship between free and total calcium concentrations in the matrix of liver and brain mitochondria
    • Chalmers S Nicholls DG 2003 The relationship between free and total calcium concentrations in the matrix of liver and brain mitochondria J Biol Chem 278 19062 19070
    • (2003) J Biol Chem , vol.278 , pp. 19062-19070
    • Chalmers, S.1    Nicholls, D.G.2
  • 107
    • 0027523160 scopus 로고
    • Coupling of cellular energy state and ion homeostasis during recovery following brain ischemia
    • Ekholm A Katsura K Kristian T Liu M Folbergrova J Siesjo BK 1993 Coupling of cellular energy state and ion homeostasis during recovery following brain ischemia Brain Res 604 185 191
    • (1993) Brain Res , vol.604 , pp. 185-191
    • Ekholm, A.1    Katsura, K.2    Kristian, T.3    Liu, M.4    Folbergrova, J.5    Siesjo, B.K.6
  • 108
    • 0019230323 scopus 로고
    • 2+-activated hydrophilic channel of the mitochondrial inner membrane by nucleotides
    • 2+-activated hydrophilic channel of the mitochondrial inner membrane by nucleotides J Membr Biol 54 231 236
    • (1980) J Membr Biol , vol.54 , pp. 231-236
    • Haworth, R.A.1    Hunter, D.R.2
  • 109
    • 0031890041 scopus 로고    scopus 로고
    • Visualization of NMDA receptor-induced mitochondrial calcium accumulation in striatal neurons
    • Peng TI Jou MJ Sheu SS Greenamyre JT 1998 Visualization of NMDA receptor-induced mitochondrial calcium accumulation in striatal neurons Exp Neurol 149 1 12
    • (1998) Exp Neurol , vol.149 , pp. 1-12
    • Peng, T.I.1    Jou, M.J.2    Sheu, S.S.3    Greenamyre, J.T.4
  • 110
    • 0034688312 scopus 로고    scopus 로고
    • Glutamate release in severe brain ischaemia is mainly by reversed uptake
    • Rossi DJ Oshima T Attwell D 2000 Glutamate release in severe brain ischaemia is mainly by reversed uptake Nature 403 316 321
    • (2000) Nature , vol.403 , pp. 316-321
    • Rossi, D.J.1    Oshima, T.2    Attwell, D.3
  • 111
    • 0036095242 scopus 로고    scopus 로고
    • NMDA-induced calcium loads recycle across the mitochondrial inner membrane of hippocampal neurons in culture
    • Wang GJ Thayer SA 2002 NMDA-induced calcium loads recycle across the mitochondrial inner membrane of hippocampal neurons in culture J Neurophysiol 87 740 749
    • (2002) J Neurophysiol , vol.87 , pp. 740-749
    • Wang, G.J.1    Thayer, S.A.2
  • 113
    • 3042595335 scopus 로고    scopus 로고
    • Excitotoxic calcium overload in a subpopulation of mitochondria triggers delayed death in hippocampal neurons
    • Pivovarova NB Nguyen HV Winters CA Brantner CA Smith CL Andrews SB 2004 Excitotoxic calcium overload in a subpopulation of mitochondria triggers delayed death in hippocampal neurons J Neurosci 24 5611 5622
    • (2004) J Neurosci , vol.24 , pp. 5611-5622
    • Pivovarova, N.B.1    Nguyen, H.V.2    Winters, C.A.3    Brantner, C.A.4    Smith, C.L.5    Andrews, S.B.6
  • 114
    • 0023220472 scopus 로고
    • Calcium in the mitochondria following brief ischemia of gerbil brain
    • Dux E Mies G Hossmann KA Siklos L 1987 Calcium in the mitochondria following brief ischemia of gerbil brain Neurosci Lett 78 295 300
    • (1987) Neurosci Lett , vol.78 , pp. 295-300
    • Dux, E.1    Mies, G.2    Hossmann, K.A.3    Siklos, L.4
  • 115
    • 0035085570 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) by oxidant stress in cerebellar granule neurons: Modulation by N-methyl-D-aspartate through calcineurin activity
    • Hallak H Ramadan B Rubin R 2001 Tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) by oxidant stress in cerebellar granule neurons: modulation by N-methyl-D-aspartate through calcineurin activity J Neurochem 77 63 70
    • (2001) J Neurochem , vol.77 , pp. 63-70
    • Hallak, H.1    Ramadan, B.2    Rubin, R.3
  • 116
    • 0027453536 scopus 로고
    • Immunosuppressant FK506 enhances phosphorylation of nitric oxide synthase and protects against glutamate neurotoxicity
    • Dawson TM Steiner JP Dawson VL Dinerman JL Uhl GR Snyder SH 1993 Immunosuppressant FK506 enhances phosphorylation of nitric oxide synthase and protects against glutamate neurotoxicity Proc Natl Acad Sci USA 90 9808 9812
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9808-9812
    • Dawson, T.M.1    Steiner, J.P.2    Dawson, V.L.3    Dinerman, J.L.4    Uhl, G.R.5    Snyder, S.H.6
  • 117
    • 0036488223 scopus 로고    scopus 로고
    • Mitochondrial permeability transition and calcium dynamics in striatal neurons upon intense NMDA receptor activation
    • Alano CC Beutner G Dirksen RT Gross RA Sheu SS 2002 Mitochondrial permeability transition and calcium dynamics in striatal neurons upon intense NMDA receptor activation J Neurochem 80 531 538
    • (2002) J Neurochem , vol.80 , pp. 531-538
    • Alano, C.C.1    Beutner, G.2    Dirksen, R.T.3    Gross, R.A.4    Sheu, S.S.5
  • 118
    • 0032860116 scopus 로고    scopus 로고
    • Cyclosporin a and its nonimmunosuppressive analogue N-Me-Val-4- cyclosporin a mitigate glucose/oxygen deprivation-induced damage to rat cultured hippocampal neurons
    • Khaspekov L Friberg H Halestrap A Viktorov I Wieloch T 1999 Cyclosporin A and its nonimmunosuppressive analogue N-Me-Val-4-cyclosporin A mitigate glucose/oxygen deprivation-induced damage to rat cultured hippocampal neurons Eur J Neurosci 11 3194 3198
    • (1999) Eur J Neurosci , vol.11 , pp. 3194-3198
    • Khaspekov, L.1    Friberg, H.2    Halestrap, A.3    Viktorov, I.4    Wieloch, T.5
  • 119
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X Kim CN Yang J Jemmerson R Wang X 1996 Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c Cell 86 147 157
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 120
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner MO 2000 The biochemistry of apoptosis Nature 407 770 776
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 121
    • 0037427440 scopus 로고    scopus 로고
    • Mitochondrial permeability transition: A common pathway to necrosis and apoptosis
    • Kim JS He L Lemasters JJ 2003 Mitochondrial permeability transition: a common pathway to necrosis and apoptosis Biochem Biophys Res Commun 304 463 470
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 463-470
    • Kim, J.S.1    He, L.2    Lemasters, J.J.3
  • 123
    • 4544298249 scopus 로고    scopus 로고
    • Mitochondrial mechanisms of neural cell apoptosis
    • Polster BM Fiskum G 2004 Mitochondrial mechanisms of neural cell apoptosis J Neurochem 90 1281 1289
    • (2004) J Neurochem , vol.90 , pp. 1281-1289
    • Polster, B.M.1    Fiskum, G.2
  • 124
    • 0037427479 scopus 로고    scopus 로고
    • Mitochondrial control of apoptosis: An introduction
    • Kroemer G 2003 Mitochondrial control of apoptosis: an introduction Biochem Biophys Res Commun 304 433 435
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 433-435
    • Kroemer, G.1
  • 126
    • 0035229427 scopus 로고    scopus 로고
    • The mitochondrion in apoptosis: How Pandora's box opens
    • Zamzami N Kroemer G 2001 The mitochondrion in apoptosis: how Pandora's box opens Nat Rev Mol Cell Biol 2 67 71
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2
  • 127
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Desagher S Martinou JC 2000 Mitochondria as the central control point of apoptosis Trends Cell Biol 10 369 377
    • (2000) Trends Cell Biol , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.C.2
  • 128
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR Reed JC 1998 Mitochondria and apoptosis Science 281 1309 1312
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 129
    • 0032504575 scopus 로고    scopus 로고
    • Mitochondria as regulators of apoptosis: Doubt no more
    • Susin SA Zamzami N Kroemer G 1998 Mitochondria as regulators of apoptosis: doubt no more Biochim Biophys Acta 1366 151 165
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 151-165
    • Susin, S.A.1    Zamzami, N.2    Kroemer, G.3
  • 130
    • 0032404536 scopus 로고    scopus 로고
    • The central executioners of apoptosis: Caspases or mitochondria?
    • Green D Kroemer G 1998 The central executioners of apoptosis: caspases or mitochondria? Trends Cell Biol 8 267 271
    • (1998) Trends Cell Biol , vol.8 , pp. 267-271
    • Green, D.1    Kroemer, G.2
  • 131
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer G Dallaporta B Resche-Rigon M 1998 The mitochondrial death/life regulator in apoptosis and necrosis Annu Rev Physiol 60 619 642
    • (1998) Annu Rev Physiol , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 135
    • 0032387842 scopus 로고    scopus 로고
    • Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition
    • Woodfield K Ruck A Brdiczka D Halestrap AP 1998 Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition Biochem J 336 287 290
    • (1998) Biochem J , vol.336 , pp. 287-290
    • Woodfield, K.1    Ruck, A.2    Brdiczka, D.3    Halestrap, A.P.4
  • 136
    • 0032401567 scopus 로고    scopus 로고
    • Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore
    • Crompton M Virji S Ward JM 1998 Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore Eur J Biochem 258 729 735
    • (1998) Eur J Biochem , vol.258 , pp. 729-735
    • Crompton, M.1    Virji, S.2    Ward, J.M.3
  • 137
    • 21244446551 scopus 로고    scopus 로고
    • Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D
    • Basso E Fante L Fowlkes J Petronilli V Forte MA Bernardi P 2005 Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D J Biol Chem 280 18558 18561
    • (2005) J Biol Chem , vol.280 , pp. 18558-18561
    • Basso, E.1    Fante, L.2    Fowlkes, J.3    Petronilli, V.4    Forte, M.A.5    Bernardi, P.6
  • 139
    • 0018269944 scopus 로고
    • The regulation of extramitochondrial free calcium ion concentration by rat liver mitochondria
    • Nicholls DG 1978 The regulation of extramitochondrial free calcium ion concentration by rat liver mitochondria Biochem J 176 463 474
    • (1978) Biochem J , vol.176 , pp. 463-474
    • Nicholls, D.G.1
  • 144
    • 0032504708 scopus 로고    scopus 로고
    • Mitochondria and neuronal glutamate excitotoxicity
    • Nicholls DG Budd SL 1998 Mitochondria and neuronal glutamate excitotoxicity Biochim Biophys Acta 1366 97 112
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 97-112
    • Nicholls, D.G.1    Budd, S.L.2
  • 145
    • 0027339920 scopus 로고
    • 2+ overload indicates early neuronal injury which precedes staining with viability indicators
    • 2+ overload indicates early neuronal injury which precedes staining with viability indicators Brain Res 607 319 323
    • (1993) Brain Res , vol.607 , pp. 319-323
    • Tymianski, M.1    Charlton, M.P.2    Carlen, P.L.3    Tator, C.H.4
  • 146
    • 0027497936 scopus 로고
    • Source specificity of early calcium neurotoxicity in cultured embryonic spinal neurons
    • Tymianski M Charlton MP Carlen PL Tator CH 1993 Source specificity of early calcium neurotoxicity in cultured embryonic spinal neurons J Neurosci 13 2085 2104
    • (1993) J Neurosci , vol.13 , pp. 2085-2104
    • Tymianski, M.1    Charlton, M.P.2    Carlen, P.L.3    Tator, C.H.4
  • 148
    • 0029117733 scopus 로고
    • Inability to restore resting intracellular calcium levels as an early indicator of delayed neuronal cell death
    • Limbrick DD Jr. Churn SB Sombati S Delorenzo RJ 1995 Inability to restore resting intracellular calcium levels as an early indicator of delayed neuronal cell death Brain Res 690 145 156
    • (1995) Brain Res , vol.690 , pp. 145-156
    • Limbrick Jr., D.D.1    Churn, S.B.2    Sombati, S.3    Delorenzo, R.J.4
  • 150
    • 0026608995 scopus 로고
    • Glutamate-induced calcium transient triggers delayed calcium overload and neurotoxicity in rat hippocampal neurons
    • Randall RD Thayer SA 1992 Glutamate-induced calcium transient triggers delayed calcium overload and neurotoxicity in rat hippocampal neurons J Neurosci 12 1882 1895
    • (1992) J Neurosci , vol.12 , pp. 1882-1895
    • Randall, R.D.1    Thayer, S.A.2
  • 152
    • 0029827804 scopus 로고    scopus 로고
    • Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells
    • Budd SL Nicholls DG 1996 Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells J Neurochem 67 2282 2291
    • (1996) J Neurochem , vol.67 , pp. 2282-2291
    • Budd, S.L.1    Nicholls, D.G.2
  • 153
    • 0028126999 scopus 로고
    • Glutamate-induced intracellular calcium changes and neurotoxicity in cortical neurons in vitro: Effect of chemical ischemia
    • Rajdev S Reynolds IJ 1994 Glutamate-induced intracellular calcium changes and neurotoxicity in cortical neurons in vitro: effect of chemical ischemia Neuroscience 62 667 679
    • (1994) Neuroscience , vol.62 , pp. 667-679
    • Rajdev, S.1    Reynolds, I.J.2
  • 154
    • 16944363081 scopus 로고    scopus 로고
    • Ionized intracellular calcium concentration predicts excitotoxic neuronal death: Observations with low-affinity fluorescent calcium indicators
    • Hyrc K Handran SD Rothman SM Goldberg MP 1997 Ionized intracellular calcium concentration predicts excitotoxic neuronal death: observations with low-affinity fluorescent calcium indicators J Neurosci 17 6669 6677
    • (1997) J Neurosci , vol.17 , pp. 6669-6677
    • Hyrc, K.1    Handran, S.D.2    Rothman, S.M.3    Goldberg, M.P.4
  • 155
    • 0024431210 scopus 로고
    • Delayed rescue of N-methyl-D-aspartate receptor-mediated neuronal injury in cortical culture
    • Hartley DM Choi DW 1989 Delayed rescue of N-methyl-D-aspartate receptor-mediated neuronal injury in cortical culture J Pharmacol Exp Ther 250 752 758
    • (1989) J Pharmacol Exp Ther , vol.250 , pp. 752-758
    • Hartley, D.M.1    Choi, D.W.2
  • 156
    • 0030987928 scopus 로고    scopus 로고
    • Secondary activation of a cation conductance is responsible for NMDA toxicity in acutely isolated hippocampal neurons
    • Chen QX Perkins KL Choi DW Wong RK 1997 Secondary activation of a cation conductance is responsible for NMDA toxicity in acutely isolated hippocampal neurons J Neurosci 17 4032 4036
    • (1997) J Neurosci , vol.17 , pp. 4032-4036
    • Chen, Q.X.1    Perkins, K.L.2    Choi, D.W.3    Wong, R.K.4
  • 157
    • 0035831137 scopus 로고    scopus 로고
    • 2+ sequestration/extrusion mechanisms following excitotoxic glutamate exposure
    • 2+ sequestration/extrusion mechanisms following excitotoxic glutamate exposure Brain Res 894 56 67
    • (2001) Brain Res , vol.894 , pp. 56-67
    • Limbrick Jr., D.D.1    Pal, S.2    Delorenzo, R.J.3
  • 158
    • 0037320279 scopus 로고    scopus 로고
    • Calcium influx constitutes the ionic basis for the maintenance of glutamate-induced extended neuronal depolarization associated with hippocampal neuronal death
    • Limbrick DD Jr. Sombati S Delorenzo RJ 2003 Calcium influx constitutes the ionic basis for the maintenance of glutamate-induced extended neuronal depolarization associated with hippocampal neuronal death Cell Calcium 33 69 81
    • (2003) Cell Calcium , vol.33 , pp. 69-81
    • Limbrick Jr., D.D.1    Sombati, S.2    Delorenzo, R.J.3
  • 162
    • 0034307759 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and glutamate excitotoxicity in cultured cerebellar granule cells
    • Ward MW Rego AC Frenguelli BG Nicholls DG 2000 Mitochondrial membrane potential and glutamate excitotoxicity in cultured cerebellar granule cells J Neurosci 20 7208 7219
    • (2000) J Neurosci , vol.20 , pp. 7208-7219
    • Ward, M.W.1    Rego, A.C.2    Frenguelli, B.G.3    Nicholls, D.G.4
  • 164
    • 3042811085 scopus 로고    scopus 로고
    • Differential contribution of plasmalemmal Na/Ca exchange isoforms to sodium-dependent calcium influx and NMDA excitotoxicity in depolarized neurons
    • Kiedrowski L Czyz A Baranauskas G Li XF Lytton J 2004 Differential contribution of plasmalemmal Na/Ca exchange isoforms to sodium-dependent calcium influx and NMDA excitotoxicity in depolarized neurons J Neurochem 90 117 128
    • (2004) J Neurochem , vol.90 , pp. 117-128
    • Kiedrowski, L.1    Czyz, A.2    Baranauskas, G.3    Li, X.F.4    Lytton, J.5
  • 165
    • 0141676771 scopus 로고    scopus 로고
    • Why did NMDA receptor antagonists fail clinical trials for stroke and traumatic brain injury?
    • Ikonomidou C Turski L 2002 Why did NMDA receptor antagonists fail clinical trials for stroke and traumatic brain injury? Lancet Neurol 1 383 386
    • (2002) Lancet Neurol , vol.1 , pp. 383-386
    • Ikonomidou, C.1    Turski, L.2
  • 167
    • 0036152391 scopus 로고    scopus 로고
    • Future of neuroprotective drugs in doubt
    • Birmingham K 2002 Future of neuroprotective drugs in doubt Nat Med 8 5
    • (2002) Nat Med , vol.8 , pp. 5
    • Birmingham, K.1
  • 168
    • 0023489906 scopus 로고
    • N-methyl-D-aspartate receptors mediate hypoxic neuronal injury in cortical culture
    • Goldberg MP Weiss JH Pham PC Choi DW 1987 N-methyl-D-aspartate receptors mediate hypoxic neuronal injury in cortical culture J Pharmacol Exp Ther 243 784 791
    • (1987) J Pharmacol Exp Ther , vol.243 , pp. 784-791
    • Goldberg, M.P.1    Weiss, J.H.2    Pham, P.C.3    Choi, D.W.4
  • 169
    • 0027328680 scopus 로고
    • Combined oxygen and glucose deprivation in cortical cell culture: Calcium-dependent and calcium-independent mechanisms of neuronal injury
    • Goldberg MP Choi DW 1993 Combined oxygen and glucose deprivation in cortical cell culture: calcium-dependent and calcium-independent mechanisms of neuronal injury J Neurosci 13 3510 3524
    • (1993) J Neurosci , vol.13 , pp. 3510-3524
    • Goldberg, M.P.1    Choi, D.W.2
  • 174
    • 0036028694 scopus 로고    scopus 로고
    • 2-Aminoethoxydiphenyl borate inhibits phototransduction and blocks voltage-gated potassium channels in Limulus ventral photoreceptors
    • Wang Y Deshpande M Payne R 2002 2-Aminoethoxydiphenyl borate inhibits phototransduction and blocks voltage-gated potassium channels in Limulus ventral photoreceptors Cell Calcium 32 209 216
    • (2002) Cell Calcium , vol.32 , pp. 209-216
    • Wang, Y.1    Deshpande, M.2    Payne, R.3
  • 175
    • 0037646985 scopus 로고    scopus 로고
    • Besides affecting intracellular calcium signaling, 2-APB reversibly blocks gap junctional coupling in confluent monolayers, thereby allowing measurement of single-cell membrane currents in undissociated cells
    • Harks EG Camina JP Peters PH Ypey DL Scheenen WJ Van Zoelen EJ Theuvenet AP 2003 Besides affecting intracellular calcium signaling, 2-APB reversibly blocks gap junctional coupling in confluent monolayers, thereby allowing measurement of single-cell membrane currents in undissociated cells FASEB J 17 941 943
    • (2003) FASEB J , vol.17 , pp. 941-943
    • Harks, E.G.1    Camina, J.P.2    Peters, P.H.3    Ypey, D.L.4    Scheenen, W.J.5    Van Zoelen, E.J.6    Theuvenet, A.P.7
  • 176
    • 0025157183 scopus 로고
    • 2+ of agonist-stimulated divalent cation entry from the refilling of the agonist-sensitive intracellular pool
    • 2+ of agonist-stimulated divalent cation entry from the refilling of the agonist-sensitive intracellular pool J Biol Chem 265 678 684
    • (1990) J Biol Chem , vol.265 , pp. 678-684
    • Kwan, C.Y.1    Putney Jr., J.W.2
  • 177
    • 0021279736 scopus 로고
    • Voltage-dependent calcium channels from brain incorporated into planar lipid bilayers
    • Nelson MT French RJ Krueger BK 1984 Voltage-dependent calcium channels from brain incorporated into planar lipid bilayers Nature 308 77 80
    • (1984) Nature , vol.308 , pp. 77-80
    • Nelson, M.T.1    French, R.J.2    Krueger, B.K.3
  • 178
    • 8544231403 scopus 로고    scopus 로고
    • Highly efficient small interfering RNA delivery to primary mammalian neurons induces MicroRNA-like effects before mRNA degradation
    • Davidson TJ Harel S Arboleda VA Prunell GF Shelanski ML Greene LA Troy CM 2004 Highly efficient small interfering RNA delivery to primary mammalian neurons induces MicroRNA-like effects before mRNA degradation J Neurosci 24 10040 10046
    • (2004) J Neurosci , vol.24 , pp. 10040-10046
    • Davidson, T.J.1    Harel, S.2    Arboleda, V.A.3    Prunell, G.F.4    Shelanski, M.L.5    Greene, L.A.6    Troy, C.M.7
  • 179
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: The penetratin system for intracellular delivery
    • Derossi D Chassaing G Prochiantz A 1998 Trojan peptides: the penetratin system for intracellular delivery Trends Cell Biol 8 84 87
    • (1998) Trends Cell Biol , vol.8 , pp. 84-87
    • Derossi, D.1    Chassaing, G.2    Prochiantz, A.3
  • 180
    • 0034176843 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and neuronal glutamate excitotoxicity: Mortality and millivolts
    • Nicholls DG Ward MW 2000 Mitochondrial membrane potential and neuronal glutamate excitotoxicity: mortality and millivolts Trends Neurosci 23 166 174
    • (2000) Trends Neurosci , vol.23 , pp. 166-174
    • Nicholls, D.G.1    Ward, M.W.2
  • 181
    • 3342941452 scopus 로고    scopus 로고
    • Relationships between superoxide levels and delayed calcium deregulation in cultured cerebellar granule cells exposed continuously to glutamate
    • Vesce S Kirk L Nicholls DG 2004 Relationships between superoxide levels and delayed calcium deregulation in cultured cerebellar granule cells exposed continuously to glutamate J Neurochem 90 683 693
    • (2004) J Neurochem , vol.90 , pp. 683-693
    • Vesce, S.1    Kirk, L.2    Nicholls, D.G.3
  • 182
    • 0037474309 scopus 로고    scopus 로고
    • Development of novel fluorescence probes that can reliably detect reactive oxygen species and distinguish specific species
    • Setsukinai K Urano Y Kakinuma K Majima HJ Nagano T 2003 Development of novel fluorescence probes that can reliably detect reactive oxygen species and distinguish specific species J Biol Chem 278 3170 3175
    • (2003) J Biol Chem , vol.278 , pp. 3170-3175
    • Setsukinai, K.1    Urano, Y.2    Kakinuma, K.3    Majima, H.J.4    Nagano, T.5
  • 185
    • 0042536473 scopus 로고    scopus 로고
    • Molecular mechanisms of calcium-dependent neurodegeneration in excitotoxicity
    • Arundine M Tymianski M 2003 Molecular mechanisms of calcium-dependent neurodegeneration in excitotoxicity Cell Calcium 34 325 337
    • (2003) Cell Calcium , vol.34 , pp. 325-337
    • Arundine, M.1    Tymianski, M.2
  • 186
    • 0028295115 scopus 로고
    • The influence of pH on cellular calcium influx during ischemia
    • Kristian T Katsura K Gido G Siesjo BK 1994 The influence of pH on cellular calcium influx during ischemia Brain Res 641 295 302
    • (1994) Brain Res , vol.641 , pp. 295-302
    • Kristian, T.1    Katsura, K.2    Gido, G.3    Siesjo, B.K.4
  • 187
    • 0029030710 scopus 로고
    • Influence of hyperglycemia and of hypercapnia on cellular calcium transients during reversible brain ischemia
    • Ekholm A Kristian T Siesjo BK 1995 Influence of hyperglycemia and of hypercapnia on cellular calcium transients during reversible brain ischemia Exp Brain Res 104 462 466
    • (1995) Exp Brain Res , vol.104 , pp. 462-466
    • Ekholm, A.1    Kristian, T.2    Siesjo, B.K.3
  • 188
    • 0026672262 scopus 로고
    • +] in the hippocampus during recovery from short-term, transient ischemia
    • +] in the hippocampus during recovery from short-term, transient ischemia J Cereb Blood Flow Metab 12 759 772
    • (1992) J Cereb Blood Flow Metab , vol.12 , pp. 759-772
    • Silver, I.A.1    Erecinska, M.2
  • 190
    • 0030047543 scopus 로고    scopus 로고
    • Calcium movements in traumatic brain injury: The role of glutamate receptor-operated ion channels
    • Nilsson P Laursen H Hillered L Hansen AJ 1996 Calcium movements in traumatic brain injury: the role of glutamate receptor-operated ion channels J Cereb Blood Flow Metab 16 262 270
    • (1996) J Cereb Blood Flow Metab , vol.16 , pp. 262-270
    • Nilsson, P.1    Laursen, H.2    Hillered, L.3    Hansen, A.J.4
  • 191
    • 0025090065 scopus 로고
    • Influence of MK-801 on brain extracellular calcium and potassium activities in severe hypoglycemia
    • Zhang ET Hansen AJ Wieloch T Lauritzen M 1990 Influence of MK-801 on brain extracellular calcium and potassium activities in severe hypoglycemia J Cereb Blood Flow Metab 10 136 139
    • (1990) J Cereb Blood Flow Metab , vol.10 , pp. 136-139
    • Zhang, E.T.1    Hansen, A.J.2    Wieloch, T.3    Lauritzen, M.4
  • 192
    • 0019846592 scopus 로고
    • Extracellular ion concentrations during spreading depression and ischemia in the rat brain cortex
    • Hansen AJ Zeuthen T 1981 Extracellular ion concentrations during spreading depression and ischemia in the rat brain cortex Acta Physiol Scand 113 437 445
    • (1981) Acta Physiol Scand , vol.113 , pp. 437-445
    • Hansen, A.J.1    Zeuthen, T.2
  • 195
    • 0014007547 scopus 로고
    • Paradoxical influence of calcium ions on the permeability of the cell membranes of the isolated rat heart
    • Zimmerman AN Hulsmann WC 1966 Paradoxical influence of calcium ions on the permeability of the cell membranes of the isolated rat heart Nature 211 646 647
    • (1966) Nature , vol.211 , pp. 646-647
    • Zimmerman, A.N.1    Hulsmann, W.C.2
  • 196
    • 0029930994 scopus 로고    scopus 로고
    • 2+-paradox in the perfused rat kidney
    • 2+-paradox in the perfused rat kidney Kidney Int 49 639 646
    • (1996) Kidney Int , vol.49 , pp. 639-646
    • Duncan, C.J.1    Morton, J.W.2
  • 197
    • 0022625322 scopus 로고
    • Calcium paradox in skeletal muscles: Physiologic and microscopic observations
    • Soza M Karpati G Carpenter S 1986 Calcium paradox in skeletal muscles: physiologic and microscopic observations Muscle Nerve 9 222 232
    • (1986) Muscle Nerve , vol.9 , pp. 222-232
    • Soza, M.1    Karpati, G.2    Carpenter, S.3
  • 199
    • 0022843927 scopus 로고
    • Ca paradox in neural injury: A hypothesis
    • Young W 1986 Ca paradox in neural injury: a hypothesis Cent Nerv Syst Trauma 3 235 251
    • (1986) Cent Nerv Syst Trauma , vol.3 , pp. 235-251
    • Young, W.1
  • 200
    • 0019411915 scopus 로고
    • Brain extracellular ion composition and EEG activity following 10 minutes ischemia in normo- and hyperglycemic rats
    • Siemkowicz E Hansen AJ 1981 Brain extracellular ion composition and EEG activity following 10 minutes ischemia in normo- and hyperglycemic rats Stroke 12 236 240
    • (1981) Stroke , vol.12 , pp. 236-240
    • Siemkowicz, E.1    Hansen, A.J.2
  • 201
    • 1842586172 scopus 로고    scopus 로고
    • Cerebral ischemia and reperfusion: The pathophysiologic concept as a basis for clinical therapy
    • Schaller B Graf R 2004 Cerebral ischemia and reperfusion: the pathophysiologic concept as a basis for clinical therapy J Cereb Blood Flow Metab 24 351 371
    • (2004) J Cereb Blood Flow Metab , vol.24 , pp. 351-371
    • Schaller, B.1    Graf, R.2
  • 203
    • 0031011668 scopus 로고    scopus 로고
    • Extracellular calcium sensed by a novel cation channel in hippocampal neurons
    • Xiong Z Lu W Macdonald JF 1997 Extracellular calcium sensed by a novel cation channel in hippocampal neurons Proc Natl Acad Sci USA 94 7012 7017
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7012-7017
    • Xiong, Z.1    Lu, W.2    MacDonald, J.F.3
  • 204
    • 1642534406 scopus 로고    scopus 로고
    • Recordings from single neocortical nerve terminals reveal a nonselective cation channel activated by decreases in extracellular calcium
    • Smith SM Bergsman JB Harata NC Scheller RH Tsien RW 2004 Recordings from single neocortical nerve terminals reveal a nonselective cation channel activated by decreases in extracellular calcium Neuron 41 243 256
    • (2004) Neuron , vol.41 , pp. 243-256
    • Smith, S.M.1    Bergsman, J.B.2    Harata, N.C.3    Scheller, R.H.4    Tsien, R.W.5
  • 206
    • 0037338889 scopus 로고    scopus 로고
    • Effect of extracellular calcium on excitability of guinea pig airway vagal afferent nerves
    • Undem BJ Oh EJ Lancaster E Weinreich D 2003 Effect of extracellular calcium on excitability of guinea pig airway vagal afferent nerves J Neurophysiol 89 1196 1204
    • (2003) J Neurophysiol , vol.89 , pp. 1196-1204
    • Undem, B.J.1    Oh, E.J.2    Lancaster, E.3    Weinreich, D.4
  • 207
    • 0030746496 scopus 로고    scopus 로고
    • Extracellular divalent cations block a cation non-selective conductance unrelated to calcium channels in rat cardiac muscle
    • Mubagwa K Stengl M Flameng W 1997 Extracellular divalent cations block a cation non-selective conductance unrelated to calcium channels in rat cardiac muscle J Physiol 502 2 235 247
    • (1997) J Physiol , vol.502 , Issue.2 , pp. 235-247
    • Mubagwa, K.1    Stengl, M.2    Flameng, W.3
  • 208
    • 84965086722 scopus 로고
    • The action of calcium on the electrical properties of squid axons
    • Frankenhaeuser B Hodgkin AL 1957 The action of calcium on the electrical properties of squid axons J Physiol 137 218 244
    • (1957) J Physiol , vol.137 , pp. 218-244
    • Frankenhaeuser, B.1    Hodgkin, A.L.2
  • 209
    • 0027175061 scopus 로고
    • Calcium release-activated calcium current in rat mast cells
    • Hoth M Penner R 1993 Calcium release-activated calcium current in rat mast cells J Physiol 465 359 386
    • (1993) J Physiol , vol.465 , pp. 359-386
    • Hoth, M.1    Penner, R.2
  • 210
  • 211
    • 0020671114 scopus 로고
    • [2 selective filters in the calcium channel of the somatic membrane of mollusk neurons]
    • Kostiuk PG Mironov SL Shuba I 1983 [2 selective filters in the calcium channel of the somatic membrane of mollusk neurons] Neirofiziologiia 15 420 427
    • (1983) Neirofiziologiia , vol.15 , pp. 420-427
    • Kostiuk, P.G.1    Mironov, S.L.2    Shuba, I.3
  • 212
    • 0021284545 scopus 로고
    • A non-selective cation conductance in frog muscle membrane blocked by micromolar external calcium ions
    • Almers W Mccleskey EW Palade PT 1984 A non-selective cation conductance in frog muscle membrane blocked by micromolar external calcium ions J Physiol 353 565 583
    • (1984) J Physiol , vol.353 , pp. 565-583
    • Almers, W.1    McCleskey, E.W.2    Palade, P.T.3
  • 213
    • 0021895277 scopus 로고
    • Currents carried by monovalent cations through calcium channels in mouse neoplastic B lymphocytes
    • Fukushima Y Hagiwara S 1985 Currents carried by monovalent cations through calcium channels in mouse neoplastic B lymphocytes J Physiol 358 255 284
    • (1985) J Physiol , vol.358 , pp. 255-284
    • Fukushima, Y.1    Hagiwara, S.2
  • 214
    • 0022531495 scopus 로고
    • Calcium channel selectivity for divalent and monovalent cations. Voltage and concentration dependence of single channel current in ventricular heart cells
    • Hess P Lansman JB Tsien RW 1986 Calcium channel selectivity for divalent and monovalent cations. Voltage and concentration dependence of single channel current in ventricular heart cells J Gen Physiol 88 293 319
    • (1986) J Gen Physiol , vol.88 , pp. 293-319
    • Hess, P.1    Lansman, J.B.2    Tsien, R.W.3
  • 215
    • 0030958262 scopus 로고    scopus 로고
    • Block of N-type calcium channels in chick sensory neurons by external sodium
    • Polo-Parada L Korn SJ 1997 Block of N-type calcium channels in chick sensory neurons by external sodium J Gen Physiol 109 693 702
    • (1997) J Gen Physiol , vol.109 , pp. 693-702
    • Polo-Parada, L.1    Korn, S.J.2
  • 218
    • 0035875963 scopus 로고    scopus 로고
    • A novel extracellular calcium sensing mechanism in voltage-gated potassium ion channels
    • Johnson JP Jr. Balser JR Bennett PB 2001 A novel extracellular calcium sensing mechanism in voltage-gated potassium ion channels J Neurosci 21 4143 4153
    • (2001) J Neurosci , vol.21 , pp. 4143-4153
    • Johnson Jr., J.P.1    Balser, J.R.2    Bennett, P.B.3
  • 220
    • 0035138842 scopus 로고    scopus 로고
    • Extracellular calcium sensing and extracellular calcium signaling
    • Brown EM Macleod RJ 2001 Extracellular calcium sensing and extracellular calcium signaling Physiol Rev 81 239 297
    • (2001) Physiol Rev , vol.81 , pp. 239-297
    • Brown, E.M.1    MacLeod, R.J.2
  • 221
    • 0026567947 scopus 로고
    • Hemi-gap-junction channels in solitary horizontal cells of the catfish retina
    • Devries SH Schwartz EA 1992 Hemi-gap-junction channels in solitary horizontal cells of the catfish retina J Physiol 445 201 230
    • (1992) J Physiol , vol.445 , pp. 201-230
    • Devries, S.H.1    Schwartz, E.A.2
  • 222
    • 0037214571 scopus 로고    scopus 로고
    • Effect of external magnesium and calcium on human connexin 46 hemichannels
    • Ebihara L Liu X Pal JD 2003 Effect of external magnesium and calcium on human connexin 46 hemichannels Biophys J 84 277 286
    • (2003) Biophys J , vol.84 , pp. 277-286
    • Ebihara, L.1    Liu, X.2    Pal, J.D.3
  • 223
    • 0032512921 scopus 로고    scopus 로고
    • 2+-sensing function of the metabotropic glutamate receptors
    • 2+-sensing function of the metabotropic glutamate receptors Science 279 1722 1725
    • (1998) Science , vol.279 , pp. 1722-1725
    • Kubo, Y.1    Miyashita, T.2    Murata, Y.3
  • 228
    • 0033545911 scopus 로고    scopus 로고
    • TRP2: A candidate transduction channel for mammalian pheromone sensory signaling
    • Liman ER Corey DP Dulac C 1999 TRP2: a candidate transduction channel for mammalian pheromone sensory signaling Proc Natl Acad Sci USA 96 5791 5796
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5791-5796
    • Liman, E.R.1    Corey, D.P.2    Dulac, C.3
  • 229
    • 0037154789 scopus 로고    scopus 로고
    • Loss of sex discrimination and male-male aggression in mice deficient for TRP2
    • Stowers L Holy TE Meister M Dulac C Koentges G 2002 Loss of sex discrimination and male-male aggression in mice deficient for TRP2 Science 295 1493 1500
    • (2002) Science , vol.295 , pp. 1493-1500
    • Stowers, L.1    Holy, T.E.2    Meister, M.3    Dulac, C.4    Koentges, G.5
  • 230
    • 0041708061 scopus 로고    scopus 로고
    • TRPC5 is a regulator of hippocampal neurite length and growth cone morphology
    • Greka A Navarro B Oancea E Duggan A Clapham DE 2003 TRPC5 is a regulator of hippocampal neurite length and growth cone morphology Nat Neurosci 6 837 845
    • (2003) Nat Neurosci , vol.6 , pp. 837-845
    • Greka, A.1    Navarro, B.2    Oancea, E.3    Duggan, A.4    Clapham, D.E.5
  • 231
    • 0033200089 scopus 로고    scopus 로고
    • Activation of a TRPC3-dependent cation current through the neurotrophin BDNF
    • Li HS Xu XZ Montell C 1999 Activation of a TRPC3-dependent cation current through the neurotrophin BDNF Neuron 24 261 273
    • (1999) Neuron , vol.24 , pp. 261-273
    • Li, H.S.1    Xu, X.Z.2    Montell, C.3
  • 233
    • 2342666609 scopus 로고    scopus 로고
    • Transient receptor potential vanilloid 4 is essential in chemotherapy-induced neuropathic pain in the rat
    • Alessandri-Haber N Dina OA Yeh JJ Parada CA Reichling DB Levine JD 2004 Transient receptor potential vanilloid 4 is essential in chemotherapy-induced neuropathic pain in the rat J Neurosci 24 4444 4452
    • (2004) J Neurosci , vol.24 , pp. 4444-4452
    • Alessandri-Haber, N.1    Dina, O.A.2    Yeh, J.J.3    Parada, C.A.4    Reichling, D.B.5    Levine, J.D.6
  • 235
    • 0033010201 scopus 로고    scopus 로고
    • Evidence for a role of Trp proteins in the oxidative stress-induced membrane conductances of porcine aortic endothelial cells
    • Balzer M Lintschinger B Groschner K 1999 Evidence for a role of Trp proteins in the oxidative stress-induced membrane conductances of porcine aortic endothelial cells Cardiovasc Res 42 543 549
    • (1999) Cardiovasc Res , vol.42 , pp. 543-549
    • Balzer, M.1    Lintschinger, B.2    Groschner, K.3
  • 236
    • 0037189484 scopus 로고    scopus 로고
    • Activation of the Cation Channel Long Transient Receptor Potential Channel 2 (LTRPC2) by Hydrogen Peroxide. a splice variant reveals a mode of activation independent of ADP-ribose
    • Wehage E Eisfeld J Heiner I Jungling E Zitt C Luckhoff A 2002 Activation of the Cation Channel Long Transient Receptor Potential Channel 2 (LTRPC2) by Hydrogen Peroxide. A splice variant reveals a mode of activation independent of ADP-ribose J Biol Chem 277 23150 23156
    • (2002) J Biol Chem , vol.277 , pp. 23150-23156
    • Wehage, E.1    Eisfeld, J.2    Heiner, I.3    Jungling, E.4    Zitt, C.5    Luckhoff, A.6
  • 239
    • 0035039598 scopus 로고    scopus 로고
    • Calcium influx via TRP channels is required to maintain PIP2 levels in Drosophila photoreceptors
    • Hardie RC Raghu P Moore S Juusola M Baines RA Sweeney ST 2001 Calcium influx via TRP channels is required to maintain PIP2 levels in Drosophila photoreceptors Neuron 30 149 159
    • (2001) Neuron , vol.30 , pp. 149-159
    • Hardie, R.C.1    Raghu, P.2    Moore, S.3    Juusola, M.4    Baines, R.A.5    Sweeney, S.T.6
  • 241
    • 0036086490 scopus 로고    scopus 로고
    • TRPC6 is a candidate channel involved in receptor-stimulated cation currents in A7r5 smooth muscle cells
    • Jung S Strotmann R Schultz G Plant TD 2002 TRPC6 is a candidate channel involved in receptor-stimulated cation currents in A7r5 smooth muscle cells Am J Physiol Cell Physiol 282 C347 C359
    • (2002) Am J Physiol Cell Physiol , vol.282
    • Jung, S.1    Strotmann, R.2    Schultz, G.3    Plant, T.D.4
  • 243
    • 10644283084 scopus 로고    scopus 로고
    • Multiple regulation by calcium of murine homologues of transient receptor potential proteins TRPC6 and TRPC7 expressed in HEK293 cell
    • Shi J Mori E Mori Y Mori M Li J Ito Y Inoue R 2004 Multiple regulation by calcium of murine homologues of transient receptor potential proteins TRPC6 and TRPC7 expressed in HEK293 cell J Physiol 561 415 432
    • (2004) J Physiol , vol.561 , pp. 415-432
    • Shi, J.1    Mori, E.2    Mori, Y.3    Mori, M.4    Li, J.5    Ito, Y.6    Inoue, R.7
  • 245
    • 0038662789 scopus 로고    scopus 로고
    • Expression profile of the transient receptor potential (TRP) family in neutrophil granulocytes: Evidence for currents through LTRPC2 induced by ADP-ribose and NAD
    • Heiner I Eisfeld J Halaszovich CR Wehage E Jungling E Zitt C Luckhoff A 2003 Expression profile of the transient receptor potential (TRP) family in neutrophil granulocytes: evidence for currents through LTRPC2 induced by ADP-ribose and NAD Biochem J 371 1045 1053
    • (2003) Biochem J , vol.371 , pp. 1045-1053
    • Heiner, I.1    Eisfeld, J.2    Halaszovich, C.R.3    Wehage, E.4    Jungling, E.5    Zitt, C.6    Luckhoff, A.7
  • 246
    • 15944417442 scopus 로고    scopus 로고
    • Cyclic ADP-ribose and hydrogen peroxide synergize with ADP-ribose in the activation of TRPM2 channels
    • Kolisek M Beck A Fleig A Penner R 2005 Cyclic ADP-ribose and hydrogen peroxide synergize with ADP-ribose in the activation of TRPM2 channels Mol Cell 18 61 69
    • (2005) Mol Cell , vol.18 , pp. 61-69
    • Kolisek, M.1    Beck, A.2    Fleig, A.3    Penner, R.4
  • 247
    • 21344437332 scopus 로고    scopus 로고
    • Function and pharmacology of TRPM cation channels
    • Harteneck C 2005 Function and pharmacology of TRPM cation channels Naunyn Schmiedebergs Arch Pharmacol 371 307 314
    • (2005) Naunyn Schmiedebergs Arch Pharmacol , vol.371 , pp. 307-314
    • Harteneck, C.1
  • 249
    • 0034023238 scopus 로고    scopus 로고
    • New functions of a long-known molecule. Emerging roles of NAD in cellular signaling
    • Ziegler M 2000 New functions of a long-known molecule. Emerging roles of NAD in cellular signaling Eur J Biochem 267 1550 1564
    • (2000) Eur J Biochem , vol.267 , pp. 1550-1564
    • Ziegler, M.1
  • 250
  • 251
    • 0141755156 scopus 로고    scopus 로고
    • Formation of novel TRPC channels by complex subunit interactions in embryonic brain
    • Strubing C Krapivinsky G Krapivinsky L Clapham DE 2003 Formation of novel TRPC channels by complex subunit interactions in embryonic brain J Biol Chem 278 39014 39019
    • (2003) J Biol Chem , vol.278 , pp. 39014-39019
    • Strubing, C.1    Krapivinsky, G.2    Krapivinsky, L.3    Clapham, D.E.4
  • 255
    • 7444230420 scopus 로고    scopus 로고
    • RNase-L regulates the stability of mitochondrial DNA-encoded mRNAs in mouse embryo fibroblasts
    • Chandrasekaran K Mehrabian Z Li XL Hassel B 2004 RNase-L regulates the stability of mitochondrial DNA-encoded mRNAs in mouse embryo fibroblasts Biochem Biophys Res Commun 325 18 23
    • (2004) Biochem Biophys Res Commun , vol.325 , pp. 18-23
    • Chandrasekaran, K.1    Mehrabian, Z.2    Li, X.L.3    Hassel, B.4
  • 260
    • 0042829363 scopus 로고    scopus 로고
    • Regulation and critical role of potassium homeostasis in apoptosis
    • Yu SP 2003 Regulation and critical role of potassium homeostasis in apoptosis Prog Neurobiol 70 363 386
    • (2003) Prog Neurobiol , vol.70 , pp. 363-386
    • Yu, S.P.1
  • 261
    • 0037040395 scopus 로고    scopus 로고
    • The TRP channels, a remarkably functional family
    • Montell C Birnbaumer L Flockerzi V 2002 The TRP channels, a remarkably functional family Cell 108 595 598
    • (2002) Cell , vol.108 , pp. 595-598
    • Montell, C.1    Birnbaumer, L.2    Flockerzi, V.3
  • 265
    • 0038673321 scopus 로고    scopus 로고
    • NAD(P)H fluorescence imaging of postsynaptic neuronal activation in murine hippocampal slices
    • Shuttleworth CW Brennan AM Connor JA 2003 NAD(P)H fluorescence imaging of postsynaptic neuronal activation in murine hippocampal slices J Neurosci 23 3196 3208
    • (2003) J Neurosci , vol.23 , pp. 3196-3208
    • Shuttleworth, C.W.1    Brennan, A.M.2    Connor, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.