메뉴 건너뛰기




Volumn 10, Issue 6, 2011, Pages 639-653

Mitochondrial DNA toxicity compromises mitochondrial dynamics and induces hippocampal antioxidant defenses

Author keywords

AP sites; DNA repair; Mitochondria; Neurodegeneration; ROS; Transgenic mice

Indexed keywords

ANTIOXIDANT; GLUTAMIC ACID; MITOCHONDRIAL DNA; REACTIVE OXYGEN METABOLITE;

EID: 79957859792     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2011.04.011     Document Type: Article
Times cited : (21)

References (72)
  • 1
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siecle
    • Saraste M. Oxidative phosphorylation at the fin de siecle. Science 1999, 283:1488-1493.
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 2
    • 42049090126 scopus 로고    scopus 로고
    • Mitochondria: the hub of cellular Ca2+ signaling
    • Szabadkai G., Duchen M.R. Mitochondria: the hub of cellular Ca2+ signaling. Physiology (Bethesda) 2008, 23:84-94.
    • (2008) Physiology (Bethesda) , vol.23 , pp. 84-94
    • Szabadkai, G.1    Duchen, M.R.2
  • 3
    • 73349091842 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • Wang C., Youle R.J. The role of mitochondria in apoptosis. Annu. Rev. Genet. 2009, 43:95-118.
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 95-118
    • Wang, C.1    Youle, R.J.2
  • 4
    • 33745274726 scopus 로고    scopus 로고
    • Mitochondria: dynamic organelles in disease, aging, and development
    • Chan D.C. Mitochondria: dynamic organelles in disease, aging, and development. Cell 2006, 125:1241-1252.
    • (2006) Cell , vol.125 , pp. 1241-1252
    • Chan, D.C.1
  • 5
    • 33745757783 scopus 로고    scopus 로고
    • Critical dependence of neurons on mitochondrial dynamics
    • Chen H., Chan D.C. Critical dependence of neurons on mitochondrial dynamics. Curr. Opin. Cell Biol. 2006, 18:453-459.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 453-459
    • Chen, H.1    Chan, D.C.2
  • 6
    • 64649093169 scopus 로고    scopus 로고
    • Mitochondrial dynamics and neurodegeneration
    • Lu B. Mitochondrial dynamics and neurodegeneration. Curr. Neurol. Neurosci. Rep. 2009, 9:212-219.
    • (2009) Curr. Neurol. Neurosci. Rep. , vol.9 , pp. 212-219
    • Lu, B.1
  • 7
    • 64349099993 scopus 로고    scopus 로고
    • The role of abnormal mitochondrial dynamics in the pathogenesis of Alzheimer's disease
    • Wang X., Su B., Zheng L., Perry G., Smith M.A., Zhu X. The role of abnormal mitochondrial dynamics in the pathogenesis of Alzheimer's disease. J. Neurochem. 2009, 109(Suppl 1):153-159.
    • (2009) J. Neurochem. , vol.109 , Issue.SUPPL 1 , pp. 153-159
    • Wang, X.1    Su, B.2    Zheng, L.3    Perry, G.4    Smith, M.A.5    Zhu, X.6
  • 8
    • 0034784359 scopus 로고    scopus 로고
    • An energy budget for signaling in the grey matter of the brain
    • Attwell D., Laughlin S.B. An energy budget for signaling in the grey matter of the brain. J. Cereb. Blood Flow Metab. 2001, 21:1133-1145.
    • (2001) J. Cereb. Blood Flow Metab. , vol.21 , pp. 1133-1145
    • Attwell, D.1    Laughlin, S.B.2
  • 10
    • 0037137704 scopus 로고    scopus 로고
    • Axonal transport of mitochondria to synapses depends on milton, a novel Drosophila protein
    • Stowers R.S., Megeath L.J., Gorska-Andrzejak J., Meinertzhagen I.A., Schwarz T.L. Axonal transport of mitochondria to synapses depends on milton, a novel Drosophila protein. Neuron 2002, 36:1063-1077.
    • (2002) Neuron , vol.36 , pp. 1063-1077
    • Stowers, R.S.1    Megeath, L.J.2    Gorska-Andrzejak, J.3    Meinertzhagen, I.A.4    Schwarz, T.L.5
  • 11
    • 23044506102 scopus 로고    scopus 로고
    • Synaptic mitochondria are critical for mobilization of reserve pool vesicles at Drosophila neuromuscular junctions
    • Verstreken P., Ly C.V., Venken K.J., Koh T.W., Zhou Y., Bellen H.J. Synaptic mitochondria are critical for mobilization of reserve pool vesicles at Drosophila neuromuscular junctions. Neuron 2005, 47:365-378.
    • (2005) Neuron , vol.47 , pp. 365-378
    • Verstreken, P.1    Ly, C.V.2    Venken, K.J.3    Koh, T.W.4    Zhou, Y.5    Bellen, H.J.6
  • 12
    • 10944269186 scopus 로고    scopus 로고
    • The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
    • Li Z., Okamoto K., Hayashi Y., Sheng M. The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses. Cell 2004, 119:873-887.
    • (2004) Cell , vol.119 , pp. 873-887
    • Li, Z.1    Okamoto, K.2    Hayashi, Y.3    Sheng, M.4
  • 13
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe D.J. Alzheimer's disease is a synaptic failure. Science 2002, 298:789-791.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 15
    • 48749085779 scopus 로고    scopus 로고
    • Dynamin-like protein 1 reduction underlies mitochondrial morphology and distribution abnormalities in fibroblasts from sporadic Alzheimer's disease patients
    • Wang X., Su B., Fujioka H., Zhu X. Dynamin-like protein 1 reduction underlies mitochondrial morphology and distribution abnormalities in fibroblasts from sporadic Alzheimer's disease patients. Am. J. Pathol. 2008, 173:470-482.
    • (2008) Am. J. Pathol. , vol.173 , pp. 470-482
    • Wang, X.1    Su, B.2    Fujioka, H.3    Zhu, X.4
  • 17
    • 27744500994 scopus 로고    scopus 로고
    • Subunit arrangement and function in NMDA receptors
    • Furukawa H., Singh S.K., Mancusso R., Gouaux E. Subunit arrangement and function in NMDA receptors. Nature 2005, 438:185-192.
    • (2005) Nature , vol.438 , pp. 185-192
    • Furukawa, H.1    Singh, S.K.2    Mancusso, R.3    Gouaux, E.4
  • 18
    • 0025366890 scopus 로고
    • A quantitative electron microscopic immunocytochemical study of the distribution and synaptic handling of glutamate in rat hippocampus
    • Ottersen O.P., Storm-Mathisen J., Bramham C., Torp R., Laake J., Gundersen V. A quantitative electron microscopic immunocytochemical study of the distribution and synaptic handling of glutamate in rat hippocampus. Prog. Brain Res. 1990, 83:99-114.
    • (1990) Prog. Brain Res. , vol.83 , pp. 99-114
    • Ottersen, O.P.1    Storm-Mathisen, J.2    Bramham, C.3    Torp, R.4    Laake, J.5    Gundersen, V.6
  • 19
    • 0018656506 scopus 로고
    • Uptake of [3H]glutamic acid in excitatory nerve endings: light and electronmicroscopic observations in the hippocampal formation of the rat
    • Storm-Mathisen J., Iversen L.L. Uptake of [3H]glutamic acid in excitatory nerve endings: light and electronmicroscopic observations in the hippocampal formation of the rat. Neuroscience 1979, 4:1237-1253.
    • (1979) Neuroscience , vol.4 , pp. 1237-1253
    • Storm-Mathisen, J.1    Iversen, L.L.2
  • 20
    • 33745202578 scopus 로고    scopus 로고
    • Regulation of Ca2+ -permeable AMPA receptors: synaptic plasticity and beyond
    • Cull-Candy S., Kelly L., Farrant M. Regulation of Ca2+ -permeable AMPA receptors: synaptic plasticity and beyond. Curr. Opin. Neurobiol. 2006, 16:288-297.
    • (2006) Curr. Opin. Neurobiol. , vol.16 , pp. 288-297
    • Cull-Candy, S.1    Kelly, L.2    Farrant, M.3
  • 21
    • 33748948429 scopus 로고    scopus 로고
    • Role of AMPA receptors in synaptic plasticity
    • Sprengel R. Role of AMPA receptors in synaptic plasticity. Cell Tissue Res. 2006, 326:447-455.
    • (2006) Cell Tissue Res. , vol.326 , pp. 447-455
    • Sprengel, R.1
  • 22
    • 13544268511 scopus 로고    scopus 로고
    • N-methyl-d-aspartate receptor subtypes: multiple roles in excitotoxicity and neurological disease
    • Waxman E.A., Lynch D.R. N-methyl-d-aspartate receptor subtypes: multiple roles in excitotoxicity and neurological disease. Neuroscientist 2005, 11:37-49.
    • (2005) Neuroscientist , vol.11 , pp. 37-49
    • Waxman, E.A.1    Lynch, D.R.2
  • 23
    • 0025368726 scopus 로고
    • Channel kinetics determine the time course of NMDA receptor-mediated synaptic currents
    • Lester R.A., Clements J.D., Westbrook G.L., Jahr C.E. Channel kinetics determine the time course of NMDA receptor-mediated synaptic currents. Nature 1990, 346:565-567.
    • (1990) Nature , vol.346 , pp. 565-567
    • Lester, R.A.1    Clements, J.D.2    Westbrook, G.L.3    Jahr, C.E.4
  • 24
    • 33747627893 scopus 로고    scopus 로고
    • Molecular mechanism of neuronal plasticity: induction and maintenance of long-term potentiation in the hippocampus
    • Miyamoto E. Molecular mechanism of neuronal plasticity: induction and maintenance of long-term potentiation in the hippocampus. J. Pharmacol. Sci. 2006, 100:433-442.
    • (2006) J. Pharmacol. Sci. , vol.100 , pp. 433-442
    • Miyamoto, E.1
  • 25
  • 26
    • 0344861878 scopus 로고    scopus 로고
    • Mitochondrial genomes: anything goes
    • Burger G., Gray M.W., Lang B.F. Mitochondrial genomes: anything goes. Trends Genet. 2003, 19:709-716.
    • (2003) Trends Genet. , vol.19 , pp. 709-716
    • Burger, G.1    Gray, M.W.2    Lang, B.F.3
  • 27
    • 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. Production of reactive oxygen species in brain mitochondria: contribution by electron transport chain and non-electron transport chain sources. Antioxid. Redox Signal. 2005, 7:1140-1149.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 1140-1149
    • Adam-Vizi, V.1
  • 28
    • 0037029132 scopus 로고    scopus 로고
    • Souza-Pinto Mitochondrial DNA repair of oxidative damage in mammalian cells
    • Bohr V.A., Stevnsner T., de N.C., Souza-Pinto Mitochondrial DNA repair of oxidative damage in mammalian cells. Gene 2002, 286:127-134.
    • (2002) Gene , vol.286 , pp. 127-134
    • Bohr, V.A.1    Stevnsner, T.2    de, N.C.3
  • 29
  • 30
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • Hoeijmakers J.H. Genome maintenance mechanisms for preventing cancer. Nature 2001, 411:366-374.
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.1
  • 31
    • 0043197852 scopus 로고    scopus 로고
    • Intracellular antioxidants: from chemical to biochemical mechanisms
    • Chaudiere J., Ferrari-Iliou R. Intracellular antioxidants: from chemical to biochemical mechanisms. Food Chem. Toxicol. 1999, 37:949-962.
    • (1999) Food Chem. Toxicol. , vol.37 , pp. 949-962
    • Chaudiere, J.1    Ferrari-Iliou, R.2
  • 33
    • 0036323863 scopus 로고    scopus 로고
    • Role of superoxide dismutases in oxidative damage and neurodegenerative disorders
    • Maier C.M., Chan P.H. Role of superoxide dismutases in oxidative damage and neurodegenerative disorders. Neuroscientist 2002, 8:323-334.
    • (2002) Neuroscientist , vol.8 , pp. 323-334
    • Maier, C.M.1    Chan, P.H.2
  • 35
    • 0033230807 scopus 로고    scopus 로고
    • Tissue-specific functions of individual glutathione peroxidases
    • Brigelius-Flohe R. Tissue-specific functions of individual glutathione peroxidases. Free Radic. Biol. Med. 1999, 27:951-965.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 951-965
    • Brigelius-Flohe, R.1
  • 36
    • 64149085276 scopus 로고    scopus 로고
    • Catalase delivery for inhibiting ROS-mediated tissue injury and tumor metastasis
    • Nishikawa M., Hashida M., Takakura Y. Catalase delivery for inhibiting ROS-mediated tissue injury and tumor metastasis. Adv. Drug Deliv. Rev. 2009, 61:319-326.
    • (2009) Adv. Drug Deliv. Rev. , vol.61 , pp. 319-326
    • Nishikawa, M.1    Hashida, M.2    Takakura, Y.3
  • 37
    • 73849144014 scopus 로고    scopus 로고
    • Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling
    • Cox A.G., Winterbourn C.C., Hampton M.B. Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling. Biochem. J. 2010, 425:313-325.
    • (2010) Biochem. J. , vol.425 , pp. 313-325
    • Cox, A.G.1    Winterbourn, C.C.2    Hampton, M.B.3
  • 39
    • 38149041804 scopus 로고    scopus 로고
    • Immunogold quantification of amino acids and proteins in complex subcellular compartments
    • Bergersen L.H., Storm-Mathisen J., Gundersen V. Immunogold quantification of amino acids and proteins in complex subcellular compartments. Nat. Protoc. 2008, 3:144-152.
    • (2008) Nat. Protoc. , vol.3 , pp. 144-152
    • Bergersen, L.H.1    Storm-Mathisen, J.2    Gundersen, V.3
  • 41
    • 0028901020 scopus 로고
    • Action of mitochondrial DNA polymerase gamma at sites of base loss or oxidative damage
    • Pinz K.G., Shibutani S., Bogenhagen D.F. Action of mitochondrial DNA polymerase gamma at sites of base loss or oxidative damage. J. Biol. Chem. 1995, 270:9202-9206.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9202-9206
    • Pinz, K.G.1    Shibutani, S.2    Bogenhagen, D.F.3
  • 42
    • 0036566855 scopus 로고    scopus 로고
    • Modulation of mitochondrial transcription in response to mtDNA depletion and repletion in HeLa cells
    • Seidel-Rogol B.L., Shadel G.S. Modulation of mitochondrial transcription in response to mtDNA depletion and repletion in HeLa cells. Nucleic Acids Res. 2002, 30:1929-1934.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1929-1934
    • Seidel-Rogol, B.L.1    Shadel, G.S.2
  • 43
    • 70449678738 scopus 로고    scopus 로고
    • Molecular dissection of reactive astrogliosis and glial scar formation
    • Sofroniew M.V. Molecular dissection of reactive astrogliosis and glial scar formation. Trends Neurosci. 2009, 32:638-647.
    • (2009) Trends Neurosci. , vol.32 , pp. 638-647
    • Sofroniew, M.V.1
  • 47
    • 66149171367 scopus 로고    scopus 로고
    • Regulation of Mn-superoxide dismutase activity and neuroprotection by STAT3 in mice after cerebral ischemia
    • Jung J.E., Kim G.S., Narasimhan P., Song Y.S., Chan P.H. Regulation of Mn-superoxide dismutase activity and neuroprotection by STAT3 in mice after cerebral ischemia. J. Neurosci. 2009, 29:7003-7014.
    • (2009) J. Neurosci. , vol.29 , pp. 7003-7014
    • Jung, J.E.1    Kim, G.S.2    Narasimhan, P.3    Song, Y.S.4    Chan, P.H.5
  • 48
    • 0033987488 scopus 로고    scopus 로고
    • Cellular distribution of superoxide dismutases in the rat CNS
    • Lindenau J., Noack H., Possel H., Asayama K., Wolf G. Cellular distribution of superoxide dismutases in the rat CNS. Glia 2000, 29:25-34.
    • (2000) Glia , vol.29 , pp. 25-34
    • Lindenau, J.1    Noack, H.2    Possel, H.3    Asayama, K.4    Wolf, G.5
  • 49
    • 0021769722 scopus 로고
    • Hydroxylation of deoxyguanosine at the C-8 position by ascorbic acid and other reducing agents
    • Kasai H., Nishimura S. Hydroxylation of deoxyguanosine at the C-8 position by ascorbic acid and other reducing agents. Nucleic Acids Res. 1984, 12:2137-2145.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 2137-2145
    • Kasai, H.1    Nishimura, S.2
  • 50
    • 0031818527 scopus 로고    scopus 로고
    • Reduction of oxidation during the preparation of DNA and analysis of 8-hydroxy-2′-deoxyguanosine
    • Hofer T., Moller L. Reduction of oxidation during the preparation of DNA and analysis of 8-hydroxy-2′-deoxyguanosine. Chem. Res. Toxicol. 1998, 11:882-887.
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 882-887
    • Hofer, T.1    Moller, L.2
  • 52
    • 38549153790 scopus 로고    scopus 로고
    • Two distinct pathways of cell death triggered by oxidative damage to nuclear and mitochondrial DNAs
    • Oka S., Ohno M., Tsuchimoto D., Sakumi K., Furuichi M., Nakabeppu Y. Two distinct pathways of cell death triggered by oxidative damage to nuclear and mitochondrial DNAs. EMBO J. 2008, 27:421-432.
    • (2008) EMBO J. , vol.27 , pp. 421-432
    • Oka, S.1    Ohno, M.2    Tsuchimoto, D.3    Sakumi, K.4    Furuichi, M.5    Nakabeppu, Y.6
  • 53
    • 16844369889 scopus 로고    scopus 로고
    • Nuclear and mitochondrial DNA repair: similar pathways?
    • Larsen N.B., Rasmussen M., Rasmussen L.J. Nuclear and mitochondrial DNA repair: similar pathways?. Mitochondrion 2005, 5:89-108.
    • (2005) Mitochondrion , vol.5 , pp. 89-108
    • Larsen, N.B.1    Rasmussen, M.2    Rasmussen, L.J.3
  • 54
    • 62349120246 scopus 로고    scopus 로고
    • DNA repair in mammalian cells: base excision repair: the long and short of it
    • Robertson A.B., Klungland A., Rognes T., Leiros I. DNA repair in mammalian cells: base excision repair: the long and short of it. Cell Mol. Life Sci. 2009, 66:981-993.
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 981-993
    • Robertson, A.B.1    Klungland, A.2    Rognes, T.3    Leiros, I.4
  • 55
    • 24344436378 scopus 로고    scopus 로고
    • Effect of aging on intracellular distribution of abasic (AP) endonuclease 1 in the mouse liver
    • Szczesny B., Mitra S. Effect of aging on intracellular distribution of abasic (AP) endonuclease 1 in the mouse liver. Mech. Ageing Dev. 2005, 126:1071-1078.
    • (2005) Mech. Ageing Dev. , vol.126 , pp. 1071-1078
    • Szczesny, B.1    Mitra, S.2
  • 56
    • 48349107170 scopus 로고    scopus 로고
    • A new APE1/Ref-1-dependent pathway leading to reduction of NF-kappaB and AP-1, and activation of their DNA-binding activity
    • Ando K., Hirao S., Kabe Y., Ogura Y., Sato I., Yamaguchi Y., Wada T., Handa H. A new APE1/Ref-1-dependent pathway leading to reduction of NF-kappaB and AP-1, and activation of their DNA-binding activity. Nucleic Acids Res. 2008, 36:4327-4336.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4327-4336
    • Ando, K.1    Hirao, S.2    Kabe, Y.3    Ogura, Y.4    Sato, I.5    Yamaguchi, Y.6    Wada, T.7    Handa, H.8
  • 57
    • 51349134457 scopus 로고    scopus 로고
    • Role of the multifunctional DNA repair and redox signaling protein Ape1/Ref-1 in cancer and endothelial cells: small-molecule inhibition of the redox function of Ape1
    • Luo M., Delaplane S., Jiang A., Reed A., He Y., Fishel M., Nyland R.L., Borch R.F., Qiao X., Georgiadis M.M., Kelley M.R. Role of the multifunctional DNA repair and redox signaling protein Ape1/Ref-1 in cancer and endothelial cells: small-molecule inhibition of the redox function of Ape1. Antioxid. Redox Signal. 2008, 10:1853-1867.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1853-1867
    • Luo, M.1    Delaplane, S.2    Jiang, A.3    Reed, A.4    He, Y.5    Fishel, M.6    Nyland, R.L.7    Borch, R.F.8    Qiao, X.9    Georgiadis, M.M.10    Kelley, M.R.11
  • 58
    • 0028058086 scopus 로고
    • The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains
    • Xanthoudakis S., Miao G.G., Curran T. The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains. Proc. Natl. Acad. Sci. U. S. A. 1994, 91:23-27.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 23-27
    • Xanthoudakis, S.1    Miao, G.G.2    Curran, T.3
  • 59
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fission and fusion in Alzheimer's disease
    • Wang X., Su B., Lee H.G., Li X., Perry G., Smith M.A., Zhu X. Impaired balance of mitochondrial fission and fusion in Alzheimer's disease. J. Neurosci. 2009, 29:9090-9103.
    • (2009) J. Neurosci. , vol.29 , pp. 9090-9103
    • Wang, X.1    Su, B.2    Lee, H.G.3    Li, X.4    Perry, G.5    Smith, M.A.6    Zhu, X.7
  • 60
    • 76249119279 scopus 로고    scopus 로고
    • Molecular approaches to understanding neural network plasticity and memory: the Kavli Prize Inaugural Symposium on Neuroscience
    • Sander M., Bergersen L.H., Storm-Mathisen J. Molecular approaches to understanding neural network plasticity and memory: the Kavli Prize Inaugural Symposium on Neuroscience. Neuroscience 2009, 163:965-976.
    • (2009) Neuroscience , vol.163 , pp. 965-976
    • Sander, M.1    Bergersen, L.H.2    Storm-Mathisen, J.3
  • 61
    • 23244449495 scopus 로고    scopus 로고
    • Morphogenesis of the dentate gyrus: what we are learning from mouse mutants
    • Li G., Pleasure S.J. Morphogenesis of the dentate gyrus: what we are learning from mouse mutants. Dev. Neurosci. 2005, 27:93-99.
    • (2005) Dev. Neurosci. , vol.27 , pp. 93-99
    • Li, G.1    Pleasure, S.J.2
  • 62
    • 0034634351 scopus 로고    scopus 로고
    • NMDA receptor-dependent synaptic reinforcement as a crucial process for memory consolidation
    • Shimizu E., Tang Y.P., Rampon C., Tsien J.Z. NMDA receptor-dependent synaptic reinforcement as a crucial process for memory consolidation. Science 2000, 290:1170-1174.
    • (2000) Science , vol.290 , pp. 1170-1174
    • Shimizu, E.1    Tang, Y.P.2    Rampon, C.3    Tsien, J.Z.4
  • 65
    • 0038305219 scopus 로고    scopus 로고
    • Synaptic transmission and plasticity in the absence of AMPA glutamate receptor GluR2 and GluR3
    • Meng Y., Zhang Y., Jia Z. Synaptic transmission and plasticity in the absence of AMPA glutamate receptor GluR2 and GluR3. Neuron 2003, 39:163-176.
    • (2003) Neuron , vol.39 , pp. 163-176
    • Meng, Y.1    Zhang, Y.2    Jia, Z.3
  • 66
    • 20344382273 scopus 로고    scopus 로고
    • Oxidative DNA damage causes mitochondrial genomic instability in Saccharomyces cerevisiae
    • Doudican N.A., Song B., Shadel G.S., Doetsch P.W. Oxidative DNA damage causes mitochondrial genomic instability in Saccharomyces cerevisiae. Mol. Cell Biol. 2005, 25:5196-5204.
    • (2005) Mol. Cell Biol. , vol.25 , pp. 5196-5204
    • Doudican, N.A.1    Song, B.2    Shadel, G.S.3    Doetsch, P.W.4
  • 67
    • 4544259868 scopus 로고    scopus 로고
    • Transcription - guarding the genome by sensing DNA damage
    • Ljungman M., Lane D.P. Transcription - guarding the genome by sensing DNA damage. Nat. Rev. Cancer 2004, 4:727-737.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 727-737
    • Ljungman, M.1    Lane, D.P.2
  • 68
    • 62349116477 scopus 로고    scopus 로고
    • The mitochondrial theory of aging: insight from transgenic and knockout mouse models
    • Jang Y.C., Remmen V.H. The mitochondrial theory of aging: insight from transgenic and knockout mouse models. Exp. Gerontol. 2009, 44:256-260.
    • (2009) Exp. Gerontol. , vol.44 , pp. 256-260
    • Jang, Y.C.1    Remmen, V.H.2
  • 70
    • 69449096141 scopus 로고    scopus 로고
    • Overexpression of SOD-2 reduces hippocampal superoxide and prevents memory deficits in a mouse model of Alzheimer's disease
    • Massaad C.A., Washington T.M., Pautler R.G., Klann E. Overexpression of SOD-2 reduces hippocampal superoxide and prevents memory deficits in a mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:13576-13581.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 13576-13581
    • Massaad, C.A.1    Washington, T.M.2    Pautler, R.G.3    Klann, E.4
  • 71
    • 34248171278 scopus 로고    scopus 로고
    • Mutant SOD1-induced neuronal toxicity is mediated by increased mitochondrial superoxide levels
    • Zimmerman M.C., Oberley L.W., Flanagan S.W. Mutant SOD1-induced neuronal toxicity is mediated by increased mitochondrial superoxide levels. J. Neurochem. 2007, 102:609-618.
    • (2007) J. Neurochem. , vol.102 , pp. 609-618
    • Zimmerman, M.C.1    Oberley, L.W.2    Flanagan, S.W.3
  • 72
    • 0000740359 scopus 로고    scopus 로고
    • The activation of the rat copper/zinc superoxide dismutase gene by hydrogen peroxide through the hydrogen peroxide-responsive element and by paraquat and heat shock through the same heat shock element
    • Yoo H.Y., Chang M.S., Rho H.M. The activation of the rat copper/zinc superoxide dismutase gene by hydrogen peroxide through the hydrogen peroxide-responsive element and by paraquat and heat shock through the same heat shock element. J. Biol. Chem. 1999, 274:23887-23892.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23887-23892
    • Yoo, H.Y.1    Chang, M.S.2    Rho, H.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.