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Volumn 8, Issue 21, 2013, Pages 2003-2014

Oxidative stress, mitochondrial damage and neurodegenerative diseases

Author keywords

Alzheimer's disease; Amyotrophic lateral sclerosis; Grants supported paper; Mitochondrial damage; Neural regeneration; Neurodegenerative diseases; Neuroregeneration; Oxidative stress; Parkinson's disease; Reactive oxygen species; Respiratory chain

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; BETA SECRETASE; CALBINDIN; CALCIUM ION; CATALASE; CYTOCHROME C OXIDASE; DNA DIRECTED DNA POLYMERASE GAMMA; FLAVINE ADENINE NUCLEOTIDE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; HYDROGEN PEROXIDE; LEUCINE RICH REPEAT KINASE 2; MITOCHONDRIAL DNA; MITOCHONDRIAL TRANSCRIPTION FACTOR A; OXOGLUTARATE DEHYDROGENASE; PARKIN; PARVALBUMIN; PEROXYNITRITE; PYRUVATE DEHYDROGENASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SERINE PROTEINASE OMI; SUCCINATE DEHYDROGENASE; SUPEROXIDE DISMUTASE; UBIQUINOL CYTOCHROME C REDUCTASE; UBIQUINONE;

EID: 84889860617     PISSN: 16735374     EISSN: 18767958     Source Type: Journal    
DOI: 10.3969/j.issn.1673-5374.2013.21.009     Document Type: Article
Times cited : (1014)

References (126)
  • 1
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin MT, Beal MF. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature. 2006;443 (7113):787-795.
    • (2006) Nature. , vol.443 , Issue.7113 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 2
    • 77956216847 scopus 로고    scopus 로고
    • Mitochondrial and cell death mechanisms in neurodegenerative diseases
    • Martin LJ. Mitochondrial and cell death mechanisms in neurodegenerative diseases. Pharmaceuticals (Basel). 2010;3(4):839-915.
    • (2010) Pharmaceuticals (Basel). , vol.3 , Issue.4 , pp. 839-915
    • Martin, L.J.1
  • 3
    • 79961000133 scopus 로고    scopus 로고
    • Neurodegenerative disorders: Restoring the balance
    • Crunkhorn S. Neurodegenerative disorders: Restoring the balance. Nat Rev Drug Discov. 2011;10(8):576.
    • (2011) Nat Rev Drug Discov. , vol.10 , Issue.8 , pp. 576
    • Crunkhorn, S.1
  • 4
    • 34249788738 scopus 로고    scopus 로고
    • Mitochondria, metabolic disturbances, oxidative stress and the kynurenine system, with focus on neurodegenerative disorders
    • Sas K, Robotka H, Toldi J, et al. Mitochondria, metabolic disturbances, oxidative stress and the kynurenine system, with focus on neurodegenerative disorders. J Neurol Sci. 2007;257(1-2):221-239.
    • (2007) J Neurol Sci. , vol.257 , Issue.1-2 , pp. 221-239
    • Sas, K.1    Robotka, H.2    Toldi, J.3
  • 5
    • 84864088343 scopus 로고    scopus 로고
    • Mitochondrial topoisomerase I is critical for mitochondrial integrity and cellular energy metabolism
    • Douarre C, Sourbier C, Dalla Rosa I, et al. Mitochondrial topoisomerase I is critical for mitochondrial integrity and cellular energy metabolism. PLoS One. 2012;7(7):e41094.
    • (2012) PLoS One. , vol.7 , Issue.7
    • Douarre, C.1    Sourbier, C.2    Dalla Rosa, I.3
  • 6
    • 0034656015 scopus 로고    scopus 로고
    • Glial cell type-specific responses to menadione-induced oxidative stress
    • Hollensworth SB, Shen C, Sim JE, et al. Glial cell type-specific responses to menadione-induced oxidative stress. Free Radic Biol Med. 2000;28(8):1161-1174.
    • (2000) Free Radic Biol Med. , vol.28 , Issue.8 , pp. 1161-1174
    • Hollensworth, S.B.1    Shen, C.2    Sim, J.E.3
  • 7
    • 26944439050 scopus 로고    scopus 로고
    • Regulation of mitochondrial respiratory chain structure and function by estro-gens/estrogen receptors and potential physiologi-cal/pathophysiological implications
    • Chen JQ, Yager JD, Russo J. Regulation of mitochondrial respiratory chain structure and function by estro-gens/estrogen receptors and potential physiologi-cal/pathophysiological implications. Biochim Biophys Acta. 2005;1746(1):1-17.
    • (2005) Biochim Biophys Acta. , vol.1746 , Issue.1 , pp. 1-17
    • Chen, J.Q.1    Yager, J.D.2    Russo, J.3
  • 8
    • 84863741781 scopus 로고    scopus 로고
    • Assembly factors of human mito-chondrial respiratory chain complexes: Physiology and pathophysiology
    • Ghezzi D, Zeviani M. Assembly factors of human mito-chondrial respiratory chain complexes: physiology and pathophysiology. Adv Exp Med Biol. 2012;748:65-106.
    • (2012) Adv Exp Med Biol. , vol.748 , pp. 65-106
    • Ghezzi, D.1    Zeviani, M.2
  • 9
    • 33846032681 scopus 로고    scopus 로고
    • Mitochondrial DNA and the mammalian oocyte
    • Shoubridge EA, Wai T. Mitochondrial DNA and the mammalian oocyte. Curr Top Dev Biol. 2007;77:87-111.
    • (2007) Curr Top Dev Biol. , vol.77 , pp. 87-111
    • Shoubridge, E.A.1    Wai, T.2
  • 10
    • 0029056231 scopus 로고
    • Mitochondrial proton conductance and H+/O ratio are independent of electron transport rate in isolated hepatocytes
    • Porter RK, Brand MD. Mitochondrial proton conductance and H+/O ratio are independent of electron transport rate in isolated hepatocytes. Biochem J. 1995;310(Pt 2):379-382.
    • (1995) Biochem J. , vol.310 , Issue.PART 2 , pp. 379-382
    • Porter, R.K.1    Brand, M.D.2
  • 11
    • 84861199913 scopus 로고    scopus 로고
    • Accumulation of nuclear and mitochondrial DNA damage in the frontal cortex cells of patients with HIV-associated neurocognitive disorders
    • Zhang Y, Wang M, Li H, et al. Accumulation of nuclear and mitochondrial DNA damage in the frontal cortex cells of patients with HIV-associated neurocognitive disorders. Brain Res. 2012;1458:1-11.
    • (2012) Brain Res. , vol.1458 , pp. 1-11
    • Zhang, Y.1    Wang, M.2    Li, H.3
  • 12
    • 0035978154 scopus 로고    scopus 로고
    • Oxidative stress in human aging and mitochondrial disease? consequences of de-fective mitochondrial respiration and impaired antioxidant enzyme system
    • Wei YH, Lu CY, Wei CY, et al. Oxidative stress in human aging and mitochondrial disease? consequences of de-fective mitochondrial respiration and impaired antioxidant enzyme system. Chin J Physiol. 2001;44(1):1-11.
    • (2001) Chin J Physiol. , vol.44 , Issue.1 , pp. 1-11
    • Wei, Y.H.1    Lu, C.Y.2    Wei, C.Y.3
  • 13
    • 79953667930 scopus 로고    scopus 로고
    • Reac-tive oxygen species production by forward and reverse electron fluxes in the mitochondrial respiratory chain
    • Selivanov VA, Votyakova TV, Pivtoraiko VN, et al. Reac-tive oxygen species production by forward and reverse electron fluxes in the mitochondrial respiratory chain. PLoS Comput Biol. 2011;7(3):e1001115.
    • (2011) PLoS Comput Biol. , vol.7 , Issue.3
    • Selivanov, V.A.1    Votyakova, T.V.2    Pivtoraiko, V.N.3
  • 14
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel T, Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. Nature. 2000;408(6809):239-247.
    • (2000) Nature. , vol.408 , Issue.6809 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 15
    • 30344432706 scopus 로고    scopus 로고
    • Role of mitochon-drial DNA in toxic responses to oxidative stress
    • Van Houten B, Woshner V, Santos JH. Role of mitochon-drial DNA in toxic responses to oxidative stress. DNA Repair (Amst). 2006;5(2):145-152.
    • (2006) DNA Repair (Amst). , vol.5 , Issue.2 , pp. 145-152
    • Van Houten, B.1    Woshner, V.2    Santos, J.H.3
  • 16
    • 84860887855 scopus 로고    scopus 로고
    • Transcriptional changes in OXPHOS complex I deficiency are related to anti-oxidant pathways and could explain the disturbed calcium homeostasis
    • Voets AM, Huigsloot M, Lindsey PJ, et al. Transcriptional changes in OXPHOS complex I deficiency are related to anti-oxidant pathways and could explain the disturbed calcium homeostasis. Biochim Biophys Acta. 2012; 1822(7):1161-1168.
    • (2012) Biochim Biophys Acta. , vol.1822 , Issue.7 , pp. 1161-1168
    • Voets, A.M.1    Huigsloot, M.2    Lindsey, P.J.3
  • 17
    • 84155165077 scopus 로고    scopus 로고
    • Aging in-creases mitochondrial DNA damage and oxidative stress in liver of rhesus monkeys
    • Castro Mdel R, Suarez E, Kraiselburd E, et al. Aging in-creases mitochondrial DNA damage and oxidative stress in liver of rhesus monkeys. Exp Gerontol. 2012;47(1): 29-37.
    • (2012) Exp Gerontol. , vol.47 , Issue.1 , pp. 29-37
    • Castro Mdel, R.1    Suarez, E.2    Kraiselburd, E.3
  • 18
    • 70349515574 scopus 로고    scopus 로고
    • Is there more to aging than mitochondrial DNA and reactive oxygen species?
    • Alexeyev MF. Is there more to aging than mitochondrial DNA and reactive oxygen species? FEBS J. 2009; 276(20):5768-5787.
    • (2009) FEBS J. , vol.276 , Issue.20 , pp. 5768-5787
    • Alexeyev, M.F.1
  • 19
    • 77950575478 scopus 로고    scopus 로고
    • Mitochondrial complex I activity and oxidative damage to mitochondrial proteins in the prefrontal cortex of patients with bipolar disorder
    • Andreazza AC, Shao L, Wang JF, et al. Mitochondrial complex I activity and oxidative damage to mitochondrial proteins in the prefrontal cortex of patients with bipolar disorder. Arch Gen Psychiatry. 2010;67(4):360-368.
    • (2010) Arch Gen Psychiatry. , vol.67 , Issue.4 , pp. 360-368
    • Andreazza, A.C.1    Shao, L.2    Wang, J.F.3
  • 20
    • 44049104339 scopus 로고    scopus 로고
    • Effects of os-cillatory electric fields on internal membranes: An analyti-cal model
    • Vajrala V, Claycomb JR, Sanabria H, et al. Effects of os-cillatory electric fields on internal membranes: an analyti-cal model. Biophys J. 2008;94(6):2043-2052.
    • (2008) Biophys J. , vol.94 , Issue.6 , pp. 2043-2052
    • Vajrala, V.1    Claycomb, J.R.2    Sanabria, H.3
  • 21
    • 12144257165 scopus 로고    scopus 로고
    • Cytoch-rome c association with the inner mitochondrial mem-brane is impaired in the CNS of G93A-SOD1 mice
    • Kirkinezos IG, Bacman SR, Hernandez D, et al. Cytoch-rome c association with the inner mitochondrial mem-brane is impaired in the CNS of G93A-SOD1 mice. J Neurosci. 2005;25(1):164-172.
    • (2005) J Neurosci. , vol.25 , Issue.1 , pp. 164-172
    • Kirkinezos, I.G.1    Bacman, S.R.2    Hernandez, D.3
  • 22
    • 0037303479 scopus 로고    scopus 로고
    • Nitric oxide-induced mitochondrial dysfunction implications for neurodegeneration
    • Stewart VC, Heales SJ. Nitric oxide-induced mitochondrial dysfunction implications for neurodegeneration. Free Radic Biol Med. 2003;34(3):287-303.
    • (2003) Free Radic Biol Med. , vol.34 , Issue.3 , pp. 287-303
    • Stewart, V.C.1    Heales, S.J.2
  • 23
    • 33749986298 scopus 로고    scopus 로고
    • Free radicals and antioxidants in normal physiological functions and human disease
    • Valko M, Leibfritz D, Moncol J, et al. Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol. 2007;39(1):44-84.
    • (2007) Int J Biochem Cell Biol. , vol.39 , Issue.1 , pp. 44-84
    • Valko, M.1    Leibfritz, D.2    Moncol, J.3
  • 24
    • 33645089917 scopus 로고    scopus 로고
    • Identification of nitrated proteins in Alzheimer's disease brain using a redox pro-teomics approach
    • Sultana R, Poon HF, Cai J, et al. Identification of nitrated proteins in Alzheimer's disease brain using a redox pro-teomics approach. Neurobiol Dis. 2006;22(1):76-87.
    • (2006) Neurobiol Dis. , vol.22 , Issue.1 , pp. 76-87
    • Sultana, R.1    Poon, H.F.2    Cai, J.3
  • 25
    • 0034237719 scopus 로고    scopus 로고
    • Energetics in the pathogenesis of neurodege-nerative diseases
    • Beal MF. Energetics in the pathogenesis of neurodege-nerative diseases. Trends Neurosci. 2000;23(7):298-304.
    • (2000) Trends Neurosci. , vol.23 , Issue.7 , pp. 298-304
    • Beal, M.F.1
  • 26
    • 48849105951 scopus 로고    scopus 로고
    • Developmental regulation of intracellular calcium homeostasis in early cardiac myocytes
    • Fu JD, Yang HT. Developmental regulation of intracellular calcium homeostasis in early cardiac myocytes. Sheng Li Xue Bao. 2006;58(2):95-103.
    • (2006) Sheng Li Xue Bao. , vol.58 , Issue.2 , pp. 95-103
    • Fu, J.D.1    Yang, H.T.2
  • 27
    • 0006295841 scopus 로고    scopus 로고
    • Melatonin-induced increased activity of the respiratory chain complexes I and IV can prevent mitochondrial damage induced by ruthe-nium red in vivo
    • Martín M, Macías M, Escames G, et al. Melatonin-induced increased activity of the respiratory chain complexes I and IV can prevent mitochondrial damage induced by ruthe-nium red in vivo. J Pineal Res. 2000;28(4):242-248.
    • (2000) J Pineal Res. , vol.28 , Issue.4 , pp. 242-248
    • Martín, M.1    Macías, M.2    Escames, G.3
  • 28
    • 84870687065 scopus 로고    scopus 로고
    • Coenzyme Q10 inhibits the release of glutamate in rat cerebrocortical nerve ter-minals by suppression of voltage-dependent calcium in-flux and mitogen-activated protein kinase signaling path-way
    • Chang Y, Huang SK, Wang SJ. Coenzyme Q10 inhibits the release of glutamate in rat cerebrocortical nerve ter-minals by suppression of voltage-dependent calcium in-flux and mitogen-activated protein kinase signaling path-way. J Agric Food Chem. 2012;60(48):11909-11918.
    • (2012) J Agric Food Chem. , vol.60 , Issue.48 , pp. 11909-11918
    • Chang, Y.1    Huang, S.K.2    Wang, S.J.3
  • 29
    • 66149088109 scopus 로고    scopus 로고
    • Inhibiting pro-death NMDA receptor signaling dependent on the NR2 PDZ ligand may not affect synaptic function or syn-aptic NMDA receptor signaling to gene expression
    • Martel MA, Soriano FX, Baxter P, et al. Inhibiting pro-death NMDA receptor signaling dependent on the NR2 PDZ ligand may not affect synaptic function or syn-aptic NMDA receptor signaling to gene expression. Channels (Austin). 2009;3(1):12-15.
    • (2009) Channels (Austin). , vol.3 , Issue.1 , pp. 12-15
    • Martel, M.A.1    Soriano, F.X.2    Baxter, P.3
  • 30
    • 34249092704 scopus 로고    scopus 로고
    • Calcium and neurodegeneration
    • Mattson MP. Calcium and neurodegeneration. Aging Cell. 2007;6(3):337-350.
    • (2007) Aging Cell. , vol.6 , Issue.3 , pp. 337-350
    • Mattson, M.P.1
  • 31
    • 33645299025 scopus 로고    scopus 로고
    • Ageing and neuronal vulnerability
    • Mattson MP, Magnus T. Ageing and neuronal vulnerability. Nat Rev Neurosci. 2006;7(4):278-294.
    • (2006) Nat Rev Neurosci. , vol.7 , Issue.4 , pp. 278-294
    • Mattson, M.P.1    Magnus, T.2
  • 32
    • 33745287476 scopus 로고    scopus 로고
    • Normal brain ageing: Models and mechan-isms
    • Toescu EC. Normal brain ageing: models and mechan-isms. Philos Trans R Soc Lond B Biol Sci. 2005; 360(1464):2347-2354.
    • (2005) Philos Trans R Soc Lond B Biol Sci. , vol.360 , Issue.1464 , pp. 2347-2354
    • Toescu, E.C.1
  • 33
    • 15144349362 scopus 로고    scopus 로고
    • Formation of S-nitrosothiols via direct nucleophilic nitrosation of thiols by peroxynitrite with elimination of hydrogen peroxide
    • van der Vliet A, Hoen PA, Wong PS, et al. Formation of S-nitrosothiols via direct nucleophilic nitrosation of thiols by peroxynitrite with elimination of hydrogen peroxide. J Biol Chem. 1998;273(46):30255-30262.
    • (1998) J Biol Chem. , vol.273 , Issue.46 , pp. 30255-30262
    • van der Vliet, A.1    Hoen, P.A.2    Wong, P.S.3
  • 34
    • 15244360536 scopus 로고    scopus 로고
    • In vivo protection of synaptosomes from oxidative stress mediated by Fe2+/H2O2 or 2, 2-azobis-(2-amidinopropane) dihy-drochloride by the glutathione mimetic tricyclodecan-9-yl-xanthogenate
    • Joshi G, Sultana R, Perluigi M, et al. In vivo protection of synaptosomes from oxidative stress mediated by Fe2+/H2O2 or 2, 2-azobis-(2-amidinopropane) dihy-drochloride by the glutathione mimetic tricyclodecan-9-yl-xanthogenate. Free Radic Biol Med. 2005;38(8): 1023-1031.
    • (2005) Free Radic Biol Med. , vol.38 , Issue.8 , pp. 1023-1031
    • Joshi, G.1    Sultana, R.2    Perluigi, M.3
  • 35
    • 84857370599 scopus 로고    scopus 로고
    • Understanding calcium waves and sparks in central neurons
    • Ross WN. Understanding calcium waves and sparks in central neurons. Nat Rev Neurosci. 2012;13(3):157-168.
    • (2012) Nat Rev Neurosci. , vol.13 , Issue.3 , pp. 157-168
    • Ross, W.N.1
  • 36
    • 71849092300 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore: A molecular target for amyotrophic lateral sclerosis ther-apy
    • Martin LJ. The mitochondrial permeability transition pore: A molecular target for amyotrophic lateral sclerosis ther-apy. Bio-chim Biophys Acta. 2010;1802(1):186-197.
    • (2010) Bio-chim Biophys Acta. , vol.1802 , Issue.1 , pp. 186-197
    • Martin, L.J.1
  • 37
    • 33748201552 scopus 로고    scopus 로고
    • Mitochondria-targeted peptide antioxidants: Novel neuroprotective agents
    • Szeto HH. Mitochondria-targeted peptide antioxidants: novel neuroprotective agents. AAPS J. 2006;8(3): E521-531.
    • (2006) AAPS J. , vol.8 , Issue.3
    • Szeto, H.H.1
  • 38
    • 4043147798 scopus 로고    scopus 로고
    • Mitochondrial superoxide: Production, biological effects, and activation of uncoupling proteins
    • Brand MD, Affourtit C, Esteves TC, et al. Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins. Free Radic Biol Med. 2004;37(6): 755-767.
    • (2004) Free Radic Biol Med. , vol.37 , Issue.6 , pp. 755-767
    • Brand, M.D.1    Affourtit, C.2    Esteves, T.C.3
  • 40
    • 34248175243 scopus 로고    scopus 로고
    • The evidence basis for coenzyme Q therapy in oxidative phosphorylation disease
    • Haas RH. The evidence basis for coenzyme Q therapy in oxidative phosphorylation disease. Mitochondrion. 2007;7 Suppl:S136-145.
    • (2007) Mitochondrion. , vol.7 , Issue.SUPPL.
    • Haas, R.H.1
  • 41
    • 84871579325 scopus 로고    scopus 로고
    • Oxygen, pH, and mitochondrial oxidative phosphorylation
    • Wilson DF, Harrison DK, Vinogradov SA. Oxygen, pH, and mitochondrial oxidative phosphorylation. J Appl Physiol. 2012;113(12):1838-1845.
    • (2012) J Appl Physiol. , vol.113 , Issue.12 , pp. 1838-1845
    • Wilson, D.F.1    Harrison, D.K.2    Vinogradov, S.A.3
  • 42
    • 0027999790 scopus 로고
    • Physiological role of mitochondrial Ca2+ transport
    • Hansford RG. Physiological role of mitochondrial Ca2+ transport. J Bioenerg Biomembr. 1994;26(5):495-508.
    • (1994) J Bioenerg Biomembr. , vol.26 , Issue.5 , pp. 495-508
    • Hansford, R.G.1
  • 43
    • 0033971898 scopus 로고    scopus 로고
    • Mitochondria and neuronal survival
    • Nicholls DG, Budd SL. 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
  • 44
    • 84858688425 scopus 로고    scopus 로고
    • Epigenetics, epidemiology and mitochondrial DNA diseases
    • Chinnery PF, Elliott HR, Hudson G, et al. Epigenetics, epidemiology and mitochondrial DNA diseases. Int J Ep-idemiol. 2012;41(1):177-187.
    • (2012) Int J Ep-idemiol. , vol.41 , Issue.1 , pp. 177-187
    • Chinnery, P.F.1    Elliott, H.R.2    Hudson, G.3
  • 45
    • 0037314215 scopus 로고    scopus 로고
    • Neuronal degeneration and mi-tochondrial dysfunction
    • Schon EA, Manfredi G. Neuronal degeneration and mi-tochondrial dysfunction. J Clin Invest. 2003;111(3): 303-312.
    • (2003) J Clin Invest. , vol.111 , Issue.3 , pp. 303-312
    • Schon, E.A.1    Manfredi, G.2
  • 46
    • 85173345256 scopus 로고    scopus 로고
    • Mitochondrial dys-function in psychiatric and neurological diseases: Cause(s), consequence(s), and implications of antioxidant therapy
    • in press
    • Kasote DM, Hegde MV, Katyare SS. Mitochondrial dys-function in psychiatric and neurological diseases: Cause(s), consequence(s), and implications of antioxidant therapy. Biofactors. in press.
    • Biofactors.
    • Kasote, D.M.1    Hegde, M.V.2    Katyare, S.S.3
  • 47
    • 56149105398 scopus 로고    scopus 로고
    • Calcium ions in neuronal degeneration
    • Wojda U, Salinska E, Kuznicki J. Calcium ions in neuronal degeneration. IUBMB Life. 2008;60(9):575-590.
    • (2008) IUBMB Life. , vol.60 , Issue.9 , pp. 575-590
    • Wojda, U.1    Salinska, E.2    Kuznicki, J.3
  • 48
    • 84863688106 scopus 로고    scopus 로고
    • Mitochondrial-and endoplasmic reticulum-associated oxidative stress in Alzheimer's disease: From pathogenesis to biomarkers
    • Ferreiro E, Baldeiras I, Ferreira IL, et al. Mitochondrial-and endoplasmic reticulum-associated oxidative stress in Alzheimer's disease: from pathogenesis to biomarkers. Int J Cell Biol. 2012;2012:735206.
    • (2012) Int J Cell Biol. , vol.2012 , pp. 735206
    • Ferreiro, E.1    Baldeiras, I.2    Ferreira, I.L.3
  • 49
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mito-chondrial function in neuronal cells
    • Anandatheerthavarada HK, Biswas G, Robin MA, et al. Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mito-chondrial function in neuronal cells. J Cell Biol. 2003; 161(1):41-54.
    • (2003) J Cell Biol. , vol.161 , Issue.1 , pp. 41-54
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Robin, M.A.3
  • 50
    • 0037096193 scopus 로고    scopus 로고
    • The relation-ship between oxidative/nitrative stress and pathological inclusions in Alzheimer's and Parkinson's diseases
    • Giasson BI, Ischiropoulos H, Lee VM, et al. The relation-ship between oxidative/nitrative stress and pathological inclusions in Alzheimer's and Parkinson's diseases. Free Radic Biol Med. 2002;32(12):1264-1275.
    • (2002) Free Radic Biol Med. , vol.32 , Issue.12 , pp. 1264-1275
    • Giasson, B.I.1    Ischiropoulos, H.2    Lee, V.M.3
  • 51
    • 3142514196 scopus 로고    scopus 로고
    • Oxidative stress in neurodegeneration: Cause or consequence?
    • Andersen JK. Oxidative stress in neurodegeneration: cause or consequence? Nat Med. 2004;10 Suppl: S18-25.
    • (2004) Nat Med. , vol.10 , Issue.SUPPL.
    • Andersen, J.K.1
  • 52
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease
    • Lustbader JW, Cirilli M, Lin C, et al. ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science. 2004;304(5669):448-452.
    • (2004) Science. , vol.304 , Issue.5669 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3
  • 53
    • 69249212441 scopus 로고    scopus 로고
    • Mitochondrial dihydrolipoyl succinyltransferase deficiency accelerates amyloid pathology and memory deficit in a transgenic mouse model of amyloid deposition
    • Dumont M, Ho DJ, Calingasan NY, et al. Mitochondrial dihydrolipoyl succinyltransferase deficiency accelerates amyloid pathology and memory deficit in a transgenic mouse model of amyloid deposition. Free Radic Biol Med. 2009;47(7):1019-1027.
    • (2009) Free Radic Biol Med. , vol.47 , Issue.7 , pp. 1019-1027
    • Dumont, M.1    Ho, D.J.2    Calingasan, N.Y.3
  • 54
    • 79955973551 scopus 로고    scopus 로고
    • Inactivation and reactivation of the mitochondrial α-ketoglutarate dehydrogenase com-plex
    • Shi Q, Xu H, Yu H, et al. Inactivation and reactivation of the mitochondrial α-ketoglutarate dehydrogenase com-plex. J Biol Chem. 2011;286(20):17640-17648.
    • (2011) J Biol Chem. , vol.286 , Issue.20 , pp. 17640-17648
    • Shi, Q.1    Xu, H.2    Yu, H.3
  • 55
    • 3242668604 scopus 로고    scopus 로고
    • Alzheimer's brains harbor somatic mtDNA control-region mutations that sup-press mitochondrial transcription and replication
    • Coskun PE, Beal MF, Wallace DC. Alzheimer's brains harbor somatic mtDNA control-region mutations that sup-press mitochondrial transcription and replication. Proc Natl Acad Sci U S A. 2004;101(29):10726-10731.
    • (2004) Proc Natl Acad Sci U S A. , vol.101 , Issue.29 , pp. 10726-10731
    • Coskun, P.E.1    Beal, M.F.2    Wallace, D.C.3
  • 56
    • 33646349444 scopus 로고    scopus 로고
    • Mitochondrial oxidative damage in aging and Alzheimer's disease: Implications for mitochondrially tar-geted antioxidant therapeutics
    • Reddy PH. Mitochondrial oxidative damage in aging and Alzheimer's disease: implications for mitochondrially tar-geted antioxidant therapeutics. J Biomed Biotechnol. 2006;2006(3):31372.
    • (2006) J Biomed Biotechnol. , vol.2006 , Issue.3 , pp. 31372
    • Reddy, P.H.1
  • 57
    • 84867516927 scopus 로고    scopus 로고
    • Mitochondrial DNA sequence variation associated with dementia and cognitive function in the elderly
    • Tranah GJ, Nalls MA, Katzman SM, et al. Mitochondrial DNA sequence variation associated with dementia and cognitive function in the elderly. J Alzheimers Dis. 2012; 32(2):357-372.
    • (2012) J Alzheimers Dis. , vol.32 , Issue.2 , pp. 357-372
    • Tranah, G.J.1    Nalls, M.A.2    Katzman, S.M.3
  • 58
    • 80051713678 scopus 로고    scopus 로고
    • C-Abl tyrosine kinase signaling: A new player in AD tau pathology
    • Estrada LD, Zanlungo SM, Alvarez AR. C-Abl tyrosine kinase signaling: a new player in AD tau pathology. Curr Alzheimer Res. 2011;8(6):643-651.
    • (2011) Curr Alzheimer Res. , vol.8 , Issue.6 , pp. 643-651
    • Estrada, L.D.1    Zanlungo, S.M.2    Alvarez, A.R.3
  • 59
    • 79958765866 scopus 로고    scopus 로고
    • c-Abl ty-rosine kinase modulates tau pathology and Cdk5 phos-phorylation in AD transgenic mice
    • Cancino GI, Perez de Arce K, Castro PU, et al. c-Abl ty-rosine kinase modulates tau pathology and Cdk5 phos-phorylation in AD transgenic mice. Neurobiol Aging. 2011;32(7):1249-1261.
    • (2011) Neurobiol Aging. , vol.32 , Issue.7 , pp. 1249-1261
    • Cancino, G.I.1    de Perez Arce, K.2    Castro, P.U.3
  • 60
    • 67849130954 scopus 로고    scopus 로고
    • Altered subcellular dis-tribution of c-Abl in Alzheimer's disease
    • Jing Z, Caltagarone J, Bowser R. Altered subcellular dis-tribution of c-Abl in Alzheimer's disease. J Alzheimers Dis. 2009;17(2):409-422.
    • (2009) J Alzheimers Dis. , vol.17 , Issue.2 , pp. 409-422
    • Jing, Z.1    Caltagarone, J.2    Bowser, R.3
  • 61
    • 85173383367 scopus 로고    scopus 로고
    • DNA damage in Alzheimer disease lymphocytes and its relation to premature centromere division
    • in press
    • Zivković L, Spremo-Potparević B, Siedlak SL, et al. DNA damage in Alzheimer disease lymphocytes and its relation to premature centromere division. Neurodegener Dis. in press.
    • Neurodegener Dis.
    • Zivković, L.1    Spremo-Potparević, B.2    Siedlak, S.L.3
  • 62
    • 84871818839 scopus 로고    scopus 로고
    • Oxidative stress modulates mitochondrial failure and cyclophilin D function in X-linked adrenoleukodystrophy
    • López-Erauskin J, Galino J, Bianchi P, et al. Oxidative stress modulates mitochondrial failure and cyclophilin D function in X-linked adrenoleukodystrophy. Brain. 2012; 135(Pt 12):3584-3598.
    • (2012) Brain. , vol.135 , Issue.PART 12 , pp. 3584-3598
    • López-Erauskin, J.1    Galino, J.2    Bianchi, P.3
  • 63
    • 84866253155 scopus 로고    scopus 로고
    • Redox regula-tion of protein function via cysteine s-nitrosylation and its relevance to neurodegenerative diseases
    • Akhtar MW, Sunico CR, Nakamura T, et al. Redox regula-tion of protein function via cysteine s-nitrosylation and its relevance to neurodegenerative diseases. Int J Cell Biol. 2012;2012:463756.
    • (2012) Int J Cell Biol. , vol.2012 , pp. 463756
    • Akhtar, M.W.1    Sunico, C.R.2    Nakamura, T.3
  • 64
    • 84858978818 scopus 로고    scopus 로고
    • Protein misfolded oligomers: Expe-rimental approaches, mechanism of formation, and structure-toxicity relationships
    • Bemporad F, Chiti F. Protein misfolded oligomers: expe-rimental approaches, mechanism of formation, and structure-toxicity relationships. Chem Biol. 2012;19(3): 315-327.
    • (2012) Chem Biol. , vol.19 , Issue.3 , pp. 315-327
    • Bemporad, F.1    Chiti, F.2
  • 65
    • 84863644570 scopus 로고    scopus 로고
    • Oxidative Stress, DNA damage, and c-Abl signaling: At the cros-sroad in neurodegenerative diseases?
    • Gonfloni S, Maiani E, Di Bartolomeo C, et al. Oxidative Stress, DNA damage, and c-Abl signaling: at the cros-sroad in neurodegenerative diseases? Int J Cell Biol. 2012;2012:683097.
    • (2012) Int J Cell Biol. , vol.2012 , pp. 683097
    • Gonfloni, S.1    Maiani, E.2    Di Bartolomeo, C.3
  • 66
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury
    • Cho DH, Nakamura T, Fang J, et al. S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury. Science. 2009;324(5923):102-105.
    • (2009) Science. , vol.324 , Issue.5923 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3
  • 67
    • 84866555095 scopus 로고    scopus 로고
    • S-nitrosylation of Cdk5: Potential implications in amyloid-β-related neuro-toxicity in Alzheimer disease
    • Qu J, Nakamura T, Holland EA, et al. S-nitrosylation of Cdk5: potential implications in amyloid-β-related neuro-toxicity in Alzheimer disease. Prion. 2012;6(4):364-370.
    • (2012) Prion. , vol.6 , Issue.4 , pp. 364-370
    • Qu, J.1    Nakamura, T.2    Holland, E.A.3
  • 68
    • 84866540615 scopus 로고    scopus 로고
    • Redox regulation of protein misfolding, mitochondrial dysfunction, synaptic damage, and cell death in neurodegenerative diseases
    • Nakamura T, Cho DH, Lipton SA. Redox regulation of protein misfolding, mitochondrial dysfunction, synaptic damage, and cell death in neurodegenerative diseases. Exp Neurol. 2012;238(1):12-21.
    • (2012) Exp Neurol. , vol.238 , Issue.1 , pp. 12-21
    • Nakamura, T.1    Cho, D.H.2    Lipton, S.A.3
  • 69
    • 43049141105 scopus 로고    scopus 로고
    • Vulnerability of glial cells to hydrogen peroxide in cultured hippocampal slices
    • Feeney CJ, Frantseva MV, Carlen PL, et al. Vulnerability of glial cells to hydrogen peroxide in cultured hippocampal slices. Brain Res. 2008;1198:1-15.
    • (2008) Brain Res. , vol.1198 , pp. 1-15
    • Feeney, C.J.1    Frantseva, M.V.2    Carlen, P.L.3
  • 70
    • 0033697350 scopus 로고    scopus 로고
    • A new link between pesticides and Parkinson's disease
    • Giasson BI, Lee VM. A new link between pesticides and Parkinson's disease. Nat Neurosci. 2000;3(12):1227-1228.
    • (2000) Nat Neurosci. , vol.3 , Issue.12 , pp. 1227-1228
    • Giasson, B.I.1    Lee, V.M.2
  • 71
    • 84867629199 scopus 로고    scopus 로고
    • Non-motor symptoms in patients with Parkinson's disease-correlations with inflammatory cytokines in serum
    • Lindqvist D, Kaufman E, Brundin L, et al. Non-motor symptoms in patients with Parkinson's disease-correlations with inflammatory cytokines in serum. PLoS One. 2012;7(10):e47387.
    • (2012) PLoS One. , vol.7 , Issue.10
    • Lindqvist, D.1    Kaufman, E.2    Brundin, L.3
  • 72
    • 76749098103 scopus 로고    scopus 로고
    • Parkinson's disease: Mitochondrial damage control
    • Abeliovich A. Parkinson's disease: Mitochondrial damage control. Nature. 2010;463(7282):744-745.
    • (2010) Nature. , vol.463 , Issue.7282 , pp. 744-745
    • Abeliovich, A.1
  • 73
    • 84878472085 scopus 로고    scopus 로고
    • PINK1 and Parkin complementarily protect dopaminergic neurons in verte-brates
    • Matsui H, Gavinio R, Asano T, et al. PINK1 and Parkin complementarily protect dopaminergic neurons in verte-brates. Hum Mol Genet. 2013;22(12):2423-2434.
    • (2013) Hum Mol Genet. , vol.22 , Issue.12 , pp. 2423-2434
    • Matsui, H.1    Gavinio, R.2    Asano, T.3
  • 74
    • 84872183363 scopus 로고    scopus 로고
    • Deletion of Mthfd1l causes embryonic lethality and neural tube and craniofacial defects in mice
    • Momb J, Lewandowski JP, Bryant JD, et al. Deletion of Mthfd1l causes embryonic lethality and neural tube and craniofacial defects in mice. Proc Natl Acad Sci U S A. 2013;110(2):549-554.
    • (2013) Proc Natl Acad Sci U S A. , vol.110 , Issue.2 , pp. 549-554
    • Momb, J.1    Lewandowski, J.P.2    Bryant, J.D.3
  • 75
    • 84866004531 scopus 로고    scopus 로고
    • Elevated ferric, calcium and magnesium ions in the brain induce protein aggrega-tion in brain mitochondria
    • Alleyne T, Mohan N, Adogwa A. Elevated ferric, calcium and magnesium ions in the brain induce protein aggrega-tion in brain mitochondria. West Indian Med J. 2012;61(2): 122-127.
    • (2012) West Indian Med J. , vol.61 , Issue.2 , pp. 122-127
    • Alleyne, T.1    Mohan, N.2    Adogwa, A.3
  • 76
    • 84875679362 scopus 로고    scopus 로고
    • Mitochondria targeted therapeu-tic approaches in Parkinson's and Huntington's diseases
    • Chaturvedi RK, Beal MF. Mitochondria targeted therapeu-tic approaches in Parkinson's and Huntington's diseases. Mol Cell Neurosci. 2013;55:101-114.
    • (2013) Mol Cell Neurosci. , vol.55 , pp. 101-114
    • Chaturvedi, R.K.1    Beal, M.F.2
  • 77
    • 84875277277 scopus 로고    scopus 로고
    • Monogenic Parkinson's disease and Par-kinsonism: Clinical phenotypes and frequencies of known mutations
    • Puschmann A. Monogenic Parkinson's disease and Par-kinsonism: Clinical phenotypes and frequencies of known mutations. Parkinsonism Relat Disord. 2013; 19(4):407-415.
    • (2013) Parkinsonism Relat Disord. , vol.19 , Issue.4 , pp. 407-415
    • Puschmann, A.1
  • 78
    • 85173361704 scopus 로고    scopus 로고
    • Deregulation of gluta-mate dehydrogenase in human neurologic disorders
    • in press
    • Plaitakis A, Zaganas I, Spanaki C. Deregulation of gluta-mate dehydrogenase in human neurologic disorders. J Neurosci Res. in press.
    • J Neurosci Res.
    • Plaitakis, A.1    Zaganas, I.2    Spanaki, C.3
  • 79
    • 84875121203 scopus 로고    scopus 로고
    • Parkinson's Dis-ease: A complex interplay of mitochondrial DNA altera-tions and oxidative stress
    • Ciccone S, Maiani E, Bellusci G, et al. Parkinson's Dis-ease: a complex interplay of mitochondrial DNA altera-tions and oxidative stress. Int J Mol Sci. 2013;14(2): 2388-2409.
    • (2013) Int J Mol Sci. , vol.14 , Issue.2 , pp. 2388-2409
    • Ciccone, S.1    Maiani, E.2    Bellusci, G.3
  • 80
    • 84878646405 scopus 로고    scopus 로고
    • ER-stress-associated functional link between Parkin and DJ-1 via a transcrip-tional cascade involving the tumor suppressor p53 and the spliced X-box binding protein XBP-1
    • Duplan E, Giaime E, Viotti J, et al. ER-stress-associated functional link between Parkin and DJ-1 via a transcrip-tional cascade involving the tumor suppressor p53 and the spliced X-box binding protein XBP-1. J Cell Sci. 2013; 126(Pt 9):2124-2133.
    • (2013) J Cell Sci. , vol.126 , Issue.PART 9 , pp. 2124-2133
    • Duplan, E.1    Giaime, E.2    Viotti, J.3
  • 81
    • 84874322054 scopus 로고    scopus 로고
    • Characterization of PINK1 (PTEN-induced Putative Kinase 1) mutations associated with Parkinson disease in mammalian cells and Droso-phila
    • Song S, Jang S, Park J, et al. Characterization of PINK1 (PTEN-induced Putative Kinase 1) mutations associated with Parkinson disease in mammalian cells and Droso-phila. J Biol Chem. 2013;288(8):5660-5672.
    • (2013) J Biol Chem. , vol.288 , Issue.8 , pp. 5660-5672
    • Song, S.1    Jang, S.2    Park, J.3
  • 82
    • 84872401374 scopus 로고    scopus 로고
    • A subcellular analysis of genetic modulation of PINK1 on mitochondrial altera-tions, autophagy and cell death
    • Lenzi P, Marongiu R, Falleni A, et al. A subcellular analysis of genetic modulation of PINK1 on mitochondrial altera-tions, autophagy and cell death. Arch Ital Biol. 2012;150(2-3):194-217.
    • (2012) Arch Ital Biol. , vol.150 , Issue.2-3 , pp. 194-217
    • Lenzi, P.1    Marongiu, R.2    Falleni, A.3
  • 83
    • 84859702745 scopus 로고    scopus 로고
    • Differential effects of UCHL1 modulation on alpha-synuclein in PD-like models of alpha-synucleinopathy
    • Cartier AE, Ubhi K, Spencer B, et al. Differential effects of UCHL1 modulation on alpha-synuclein in PD-like models of alpha-synucleinopathy. PLoS One. 2012;7(4):e34713.
    • (2012) PLoS One. , vol.7 , Issue.4
    • Cartier, A.E.1    Ubhi, K.2    Spencer, B.3
  • 84
    • 84859776138 scopus 로고    scopus 로고
    • Excess α-synuclein worsens disease in mice lacking ubiquitin carboxy-terminal hydrolase L1
    • Shimshek DR, Schweizer T, Schmid P, et al. Excess α-synuclein worsens disease in mice lacking ubiquitin carboxy-terminal hydrolase L1. Sci Rep. 2012;2:262.
    • (2012) Sci Rep. , vol.2 , pp. 262
    • Shimshek, D.R.1    Schweizer, T.2    Schmid, P.3
  • 85
    • 84866696003 scopus 로고    scopus 로고
    • Cellular re-programming: A new approach to modelling Parkinson's disease
    • Hartfield EM, Fernandes HJ, Vowles J, et al. Cellular re-programming: a new approach to modelling Parkinson's disease. Biochem Soc Trans. 2012;40(5):1152-1157.
    • (2012) Biochem Soc Trans. , vol.40 , Issue.5 , pp. 1152-1157
    • Hartfield, E.M.1    Fernandes, H.J.2    Vowles, J.3
  • 86
    • 84875640261 scopus 로고    scopus 로고
    • Interplay of LRRK2 with chaperone-mediated autophagy
    • Orenstein SJ, Kuo SH, Tasset I, et al. Interplay of LRRK2 with chaperone-mediated autophagy. Nat Neurosci. 2013; 16(4):394-406.
    • (2013) Nat Neurosci. , vol.16 , Issue.4 , pp. 394-406
    • Orenstein, S.J.1    Kuo, S.H.2    Tasset, I.3
  • 87
    • 70349913868 scopus 로고    scopus 로고
    • Nur (R1) turing a notion on the etiopathoge-nesis of Parkinson's disease
    • Federoff HJ. Nur (R1) turing a notion on the etiopathoge-nesis of Parkinson's disease. Neurotox Res. 2009;16(3): 261-270.
    • (2009) Neurotox Res. , vol.16 , Issue.3 , pp. 261-270
    • Federoff, H.J.1
  • 88
    • 84863456841 scopus 로고    scopus 로고
    • Conditional expres-sion of Parkinson's disease-related mutant α-synuclein in the midbrain dopaminergic neurons causes progressive neurodegeneration and degradation of transcription factor nuclear receptor related 1
    • Lin X, Parisiadou L, Sgobio C, et al. Conditional expres-sion of Parkinson's disease-related mutant α-synuclein in the midbrain dopaminergic neurons causes progressive neurodegeneration and degradation of transcription factor nuclear receptor related 1. J Neurosci. 2012;32(27): 9248-9264.
    • (2012) J Neurosci. , vol.32 , Issue.27 , pp. 9248-9264
    • Lin, X.1    Parisiadou, L.2    Sgobio, C.3
  • 89
    • 82555192473 scopus 로고    scopus 로고
    • Novel variant Pro143Ala in HTRA2 contributes to Parkinson's disease by inducing hyperphosphorylation of HTRA2 protein in mitochondria
    • Lin CH, Chen ML, Chen GS, et al. Novel variant Pro143Ala in HTRA2 contributes to Parkinson's disease by inducing hyperphosphorylation of HTRA2 protein in mitochondria. Hum Genet. 2011;130(6):817-827.
    • (2011) Hum Genet. , vol.130 , Issue.6 , pp. 817-827
    • Lin, C.H.1    Chen, M.L.2    Chen, G.S.3
  • 90
    • 84863287993 scopus 로고    scopus 로고
    • Cerebrospinal fluid amy-loid β and tau in LRRK2 mutation carriers
    • Aasly JO, Shi M, Sossi V, et al. Cerebrospinal fluid amy-loid β and tau in LRRK2 mutation carriers. Neurology. 2012;78(1):55-61.
    • (2012) Neurology. , vol.78 , Issue.1 , pp. 55-61
    • Aasly, J.O.1    Shi, M.2    Sossi, V.3
  • 91
    • 79957596330 scopus 로고    scopus 로고
    • Disentangling the role of the tau gene locus in sporadic tauopathies
    • Vandrovcova J, Anaya F, Kay V, et al. Disentangling the role of the tau gene locus in sporadic tauopathies. Curr Alzheimer Res. 2010;7(8):726-734.
    • (2010) Curr Alzheimer Res. , vol.7 , Issue.8 , pp. 726-734
    • Vandrovcova, J.1    Anaya, F.2    Kay, V.3
  • 92
    • 84859421209 scopus 로고    scopus 로고
    • A mitochon-drial etiology of Alzheimer and Parkinson disease
    • Coskun P, Wyrembak J, Schriner SE, et al. A mitochon-drial etiology of Alzheimer and Parkinson disease. Bio-chim Biophys Acta. 2012;1820(5):553-564.
    • (2012) Bio-chim Biophys Acta. , vol.1820 , Issue.5 , pp. 553-564
    • Coskun, P.1    Wyrembak, J.2    Schriner, S.E.3
  • 93
    • 77953229747 scopus 로고    scopus 로고
    • Missing pieces in the Parkinson's disease puzzle
    • Obeso JA, Rodriguez-Oroz MC, Goetz CG, et al. Missing pieces in the Parkinson's disease puzzle. Nat Med. 2010;16(6):653-661.
    • (2010) Nat Med. , vol.16 , Issue.6 , pp. 653-661
    • Obeso, J.A.1    Rodriguez-Oroz, M.C.2    Goetz, C.G.3
  • 94
    • 84889772556 scopus 로고    scopus 로고
    • Prion-like mechanisms in epileptogenesis
    • in press
    • Orzi F, Casolla B, Rocchi R, et al. Prion-like mechanisms in epileptogenesis. Neurol Sci. in press.
    • Neurol Sci.
    • Orzi, F.1    Casolla, B.2    Rocchi, R.3
  • 95
    • 53149087460 scopus 로고    scopus 로고
    • Mitochondrial alterations in Parkinson's disease: New clues
    • Vila M, Ramonet D, Perier C. Mitochondrial alterations in Parkinson's disease: new clues. J Neurochem. 2008; 107(2):317-328.
    • (2008) J Neurochem. , vol.107 , Issue.2 , pp. 317-328
    • Vila, M.1    Ramonet, D.2    Perier, C.3
  • 96
    • 77957020116 scopus 로고    scopus 로고
    • Gene-environment interac-tions in Parkinson's disease: The importance of animal modeling
    • Horowitz MP, Greenamyre JT. Gene-environment interac-tions in Parkinson's disease: the importance of animal modeling. Clin Pharmacol Ther. 2010;88(4):467-474.
    • (2010) Clin Pharmacol Ther. , vol.88 , Issue.4 , pp. 467-474
    • Horowitz, M.P.1    Greenamyre, J.T.2
  • 97
    • 84868575932 scopus 로고    scopus 로고
    • Mitochondrial quality control mediated by PINK1 and Parkin: Links to Parkin-sonism
    • Narendra D, Walker JE, Youle R. Mitochondrial quality control mediated by PINK1 and Parkin: links to Parkin-sonism. Cold Spring Harb Perspect Biol. 2012;4(11). pii:a011338.
    • (2012) Cold Spring Harb Perspect Biol. , vol.4 , Issue.11
    • Narendra, D.1    Walker, J.E.2    Youle, R.3
  • 98
    • 21344456506 scopus 로고    scopus 로고
    • Intravesicular localization and exocytosis of alpha-synuclein and its aggregates
    • Lee HJ, Patel S, Lee SJ. Intravesicular localization and exocytosis of alpha-synuclein and its aggregates. J Neu-rosci. 2005;25(25):6016-6024.
    • (2005) J Neu-rosci. , vol.25 , Issue.25 , pp. 6016-6024
    • Lee, H.J.1    Patel, S.2    Lee, S.J.3
  • 99
    • 69249096578 scopus 로고    scopus 로고
    • Loss of parkin or PINK1 function increases Drp1-dependent mitochondrial frag-mentation
    • Lutz AK, Exner N, Fett ME, et al. Loss of parkin or PINK1 function increases Drp1-dependent mitochondrial frag-mentation. J Biol Chem. 2009;284(34):22938-22951.
    • (2009) J Biol Chem. , vol.284 , Issue.34 , pp. 22938-22951
    • Lutz, A.K.1    Exner, N.2    Fett, M.E.3
  • 100
    • 67650243261 scopus 로고    scopus 로고
    • Parkin-induced mitophagy in the pathogenesis of Parkinson disease
    • Narendra D, Tanaka A, Suen DF, et al. Parkin-induced mitophagy in the pathogenesis of Parkinson disease. Au-tophagy. 2009;5(5):706-708.
    • (2009) Au-tophagy. , vol.5 , Issue.5 , pp. 706-708
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3
  • 101
    • 84864928966 scopus 로고    scopus 로고
    • Oxidative stress in genetic mouse models of Parkinson's disease
    • Varçin M, Bentea E, Michotte Y, et al. Oxidative stress in genetic mouse models of Parkinson's disease. Oxid Med Cell Longev. 2012;2012:624925.
    • (2012) Oxid Med Cell Longev. , vol.2012 , pp. 624925
    • Varçin, M.1    Bentea, E.2    Michotte, Y.3
  • 102
    • 16844366080 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and its role in motor neuron degeneration in ALS
    • Manfredi G, Xu Z. Mitochondrial dysfunction and its role in motor neuron degeneration in ALS. Mitochondrion. 2005;5(2):77-87.
    • (2005) Mitochondrion. , vol.5 , Issue.2 , pp. 77-87
    • Manfredi, G.1    Xu, Z.2
  • 103
    • 84863644562 scopus 로고    scopus 로고
    • Recent advances in the treatment of neurodegenerative diseases based on GSH delivery systems
    • Cacciatore I, Baldassarre L, Fornasari E, et al. Recent advances in the treatment of neurodegenerative diseases based on GSH delivery systems. Oxid Med Cell Longev. 2012;2012:240146.
    • (2012) Oxid Med Cell Longev. , vol.2012 , pp. 240146
    • Cacciatore, I.1    Baldassarre, L.2    Fornasari, E.3
  • 104
    • 84875472017 scopus 로고    scopus 로고
    • The role of free radicals in the aging brain and Parkinson's disease: Convergence and parallelism
    • Kumar H, Lim HW, More SV, et al. The role of free radicals in the aging brain and Parkinson's disease: convergence and parallelism. Int J Mol Sci. 2012;13(8):10478-10504.
    • (2012) Int J Mol Sci. , vol.13 , Issue.8 , pp. 10478-10504
    • Kumar, H.1    Lim, H.W.2    More, S.V.3
  • 105
    • 84864340580 scopus 로고    scopus 로고
    • Mitochondrial dys-function and oxidative stress promote apoptotic cell death in the striatum via cytochrome c/caspase-3 signaling cascade following chronic rotenone intoxication in rats
    • Lin TK, Cheng CH, Chen SD, et al. Mitochondrial dys-function and oxidative stress promote apoptotic cell death in the striatum via cytochrome c/caspase-3 signaling cascade following chronic rotenone intoxication in rats. Int J Mol Sci. 2012;13(7):8722-8739.
    • (2012) Int J Mol Sci. , vol.13 , Issue.7 , pp. 8722-8739
    • Lin, T.K.1    Cheng, C.H.2    Chen, S.D.3
  • 106
    • 37049004489 scopus 로고    scopus 로고
    • Mitochondria in the aetiology and patho-genesis of Parkinson's disease
    • Schapira, AH. Mitochondria in the aetiology and patho-genesis of Parkinson's disease. Lancet Neurol. 2008;7(1): 97-109.
    • (2008) Lancet Neurol. , vol.7 , Issue.1 , pp. 97-109
    • Schapira, A.H.1
  • 107
    • 0027164824 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen DR. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 1993;364(6435):362.
    • (1993) Nature. , vol.364 , Issue.6435 , pp. 362
    • Rosen, D.R.1
  • 108
    • 33748795566 scopus 로고    scopus 로고
    • Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials
    • Ferri A, Cozzolino M, Crosio C, et al. Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials. Proc Natl Acad Sci U S A. 2006; 103(37):13860-13865.
    • (2006) Proc Natl Acad Sci U S A. , vol.103 , Issue.37 , pp. 13860-13865
    • Ferri, A.1    Cozzolino, M.2    Crosio, C.3
  • 109
    • 33846087291 scopus 로고    scopus 로고
    • Mitochondrial alterations in the spinal cord of patients with sporadic amyotrophic lateral sclerosis
    • Sasaki S, Iwata M. Mitochondrial alterations in the spinal cord of patients with sporadic amyotrophic lateral sclerosis. J Neuropathol Exp Neurol. 2007;66(1):10-16.
    • (2007) J Neuropathol Exp Neurol. , vol.66 , Issue.1 , pp. 10-16
    • Sasaki, S.1    Iwata, M.2
  • 110
    • 23644462197 scopus 로고    scopus 로고
    • Ultrastructural study of aggregates in the spinal cord of transgenic mice with a G93A mutant SOD1 gene
    • Sasaki S, Warita H, Murakami T, et al. Ultrastructural study of aggregates in the spinal cord of transgenic mice with a G93A mutant SOD1 gene. Acta Neuropathol. 2005;109(3):247-255.
    • (2005) Acta Neuropathol. , vol.109 , Issue.3 , pp. 247-255
    • Sasaki, S.1    Warita, H.2    Murakami, T.3
  • 111
    • 77955961922 scopus 로고    scopus 로고
    • Misfolded mutant SOD1 directly inhibits VDAC1 conductance in a mouse model of inherited ALS
    • Israelson A, Arbel N, Da Cruz S, et al. Misfolded mutant SOD1 directly inhibits VDAC1 conductance in a mouse model of inherited ALS. Neuron. 2010;67(4):575-587.
    • (2010) Neuron. , vol.67 , Issue.4 , pp. 575-587
    • Israelson, A.1    Arbel, N.2    Da Cruz, S.3
  • 112
    • 66749104344 scopus 로고    scopus 로고
    • Mitochondrial function, morphol-ogy, and axonal transport in amyotrophic lateral sclerosis
    • Magrané J, Manfredi G. Mitochondrial function, morphol-ogy, and axonal transport in amyotrophic lateral sclerosis. Antioxid Redox Signal. 2009;11(7):1615-1626.
    • (2009) Antioxid Redox Signal. , vol.11 , Issue.7 , pp. 1615-1626
    • Magrané, J.1    Manfredi, G.2
  • 113
    • 77956183828 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and intracellular calcium dysregulation in ALS
    • Kawamata H, Manfredi G. Mitochondrial dysfunction and intracellular calcium dysregulation in ALS. Mech Ageing Dev. 2010;131(7-8):517-526.
    • (2010) Mech Ageing Dev. , vol.131 , Issue.7-8 , pp. 517-526
    • Kawamata, H.1    Manfredi, G.2
  • 114
    • 58149234264 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis linked to a novel SOD1 mutation with muscle mitochondrial dysfunction
    • Corti S, Donadoni C, Ronchi D, et al. Amyotrophic lateral sclerosis linked to a novel SOD1 mutation with muscle mitochondrial dysfunction. J Neurol Sci. 2009;276(1-2): 170-174.
    • (2009) J Neurol Sci. , vol.276 , Issue.1-2 , pp. 170-174
    • Corti, S.1    Donadoni, C.2    Ronchi, D.3
  • 115
    • 0036176613 scopus 로고    scopus 로고
    • Mitochondrial involve-ment in amyotrophic lateral sclerosis
    • Menzies FM, Ince PG, Shaw PJ. Mitochondrial involve-ment in amyotrophic lateral sclerosis. Neurochem Int. 2002;40(6):543-551.
    • (2002) Neurochem Int. , vol.40 , Issue.6 , pp. 543-551
    • Menzies, F.M.1    Ince, P.G.2    Shaw, P.J.3
  • 116
    • 36348993804 scopus 로고    scopus 로고
    • Mitochondrial alterations in dorsal root ganglion cells in sporadic amyotrophic lateral sclerosis
    • Sasaki S, Horie Y, Iwata M. Mitochondrial alterations in dorsal root ganglion cells in sporadic amyotrophic lateral sclerosis. Acta Neuropathol. 2007;114 (6):633-639.
    • (2007) Acta Neuropathol. , vol.114 , Issue.6 , pp. 633-639
    • Sasaki, S.1    Horie, Y.2    Iwata, M.3
  • 117
    • 27544484846 scopus 로고    scopus 로고
    • Are mitochondria critical in the pa-thogenesis of Alzheimer's disease?
    • Reddy PH, Beal MF. Are mitochondria critical in the pa-thogenesis of Alzheimer's disease? Brain Res Brain Res Rev. 2005;49(3):618-632.
    • (2005) Brain Res Brain Res Rev. , vol.49 , Issue.3 , pp. 618-632
    • Reddy, P.H.1    Beal, M.F.2
  • 118
    • 84872127080 scopus 로고    scopus 로고
    • Adaptive down-regulation of mitochondrial function in down syn-drome
    • Helguera P, Seiglie J, Rodriguez J, et al. Adaptive down-regulation of mitochondrial function in down syn-drome. Cell Metab. 2013;17(1):132-140.
    • (2013) Cell Metab. , vol.17 , Issue.1 , pp. 132-140
    • Helguera, P.1    Seiglie, J.2    Rodriguez, J.3
  • 119
    • 84866395321 scopus 로고    scopus 로고
    • Mi-tochondrial DNA damage is associated with reduced mi-tochondrial bioenergetics in Huntington's disease
    • Siddiqui A, Rivera-Sánchez S, Castro Mdel R, et al. Mi-tochondrial DNA damage is associated with reduced mi-tochondrial bioenergetics in Huntington's disease. Free Radic Biol Med. 2012;53(7):1478-1488.
    • (2012) Free Radic Biol Med. , vol.53 , Issue.7 , pp. 1478-1488
    • Siddiqui, A.1    Rivera-Sánchez, S.2    Castro Mdel, R.3
  • 120
    • 84856518837 scopus 로고    scopus 로고
    • Rapamycin re-duces oxidative stress in frataxin-deficient yeast cells
    • Marobbio CM, Pisano I, Porcelli V, et al. Rapamycin re-duces oxidative stress in frataxin-deficient yeast cells. Mitochondrion. 2012;12(1):156-161.
    • (2012) Mitochondrion. , vol.12 , Issue.1 , pp. 156-161
    • Marobbio, C.M.1    Pisano, I.2    Porcelli, V.3
  • 121
    • 84867637537 scopus 로고    scopus 로고
    • Novel frataxin isoforms may contribute to the pathological mechanism of friedreich ataxia
    • Xia H, Cao Y, Dai X, et al. Novel frataxin isoforms may contribute to the pathological mechanism of friedreich ataxia. PLoS One. 2012;7(10):e47847.
    • (2012) PLoS One. , vol.7 , Issue.10
    • Xia, H.1    Cao, Y.2    Dai, X.3
  • 122
    • 77954930779 scopus 로고    scopus 로고
    • Friedreich ataxia: Molecular mechanisms, redox considerations, and thera-peutic opportunities
    • Santos R, Lefevre S, Sliwa D, et al. Friedreich ataxia: molecular mechanisms, redox considerations, and thera-peutic opportunities. Antioxid Redox Signal. 2010;13(5): 651-690.
    • (2010) Antioxid Redox Signal. , vol.13 , Issue.5 , pp. 651-690
    • Santos, R.1    Lefevre, S.2    Sliwa, D.3
  • 123
    • 56049088295 scopus 로고    scopus 로고
    • Coenzyme Q10 and vitamin E deficiency in Friedreich's ataxia: Predictor of efficacy of vitamin E and coenzyme Q10 therapy
    • Cooper JM, Korlipara LV, Hart PE, et al. Coenzyme Q10 and vitamin E deficiency in Friedreich's ataxia: predictor of efficacy of vitamin E and coenzyme Q10 therapy. Eur J Neurol. 2008;15(12):1371-1379.
    • (2008) Eur J Neurol. , vol.15 , Issue.12 , pp. 1371-1379
    • Cooper, J.M.1    Korlipara, L.V.2    Hart, P.E.3
  • 124
    • 46349110018 scopus 로고    scopus 로고
    • Targeting lipophilic cations to mitochondria
    • Murphy MP. Targeting lipophilic cations to mitochondria. Biochim Biophys Acta. 2008;1777(7-8):1028-1031.
    • (2008) Biochim Biophys Acta. , vol.1777 , Issue.7-8 , pp. 1028-1031
    • Murphy, M.P.1
  • 125
    • 71849088759 scopus 로고    scopus 로고
    • Mitochondria: A thera-peutic target in neurodegeneration
    • Moreira PI, Zhu X, Wang X, et al. Mitochondria: a thera-peutic target in neurodegeneration. Biochim Biophys Acta. 2010;1802(1):212-220.
    • (2010) Biochim Biophys Acta. , vol.1802 , Issue.1 , pp. 212-220
    • Moreira, P.I.1    Zhu, X.2    Wang, X.3
  • 126
    • 80455174241 scopus 로고    scopus 로고
    • Neuropro-tective role of dopamine agonists: Evidence from animal models and clinical studies
    • Herrero MT, Pagonabarraga J, Linazasoro G. Neuropro-tective role of dopamine agonists: evidence from animal models and clinical studies. Neurologist. 2011;17(6 Suppl 1):S54-66.
    • (2011) Neurologist. , vol.17 , Issue.6 SUPPL. 1
    • Herrero, M.T.1    Pagonabarraga, J.2    Linazasoro, G.3


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