메뉴 건너뛰기




Volumn 11, Issue 2, 2011, Pages 98-106

Mitochondria: The headquarters in ischemia-induced neuronal death

Author keywords

Apoptosis; Minocycline; Mitochondrial permeability; Necrosis; Neuroprotection; Pharmacological target; Stroke

Indexed keywords

APOPTOSIS INDUCING FACTOR; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CALCIUM; CASPASE 9; CYTOCHROME C; ENDONUCLEASE G; MINOCYCLINE; PLACEBO; REACTIVE OXYGEN METABOLITE; TISSUE PLASMINOGEN ACTIVATOR; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 79959319233     PISSN: 18715249     EISSN: 18756166     Source Type: Journal    
DOI: 10.2174/187152411796011358     Document Type: Review
Times cited : (30)

References (114)
  • 1
    • 26444539696 scopus 로고    scopus 로고
    • The existence and evolution of diffusion-perfusion mismatched tissue in white and gray matter after acute stroke
    • Koga, M.; Reutens, D.C.; Wright, P.; Phan, T.; Markus, R.; Pedreira, B.; Fitt, G.; Lim, I.; Donnan, G.A. The existence and evolution of diffusion-perfusion mismatched tissue in white and gray matter after acute stroke. Stroke, 2005, 36(10), 2132-2137.
    • (2005) Stroke , vol.36 , Issue.10 , pp. 2132-2137
    • Koga, M.1    Reutens, D.C.2    Wright, P.3    Phan, T.4    Markus, R.5    Pedreira, B.6    Fitt, G.7    Lim, I.8    Donnan, G.A.9
  • 5
    • 77951477328 scopus 로고    scopus 로고
    • An overview of investigational antiapoptotic drugs with potential application for the treatment of neurodegenerative disorders
    • Camins, A.; Sureda, F.X.; Junyent, F.; Verdaguer, E.; Folch, J.; Beas-Zarate, C.; Pallas, M. An overview of investigational antiapoptotic drugs with potential application for the treatment of neurodegenerative disorders. Expert Opin. Investig. Drugs, 2010, 19(5), 587-604.
    • (2010) Expert Opin. Investig. Drugs. , vol.19 , Issue.5 , pp. 587-604
    • Camins, A.1    Sureda, F.X.2    Junyent, F.3    Verdaguer, E.4    Folch, J.5    Beas-Zarate, C.6    Pallas, M.7
  • 6
    • 0034016574 scopus 로고    scopus 로고
    • Mass spectrometric identification of proteins released from mitochondria undergoing permeability transition
    • Patterson, S.D.; Spahr, C.S.; Daugas, E.; Susin, S.A.; Irinopoulou, T.; Koehler, C.; Kroemer, G. Mass spectrometric identification of proteins released from mitochondria undergoing permeability transition. Cell Death Differ., 2000, 7(2), 137-144.
    • (2000) Cell Death Differ , vol.7 , Issue.2 , pp. 137-144
    • Patterson, S.D.1    Spahr, C.S.2    Daugas, E.3    Susin, S.A.4    Irinopoulou, T.5    Koehler, C.6    Kroemer, G.7
  • 7
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer, G.; Reed, J.C. Mitochondrial control of cell death. Nat. Med., 2000, 6(5), 513-519.
    • (2000) Nat. Med. , vol.6 , Issue.5 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 8
    • 67649965950 scopus 로고    scopus 로고
    • The mitochondrial death pathway: A promising therapeutic target in diseases
    • Gupta, S.; Kass, G.E.; Szegezdi, E.; Joseph, B. The mitochondrial death pathway: a promising therapeutic target in diseases. J. Cell. Mol. Med., 2009, 13(6), 1004-1033.
    • (2009) J. Cell. Mol. Med. , vol.13 , Issue.6 , pp. 1004-1033
    • Gupta, S.1    Kass, G.E.2    Szegezdi, E.3    Joseph, B.4
  • 9
    • 67649794783 scopus 로고    scopus 로고
    • New insights into mitochondrial structure during cell death
    • Perkins, G.; Bossy-Wetzel, E.; Ellisman, M.H. New insights into mitochondrial structure during cell death. Exp. Neurol., 2009, 218(2), 183-192.
    • (2009) Exp. Neurol. , vol.218 , Issue.2 , pp. 183-192
    • Perkins, G.1    Bossy-Wetzel, E.2    Ellisman, M.H.3
  • 11
    • 67649460932 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in neuronal injury
    • Galluzzi, L.; Blomgren, K.; Kroemer, G. Mitochondrial membrane permeabilization in neuronal injury. Nat. Rev. Neurosci., 2009, 10(7), 481-494.
    • (2009) Nat. Rev. Neurosci. , vol.10 , Issue.7 , pp. 481-494
    • Galluzzi, L.1    Blomgren, K.2    Kroemer, G.3
  • 12
    • 77954755957 scopus 로고    scopus 로고
    • Mitochondrial biology in Alzheimer's disease pathogenesis
    • Galindo, M.F.; Ikuta, I.; Zhu, X.; Casadesus, G.; Jordan, J. Mitochondrial biology in Alzheimer's disease pathogenesis. J. Neurochem., 2010, 114(4), 933-945.
    • (2010) J. Neurochem. , vol.114 , Issue.4 , pp. 933-945
    • Galindo, M.F.1    Ikuta, I.2    Zhu, X.3    Casadesus, G.4    Jordan, J.5
  • 13
    • 67649772111 scopus 로고    scopus 로고
    • The role of mitochondrial transition pore, and its modulation, in traumatic brain injury and delayed neurodegeneration after TBI
    • Mazzeo, A.T.; Beat, A.; Singh, A.; Bullock, M.R. The role of mitochondrial transition pore, and its modulation, in traumatic brain injury and delayed neurodegeneration after TBI. Exp. Neurol., 2009, 218(2), 363-370.
    • (2009) Exp. Neurol. , vol.218 , Issue.2 , pp. 363-370
    • Mazzeo, A.T.1    Beat, A.2    Singh, A.3    Bullock, M.R.4
  • 14
    • 0036175596 scopus 로고    scopus 로고
    • Mitochondrial contributions to tissue damage in stroke
    • Sims, N.R.; Anderson, M.F. Mitochondrial contributions to tissue damage in stroke. Neurochem. Int., 2002, 40(6), 511-526.
    • (2002) Neurochem. Int. , vol.40 , Issue.6 , pp. 511-526
    • Sims, N.R.1    Anderson, M.F.2
  • 15
    • 72149093510 scopus 로고    scopus 로고
    • Mitochondria, oxidative metabolism and cell death in stroke
    • Sims, N.R.; Muyderman, H. Mitochondria, oxidative metabolism and cell death in stroke. Biochim. Biophys. Acta, 2010, 1802(1), 80-91.
    • (2010) Biochim. Biophys. Acta. , vol.1802 , Issue.1 , pp. 80-91
    • Sims, N.R.1    Muyderman, H.2
  • 16
    • 0242401920 scopus 로고    scopus 로고
    • Role and regulation of p53 in depolarization-induced neuronal death
    • Jordan, J.; Galindo, M.F.; Gonzalez-Garcia, C.; Cena, V. Role and regulation of p53 in depolarization-induced neuronal death. Neuroscience, 2003, 122(3), 707-715.
    • (2003) Neuroscience , vol.122 , Issue.3 , pp. 707-715
    • Jordan, J.1    Galindo, M.F.2    Gonzalez-Garcia, C.3    Cena, V.4
  • 17
    • 0028799654 scopus 로고
    • Calcium: Still center-stage in hypoxic-ischemic neuronal death
    • Choi, D.W. Calcium: still center-stage in hypoxic-ischemic neuronal death. Trends Neurosci., 1995, 18(2), 58-60.
    • (1995) Trends Neurosci , vol.18 , Issue.2 , pp. 58-60
    • Choi, D.W.1
  • 18
    • 0030567766 scopus 로고    scopus 로고
    • Calcium-related damage in ischemia
    • Kristian, T.; Siesjo, B.K. Calcium-related damage in ischemia. Life Sci., 1996, 59(5-6), 357-367.
    • (1996) Life Sci , vol.59 , Issue.5-6 , pp. 357-367
    • Kristian, T.1    Siesjo, B.K.2
  • 19
    • 0033199996 scopus 로고    scopus 로고
    • Pathobiology of ischaemic stroke: An integrated view
    • Dirnagl, U.; Iadecola, C.; Moskowitz, M.A. Pathobiology of ischaemic stroke: an integrated view. Trends Neurosci., 1999, 22(9), 391-397.
    • (1999) Trends Neurosci , vol.22 , Issue.9 , pp. 391-397
    • Dirnagl, U.1    Iadecola, C.2    Moskowitz, M.A.3
  • 20
    • 0029926299 scopus 로고    scopus 로고
    • Glutamate excitotoxicity in transient global cerebral ischemia
    • Paschen, W. Glutamate excitotoxicity in transient global cerebral ischemia. Acta Neurobiol. Exp. (Wars.), 1996, 56(1), 313-322.
    • (1996) Acta Neurobiol. Exp. (Wars.) , vol.56 , Issue.1 , pp. 313-322
    • Paschen, W.1
  • 21
    • 74549206659 scopus 로고    scopus 로고
    • Blocking the deadly effects of the NMDA receptor in stroke
    • Martin, H.G.; Wang, Y.T. Blocking the deadly effects of the NMDA receptor in stroke. Cell, 2010, 140(2), 174-176.
    • (2010) Cell , vol.140 , Issue.2 , pp. 174-176
    • Martin, H.G.1    Wang, Y.T.2
  • 24
    • 43049183344 scopus 로고    scopus 로고
    • Recommendations and treatment strategies for the management of acute ischemic stroke
    • Segura, T.; Calleja, S.; Jordan, J. Recommendations and treatment strategies for the management of acute ischemic stroke. Expert Opin. Pharmacother., 2008, 9(7), 1071-1085.
    • (2008) Expert Opin. Pharmacother. , vol.9 , Issue.7 , pp. 1071-1085
    • Segura, T.1    Calleja, S.2    Jordan, J.3
  • 25
    • 77951251430 scopus 로고    scopus 로고
    • Necroptosis as an alternative form of programmed cell death
    • Christofferson, D.E.; Yuan, J. Necroptosis as an alternative form of programmed cell death. Curr. Opin. Cell Biol., 2010, 22(2), 263-268.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , Issue.2 , pp. 263-268
    • Christofferson, D.E.1    Yuan, J.2
  • 26
    • 33644763298 scopus 로고    scopus 로고
    • Inhibition of ADP/ATP exchange in receptor-interacting protein-mediated necrosis
    • Temkin, V.; Huang, Q.; Liu, H.; Osada, H.; Pope, R.M. Inhibition of ADP/ATP exchange in receptor-interacting protein-mediated necrosis. Mol. Cell. Biol., 2006, 26(6), 2215-2225.
    • (2006) Mol. Cell. Biol. , vol.26 , Issue.6 , pp. 2215-2225
    • Temkin, V.1    Huang, Q.2    Liu, H.3    Osada, H.4    Pope, R.M.5
  • 27
    • 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., 1999, 249(2), 396-403.
    • (1999) Exp. Cell Res. , vol.249 , Issue.2 , pp. 396-403
    • Leist, M.1    Single, B.2    Naumann, H.3    Fava, E.4    Simon, B.5    Kuhnle, S.6    Nicotera, P.7
  • 28
    • 0032127595 scopus 로고    scopus 로고
    • Neuronal calcium signaling
    • Berridge, M.J. Neuronal calcium signaling. Neuron, 1998, 21(1), 13-26.
    • (1998) Neuron , vol.21 , Issue.1 , pp. 13-26
    • Berridge, M.J.1
  • 29
    • 0032531818 scopus 로고    scopus 로고
    • Calcium--a life and death signal
    • Berridge, M.J.; Bootman, M.D.; Lipp, P. Calcium--a life and death signal. Nature, 1998, 395(6703), 645-648.
    • (1998) Nature , vol.395 , Issue.6703 , pp. 645-648
    • Berridge, M.J.1    Bootman, M.D.2    Lipp, P.3
  • 30
    • 0025292743 scopus 로고
    • Mechanisms by which mitochondria transport calcium
    • Gunter, T.E.; Pfeiffer, D.R. Mechanisms by which mitochondria transport calcium. Am. J. Physiol., 1990, 258(5 Pt 1), C755-786.
    • (1990) Am. J. Physiol. , vol.258 , Issue.5 PART 1
    • Gunter, T.E.1    Pfeiffer, D.R.2
  • 31
    • 0022308360 scopus 로고
    • Ca2+ transport by mammalian mitochondria and its role in hormone action
    • Denton, R.M.; McCormack, J.G. Ca2+ transport by mammalian mitochondria and its role in hormone action. Am. J. Physiol., 1985, 249(6 Pt 1), E543-554.
    • (1985) Am. J. Physiol. , vol.249 , Issue.6 PART 1
    • Denton, R.M.1    McCormack, J.G.2
  • 32
    • 0029827804 scopus 로고    scopus 로고
    • Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells
    • Budd, S.L.; Nicholls, D.G. Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells. J. Neurochem., 1996, 67(6), 2282-2291.
    • (1996) J. Neurochem. , vol.67 , Issue.6 , pp. 2282-2291
    • Budd, S.L.1    Nicholls, D.G.2
  • 33
    • 10244257617 scopus 로고    scopus 로고
    • The integration of mitochondrial calcium transport and storage
    • Nicholls, D.G.; Chalmers, S. The integration of mitochondrial calcium transport and storage. J. Bioenerg. Biomembr., 2004, 36(4), 277-281.
    • (2004) J. Bioenerg. Biomembr. , vol.36 , Issue.4 , pp. 277-281
    • Nicholls, D.G.1    Chalmers, S.2
  • 34
    • 38449092423 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore
    • discussion 164-159
    • Bernardi, P.; Forte, M. The mitochondrial permeability transition pore. Novartis Found. Symp., 2007, 287, 157-164; discussion 164-159.
    • (2007) Novartis Found. Symp. , vol.287 , pp. 157-164
    • Bernardi, P.1    Forte, M.2
  • 35
    • 33746824336 scopus 로고    scopus 로고
    • Elevated cytosolic Na+ decreases mitochondrial Ca2+ uptake during excitation-contraction coupling and impairs energetic adaptation in cardiac myocytes
    • Maack, C.; Cortassa, S.; Aon, M.A.; Ganesan, A.N.; Liu, T.; O'Rourke, B. Elevated cytosolic Na+ decreases mitochondrial Ca2+ uptake during excitation-contraction coupling and impairs energetic adaptation in cardiac myocytes. Circ. Res., 2006, 99(2), 172-182.
    • (2006) Circ. Res. , vol.99 , Issue.2 , pp. 172-182
    • Maack, C.1    Cortassa, S.2    Aon, M.A.3    Ganesan, A.N.4    Liu, T.5    O'Rourke, B.6
  • 36
    • 0242582202 scopus 로고    scopus 로고
    • Synchronized whole cell oscillations in mitochondrial metabolism triggered by a local release of reactive oxygen species in cardiac myocytes
    • Aon, M.A.; Cortassa, S.; Marban, E.; O'Rourke, B. Synchronized whole cell oscillations in mitochondrial metabolism triggered by a local release of reactive oxygen species in cardiac myocytes. J. Biol. Chem., 2003, 278(45), 44735-44744.
    • (2003) J. Biol. Chem. , vol.278 , Issue.45 , pp. 44735-44744
    • Aon, M.A.1    Cortassa, S.2    Marban, E.3    O'Rourke, B.4
  • 37
    • 0036773295 scopus 로고    scopus 로고
    • Cardiac energy metabolism homeostasis: Role of cytosolic calcium
    • Balaban, R.S. Cardiac energy metabolism homeostasis: role of cytosolic calcium. J. Mol. Cell. Cardiol., 2002, 34(10), 1259-1271.
    • (2002) J. Mol. Cell. Cardiol. , vol.34 , Issue.10 , pp. 1259-1271
    • Balaban, R.S.1
  • 38
    • 67349147645 scopus 로고    scopus 로고
    • Mitochondrial calcium transport and mitochondrial dysfunction after global brain ischemia in rat hippocampus
    • Racay, P.; Tatarkova, Z.; Chomova, M.; Hatok, J.; Kaplan, P.; Dobrota, D. Mitochondrial calcium transport and mitochondrial dysfunction after global brain ischemia in rat hippocampus. Neurochem. Res., 2009, 34(8), 1469-1478.
    • (2009) Neurochem. Res. , vol.34 , Issue.8 , pp. 1469-1478
    • Racay, P.1    Tatarkova, Z.2    Chomova, M.3    Hatok, J.4    Kaplan, P.5    Dobrota, D.6
  • 39
    • 77549083577 scopus 로고    scopus 로고
    • Calcium, ischemia and excitotoxicity
    • Szydlowska, K.; Tymianski, M. Calcium, ischemia and excitotoxicity. Cell Calcium, 2010, 47(2), 122-129.
    • (2010) Cell Calcium , vol.47 , Issue.2 , pp. 122-129
    • Szydlowska, K.1    Tymianski, M.2
  • 40
    • 0032421139 scopus 로고    scopus 로고
    • Neuronal excitotoxicity: The role of mitochondria
    • Nicholls, D.G.; Budd, S.L. Neuronal excitotoxicity: the role of mitochondria. Biofactors, 1998, 8(3-4), 287-299.
    • (1998) Biofactors , vol.8 , Issue.3-4 , pp. 287-299
    • Nicholls, D.G.1    Budd, S.L.2
  • 41
    • 0032504708 scopus 로고    scopus 로고
    • Mitochondria and neuronal glutamate excitotoxicity
    • Nicholls, D.G.; Budd, S.L. Mitochondria and neuronal glutamate excitotoxicity. Biochim. Biophys. Acta, 1998, 1366(1-2), 97-112.
    • (1998) Biochim. Biophys. Acta. , vol.1366 , Issue.1-2 , pp. 97-112
    • Nicholls, D.G.1    Budd, S.L.2
  • 42
    • 0033386202 scopus 로고    scopus 로고
    • Mitochondria in neurodegeneration: Bioenergetic function in cell life and death
    • Murphy, A.N.; Fiskum, G.; Beal, M.F. Mitochondria in neurodegeneration: bioenergetic function in cell life and death. J. Cereb. Blood. Flow. Metab., 1999, 19(3), 231-245.
    • (1999) J. Cereb. Blood. Flow. Metab. , vol.19 , Issue.3 , pp. 231-245
    • Murphy, A.N.1    Fiskum, G.2    Beal, M.F.3
  • 43
    • 0024475202 scopus 로고
    • Delayed increase of Ca2+ influx elicited by glutamate: Role in neuronal death. Mol
    • Manev, H.; Favaron, M.; Guidotti, A.; Costa, E. Delayed increase of Ca2+ influx elicited by glutamate: role in neuronal death. Mol. Pharmacol., 1989, 36(1), 106-112.
    • (1989) Pharmacol , vol.36 , Issue.1 , pp. 106-112
    • Manev, H.1    Favaron, M.2    Guidotti, A.3    Costa, E.4
  • 44
    • 0026608995 scopus 로고
    • Glutamate-induced calcium transient triggers delayed calcium overload and neurotoxicity in rat hippocampal neurons
    • Randall, R.D.; Thayer, S.A. Glutamate-induced calcium transient triggers delayed calcium overload and neurotoxicity in rat hippocampal neurons. J. Neurosci., 1992, 12(5), 1882-1895.
    • (1992) J. Neurosci. , vol.12 , Issue.5 , pp. 1882-1895
    • Randall, R.D.1    Thayer, S.A.2
  • 45
    • 0027497936 scopus 로고
    • Source specificity of early calcium neurotoxicity in cultured embryonic spinal neurons
    • Tymianski, M.; Charlton, M.P.; Carlen, P.L.; Tator, C.H. Source specificity of early calcium neurotoxicity in cultured embryonic spinal neurons. J. Neurosci., 1993, 13(5), 2085-2104.
    • (1993) J. Neurosci. , vol.13 , Issue.5 , pp. 2085-2104
    • Tymianski, M.1    Charlton, M.P.2    Carlen, P.L.3    Tator, C.H.4
  • 46
    • 0033971898 scopus 로고    scopus 로고
    • Mitochondria and neuronal survival
    • Nicholls, D.G.; Budd, S.L. Mitochondria and neuronal survival. Physiol. Rev., 2000, 80(1), 315-360.
    • (2000) Physiol. Rev. , vol.80 , Issue.1 , pp. 315-360
    • Nicholls, D.G.1    Budd, S.L.2
  • 47
    • 0042035647 scopus 로고    scopus 로고
    • Interactions between mitochondrial bioenergetics and cytoplasmic calcium in cultured cerebellar granule cells
    • Nicholls, D.G.; Vesce, S.; Kirk, L.; Chalmers, S. Interactions between mitochondrial bioenergetics and cytoplasmic calcium in cultured cerebellar granule cells. Cell Calcium, 2003, 34(4-5), 407-424.
    • (2003) Cell Calcium , vol.34 , Issue.4-5 , pp. 407-424
    • Nicholls, D.G.1    Vesce, S.2    Kirk, L.3    Chalmers, S.4
  • 48
    • 0027339920 scopus 로고
    • Secondary Ca2+ overload indicates early neuronal injury which precedes staining with viability indicators
    • Tymianski, M.; Charlton, M.P.; Carlen, P.L.; Tator, C.H. Secondary Ca2+ overload indicates early neuronal injury which precedes staining with viability indicators. Brain Res., 1993, 607(1-2), 319-323.
    • (1993) Brain Res , vol.607 , Issue.1-2 , pp. 319-323
    • Tymianski, M.1    Charlton, M.P.2    Carlen, P.L.3    Tator, C.H.4
  • 49
    • 0028063326 scopus 로고
    • Complex correlation between excitatory amino acidinduced increase in the intracellular Ca2+ concentration and subsequent loss of neuronal function in individual neocortical neurons in culture
    • Witt, M.R.; Dekermendjian, K.; Frandsen, A.; Schousboe, A.; Nielsen, M. Complex correlation between excitatory amino acidinduced increase in the intracellular Ca2+ concentration and subsequent loss of neuronal function in individual neocortical neurons in culture. Proc. Natl Acad. Sci. USA, 1994, 91(25), 12303-12307.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , Issue.25 , pp. 12303-12307
    • Witt, M.R.1    Dekermendjian, K.2    Frandsen, A.3    Schousboe, A.4    Nielsen, M.5
  • 50
    • 0029117733 scopus 로고
    • Inability to restore resting intracellular calcium levels as an early indicator of delayed neuronal cell death
    • Limbrick, D.D., Jr.; Churn, S.B.; Sombati, S.; DeLorenzo, R.J. Inability to restore resting intracellular calcium levels as an early indicator of delayed neuronal cell death. Brain Res., 1995, 690(2), 145-156.
    • (1995) Brain Res , vol.690 , Issue.2 , pp. 145-156
    • Limbrick Jr., D.D.1    Churn, S.B.2    Sombati, S.3    Delorenzo, R.J.4
  • 51
    • 50549096439 scopus 로고    scopus 로고
    • Mitochondrial Ca2+ overload underlies Abeta oligomers neurotoxicity providing an unexpected mechanism of neuroprotection by NSAIDs
    • Sanz-Blasco, S.; Valero, R.A.; Rodriguez-Crespo, I.; Villalobos, C.; Nunez, L. Mitochondrial Ca2+ overload underlies Abeta oligomers neurotoxicity providing an unexpected mechanism of neuroprotection by NSAIDs. PLoS One, 2008, 3(7), e2718.
    • (2008) PLoS One , vol.3 , Issue.7
    • Sanz-Blasco, S.1    Valero, R.A.2    Rodriguez-Crespo, I.3    Villalobos, C.4    Nunez, L.5
  • 52
    • 0030969868 scopus 로고    scopus 로고
    • Superoxide production by the mitochondrial respiratory chain
    • Turrens, J.F. Superoxide production by the mitochondrial respiratory chain. Biosci. Rep., 1997, 17(1), 3-8.
    • (1997) Biosci. Rep. , vol.17 , Issue.1 , pp. 3-8
    • Turrens, J.F.1
  • 53
    • 0345258510 scopus 로고    scopus 로고
    • Regulation of hypertrophic and apoptotic signaling pathways by reactive oxygen species in cardiac myocytes
    • Sabri, A.; Hughie, H.H.; Lucchesi, P.A. Regulation of hypertrophic and apoptotic signaling pathways by reactive oxygen species in cardiac myocytes. Antioxid. Redox Signal., 2003, 5(6), 731-740.
    • (2003) Antioxid. Redox Signal. , vol.5 , Issue.6 , pp. 731-740
    • Sabri, A.1    Hughie, H.H.2    Lucchesi, P.A.3
  • 54
    • 0031849502 scopus 로고    scopus 로고
    • Causative role of oxyradicals in myocardial stunning: A proven hypothesis. A brief review of the evidence demonstrating a major role of reactive oxygen species in several forms of postischemic dysfunction
    • Bolli, R. Causative role of oxyradicals in myocardial stunning: a proven hypothesis. A brief review of the evidence demonstrating a major role of reactive oxygen species in several forms of postischemic dysfunction. Basic Res. Cardiol., 1998, 93(3), 156-162.
    • (1998) Basic Res. Cardiol. , vol.93 , Issue.3 , pp. 156-162
    • Bolli, R.1
  • 55
    • 3042856265 scopus 로고    scopus 로고
    • Role of oxidative stress in cardiac remodelling after myocardial infarction
    • Grieve, D.J.; Byrne, J.A.; Cave, A.C.; Shah, A.M. Role of oxidative stress in cardiac remodelling after myocardial infarction. Heart Lung Circ., 2004, 13(2), 132-138.
    • (2004) Heart Lung Circ , vol.13 , Issue.2 , pp. 132-138
    • Grieve, D.J.1    Byrne, J.A.2    Cave, A.C.3    Shah, A.M.4
  • 56
    • 4043077961 scopus 로고    scopus 로고
    • Molecular mediators of hepatic steatosis and liver injury
    • Browning, J.D.; Horton, J.D. Molecular mediators of hepatic steatosis and liver injury. J. Clin. Invest., 2004, 114(2), 147-152.
    • (2004) J. Clin. Invest. , vol.114 , Issue.2 , pp. 147-152
    • Browning, J.D.1    Horton, J.D.2
  • 57
    • 0036275522 scopus 로고    scopus 로고
    • Nitric oxide and superoxide, a deadly cocktail
    • Estevez, A.G.; Jordan, J. Nitric oxide and superoxide, a deadly cocktail. Ann. N. Y. Acad. Sci., 2002, 962, 207-211.
    • (2002) Ann. N. Y. Acad. Sci. , vol.962 , pp. 207-211
    • Estevez, A.G.1    Jordan, J.2
  • 58
    • 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., 2001, 359(Pt 1), 139-145.
    • (2001) Biochem. J. , vol.359 , Issue.PART 1 , 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
  • 59
    • 0141510019 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial complex I due to peroxynitrite: Identification of reactive tyrosines by mass spectrometry
    • Murray, J.; Taylor, S.W.; Zhang, B.; Ghosh, S.S.; Capaldi, R.A. Oxidative damage to mitochondrial complex I due to peroxynitrite: identification of reactive tyrosines by mass spectrometry. J. Biol. Chem., 2003, 278(39), 37223-37230.
    • (2003) J. Biol. Chem. , vol.278 , Issue.39 , pp. 37223-37230
    • Murray, J.1    Taylor, S.W.2    Zhang, B.3    Ghosh, S.S.4    Capaldi, R.A.5
  • 60
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown, G.C.; Cooper, C.E. Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase. FEBS Lett., 1994, 356(2-3), 295-298.
    • (1994) FEBS Lett , vol.356 , Issue.2-3 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 61
    • 34248207189 scopus 로고    scopus 로고
    • Coenzyme Q treatment of neurodegenerative diseases of aging
    • Galpern, W.R.; Cudkowicz, M.E. Coenzyme Q treatment of neurodegenerative diseases of aging. Mitochondrion, 2007, 7 Suppl, S146-153.
    • (2007) Mitochondrion , vol.7 , Issue.SUPPL.
    • Galpern, W.R.1    Cudkowicz, M.E.2
  • 62
    • 0031255803 scopus 로고    scopus 로고
    • Oral coenzyme Q10 administration prevents the development of ischemic brain lesions in a rabbit model of symptomatic vasospasm
    • Grieb, P.; Ryba, M.S.; Sawicki, J.; Chrapusta, S.J. Oral coenzyme Q10 administration prevents the development of ischemic brain lesions in a rabbit model of symptomatic vasospasm. Acta Neuropathol., 1997, 94(4), 363-368.
    • (1997) Acta Neuropathol , vol.94 , Issue.4 , pp. 363-368
    • Grieb, P.1    Ryba, M.S.2    Sawicki, J.3    Chrapusta, S.J.4
  • 63
    • 0033250594 scopus 로고    scopus 로고
    • Effect of coenzyme Q10 (CoQ10) on superoxide dismutase activity in ET-1 and ET-3 experimental models of cerebral ischemia in the rat
    • Ostrowski, R.P. Effect of coenzyme Q10 (CoQ10) on superoxide dismutase activity in ET-1 and ET-3 experimental models of cerebral ischemia in the rat. Folia Neuropathol., 1999, 37(4), 247-251.
    • (1999) Folia Neuropathol , vol.37 , Issue.4 , pp. 247-251
    • Ostrowski, R.P.1
  • 64
    • 0034665834 scopus 로고    scopus 로고
    • CoQ10 fails to protect brain against focal and global ischemia in rats
    • Li, H.; Klein, G.; Sun, P.; Buchan, A.M. CoQ10 fails to protect brain against focal and global ischemia in rats. Brain Res., 2000, 877(1), 7-11.
    • (2000) Brain Res , vol.877 , Issue.1 , pp. 7-11
    • Li, H.1    Klein, G.2    Sun, P.3    Buchan, A.M.4
  • 66
    • 0029854155 scopus 로고    scopus 로고
    • ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane
    • Rostovtseva, T.; Colombini, M. ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane. J. Biol. Chem., 1996, 271(45), 28006-28008.
    • (1996) J. Biol. Chem. , vol.271 , Issue.45 , pp. 28006-28008
    • Rostovtseva, T.1    Colombini, M.2
  • 67
    • 0034724190 scopus 로고    scopus 로고
    • BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death
    • Shimizu, S.; Konishi, A.; Kodama, T.; Tsujimoto, Y. BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death. Proc. Natl Acad. Sci. USA, 2000, 97(7), 3100-3105.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , Issue.7 , pp. 3100-3105
    • Shimizu, S.1    Konishi, A.2    Kodama, T.3    Tsujimoto, Y.4
  • 68
    • 77955055915 scopus 로고    scopus 로고
    • Viability of saccharomyces cerevisiae cells following exposure to H2O2 and protective effect of minocycline depend on the presence of VDAC
    • Galganska, H.; Karachitos, A.; Baranek, M.; Budzinska, M.; Jordan, J.; Kmita, H. Viability of Saccharomyces cerevisiae cells following exposure to H2O2 and protective effect of minocycline depend on the presence of VDAC. Eur. J. Pharmacol., 2010, 643(1), 42-47.
    • (2010) Eur. J. Pharmacol. , vol.643 , Issue.1 , pp. 42-47
    • Galganska, H.1    Karachitos, A.2    Baranek, M.3    Budzinska, M.4    Jordan, J.5    Kmita, H.6
  • 69
    • 0041810128 scopus 로고    scopus 로고
    • The adenine nucleotide translocase: A central component of the mitochondrial permeability transition pore and key player in cell death
    • Halestrap, A.P.; Brenner, C. The adenine nucleotide translocase: a central component of the mitochondrial permeability transition pore and key player in cell death. Curr. Med. Chem., 2003, 10(16), 1507-1525.
    • (2003) Curr. Med. Chem. , vol.10 , Issue.16 , pp. 1507-1525
    • Halestrap, A.P.1    Brenner, C.2
  • 70
    • 0036478989 scopus 로고    scopus 로고
    • The permeability transition pore complex: Another view
    • Halestrap, A.P.; McStay, G.P.; Clarke, S.J. The permeability transition pore complex: another view. Biochimie, 2002, 84(2-3), 153-166.
    • (2002) Biochimie , vol.84 , Issue.2-3 , pp. 153-166
    • Halestrap, A.P.1    McStay, G.P.2    Clarke, S.J.3
  • 72
    • 0032528154 scopus 로고    scopus 로고
    • Cyclosporin A, but not FK 506, protects mitochondria and neurons against hypoglycemic damage and implicates the mitochondrial permeability transition in cell death
    • Friberg, H.; Ferrand-Drake, M.; Bengtsson, F.; Halestrap, A.P.; Wieloch, T. Cyclosporin A, but not FK 506, protects mitochondria and neurons against hypoglycemic damage and implicates the mitochondrial permeability transition in cell death. J. Neurosci., 1998, 18(14), 5151-5159.
    • (1998) J. Neurosci. , vol.18 , Issue.14 , pp. 5151-5159
    • Friberg, H.1    Ferrand-Drake, M.2    Bengtsson, F.3    Halestrap, A.P.4    Wieloch, T.5    Cyclosporin, A.6
  • 73
    • 0032504709 scopus 로고    scopus 로고
    • Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury of the heart
    • Halestrap, A.P.; Kerr, P.M.; Javadov, S.; Woodfield, K.Y. Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury of the heart. Biochim. Biophys. Acta, 1998, 1366(1-2), 79-94.
    • (1998) Biochim. Biophys. Acta. , vol.1366 , Issue.1-2 , pp. 79-94
    • Halestrap, A.P.1    Kerr, P.M.2    Javadov, S.3    Woodfield, K.Y.4
  • 74
    • 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., 1999, 341 (Pt 2), 233-249.
    • (1999) Biochem. J. , vol.341 , Issue.PART 2 , pp. 233-249
    • Crompton, M.1
  • 76
    • 15844404722 scopus 로고    scopus 로고
    • Biochemistry: A pore way to die
    • Halestrap, A. Biochemistry: a pore way to die. Nature, 2005, 434(7033), 578-579.
    • (2005) Nature , vol.434 , Issue.7033 , pp. 578-579
    • Halestrap, A.1
  • 77
    • 0033556544 scopus 로고    scopus 로고
    • The mitochondrial permeability transition mediates both necrotic and apoptotic death of hepatocytes exposed to Br-A23187
    • Qian, T.; Herman, B.; Lemasters, J.J. The mitochondrial permeability transition mediates both necrotic and apoptotic death of hepatocytes exposed to Br-A23187. Toxicol. Appl. Pharmacol., 1999, 154(2), 117-125.
    • (1999) Toxicol. Appl. Pharmacol. , vol.154 , Issue.2 , pp. 117-125
    • Qian, T.1    Herman, B.2    Lemasters, J.J.3
  • 78
    • 0034642510 scopus 로고    scopus 로고
    • Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis
    • Costantini, P.; Belzacq, A.S.; Vieira, H.L.; Larochette, N.; de Pablo, M.A.; Zamzami, N.; Susin, S.A.; Brenner, C.; Kroemer, G. Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis. Oncogene, 2000, 19(2), 307-314.
    • (2000) Oncogene , vol.19 , Issue.2 , pp. 307-314
    • Costantini, P.1    Belzacq, A.S.2    Vieira, H.L.3    Larochette, N.4    de Pablo, M.A.5    Zamzami, N.6    Susin, S.A.7    Brenner, C.8    Kroemer, G.9
  • 80
    • 1642464737 scopus 로고    scopus 로고
    • Oxidative stress underlies the mechanism for Ca(2+)-induced permeability transition of mitochondria
    • Kanno, T.; Sato, E.E.; Muranaka, S.; Fujita, H.; Fujiwara, T.; Utsumi, T.; Inoue, M.; Utsumi, K. Oxidative stress underlies the mechanism for Ca(2+)-induced permeability transition of mitochondria. Free Radic. Res., 2004, 38(1), 27-35.
    • (2004) Free Radic. Res. , vol.38 , Issue.1 , pp. 27-35
    • Kanno, T.1    Sato, E.E.2    Muranaka, S.3    Fujita, H.4    Fujiwara, T.5    Utsumi, T.6    Inoue, M.7    Utsumi, K.8
  • 81
    • 0037025058 scopus 로고    scopus 로고
    • The mechanisms of neuronal death produced by mitochondrial toxin 3-nitropropionic acid: The roles of N-methyl-D-aspartate glutamate receptors and mitochondrial calcium overload
    • Lee, W.T.; Yin, H.S.; Shen, Y.Z. The mechanisms of neuronal death produced by mitochondrial toxin 3-nitropropionic acid: the roles of N-methyl-D-aspartate glutamate receptors and mitochondrial calcium overload. Neuroscience, 2002, 112(3), 707-716.
    • (2002) Neuroscience , vol.112 , Issue.3 , pp. 707-716
    • Lee, W.T.1    Yin, H.S.2    Shen, Y.Z.3
  • 82
    • 1442274934 scopus 로고    scopus 로고
    • Mitochondrial calcium, oxidative stress and apoptosis in a neurodegenerative disease model induced by 3-nitropropionic acid
    • Rosenstock, T.R.; Carvalho, A.C.; Jurkiewicz, A.; Frussa-Filho, R.; Smaili, S.S. Mitochondrial calcium, oxidative stress and apoptosis in a neurodegenerative disease model induced by 3-nitropropionic acid. J. Neurochem., 2004, 88(5), 1220-1228.
    • (2004) J. Neurochem. , vol.88 , Issue.5 , pp. 1220-1228
    • Rosenstock, T.R.1    Carvalho, A.C.2    Jurkiewicz, A.3    Frussa-Filho, R.4    Smaili, S.S.5
  • 83
    • 0027772027 scopus 로고
    • On the involvement of a mitochondrial pore in reperfusion injury
    • Crompton, M.; Andreeva, L. On the involvement of a mitochondrial pore in reperfusion injury. Basic Res. Cardiol., 1993, 88(5), 513-523.
    • (1993) Basic Res. Cardiol. , vol.88 , Issue.5 , pp. 513-523
    • Crompton, M.1    Andreeva, L.2
  • 84
    • 0032775546 scopus 로고    scopus 로고
    • Lipid peroxidation and alterations to oxidative metabolism in mitochondria isolated from rat heart subjected to ischemia and reperfusion
    • Paradies, G.; Petrosillo, G.; Pistolese, M.; Di Venosa, N.; Serena, D.; Ruggiero, F.M. Lipid peroxidation and alterations to oxidative metabolism in mitochondria isolated from rat heart subjected to ischemia and reperfusion. Free Radic. Biol. Med., 1999, 27(1-2), 42-50.
    • (1999) Free Radic. Biol. Med. , vol.27 , Issue.1-2 , pp. 42-50
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Di Venosa, N.4    Serena, D.5    Ruggiero, F.M.6
  • 85
    • 0037664459 scopus 로고    scopus 로고
    • Reactive oxygen species induce swelling and cytochrome c release but not transmembrane depolarization in isolated rat brain mitochondria. Br
    • Galindo, M.F.; Jordan, J.; Gonzalez-Garcia, C.; Cena, V. Reactive oxygen species induce swelling and cytochrome c release but not transmembrane depolarization in isolated rat brain mitochondria. Br. J. Pharmacol., 2003, 139(4), 797-804.
    • (2003) J. Pharmacol. , vol.139 , Issue.4 , pp. 797-804
    • Galindo, M.F.1    Jordan, J.2    Gonzalez-Garcia, C.3    Cena, V.4
  • 86
    • 0037023211 scopus 로고    scopus 로고
    • Effect of NXY-059 on secondary mitochondrial dysfunction after transient focal ischemia; comparison with cyclosporin A
    • Yoshimoto, T.; Kristian, T.; Hu, B.; Ouyang, Y.B.; Siesjo, B.K. Effect of NXY-059 on secondary mitochondrial dysfunction after transient focal ischemia; comparison with cyclosporin A. Brain Res., 2002, 932(1-2), 99-109.
    • (2002) Brain Res , vol.932 , Issue.1-2 , pp. 99-109
    • Yoshimoto, T.1    Kristian, T.2    Hu, B.3    Ouyang, Y.B.4    Siesjo, B.K.5
  • 87
    • 0033612939 scopus 로고    scopus 로고
    • Posttreatment with the immunosuppressant cyclosporin A in transient focal ischemia
    • Yoshimoto, T.; Siesjo, B.K. Posttreatment with the immunosuppressant cyclosporin A in transient focal ischemia. Brain Res., 1999, 839(2), 283-291.
    • (1999) Brain Res , vol.839 , Issue.2 , pp. 283-291
    • Yoshimoto, T.1    Siesjo, B.K.2
  • 88
    • 0035957808 scopus 로고    scopus 로고
    • Cyclosporin A, but not FK506, prevents the downregulation of phosphorylated Akt after transient focal ischemia in the rat
    • Yoshimoto, T.; Uchino, H.; He, Q.P.; Li, P.A.; Siesjo, B.K. Cyclosporin A, but not FK506, prevents the downregulation of phosphorylated Akt after transient focal ischemia in the rat. Brain Res., 2001, 899(1-2), 148-158.
    • (2001) Brain Res , vol.899 , Issue.1-2 , pp. 148-158
    • Yoshimoto, T.1    Uchino, H.2    He, Q.P.3    Li, P.A.4    Siesjo, B.K.5
  • 89
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa, T.; Shimizu, S.; Watanabe, T.; Yamaguchi, O.; Otsu, K.; Yamagata, H.; Inohara, H.; Kubo, T.; Tsujimoto, Y. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature, 2005, 434(7033), 652-658.
    • (2005) Nature , vol.434 , Issue.7033 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3    Yamaguchi, O.4    Otsu, K.5    Yamagata, H.6    Inohara, H.7    Kubo, T.8    Tsujimoto, Y.9
  • 91
    • 33751504957 scopus 로고    scopus 로고
    • Upgrading the BCL-2 network
    • Galonek, H.L.; Hardwick, J.M. Upgrading the BCL-2 network. Nat. Cell Biol., 2006, 8(12), 1317-1319.
    • (2006) Nat. Cell Biol. , vol.8 , Issue.12 , pp. 1317-1319
    • Galonek, H.L.1    Hardwick, J.M.2
  • 92
    • 0028274733 scopus 로고
    • Multiple subcellular localization of bcl-2: Detection in nuclear outer membrane, endoplasmic reticulum membrane, and mitochondrial membranes
    • Akao, Y.; Otsuki, Y.; Kataoka, S.; Ito, Y.; Tsujimoto, Y. Multiple subcellular localization of bcl-2: detection in nuclear outer membrane, endoplasmic reticulum membrane, and mitochondrial membranes. Cancer Res., 1994, 54(9), 2468-2471.
    • (1994) Cancer Res , vol.54 , Issue.9 , pp. 2468-2471
    • Akao, Y.1    Otsuki, Y.2    Kataoka, S.3    Ito, Y.4    Tsujimoto, Y.5
  • 93
    • 0027362667 scopus 로고
    • Investigation of the subcellular distribution of the bcl-2 oncoprotein: Residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes
    • Krajewski, S.; Tanaka, S.; Takayama, S.; Schibler, M.J.; Fenton, W.; Reed, J.C. Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res., 1993, 53(19), 4701-4714.
    • (1993) Cancer Res , vol.53 , Issue.19 , pp. 4701-4714
    • Krajewski, S.1    Tanaka, S.2    Takayama, S.3    Schibler, M.J.4    Fenton, W.5    Reed, J.C.6
  • 94
    • 77956410991 scopus 로고    scopus 로고
    • Neuroprotective effect of Bax-inhibiting peptide on neonatal brain injury
    • Wang, X.; Han, W.; Du, X.; Zhu, C.; Carlsson, Y.; Mallard, C.; Jacotot, E.; Hagberg, H. Neuroprotective effect of Bax-inhibiting peptide on neonatal brain injury. Stroke, 2010, 41(9), 2050-2055.
    • (2010) Stroke , vol.41 , Issue.9 , pp. 2050-2055
    • Wang, X.1    Han, W.2    Du, X.3    Zhu, C.4    Carlsson, Y.5    Mallard, C.6    Jacotot, E.7    Hagberg, H.8
  • 95
    • 0029070924 scopus 로고
    • Essential role of adenosine, adenosine A1 receptors, and ATP-sensitive K+ channels in cerebral ischemic preconditioning
    • Heurteaux, C.; Lauritzen, I.; Widmann, C.; Lazdunski, M. Essential role of adenosine, adenosine A1 receptors, and ATP-sensitive K+ channels in cerebral ischemic preconditioning. Proc. Natl Acad. Sci. USA, 1995, 92(10), 4666-4670.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , Issue.10 , pp. 4666-4670
    • Heurteaux, C.1    Lauritzen, I.2    Widmann, C.3    Lazdunski, M.4
  • 96
    • 51249100204 scopus 로고    scopus 로고
    • Mitochondrial-mediated suppression of ROS production upon exposure of neurons to lethal stress: Mitochondrial targeted preconditioning
    • Busija, D.W.; Gaspar, T.; Domoki, F.; Katakam, P.V.; Bari, F. Mitochondrial-mediated suppression of ROS production upon exposure of neurons to lethal stress: mitochondrial targeted preconditioning. Adv. Drug Deliv. Rev., 2008, 60(13-14), 1471-1477.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , Issue.13-14 , pp. 1471-1477
    • Busija, D.W.1    Gaspar, T.2    Domoki, F.3    Katakam, P.V.4    Bari, F.5
  • 97
    • 38349124184 scopus 로고    scopus 로고
    • Molecular physiology of preconditioninginduced brain tolerance to ischemia
    • Obrenovitch, T.P. Molecular physiology of preconditioninginduced brain tolerance to ischemia. Physiol. Rev., 2008, 88(1), 211-247.
    • (2008) Physiol. Rev. , vol.88 , Issue.1 , pp. 211-247
    • Obrenovitch, T.P.1
  • 98
    • 0035209457 scopus 로고    scopus 로고
    • Ischemic preconditioning preserves mitochondrial function after global cerebral ischemia in rat hippocampus
    • Dave, K.R.; Saul, I.; Busto, R.; Ginsberg, M.D.; Sick, T.J.; Perez- Pinzon, M.A. Ischemic preconditioning preserves mitochondrial function after global cerebral ischemia in rat hippocampus. J. Cereb. Blood Flow Metab., 2001, 21(12), 1401-1410.
    • (2001) J. Cereb. Blood Flow Metab. , vol.21 , Issue.12 , pp. 1401-1410
    • Dave, K.R.1    Saul, I.2    Busto, R.3    Ginsberg, M.D.4    Sick, T.J.5    Perez-Pinzon, M.A.6
  • 99
    • 34848857903 scopus 로고    scopus 로고
    • Effect of ischemic preconditioning on mitochondrial dysfunction and mitochondrial p53 translocation after transient global cerebral ischemia in rats
    • Racay, P.; Tatarkova, Z.; Drgova, A.; Kaplan, P.; Dobrota, D. Effect of ischemic preconditioning on mitochondrial dysfunction and mitochondrial p53 translocation after transient global cerebral ischemia in rats. Neurochem. Res., 2007, 32(11), 1823-1832.
    • (2007) Neurochem. Res. , vol.32 , Issue.11 , pp. 1823-1832
    • Racay, P.1    Tatarkova, Z.2    Drgova, A.3    Kaplan, P.4    Dobrota, D.5
  • 100
    • 33845548578 scopus 로고    scopus 로고
    • The changes in endogenous antioxidant enzyme activity after postconditioning
    • Danielisova, V.; Nemethova, M.; Gottlieb, M.; Burda, J. The changes in endogenous antioxidant enzyme activity after postconditioning. Cell. Mol. Neurobiol., 2006, 26(7-8), 1181-1191.
    • (2006) Cell. Mol. Neurobiol. , vol.26 , Issue.7-8 , pp. 1181-1191
    • Danielisova, V.1    Nemethova, M.2    Gottlieb, M.3    Burda, J.4
  • 101
    • 38449090057 scopus 로고    scopus 로고
    • Minoxidil prevents 3,4- methylenedioxymethamphetamine-induced serotonin depletions: Role of mitochondrial ATP-sensitive potassium channels, Akt and ERK
    • Goni-Allo, B.; Puerta, E.; Ramos, M.; Lasheras, B.; Jordan, J.; Aguirre, N. Minoxidil prevents 3,4- methylenedioxymethamphetamine-induced serotonin depletions: role of mitochondrial ATP-sensitive potassium channels, Akt and ERK. J. Neurochem., 2008, 104(4), 914-925.
    • (2008) J. Neurochem. , vol.104 , Issue.4 , pp. 914-925
    • Goni-Allo, B.1    Puerta, E.2    Ramos, M.3    Lasheras, B.4    Jordan, J.5    Aguirre, N.6
  • 102
    • 58149357087 scopus 로고    scopus 로고
    • Phosphodiesterase 5 inhibitors prevent 3,4- methylenedioxymethamphetamine-induced 5-HT deficits in the rat
    • Puerta, E.; Hervias, I.; Goni-Allo, B.; Lasheras, B.; Jordan, J.; Aguirre, N. Phosphodiesterase 5 inhibitors prevent 3,4- methylenedioxymethamphetamine-induced 5-HT deficits in the rat. J. Neurochem., 2009, 108(3), 755-766.
    • (2009) J. Neurochem. , vol.108 , Issue.3 , pp. 755-766
    • Puerta, E.1    Hervias, I.2    Goni-Allo, B.3    Lasheras, B.4    Jordan, J.5    Aguirre, N.6
  • 103
    • 34547130863 scopus 로고    scopus 로고
    • The role of mitochondria in protection of the heart by preconditioning
    • Halestrap, A.P.; Clarke, S.J.; Khaliulin, I. The role of mitochondria in protection of the heart by preconditioning. Biochim. Biophys. Acta, 2007, 1767(8), 1007-1031.
    • (2007) Biochim. Biophys. Acta. , vol.1767 , Issue.8 , pp. 1007-1031
    • Halestrap, A.P.1    Clarke, S.J.2    Khaliulin, I.3
  • 104
    • 48849099462 scopus 로고    scopus 로고
    • Endogenous neuroprotection: Mitochondria as gateways to cerebral preconditioning?
    • Dirnagl, U.; Meisel, A. Endogenous neuroprotection: mitochondria as gateways to cerebral preconditioning? Neuropharmacology, 2008, 55(3), 334-344.
    • (2008) Neuropharmacology , vol.55 , Issue.3 , pp. 334-344
    • Dirnagl, U.1    Meisel, A.2
  • 105
    • 77956916990 scopus 로고    scopus 로고
    • The use of elevation and dependency to enhance the predictive value of transcutaneous oxygen pressure measurements in the assessment of foot amputation healing
    • Andrews, K.L.; Boon, A.J.; Dib, M.; Liedl, D.A.; Yacyshyn, A.; Yacyshyn, V. The use of elevation and dependency to enhance the predictive value of transcutaneous oxygen pressure measurements in the assessment of foot amputation healing. PM. R., 2005, 2(9), 829-834.
    • (2005) PM. R. , vol.2 , Issue.9 , pp. 829-834
    • Andrews, K.L.1    Boon, A.J.2    Dib, M.3    Liedl, D.A.4    Yacyshyn, A.5    Yacyshyn, V.6
  • 106
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov, S.S.; Skulachev, V.P.; Starkov, A.A. High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett., 1997, 416(1), 15-18.
    • (1997) FEBS Lett , vol.416 , Issue.1 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 107
    • 0038443821 scopus 로고    scopus 로고
    • Mitochondrial uncoupling protein-2 protects the immature brain from excitotoxic neuronal death
    • Sullivan, P.G.; Dube, C.; Dorenbos, K.; Steward, O.; Baram, T.Z. Mitochondrial uncoupling protein-2 protects the immature brain from excitotoxic neuronal death. Ann. Neurol., 2003, 53(6), 711-717.
    • (2003) Ann. Neurol , vol.53 , Issue.6 , pp. 711-717
    • Sullivan, P.G.1    Dube, C.2    Dorenbos, K.3    Steward, O.4    Baram, T.Z.5
  • 108
    • 0242468451 scopus 로고    scopus 로고
    • Uncoupling protein 2 prevents neuronal death including that occurring during seizures: A mechanism for preconditioning
    • Diano, S.; Matthews, R.T.; Patrylo, P.; Yang, L.; Beal, M.F.; Barnstable, C.J.; Horvath, T.L. Uncoupling protein 2 prevents neuronal death including that occurring during seizures: a mechanism for preconditioning. Endocrinology, 2003, 144(11), 5014-5021.
    • (2003) Endocrinology , vol.144 , Issue.11 , pp. 5014-5021
    • Diano, S.1    Matthews, R.T.2    Patrylo, P.3    Yang, L.4    Beal, M.F.5    Barnstable, C.J.6    Horvath, T.L.7
  • 109
    • 9644295698 scopus 로고    scopus 로고
    • Clinical potential of minocycline for neurodegenerative disorders
    • Blum, D.; Chtarto, A.; Tenenbaum, L.; Brotchi, J.; Levivier, M. Clinical potential of minocycline for neurodegenerative disorders. Neurobiol. Dis., 2004, 17(3), 359-366.
    • (2004) Neurobiol. Dis. , vol.17 , Issue.3 , pp. 359-366
    • Blum, D.1    Chtarto, A.2    Tenenbaum, L.3    Brotchi, J.4    Levivier, M.5
  • 110
    • 77954457577 scopus 로고    scopus 로고
    • Minocycline chelates Ca2+, binds to membranes, and depolarizes mitochondria by formation of Ca2+-dependent ion channels
    • Antonenko, Y.N.; Rokitskaya, T.I.; Cooper, A.J.; Krasnikov, B.F. Minocycline chelates Ca2+, binds to membranes, and depolarizes mitochondria by formation of Ca2+-dependent ion channels. J. Bioenerg. Biomembr., 2010, 42(2), 151-163.
    • (2010) J. Bioenerg. Biomembr. , vol.42 , Issue.2 , pp. 151-163
    • Antonenko, Y.N.1    Rokitskaya, T.I.2    Cooper, A.J.3    Krasnikov, B.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.