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Volumn 12, Issue 6, 2011, Pages 790-799

Mitophagy in neurodegeneration: An opportunity for therapy?

Author keywords

Alzheimer's disease; Mitochondrial dysfunction; Mitophagy; Parkinson's disease; Potential therapy

Indexed keywords

ALZHEIMER DISEASE; AUTOPHAGY; DISORDERS OF MITOCHONDRIAL FUNCTIONS; HUMAN; MOLECULAR BIOLOGY; NERVE DEGENERATION; NONHUMAN; PARKINSON DISEASE; REVIEW;

EID: 79955585040     PISSN: 13894501     EISSN: None     Source Type: Journal    
DOI: 10.2174/138945011795528813     Document Type: Review
Times cited : (28)

References (124)
  • 1
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • Newmeyer DD, Ferguson-Miller S. Mitochondria: releasing power for life and unleashing the machineries of death. Cell 2003; 112: 481-90.
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 2
    • 65449139544 scopus 로고    scopus 로고
    • Mitochondria, calcium and cell death: A deadly triad in neurodegeneration
    • Celsi F, Pizzo P, Brini M, et al. Mitochondria, calcium and cell death: a deadly triad in neurodegeneration. Biochim Biophys Acta 2009; 1787: 335-44.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 335-344
    • Celsi, F.1    Pizzo, P.2    Brini, M.3
  • 3
    • 67649687039 scopus 로고    scopus 로고
    • An integrative view of the role of oxidative stress, mitochondria and insulin in Alzheimer's disease
    • Moreira PI, Duarte AI, Santos MS, Rego AC, Oliveira CR. An integrative view of the role of oxidative stress, mitochondria and insulin in Alzheimer's disease. J Alzheimers Dis 2009; 16: 741-61.
    • (2009) J Alzheimers Dis , vol.16 , pp. 741-761
    • Moreira, P.I.1    Duarte, A.I.2    Santos, M.S.3    Rego, A.C.4    Oliveira, C.R.5
  • 4
    • 64949161526 scopus 로고    scopus 로고
    • Respiratory function decline and DNA mutation in mitochondria, oxidative stress and altered gene expression during aging
    • Wei YH, Wu SB, Ma YS, Lee HC. Respiratory function decline and DNA mutation in mitochondria, oxidative stress and altered gene expression during aging. Chang Gung Med J. 2009; 32: 113-32.
    • (2009) Chang Gung Med J. , vol.32 , pp. 113-132
    • Wei, Y.H.1    Wu, S.B.2    Ma, Y.S.3    Lee, H.C.4
  • 5
    • 13944278132 scopus 로고    scopus 로고
    • Mtiochondria oxidants and aging
    • Balaban RS, Nemoto S, Finkel T. Mtiochondria oxidants and aging. Cell 2005; 120: 483-95.
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 6
    • 0142213542 scopus 로고    scopus 로고
    • The free radical theory of aging
    • Harman D. The free radical theory of aging. Antioxid Redox Signal 2003; 5: 557-61.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 557-561
    • Harman, D.1
  • 7
    • 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: 787-95.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 8
    • 33745192802 scopus 로고    scopus 로고
    • Supression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara T, Nakamura K, Matsui M, et al. Supression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 2006; 441: 885-889.
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3
  • 9
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu M, Waguri S, Chiba T, et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 2006; 441: 880-84.
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3
  • 10
    • 70449727080 scopus 로고    scopus 로고
    • Autophagy promotes synapse development in Drosophila
    • Shen W, Ganetzky B. Autophagy promotes synapse development in Drosophila. J Cell Biol 2009; 187: 71-9.
    • (2009) J Cell Biol , vol.187 , pp. 71-79
    • Shen, W.1    Ganetzky, B.2
  • 11
    • 69949180640 scopus 로고    scopus 로고
    • TOR-mediated autophagy regulates cell death in Drosophila neurodegenerative disease
    • Wang T, Lao U, Edgar BA. TOR-mediated autophagy regulates cell death in Drosophila neurodegenerative disease. J Cell Biol 2009; 186: 703-11.
    • (2009) J Cell Biol , vol.186 , pp. 703-711
    • Wang, T.1    Lao, U.2    Edgar, B.A.3
  • 12
    • 48249103491 scopus 로고    scopus 로고
    • Neurodegenerative lysosomal disorders: A continuum from development to late age
    • Nixon RA, Yang DS, Lee JH. Neurodegenerative lysosomal disorders: a continuum from development to late age. Autophagy 2008; 4-5: 590-99.
    • (2008) Autophagy , vol.4-5 , pp. 590-599
    • Nixon, R.A.1    Yang, D.S.2    Lee, J.H.3
  • 13
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: From phenomenology to molecular understanding in less than a decade
    • Klionsky DJ. Autophagy: from phenomenology to molecular understanding in less than a decade. Nat Rev Mol Cell Biol 2007; 8: 931-7.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 931-937
    • Klionsky, D.J.1
  • 14
    • 58149084405 scopus 로고    scopus 로고
    • Ordered organelle degradation during starvation-induced autophagy
    • Kristensen AR, Schandorff S, Høyer-Hansen M, et al. Ordered organelle degradation during starvation-induced autophagy. Mol Cell Proteom 2008; 7: 2419-28.
    • (2008) Mol Cell Proteom , vol.7 , pp. 2419-2428
    • Kristensen, A.R.1    Schandorff, S.2    Høyer-Hansen, M.3
  • 15
    • 0000189281 scopus 로고
    • Cellular differentiation in the kidneys of newborn mice studied with the electron microscope
    • Clark SL Jr. Cellular differentiation in the kidneys of newborn mice studied with the electron microscope. J Biophys Biochem Cytol 1957; 3: 349-62.
    • (1957) J Biophys Biochem Cytol , vol.3 , pp. 349-362
    • Clark Jr., S.L.1
  • 16
    • 0000730374 scopus 로고
    • Cytoplasmic components in hepatic cell lysosomes
    • Ashford TP, Porter KR. Cytoplasmic components in hepatic cell lysosomes. J Cell Biol 1962; 12: 198-202.
    • (1962) J Cell Biol , vol.12 , pp. 198-202
    • Ashford, T.P.1    Porter, K.R.2
  • 17
    • 16844366524 scopus 로고    scopus 로고
    • Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging
    • Lemasters JJ. Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging. Rejuvenation Res 2005; 8: 3-5.
    • (2005) Rejuvenation Res , vol.8 , pp. 3-5
    • Lemasters, J.J.1
  • 18
    • 33745866310 scopus 로고    scopus 로고
    • Autophagic stress in neuronal injury and disease
    • Chu CT. Autophagic stress in neuronal injury and disease. J Neuropathol Exp Neurol 2006; 65: 423-32.
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 423-432
    • Chu, C.T.1
  • 19
    • 44149124887 scopus 로고    scopus 로고
    • Autophagy in neuroprotection and neurodegeneration: A question of balance
    • Cherra III SJ, Chu CT. Autophagy in neuroprotection and neurodegeneration: a question of balance. Future Neurol 2008; 3: 309-23.
    • (2008) Future Neurol , vol.3 , pp. 309-323
    • Cherra III, S.J.1    Chu, C.T.2
  • 20
    • 41749114288 scopus 로고    scopus 로고
    • Autophagy: Basic principles and relevance to disease
    • Kundu M, Thompson CB. Autophagy: basic principles and relevance to disease. Annu Rev Pathol Mech Dis 2008; 3: 427-55.
    • (2008) Annu Rev Pathol Mech Dis , vol.3 , pp. 427-455
    • Kundu, M.1    Thompson, C.B.2
  • 21
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: Core machinery and adaptations
    • Xie Z, Klonsky DJ. Autophagosome formation: core machinery and adaptations. Nat Cell Biol 2007; 9: 1102-9.
    • (2007) Nat Cell Biol , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klonsky, D.J.2
  • 22
    • 48949098967 scopus 로고    scopus 로고
    • New insights into the mechanisms of macroautophagy in mammalian cells
    • Eskelinen E-L. New insights into the mechanisms of macroautophagy in mammalian cells. Int Rev Cell Mol Biol 2008; 266: 207-47.
    • (2008) Int Rev Cell Mol Biol , vol.266 , pp. 207-247
    • Eskelinen, E.-L.1
  • 24
    • 57849136841 scopus 로고    scopus 로고
    • Autophagy: Principles and significance in health and disease
    • Todde V, Veenhuis M, van der Klei IJ. Autophagy: principles and significance in health and disease. Biochim Biophys Acta 2009; 1792: 3-13.
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 3-13
    • Todde, V.1    Veenhuis, M.2    van der Klei, I.J.3
  • 25
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • Yamamoto A, Tagawa Y, Yoshimori T, Moriyama Y, Masaki R, Tashiro Y. Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct Funct 1998; 23: 33-42.
    • (1998) Cell Struct Funct , vol.23 , pp. 33-42
    • Yamamoto, A.1    Tagawa, Y.2    Yoshimori, T.3    Moriyama, Y.4    Masaki, R.5    Tashiro, Y.6
  • 26
    • 7244255989 scopus 로고    scopus 로고
    • Role for Rab7 in maturation of late autophagic vacuoles
    • Jager S, Bucci C, Tanida I, et al. Role for Rab7 in maturation of late autophagic vacuoles. J Cell Sci 2004; 117: 4837-48.
    • (2004) J Cell Sci , vol.117 , pp. 4837-4848
    • Jager, S.1    Bucci, C.2    Tanida, I.3
  • 27
    • 26844531363 scopus 로고    scopus 로고
    • Maturation of autophagic vacuoles in mammalian cells
    • Eskelinen E-L. Maturation of autophagic vacuoles in mammalian cells. Autophagy 2005; 1: 1-10.
    • (2005) Autophagy , vol.1 , pp. 1-10
    • Eskelinen, E.-L.1
  • 28
    • 4644273585 scopus 로고    scopus 로고
    • Uth1p is involved in the autophagic degradation of mitochondria
    • Kissova I, Deffieu M, Manon S, Camougrand N. Uth1p is involved in the autophagic degradation of mitochondria. J Biol Chem 2004; 279: 39068-74.
    • (2004) J Biol Chem , vol.279 , pp. 39068-39074
    • Kissova, I.1    Deffieu, M.2    Manon, S.3    Camougrand, N.4
  • 29
    • 34247172582 scopus 로고    scopus 로고
    • Aup1p, a yeast mitochondrial protein phosphatase homolog, is required for efficient stationary phase mitophagy and cell survival
    • Tal R, Winter G, Ecker N, Klionsky DJ, Abeliovich H. Aup1p, a yeast mitochondrial protein phosphatase homolog, is required for efficient stationary phase mitophagy and cell survival. J Biol Chem 2007; 282: 5617-24.
    • (2007) J Biol Chem , vol.282 , pp. 5617-5624
    • Tal, R.1    Winter, G.2    Ecker, N.3    Klionsky, D.J.4    Abeliovich, H.5
  • 30
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • Kanki T, Wang K, Cao Y, Baba M, Klionsky DJ. Atg32 is a mitochondrial protein that confers selectivity during mitophagy. Dev Cell 2009; 17: 98-109.
    • (2009) Dev Cell , vol.17 , pp. 98-109
    • Kanki, T.1    Wang, K.2    Cao, Y.3    Baba, M.4    Klionsky, D.J.5
  • 31
    • 57749121573 scopus 로고    scopus 로고
    • Mitophagy in yeast occurs through a selective mechanism
    • Kanki T, Klionsky DJ. Mitophagy in yeast occurs through a selective mechanism. J Biol Chem 2008; 283: 32386-93.
    • (2008) J Biol Chem , vol.283 , pp. 32386-32393
    • Kanki, T.1    Klionsky, D.J.2
  • 32
    • 67650246357 scopus 로고    scopus 로고
    • Mitochondriaanchored receptor Atg32 mediates degradation of mitochondria via selective autophagy
    • Okamoto K, Kondo-Okamoto N, Ohsumi Y. Mitochondriaanchored receptor Atg32 mediates degradation of mitochondria via selective autophagy. Dev Cell 2009; 17: 87-97.
    • (2009) Dev Cell , vol.17 , pp. 87-97
    • Okamoto, K.1    Kondo-Okamoto, N.2    Ohsumi, Y.3
  • 35
    • 34250811414 scopus 로고    scopus 로고
    • The role of autophagy in mitochondria maintenance: Characterization of mitochondrial functions in autophagy-deficient S. cerevisiae strains
    • Zhang Y, Qi H, Taylor R, Xu W, Liu LF, Jin S. The role of autophagy in mitochondria maintenance: characterization of mitochondrial functions in autophagy-deficient S. cerevisiae strains. Autophagy 2007; 3: 337-46.
    • (2007) Autophagy , vol.3 , pp. 337-346
    • Zhang, Y.1    Qi, H.2    Taylor, R.3    Xu, W.4    Liu, L.F.5    Jin, S.6
  • 36
    • 36549002757 scopus 로고    scopus 로고
    • Giant mitochondria do not fuse and exchange their contents with normal mitochondria
    • Navratil M, Terman A, Arriaga EA. Giant mitochondria do not fuse and exchange their contents with normal mitochondria. Exp Cell Res 2008; 314: 164-72.
    • (2008) Exp Cell Res , vol.314 , pp. 164-172
    • Navratil, M.1    Terman, A.2    Arriaga, E.A.3
  • 37
    • 38549110110 scopus 로고    scopus 로고
    • Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
    • Twig G, Elorza A, Molina AJ, et al. Fission and selective fusion govern mitochondrial segregation and elimination by autophagy. EMBO J 2008; 27: 433-46.
    • (2008) EMBO J , vol.27 , pp. 433-446
    • Twig, G.1    Elorza, A.2    Molina, A.J.3
  • 38
    • 0034938453 scopus 로고    scopus 로고
    • Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria
    • Ono T, Isobe K, Nakada K, Hayashi JI. Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria. Nat Genet 2001; 28: 272-5.
    • (2001) Nat Genet , vol.28 , pp. 272-275
    • Ono, T.1    Isobe, K.2    Nakada, K.3    Hayashi, J.I.4
  • 39
    • 0035487007 scopus 로고    scopus 로고
    • The mitochondrial permeability transition initiates autophagy in rat hepatocytes
    • Elmore SP, Qian T, Grissom SF, Lemasters JJ. The mitochondrial permeability transition initiates autophagy in rat hepatocytes. FASEB J 2001; 15: 2286-7.
    • (2001) FASEB J , vol.15 , pp. 2286-2287
    • Elmore, S.P.1    Qian, T.2    Grissom, S.F.3    Lemasters, J.J.4
  • 41
    • 54049138387 scopus 로고    scopus 로고
    • Mechanisms of neuronal death in disease: Defining the models and the players
    • Ribe EM, Serrano-Saiz E, Akpan N, Troy CM. Mechanisms of neuronal death in disease: defining the models and the players. Biochem J 2008; 415: 165-82.
    • (2008) Biochem J , vol.415 , pp. 165-182
    • Ribe, E.M.1    Serrano-Saiz, E.2    Akpan, N.3    Troy, C.M.4
  • 42
    • 58149376131 scopus 로고    scopus 로고
    • Coenzyme Q deficiency triggers mitochondria degradation by mitophagy
    • Rodríguez-Hernández A, Cordero MD, Salviati L, et al. Coenzyme Q deficiency triggers mitochondria degradation by mitophagy. Autophagy 2009; 5: 19-32.
    • (2009) Autophagy , vol.5 , pp. 19-32
    • Rodríguez-Hernández, A.1    Cordero, M.D.2    Salviati, L.3
  • 44
    • 34249821079 scopus 로고    scopus 로고
    • Brain mitochondrial dysfunction as a link between Alzheimer's disease and diabetes
    • Moreira PI, Santos MS, Seiça R, Oliveira CR. Brain mitochondrial dysfunction as a link between Alzheimer's disease and diabetes. J Neurol Sci 2007; 257: 206-14.
    • (2007) J Neurol Sci , vol.257 , pp. 206-214
    • Moreira, P.I.1    Santos, M.S.2    Seiça, R.3    Oliveira, C.R.4
  • 45
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP. How mitochondria produce reactive oxygen species. Biochem J 2009; 417: 1-13.
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 46
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W. Free radicals in the physiological control of cell function. Physiol Rev 2002; 82: 47-95.
    • (2002) Physiol Rev , vol.82 , pp. 47-95
    • Droge, W.1
  • 47
    • 35848932278 scopus 로고    scopus 로고
    • Signaling functions of free radicals superoxide & nitric oxide under physiological & pathological conditions
    • Afanas'ev IB. Signaling functions of free radicals superoxide & nitric oxide under physiological & pathological conditions. Mol Biotechnol 2007; 37: 2-4.
    • (2007) Mol Biotechnol , vol.37 , pp. 2-4
    • Afanas'ev, I.B.1
  • 49
    • 57649233079 scopus 로고    scopus 로고
    • The role of mitochondria in reactive oxygen species metabolism and signaling
    • Starkov AA. The role of mitochondria in reactive oxygen species metabolism and signaling. Ann NY Acad Sci 2008; 1147: 37-52.
    • (2008) Ann NY Acad Sci , vol.1147 , pp. 37-52
    • Starkov, A.A.1
  • 51
    • 0025353255 scopus 로고
    • Neurotransmitter release
    • Zimmermann H. Neurotransmitter release. FEBS Lett 1990; 268: 394-99.
    • (1990) FEBS Lett , vol.268 , pp. 394-399
    • Zimmermann, H.1
  • 53
    • 0034668946 scopus 로고    scopus 로고
    • Mitochondria as all-round players of the calcium game
    • Rizzuto R, Bernardi P, Pozzan T. Mitochondria as all-round players of the calcium game. J Physiol 2000; 529: 37-47.
    • (2000) J Physiol , vol.529 , pp. 37-47
    • Rizzuto, R.1    Bernardi, P.2    Pozzan, T.3
  • 54
    • 0033153535 scopus 로고    scopus 로고
    • Calcium-and activity-dependent synaptic plasticity
    • Zucker RS. Calcium-and activity-dependent synaptic plasticity. Curr Opin Neurobiol 1999; 9: 305-13.
    • (1999) Curr Opin Neurobiol , vol.9 , pp. 305-313
    • Zucker, R.S.1
  • 55
    • 0034043203 scopus 로고    scopus 로고
    • CaM-kinases: Modulators of synaptic plasticity
    • Soderling TR. CaM-kinases: modulators of synaptic plasticity. Curr Opin Neurobiol 2000; 10: 375-80.
    • (2000) Curr Opin Neurobiol , vol.10 , pp. 375-380
    • Soderling, T.R.1
  • 57
    • 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: 575-90.
    • (2008) IUBMB Life , vol.60 , pp. 575-590
    • Wojda, U.1    Salinska, E.2    Kuznicki, J.3
  • 59
    • 34648831384 scopus 로고    scopus 로고
    • Alzheimer's disease: A lesson from mitochondrial dysfunction
    • Moreira PI, Santos MS, Oliveira CR. Alzheimer's disease: a lesson from mitochondrial dysfunction. Antioxid Redox Signal 2007; 9: 1621-30.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 1621-1630
    • Moreira, P.I.1    Santos, M.S.2    Oliveira, C.R.3
  • 60
    • 33746237577 scopus 로고    scopus 로고
    • To be or not to be toxic: Aggregates in Huntington and Alzheimer disease
    • Slow EJ, Graham RK, Hayden MR. To be or not to be toxic: aggregates in Huntington and Alzheimer disease. Trends Genet 2006; 22: 408-11.
    • (2006) Trends Genet , vol.22 , pp. 408-411
    • Slow, E.J.1    Graham, R.K.2    Hayden, M.R.3
  • 61
    • 33644861975 scopus 로고    scopus 로고
    • Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis
    • Glabe CG, Kayed R. Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis. Neurology 2006; 66: S74-78.
    • (2006) Neurology , vol.66
    • Glabe, C.G.1    Kayed, R.2
  • 62
    • 0034052607 scopus 로고    scopus 로고
    • Oxidative insults are associated with apolipoprotein E genotype in Alzheimer's disease brain
    • Ramassamy C, Averill D, Beffert U, et al. Oxidative insults are associated with apolipoprotein E genotype in Alzheimer's disease brain. Neurobiol Dis 2000; 7: 23-37.
    • (2000) Neurobiol Dis , vol.7 , pp. 23-37
    • Ramassamy, C.1    Averill, D.2    Beffert, U.3
  • 63
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-_ in Alzheimer's disease
    • LaFerla FM, Green KN, Oddo S. Intracellular amyloid-_ in Alzheimer's disease. Nat Rev Neurosci 2007; 8: 499-509.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • LaFerla, F.M.1    Green, K.N.2    Oddo, S.3
  • 64
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid _-peptide
    • Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid _-peptide. Nat Rev Mol Cell Biol 2007; 8: 101-12.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 65
    • 0026408619 scopus 로고
    • Cytochrome oxidase deficiency in Alzheimer's disease
    • Parker Jr. WD. Cytochrome oxidase deficiency in Alzheimer's disease. Ann NY Acad Sci 1991; 640: 59-64.
    • (1991) Ann NY Acad Sci , vol.640 , pp. 59-64
    • Parker Jr., W.D.1
  • 66
    • 0034612075 scopus 로고    scopus 로고
    • A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients
    • Maurer I, Zierz S, Moller HJ. A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients. Neurobiol Aging 2000; 21: 455-62.
    • (2000) Neurobiol Aging , vol.21 , pp. 455-462
    • Maurer, I.1    Zierz, S.2    Moller, H.J.3
  • 67
    • 0034923434 scopus 로고    scopus 로고
    • Oxidative damage is the earliest event in Alzheimer disease
    • Nunomura A, Perry G, Aliev G, et al. Oxidative damage is the earliest event in Alzheimer disease. J Neuropathol Exp Neurol 2001; 60: 759-67.
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 759-767
    • Nunomura, A.1    Perry, G.2    Aliev, G.3
  • 68
    • 27544484846 scopus 로고    scopus 로고
    • Are mitochondria critical in the pathogenesis of Alzheimer's disease?
    • Reddy PH, Beal MF. Are mitochondria critical in the pathogenesis of Alzheimer's disease? Brain Res Brain Res Rev 2005; 49: 618-32.
    • (2005) Brain Res Brain Res Rev , vol.49 , pp. 618-632
    • Reddy, P.H.1    Beal, M.F.2
  • 69
    • 33746256557 scopus 로고    scopus 로고
    • Mitochondrial alterations in Alzheimer's disease
    • Baloyannis SJ. Mitochondrial alterations in Alzheimer's disease. J Alzheimers Dis 2006; 9: 119-26.
    • (2006) J Alzheimers Dis , vol.9 , pp. 119-126
    • Baloyannis, S.J.1
  • 70
    • 43849096294 scopus 로고    scopus 로고
    • Brain oxidative stress in a triple-transgenic mouse model of Alzheimer disease
    • Resende R, Moreira PI, Proença T, et al. Brain oxidative stress in a triple-transgenic mouse model of Alzheimer disease. Free Radic Biol Med 2008; 44: 2051-7.
    • (2008) Free Radic Biol Med , vol.44 , pp. 2051-2057
    • Resende, R.1    Moreira, P.I.2    Proença, T.3
  • 71
    • 35348923542 scopus 로고    scopus 로고
    • Cytochrome c oxidase deficiency in neurons decreases both oxidative stress and amyloid formation in a mouse model of Alzheimer's disease
    • Fukui H, Diaz F, Garcia S, Moraes CT. Cytochrome c oxidase deficiency in neurons decreases both oxidative stress and amyloid formation in a mouse model of Alzheimer's disease. Proc Natl Acad Sci USA 2007; 104: 14163-68.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 14163-14168
    • Fukui, H.1    Diaz, F.2    Garcia, S.3    Moraes, C.T.4
  • 72
    • 51349110166 scopus 로고    scopus 로고
    • The amyloid _-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae
    • Petersen CAH, Alikhani N, Behbahani H, et al. The amyloid _-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae. Proc Natl Acad Sci USA 2008; 105: 13145-50.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13145-13150
    • Petersen, C.A.H.1    Alikhani, N.2    Behbahani, H.3
  • 73
    • 3342880690 scopus 로고    scopus 로고
    • A role for heme in Alzheimer's disease: Heme binds amyloid b and has altered metabolism
    • Atamna H, Frey WH 2nd. A role for heme in Alzheimer's disease: heme binds amyloid b and has altered metabolism. Proc Natl Acad Sci USA 2004; 101, 11153-8.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11153-11158
    • Atamna, H.1    Frey II, W.H.2
  • 74
    • 33751103136 scopus 로고    scopus 로고
    • Heme binding to amyloid-b peptide: Mechanistic role in Alzheimer's disease
    • Atamna H. Heme binding to amyloid-b peptide: mechanistic role in Alzheimer's disease. J Alzheimers Dis 2006; 10: 255-66.
    • (2006) J Alzheimers Dis , vol.10 , pp. 255-266
    • Atamna, H.1
  • 75
    • 20144388830 scopus 로고    scopus 로고
    • ABAD enhances A_-induced cell stress via mitochondrial dysfunction
    • Takuma K, Takuma K, Yao J, et al. ABAD enhances A_-induced cell stress via mitochondrial dysfunction. FASEB J 2005; 19: 597-8.
    • (2005) FASEB J , vol.19 , pp. 597-598
    • Takuma, K.1    Takuma, K.2    Yao, J.3
  • 77
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction
    • Devi L, Prabhu BM, Galati DF, Avadhani NG, Anandatheerthavarada HK. Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction. J Neurosci 2006; 26: 9057-68.
    • (2006) J Neurosci , vol.26 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 78
    • 0035780141 scopus 로고    scopus 로고
    • Amyloid betapeptide promotes permeability transition pore in brain mitochondria
    • Moreira PI, Santos MS, Moreno A, Oliveira C. Amyloid betapeptide promotes permeability transition pore in brain mitochondria. Biosci Rep 2001; 21: 789-800.
    • (2001) Biosci Rep , vol.21 , pp. 789-800
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.3    Oliveira, C.4
  • 79
    • 0037100213 scopus 로고    scopus 로고
    • Effect of amyloid beta-peptide on permeability transition pore: A comparative study
    • Moreira PI, Santos MS, Moreno A, Rego AC, Oliveira C. Effect of amyloid beta-peptide on permeability transition pore: a comparative study. J Neurosci Res 2002; 69: 257-67.
    • (2002) J Neurosci Res , vol.69 , pp. 257-267
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.3    Rego, A.C.4    Oliveira, C.5
  • 80
    • 0038321341 scopus 로고    scopus 로고
    • Increased vulnerability of brain mitochondria in diabetic (Goto-Kakizaki) rats with aging and amyloid-beta exposure
    • Moreira PI, Santos MS, Moreno AM, Seiça R, Oliveira CR. Increased vulnerability of brain mitochondria in diabetic (Goto-Kakizaki) rats with aging and amyloid-beta exposure. Diabetes 2003; 52: 1449-56.
    • (2003) Diabetes , vol.52 , pp. 1449-1456
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.M.3    Seiça, R.4    Oliveira, C.R.5
  • 81
    • 53549129483 scopus 로고    scopus 로고
    • Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease
    • Du H, Guo L, Fang F, et al. Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease. Nat Med 2008; 14: 1097-105.
    • (2008) Nat Med , vol.14 , pp. 1097-1105
    • Du, H.1    Guo, L.2    Fang, F.3
  • 82
    • 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: 102-5.
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3
  • 83
    • 58049218922 scopus 로고    scopus 로고
    • Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins
    • Wang X, Su B, Siedlak SL, et al. Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins. Proc Natl Acad Sci USA 2008; 105: 19318-23.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19318-19323
    • Wang, X.1    Su, B.2    Siedlak, S.L.3
  • 84
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fission and fusion in Alzheimer's disease
    • Wang X, Su B, Lee HG, et al. Impaired balance of mitochondrial fission and fusion in Alzheimer's disease. J Neurosci 2009; 29: 9090-103.
    • (2009) J Neurosci , vol.29 , pp. 9090-9103
    • Wang, X.1    Su, B.2    Lee, H.G.3
  • 85
    • 48149108245 scopus 로고    scopus 로고
    • Protein aggregation in the brain: The molecular basis for Alzheimer's and Parkinson's diseases
    • Irvine GB, El-Agnaf OM, Shankar GM, Walsh DM. Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases. Mol Med 2008; 14: 451-64.
    • (2008) Mol Med , vol.14 , pp. 451-464
    • Irvine, G.B.1    El-Agnaf, O.M.2    Shankar, G.M.3    Walsh, D.M.4
  • 86
    • 38449091923 scopus 로고    scopus 로고
    • The autophagy-lysosomal degradation pathway: Role in neurodegenerative disease and therapy
    • Shacka JJ, Roth KA, Zhang J. The autophagy-lysosomal degradation pathway: role in neurodegenerative disease and therapy. Front Biosci 2008; 13: 718-36.
    • (2008) Front Biosci , vol.13 , pp. 718-736
    • Shacka, J.J.1    Roth, K.A.2    Zhang, J.3
  • 87
    • 67649756320 scopus 로고    scopus 로고
    • Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease
    • Büeler H. Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease. Exp Neurol 2009; 218: 235-46.
    • (2009) Exp Neurol , vol.218 , pp. 235-246
    • Büeler, H.1
  • 88
    • 0037338634 scopus 로고    scopus 로고
    • Parkin prevents mitochondrial swelling cytochrome c release in mitochondriadependent cell death
    • Darios F, Corti O, Lucking CB, et al. Parkin prevents mitochondrial swelling cytochrome c release in mitochondriadependent cell death. Hum Mol Genet 2003; 12: 517-26.
    • (2003) Hum Mol Genet , vol.12 , pp. 517-526
    • Darios, F.1    Corti, O.2    Lucking, C.B.3
  • 89
    • 33747179913 scopus 로고    scopus 로고
    • Parkin affects mitochondrial function and apoptosis in neuronal and myogenic cells
    • Kuroda Y, Mitsui T, Kunishige M, Matsumoto T. Parkin affects mitochondrial function and apoptosis in neuronal and myogenic cells. Biochem Biophys Res Commun 2006; 348: 787-93.
    • (2006) Biochem Biophys Res Commun , vol.348 , pp. 787-793
    • Kuroda, Y.1    Mitsui, T.2    Kunishige, M.3    Matsumoto, T.4
  • 90
    • 70349150536 scopus 로고    scopus 로고
    • Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function
    • Davison EJ, Pennington K, Hung CC, et al. Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function. Proteomics 2009; 9: 4284-97.
    • (2009) Proteomics , vol.9 , pp. 4284-4297
    • Davison, E.J.1    Pennington, K.2    Hung, C.C.3
  • 91
    • 2442481789 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative damage in parkin-deficient mice
    • Palacino JJ, Sagi D, Goldberg MS, et al. Mitochondrial dysfunction and oxidative damage in parkin-deficient mice. J Biol Chem 2004; 279: 18614-22.
    • (2004) J Biol Chem , vol.279 , pp. 18614-18622
    • Palacino, J.J.1    Sagi, D.2    Goldberg, M.S.3
  • 92
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T, Asakawa S, Hattori N, et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 1998; 392: 605-8.
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3
  • 93
    • 0345490853 scopus 로고    scopus 로고
    • A wide variety of mutations in the parkin gene are responsible for autosomal recessive Parkinsonism in Europe. French Parkinson's Disease Genetics Study Group and the European Consortium on Genetic Susceptibility in Parkinson's Disease
    • Abbas N, Lucking CB, Ricard S, et al. A wide variety of mutations in the parkin gene are responsible for autosomal recessive Parkinsonism in Europe. French Parkinson's Disease Genetics Study Group and the European Consortium on Genetic Susceptibility in Parkinson's Disease. Hum Mol Genet 1999; 8: 567-74.
    • (1999) Hum Mol Genet , vol.8 , pp. 567-574
    • Abbas, N.1    Lucking, C.B.2    Ricard, S.3
  • 94
    • 33746080412 scopus 로고    scopus 로고
    • Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin
    • Yang Y, Gehrke S, Imai Y, et al. Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc Natl Acad Sci USA 2006; 103: 10793-8.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10793-10798
    • Yang, Y.1    Gehrke, S.2    Imai, Y.3
  • 95
    • 55749090654 scopus 로고    scopus 로고
    • The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila
    • Deng H, Dodson MW, Huang H, Guo M. The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc Natl Acad Sci USA 2008; 105: 14503-8.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14503-14508
    • Deng, H.1    Dodson, M.W.2    Huang, H.3    Guo, M.4
  • 96
    • 36049038504 scopus 로고    scopus 로고
    • Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin
    • Exner N, Treske B, Paquet D, et al. Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin. J Neurosci 2007; 27: 12413-8.
    • (2007) J Neurosci , vol.27 , pp. 12413-12418
    • Exner, N.1    Treske, B.2    Paquet, D.3
  • 97
    • 56049091236 scopus 로고    scopus 로고
    • PINK1 controls mitochondrial localization of Parkin through direct phosphorylation
    • Kim Y, Park J, Kim S, et al. PINK1 controls mitochondrial localization of Parkin through direct phosphorylation. Biochem Biophys Res Commun 2008; 377: 975-80.
    • (2008) Biochem Biophys Res Commun , vol.377 , pp. 975-980
    • Kim, Y.1    Park, J.2    Kim, S.3
  • 98
    • 34547127902 scopus 로고    scopus 로고
    • PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1
    • Pridgeon JW, Olzmann JA, Chin LS, Li L. PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. PLoS Biol 2007; 5: 1494-503.
    • (2007) PLoS Biol , vol.5 , pp. 1494-1503
    • Pridgeon, J.W.1    Olzmann, J.A.2    Chin, L.S.3    Li, L.4
  • 99
    • 35748935851 scopus 로고    scopus 로고
    • The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1
    • Plun-Favreau H, Klupsch K, Moisoi N, Gandhi S, Kjaer S, Frith D. The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1. Nat Cell Biol 2007; 9: 1243-52.
    • (2007) Nat Cell Biol , vol.9 , pp. 1243-1252
    • Plun-Favreau, H.1    Klupsch, K.2    Moisoi, N.3    Gandhi, S.4    Kjaer, S.5    Frith, D.6
  • 100
    • 62749113469 scopus 로고    scopus 로고
    • Silencing of PINK1 expression affects mitochondrial DNA and oxidative phosphorylation in dopaminergic cells
    • Gegg ME, Cooper JM, Schapira AH, Taanman JW. Silencing of PINK1 expression affects mitochondrial DNA and oxidative phosphorylation in dopaminergic cells. PLoS One 2009; 4: e4756.
    • (2009) PLoS One , vol.4
    • Gegg, M.E.1    Cooper, J.M.2    Schapira, A.H.3    Taanman, J.W.4
  • 101
    • 61649088435 scopus 로고    scopus 로고
    • PINK1-associated Parkinson's disease is caused by neuronal vulnerability to calciuminduced cell death
    • Gandhi S, Wood-Kaczmar A, Yao Z, et al. PINK1-associated Parkinson's disease is caused by neuronal vulnerability to calciuminduced cell death. Mol Cell 2009; 33: 627-38.
    • (2009) Mol Cell , vol.33 , pp. 627-638
    • Gandhi, S.1    Wood-Kaczmar, A.2    Yao, Z.3
  • 102
    • 43649104579 scopus 로고    scopus 로고
    • Mitochondrial autophagy is an HIF-1-dependent adaptive metabolic response to hypoxia
    • Zhang H, Bosch-Marce M, Shimoda LA, et al. Mitochondrial autophagy is an HIF-1-dependent adaptive metabolic response to hypoxia. J Biol Chem 2008; 283: 10892-903.
    • (2008) J Biol Chem , vol.283 , pp. 10892-10903
    • Zhang, H.1    Bosch-Marce, M.2    Shimoda, L.A.3
  • 103
    • 70349750492 scopus 로고    scopus 로고
    • Rapamycin protects against rotenone-induced apoptosis through autophagy induction
    • Pan T, Rawal P, Wu Y, Xie W, Jankovic J, Le W. Rapamycin protects against rotenone-induced apoptosis through autophagy induction. Neuroscience 2009; 164: 541-51.
    • (2009) Neuroscience , vol.164 , pp. 541-551
    • Pan, T.1    Rawal, P.2    Wu, Y.3    Xie, W.4    Jankovic, J.5    Le, W.6
  • 104
    • 33847048316 scopus 로고    scopus 로고
    • Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death
    • Zhu JH, Horbinski C, Guo F, Watkins S, Uchiyama Y, Chu CT. Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death. Am J Pathol 2007; 170: 75-86.
    • (2007) Am J Pathol , vol.170 , pp. 75-86
    • Zhu, J.H.1    Horbinski, C.2    Guo, F.3    Watkins, S.4    Uchiyama, Y.5    Chu, C.T.6
  • 106
    • 35848931249 scopus 로고    scopus 로고
    • Increased autophagic degradation of mitochondria in Alzheimer disease
    • Moreira PI, Siedlak SL, Wang X, et al. Increased autophagic degradation of mitochondria in Alzheimer disease. Autophagy 2007; 3: 614-5.
    • (2007) Autophagy , vol.3 , pp. 614-615
    • Moreira, P.I.1    Siedlak, S.L.2    Wang, X.3
  • 107
    • 51349125291 scopus 로고    scopus 로고
    • Neuronal apoptosis and autophagy cross talk in aging PS/APP mice, a model of Alzheimer's disease
    • Yang DS, Kumar A, Stavrides P, et al. Neuronal apoptosis and autophagy cross talk in aging PS/APP mice, a model of Alzheimer's disease. Am J Pathol 2008; 173: 665-81.
    • (2008) Am J Pathol , vol.173 , pp. 665-681
    • Yang, D.S.1    Kumar, A.2    Stavrides, P.3
  • 108
    • 45749114895 scopus 로고    scopus 로고
    • The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid _ accumulation in mice
    • Pickford F, Masliah E, Britschgi M, et al. The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid _ accumulation in mice. J Clin Invest 2008; 118: 2190-9.
    • (2008) J Clin Invest , vol.118 , pp. 2190-2199
    • Pickford, F.1    Masliah, E.2    Britschgi, M.3
  • 109
    • 66349120877 scopus 로고    scopus 로고
    • Autophagy protects neuron from A_-induced cytotoxicity
    • Hung SY, Huang WP, Liou HC, Fu WM. Autophagy protects neuron from A_-induced cytotoxicity. Autophagy 2009; 5: 502-10.
    • (2009) Autophagy , vol.5 , pp. 502-510
    • Hung, S.Y.1    Huang, W.P.2    Liou, H.C.3    Fu, W.M.4
  • 110
    • 0028947294 scopus 로고
    • Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system
    • Cataldo AM, Barnett JL, Berman SA, et al. Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: evidence for early up-regulation of the endosomal-lysosomal system. Neuron 1995; 14: 671-80.
    • (1995) Neuron , vol.14 , pp. 671-680
    • Cataldo, A.M.1    Barnett, J.L.2    Berman, S.A.3
  • 111
    • 14844303381 scopus 로고    scopus 로고
    • Extensive involvement of autophagy in Alzheimer disease: An immuno-electron microscopy study
    • Nixon RA, Wegiel J, Kumar A, et al. Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study. J Neuropathol Exp Neurol 2005; 64: 113-22.
    • (2005) J Neuropathol Exp Neurol , vol.64 , pp. 113-122
    • Nixon, R.A.1    Wegiel, J.2    Kumar, A.3
  • 112
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer's disease
    • Boland B, Kumar A, Lee S, et al. Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease. J Neurosci 2008; 28: 6926-37.
    • (2008) J Neurosci , vol.28 , pp. 6926-6937
    • Boland, B.1    Kumar, A.2    Lee, S.3
  • 113
    • 58449101589 scopus 로고    scopus 로고
    • Abeta42-induced neurodegeneration via an age-dependent autophagiclysosomal injury in Drosophila
    • Ling D, Song HJ, Garza D, Neufeld TP, Salvaterra PM. Abeta42-induced neurodegeneration via an age-dependent autophagiclysosomal injury in Drosophila. PLoS ONE 2009; 4: e4201.
    • (2009) PLoS ONE , vol.4
    • Ling, D.1    Song, H.J.2    Garza, D.3    Neufeld, T.P.4    Salvaterra, P.M.5
  • 114
    • 58149173970 scopus 로고    scopus 로고
    • Oxidative stress induces macroautophagy of amyloid _-protein and ensuing apoptosis
    • Zheng L, Kågedal K, Dehvari N, et al. Oxidative stress induces macroautophagy of amyloid _-protein and ensuing apoptosis. Free Radic Biol Med 2009; 46: 422-9.
    • (2009) Free Radic Biol Med , vol.46 , pp. 422-429
    • Zheng, L.1    Kågedal, K.2    Dehvari, N.3
  • 115
    • 0032526652 scopus 로고    scopus 로고
    • Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Abeta1-42 pathogenesis
    • Yang AJ, Chandswangbhuvana D, Margol L, Glabe CG. Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Abeta1-42 pathogenesis. J Neurosci Res 1998; 52: 691-8.
    • (1998) J Neurosci Res , vol.52 , pp. 691-698
    • Yang, A.J.1    Chandswangbhuvana, D.2    Margol, L.3    Glabe, C.G.4
  • 116
    • 0035110055 scopus 로고    scopus 로고
    • Lysosomal membrane damage in soluble Abeta-mediated cell death in Alzheimer's disease
    • Ditaranto K, Tekirian TL, Yang AJ. Lysosomal membrane damage in soluble Abeta-mediated cell death in Alzheimer's disease. Neurobiol Dis 2001; 8: 19-31.
    • (2001) Neurobiol Dis , vol.8 , pp. 19-31
    • Ditaranto, K.1    Tekirian, T.L.2    Yang, A.J.3
  • 117
    • 48749085779 scopus 로고    scopus 로고
    • Dynamin-like protein 1 reduction underlies mitochondrial morphology and distribution abnormalities in fibroblasts from sporadic Alzheimer's disease patients
    • Wang X, Su B, Fujioka H, Zhu X. Dynamin-like protein 1 reduction underlies mitochondrial morphology and distribution abnormalities in fibroblasts from sporadic Alzheimer's disease patients. Am J Pathol 2008; 173: 470-82.
    • (2008) Am J Pathol , vol.173 , pp. 470-482
    • Wang, X.1    Su, B.2    Fujioka, H.3    Zhu, X.4
  • 118
    • 58149302896 scopus 로고    scopus 로고
    • Parkin mitochondria in the autophagosome
    • McBride HM. Parkin mitochondria in the autophagosome. J Cell Biol 2008; 183: 757-9.
    • (2008) J Cell Biol , vol.183 , pp. 757-759
    • McBride, H.M.1
  • 119
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D, Tanaka A, Suen DF, Youle RJ. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 2008; 183: 795-803.
    • (2008) J Cell Biol , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 120
    • 67649399288 scopus 로고    scopus 로고
    • Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission
    • Dagda RK, Cherra SJ 3rd, Kulich SM, Tandon A, Park D, Chu CT. Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J Biol Chem 2009; 284: 13843-55.
    • (2009) J Biol Chem , vol.284 , pp. 13843-13855
    • Dagda, R.K.1    Cherra III, S.J.2    Kulich, S.M.3    Tandon, A.4    Park, D.5    Chu, C.T.6
  • 121
    • 73449111577 scopus 로고    scopus 로고
    • Mitochondrial autophagy as a compensatory response to PINK1 deficiency
    • Cherra SJ 3rd, Dagda RK, Tandon A, Chu CT. Mitochondrial autophagy as a compensatory response to PINK1 deficiency. Autophagy 2009; 5: 1213-4.
    • (2009) Autophagy , vol.5 , pp. 1213-1214
    • Cherra III, S.J.1    Dagda, R.K.2    Tandon, A.3    Chu, C.T.4
  • 122
    • 78649463381 scopus 로고    scopus 로고
    • Mitofusin-1 and Mitofusin-2 are ubiquitinated in a PINK1/parkin dependent manner upon induction of mitophagy
    • Gegg ME, Cooper JM, Chau KY, Rojo M, Schapira AH, Taanman JW. Mitofusin-1 and Mitofusin-2 are ubiquitinated in a PINK1/parkin dependent manner upon induction of mitophagy. Hum Mol Genet 2010; 19: 4861-70.
    • (2010) Hum Mol Genet , vol.19 , pp. 4861-4870
    • Gegg, M.E.1    Cooper, J.M.2    Chau, K.Y.3    Rojo, M.4    Schapira, A.H.5    Taanman, J.W.6
  • 124
    • 44349195101 scopus 로고    scopus 로고
    • Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery
    • Yang Y, Ouyang Y, Yang L, et al. Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery. Proc Natl Acad Sci USA 2008; 105: 7070-5.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7070-7075
    • Yang, Y.1    Ouyang, Y.2    Yang, L.3


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