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Volumn 8, Issue 3, 2013, Pages 333-346

Impairment of mitochondrial dynamics: A target for the treatment of neurological disorders?

Author keywords

fission; fusion; mitochondria; neurological disease; neuronal damage

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; BH3 PROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; CYTOCHROME C; DJ 1 PROTEIN; DRP1 PROTEIN; GUANOSINE TRIPHOSPHATE; HYDROGEN PEROXIDE; HYDROXYL RADICAL; LEUCINE RICH REPEAT KINASE 2; MITOCHONDRIAL DNA; MITOCHONDRIAL PROTEIN; MITOFUSIN 1; MITOFUSIN 2; OPA1 PROTEIN; PARKIN; PROCASPASE 9; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; REACTIVE OXYGEN METABOLITE; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; UNCLASSIFIED DRUG;

EID: 84877282837     PISSN: 14796708     EISSN: 17486971     Source Type: Journal    
DOI: 10.2217/fnl.13.8     Document Type: Review
Times cited : (4)

References (182)
  • 1
    • 0030465635 scopus 로고    scopus 로고
    • Mitochondrial genetics and human disease
    • Grossman LI, Shoubridge EA. Mitochondrial genetics and human disease. Bioessays 18(12), 983-991 (1996).
    • (1996) Bioessays , vol.18 , Issue.12 , pp. 983-991
    • Grossman, L.I.1    Shoubridge, E.A.2
  • 3
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G, Reed JC. Mitochondrial control of cell death. Nat. Med. 6(5), 513-519 (2000).
    • (2000) Nat. Med. , vol.6 , Issue.5 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 5
    • 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, Vecsei L. Mitochondria, metabolic disturbances, oxidative stress and the kynurenine system, with focus on neurodegenerative disorders. J. Neurol. Sci. 257(1-2), 221-239 (2007).
    • (2007) J. Neurol. Sci. , vol.257 , Issue.1-2 , pp. 221-239
    • Sas, K.1    Robotka, H.2    Toldi, J.3    Vecsei, L.4
  • 6
    • 84859920313 scopus 로고    scopus 로고
    • Mitochondria-associated membranes (MAMs) as hotspot Ca (2+) signaling units
    • Bononi A, Missiroli S, Poletti F et al. Mitochondria-associated membranes (MAMs) as hotspot Ca(2+) signaling units. Adv. Exp. Med. Biol. 740, 411-437 (2012).
    • (2012) Adv. Exp. Med. Biol. , vol.740 , pp. 411-437
    • Bononi, A.1    Missiroli, S.2    Poletti, F.3
  • 8
    • 84863225093 scopus 로고    scopus 로고
    • Mitochondrial Ca(2+) and neurodegeneration
    • Cali T, Ottolini D, Brini M. Mitochondrial Ca(2+) and neurodegeneration. Cell Calcium 52(1), 73-85 (2012).
    • (2012) Cell Calcium , vol.52 , Issue.1 , pp. 73-85
    • Cali, T.1    Ottolini, D.2    Brini, M.3
  • 9
    • 84863218983 scopus 로고    scopus 로고
    • Mitochondrial Ca(2+) and apoptosis
    • Giorgi C, Baldassari F, Bononi A et al. Mitochondrial Ca(2+) and apoptosis. Cell Calcium 52(1), 36-43 (2012).
    • (2012) Cell Calcium , vol.52 , Issue.1 , pp. 36-43
    • Giorgi, C.1    Baldassari, F.2    Bononi, A.3
  • 10
    • 80052627393 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in Ca(2+)-dependent apoptosis and necrosis
    • Rasola A, Bernardi P. Mitochondrial permeability transition in Ca(2+)-dependent apoptosis and necrosis. Cell Calcium 50(3), 222-233 (2011).
    • (2011) Cell Calcium , vol.50 , Issue.3 , pp. 222-233
    • Rasola, A.1    Bernardi, P.2
  • 11
    • 0345600249 scopus 로고    scopus 로고
    • The division of endosymbiotic organelles
    • Osteryoung KW, Nunnari J. The division of endosymbiotic organelles. Science 302(5651), 1698-1704 (2003).
    • (2003) Science , vol.302 , Issue.5651 , pp. 1698-1704
    • Osteryoung, K.W.1    Nunnari, J.2
  • 13
    • 0038243184 scopus 로고    scopus 로고
    • Origins and consequences of mitochondrial variation in vertebrate muscle
    • Moyes CD, Hood DA. Origins and consequences of mitochondrial variation in vertebrate muscle. Annu. Rev. Physiol. 65, 177-201 (2003).
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 177-201
    • Moyes, C.D.1    Hood, D.A.2
  • 14
    • 26444552841 scopus 로고    scopus 로고
    • The significance of mitochondria for embryo development in cloned farm animals
    • Schatten H, Prather RS, Sun QY. The significance of mitochondria for embryo development in cloned farm animals. Mitochondrion 5(5), 303-321 (2005).
    • (2005) Mitochondrion , vol.5 , Issue.5 , pp. 303-321
    • Schatten, H.1    Prather, R.S.2    Sun, Q.Y.3
  • 15
    • 4143051638 scopus 로고    scopus 로고
    • Energy metabolism in mammalian brain during development
    • Erecinska M, Cherian S, Silver IA. Energy metabolism in mammalian brain during development. Prog. Neurobiol. 73(6), 397-445 (2004).
    • (2004) Prog. Neurobiol. , vol.73 , Issue.6 , pp. 397-445
    • Erecinska, M.1    Cherian, S.2    Silver, I.A.3
  • 16
    • 0038177515 scopus 로고    scopus 로고
    • Molecular signaling in death receptor and mitochondrial pathways of apoptosis (review)
    • Gupta S. Molecular signaling in death receptor and mitochondrial pathways of apoptosis (review). Int. J. Oncol. 22(1), 15-20 (2003).
    • (2003) Int. J. Oncol. , vol.22 , Issue.1 , pp. 15-20
    • Gupta, S.1
  • 17
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science 281(5381), 1309-1312 (1998).
    • (1998) Science , vol.281 , Issue.5381 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 18
    • 73349091842 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • Wang C, Youle RJ. The role of mitochondria in apoptosis. Annu. Rev. Genet. 43, 95-118 (2009).
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 95-118
    • Wang, C.1    Youle, R.J.2
  • 19
    • 25844520458 scopus 로고    scopus 로고
    • Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism
    • Jezek P, Hlavata L. Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism. Int. J. Biochem. Cell Biol. 37(12), 2478-2503 (2005).
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , Issue.12 , pp. 2478-2503
    • Jezek, P.1    Hlavata, L.2
  • 21
    • 33745628757 scopus 로고    scopus 로고
    • Generation of superoxide by the mitochondrial complex i
    • Grivennikova VG, Vinogradov AD. Generation of superoxide by the mitochondrial complex I. Biochim. Biophys. Acta 1757(5-6), 553-561 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1757 , Issue.5-6 , pp. 553-561
    • Grivennikova, V.G.1    Vinogradov, A.D.2
  • 22
    • 0035062753 scopus 로고    scopus 로고
    • Invited review: Manganese superoxide dismutase in disease
    • Macmillan-Crow LA, Cruthirds DL. Invited review: manganese superoxide dismutase in disease. Free Radic. Res. 34(4), 325-336 (2001).
    • (2001) Free Radic. Res. , vol.34 , Issue.4 , pp. 325-336
    • MacMillan-Crow, L.A.1    Cruthirds, D.L.2
  • 24
    • 0033965412 scopus 로고    scopus 로고
    • Role of the BH3 (Bcl-2 homology 3) domain in the regulation of apoptosis and Bcl-2-related proteins
    • Lutz RJ. Role of the BH3 (Bcl-2 homology 3) domain in the regulation of apoptosis and Bcl-2-related proteins. Biochem. Soc. Trans. 28(2), 51-56 (2000).
    • (2000) Biochem. Soc. Trans. , vol.28 , Issue.2 , pp. 51-56
    • Lutz, R.J.1
  • 25
    • 0033258120 scopus 로고    scopus 로고
    • Bcl-2 proteins: Regulators of apoptosis or of mitochondrial homeostasis?
    • Vander Heiden MG, Thompson CB. Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis? Nat. Cell. Biol. 1(8), E209-E216 (1999).
    • (1999) Nat. Cell. Biol. , vol.1 , Issue.8
    • Vander Heiden, M.G.1    Thompson, C.B.2
  • 26
    • 27544471076 scopus 로고    scopus 로고
    • The mitochondrial death squad: Hardened killers or innocent bystanders?
    • Ekert PG, Vaux DL. The mitochondrial death squad: hardened killers or innocent bystanders? Curr. Opin. Cell Biol. 17(6), 626-630 (2005).
    • (2005) Curr. Opin. Cell Biol. , vol.17 , Issue.6 , pp. 626-630
    • Ekert, P.G.1    Vaux, D.L.2
  • 27
    • 2142758117 scopus 로고    scopus 로고
    • Mitochondrial dynamics in mammals
    • Chen H, Chan DC. Mitochondrial dynamics in mammals. Curr. Top. Dev. Biol. 59, 119-144 (2004).
    • (2004) Curr. Top. Dev. Biol. , vol.59 , pp. 119-144
    • Chen, H.1    Chan, D.C.2
  • 29
    • 0842302344 scopus 로고    scopus 로고
    • Mitochondrial morphology is dynamic and varied
    • Rube DA, van der Bliek AM. Mitochondrial morphology is dynamic and varied. Mol. Cell. Biochem. 256-257(1-2), 331-339 (2004).
    • (2004) Mol. Cell. Biochem. , vol.256-257 , Issue.1-2 , pp. 331-339
    • Rube, D.A.1    Van Der Bliek, A.M.2
  • 30
    • 79960467546 scopus 로고    scopus 로고
    • Stem cell induced cardiac regeneration: Fusion/mitochondrial exchange and/or transdifferentiation?
    • Song YH, Pinkernell K, Alt E. Stem cell induced cardiac regeneration: fusion/mitochondrial exchange and/or transdifferentiation? Cell Cycle 10(14), 2281-2286 (2011).
    • (2011) Cell Cycle , vol.10 , Issue.14 , pp. 2281-2286
    • Song, Y.H.1    Pinkernell, K.2    Alt, E.3
  • 31
    • 84856056846 scopus 로고    scopus 로고
    • Mitochondrial transport in neurons: Impact on synaptic homeostasis and neurodegeneration
    • Sheng ZH, Cai Q. Mitochondrial transport in neurons: impact on synaptic homeostasis and neurodegeneration. Nat. Rev. Neurosci. 13(2), 77-93 (2012).
    • (2012) Nat. Rev. Neurosci. , vol.13 , Issue.2 , pp. 77-93
    • Zh, S.1    Cai, Q.2
  • 32
    • 0033194038 scopus 로고    scopus 로고
    • The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast
    • Bleazard W, McCaffery JM, King EJ et al. The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast. Nat. Cell. Biol. 1(5), 298-304 (1999).
    • (1999) Nat. Cell. Biol. , vol.1 , Issue.5 , pp. 298-304
    • Bleazard, W.1    McCaffery, J.M.2    King, E.J.3
  • 33
    • 0033934232 scopus 로고    scopus 로고
    • Divide and multiply: Organelle partitioning in yeast
    • Catlett NL, Weisman LS. Divide and multiply: organelle partitioning in yeast. Curr. Opin. Cell Biol. 12(4), 509-516 (2000).
    • (2000) Curr. Opin. Cell Biol. , vol.12 , Issue.4 , pp. 509-516
    • Catlett, N.L.1    Weisman, L.S.2
  • 34
    • 77951096150 scopus 로고    scopus 로고
    • Mitochondrial dynamics - Fusion, fission, movement, and mitophagy - In neurodegenerative diseases
    • Chen H, Chan DC. Mitochondrial dynamics - fusion, fission, movement, and mitophagy - in neurodegenerative diseases. Hum. Mol. Genet. 18(R2), R169-R176 (2009).
    • (2009) Hum. Mol. Genet. , vol.18 , Issue.R2
    • Chen, H.1    Chan, D.C.2
  • 35
    • 27744491193 scopus 로고    scopus 로고
    • Emerging functions of mammalian mitochondrial fusion and fission
    • Chen H, Chan DC. Emerging functions of mammalian mitochondrial fusion and fission. Hum. Mol. Genet. 14(Spec. No 2), R283-R289 (2005).
    • (2005) Hum. Mol. Genet. , vol.14 , Issue.SPEC. NO 2
    • Chen, H.1    Chan, D.C.2
  • 36
    • 33745274726 scopus 로고    scopus 로고
    • Mitochondria: Dynamic organelles in disease, aging, and development
    • Chan DC. Mitochondria: dynamic organelles in disease, aging, and development. Cell 125(7), 1241-1252 (2006).
    • (2006) Cell , vol.125 , Issue.7 , pp. 1241-1252
    • Chan, D.C.1
  • 37
    • 78149360191 scopus 로고    scopus 로고
    • Mitochondrial fission and fusion
    • Scott I, Youle RJ. Mitochondrial fission and fusion. Essays Biochem. 47, 85-98 (2010).
    • (2010) Essays Biochem. , vol.47 , pp. 85-98
    • Scott, I.1    Youle, R.J.2
  • 38
    • 35448960851 scopus 로고    scopus 로고
    • Functions and dysfunctions of mitochondrial dynamics
    • Detmer SA, Chan DC. Functions and dysfunctions of mitochondrial dynamics. Nat. Rev. Mol. Cell Biol. 8(11), 870-879 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , Issue.11 , pp. 870-879
    • Detmer, S.A.1    Chan, D.C.2
  • 39
    • 84864304711 scopus 로고
    • Mitochondrial DNA damage and its consequences for mitochondrial gene expression
    • Cline SD. Mitochondrial DNA damage and its consequences for mitochondrial gene expression. Biochim. Biophys. Acta 1819(9-10), 979-991 (2012).
    • (1819) Biochim. Biophys. Acta , vol.9-10 , pp. 979-991
    • Cline, S.D.1
  • 40
    • 80055078025 scopus 로고    scopus 로고
    • Role and treatment of mitochondrial DNA-related mitochondrial dysfunction in sporadic neurodegenerative diseases
    • Swerdlow RH. Role and treatment of mitochondrial DNA-related mitochondrial dysfunction in sporadic neurodegenerative diseases. Curr. Pharm. Des. 17(31), 3356-3373 (2011).
    • (2011) Curr. Pharm. Des. , vol.17 , Issue.31 , pp. 3356-3373
    • Swerdlow, R.H.1
  • 41
    • 0036189213 scopus 로고    scopus 로고
    • Mitochondrial DNA - Related mitochondrial dysfunction in neurodegenerative diseases
    • Swerdlow RH. Mitochondrial DNA - related mitochondrial dysfunction in neurodegenerative diseases. Arch. Pathol. Lab. Med. 126(3), 271-280 (2002).
    • (2002) Arch. Pathol. Lab. Med. , vol.126 , Issue.3 , pp. 271-280
    • Swerdlow, R.H.1
  • 42
    • 45349094984 scopus 로고    scopus 로고
    • Mitochondrial dynamics and apoptosis
    • Suen DF, Norris KL, Youle RJ. Mitochondrial dynamics and apoptosis. Genes Dev. 22(12), 1577-1590 (2008).
    • (2008) Genes Dev. , vol.22 , Issue.12 , pp. 1577-1590
    • Suen, D.F.1    Norris, K.L.2    Youle, R.J.3
  • 43
    • 79960230433 scopus 로고    scopus 로고
    • Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics
    • Martinou JC, Youle RJ. Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics. Dev. Cell 21(1), 92-101 (2011).
    • (2011) Dev. Cell , vol.21 , Issue.1 , pp. 92-101
    • Martinou, J.C.1    Youle, R.J.2
  • 44
    • 78149270060 scopus 로고    scopus 로고
    • [Mitochondrial dynamics during apoptosis]
    • Castanier C, Arnoult D. [Mitochondrial dynamics during apoptosis]. Med. Sci. (Paris) 26(10), 830-835 (2010).
    • (2010) Med. Sci. (Paris) , vol.26 , Issue.10 , pp. 830-835
    • Castanier, C.1    Arnoult, D.2
  • 45
    • 78149359813 scopus 로고    scopus 로고
    • Mitochondrial fission/fusion dynamics and apoptosis
    • Sheridan C, Martin SJ. Mitochondrial fission/fusion dynamics and apoptosis. Mitochondrion 10(6), 640-648 (2010).
    • (2010) Mitochondrion , vol.10 , Issue.6 , pp. 640-648
    • Sheridan, C.1    Martin, S.J.2
  • 46
    • 84862909353 scopus 로고    scopus 로고
    • The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways
    • Wang Z, Jiang H, Chen S, Du F, Wang X. The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. Cell 148(1-2), 228-243 (2012).
    • (2012) Cell , vol.148 , Issue.1-2 , pp. 228-243
    • Wang, Z.1    Jiang, H.2    Chen, S.3    Du, F.4    Wang, X.5
  • 47
    • 84855462583 scopus 로고    scopus 로고
    • Mitochondrial fission in endothelial cells after simulated ischemia/reperfusion: Role of nitric oxide and reactive oxygen species
    • Giedt RJ, Yang C, Zweier JL, Matzavinos A, Alevriadou BR. Mitochondrial fission in endothelial cells after simulated ischemia/reperfusion: role of nitric oxide and reactive oxygen species. Free Radic. Biol. Med. 52(2), 348-356 (2012).
    • (2012) Free Radic. Biol. Med. , vol.52 , Issue.2 , pp. 348-356
    • Giedt, R.J.1    Yang, C.2    Zweier, J.L.3    Matzavinos, A.4    Alevriadou, B.R.5
  • 48
    • 84555195856 scopus 로고    scopus 로고
    • Autophagy, mitochondria and oxidative stress: Cross-talk and redox signalling
    • Lee J, Giordano S, Zhang J. Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling. Biochem. J. 441(2), 523-540 (2012).
    • (2012) Biochem. J. , vol.441 , Issue.2 , pp. 523-540
    • Lee, J.1    Giordano, S.2    Zhang, J.3
  • 49
    • 84856368290 scopus 로고    scopus 로고
    • Dynamic regulation of mitochondrial network and oxidative functions during 3T3-L1 fat cell differentiation
    • Ducluzeau PH, Priou M, Weitheimer M et al. Dynamic regulation of mitochondrial network and oxidative functions during 3T3-L1 fat cell differentiation. J. Physiol. Biochem. 67(3), 285-296 (2011).
    • (2011) J. Physiol. Biochem. , vol.67 , Issue.3 , pp. 285-296
    • Ducluzeau, P.H.1    Priou, M.2    Weitheimer, M.3
  • 52
    • 77957358299 scopus 로고    scopus 로고
    • Mitochondrial dynamics in cell death and neurodegeneration
    • Cho DH, Nakamura T, Lipton SA. Mitochondrial dynamics in cell death and neurodegeneration. Cell. Mol. Life Sci. 67(20), 3435-3447 (2010).
    • (2010) Cell. Mol. Life Sci. , vol.67 , Issue.20 , pp. 3435-3447
    • Cho, D.H.1    Nakamura, T.2    Lipton, S.A.3
  • 54
    • 77955298543 scopus 로고    scopus 로고
    • Dynamic regulation of mitochondrial fission through modification of the dynamin-related protein Drp1
    • Chang CR, Blackstone C. Dynamic regulation of mitochondrial fission through modification of the dynamin-related protein Drp1. Ann. NY Acad. Sci. 1201, 34-39 (2010).
    • (2010) Ann. NY Acad. Sci. , vol.1201 , pp. 34-39
    • Chang, C.R.1    Blackstone, C.2
  • 55
    • 0035166814 scopus 로고    scopus 로고
    • Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells
    • Smirnova E, Griparic L, Shurland DL, van der Bliek AM. Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol. Biol. Cell. 12(8), 2245-2256 (2001).
    • (2001) Mol. Biol. Cell. , vol.12 , Issue.8 , pp. 2245-2256
    • Smirnova, E.1    Griparic, L.2    Shurland, D.L.3    Van Der Bliek, A.M.4
  • 56
    • 0043092647 scopus 로고    scopus 로고
    • The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1
    • Yoon Y, Krueger EW, Oswald BJ, McNiven MA. The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1. Mol. Cell. Biol. 23(15), 5409-5420 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , Issue.15 , pp. 5409-5420
    • Yoon, Y.1    Krueger, E.W.2    Oswald, B.J.3    McNiven, M.A.4
  • 57
    • 0141592470 scopus 로고    scopus 로고
    • HFis1, a novel component of the mammalian mitochondrial fission machinery
    • James DI, Parone PA, Mattenberger Y, Martinou JC. hFis1, a novel component of the mammalian mitochondrial fission machinery. J. Biol. Chem. 278(38), 36373-36379 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.38 , pp. 36373-36379
    • James, D.I.1    Parone, P.A.2    Mattenberger, Y.3    Martinou, J.C.4
  • 58
    • 78650167618 scopus 로고    scopus 로고
    • Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells
    • Otera H, Wang C, Cleland MM et al. Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells. J. Cell Biol. 191(6), 1141-1158 (2010).
    • J. Cell Biol. , vol.191 , Issue.6 , pp. 1141-1158
    • Otera, H.1    Wang, C.2    Cleland, M.M.3
  • 60
    • 79960621726 scopus 로고    scopus 로고
    • Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission
    • Zhao J, Liu T, Jin S et al. Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission. EMBO J. 30(14), 2762-2778 (2011
    • (2011) EMBO J. , vol.30 , Issue.14 , pp. 2762-2778
    • Zhao, J.1    Liu, T.2    Jin, S.3
  • 61
    • 84874639591 scopus 로고    scopus 로고
    • Mff F. MiD49 and MiD51 mediate Drp1 recruitment in mitochondrial fission
    • Loson OC, Song Z, Chen H, Chan DC. Fis1, Mff, MiD49 and MiD51 mediate Drp1 recruitment in mitochondrial fission. Mol. Biol. Cell. 24(5), 659-667 (2013).
    • (2013) Mol. Biol. Cell. , vol.24 , Issue.5 , pp. 659-667
    • Loson, O.C.1    Song, Z.2    Chen, H.3    Chan, D.C.4
  • 62
    • 25444514731 scopus 로고    scopus 로고
    • Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network: New implications for Charcot-Marie-Tooth disease
    • Niemann A, Ruegg M, La Padula V, Schenone A, Suter U. Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network: new implications for Charcot-Marie-Tooth disease. J. Cell Biol. 170(7), 1067-1078 (2005).
    • (2005) J. Cell Biol. , vol.170 , Issue.7 , pp. 1067-1078
    • Niemann, A.1    Ruegg, M.2    La Padula, V.3    Schenone, A.4    Suter, U.5
  • 63
    • 4644242944 scopus 로고    scopus 로고
    • Endophilin B1 is required for the maintenance of mitochondrial morphology
    • Karbowski M, Jeong SY, Youle RJ. Endophilin B1 is required for the maintenance of mitochondrial morphology. J. Cell Biol. 166(7), 1027-1039 (2004).
    • (2004) J. Cell Biol. , vol.166 , Issue.7 , pp. 1027-1039
    • Karbowski, M.1    Jeong, S.Y.2    Youle, R.J.3
  • 64
    • 23844539004 scopus 로고    scopus 로고
    • The mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells
    • Tondera D, Czauderna F, Paulick K, Schwarzer R, Kaufmann J, Santel A. The mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells. J. Cell Sci. 118(Pt 14), 3049-3059 (2005).
    • (2005) J. Cell Sci. , vol.118 , Issue.PART 14 , pp. 3049-3059
    • Tondera, D.1    Czauderna, F.2    Paulick, K.3    Schwarzer, R.4    Kaufmann, J.5    Santel, A.6
  • 65
    • 69449090286 scopus 로고    scopus 로고
    • The novel conserved mitochondrial inner-membrane protein MTGM regulates mitochondrial morphology and cell proliferation
    • Zhao J, Liu T, Jin SB et al. The novel conserved mitochondrial inner-membrane protein MTGM regulates mitochondrial morphology and cell proliferation. J. Cell Sci. 122(Pt 13), 2252-2262 (2009).
    • (2009) J. Cell Sci. , vol.122 , Issue.PART 13 , pp. 2252-2262
    • Zhao, J.1    Liu, T.2    Jin, S.B.3
  • 66
    • 77950668890 scopus 로고    scopus 로고
    • The AAA+ ATPase ATAD3A controls mitochondrial dynamics at the interface of the inner and outer membranes
    • Gilquin B, Taillebourg E, Cherradi N et al. The AAA+ ATPase ATAD3A controls mitochondrial dynamics at the interface of the inner and outer membranes. Mol. Cell. Biol. 30(8), 1984-1996 (2010).
    • (2010) Mol. Cell. Biol. , vol.30 , Issue.8 , pp. 1984-1996
    • Gilquin, B.1    Taillebourg, E.2    Cherradi, N.3
  • 67
    • 79957937433 scopus 로고    scopus 로고
    • Dynamin-related protein 1 and mitochondrial fragmentation in neurodegenerative diseases
    • Reddy PH, Reddy TP, Manczak M, Calkins MJ, Shirendeb U, Mao P. Dynamin-related protein 1 and mitochondrial fragmentation in neurodegenerative diseases. Brain Res. Rev. 67(1-2), 103-118 (2011).
    • (2011) Brain Res. Rev. , vol.67 , Issue.1-2 , pp. 103-118
    • Reddy, P.H.1    Reddy, T.P.2    Manczak, M.3    Calkins, M.J.4    Shirendeb, U.5    Mao, P.6
  • 68
    • 48849085973 scopus 로고    scopus 로고
    • Shaping mitochondria: The complex posttranslational regulation of the mitochondrial fission protein DRP1
    • Santel A, Frank S. Shaping mitochondria: the complex posttranslational regulation of the mitochondrial fission protein DRP1. IUBMB Life 60(7), 448-455 (2008).
    • (2008) IUBMB Life , vol.60 , Issue.7 , pp. 448-455
    • Santel, A.1    Frank, S.2
  • 69
    • 64749114270 scopus 로고    scopus 로고
    • Bcl-x L increases mitochondrial fission, fusion, and biomass in neurons
    • Berman SB, Chen YB, Qi B et al. Bcl-x L increases mitochondrial fission, fusion, and biomass in neurons. J. Cell Biol. 184(5), 707-719 (2009).
    • (2009) J. Cell Biol. , vol.184 , Issue.5 , pp. 707-719
    • Berman, S.B.1    Chen, Y.B.2    Qi, B.3
  • 70
    • 78751482244 scopus 로고    scopus 로고
    • Bcl-2 proteins and autophagy regulate mitochondrial dynamics during programmed cell death in the Drosophila ovary
    • Tanner EA, Blute TA, Brachmann CB, McCall K. Bcl-2 proteins and autophagy regulate mitochondrial dynamics during programmed cell death in the Drosophila ovary. Development 138(2), 327-338 (2011).
    • (2011) Development , vol.138 , Issue.2 , pp. 327-338
    • Tanner, E.A.1    Blute, T.A.2    Brachmann, C.B.3    McCall, K.4
  • 71
    • 70449107007 scopus 로고    scopus 로고
    • Emerging role for members of the Bcl-2 family in mitochondrial morphogenesis
    • Autret A, Martin SJ. Emerging role for members of the Bcl-2 family in mitochondrial morphogenesis. Mol. Cell 36(3), 355-363 (2009).
    • (2009) Mol. Cell , vol.36 , Issue.3 , pp. 355-363
    • Autret, A.1    Martin, S.J.2
  • 72
    • 78649679754 scopus 로고    scopus 로고
    • Bax is essential for Drp1-mediated mitochondrial fission but not for mitochondrial outer membrane permeabilization caused by photodynamic therapy
    • Wu S, Zhou F, Zhang Z, Xing D. Bax is essential for Drp1-mediated mitochondrial fission but not for mitochondrial outer membrane permeabilization caused by photodynamic therapy. J. Cell. Physiol. 226(2), 530-541 (2011).
    • (2011) J. Cell. Physiol. , vol.226 , Issue.2 , pp. 530-541
    • Wu, S.1    Zhou, F.2    Zhang, Z.3    Xing, D.4
  • 74
    • 34547442346 scopus 로고    scopus 로고
    • Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins
    • Brooks C, Wei Q, Feng L et al. Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins. Proc. Natl Acad. Sci. USA 104(28), 11649-11654 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , Issue.28 , pp. 11649-11654
    • Brooks, C.1    Wei, Q.2    Feng, L.3
  • 75
    • 33644859410 scopus 로고    scopus 로고
    • Role for CED-9 and Egl-1 as regulators of mitochondrial fission and fusion dynamics
    • Delivani P, Adrain C, Taylor RC, Duriez PJ, Martin SJ. Role for CED-9 and Egl-1 as regulators of mitochondrial fission and fusion dynamics. Mol. Cell 21(6), 761-773 (2006).
    • (2006) Mol. Cell , vol.21 , Issue.6 , pp. 761-773
    • Delivani, P.1    Adrain, C.2    Taylor, R.C.3    Duriez, P.J.4    Martin, S.J.5
  • 76
    • 80054765894 scopus 로고    scopus 로고
    • A molecular switch that governs mitochondrial fusion and fission mediated by the BCL2-like protein CED-9 of Caenorhabditis elegans
    • Lu Y, Rolland SG, Conradt B. A molecular switch that governs mitochondrial fusion and fission mediated by the BCL2-like protein CED-9 of Caenorhabditis elegans. Proc. Natl Acad. Sci. USA 108(41), E813-E822 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , Issue.41
    • Lu, Y.1    Rolland, S.G.2    Conradt, B.3
  • 77
    • 33644856970 scopus 로고    scopus 로고
    • CED-9 and EGL-1: A duo also regulating mitochondrial network morphology
    • Estaquier J, Arnoult D. CED-9 and EGL-1: a duo also regulating mitochondrial network morphology. Mol. Cell 21(6), 730-732 (2006).
    • (2006) Mol. Cell , vol.21 , Issue.6 , pp. 730-732
    • Estaquier, J.1    Arnoult, D.2
  • 78
    • 69449104405 scopus 로고    scopus 로고
    • The BCL-2-like protein CED-9 of C. elegans promotes FZO-1/Mfn1,2- and EAT-3/Opa1- dependent mitochondrial fusion
    • Rolland SG, Lu Y, David CN, Conradt B. The BCL-2-like protein CED-9 of C. elegans promotes FZO-1/Mfn1,2- and EAT-3/Opa1- dependent mitochondrial fusion. J. Cell Biol. 186(4), 525-540 (2009).
    • (2009) J. Cell Biol. , vol.186 , Issue.4 , pp. 525-540
    • Rolland, S.G.1    Lu, Y.2    David, C.N.3    Conradt, B.4
  • 79
    • 0032547845 scopus 로고    scopus 로고
    • Mitochondrial fusion in yeast requires the transmembrane GTPase Fzo1p
    • Hermann GJ, Thatcher JW, Mills JP et al. Mitochondrial fusion in yeast requires the transmembrane GTPase Fzo1p. J. Cell Biol. 143(2), 359-373 (1998).
    • (1998) J. Cell Biol. , vol.143 , Issue.2 , pp. 359-373
    • Hermann, G.J.1    Thatcher, J.W.2    Mills, J.P.3
  • 80
    • 0032493625 scopus 로고    scopus 로고
    • Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae
    • Rapaport D, Brunner M, Neupert W, Westermann B. Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae. J. Biol. Chem. 273(32), 20150-20155 (1998).
    • (1998) J. Biol. Chem. , vol.273 , Issue.32 , pp. 20150-20155
    • Rapaport, D.1    Brunner, M.2    Neupert, W.3    Westermann, B.4
  • 81
    • 34547601410 scopus 로고    scopus 로고
    • Mitochondrial fusion protects against neurodegeneration in the cerebellum
    • Chen H, McCaffery JM, Chan DC. Mitochondrial fusion protects against neurodegeneration in the cerebellum. Cell 130(3), 548-562 (2007).
    • (2007) Cell , vol.130 , Issue.3 , pp. 548-562
    • Chen, H.1    McCaffery, J.M.2    Chan, D.C.3
  • 82
    • 84864702229 scopus 로고    scopus 로고
    • MFN2 mutations cause compensatory mitochondrial DNA proliferation
    • 1-3; author reply e220, 1-3
    • Sitarz KS, Yu-Wai-Man P, Pyle A et al. MFN2 mutations cause compensatory mitochondrial DNA proliferation. Brain 135(Pt 8), e219, 1-3; author reply e220, 1-3 (2012).
    • Brain , vol.135 , Issue.PART 8
    • Sitarz, K.S.1    Yu-Wai-Man, P.2    Pyle, A.3
  • 83
    • 77951737783 scopus 로고    scopus 로고
    • Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations
    • Chen H, Vermulst M, Wang YE et al. Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations. Cell 141(2), 280-289 (2010).
    • (2010) Cell , vol.141 , Issue.2 , pp. 280-289
    • Chen, H.1    Vermulst, M.2    Wang, Y.E.3
  • 84
    • 0026544936 scopus 로고
    • Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin
    • Jones BA, Fangman WL. Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin. Genes Dev. 6(3), 380-389 (1992).
    • (1992) Genes Dev. , vol.6 , Issue.3 , pp. 380-389
    • Jones, B.A.1    Fangman, W.L.2
  • 85
    • 78651480831 scopus 로고    scopus 로고
    • OPA1 links human mitochondrial genome maintenance to mtDNA replication and distribution
    • Elachouri G, Vidoni S, Zanna C et al. OPA1 links human mitochondrial genome maintenance to mtDNA replication and distribution. Genome Res. 21(1), 12-20 (2011).
    • (2011) Genome Res. , vol.21 , Issue.1 , pp. 12-20
    • Elachouri, G.1    Vidoni, S.2    Zanna, C.3
  • 86
    • 38849192448 scopus 로고    scopus 로고
    • OPA1 mutations induce mitochondrial DNA instability and optic atrophy 'plus' phenotypes
    • Amati-Bonneau P, Valentino ML, Reynier P et al. OPA1 mutations induce mitochondrial DNA instability and optic atrophy 'plus' phenotypes. Brain 131(Pt 2), 338-351 (2008).
    • (2008) Brain , vol.131 , Issue.PART 2 , pp. 338-351
    • Amati-Bonneau, P.1    Valentino, M.L.2    Reynier, P.3
  • 87
    • 38849151612 scopus 로고    scopus 로고
    • Mutation of OPA1 causes dominant optic atrophy with external ophthalmoplegia, ataxia, deafness and multiple mitochondrial DNA deletions: A novel disorder of mtDNA maintenance
    • Hudson G, Amati-Bonneau P, Blakely EL et al. Mutation of OPA1 causes dominant optic atrophy with external ophthalmoplegia, ataxia, deafness and multiple mitochondrial DNA deletions: a novel disorder of mtDNA maintenance. Brain 131(Pt 2), 329-337 (2008).
    • (2008) Brain , vol.131 , Issue.PART 2 , pp. 329-337
    • Hudson, G.1    Amati-Bonneau, P.2    Blakely, E.L.3
  • 88
    • 79955368211 scopus 로고    scopus 로고
    • A clinically complex form of dominant optic atrophy (OPA8) maps on chromosome 16
    • Carelli V, Schimpf S, Fuhrmann N et al. A clinically complex form of dominant optic atrophy (OPA8) maps on chromosome 16. Hum. Mol. Genet. 20(10), 1893-1905 (2011).
    • (2011) Hum. Mol. Genet. , vol.20 , Issue.10 , pp. 1893-1905
    • Carelli, V.1    Schimpf, S.2    Fuhrmann, N.3
  • 89
    • 84856725391 scopus 로고    scopus 로고
    • The MFN2 gene is responsible for mitochondrial DNA instability and optic atrophy 'plus' phenotype
    • Rouzier C, Bannwarth S, Chaussenot A et al. The MFN2 gene is responsible for mitochondrial DNA instability and optic atrophy 'plus' phenotype. Brain 135(Pt 1), 23-34 (2012).
    • (2012) Brain , vol.135 , Issue.PART 1 , pp. 23-34
    • Rouzier, C.1    Bannwarth, S.2    Chaussenot, A.3
  • 90
    • 52449134835 scopus 로고    scopus 로고
    • Preventing mitochondrial fission impairs mitochondrial function and leads to loss of mitochondrial DNA
    • Parone PA, Da Cruz S, Tondera D et al. Preventing mitochondrial fission impairs mitochondrial function and leads to loss of mitochondrial DNA. PLoS ONE 3(9), e3257 (2008).
    • (2008) PLoS ONE , vol.3 , Issue.9
    • Parone, P.A.1    Da Cruz, S.2    Tondera, D.3
  • 91
    • 69449101151 scopus 로고    scopus 로고
    • Inhibition of mitochondrial fission favours mutant over wild-type mitochondrial DNA
    • Malena A, Loro E, Di Re M, Holt IJ, Vergani L. Inhibition of mitochondrial fission favours mutant over wild-type mitochondrial DNA. Hum. Mol. Genet. 18(18), 3407-3416 (2009).
    • (2009) Hum. Mol. Genet. , vol.18 , Issue.18 , pp. 3407-3416
    • Malena, A.1    Loro, E.2    Di Re, M.3    Holt, I.J.4    Vergani, L.5
  • 92
    • 84856723741 scopus 로고    scopus 로고
    • Dysfunctional mitochondrial maintenance: What breaks the circle of life?
    • Yu-Wai-Man P, Chinnery PF. Dysfunctional mitochondrial maintenance: what breaks the circle of life? Brain 135(Pt 1), 9-11 (2012).
    • (2012) Brain , vol.135 , Issue.PART 1 , pp. 9-11
    • Yu-Wai-Man, P.1    Chinnery, P.F.2
  • 93
    • 71849085539 scopus 로고    scopus 로고
    • Mitochondrial trafficking and morphology in neuronal injury
    • Rintoul GL, Reynolds IJ. Mitochondrial trafficking and morphology in neuronal injury. Biochim. Biophys. Acta 1802(1), 143-150 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1802 , Issue.1 , pp. 143-150
    • Rintoul, G.L.1    Reynolds, I.J.2
  • 95
    • 64649093169 scopus 로고    scopus 로고
    • Mitochondrial dynamics and neurodegeneration
    • Lu B. Mitochondrial dynamics and neurodegeneration. Curr. Neurol. Neurosci. Rep. 9(3), 212-219 (2009).
    • (2009) Curr. Neurol. Neurosci. Rep. , vol.9 , Issue.3 , pp. 212-219
    • Lu, B.1
  • 97
    • 33646194845 scopus 로고    scopus 로고
    • Dysregulation of mitochondrial fusion and fission: An emerging concept in neurodegeneration
    • Frank S. Dysregulation of mitochondrial fusion and fission: an emerging concept in neurodegeneration. Acta Neuropathol. 111(2), 93-100 (2006).
    • (2006) Acta Neuropathol. , vol.111 , Issue.2 , pp. 93-100
    • Frank, S.1
  • 98
    • 34848919465 scopus 로고    scopus 로고
    • Mutations in the mitofusin 2 gene are the most common cause of Charcot-Marie-Tooth type 2 disease
    • Soltysinska E, Kabzinska D, Kochanski A. [Mutations in the mitofusin 2 gene are the most common cause of Charcot-Marie-Tooth type 2 disease]. Neurol. Neurochir. Pol. 41(4), 350-354 (2007).
    • (2007) Neurol. Neurochir. Pol. , vol.41 , Issue.4 , pp. 350-354
    • Soltysinska, E.1    Kabzinska, D.2    Kochanski, A.3
  • 99
    • 67649803117 scopus 로고    scopus 로고
    • Role of mitofusin 2 mutations in the physiopathology of Charcot-Marie-Tooth disease type 2A
    • Cartoni R, Martinou JC. Role of mitofusin 2 mutations in the physiopathology of Charcot-Marie-Tooth disease type 2A. Exp. Neurol. 218(2), 268-273 (2009).
    • (2009) Exp. Neurol. , vol.218 , Issue.2 , pp. 268-273
    • Cartoni, R.1    Martinou, J.C.2
  • 100
    • 84868127674 scopus 로고    scopus 로고
    • Loss of Mfn2 results in progressive, retrograde degeneration of dopaminergic neurons in the nigrostriatal circuit
    • Pham AH, Meng S, Chu QN, Chan DC. Loss of Mfn2 results in progressive, retrograde degeneration of dopaminergic neurons in the nigrostriatal circuit. Hum. Mol. Genet. 21(22), 4817-4826 (2012).
    • (2012) Hum. Mol. Genet. , vol.21 , Issue.22 , pp. 4817-4826
    • Pham, A.H.1    Meng, S.2    Chu, Q.N.3    Chan, D.C.4
  • 101
    • 84868110583 scopus 로고    scopus 로고
    • Mitofusin 2 is necessary for striatal axonal projections of midbrain dopamine neurons
    • Lee S, Sterky FH, Mourier A et al. Mitofusin 2 is necessary for striatal axonal projections of midbrain dopamine neurons. Hum. Mol. Genet. 21(22), 4827-4835 (2012).
    • (2012) Hum. Mol. Genet. , vol.21 , Issue.22 , pp. 4827-4835
    • Lee, S.1    Sterky, F.H.2    Mourier, A.3
  • 102
    • 84861227901 scopus 로고    scopus 로고
    • Disorders of the optic nerve in mitochondrial cytopathies: New ideas on pathogenesis and therapeutic targets
    • Sitarz KS, Chinnery PF, Yu-Wai-Man P. Disorders of the optic nerve in mitochondrial cytopathies: new ideas on pathogenesis and therapeutic targets. Curr. Neurol. Neurosci. Rep. 12(3), 308-317 (2012).
    • (2012) Curr. Neurol. Neurosci. Rep. , vol.12 , Issue.3 , pp. 308-317
    • Sitarz, K.S.1    Chinnery, P.F.2    Yu-Wai-Man, P.3
  • 103
    • 0037424239 scopus 로고    scopus 로고
    • Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis
    • Olichon A, Baricault L, Gas N et al. Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis. J. Biol. Chem. 278(10), 7743-7746 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.10 , pp. 7743-7746
    • Olichon, A.1    Baricault, L.2    Gas, N.3
  • 104
    • 34147223220 scopus 로고    scopus 로고
    • Effects of OPA1 mutations on mitochondrial morphology and apoptosis: Relevance to ADOA pathogenesis
    • Olichon A, Landes T, Arnaune-Pelloquin L et al. Effects of OPA1 mutations on mitochondrial morphology and apoptosis: relevance to ADOA pathogenesis. J. Cell. Physiol. 211(2), 423-430 (2007).
    • (2007) J. Cell. Physiol. , vol.211 , Issue.2 , pp. 423-430
    • Olichon, A.1    Landes, T.2    Arnaune-Pelloquin, L.3
  • 105
    • 9144238312 scopus 로고    scopus 로고
    • Deficit of in vivo mitochondrial ATP production in OPA1-related dominant optic atrophy
    • Lodi R, Tonon C, Valentino ML et al. Deficit of in vivo mitochondrial ATP production in OPA1-related dominant optic atrophy. Ann. Neurol. 56(5), 719-723 (2004).
    • (2004) Ann. Neurol. , vol.56 , Issue.5 , pp. 719-723
    • Lodi, R.1    Tonon, C.2    Valentino, M.L.3
  • 106
    • 46749111893 scopus 로고    scopus 로고
    • Hereditary optic neuropathies share a common mitochondrial coupling defect
    • Chevrollier A, Guillet V, Loiseau D et al. Hereditary optic neuropathies share a common mitochondrial coupling defect. Ann. Neurol. 63(6), 794-798 (2008).
    • (2008) Ann. Neurol. , vol.63 , Issue.6 , pp. 794-798
    • Chevrollier, A.1    Guillet, V.2    Loiseau, D.3
  • 107
    • 84872356908 scopus 로고    scopus 로고
    • Loss of OPA1 disturbs cellular calcium homeostasis and sensitizes for excitotoxicity
    • Kushnareva YE, Gerencser AA, Bossy B et al. Loss of OPA1 disturbs cellular calcium homeostasis and sensitizes for excitotoxicity. Cell Death Differ. 20(2), 353-3652013).
    • (2013) Cell Death Differ. , vol.20 , Issue.2 , pp. 353-365
    • Kushnareva, Y.E.1    Gerencser, A.A.2    Bossy, B.3
  • 108
    • 41149111891 scopus 로고    scopus 로고
    • Bcl-xL induces Drp1-dependent synapse formation in cultured hippocampal neurons
    • Li H, Chen Y, Jones AF et al. Bcl-xL induces Drp1-dependent synapse formation in cultured hippocampal neurons. Proc. Natl Acad. Sci. USA 105(6), 2169-2174 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.6 , pp. 2169-2174
    • Li, H.1    Chen, Y.2    Jones, A.F.3
  • 109
    • 68249087424 scopus 로고    scopus 로고
    • Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice
    • Ishihara N, Nomura M, Jofuku A et al. Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice. Nat. Cell. Biol. 11(8), 958-966 (2009).
    • (2009) Nat. Cell. Biol. , vol.11 , Issue.8 , pp. 958-966
    • Ishihara, N.1    Nomura, M.2    Jofuku, A.3
  • 110
    • 70349944660 scopus 로고    scopus 로고
    • The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice
    • Wakabayashi J, Zhang Z, Wakabayashi N et al. The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice. J. Cell Biol. 186(6), 805-816 (2009).
    • (2009) J. Cell Biol. , vol.186 , Issue.6 , pp. 805-816
    • Wakabayashi, J.1    Zhang, Z.2    Wakabayashi, N.3
  • 111
    • 84862605918 scopus 로고    scopus 로고
    • Mitochondrial division ensures the survival of postmitotic neurons by suppressing oxidative damage
    • Kageyama Y, Zhang Z, Roda R et al. Mitochondrial division ensures the survival of postmitotic neurons by suppressing oxidative damage. J. Cell Biol. (4), 535-551 (2012).
    • (2012) J. Cell Biol. , Issue.4 , pp. 535-551
    • Kageyama, Y.1    Zhang, Z.2    Roda, R.3
  • 113
    • 75549084672 scopus 로고    scopus 로고
    • Expression of beclin1 and LC3 after rat's skin contusion
    • Yan FP, Chen YJ, Huang XH. [Expression of beclin1 and LC3 after rat's skin contusion]. Fa Yi Xue Za Zhi 23(1), 11-13 (2007).
    • (2007) Fa Yi Xue Za Zhi , vol.23 , Issue.1 , pp. 11-13
    • Yan, F.P.1    Chen, Y.J.2    Huang, X.H.3
  • 114
    • 34648859471 scopus 로고    scopus 로고
    • Oxidative damage in mild cognitive impairment and early Alzheimer's disease
    • Lovell MA, Markesbery WR. Oxidative damage in mild cognitive impairment and early Alzheimer's disease. J. Neurosci. Res. 85(14), 3036-3040 (2007).
    • (2007) J. Neurosci. Res. , vol.85 , Issue.14 , pp. 3036-3040
    • Lovell, M.A.1    Markesbery, W.R.2
  • 115
    • 79958721260 scopus 로고    scopus 로고
    • Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: Implications for neuronal damage
    • Manczak M, Calkins MJ, Reddy PH. Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: implications for neuronal damage. Hum. Mol. Genet. 20(13), 2495-2509 (2011).
    • (2011) Hum. Mol. Genet. , vol.20 , Issue.13 , pp. 2495-2509
    • Manczak, M.1    Calkins, M.J.2    Reddy, P.H.3
  • 116
    • 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 324(5923), 102-105 (2009).
    • (2009) Science , vol.324 , Issue.5923 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3
  • 117
    • 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 105(49), 19318-19323 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.49 , pp. 19318-19323
    • Wang, X.1    Su, B.2    Siedlak, S.L.3
  • 118
    • 77956207531 scopus 로고    scopus 로고
    • Mitochondria-targeted antioxidants protect against amyloid-beta toxicity in Alzheimer's disease neurons
    • Manczak M, Mao P, Calkins MJ et al. Mitochondria-targeted antioxidants protect against amyloid-beta toxicity in Alzheimer's disease neurons. J. Alzheimers Dis. 20(Suppl. 2), S609-S631 (2010).
    • (2010) J. Alzheimers Dis. , vol.20 , Issue.SUPPL. 2
    • Manczak, M.1    Mao, P.2    Calkins, M.J.3
  • 119
    • 84865352799 scopus 로고    scopus 로고
    • Tau promotes neurodegeneration via DRP1 mislocalization in vivo
    • Duboff B, Gotz J, Feany MB. Tau promotes neurodegeneration via DRP1 mislocalization in vivo. Neuron 75(4), 618-632 (2012).
    • (2012) Neuron , vol.75 , Issue.4 , pp. 618-632
    • Duboff, B.1    Gotz, J.2    Feany, M.B.3
  • 120
    • 49849090871 scopus 로고    scopus 로고
    • Neuropsychological and psychiatric changes after deep brain stimulation for Parkinson's disease: A randomised, multicentre study
    • Witt K, Daniels C, Reiff J et al. Neuropsychological and psychiatric changes after deep brain stimulation for Parkinson's disease: a randomised, multicentre study. Lancet Neurol. 7(7), 605-614 (2008).
    • (2008) Lancet Neurol. , vol.7 , Issue.7 , pp. 605-614
    • Witt, K.1    Daniels, C.2    Reiff, J.3
  • 121
    • 84866241815 scopus 로고    scopus 로고
    • Mitochondrial dynamics and mitophagy in the 6-hydroxydopamine preclinical model of Parkinson's disease
    • Galindo MF, Solesio ME, Atienzar-Aroca S, Zamora MJ, Jordan Bueso J. Mitochondrial dynamics and mitophagy in the 6-hydroxydopamine preclinical model of Parkinson's disease. Parkinsons Dis. 2012, 131058 (2012).
    • (2012) Parkinsons Dis. , vol.2012 , pp. 131058
    • Galindo, M.F.1    Solesio, M.E.2    Atienzar-Aroca, S.3    Zamora, M.J.4    Jordan Bueso, J.5
  • 122
    • 84868574626 scopus 로고    scopus 로고
    • The mitochondria-targeted anti-oxidant MitoQ reduces aspects of mitochondrial fission in the 6-OHDA cell model of Parkinson's disease
    • Solesio ME, Prime TA, Logan A et al. The mitochondria-targeted anti-oxidant MitoQ reduces aspects of mitochondrial fission in the 6-OHDA cell model of Parkinson's disease. Biochim. Biophys. Acta 1832(1), 174-182 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1832 , Issue.1 , pp. 174-182
    • Solesio, M.E.1    Prime, T.A.2    Logan, A.3
  • 123
    • 33748028841 scopus 로고    scopus 로고
    • Nitric oxide-induced mitochondrial fission is regulated by dynamin-related GTPases in neurons
    • Barsoum MJ, Yuan H, Gerencser AA et al. Nitric oxide-induced mitochondrial fission is regulated by dynamin-related GTPases in neurons. EMBO J. 25(16), 3900-3911 (2006).
    • (2006) EMBO J. , vol.25 , Issue.16 , pp. 3900-3911
    • Barsoum, M.J.1    Yuan, H.2    Gerencser, A.A.3
  • 124
    • 80052794422 scopus 로고    scopus 로고
    • DLP1-dependent mitochondrial fragmentation mediates 1-methyl-4- phenylpyridinium toxicity in neurons: Implications for Parkinson's disease
    • Wang X, Su B, Liu W et al. DLP1-dependent mitochondrial fragmentation mediates 1-methyl-4-phenylpyridinium toxicity in neurons: implications for Parkinson's disease. Aging Cell 10(5), 807-823 (2011).
    • (2011) Aging Cell , vol.10 , Issue.5 , pp. 807-823
    • Wang, X.1    Su, B.2    Liu, W.3
  • 125
    • 77955029885 scopus 로고    scopus 로고
    • Effect of endogenous mutant and wild-type PINK1 on Parkin in fibroblasts from Parkinson disease patients
    • Rakovic A, Grunewald A, Seibler P et al. Effect of endogenous mutant and wild-type PINK1 on Parkin in fibroblasts from Parkinson disease patients. Hum. Mol. Genet. 19(16), 3124-3137 (2010).
    • (2010) Hum. Mol. Genet. , vol.19 , Issue.16 , pp. 3124-3137
    • Rakovic, A.1    Grunewald, A.2    Seibler, P.3
  • 126
    • 79952369437 scopus 로고    scopus 로고
    • Mutations in PINK1 and Parkin impair ubiquitination of mitofusins in human fibroblasts
    • Rakovic A, Grunewald A, Kottwitz J et al. Mutations in PINK1 and Parkin impair ubiquitination of mitofusins in human fibroblasts. PLoS ONE 6(3), e16746 (2011).
    • (2011) PLoS ONE , vol.6 , Issue.3
    • Rakovic, A.1    Grunewald, A.2    Kottwitz, J.3
  • 127
    • 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 105(38), 14503-14508 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.38 , pp. 14503-14508
    • Deng, H.1    Dodson, M.W.2    Huang, H.3    Guo, M.4
  • 129
    • 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 105(19), 7070-7075 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.19 , pp. 7070-7075
    • Yang, Y.1    Ouyang, Y.2    Yang, L.3
  • 130
    • 79960826207 scopus 로고    scopus 로고
    • The PINK1/ Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons
    • Yu W, Sun Y, Guo S, Lu B. The PINK1/ Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons. Hum. Mol. Genet. 20(16), 3227-3240 (2011).
    • (2011) Hum. Mol. Genet. , vol.20 , Issue.16 , pp. 3227-3240
    • Yu, W.1    Sun, Y.2    Guo, S.3    Lu, B.4
  • 131
    • 84860539187 scopus 로고    scopus 로고
    • Parkinson's disease-associated DJ-1 mutations impair mitochondrial dynamics and cause mitochondrial dysfunction
    • Wang X, Petrie TG, Liu Y, Liu J, Fujioka H, Zhu X. Parkinson's disease-associated DJ-1 mutations impair mitochondrial dynamics and cause mitochondrial dysfunction. J. Neurochem. 121(5), 830-839 (2012).
    • (2012) J. Neurochem. , vol.121 , Issue.5 , pp. 830-839
    • Wang, X.1    Petrie, T.G.2    Liu, Y.3    Liu, J.4    Fujioka, H.5    Zhu, X.6
  • 132
    • 81255149611 scopus 로고    scopus 로고
    • The role of calcium and mitochondrial oxidant stress in the loss of substantia nigra pars compacta dopaminergic neurons in Parkinson's disease
    • Surmeier DJ, Guzman JN, Sanchez-Padilla J, Schumacker PT. The role of calcium and mitochondrial oxidant stress in the loss of substantia nigra pars compacta dopaminergic neurons in Parkinson's disease. Neuroscience 198, 221-231 (2011).
    • Neuroscience , vol.198 , Issue.221-231 , pp. 2011
    • Surmeier, D.J.1    Guzman, J.N.2    Sanchez-Padilla, J.3    Schumacker, P.T.4
  • 133
    • 84866729462 scopus 로고    scopus 로고
    • Calcium entry induces mitochondrial oxidant stress in vagal neurons at risk in Parkinson's disease
    • Goldberg JA, Guzman JN, Estep CM et al. Calcium entry induces mitochondrial oxidant stress in vagal neurons at risk in Parkinson's disease. Nat. Neurosci. 15(10), 1414-1421 (2012).
    • (2012) Nat. Neurosci. , vol.15 , Issue.10 , pp. 1414-1421
    • Goldberg, J.A.1    Guzman, J.N.2    Estep, C.M.3
  • 134
    • 84864940539 scopus 로고    scopus 로고
    • L166P mutant DJ-1 promotes cell death by dissociating Bax from mitochondrial Bcl-XL
    • Ren H, Fu K, Mu C, Zhen X, Wang G. L166P mutant DJ-1 promotes cell death by dissociating Bax from mitochondrial Bcl-XL. Mol. Neurodegener. 7, 40 (2012).
    • (2012) Mol. Neurodegener. , vol.7 , Issue.40
    • Ren, H.1    Fu, K.2    Mu, C.3    Zhen, X.4    Wang, G.5
  • 135
    • 84868087279 scopus 로고    scopus 로고
    • ROS-dependent regulation of Parkin and DJ-1 localization during oxidative stress in neurons
    • Joselin AP, Hewitt SJ, Callaghan SM et al. ROS-dependent regulation of Parkin and DJ-1 localization during oxidative stress in neurons. Hum. Mol. Genet. 21(22), 4888-4903 (2012).
    • (2012) Hum. Mol. Genet. , vol.21 , Issue.22 , pp. 4888-4903
    • Joselin, A.P.1    Hewitt, S.J.2    Callaghan, S.M.3
  • 136
    • 84863728713 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 disturbs mitochondrial dynamics via dynamin-like protein
    • Niu J, Yu M, Wang C, Xu Z. Leucine-rich repeat kinase 2 disturbs mitochondrial dynamics via dynamin-like protein. J. Neurochem. 122(3), 650-658 (2012).
    • (2012) J. Neurochem. , vol.122 , Issue.3 , pp. 650-658
    • Niu, J.1    Yu, M.2    Wang, C.3    Xu, Z.4
  • 138
    • 79953231682 scopus 로고    scopus 로고
    • Parkin ubiquitinates Drp1 for proteasome-dependent degradation: Implication of dysregulated mitochondrial dynamics in Parkinson disease
    • Wang H, Song P, Du L et al. Parkin ubiquitinates Drp1 for proteasome-dependent degradation: implication of dysregulated mitochondrial dynamics in Parkinson disease. J. Biol. Chem. 286(13), 11649-11658 (2011).
    • (2011) J. Biol. Chem. , vol.286 , Issue.13 , pp. 11649-11658
    • Wang, H.1    Song, P.2    Du, L.3
  • 139
    • 78650729600 scopus 로고    scopus 로고
    • Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
    • Tanaka A, Cleland MM, Xu S et al. Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin. J. Cell Biol. 191(7), 1367-13802010).
    • (2010) J. Cell Biol. , vol.191 , Issue.7 , pp. 1367-1380
    • Tanaka, A.1    Cleland, M.M.2    Xu, S.3
  • 140
    • 77951235489 scopus 로고    scopus 로고
    • Perturbations in mitochondrial dynamics induced by human mutant PINK1 can be rescued by the mitochondrial division inhibitor mdivi-1
    • Cui M, Tang X, Christian WV, Yoon Y, Tieu K. Perturbations in mitochondrial dynamics induced by human mutant PINK1 can be rescued by the mitochondrial division inhibitor mdivi-1. J. Biol. Chem. 285(15), 11740-11752 (2010).
    • (2010) J. Biol. Chem. , vol.285 , Issue.15 , pp. 11740-11752
    • Cui, M.1    Tang, X.2    Christian, W.V.3    Yoon, Y.4    Tieu, K.5
  • 141
    • 75749156257 scopus 로고    scopus 로고
    • PINK1 is selectively stabilized on impaired mitochondria to activate Parkin
    • Narendra DP, Jin SM, Tanaka A et al. PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biol. 8(1), e1000298 (2010).
    • (2010) PLoS Biol. , vol.8 , Issue.1
    • Narendra, D.P.1    Jin, S.M.2    Tanaka, A.3
  • 142
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group. Cell 72(6), 971-983 (1993).
    • (1993) Cell , vol.72 , Issue.6 , pp. 971-983
  • 143
    • 57649187103 scopus 로고    scopus 로고
    • Mitochondria and Huntington's disease pathogenesis: Insight from genetic and chemical models
    • Browne SE. Mitochondria and Huntington's disease pathogenesis: insight from genetic and chemical models. Ann. NY Acad. Sci. 1147, 358-382 (2008).
    • (2008) Ann. NY Acad. Sci. , vol.1147 , pp. 358-382
    • Browne, S.E.1
  • 144
    • 84863591434 scopus 로고    scopus 로고
    • MRI findings, patterns of disease distribution, and muscle fat fraction calculation in five patients with Charcot-Marie-Tooth type 2 F disease
    • Gaeta M, Mileto A, Mazzeo A et al. MRI findings, patterns of disease distribution, and muscle fat fraction calculation in five patients with Charcot-Marie-Tooth type 2 F disease. Skeletal Radiol. 41(5), 515-524 (2012).
    • (2012) Skeletal Radiol. , vol.41 , Issue.5 , pp. 515-524
    • Gaeta, M.1    Mileto, A.2    Mazzeo, A.3
  • 145
    • 44449131447 scopus 로고    scopus 로고
    • Huntington's disease: From pathology and genetics to potential therapies
    • Imarisio S, Carmichael J, Korolchuk V et al. Huntington's disease: from pathology and genetics to potential therapies. Biochem. J. 412(2), 191-209 (2008).
    • (2008) Biochem. J. , vol.412 , Issue.2 , pp. 191-209
    • Imarisio, S.1    Carmichael, J.2    Korolchuk, V.3
  • 146
    • 69049090808 scopus 로고    scopus 로고
    • Mitochondrial reticulum network dynamics in relation to oxidative stress, redox regulation, and hypoxia
    • Jezek P, Plecitá-Hlavatá L. Mitochondrial reticulum network dynamics in relation to oxidative stress, redox regulation, and hypoxia. Int. J. Biochem. Cell Biol. 41(10), 1790-1804 (2009).
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , Issue.10 , pp. 1790-1804
    • Jezek, P.1    Plecitá-Hlavatá, L.2
  • 147
    • 67349120572 scopus 로고    scopus 로고
    • Complex II inhibition by 3-NP causes mitochondrial fragmentation and neuronal cell death via an NMDA- and ROS-dependent pathway
    • Liot G, Bossy B, Lubitz S, Kushnareva Y, Sejbuk N, Bossy-Wetzel E. Complex II inhibition by 3-NP causes mitochondrial fragmentation and neuronal cell death via an NMDA- and ROS-dependent pathway. Cell Death Differ. 16(6), 899-909 (2009).
    • (2009) Cell Death Differ. , vol.16 , Issue.6 , pp. 899-909
    • Liot, G.1    Bossy, B.2    Lubitz, S.3    Kushnareva, Y.4    Sejbuk, N.5    Bossy-Wetzel, E.6
  • 148
    • 79952443408 scopus 로고    scopus 로고
    • Mutant huntingtin binds the mitochondrial fission GTPase dynamin-related protein-1 and increases its enzymatic activity
    • Song W, Chen J, Petrilli A et al. Mutant huntingtin binds the mitochondrial fission GTPase dynamin-related protein-1 and increases its enzymatic activity. Nat. Med. 17(3), 377-382 (2011).
    • (2011) Nat. Med. , vol.17 , Issue.3 , pp. 377-382
    • Song, W.1    Chen, J.2    Petrilli, A.3
  • 149
    • 78650284389 scopus 로고    scopus 로고
    • Mitochondrial fission and cristae disruption increase the response of cell models of Huntington's disease to apoptotic stimuli
    • Costa V, Giacomello M, Hudec R et al. Mitochondrial fission and cristae disruption increase the response of cell models of Huntington's disease to apoptotic stimuli. EMBO Mol. Med. 2(12), 490-503 (2010).
    • (2010) EMBO Mol. Med. , vol.2 , Issue.12 , pp. 490-503
    • Costa, V.1    Giacomello, M.2    Hudec, R.3
  • 150
    • 84855395163 scopus 로고    scopus 로고
    • Mutant huntingtin's interaction with mitochondrial protein Drp1 impairs mitochondrial biogenesis and causes defective axonal transport and synaptic degeneration in Huntington's disease
    • Shirendeb UP, Calkins MJ, Manczak M et al. Mutant huntingtin's interaction with mitochondrial protein Drp1 impairs mitochondrial biogenesis and causes defective axonal transport and synaptic degeneration in Huntington's disease. Hum. Mol. Genet. 21(2), 406-420 (2012).
    • (2012) Hum. Mol. Genet. , vol.21 , Issue.2 , pp. 406-420
    • Shirendeb, U.P.1    Calkins, M.J.2    Manczak, M.3
  • 151
    • 58949099388 scopus 로고    scopus 로고
    • Effects of overexpression of huntingtin proteins on mitochondrial integrity
    • Wang H, Lim PJ, Karbowski M, Monteiro MJ. Effects of overexpression of huntingtin proteins on mitochondrial integrity. Hum. Mol. Genet. 18(4), 737-752 (2009).
    • (2009) Hum. Mol. Genet. , vol.18 , Issue.4 , pp. 737-752
    • Wang, H.1    Lim, P.J.2    Karbowski, M.3    Monteiro, M.J.4
  • 152
    • 84855165944 scopus 로고    scopus 로고
    • Mutant huntingtin, abnormal mitochondrial dynamics, defective axonal transport of mitochondria, and selective synaptic degeneration in Huntington's disease
    • Reddy PH, Shirendeb UP. Mutant huntingtin, abnormal mitochondrial dynamics, defective axonal transport of mitochondria, and selective synaptic degeneration in Huntington's disease. Biochim. Biophys. Acta 1822(2), 101-110 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1822 , Issue.2 , pp. 101-110
    • Reddy, P.H.1    Shirendeb, U.P.2
  • 153
    • 66749104344 scopus 로고    scopus 로고
    • Mitochondrial function, morphology, and axonal transport in amyotrophic lateral sclerosis
    • Magrane J, Manfredi G. Mitochondrial function, morphology, and axonal transport in amyotrophic lateral sclerosis. Antioxid. Redox Signal. 11(7), 1615-1626 (2009).
    • (2009) Antioxid. Redox Signal. , vol.11 , Issue.7 , pp. 1615-1626
    • Magrane, J.1    Manfredi, G.2
  • 154
    • 84857055792 scopus 로고    scopus 로고
    • Mitochondria in motor nerve terminals: Function in health and in mutant superoxide dismutase 1 mouse models of familial ALS
    • Barrett EF, Barrett JN, David G. Mitochondria in motor nerve terminals: function in health and in mutant superoxide dismutase 1 mouse models of familial ALS. J. Bioenerg. Biomembr. 43(6), 581-586 (2011).
    • (2011) J. Bioenerg. Biomembr. , vol.43 , Issue.6 , pp. 581-586
    • Barrett, E.F.1    Barrett, J.N.2    David, G.3
  • 155
    • 79959462293 scopus 로고    scopus 로고
    • Review: The role of mitochondria in the pathogenesis of amyotrophic lateral sclerosis
    • Duffy LM, Chapman AL, Shaw PJ, Grierson AJ. Review: the role of mitochondria in the pathogenesis of amyotrophic lateral sclerosis. Neuropathol. Appl. Neurobiol. 37(4), 336-352 (2011).
    • (2011) Neuropathol. Appl. Neurobiol. , vol.37 , Issue.4 , pp. 336-352
    • Duffy, L.M.1    Chapman, A.L.2    Shaw, P.J.3    Grierson, A.J.4
  • 156
    • 77955036882 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain dysfunction in muscle from patients with amyotrophic lateral sclerosis
    • Crugnola V, Lamperti C, Lucchini V et al. Mitochondrial respiratory chain dysfunction in muscle from patients with amyotrophic lateral sclerosis. Arch. Neurol. 67(7), 849-854 (2010).
    • (2010) Arch. Neurol. , vol.67 , Issue.7 , pp. 849-854
    • Crugnola, V.1    Lamperti, C.2    Lucchini, V.3
  • 157
    • 0032716335 scopus 로고    scopus 로고
    • Visualization of defective mitochondrial function in skeletal muscle fibers of patients with sporadic amyotrophic lateral sclerosis
    • Vielhaber S, Winkler K, Kirches E et al. Visualization of defective mitochondrial function in skeletal muscle fibers of patients with sporadic amyotrophic lateral sclerosis. J. Neurol. Sci. 169(1-2), 133-139 (1999).
    • (1999) J. Neurol. Sci. , vol.169 , Issue.1-2 , pp. 133-139
    • Vielhaber, S.1    Winkler, K.2    Kirches, E.3
  • 159
    • 70449417623 scopus 로고    scopus 로고
    • Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities
    • Magrane J, Hervias I, Henning MS, Damiano M, Kawamata H, Manfredi G. Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities. Hum. Mol. Genet. 18(23), 4552-4564 (2009).
    • (2009) Hum. Mol. Genet. , vol.18 , Issue.23 , pp. 4552-4564
    • Magrane, J.1    Hervias, I.2    Henning, M.S.3    Damiano, M.4    Kawamata, H.5    Manfredi, G.6
  • 160
    • 77958495868 scopus 로고    scopus 로고
    • Glutaredoxin 2 prevents aggregation of mutant SOD1 in mitochondria and abolishes its toxicity
    • Ferri A, Fiorenzo P, Nencini M et al. Glutaredoxin 2 prevents aggregation of mutant SOD1 in mitochondria and abolishes its toxicity. Hum. Mol. Genet. 19(22), 4529-4542 (2010).
    • (2010) Hum. Mol. Genet. , vol.19 , Issue.22 , pp. 4529-4542
    • Ferri, A.1    Fiorenzo, P.2    Nencini, M.3
  • 161
    • 84872683148 scopus 로고    scopus 로고
    • Mutant SOD1G93A triggers mitochondrial fragmentation in spinal cord motor neurons: Neuroprotection by SIRT3 and PGC-1alpha
    • Song W, Song Y, Kincaid B, Bossy B, Bossy-Wetzel E. Mutant SOD1G93A triggers mitochondrial fragmentation in spinal cord motor neurons: neuroprotection by SIRT3 and PGC-1alpha. Neurobiol. Dis. 51, 72-81 (2012).
    • (2012) Neurobiol. Dis. , vol.51 , pp. 72-81
    • Song, W.1    Song, Y.2    Kincaid, B.3    Bossy, B.4    Bossy-Wetzel, E.5
  • 162
    • 34247574690 scopus 로고    scopus 로고
    • Reactive structural dynamics of synaptic mitochondria in ischemic delayed neuronal death
    • Bertoni-Freddari C, Fattoretti P, Casoli T et al. Reactive structural dynamics of synaptic mitochondria in ischemic delayed neuronal death. Ann. NY Acad. Sci. 1090, 26-34 (2006).
    • (2006) Ann. NY Acad. Sci. , vol.1090 , pp. 26-34
    • Bertoni-Freddari, C.1    Fattoretti, P.2    Casoli, T.3
  • 163
    • 84860640762 scopus 로고    scopus 로고
    • Dynamic changes of mitochondrial fission proteins after transient cerebral ischemia in mice
    • Liu W, Tian F, Kurata T, Morimoto N, Abe K. Dynamic changes of mitochondrial fission proteins after transient cerebral ischemia in mice. Brain Res. 1456, 94-99 (2012).
    • (2012) Brain Res. , vol.1456 , pp. 94-99
    • Liu, W.1    Tian, F.2    Kurata, T.3    Morimoto, N.4    Abe, K.5
  • 164
    • 84862786010 scopus 로고    scopus 로고
    • Dynamic changes of mitochondrial fusion and fission proteins after transient cerebral ischemia in mice
    • Liu W, Tian F, Kurata T, Morimoto N, Abe K. Dynamic changes of mitochondrial fusion and fission proteins after transient cerebral ischemia in mice. J. Neurosci. Res. 90(6), 1183-1189 (2012).
    • (2012) J. Neurosci. Res. , vol.90 , Issue.6 , pp. 1183-1189
    • Liu, W.1    Tian, F.2    Kurata, T.3    Morimoto, N.4    Abe, K.5
  • 165
    • 84865187064 scopus 로고    scopus 로고
    • Inhibition of Drp1 provides neuroprotection in vitro and in vivo
    • Grohm J, Kim SW, Mamrak U et al. Inhibition of Drp1 provides neuroprotection in vitro and in vivo. Cell Death Differ. 19(9), 1446-1458 (2012).
    • (2012) Cell Death Differ. , vol.19 , Issue.9 , pp. 1446-1458
    • Grohm, J.1    Kim, S.W.2    Mamrak, U.3
  • 166
    • 79551649906 scopus 로고    scopus 로고
    • Evidence that OGG1 glycosylase protects neurons against oxidative DNA damage and cell death under ischemic conditions
    • Liu D, Croteau DL, Souza-Pinto N et al. Evidence that OGG1 glycosylase protects neurons against oxidative DNA damage and cell death under ischemic conditions. J. Cereb. Blood Flow Metab. 31(2), 680-692 (2011).
    • (2011) J. Cereb. Blood Flow Metab. , vol.31 , Issue.2 , pp. 680-692
    • Liu, D.1    Croteau, D.L.2    Souza-Pinto, N.3
  • 167
    • 71849114477 scopus 로고    scopus 로고
    • Marine compound Xyloketal B protects PC12 cells against OGD-induced cell damage
    • Zhao J, Li L, Ling C et al. Marine compound Xyloketal B protects PC12 cells against OGD-induced cell damage. Brain Res. 1302, 240-247 (2009).
    • (2009) Brain Res. , vol.1302 , pp. 240-247
    • Zhao, J.1    Li, L.2    Ling, C.3
  • 168
    • 78751470559 scopus 로고    scopus 로고
    • Aberrant mitochondrial fission in neurons induced by protein kinase C{delta} under oxidative stress conditions in vivo
    • Qi X, Disatnik MH, Shen N, Sobel RA, Mochly-Rosen D. Aberrant mitochondrial fission in neurons induced by protein kinase C{delta} under oxidative stress conditions in vivo. Mol. Biol. Cell 22(2), 256-265 (2011).
    • (2011) Mol. Biol. Cell , vol.22 , Issue.2 , pp. 256-265
    • Qi, X.1    Disatnik, M.H.2    Shen, N.3    Sobel, R.A.4    Mochly-Rosen, D.5
  • 169
    • 33746881744 scopus 로고    scopus 로고
    • Mitochondria in DRG neurons undergo hyperglycemic mediated injury through Bim, Bax and the fission protein Drp1
    • Leinninger GM, Backus C, Sastry AM, Yi YB, Wang CW, Feldman EL. Mitochondria in DRG neurons undergo hyperglycemic mediated injury through Bim, Bax and the fission protein Drp1. Neurobiol. Dis. 23(1), 11-22 (2006).
    • (2006) Neurobiol. Dis. , vol.23 , Issue.1 , pp. 11-22
    • Leinninger, G.M.1    Backus, C.2    Sastry, A.M.3    Yi, Y.B.4    Wang, C.W.5    Feldman, E.L.6
  • 170
    • 84862309959 scopus 로고    scopus 로고
    • Enhanced autophagy plays a cardinal role in mitochondrial dysfunction in Type 2 diabetic Goto-Kakizaki (GK) rats: Ameliorating effects of (-)-epigallocatechin-3-gallate
    • Yan J, Feng Z, Liu J et al. Enhanced autophagy plays a cardinal role in mitochondrial dysfunction in Type 2 diabetic Goto-Kakizaki (GK) rats: ameliorating effects of (-)-epigallocatechin-3-gallate. J. Nutr. Biochem. 23(7), 716-724 (2012).
    • (2012) J. Nutr. Biochem. , vol.23 , Issue.7 , pp. 716-724
    • Yan, J.1    Feng, Z.2    Liu, J.3
  • 171
    • 84855389514 scopus 로고    scopus 로고
    • Diabetic retinopathy and damage to mitochondrial structure and transport machinery
    • Zhong Q, Kowluru R A. Diabetic retinopathy and damage to mitochondrial structure and transport machinery. Invest. Ophthalmol. Vis. Sci. 52(12), 8739-8746 (2011).
    • (2011) Invest. Ophthalmol. Vis. Sci. , vol.52 , Issue.12 , pp. 8739-8746
    • Zhong, Q.1    Kowluru, R.A.2
  • 172
    • 38849099158 scopus 로고    scopus 로고
    • Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer membrane permeabilization
    • Cassidy-Stone A, Chipuk JE, Ingerman E et al. Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer membrane permeabilization. Dev. Cell 14(2), 193-204 (2008).
    • (2008) Dev. Cell , vol.14 , Issue.2 , pp. 193-204
    • Cassidy-Stone, A.1    Chipuk, J.E.2    Ingerman, E.3
  • 173
    • 39549092425 scopus 로고    scopus 로고
    • A chemical inhibitor of DRP1 uncouples mitochondrial fission and apoptosis
    • Tanaka A, Youle RJ. A chemical inhibitor of DRP1 uncouples mitochondrial fission and apoptosis. Mol. Cell 29(4), 409-410 (2008).
    • (2008) Mol. Cell , vol.29 , Issue.4 , pp. 409-410
    • Tanaka, A.1    Youle, R.J.2
  • 174
    • 66449121454 scopus 로고    scopus 로고
    • Regulation of mitochondrial dynamics in acute kidney injury in cell culture and rodent models
    • Brooks C, Wei Q, Cho SG, Dong Z. Regulation of mitochondrial dynamics in acute kidney injury in cell culture and rodent models. J. Clin. Invest. 119(5), 1275-1285 (2009).
    • (2009) J. Clin. Invest. , vol.119 , Issue.5 , pp. 1275-1285
    • Brooks, C.1    Wei, Q.2    Cho, S.G.3    Dong, Z.4
  • 175
    • 79961238706 scopus 로고    scopus 로고
    • Role of Drp1, a key mitochondrial fission protein, in neuropathic pain
    • Ferrari LF, Chum A, Bogen O, Reichling DB, Levine JD. Role of Drp1, a key mitochondrial fission protein, in neuropathic pain. J. Neurosci. 31(31), 11404-11410 (2011).
    • (2011) J. Neurosci. , vol.31 , Issue.31 , pp. 11404-11410
    • Ferrari, L.F.1    Chum, A.2    Bogen, O.3    Reichling, D.B.4    Levine, J.D.5
  • 176
    • 77952236126 scopus 로고    scopus 로고
    • Inhibiting mitochondrial fission protects the heart against ischemia/reperfusion injury
    • Ong SB, Subrayan S, Lim SY, Yellon DM, Davidson SM, Hausenloy DJ. Inhibiting mitochondrial fission protects the heart against ischemia/reperfusion injury. Circulation 121(18), 2012-2022 (2010).
    • (2010) Circulation , vol.121 , Issue.18 , pp. 2012-2022
    • Ong, S.B.1    Subrayan, S.2    Lim, S.Y.3    Yellon, D.M.4    Davidson, S.M.5    Hausenloy, D.J.6
  • 177
    • 38149091885 scopus 로고    scopus 로고
    • Sustained pharmacological inhibition of deltaPKC protects against hypertensive encephalopathy through prevention of blood-brain barrier breakdown in rats
    • Qi X, Inagaki K, Sobel RA, Mochly-Rosen D. Sustained pharmacological inhibition of deltaPKC protects against hypertensive encephalopathy through prevention of blood-brain barrier breakdown in rats. J. Clin. Invest. 118(1), 173-182 (2008).
    • (2008) J. Clin. Invest. , vol.118 , Issue.1 , pp. 173-182
    • Qi, X.1    Inagaki, K.2    Sobel, R.A.3    Mochly-Rosen, D.4
  • 178
    • 3843146318 scopus 로고    scopus 로고
    • Protein kinase C delta mediates cerebral reperfusion injury in vivo
    • Bright R, Raval AP, Dembner JM et al. Protein kinase C delta mediates cerebral reperfusion injury in vivo. J. Neurosci. 24(31), 6880-6888 (2004).
    • (2004) J. Neurosci. , vol.24 , Issue.31 , pp. 6880-6888
    • Bright, R.1    Raval, A.P.2    Dembner, J.M.3
  • 179
    • 84876312885 scopus 로고    scopus 로고
    • Novel Drp1 inhibitor diminishes aberrant mitochondrial fission and neurotoxicity
    • doi:10.1242/jcs.114439 Epub ahead of print
    • Qi X, Qvit N, Su YC, Mochly-Rosen D. Novel Drp1 inhibitor diminishes aberrant mitochondrial fission and neurotoxicity. J. Cell Sci. doi:10.1242/jcs.114439 (2012) (Epub ahead of print).
    • (2012) J. Cell Sci.
    • Qi, X.1    Qvit, N.2    Su, Y.C.3    Mochly-Rosen, D.4
  • 180
    • 25444474703 scopus 로고    scopus 로고
    • Mitochondria take center stage in aging and neurodegeneration
    • Beal MF. Mitochondria take center stage in aging and neurodegeneration. Ann. Neurol. 58, 495-505 (2005).
    • (2005) Ann. Neurol. , vol.58 , pp. 495-505
    • Beal, M.F.1
  • 181
    • 34047173074 scopus 로고    scopus 로고
    • Mitochondrial bioenergetics and structural network organization
    • Benard G, Bellance N, James D et al. Mitochondrial bioenergetics and structural network organization. J. Cell Sci. 120, 838-848 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 838-848
    • Benard, G.1    Bellance, N.2    James, D.3


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