메뉴 건너뛰기




Volumn 62, Issue , 2013, Pages 4-12

SOD2 in mitochondrial dysfunction and neurodegeneration

Author keywords

Aging; Free radicals; Mitochondria; Neurodegeneration; Oxidative stress; Superoxide dismutase

Indexed keywords

1,2,3,6 TETRAHYDRO 1 METHYL 4 PHENYLPYRIDINE; AMYLOID BETA PROTEIN; GELATINASE B; HYDROGEN PEROXIDE; IDEBENONE; MANGANESE SUPEROXIDE DISMUTASE; NUCLEIC ACID; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR FOXO; UBIDECARENONE;

EID: 84884908350     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2013.05.027     Document Type: Review
Times cited : (270)

References (135)
  • 1
    • 0015319592 scopus 로고
    • The biologic clock: The mitochondria?
    • Harman, D. The biologic clock: the mitochondria? J. Am. Geriatr. Soc 20: 145-147; 1972.
    • (1972) J. Am. Geriatr. Soc , vol.20 , pp. 145-147
    • Harman, D.1
  • 3
    • 84655164280 scopus 로고    scopus 로고
    • The role of metallo-biology and amyloid-ß peptides in Alzheimer's disease
    • Roberts, BR; Ryan, TM; Bush, AI; Masters, CL; Duce, JA. The role of metallo-biology and amyloid-ß peptides in Alzheimer's disease. J. Neurochem 120: 149-166; 2011.
    • (2011) J. Neurochem , vol.120 , pp. 149-166
    • Roberts, B.R.1    Ryan, T.M.2    Bush, A.I.3    Masters, C.L.4    Duce, J.A.5
  • 5
    • 84875697145 scopus 로고    scopus 로고
    • Metal dyshomeostasis and oxidative stress in Alzheimer's disease
    • Greenough, MA; Camakaris, J; Bush, AI. Metal dyshomeostasis and oxidative stress in Alzheimer's disease. Neurochem. Int 62: 540-555; 2013.
    • (2013) Neurochem. Int , vol.62 , pp. 540-555
    • Greenough, M.A.1    Camakaris, J.2    Bush, A.I.3
  • 6
    • 84877999402 scopus 로고    scopus 로고
    • The metal theory of alzheimer's disease
    • Bush, AI. The metal theory of Alzheimer's disease. J. Alzheimers Dis 33(Suppl. 1): S277-281; 2013.
    • (2013) J. Alzheimers Dis , vol.33 , Issue.SUPPL. 1
    • Bush, A.I.1
  • 7
    • 3142514196 scopus 로고    scopus 로고
    • Oxidative stress in neurodegeneration: Cause or consequence?
    • Andersen, JK. Oxidative stress in neurodegeneration: cause or consequence? Nat. Med 10(Suppl):S18-25; 2004. (Pubitemid 38901863)
    • (2004) Nature Medicine , vol.10 , Issue.SUPPL.
    • Andersen, J.K.1
  • 8
    • 0021745377 scopus 로고
    • Extracellular superoxide dismutase in human tissues and human cell lines
    • Marklund, SL. Extracellular superoxide dismutase in human tissues and human cell lines. J. Clin. Invest 74 : 1398-1403; 1984. (Pubitemid 15206836)
    • (1984) Journal of Clinical Investigation , vol.74 , Issue.4 , pp. 1398-1403
    • Marklund, S.L.1
  • 9
    • 0028805056 scopus 로고
    • The interstitium of the human arterial wall contains very large amounts of extracellular superoxide dismutase
    • Strålin, P; Karlsson, K; Johansson, BO; Marklund, SL. The interstitium of the human arterial wall contains very large amounts of extracellular superoxide dismutase. Arterioscler. Thromb. Vasc. Biol 15: 2032-2036; 1995.
    • (1995) Arterioscler. Thromb. Vasc. Biol , vol.15 , pp. 2032-2036
    • Strålin, P.1    Karlsson, K.2    Johansson, B.O.3    Marklund, S.L.4
  • 10
    • 0034201168 scopus 로고    scopus 로고
    • Regulation of the vascular extracellular superoxide dismutase by nitric oxide and exercise training
    • Fukai, T; Siegfried, MR; Ushio-Fukai, M; Cheng, Y; Kojda, G; Harrison, DG. Regulation of the vascular extracellular superoxide dismutase by nitric oxide and exercise training. J. Clin. Invest 105: 1631-1639; 2000.
    • (2000) J. Clin. Invest , vol.105 , pp. 1631-1639
    • Fukai, T.1    Siegfried, M.R.2    Ushio-Fukai, M.3    Cheng, Y.4    Kojda, G.5    Harrison, D.G.6
  • 11
    • 0142012094 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase in biology and medicine
    • DOI 10.1016/S0891-5849(03)00275-2
    • Fattman, CL; Schaefer, LM; Oury, TD. Extracellular superoxide dismutase in biology and medicine. Free Radic. Biol. Med. 35: 236-256; 2003. (Pubitemid 37288924)
    • (2003) Free Radical Biology and Medicine , vol.35 , Issue.3 , pp. 236-256
    • Fattman, C.L.1    Schaefer, L.M.2    Oury, T.D.3
  • 12
    • 79961193678 scopus 로고    scopus 로고
    • Superoxide dismutases: Role in redox signaling, vascular function, and diseases
    • Fukai, T; Ushio-Fukai, M. Superoxide dismutases: role in redox signaling, vascular function, and diseases. Antioxid. Redox Signaling 15: 1583-1606; 2011.
    • (2011) Antioxid. Redox Signaling , vol.15 , pp. 1583-1606
    • Fukai, T.1    Ushio-Fukai, M.2
  • 13
    • 0035149749 scopus 로고    scopus 로고
    • Reactive oxygen radicals in signaling and damage in the ischemic brain
    • Chan, PH. Reactive oxygen radicals in signaling and damage in the ischemic brain. J. Cereb. Blood Flow Metab 21: 2-14; 20 01.
    • (2001) J. Cereb. Blood Flow Metab , vol.21 , pp. 20-14
    • Chan, P.H.1
  • 14
    • 0026476480 scopus 로고
    • Copper chang ly. Zinc superoxide dismutase is primarily a cytosolic protein in human cells
    • Crapo, JD; Oury, T; Rabouille, C; Slot, JW; Copper, Chang LY. zinc superoxide dismutase is primarily a cytosolic protein in human cells. Proc. Natl. Acad. Sci. USA 89: 10405-10409; 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10405-10409
    • Crapo, J.D.1    Oury, T.2    Rabouille, C.3    Slot, J.W.4
  • 15
    • 0035851122 scopus 로고    scopus 로고
    • A fraction of yeast Cu, Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria: A physiological role for SOD1 in guarding against mitochondrial oxidative damage
    • Sturtz, LA; Diekert, K; Jensen, LT; Lill, R; Culotta, VC. A fraction of yeast Cu, Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria: a physiological role for SOD1 in guarding against mitochondrial oxidative damage. J. Biol. Chem 276: 38084-38089; 2001.
    • (2001) J. Biol. Chem , vol.276 , pp. 38084-38089
    • Sturtz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Culotta, V.C.5
  • 16
    • 14944385595 scopus 로고    scopus 로고
    • Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice
    • DOI 10.1523/JNEUROSCI.4385-04.2005
    • Vijayvergiya, C; Beal, MF; Buck, J; Manfredi, G. Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice. J. Neurosci 25: 2463-2470; 2005. (Pubitemid 40365156)
    • (2005) Journal of Neuroscience , vol.25 , Issue.10 , pp. 2463-2470
    • Vijayvergiya, C.1    Beal, M.F.2    Buck, J.3    Manfredi, G.4
  • 17
    • 54449092952 scopus 로고    scopus 로고
    • Different regulation of wild-type and mutant cu zn superoxide dismutase localization in mammalian mitochondria
    • Kawamata, H; Manfredi, G. Different regulation of wild-type and mutant Cu, Zn superoxide dismutase localization in mammalian mitochondria. Hum. Mol. Genet 17: 3303-3317; 2008.
    • (2008) Hum. Mol. Genet , vol.17 , pp. 3303-3317
    • Kawamata, H.1    Manfredi, G.2
  • 18
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
    • Okado-Matsumoto, A; Fridovich, I. Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria. J. Biol. Chem 276: 38388-38393; 2001.
    • (2001) J. Biol. Chem , vol.276 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 19
    • 84857055792 scopus 로고    scopus 로고
    • Mitochondria in motor nerve terminals: Function in health and in mutant superoxide dismutase 1 mouse models of familial ALS
    • Barrett, EF; Barrett, JN; David, G. Mitochondria in motor nerve terminals: function in health and in mutant superoxide dismutase 1 mouse models of familial ALS. J. Bioenerg. Biomembr 43: 581-586; 2011.
    • (2011) J. Bioenerg. Biomembr , vol.43 , pp. 581-586
    • Barrett, E.F.1    Barrett, J.N.2    David, G.3
  • 20
    • 84857063826 scopus 로고    scopus 로고
    • SOD1 and mitochondria in ALS: A dangerous liaison
    • Carrì, MT; Cozzolino, M. SOD1 and mitochondria in ALS: a dangerous liaison. J. Bioenerg. Biomembr. 43: 593-599; 2011.
    • (2011) J. Bioenerg. Biomembr , vol.43 , pp. 593-599
    • Carrì, M.T.1    Cozzolino, M.2
  • 22
    • 0015694842 scopus 로고
    • Mitochondrial superoxide dismutase
    • Weisiger, RA; Fridovich, I. Mitochondrial superoxide dismutase. J. Biol. Chem. 248: 4793-4796; 1973.
    • (1973) J. Biol. Chem , vol.248 , pp. 4793-4796
    • Weisiger, R.A.1    Fridovich, I.2
  • 23
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, MP. How mitochondria produce reactive oxygen species. Biochem. J. 417: 1; 2009.
    • (2009) Biochem. J. , vol.417 , pp. 1
    • Murphy, M.P.1
  • 24
    • 0032053161 scopus 로고    scopus 로고
    • Oxygen toxicity: A radical explanation
    • Fridovich, I. Oxygen toxicity: a radical explanation. J. Exp. Biol. 201: 1203-1209; 1998. (Pubitemid 28278324)
    • (1998) Journal of Experimental Biology , vol.201 , Issue.8 , pp. 1203-1209
    • Fridovich, I.1
  • 25
    • 0025981361 scopus 로고
    • Protein lipid and dna repair systems in oxidative stress: The free-radical theory of aging revisited
    • Pacifici, RE; Davies, KJ. Protein, lipid and DNA repair systems in oxidative stress: the free-radical theory of aging revisited. Gerontology 37: 166-180; 1991.
    • (1991) Gerontology , vol.37 , pp. 166-180
    • Pacifici, R.E.1    Davies, K.J.2
  • 26
    • 0025942074 scopus 로고
    • Age-related elevation of lipid peroxidation products: Diminution of superoxide dismutase activity in the central nervous system of rats
    • Gupta, A; Hasan, M; Chander, R; Kapoor, NK. Age-related elevation of lipid peroxidation products: diminution of superoxide dismutase activity in the central nervous system of rats. Gerontology 37: 305-309; 1991.
    • (1991) Gerontology , vol.37 , pp. 305-309
    • Gupta, A.1    Hasan, M.2    Chander, R.3    Kapoor, N.K.4
  • 27
    • 84855352363 scopus 로고    scopus 로고
    • Death by protein damage in irradiated cells
    • Daly, MJ. Death by protein damage in irradiated cells. DNA Repair 11 : 12-21; 2012.
    • (2012) DNA Repair , vol.11 , pp. 12-21
    • Daly, M.J.1
  • 28
    • 78650142376 scopus 로고    scopus 로고
    • Protein oxidative modifications in the ageing brain: Consequence for the onset of neurodegenerative disease
    • Grimm, S; Hoehn, A; Davies, KJ; Grune, T. Protein oxidative modifications in the ageing brain: consequence for the onset of neurodegenerative disease. Free Radic. Res 45: 73-88; 2011.
    • (2011) Free Radic. Res , vol.45 , pp. 73-88
    • Grimm, S.1    Hoehn, A.2    Davies, K.J.3    Grune, T.4
  • 29
    • 0041669528 scopus 로고    scopus 로고
    • The proteasomal system and HNE-modified proteins
    • DOI 10.1016/S0098-2997(03)00014-1
    • Grune, T; Davies, KJA. The proteasomal system and HNE-modified proteins. Mol. Aspects Med 24: 195-204; 2003. (Pubitemid 36945019)
    • (2003) Molecular Aspects of Medicine , vol.24 , Issue.4-5 , pp. 195-204
    • Grune, T.1    Davies, K.J.A.2
  • 31
    • 0021271971 scopus 로고
    • Clinical diagnosis of alzheimer's disease
    • Report Of The NINCDS-ADRDA Work Group Under The Auspices Of Department of Health and Human Services Task Force on Alzheimer's Disease
    • McKhann, G; Drachman, D; Folstein, M; Katzman, R; Price, D; Stadlan, EM. Clinical diagnosis of Alzheimer's disease: report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease. Neurology 34: 939-944; 1984.
    • (1984) Neurology , vol.34 , pp. 939-944
    • McKhann, G.1    Drachman, D.2    Folstein, M.3    Katzman, R.4    Price, D.5    Stadlan, E.M.6
  • 32
  • 35
    • 0036591849 scopus 로고    scopus 로고
    • Lipid peroxidation and protein oxidation in Alzheimer's disease brain: Potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress
    • DOI 10.1016/S0891-5849(02)00794-3, PII S0891584902007943
    • Butterfield, DA; Lauderback, CM. Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid ß-peptide-associated free radical oxidative stress. Free Radic. Biol. Med 32: 1050-1060; 2002. (Pubitemid 34603342)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.11 , pp. 1050-1060
    • Butterfield D.Allan1    Lauderback, C.M.2
  • 36
    • 33947644871 scopus 로고    scopus 로고
    • Protein oxidation and lipid peroxidation in brain of subjects with Alzheimer's disease: Insights into mechanism of neurodegeneration from redox proteomics
    • Sultana, R; Perluigi, M; Butterfield, DA. Protein oxidation and lipid peroxida-tion in brain of subjects with Alzheimer's disease: insights into mechanism of neurodegeneration from redox proteomics. Antioxid. Redox Signaling 8: 2021-2037; 2006. (Pubitemid 46499264)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.11-12 , pp. 2021-2037
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 38
    • 77953257870 scopus 로고    scopus 로고
    • Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease
    • Butterfield DA, Bader Lange ML, Sultana R. Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 2010, 1801: 924-929.
    • (2010) Biochim. Biophys. Acta Mol. Cell Biol. Lipids , vol.1801 , pp. 924-929
    • Butterfield, D.A.1    Bader Lange, M.L.2    Sultana, R.3
  • 40
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • DOI 10.1038/nature05292, PII NATURE05292
    • Lin, MT; Beal, MF. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443: 787-795; 2006. (Pubitemid 44622683)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 41
    • 84859709003 scopus 로고    scopus 로고
    • Mitochondria-specific accumulation of amyloid ß induces mitochondrial dysfunction leading to apoptotic cell death
    • Cha, M-Y; Han, S-H; Son, SM; Hong, H-S; Choi, Y-J; Byun, J; Mook-Jung, I. Mitochondria-specific accumulation of amyloid ß induces mitochondrial dysfunction leading to apoptotic cell death. PLoS One 7:e34929; 2012.
    • (2012) PLoS One , vol.7
    • Cha, M.-Y.1    Han, S.-H.2    Son, S.M.3    Hong, H.-S.4    Choi, Y.-J.5    Byun, J.6    Mook-Jung, I.7
  • 42
    • 0036272650 scopus 로고    scopus 로고
    • Beta-Amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • DOI 10.1046/j.0022-3042.2001.00681.x
    • Casley, CS; Canevari, L; Land, JM; Clark, JB; Sharpe, MA. Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities. J. Neurochem 80: 91-100; 2002. (Pubitemid 34614581)
    • (2002) Journal of Neurochemistry , vol.80 , Issue.1 , pp. 91-100
    • Casley, C.S.1    Canevari, L.2    Land, J.M.3    Clark, J.B.4    Sharpe, M.A.5
  • 44
    • 77953507107 scopus 로고    scopus 로고
    • Mitochondrial, DNA mutations in disease and aging
    • Wallace, DC.; Mitochondrial, DNA mutations in disease and aging. Environ. Mol. Mutagen. 51: 440-450; 2010.
    • (2010) Environ. Mol. Mutagen , vol.51 , pp. 440-450
    • Wallace, D.C.1
  • 45
    • 84870035165 scopus 로고    scopus 로고
    • No consistent bioenergetic defects in presynaptic nerve terminals isolated from mouse models of alzheimer's disease
    • Choi, SW; Gerencser, AA; Ng, R; Flynn, JM; Melov, S; Danielson, SR, et al. No consistent bioenergetic defects in presynaptic nerve terminals isolated from mouse models of Alzheimer's disease. J. Neurosci 32: 16775-16784; 2012.
    • (2012) J. Neurosci , vol.32 , pp. 16775-16784
    • Choi, S.W.1    Gerencser, A.A.2    Ng, R.3    Flynn, J.M.4    Melov, S.5    Danielson, S.R.6
  • 48
    • 33646922865 scopus 로고    scopus 로고
    • Reduction in mitochondrial superoxide dismutase modulates Alzheimer's disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice
    • DOI 10.1523/JNEUROSCI.0482-06.2006
    • Esposito, L; Raber, J; Kekonius, L; Yan, F; Yu, GQ; Bien-Ly, N, et al. Reduction in mitochondrial superoxide dismutase modulates Alzheimer's disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice. J. Neurosci 26: 5167-5179; 2006. (Pubitemid 44315298)
    • (2006) Journal of Neuroscience , vol.26 , Issue.19 , pp. 5167-5179
    • Esposito, L.1    Raber, J.2    Kekonius, L.3    Yan, F.4    Yu, G.-Q.5    Bien-Ly, N.6    Puolivali, J.7    Scearce-Levie, K.8    Masliah, E.9    Mucke, L.10
  • 49
    • 79955764600 scopus 로고    scopus 로고
    • Amyloid-induced impairments in hippocampal synaptic plasticity are rescued by decreasing mitochondrial superoxide
    • Ma, T; Hoeffer, CA; Wong, H; Massaad, CA; Zhou, P; Iadecola, C, et al. Amyloid-induced impairments in hippocampal synaptic plasticity are rescued by decreasing mitochondrial superoxide. J. Neurosci 31: 5589-5595; 2011.
    • (2011) J. Neurosci , vol.31 , pp. 5589-5595
    • Ma, T.1    Hoeffer, C.A.2    Wong, H.3    Massaad, C.A.4    Zhou, P.5    Iadecola, C.6
  • 50
    • 84872729641 scopus 로고    scopus 로고
    • Parkinson's disease and parkinsonism: Neuropathology
    • Dickson, DW. Parkinson's disease and parkinsonism: neuropathology. Cold Spring Harbor Perspect. Med 2:a009258; 2012, http://dx.doi.org/10.1101/ cshperspect.a009258.
    • (2012) Cold spring harbor perspect Med , vol.2
    • Dickson, D.W.1
  • 52
    • 84875277277 scopus 로고    scopus 로고
    • Monogenic parkinson's disease and parkinsonism: Clinical phenotypes and frequencies of known mutations
    • Puschmann, A. Monogenic Parkinson's disease and parkinsonism: clinical phenotypes and frequencies of known mutations. Parkinsonism Relat. Disord 19: 407-415; 2013.
    • (2013) Parkinsonism Relat. Disord , vol.19 , pp. 407-415
    • Puschmann, A.1
  • 57
    • 0031578774 scopus 로고    scopus 로고
    • Increased mitochondrial superoxide dismutase activity in Parkinson's disease but not amyotrophic lateral sclerosis motor cortex
    • DOI 10.1016/S0304-3940(97)00905-1, PII S0304394097009051
    • Radunovic, A; Porto, WG; Zeman, S; Leigh, PN. Increased mitochondrial superoxide dismutase activity in Parkinson's disease but not amyotrophic lateral sclerosis motor cortex. Neurosci. Lett 239: 105-108; 1997. (Pubitemid 28060211)
    • (1997) Neuroscience Letters , vol.239 , Issue.2-3 , pp. 105-108
    • Radunovic, A.1    Porto, W.G.2    Zeman, S.3    Leigh, P.N.4
  • 58
    • 33947205041 scopus 로고    scopus 로고
    • Abnormal levels of prohibitin and ATP synthase in the substantia nigra and frontal cortex in Parkinson's disease
    • DOI 10.1016/j.neulet.2007.01.026, PII S0304394007000547
    • Ferrer, I; Perez, E; Dalfo, E; Barrachina, M. Abnormal levels of prohibitin and ATP synthase in the substantia nigra and frontal cortex in Parkinson's disease. Neurosci. Lett 415: 205-209; 2007. (Pubitemid 46420396)
    • (2007) Neuroscience Letters , vol.415 , Issue.3 , pp. 205-209
    • Ferrer, I.1    Perez, E.2    Dalfo, E.3    Barrachina, M.4
  • 59
    • 0032748301 scopus 로고    scopus 로고
    • Hydroxyl radical and superoxide dismutase in blood of patients with Parkinson's disease: Relationship to clinical data
    • DOI 10.1016/S0022-510X(99)00192-6, PII S0022510X99001926
    • Ihara, Y; Chuda, M; Kuroda, S; Hayabara, T. Hydroxyl radical and superoxide dismutase in blood of patients with Parkinson's disease: relationship to clinical data. J. Neurol. Sci 170: 90-95; 1999. (Pubitemid 29528530)
    • (1999) Journal of the Neurological Sciences , vol.170 , Issue.2 , pp. 90-95
    • Ihara, Y.1    Chuda, D.2    Kuroda, S.3    Hayabara, T.4
  • 60
    • 0023766185 scopus 로고
    • Oxygen toxicity protecting enzymes in Parkinson's disease: Increase of superoxide dismutase-like activity in the substantia nigra and basal nucleus
    • Marttila, RJ; Lorentz, H; Rinne, UK. Oxygen toxicity protecting enzymes in Parkinson's disease: increase of superoxide dismutase-like activity in the substantia nigra and basal nucleus. J. Neurol. Sci 86: 321-331; 1988.
    • (1988) J. Neurol. Sci , vol.86 , pp. 321-331
    • Marttila, R.J.1    Lorentz, H.2    Rinne, U.K.3
  • 61
    • 81255149611 scopus 로고    scopus 로고
    • The role of calcium and mitochondrial oxidant stress in the loss of substantia nigra pars compacta dopaminergic neurons in parkinson's disease
    • Surmeier, DJ; Guzman, JN; Sanchez-Padilla, J; Schumacker, PT. The role of calcium and mitochondrial oxidant stress in the loss of substantia nigra pars compacta dopaminergic neurons in Parkinson's disease. Neuroscience 198: 221-231; 2011.
    • (2011) Neuroscience , vol.198 , pp. 221-231
    • Surmeier, D.J.1    Guzman, J.N.2    Sanchez-Padilla, J.3    Schumacker, P.T.4
  • 63
    • 79961207643 scopus 로고    scopus 로고
    • Evaluation of markers of oxidative stress, antioxidant function and astrocytic proliferation in the striatum and frontal cortex of Parkinson's disease brains
    • Mythri, RB; Venkateshappa, C; Harish, G; Mahadevan, A; Muthane, UB; Yasha, TC, et al. Evaluation of markers of oxidative stress, antioxidant function and astrocytic proliferation in the striatum and frontal cortex of Parkinson's disease brains. Neurochem. Res 36: 1452-1463; 2011.
    • (2011) Neurochem. Res , vol.36 , pp. 1452-1463
    • Mythri, R.B.1    Venkateshappa, C.2    Harish, G.3    Mahadevan, A.4    Muthane, U.B.5    Yasha, T.C.6
  • 64
    • 67649329442 scopus 로고    scopus 로고
    • Oxidative stress and Parkinson's disease
    • Vinken, P. J., Bruyn, G. W., editors. Amsterdam: Elsevier;
    • Jenner, P. Oxidative stress and Parkinson's disease. In: Vinken, P. J., Bruyn, G. W., editors. Handbook of Clinical Neurology, Vol. 83. Amsterdam: Elsevier; 2007. p. 507-520.
    • (2007) Handbook of Clinical Neurology , vol.83 , pp. 507-520
    • Jenner, P.1
  • 65
    • 0035706410 scopus 로고    scopus 로고
    • Neurotoxicity of MPTP
    • DOI 10.1046/j.1440-1789.2001.00402.x
    • Fukuda, T. Neurotoxicity of MPTP. Neuropathology 21: 323-332; 2001. (Pubitemid 34130640)
    • (2001) Neuropathology , vol.21 , Issue.4 , pp. 323-332
    • Fukuda, T.1
  • 66
    • 0027504297 scopus 로고
    • Advances in our understanding of the mechanisms of the neurotoxicity of MPTP and related compounds
    • Tipton, KF; Singer, TP. Advances in our understanding of the mechanisms of the neurotoxicity of MPTP and related compounds. J. Neurochem 61: 1191-1206; 1993. (Pubitemid 23285075)
    • (1993) Journal of Neurochemistry , vol.61 , Issue.4 , pp. 1191-1206
    • Tipton, K.F.1    Singer, T.P.2
  • 68
    • 84864150600 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Parkinson's disease: Molecular mechanisms and pathophysiological consequences
    • Exner, N; Lutz, AK; Haass, C; Winklhofer, KF. Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences. EMBO J. 31: 3038-3062; 2012.
    • (2012) EMBO J. , vol.31 , pp. 3038-3062
    • Exner, N.1    Lutz, A.K.2    Haass, C.3    Winklhofer, K.F.4
  • 69
    • 76049085234 scopus 로고    scopus 로고
    • Mitochondrial superoxide dismutase SOD2, but not cytosolic SOD1, plays a critical role in protection against glutamate-induced oxidative stress and cell death in HT22 neuronal cells
    • Fukui, M; Zhu, BT. Mitochondrial superoxide dismutase SOD2, but not cytosolic SOD1, plays a critical role in protection against glutamate-induced oxidative stress and cell death in HT22 neuronal cells. Free Radic. Biol. Med 48: 821-830; 2010.
    • (2010) Free Radic. Biol. Med , vol.48 , pp. 821-830
    • Fukui, M.1    Zhu, B.T.2
  • 70
    • 3042654997 scopus 로고    scopus 로고
    • Does cellular iron dysregulation play a causative role in Parkinson's disease?
    • DOI 10.1016/j.arr.2004.01.003, PII S1568163704000145
    • Kaur, D; Andersen, J. Does cellular iron dysregulation play a causative role in Parkinson's disease? Ageing Res Rev 3: 327-343; 2004. (Pubitemid 38844698)
    • (2004) Ageing Research Reviews , vol.3 , Issue.3 , pp. 327-343
    • Kaur, D.1    Andersen, J.2
  • 71
    • 34250334136 scopus 로고    scopus 로고
    • Absence of dopaminergic neuronal degeneration and oxidative damage in aged DJ-1-deficient mice
    • Yamaguchi, H; Shen, J. Absence of dopaminergic neuronal degeneration and oxidative damage in aged DJ-1-deficient mice. Mol. Neurodegener 2: 10; 2007.
    • (2007) Mol. Neurodegener , vol.2 , pp. 10
    • Yamaguchi, H.1    Shen, J.2
  • 73
    • 84864095875 scopus 로고    scopus 로고
    • DJ-1 protein protects dopaminergic neurons against 6-OHDA/mg-132-induced neurotoxicity in rats
    • Sun, SY; An, CN; Pu, XP. DJ-1 protein protects dopaminergic neurons against 6-OHDA/mg-132-induced neurotoxicity in rats. Brain Res. Bull 88: 609-616; 2012.
    • (2012) Brain Res. Bull , vol.88 , pp. 609-616
    • Sun, S.Y.1    An, C.N.2    Pu, X.P.3
  • 74
    • 84859759299 scopus 로고    scopus 로고
    • Silent information regulator 2 (sir2) and forkhead box O (FOXO) complement mitochondrial dysfunction and dopaminergic neuron loss in Drosophila pten-induced kinase 1 (PINK1) null mutant
    • Koh, H; Kim, H; Kim, MJ; Park, J; Lee, HJ; Chung, J. Silent information regulator 2 (sir2) and forkhead box O (FOXO) complement mitochondrial dysfunction and dopaminergic neuron loss in Drosophila pten-induced kinase 1 (PINK1) null mutant. J. Biol. Chem 287: 12750-12758; 2012.
    • (2012) J. Biol. Chem , vol.287 , pp. 12750-12758
    • Koh, H.1    Kim, H.2    Kim, M.J.3    Park, J.4    Lee, H.J.5    Chung, J.6
  • 75
    • 77955487488 scopus 로고    scopus 로고
    • The science of stroke: Mechanisms in search of treatments
    • Moskowitz, MA; Lo, EH; Iadecola, C. The science of stroke: mechanisms in search of treatments. Neuron 67: 181-198; 2010.
    • (2010) Neuron , vol.67 , pp. 181-198
    • Moskowitz, M.A.1    Lo, E.H.2    Iadecola, C.3
  • 76
    • 27544474355 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain and free radical generation in stroke
    • DOI 10.1016/j.freeradbiomed.2005.07.010, PII S0891584905003977
    • Moro, MA; Almeida, A; Bolaños, JP; Lizasoain, I. Mitochondrial respiratory chain and free radical generation in stroke. Free Radic. Biol. Med 39: 1291-1304; 2005. (Pubitemid 41540085)
    • (2005) Free Radical Biology and Medicine , vol.39 , Issue.10 , pp. 1291-1304
    • Moro, M.A.1    Almeida, A.2    Bolanos, J.P.3    Lizasoain, I.4
  • 77
    • 3342967838 scopus 로고    scopus 로고
    • Metabolic stages, mitochondria and calcium in hypoxic/ischemic brain damage
    • DOI 10.1016/j.ceca.2004.02.016, PII S0143416004000600
    • Kristián, T. Metabolic stages, mitochondria and calcium in hypoxic/ischemic brain damage. Cell Calcium 36: 221-233; 2004. (Pubitemid 38992349)
    • (2004) Cell Calcium , vol.36 , Issue.3-4 , pp. 221-233
    • Kristian, T.1
  • 79
    • 22544462551 scopus 로고    scopus 로고
    • Antioxidant strategies in the treatment of stroke
    • DOI 10.1016/j.freeradbiomed.2005.05.003, PII S0891584905002662
    • Margaill, I; Plotkine, M; Lerouet, D. Antioxidant strategies in the treatment of stroke. Free Radic. Biol. Med. 39: 429-443; 2005. (Pubitemid 41021642)
    • (2005) Free Radical Biology and Medicine , vol.39 , Issue.4 , pp. 429-443
    • Margaill, I.1    Plotkine, M.2    Lerouet, D.3
  • 80
    • 79952850719 scopus 로고    scopus 로고
    • Oxidative stress in ischemic brain damage: Mechanisms of cell death and potential molecular targets for neuroprotection
    • Chen, H; Yoshioka, H; Kim, GS; Jung, JE; Okami, N; Sakata, H, et al. Oxidative stress in ischemic brain damage: mechanisms of cell death and potential molecular targets for neuroprotection. Antioxid. Redox Signaling 14: 1505-1517; 2011.
    • (2011) Antioxid. Redox Signaling , vol.14 , pp. 1505-1517
    • Chen, H.1    Yoshioka, H.2    Kim, G.S.3    Jung, J.E.4    Okami, N.5    Sakata, H.6
  • 81
    • 38149001645 scopus 로고    scopus 로고
    • Oxidative stress and matrix metalloproteinase-9 in acute ischemic stroke: The biomarker evaluation for antioxidant therapies in stroke (beat-stroke) study
    • Kelly, PJ; Morrow, JD; Ning, M; Koroshetz, W; Lo, EH; Terry, E, et al. Oxidative stress and matrix metalloproteinase-9 in acute ischemic stroke: the Biomarker Evaluation for Antioxidant Therapies in Stroke (BEAT-Stroke) Study. Stroke 39: 100-104; 2008.
    • (2008) Stroke , vol.39 , pp. 100-104
    • Kelly, P.J.1    Morrow, J.D.2    Ning, M.3    Koroshetz, W.4    Lo, E.H.5    Terry, E.6
  • 84
    • 79651475501 scopus 로고    scopus 로고
    • Lipoic acid protects against reperfusion injury in the early stages of cerebral ischemia
    • Connell, BJ; Saleh, M; Khan, BV; Saleh, TM. Lipoic acid protects against reperfusion injury in the early stages of cerebral ischemia. Brain Res 1375: 128-136; 2011.
    • (2011) Brain Res , vol.1375 , pp. 128-136
    • Connell, B.J.1    Saleh, M.2    Khan, B.V.3    Saleh, T.M.4
  • 85
    • 66149171367 scopus 로고    scopus 로고
    • Regulation of mn-superoxide dismutase activity and neuroprotection by stat3 in mice after cerebral ischemia
    • Jung, JE; Kim, GS; Narasimhan, P; Song, YS; Chan, PH. Regulation of Mn-superoxide dismutase activity and neuroprotection by STAT3 in mice after cerebral ischemia. J. Neurosci 29: 7003-7014; 2009.
    • (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
  • 86
    • 84871246768 scopus 로고    scopus 로고
    • Identification of new therapeutic targets by genome-wide analysis of gene expression in the ipsilateral cortex of aged rats after stroke
    • Buga, A-M; Scholz, CJ; Kumar, S; Herndon, JG; Alexandru, D; Cojocaru, GR, et al. Identification of new therapeutic targets by genome-wide analysis of gene expression in the ipsilateral cortex of aged rats after stroke. PLoS One 7: e50985; 2012.
    • (2012) PLoS One , vol.7
    • Buga, A.-M.1    Scholz, C.J.2    Kumar, S.3    Herndon, J.G.4    Alexandru, D.5    Cojocaru, G.R.6
  • 89
    • 79956365255 scopus 로고    scopus 로고
    • Morphological changes in nerve cells during normal aging
    • Pannese, E. Morphological changes in nerve cells during normal aging. Brain Struct. Funct 216: 85-89; 2011.
    • (2011) Brain Struct. Funct , vol.216 , pp. 85-89
    • Pannese, E.1
  • 92
    • 79958773159 scopus 로고    scopus 로고
    • Age-related alterations in mitochondrial physiological parameters and nitric oxide production in synaptic and non-synaptic brain cortex mitochondria
    • Lores-Arnaiz, S; Bustamante, J. Age-related alterations in mitochondrial physiological parameters and nitric oxide production in synaptic and non-synaptic brain cortex mitochondria. Neuroscience 188: 117 -124; 2011.
    • (2011) Neuroscience , vol.188 , pp. 117-124
    • Lores-Arnaiz, S.1    Bustamante, J.2
  • 94
    • 79954596666 scopus 로고    scopus 로고
    • Reactive oxygen species in the regulation of synaptic plasticity and memory
    • Massaad, CA; Klann, E. Reactive oxygen species in the regulation of synaptic plasticity and memory. Antioxid. Redox Signaling 14: 2013-2054; 2011.
    • (2011) Antioxid. Redox Signaling , vol.14 , pp. 2013-2054
    • Massaad, C.A.1    Klann, E.2
  • 95
    • 0035032925 scopus 로고    scopus 로고
    • Impairment of learning and memory in rats caused by oxidative stress and aging, and changes in antioxidative defense systems
    • Fukui, K; Onodera, K; Shinkai, T; Suzuki, S; Urano, S. Impairment of learning and memory in rats caused by oxidative stress and aging, and changes in antioxidative defense systems. Ann. N. Y. Acad. Sci 928: 168-175; 2001. (Pubitemid 32386078)
    • (2001) Annals of the New York Academy of Sciences , vol.928 , pp. 168-175
    • Fukui, K.1    Onodera, K.2    Shinkai, T.3    Suzuki, S.4    Urano, S.5
  • 97
    • 0033774075 scopus 로고    scopus 로고
    • Cognitive decline is associated with systemic oxidative stress: The eva study. Etude du vieillissement arteriel
    • Berr, C; Balansard, B; Arnaud, J; Roussel, AM; Alperovitch, A. Cognitive decline is associated with systemic oxidative stress: the EVA Study. Etude du Vieillissement Arteriel. J. Am. Geriatr. Soc 48: 1285-1291; 2000.
    • (2000) J. Am. Geriatr. Soc , vol.48 , pp. 1285-1291
    • Berr, C.1    Balansard, B.2    Arnaud, J.3    Roussel, A.M.4    Alperovitch, A.5
  • 99
    • 84859422638 scopus 로고    scopus 로고
    • Conflict of evidence: Carotenoids and other micronutrients in the prevention and treatment of cognitive impairment
    • Polidori, MC; De Spirt, S; Stahl, W; Pientka, L. Conflict of evidence: carotenoids and other micronutrients in the prevention and treatment of cognitive impairment. BioFactors 38: 167-171; 2012.
    • (2012) BioFactors , vol.38 , pp. 167-171
    • Polidori, M.C.1    De Spirt, S.2    Stahl, W.3    Pientka, L.4
  • 100
    • 74149083183 scopus 로고    scopus 로고
    • Prevention of cognitive deficits and brain oxidative stress with superoxide dismutase/catalase mimetics in aged mice
    • Clausen, A; Doctrow, S; Baudry, M. Prevention of cognitive deficits and brain oxidative stress with superoxide dismutase/catalase mimetics in aged mice. Neurobiol. Aging 31: 425-433; 2010.
    • (2010) Neurobiol. Aging , vol.31 , pp. 425-433
    • Clausen, A.1    Doctrow, S.2    Baudry, M.3
  • 101
    • 84899772095 scopus 로고    scopus 로고
    • Mild cognitive impairment and dementia: The importance of modifiable risk factors
    • Etgen, T; Sander, D; Bickel, H; Forstl, H. Mild cognitive impairment and dementia: the importance of modifiable risk factors. Dtsch. Arzteblatt Int 108: 743-750; 2011.
    • (2011) Dtsch. Arzteblatt Int , vol.108 , pp. 743-750
    • Etgen, T.1    Sander, D.2    Bickel, H.3    Forstl, H.4
  • 102
    • 78651396680 scopus 로고    scopus 로고
    • Cognitive function in elderly marathon runners: Cross-sectional data from the marathon trial (APSOEM)
    • Winker, R; Lukas, I; Perkmann, T; Haslacher, H; Ponocny, E; Lehrner, J, et al. Cognitive function in elderly marathon runners: cross-sectional data from the marathon trial (APSOEM). Wien. Klin. Wochenschr 122: 704-716; 2010.
    • (2010) Wien. Klin. Wochenschr , vol.122 , pp. 704-716
    • Winker, R.1    Lukas, I.2    Perkmann, T.3    Haslacher, H.4    Ponocny, E.5    Lehrner, J.6
  • 104
    • 20044379872 scopus 로고    scopus 로고
    • Exercise and hormesis: Oxidative stress-related adaptation for successful aging
    • DOI 10.1007/s10522-004-7386-7
    • Radak, Z; Chung, HY; Goto, S. Exercise and hormesis: oxidative stress-related adaptation for successful aging. Biogerontology 6: 71-75; 2005. (Pubitemid 41583294)
    • (2005) Biogerontology , vol.6 , Issue.1 , pp. 71-75
    • Radak, Z.1    Chung, H.Y.2    Goto, S.3
  • 105
    • 84855778465 scopus 로고    scopus 로고
    • High-intensity physical activity modulates diet effects on cere-brospinal amyloid-beta levels in normal aging and mild cognitive impairment
    • Baker, LD; Bayer-Carter, JL; Skinner, J; Montine, TJ; Cholerton, BA; Callaghan, M, et al. High-intensity physical activity modulates diet effects on cere-brospinal amyloid-beta levels in normal aging and mild cognitive impairment. J. Alzheimers Dis 28: 137-146; 2012.
    • (2012) J. Alzheimers Dis , vol.28 , pp. 137-146
    • Baker, L.D.1    Bayer-Carter, J.L.2    Skinner, J.3    Montine, T.J.4    Cholerton, B.A.5    Callaghan, M.6
  • 107
    • 0028827252 scopus 로고
    • Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
    • Li, Y; Huang, TT; Carlson, EJ; Melov, S; Ursell, PC; Olson, JL, et al. Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat. Genet 11 : 376-381; 1995.
    • (1995) Nat. Genet , vol.11 , pp. 376-381
    • Li, Y.1    Huang, T.T.2    Carlson, E.J.3    Melov, S.4    Ursell, P.C.5    Olson, J.L.6
  • 109
    • 0032815110 scopus 로고    scopus 로고
    • Mouse models of mitochondrial disease, oxidative stress, and senescence
    • DOI 10.1016/S0921-8777(99)00031-2, PII S0921877799000312
    • Melov, S; Coskun, P; Wallace, D. Mouse models of mitochondrial disease, oxidative stress, and senescence. Mutat. Res. 434: 233-242; 1999. (Pubitemid 29352258)
    • (1999) Mutation Research - DNA Repair , vol.434 , Issue.3 , pp. 233-242
    • Melov, S.1    Coskun, P.E.2    Wallace, D.C.3
  • 110
  • 111
    • 0942298545 scopus 로고    scopus 로고
    • Endogenous mitochondrial oxidative stress: Neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice
    • DOI 10.1046/j.1471-4159.2003.02195.x
    • Hinerfeld, D; Traini, MD; Weinberger, RP; Cochran, B; Doctrow, SR; Harry, J; Melov, S. Endogenous mitochondrial oxidative stress: neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious anti-oxidant therapy in superoxide dismutase 2 null mice. J. Neurochem 88: 657-667; 2004. (Pubitemid 38140210)
    • (2004) Journal of Neurochemistry , vol.88 , Issue.3 , pp. 657-667
    • Hinerfeld, D.1    Traini, M.D.2    Weinberger, R.P.3    Cochran, B.4    Doctrow, S.R.5    Harry, J.6    Melov, S.7
  • 112
    • 0033135367 scopus 로고    scopus 로고
    • Manganese superoxide dismutase mediates the early release of mitochondrial cytochrome C and subsequent DNA fragmentation after permanent focal cerebral ischemia in mice
    • Fujimura, M; Morita-Fujimura, Y; Kawase, M; Copin, JC; Calagui, B; Epstein, CJ; Chan, PH. Manganese superoxide dismutase mediates the early release of mitochondrial cytochrome C and subsequent DNA fragmentation after permanent focal cerebral ischemia in mice. J. Neurosci 19: 3414-3422; 1999. (Pubitemid 29203121)
    • (1999) Journal of Neuroscience , vol.19 , Issue.9 , pp. 3414-3422
    • Fujimura, M.1    Morita-Fujimura, Y.2    Kawase, M.3    Copin, J.-C.4    Calagui, B.5    Epstein, C.J.6    Chan, P.H.7
  • 113
    • 0035155759 scopus 로고    scopus 로고
    • Mice with a partial deficiency of manganese superoxide dismutase show increased vulnerability to the mitochondrial toxins malonate, 3-nitropropionic acid, and MPTP
    • DOI 10.1006/exnr.2000.7525
    • Andreassen, OA; Ferrante, RJ; Dedeoglu, A; Albers, DW; Klivenyi, P; Carlson, EJ, et al. Mice with a partial deficiency of manganese superoxide dismutase show increased vulnerability to the mitochondrial toxins malonate. 3-nitropropionic acid, and MPTP. Exp. Neurol 167: 189-195; 2001. (Pubitemid 32066422)
    • (2001) Experimental Neurology , vol.167 , Issue.1 , pp. 189-195
    • Andreassen, O.A.1    Ferrante, R.J.2    Dedeoglu, A.3    Albers, D.W.4    Klivenyi, P.5    Carlson, E.J.6    Epstein, C.J.7    Beal M.Flint8
  • 114
    • 0035500460 scopus 로고    scopus 로고
    • Genetic modification of prenatal lethality and dilated cardiomyopathy in Mn superoxide dismutase mutant mice
    • DOI 10.1016/S0891-5849(01)00694-3, PII S0891584901006943
    • Huang, TT; Carlson, EJ; Kozy, HM; Mantha, S; Goodman, SI; Ursell, PC; Epstein, CJ. Genetic modification of prenatal lethality and dilated cardiomyo-pathy in Mn superoxide dismutase mutant mice. Free Radic. Biol. Med 31: 110 1 -1110; 2001. (Pubitemid 33000132)
    • (2001) Free Radical Biology and Medicine , vol.31 , Issue.9 , pp. 1101-1110
    • Huang, T.-T.1    Carlson, E.J.2    Kozy, H.M.3    Mantha, S.4    Goodman, S.I.5    Ursell, P.C.6    Epstein, C.J.7
  • 117
    • 33846345418 scopus 로고    scopus 로고
    • Hippocampal long-term potentiation, memory, and longevity in mice that overexpress mitochondrial superoxide dismutase
    • DOI 10.1016/j.nlm.2006.10.003, PII S1074742706001511
    • Hu, D; Cao, P; Thiels, E; Chu, CT; Wu, GY; Oury, TD; Klann, E. Hippocampal long-term potentiation, memory, and longevity in mice that overexpress mitochon-drial superoxide dismutase. Neurobiol. Learn. Mem. 87: 372-384; 2007. (Pubitemid 46137009)
    • (2007) Neurobiology of Learning and Memory , vol.87 , Issue.3 , pp. 372-384
    • Hu, D.1    Cao, P.2    Thiels, E.3    Chu, C.T.4    Wu, G.-y.5    Oury, T.D.6    Klann, E.7
  • 118
    • 70350439125 scopus 로고    scopus 로고
    • Overexpression of Mn superoxide dismutase does not increase life span in mice
    • Jang, YC; Perez, VI; Song, W; Lustgarten, MS; Salmon, AB; Mele, J, et al. Overexpression of Mn superoxide dismutase does not increase life span in mice. J. Gerontol 64: 1114 -1125; 2009.
    • (2009) J. Gerontol , vol.64 , pp. 1114-1125
    • Jang, Y.C.1    Perez, V.I.2    Song, W.3    Lustgarten, M.S.4    Salmon, A.B.5    Mele, J.6
  • 119
    • 84886089951 scopus 로고    scopus 로고
    • Improvements in a mouse model of Alzheimer's disease through SOD2 overexpression are due to functional and not structural alterations
    • Bitner, BR; Perez-Torres, CJ; Hu, L; Inoue, T; Pautler, RG. Improvements in a mouse model of Alzheimer's disease through SOD2 overexpression are due to functional and not structural alterations. Magn. Reson. Insights 5: 1-6; 2012.
    • (2012) Magn. Reson. Insights , vol.5 , pp. 1-6
    • Bitner, B.R.1    Perez-Torres, C.J.2    Hu, L.3    Inoue, T.4    Pautler, R.G.5
  • 120
    • 0029064203 scopus 로고
    • Targeted disruption of mouse egf receptor: Effect of genetic background on mutant phenotype
    • Threadgill, DW; Dlugosz, AA; Hansen, LA; Tennenbaum, T; Lichti, U; Yee, D, et al. Targeted disruption of mouse EGF receptor: effect of genetic background on mutant phenotype. Science 269: 230-234; 1995.
    • (1995) Science , vol.269 , pp. 230-234
    • Threadgill, D.W.1    Dlugosz, A.A.2    Hansen, L.A.3    Tennenbaum, T.4    Lichti, U.5    Yee, D.6
  • 121
    • 57649178442 scopus 로고    scopus 로고
    • Oxidative stress and energy crises in neuronal dysfunction
    • Nicholls, DG. Oxidative stress and energy crises in neuronal dysfunction. Ann. N. Y. Acad. Sci 114 7: 53-60; 2008.
    • (2008) Ann. N. Y. Acad. Sci , vol.1147 , pp. 53-60
    • Nicholls, D.G.1
  • 122
    • 0030758077 scopus 로고    scopus 로고
    • A controlled study of 2 doses of idebenone in the treatment of Alzheimer's disease
    • Weyer, G; Babej-Dolle, RM; Hadler, D; Hofmann, S; Herrmann, WM. A controlled study of 2 doses of idebenone in the treatment of Alzheimer's disease. Neuropsychobiology 36: 73-82; 1997. (Pubitemid 27331264)
    • (1997) Neuropsychobiology , vol.36 , Issue.2 , pp. 73-82
    • Weyer, G.1    Babej-Dolle, R.M.2    Hadler, D.3    Hofmann, S.4    Herrmann, W.M.5
  • 123
    • 0031593616 scopus 로고    scopus 로고
    • Sustained efficacy and safety of idebenone in the treatment of Alzheimer's disease: Update on a 2-year double-blind multicentre study
    • Gutzmann H, Hadler D. Sustained efficacy and safety of idebenone in the treatment of Alzheimer's disease: update on a 2-year double-blind multi-centre study. J. Neural Transm. Suppl. 1998, 54: 301-310. (Pubitemid 28539367)
    • (1998) Journal of Neural Transmission, Supplement , Issue.54 , pp. 301-310
    • Gutzmann, H.1    Hadler, D.2
  • 125
    • 57649221161 scopus 로고    scopus 로고
    • Evidence of oxidative stress in Alzheimer's disease brain and antioxidant therapy
    • Praticò, D. Evidence of oxidative stress in Alzheimer's disease brain and antioxidant therapy. Ann. N. Y. Acad. Sci 114 7: 70-78; 2008.
    • (2008) Ann. N. Y. Acad. Sci , vol.1147 , pp. 70-78
    • Praticò, D.1
  • 127
    • 80155177695 scopus 로고    scopus 로고
    • The evidence for disease modification in Parkinson's disease
    • Lew, MF. The evidence for disease modification in Parkinson's disease. Int. J. Neurosci 121(Suppl. 2): 18-26; 2011.
    • (2011) Int. J. Neurosci , vol.121 , Issue.SUPPL. 2 , pp. 18-26
    • Lew, M.F.1
  • 128
    • 77955792985 scopus 로고    scopus 로고
    • A double-blind, placebo-controlled study to assess the mitochondria-targeted antioxidant mitoQ as a disease-modifying therapy in Parkinson's disease
    • Snow, BJ; Rolfe, FL; Lockhart, MM; Frampton, CM; O'Sullivan, JD; Fung, V, et al. A double-blind, placebo-controlled study to assess the mitochondria-targeted antioxidant mitoQ as a disease-modifying therapy in Parkinson's disease. Mov. Disord 25: 1670-1674; 2010.
    • (2010) Mov. Disord , vol.25 , pp. 1670-1674
    • Snow, B.J.1    Rolfe, F.L.2    Lockhart, M.M.3    Frampton, C.M.4    O'Sullivan, J.D.5    Fung, V.6
  • 132
    • 53449102261 scopus 로고    scopus 로고
    • Neither vitamin e nor donepezil delays progression from amnestic mild cognitive impairment to Alzheimer's disease in the long term
    • Blacker, D. Neither vitamin E nor donepezil delays progression from amnestic mild cognitive impairment to Alzheimer's disease in the long term. Evid. Based Ment. Health 9: 20; 2006.
    • (2006) Evid. Based Ment. Health , vol.9 , pp. 20
    • Blacker, D.1
  • 133
    • 84886089951 scopus 로고    scopus 로고
    • Improvements in a mouse model of Alzheimer's disease through SOD2 overexpression are due to functional and not structural alterations
    • Pautler, Bitner BR; Perez-Torres, CJ; Hu, L; Inoue, T Pautler. Improvements in a mouse model of Alzheimer's disease through SOD2 overexpression are due to functional and not structural alterations. Magn. Reson. Insights 29: 1-6; 2012.
    • (2012) Magn. Reson. Insights , vol.29 , pp. 1-6
    • Pautler Bitner, B.R.1    Perez-Torres, C.J.2    Hu, L.3    Inoue, T.P.4
  • 134
    • 33745154155 scopus 로고    scopus 로고
    • Conditional knockout of Mn superoxide dismutase in postnatal motor neurons reveals resistance to mitochondrial generated superoxide radicals
    • DOI 10.1016/j.nbd.2006.02.014, PII S0969996106000507
    • Misawa, H; Nakata, K; Matsuura, J; Moriwaki, Y; Kawashima, K; Shimizu, T, et al. Conditional knockout of Mn superoxide dismutase in postnatal motor neurons reveals resistance to mitochondrial generated superoxide radicals. Neurobiol. Dis 23: 169-177; 2006. (Pubitemid 43903638)
    • (2006) Neurobiology of Disease , vol.23 , Issue.1 , pp. 169-177
    • Misawa, H.1    Nakata, K.2    Matsuura, J.3    Moriwaki, Y.4    Kawashima, K.5    Shimizu, T.6    Shirasawa, T.7    Takahashi, R.8
  • 135
    • 84861663194 scopus 로고    scopus 로고
    • Neurodegeneration and early lethality in superoxide dismutase 2-deficient mice: A comprehensive analysis of the central and peripheral nervous systems
    • Oh, SS; Sullivan, KA; Wilkinson, JE; Backus, C; Hayes, JM; Sakowski, SA; Feldman, EL. Neurodegeneration and early lethality in superoxide dismutase 2-deficient mice: a comprehensive analysis of the central and peripheral nervous systems. Neuroscience 212: 201-213; 2012.)
    • (2012) Neuroscience , vol.212 , pp. 201-213
    • Oh, S.S.1    Sullivan, K.A.2    Wilkinson, J.E.3    Backus, C.4    Hayes, J.M.5    Sakowski, S.A.6    Feldman, E.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.