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Volumn 9, Issue MAY, 2015, Pages

How the Wnt signaling pathway protects from neurodegeneration: The mitochondrial scenario

Author keywords

Alzheimer s disease; Amyloid beta; Drp1; Electron microscopy; Mitochondrial dynamics; Permeability transition; Wnt

Indexed keywords

1, 2, 3, 6 TETRAHYDRO 1 METHYL 4 PHENYLPYRIDINE; ALPHA SYNUCLEIN; AMYLOID; AMYLOID BETA PROTEIN; CYCLOPHILIN D; DYNAMIN; GLYCOGEN SYNTHASE KINASE 3BETA; HEXOKINASE; LIGAND; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; MITOFUSIN 1; MITOFUSIN 2; N BENZYL 1, 2, 3, 4, 8, 9 HEXAHYDRO 6 (4 HYDROXYBENZYL) 8 (1 NAPHTHYLMETHYL) 4, 7 DIOXO 2H PYRAZINO [1, 2 A] PYRIMIDINE 1 (6H) CARBOXAMIDE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; OLIGOMER; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; WNT3A LIGAND; WNT5A LIGAND;

EID: 84929579761     PISSN: 16625102     EISSN: None     Source Type: Journal    
DOI: 10.3389/fncel.2015.00166     Document Type: Article
Times cited : (57)

References (170)
  • 1
    • 84859107964 scopus 로고    scopus 로고
    • Cellular models to investigate biochemical pathways in Parkinson’s disease
    • Alberio, T., Lopiano, L., and Fasano, M. (2012). Cellular models to investigate biochemical pathways in Parkinson’s disease. FEBS J. 279, 1146-1155. doi: 10.1111/j.1742-4658.2012.08516.x
    • (2012) FEBS J , vol.279 , pp. 1146-1155
    • Alberio, T.1    Lopiano, L.2    Fasano, M.3
  • 2
    • 0027330273 scopus 로고
    • Characterization of Ca2+ signals induced in hippocampal CA1 neurones by the synaptic activation of NMDA receptors
    • Alford, S., Frenguelli, B. G., Schofield, J. G., and Collingridge, G. L. (1993). Characterization of Ca2+ signals induced in hippocampal CA1 neurones by the synaptic activation of NMDA receptors. J. Physiol. 469, 693-716. doi: 10.1113/jphysiol.1993.sp019838
    • (1993) J. Physiol , vol.469 , pp. 693-716
    • Alford, S.1    Frenguelli, B.G.2    Schofield, J.G.3    Collingridge, G.L.4
  • 3
    • 2942578107 scopus 로고    scopus 로고
    • Wnt-3a overcomes beta-amyloid toxicity in rat hippocampal neurons. Exp
    • Alvarez, A. R., Godoy, J. A., Mullendorff, K., Olivares, G. H., Bronfman, M., and Inestrosa, N. C. (2004). Wnt-3a overcomes beta-amyloid toxicity in rat hippocampal neurons. Exp. Cell Res. 297, 186-196. doi: 10.1016/j.yexcr.2004.02.028
    • (2004) Cell Res , vol.297 , pp. 186-196
    • Alvarez, A.R.1    Godoy, J.A.2    Mullendorff, K.3    Olivares, G.H.4    Bronfman, M.5    Inestrosa, N.C.6
  • 5
    • 84921717789 scopus 로고    scopus 로고
    • (2015). ‘‘Monitoring mitochondrial membranes permeability in live neurons and mitochondrial swelling through electron microscopy analysis,’’
    • eds L. Lossi and A. Merighi (New York: Springer
    • Arrázola, M. S., and Inestrosa, N. C. (2015). ‘‘Monitoring mitochondrial membranes permeability in live neurons and mitochondrial swelling through electron microscopy analysis,’’ in Neuronal Cell Death. Methods in Molecular Biology (Vol. 1254), eds L. Lossi and A. Merighi (New York: Springer), 87-97.
    • Neuronal Cell Death. Methods in Molecular Biology (Vol. 1254) , pp. 87-97
    • Arrázola, M.S.1    Inestrosa, N.C.2
  • 6
    • 70449699789 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase type IV is a target gene of the Wnt/beta-catenin signaling pathway
    • Arrázola, M. S., Varela-Nallar, L., Colombres, M., Toledo, E. M., Cruzat, F., Pavez, L., et al. (2009). Calcium/calmodulin-dependent protein kinase type IV is a target gene of the Wnt/beta-catenin signaling pathway. J. Cell. Physiol. 221, 658-667. doi: 10.1002/jcp.21902
    • (2009) J. Cell. Physiol , vol.221 , pp. 658-667
    • Arrázola, M.S.1    Varela-Nallar, L.2    Colombres, M.3    Toledo, E.M.4    Cruzat, F.5    Pavez, L.6
  • 7
    • 0031017323 scopus 로고    scopus 로고
    • Mitochondrial participation in the intracellular Ca2+ network
    • Babcock, D. F., Herrington, J., Goodwin, P. C., Park, Y. B., and Hille, B. (1997). Mitochondrial participation in the intracellular Ca2+ network. J. Cell Biol. 136, 833-844. doi: 10.1083/jcb.136.4.833
    • (1997) J. Cell Biol , vol.136 , pp. 833-844
    • Babcock, D.F.1    Herrington, J.2    Goodwin, P.C.3    Park, Y.B.4    Hille, B.5
  • 8
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., et al. (2005). Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 434, 658-662. doi: 10.1038/nature03434
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1    Kaiser, R.A.2    Purcell, N.H.3    Blair, N.S.4    Osinska, H.5    Hambleton, M.A.6
  • 9
    • 84876374851 scopus 로고    scopus 로고
    • Early selective vulnerability of synapses and synaptic mitochondria in the hippocampal CA1 region of the Tg2576 mouse model of Alzheimer’s disease
    • Balietti, M., Giorgetti, B., Casoli, T., Solazzi, M., Tamagnini, F., Burattini, C., et al. (2013). Early selective vulnerability of synapses and synaptic mitochondria in the hippocampal CA1 region of the Tg2576 mouse model of Alzheimer’s disease. J. Alzheimers Dis. 34, 887-896. doi: 10.3233/JAD-121711
    • (2013) J. Alzheimers Dis , vol.34 , pp. 887-896
    • Balietti, M.1    Giorgetti, B.2    Casoli, T.3    Solazzi, M.4    Tamagnini, F.5    Burattini, C.6
  • 10
    • 33748028841 scopus 로고    scopus 로고
    • Nitric oxide-induced mitochondrial fission is regulated by dynamin-related GTPases in neurons
    • Barsoum, M. J., Yuan, H., Gerencser, A. A., Liot, G., Kushnareva, Y., Gräber, S., et al. (2006). Nitric oxide-induced mitochondrial fission is regulated by dynamin-related GTPases in neurons. EMBO J. 25, 3900-3911. doi: 10.1038/sj.emboj.7601253
    • (2006) EMBO J , vol.25 , pp. 3900-3911
    • Barsoum, M.J.1    Yuan, H.2    Gerencser, A.A.3    Liot, G.4    Kushnareva, Y.5    Gräber, S.6
  • 11
    • 67349093525 scopus 로고    scopus 로고
    • Clearance mechanisms of Alzheimer’s amyloid-beta peptide: Implications for therapeutic design and diagnostic tests
    • Bates, K. A., Verdile, G., Li, Q.-X., Ames, D., Hudson, P., Masters, C. L., et al. (2009). Clearance mechanisms of Alzheimer’s amyloid-beta peptide: implications for therapeutic design and diagnostic tests. Mol. Psychiatry 14, 469-486. doi: 10.1038/mp.2008.96
    • (2009) Mol. Psychiatry , vol.14 , pp. 469-486
    • Bates, K.A.1    Verdile, G.2    Li, Q.-X.3    Ames, D.4    Hudson, P.5    Masters, C.L.6
  • 12
    • 0032127595 scopus 로고    scopus 로고
    • Neuronal calcium signaling
    • Berridge, M. J. (1998). Neuronal calcium signaling. Neuron 21, 13-26. doi: 10.1016/s0896-6273(00)80510-3
    • (1998) Neuron , vol.21 , pp. 13-26
    • Berridge, M.J.1
  • 13
    • 79959907270 scopus 로고    scopus 로고
    • Calcium signalling and Alzheimer’s disease
    • Berridge, M. J. (2011). Calcium signalling and Alzheimer’s disease. Neurochem. Res. 36, 1149-1156. doi: 10.1007/s11064-010-0371-4
    • (2011) Neurochem. Res , vol.36 , pp. 1149-1156
    • Berridge, M.J.1
  • 14
    • 50249135503 scopus 로고    scopus 로고
    • Neuronal calcium mishandling and the pathogenesis of Alzheimer’s disease
    • Bezprozvanny, I., and Mattson, M. P. (2008). Neuronal calcium mishandling and the pathogenesis of Alzheimer’s disease. Trends Neurosci. 31, 454-463. doi: 10.1016/j.tins.2008.06.005
    • (2008) Trends Neurosci , vol.31 , pp. 454-463
    • Bezprozvanny, I.1    Mattson, M.P.2
  • 15
    • 0037101606 scopus 로고    scopus 로고
    • Presynaptic mitochondrial calcium sequestration influences transmission at mammalian central synapses
    • Billups, B., and Forsythe, I. D. (2002). Presynaptic mitochondrial calcium sequestration influences transmission at mammalian central synapses. J. Neurosci. 22, 5840-5847.
    • (2002) J. Neurosci , vol.22 , pp. 5840-5847
    • Billups, B.1    Forsythe, I.D.2
  • 16
    • 84859108554 scopus 로고    scopus 로고
    • Animal models of Parkinson’s disease
    • Blandini, F., and Armentero, M.-T. (2012). Animal models of Parkinson’s disease. FEBS J. 279, 1156-1166. doi: 10.1111/j.1742-4658.2012.08491.x
    • (2012) FEBS J , vol.279 , pp. 1156-1166
    • Blandini, F.1    Armentero, M.-T.2
  • 17
    • 84926258887 scopus 로고    scopus 로고
    • Disturbed mitochondrial dynamics and neurodegenerative disorders
    • Burté, F., Carelli, V., Chinnery, P. F., and Yu-Wai-Man, P. (2015). Disturbed mitochondrial dynamics and neurodegenerative disorders. Nat. Rev. Neurol. 11, 11-24. doi: 10.1038/nrneurol.2014.228
    • (2015) Nat. Rev. Neurol , vol.11 , pp. 11-24
    • Burté, F.1    Carelli, V.2    Chinnery, P.F.3    Yu-Wai-Man, P.4
  • 18
    • 0032810909 scopus 로고    scopus 로고
    • β-Amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria
    • Canevari, L., Clark, J. B., and Bates, T. E. (1999). β-Amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria. FEBS Lett. 457, 131-134. doi: 10.1016/s0014-5793(99)01028-5
    • (1999) FEBS Lett , vol.457 , pp. 131-134
    • Canevari, L.1    Clark, J.B.2    Bates, T.E.3
  • 19
    • 28744449206 scopus 로고    scopus 로고
    • Mitochondrial Aβ: A potential focal point for neuronal metabolic dysfunction in Alzheimer’s disease
    • Caspersen, C., Wang, N., Yao, J., Sosunov, A., Chen, X., Lustbader, J. W., et al. (2005). Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer’s disease. FASEB J. 19, 2040-2041. doi: 10.1096/fj.05-3735fje
    • (2005) FASEB J , vol.19 , pp. 2040-2041
    • Caspersen, C.1    Wang, N.2    Yao, J.3    Sosunov, A.4    Chen, X.5    Lustbader, J.W.6
  • 20
    • 65449139544 scopus 로고    scopus 로고
    • Mitochondria, calcium and cell death: A deadly triad in neurodegeneration
    • Celsi, F., Pizzo, P., Brini, M., Leo, S., Fotino, C., Pinton, P., et al. (2009). Mitochondria, calcium and cell death: a deadly triad in neurodegeneration. Biochim. Biophys. Acta 1787, 335-344. doi: 10.1016/j.bbabio.2009.02.021
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 335-344
    • Celsi, F.1    Pizzo, P.2    Brini, M.3    Leo, S.4    Fotino, C.5    Pinton, P.6
  • 22
    • 45249108473 scopus 로고    scopus 로고
    • Structure-function implications in Alzheimer’s disease: Effect of Aβ oligomers at central synapses
    • Cerpa, W., Dinamarca, M. C., and Inestrosa, N. C. (2008). Structure-function implications in Alzheimer’s disease: effect of Aβ oligomers at central synapses. Curr. Alzheimer Res. 5, 233-243. doi: 10.2174/156720508784533321
    • (2008) Curr. Alzheimer Res , vol.5 , pp. 233-243
    • Cerpa, W.1    Dinamarca, M.C.2    Inestrosa, N.C.3
  • 23
    • 77249117920 scopus 로고    scopus 로고
    • Wnt-5a occludes Aβ oligomer-induced depression of glutamatergic transmission in hippocampal neurons
    • Cerpa, W., Farías, G. G., Godoy, J. A., Fuenzalida, M., Bonansco, C., and Inestrosa, N. C. (2010). Wnt-5a occludes Aβ oligomer-induced depression of glutamatergic transmission in hippocampal neurons. Mol. Neurodegener. 5:3. doi: 10.1186/1750-1326-5-3
    • (2010) Mol. Neurodegener , vol.5 , pp. 3
    • Cerpa, W.1    Farías, G.G.2    Godoy, J.A.3    Fuenzalida, M.4    Bonansco, C.5    Inestrosa, N.C.6
  • 25
    • 49649088889 scopus 로고    scopus 로고
    • Frizzled-1 is involved in the neuroprotective effect of Wnt3a against Aβ oligomers
    • Chacón, M. A., Varela-Nallar, L., and Inestrosa, N. C. (2008). Frizzled-1 is involved in the neuroprotective effect of Wnt3a against Aβ oligomers. J. Cell. Physiol. 217, 215-227. doi: 10.1002/jcp.21497
    • (2008) J. Cell. Physiol , vol.217 , pp. 215-227
    • Chacón, M.A.1    Varela-Nallar, L.2    Inestrosa, N.C.3
  • 26
    • 77955298543 scopus 로고    scopus 로고
    • Dynamic regulation of mitochondrial fission through modification of the dynamin-related protein Drp1
    • Chang, C.-R., and Blackstone, C. (2010). Dynamic regulation of mitochondrial fission through modification of the dynamin-related protein Drp1. Ann. N Y Acad. Sci. 1201, 34-39. doi: 10.1111/j.1749-6632.2010.05629.x
    • (2010) Ann. N Y Acad. Sci , vol.1201 , pp. 34-39
    • Chang, C.-R.1    Blackstone, C.2
  • 27
    • 77957798188 scopus 로고    scopus 로고
    • A lethal de novo mutation in the middle domain of the dynamin-related GTPase Drp1 impairs higher order assembly and mitochondrial division
    • Chang, C.-R., Manlandro, C. M., Arnoult, D., Stadler, J., Posey, A. E., Hill, R. B., et al. (2010). A lethal de novo mutation in the middle domain of the dynamin-related GTPase Drp1 impairs higher order assembly and mitochondrial division. J. Biol. Chem. 285, 32494-32503. doi: 10.1074/jbc.m110.142430
    • (2010) J. Biol. Chem , vol.285 , pp. 32494-32503
    • Chang, C.-R.1    Manlandro, C.M.2    Arnoult, D.3    Stadler, J.4    Posey, A.E.5    Hill, R.B.6
  • 28
    • 77956201762 scopus 로고    scopus 로고
    • Role of mitochondrial amyloid-beta in Alzheimer’s disease
    • Chen, J. X., and Yan, S. S. (2010). Role of mitochondrial amyloid-beta in Alzheimer’s disease. J. Alzheimers Dis. 20(Suppl. 2), S569-S578. doi: 10.3233/JAD-2010-100357
    • (2010) J. Alzheimers Dis , vol.20 , pp. 569-578
    • Chen, J.X.1    Yan, S.S.2
  • 29
    • 46649106720 scopus 로고    scopus 로고
    • Hexokinase II detachment from mitochondria triggers apoptosis through the permeability transition pore independent of voltage-dependent anion channels
    • Chiara, F., Castellaro, D., Marin, O., Petronilli, V., Brusilow, W. S., Juhaszova, M., et al. (2008). Hexokinase II detachment from mitochondria triggers apoptosis through the permeability transition pore independent of voltage-dependent anion channels. PLoS One 3:e1852. doi: 10.1371/journal.pone.0001852
    • (2008) Plos One , vol.3
    • Chiara, F.1    Castellaro, D.2    Marin, O.3    Petronilli, V.4    Brusilow, W.S.5    Juhaszova, M.6
  • 30
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury
    • Cho, D.-H., Nakamura, T., Fang, J., Cieplak, P., Godzik, A., Gu, Z., et al. (2009). S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury. Science 324, 102-105. doi: 10.1126/science.1171091
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.-H.1    Nakamura, T.2    Fang, J.3    Cieplak, P.4    Godzik, A.5    Gu, Z.6
  • 31
    • 77952515576 scopus 로고    scopus 로고
    • An overview of APP processing enzymes and products
    • Chow, V. W., Mattson, M. P., Wong, P. C., and Gleichmann, M. (2010). An overview of APP processing enzymes and products. Neuromolecular Med. 12, 1-12. doi: 10.1007/s12017-009-8104-z
    • (2010) Neuromolecular Med , vol.12 , pp. 1-12
    • Chow, V.W.1    Mattson, M.P.2    Wong, P.C.3    Gleichmann, M.4
  • 33
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function
    • Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., et al. (2005). Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat. Neurosci. 8, 79-84. doi: 10.1038/nn1372
    • (2005) Nat. Neurosci , vol.8 , pp. 79-84
    • Cleary, J.P.1    Walsh, D.M.2    Hofmeister, J.J.3    Shankar, G.M.4    Kuskowski, M.A.5    Selkoe, D.J.6
  • 34
    • 84861986053 scopus 로고    scopus 로고
    • Wnt/β-catenin signaling and disease
    • Clevers, H., and Nusse, R. (2012). Wnt/β-catenin signaling and disease. Cell 149, 1192-1205. doi: 10.1016/j.cell.2012.05.012
    • (2012) Cell , vol.149 , pp. 1192-1205
    • Clevers, H.1    Nusse, R.2
  • 35
    • 0028075423 scopus 로고
    • Recruitment of mitochondrial cyclophilin to the mitochondrial inner membrane under conditions of oxidative stress that enhance the opening of a calcium-sensitive non-specific channel
    • Connern, C. P., and Halestrap, A. P. (1994). Recruitment of mitochondrial cyclophilin to the mitochondrial inner membrane under conditions of oxidative stress that enhance the opening of a calcium-sensitive non-specific channel. Biochem. J. 302(Pt. 2), 321-324.
    • (1994) Biochem. J , vol.302 , pp. 321-324
    • Connern, C.P.1    Halestrap, A.P.2
  • 36
    • 34848840991 scopus 로고    scopus 로고
    • Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death
    • Cribbs, J. T., and Strack, S. (2007). Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death. EMBO Rep. 8, 939-944. doi: 10.1038/sj.embor.7401062
    • (2007) EMBO Rep , vol.8 , pp. 939-944
    • Cribbs, J.T.1    Strack, S.2
  • 37
    • 0032401567 scopus 로고    scopus 로고
    • Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore
    • Crompton, M., Virji, S., and Ward, J. M. (1998). Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore. Eur. J. Biochem. 258, 729-735. doi: 10.1046/j.1432-1327.1998.2580729.x
    • (1998) Eur. J. Biochem , vol.258 , pp. 729-735
    • Crompton, M.1    Virji, S.2    Ward, J.M.3
  • 38
    • 77954118871 scopus 로고    scopus 로고
    • Wnt-5a modulates recycling of functional GABAA receptors on hippocampal neurons
    • Cuitino, L., Godoy, J. A., Farías, G. G., Couve, A., Bonansco, C., Fuenzalida, M., et al. (2010). Wnt-5a modulates recycling of functional GABAA receptors on hippocampal neurons. J. Neurosci. 30, 8411-8420. doi: 10.1523/JNEUROSCI.5736-09.2010
    • (2010) J. Neurosci , vol.30 , pp. 8411-8420
    • Cuitino, L.1    Godoy, J.A.2    Farías, G.G.3    Couve, A.4    Bonansco, C.5    Fuenzalida, M.6
  • 39
    • 0037220599 scopus 로고    scopus 로고
    • Activation of Wnt signaling rescues neurodegeneration and behavioral impairments induced by beta-amyloid fibrils
    • De Ferrari, G. V., Chacón, M. A., Barría, M. I., Garrido, J. L., Godoy, J. A., Olivares, G., et al. (2003). Activation of Wnt signaling rescues neurodegeneration and behavioral impairments induced by beta-amyloid fibrils. Mol. Psychiatry 8, 195-208. doi: 10.1038/sj.mp.4001208
    • (2003) Mol. Psychiatry , vol.8 , pp. 195-208
    • De Ferrari, G.V.1    Chacón, M.A.2    Barría, M.I.3    Garrido, J.L.4    Godoy, J.A.5    Olivares, G.6
  • 40
    • 0033850796 scopus 로고    scopus 로고
    • Wnt signaling function in Alzheimer’s disease
    • De Ferrari, G. V., and Inestrosa, N. C. (2000). Wnt signaling function in Alzheimer’s disease. Brain Res. Brain Res. Rev. 33, 1-12. doi: 10.1016/S0165-0173(00)00021-7
    • (2000) Brain Res. Brain Res. Rev , vol.33 , pp. 1-12
    • De Ferrari, G.V.1    Inestrosa, N.C.2
  • 41
    • 77951251848 scopus 로고    scopus 로고
    • Calcium signaling and amyloid toxicity in Alzheimer disease
    • Demuro, A., Parker, I., and Stutzmann, G. E. (2010). Calcium signaling and amyloid toxicity in Alzheimer disease. J. Biol. Chem. 285, 12463-12468. doi: 10.1074/jbc.R109.080895
    • (2010) J. Biol. Chem , vol.285 , pp. 12463-12468
    • Demuro, A.1    Parker, I.2    Stutzmann, G.E.3
  • 42
  • 43
    • 35448960851 scopus 로고    scopus 로고
    • Functions and dysfunctions of mitochondrial dynamics
    • Detmer, S. A., and Chan, D. C. (2007). Functions and dysfunctions of mitochondrial dynamics. Nat. Rev. Mol. Cell Biol. 8, 870-879. doi: 10.1038/nrm2275
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 870-879
    • Detmer, S.A.1    Chan, D.C.2
  • 44
    • 71949090833 scopus 로고    scopus 로고
    • Mitochondrial trafficking of APP and alpha synuclein: Relevance to mitochondrial dysfunction in Alzheimer’s and Parkinson’s diseases
    • Devi, L., and Anandatheerthavarada, H. K. (2010). Mitochondrial trafficking of APP and alpha synuclein: relevance to mitochondrial dysfunction in Alzheimer’s and Parkinson’s diseases. Biochim. Biophys. Acta 1802, 11-19. doi: 10.1016/j.bbadis.2009.07.007
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 11-19
    • Devi, L.1    Anandatheerthavarada, H.K.2
  • 45
    • 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, B. M., Galati, D. F., Avadhani, N. G., and Anandatheerthavarada, H. K. (2006). Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer’s disease brain is associated with mitochondrial dysfunction. J. Neurosci. 26, 9057-9068. doi: 10.1523/jneurosci.1469-06.2006
    • (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
  • 46
    • 33750284656 scopus 로고    scopus 로고
    • Hyperforin prevents β-amyloid neurotoxicity and spatial memory impairments by disaggregation of Alzheimer’s amyloid-beta-deposits
    • Dinamarca, M. C., Cerpa, W., Garrido, J., Hancke, J. L., and Inestrosa, N. C. (2006). Hyperforin prevents β-amyloid neurotoxicity and spatial memory impairments by disaggregation of Alzheimer’s amyloid-beta-deposits. Mol. Psychiatry 11, 1032-1048. doi: 10.1038/sj.mp.4001866
    • (2006) Mol. Psychiatry , vol.11 , pp. 1032-1048
    • Dinamarca, M.C.1    Cerpa, W.2    Garrido, J.3    Hancke, J.L.4    Inestrosa, N.C.5
  • 47
    • 77249136019 scopus 로고    scopus 로고
    • Amyloid-β-Acetylcholinesterase complexes potentiate neurodegenerative changes induced by the Aβ peptide. Implications for the pathogenesis of Alzheimer’s disease
    • Dinamarca, M. C., Sagal, J. P., Quintanilla, R. A., Godoy, J. A., Arrázola, M. S., and Inestrosa, N. C. (2010). Amyloid-β-Acetylcholinesterase complexes potentiate neurodegenerative changes induced by the Aβ peptide. Implications for the pathogenesis of Alzheimer’s disease. Mol. Neurodegener. 5:4. doi: 10.1186/1750-1326-5-4
    • (2010) Mol. Neurodegener , vol.5 , pp. 4
    • Dinamarca, M.C.1    Sagal, J.P.2    Quintanilla, R.A.3    Godoy, J.A.4    Arrázola, M.S.5    Inestrosa, N.C.6
  • 48
    • 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., Chen, D., Sosunov, A. A., McKhann, G. M., et al. (2008). Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer’s disease. Nat. Med. 14, 1097-1105. doi: 10.1038/nm.1868
    • (2008) Nat. Med , vol.14 , pp. 1097-1105
    • Du, H.1    Guo, L.2    Fang, F.3    Chen, D.4    Sosunov, A.A.5    McKhann, G.M.6
  • 49
    • 78649815388 scopus 로고    scopus 로고
    • Early deficits in synaptic mitochondria in an Alzheimer’s disease mouse model
    • Du, H., Guo, L., Yan, S., Sosunov, A. A., McKhann, G. M., and Yan, S. S. (2010). Early deficits in synaptic mitochondria in an Alzheimer’s disease mouse model. Proc. Natl. Acad. Sci. U S A 107, 18670-18675. doi: 10.1073/pnas.1006586107
    • (2010) Proc. Natl. Acad. Sci. U S A , vol.107 , pp. 18670-18675
    • Du, H.1    Guo, L.2    Yan, S.3    Sosunov, A.A.4    McKhann, G.M.5    Yan, S.S.6
  • 50
    • 77649184822 scopus 로고    scopus 로고
    • Mitochondrial medicine for neurodegenerative diseases
    • Du, H., and Yan, S. S. (2010a). Mitochondrial medicine for neurodegenerative diseases. Int. J. Biochem. Cell Biol. 42, 560-572. doi: 10.1016/j.biocel.2010.01.004
    • (2010) Int. J. Biochem. Cell Biol , vol.42 , pp. 560-572
    • Du, H.1    Yan, S.S.2
  • 51
    • 72149118206 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore in Alzheimer’s disease: Cyclophilin D and amyloid beta
    • Du, H., and Yan, S. S. (2010b). Mitochondrial permeability transition pore in Alzheimer’s disease: cyclophilin D and amyloid beta. Biochim. Biophys. Acta 1802, 198-204. doi: 10.1016/j.bbadis.2009.07.005
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 198-204
    • Du, H.1    Yan, S.S.2
  • 52
    • 0642375798 scopus 로고    scopus 로고
    • Mitochondrial dysfunction, apoptotic cell death and Alzheimer’s disease
    • Eckert, A., Keil, U., Marques, C. A., Bonert, A., Frey, C., Schüssel, K., et al. (2003). Mitochondrial dysfunction, apoptotic cell death and Alzheimer’s disease. Biochem. Pharmacol. 66, 1627-1634. doi: 10.1016/s0006-2952(03)00534-3
    • (2003) Biochem. Pharmacol , vol.66 , pp. 1627-1634
    • Eckert, A.1    Keil, U.2    Marques, C.A.3    Bonert, A.4    Frey, C.5    Schüssel, K.6
  • 53
    • 65649097647 scopus 로고    scopus 로고
    • Cyclophilin D interacts with Bcl2 and exerts an anti-apoptotic effect
    • Eliseev, R. A., Malecki, J., Lester, T., Zhang, Y., Humphrey, J., and Gunter, T. E. (2009). Cyclophilin D interacts with Bcl2 and exerts an anti-apoptotic effect. J. Biol. Chem. 284, 9692-9699. doi: 10.1074/jbc.M808750200
    • (2009) J. Biol. Chem , vol.284 , pp. 9692-9699
    • Eliseev, R.A.1    Malecki, J.2    Lester, T.3    Zhang, Y.4    Humphrey, J.5    Gunter, T.E.6
  • 54
    • 4344587136 scopus 로고    scopus 로고
    • A small molecule inhibitor of beta-catenin/CREB-binding protein transcription
    • Emami, K. H., Nguyen, C., Ma, H., Kim, D. H., Jeong, K. W., Eguchi, M., et al. (2004). A small molecule inhibitor of beta-catenin/CREB-binding protein transcription. Proc. Natl. Acad. Sci. U S A 101, 12682-12687. doi: 10.1073/pnas.0404875101
    • (2004) Proc. Natl. Acad. Sci. U S A , vol.101 , pp. 12682-12687
    • Emami, K.H.1    Nguyen, C.2    Ma, H.3    Kim, D.H.4    Jeong, K.W.5    Eguchi, M.6
  • 55
    • 0142058391 scopus 로고    scopus 로고
    • Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion
    • Eura, Y., Ishihara, N., Yokota, S., and Mihara, K. (2003). Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion. J. Biochem. 134, 333-344. doi: 10.1093/jb/mvg150
    • (2003) J. Biochem , vol.134 , pp. 333-344
    • Eura, Y.1    Ishihara, N.2    Yokota, S.3    Mihara, K.4
  • 56
    • 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., Holmström, K., Schiesling, C., Gispert, S., et al. (2007). Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin. J. Neurosci. 27, 12413-12418. doi: 10.1523/jneurosci.0719-07.2007
    • (2007) J. Neurosci , vol.27 , pp. 12413-12418
    • Exner, N.1    Treske, B.2    Paquet, D.3    Holmström, K.4    Schiesling, C.5    Gispert, S.6
  • 57
    • 67650136764 scopus 로고    scopus 로고
    • Wnt-5a/JNK signaling promotes the clustering of PSD-95 in hippocampal neurons
    • Farías, G. G., Alfaro, I. E., Cerpa, W., Grabowski, C. P., Godoy, J. A., Bonansco, C., et al. (2009). Wnt-5a/JNK signaling promotes the clustering of PSD-95 in hippocampal neurons. J. Biol. Chem. 284, 15857-15866. doi: 10.1074/jbc.m808986200
    • (2009) J. Biol. Chem , vol.284 , pp. 15857-15866
    • Farías, G.G.1    Alfaro, I.E.2    Cerpa, W.3    Grabowski, C.P.4    Godoy, J.A.5    Bonansco, C.6
  • 58
    • 34248547813 scopus 로고    scopus 로고
    • Soluble protein oligomers as emerging toxins in Alzheimer’s and other amyloid diseases
    • Ferreira, S. T., Vieira, M. N. N., and De Felice, F. G. (2007). Soluble protein oligomers as emerging toxins in Alzheimer’s and other amyloid diseases. IUBMB Life 59, 332-345. doi: 10.1080/15216540701283882
    • (2007) IUBMB Life , vol.59 , pp. 332-345
    • Ferreira, S.T.1    Vieira, M.2    De Felice, F.G.3
  • 60
    • 0035985936 scopus 로고    scopus 로고
    • Mitochondrial permeability transition can be directly monitored in living neurons
    • Gillessen, T., Grasshoff, C., and Szinicz, L. (2002). Mitochondrial permeability transition can be directly monitored in living neurons. Biomed. Pharmacother. 56, 186-193. doi: 10.1016/s0753-3322(02)00184-1
    • (2002) Biomed. Pharmacother , vol.56 , pp. 186-193
    • Gillessen, T.1    Grasshoff, C.2    Szinicz, L.3
  • 61
    • 84919935176 scopus 로고    scopus 로고
    • Wnt-5a ligand modulates mitochondrial fission-fusion in rat hippocampal neurons
    • Godoy, J. A., Arrázola, M. S., Ordenes, D., Silva-Alvarez, C., Braidy, N., and Inestrosa, N. C. (2014). Wnt-5a ligand modulates mitochondrial fission-fusion in rat hippocampal neurons. J. Biol. Chem. 289, 36179-36193. doi: 10.1074/jbc.M114.557009
    • (2014) J. Biol. Chem , vol.289 , pp. 36179-36193
    • Godoy, J.A.1    Arrázola, M.S.2    Ordenes, D.3    Silva-Alvarez, C.4    Braidy, N.5    Inestrosa, N.C.6
  • 62
    • 44449133771 scopus 로고    scopus 로고
    • Inhibition of GSK3beta by postconditioning is required to prevent opening of the mitochondrial permeability transition pore during reperfusion
    • Gomez, L., Paillard, M., Thibault, H., Derumeaux, G., and Ovize, M. (2008). Inhibition of GSK3beta by postconditioning is required to prevent opening of the mitochondrial permeability transition pore during reperfusion. Circulation 117, 2761-2768. doi: 10.1161/CIRCULATIONAHA.107.755066
    • (2008) Circulation , vol.117 , pp. 2761-2768
    • Gomez, L.1    Paillard, M.2    Thibault, H.3    Derumeaux, G.4    Ovize, M.5
  • 63
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer’s amyloid beta-peptide
    • Haass, C., and Selkoe, D. J. (2007). Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid beta-peptide. Nat. Rev. Mol. Cell Biol. 8, 101-112. doi: 10.1038/nrm2101
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 64
    • 67349117275 scopus 로고    scopus 로고
    • What is the mitochondrial permeability transition pore
    • Halestrap, A. P. (2009). What is the mitochondrial permeability transition pore? J. Mol. Cell. Cardiol. 46, 821-831. doi: 10.1016/j.yjmcc.2009.02.021
    • (2009) J. Mol. Cell. Cardiol , vol.46 , pp. 821-831
    • Halestrap, A.P.1
  • 65
    • 0030826778 scopus 로고    scopus 로고
    • Cyclosporin A binding to mitochondrial cyclophilin inhibits the permeability transition pore and protects hearts from ischaemia/reperfusion injury
    • Halestrap, A. P., Connern, C. P., Griffiths, E. J., and Kerr, P. M. (1997). Cyclosporin A binding to mitochondrial cyclophilin inhibits the permeability transition pore and protects hearts from ischaemia/reperfusion injury. Mol. Cell. Biochem. 174, 167-172. doi: 10.1007/978-1-4615-6111-8_25
    • (1997) Mol. Cell. Biochem , vol.174 , pp. 167-172
    • Halestrap, A.P.1    Connern, C.P.2    Griffiths, E.J.3    Kerr, P.M.4
  • 66
    • 51349110166 scopus 로고    scopus 로고
    • The amyloid beta-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae
    • Hansson Petersen, C. A., Alikhani, N., Behbahani, H., Wiehager, B., Pavlov, P. F., Alafuzoff, I., et al. (2008). The amyloid beta-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae. Proc. Natl. Acad. Sci. U S A 105, 13145-13150. doi: 10.1073/pnas.0806192105
    • (2008) Proc. Natl. Acad. Sci. U S A , vol.105 , pp. 13145-13150
    • Hansson Petersen, C.A.1    Alikhani, N.2    Behbahani, H.3    Wiehager, B.4    Pavlov, P.F.5    Alafuzoff, I.6
  • 67
    • 0026597063 scopus 로고
    • Alzheimer’s disease: The amyloid cascade hypothesis
    • Hardy, J. A., and Higgins, G. A. (1992). Alzheimer’s disease: the amyloid cascade hypothesis. Science 256, 184-185. doi: 10.1126/science.1566067
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 68
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer’s disease: Progress and problems on the road to therapeutics
    • Hardy, J., and Selkoe, D. J. (2002). The amyloid hypothesis of Alzheimer’s disease: progress and problems on the road to therapeutics. Science 297, 353-356. doi: 10.1126/science.1072994
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 69
    • 84896807547 scopus 로고    scopus 로고
    • Regulating Wnt signaling: A strategy to prevent neurodegeneration and induce regeneration
    • Harvey, K., and Marchetti, B. (2014). Regulating Wnt signaling: a strategy to prevent neurodegeneration and induce regeneration. J. Mol. Cell Biol. 6, 1-2.doi: 10.1093/jmcb/mju002
    • (2014) J. Mol. Cell Biol , vol.6 , pp. 1-2
    • Harvey, K.1    Marchetti, B.2
  • 70
    • 84909619435 scopus 로고    scopus 로고
    • The regulation of mitochondrial dynamics
    • Hoppins, S. (2014). The regulation of mitochondrial dynamics. Curr. Opin. Cell Biol. 29, 46-52. doi: 10.1016/j.ceb.2014.03.005
    • (2014) Curr. Opin. Cell Biol , vol.29 , pp. 46-52
    • Hoppins, S.1
  • 71
    • 34250204271 scopus 로고    scopus 로고
    • The machines that divide and fuse mitochondria
    • Hoppins, S., Lackner, L., and Nunnari, J. (2007). The machines that divide and fuse mitochondria. Annu. Rev. Biochem. 76, 751-780. doi: 10.1146/annurev.biochem.76.071905.090048
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 751-780
    • Hoppins, S.1    Lackner, L.2    Nunnari, J.3
  • 72
    • 75549087261 scopus 로고    scopus 로고
    • Emerging roles of Wnts in the adult nervous system
    • Inestrosa, N. C., and Arenas, E. (2010). Emerging roles of Wnts in the adult nervous system. Nat. Rev. Neurosci. 11, 77-86. doi: 10.1038/nrn2755
    • (2010) Nat. Rev. Neurosci , vol.11 , pp. 77-86
    • Inestrosa, N.C.1    Arenas, E.2
  • 73
    • 84896828867 scopus 로고    scopus 로고
    • Wnt signaling in the nervous system and in Alzheimer’s disease
    • Inestrosa, N. C., and Varela-Nallar, L. (2014). Wnt signaling in the nervous system and in Alzheimer’s disease. J. Mol. Cell Biol. 6, 64-74. doi: 10.1093/jmcb/mjt051
    • (2014) J. Mol. Cell Biol , vol.6 , pp. 64-74
    • Inestrosa, N.C.1    Varela-Nallar, L.2
  • 74
    • 84926619878 scopus 로고    scopus 로고
    • Wnt signalling in neuronal differentiation and development
    • Inestrosa, N. C., and Varela-Nallar, L. (2015). Wnt signalling in neuronal differentiation and development. Cell Tissue Res. 359, 215-223. doi: 10.1007/s00441-014-1996-4
    • (2015) Cell Tissue Res , vol.359 , pp. 215-223
    • Inestrosa, N.C.1    Varela-Nallar, L.2
  • 75
    • 84872833228 scopus 로고    scopus 로고
    • Mitochondrial dynamics in neurodegeneration
    • Itoh, K., Nakamura, K., Iijima, M., and Sesaki, H. (2013). Mitochondrial dynamics in neurodegeneration. Trends Cell Biol. 23, 64-71. doi: 10.1016/j.tcb.2012.10.006
    • (2013) Trends Cell Biol , vol.23 , pp. 64-71
    • Itoh, K.1    Nakamura, K.2    Iijima, M.3    Sesaki, H.4
  • 76
    • 85047692700 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3β mediates convergence of protection signaling to inhibit the mitochondrial permeability transition pore
    • Juhaszova, M., Zorov, D. B., Kim, S., Pepe, S., Fu, Q., Fishbein, K. W., et al. (2004). Glycogen synthase kinase-3β mediates convergence of protection signaling to inhibit the mitochondrial permeability transition pore. J. Clin. Invest. 113, 1535-1549. doi: 10.1172/JCI200419906
    • (2004) J. Clin. Invest , vol.113 , pp. 1535-1549
    • Juhaszova, M.1    Zorov, D.B.2    Kim, S.3    Pepe, S.4    Fu, Q.5    Fishbein, K.W.6
  • 77
    • 67649882599 scopus 로고    scopus 로고
    • Role of glycogen synthase kinase-3beta in cardioprotection
    • Juhaszova, M., Zorov, D. B., Yaniv, Y., Nuss, H. B., Wang, S., and Sollott, S. J. (2009). Role of glycogen synthase kinase-3beta in cardioprotection. Circ. Res. 104, 1240-1252. doi: 10.1161/CIRCRESAHA.109.197996
    • (2009) Circ. Res , vol.104 , pp. 1240-1252
    • Juhaszova, M.1    Zorov, D.B.2    Yaniv, Y.3    Nuss, H.B.4    Wang, S.5    Sollott, S.J.6
  • 78
    • 79959655354 scopus 로고    scopus 로고
    • Mitochondrial division: Molecular machinery and physiological functions
    • Kageyama, Y., Zhang, Z., and Sesaki, H. (2011). Mitochondrial division: molecular machinery and physiological functions. Curr. Opin. Cell Biol. 23, 427-434.doi: 10.1016/j.ceb.2011.04.009
    • (2011) Curr. Opin. Cell Biol , vol.23 , pp. 427-434
    • Kageyama, Y.1    Zhang, Z.2    Sesaki, H.3
  • 79
    • 0029776032 scopus 로고    scopus 로고
    • A molecular mechanism for the effect of lithium on development
    • Klein, P. S., and Melton, D. A. (1996). A molecular mechanism for the effect of lithium on development. Proc. Natl. Acad. Sci. U S A 93, 8455-8459. doi: 10.1073/pnas.93.16.8455
    • (1996) Proc. Natl. Acad. Sci. U S A , vol.93 , pp. 8455-8459
    • Klein, P.S.1    Melton, D.A.2
  • 80
    • 84897548778 scopus 로고    scopus 로고
    • Quality control in mitochondria: Use it, break it, fix it, trash it
    • Kornmann, B. (2014). Quality control in mitochondria: use it, break it, fix it, trash it. F1000Prime Rep. 6:15. doi: 10.12703/P6-15
    • (2014) F1000prime Rep , vol.6 , pp. 15
    • Kornmann, B.1
  • 81
    • 3843075121 scopus 로고    scopus 로고
    • Structural basis of mitochondrial tethering by mitofusin complexes
    • Koshiba, T., Detmer, S. A., Kaiser, J. T., Chen, H., McCaffery, J. M., and Chan, D. C. (2004). Structural basis of mitochondrial tethering by mitofusin complexes. Science 305, 858-862. doi: 10.1126/science.1099793
    • (2004) Science , vol.305 , pp. 858-862
    • Koshiba, T.1    Detmer, S.A.2    Kaiser, J.T.3    Chen, H.4    McCaffery, J.M.5    Chan, D.C.6
  • 82
    • 0033231549 scopus 로고    scopus 로고
    • C. Elegans dynamin-related protein DRP-1 controls severing of the mitochondrial outer membrane
    • Labrousse, A. M., Zappaterra, M. D., Rube, D. A., and van der Bliek, A. M. (1999). C. elegans dynamin-related protein DRP-1 controls severing of the mitochondrial outer membrane. Mol. Cell 4, 815-826. doi: 10.1016/s1097-2765(00)80391-3
    • (1999) Mol. Cell , vol.4 , pp. 815-826
    • Labrousse, A.M.1    Zappaterra, M.D.2    Rube, D.A.3    Van Der Bliek, A.M.4
  • 83
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer’s disease
    • LaFerla, F. M. (2002). Calcium dyshomeostasis and intracellular signalling in Alzheimer’s disease. Nat. Rev. Neurosci. 3, 862-872. doi: 10.1038/nrn960
    • (2002) Nat. Rev. Neurosci , vol.3 , pp. 862-872
    • Laferla, F.M.1
  • 84
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins
    • Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., et al. (1998). Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. U S A 95, 6448-6453. doi: 10.1073/pnas.95.11.6448
    • (1998) Proc. Natl. Acad. Sci. U S A , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5    Liosatos, M.6
  • 85
    • 67249087641 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake
    • Li, S., Hong, S., Shepardson, N. E., Walsh, D. M., Shankar, G. M., and Selkoe, D. (2009). Soluble oligomers of amyloid beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake. Neuron 62, 788-801. doi: 10.1016/j.neuron.2009.05.012
    • (2009) Neuron , vol.62 , pp. 788-801
    • Li, S.1    Hong, S.2    Shepardson, N.E.3    Walsh, D.M.4    Shankar, G.M.5    Selkoe, D.6
  • 86
    • 10944269186 scopus 로고    scopus 로고
    • The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
    • Li, Z., Okamoto, K.-I., Hayashi, Y., and Sheng, M. (2004). The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses. Cell 119, 873-887. doi: 10.1016/j.cell.2004.11.003
    • (2004) Cell , vol.119 , pp. 873-887
    • Li, Z.1    Okamoto, K.-I.2    Hayashi, Y.3    Sheng, M.4
  • 87
    • 25844432119 scopus 로고    scopus 로고
    • Wnt signalling regulates adult hippocampal neurogenesis
    • Lie, D.-C., Colamarino, S. A., Song, H.-J., Désiré, L., Mira, H., Consiglio, A., et al. (2005). Wnt signalling regulates adult hippocampal neurogenesis. Nature 437, 1370-1375. doi: 10.1038/nature04108
    • (2005) Nature , vol.437 , pp. 1370-1375
    • Lie, D.-C.1    Colamarino, S.A.2    Song, H.-J.3    Désiré, L.4    Mira, H.5    Consiglio, A.6
  • 88
    • 84907985969 scopus 로고    scopus 로고
    • Deficiency in LRP6-mediated Wnt signaling contributes to synaptic abnormalities and amyloid pathology in Alzheimer’s disease
    • Liu, C.-C., Tsai, C.-W., Deak, F., Rogers, J., Penuliar, M., Sung, Y. M., et al. (2014). Deficiency in LRP6-mediated Wnt signaling contributes to synaptic abnormalities and amyloid pathology in Alzheimer’s disease. Neuron 84, 63-77. doi: 10.1016/j.neuron.2014.08.048
    • (2014) Neuron , vol.84 , pp. 63-77
    • Liu, C.-C.1    Tsai, C.-W.2    Deak, F.3    Rogers, J.4    Penuliar, M.5    Sung, Y.M.6
  • 89
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Aβ to mitochondrial toxicity in Alzheimer’s disease
    • Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., et al. (2004). ABAD directly links Aβ to mitochondrial toxicity in Alzheimer’s disease. Science 304, 448-452. doi: 10.1126/science.1091230
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3    Xu, H.W.4    Takuma, K.5    Wang, N.6
  • 90
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A beta accumulation in Alzheimer’s disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., and Reddy, P. H. (2006). Mitochondria are a direct site of A beta accumulation in Alzheimer’s disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum. Mol. Genet. 15, 1437-1449. doi: 10.1093/hmg/ddl066
    • (2006) Hum. Mol. Genet , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Reddy, P.H.6
  • 91
    • 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, M. J., and Reddy, P. H. (2011). 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, 2495-2509. doi: 10.1093/hmg/ddr139
    • (2011) Hum. Mol. Genet , vol.20 , pp. 2495-2509
    • Manczak, M.1    Calkins, M.J.2    Reddy, P.H.3
  • 92
    • 84861130196 scopus 로고    scopus 로고
    • Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer’s disease neurons: Implications for mitochondrial dysfunction and neuronal damage
    • Manczak, M., and Reddy, P. H. (2012). Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer’s disease neurons: implications for mitochondrial dysfunction and neuronal damage. Hum. Mol. Genet. 21, 2538-2547. doi: 10.1093/hmg/dds072
    • (2012) Hum. Mol. Genet , vol.21 , pp. 2538-2547
    • Manczak, M.1    Reddy, P.H.2
  • 93
    • 0001061413 scopus 로고    scopus 로고
    • Intracellular calcium-release channels: Regulators of cell life and death
    • Marks, A. R. (1997). Intracellular calcium-release channels: regulators of cell life and death. Am. J. Physiol. 272, H597-H605.
    • (1997) Am. J. Physiol , vol.272
    • Marks, A.R.1
  • 94
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer’s disease
    • Mattson, M. P. (2004). Pathways towards and away from Alzheimer’s disease. Nature 430, 631-639. doi: 10.1038/nature02621
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 95
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson, M. P., Cheng, B., Davis, D., Bryant, K., Lieberburg, I., and Rydel, R. E. (1992). β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12, 376-389
    • (1992) J. Neurosci , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 96
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer’s disease
    • McLean, C. A., Cherny, R. A., Fraser, F. W., Fuller, S. J., Smith, M. J., Beyreuther, K., et al. (1999). Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer’s disease. Ann. Neurol. 46, 860-866. doi: 10.1002/1531-8249(199912)46:6<860::aid-ana8>3.0.co;2-m
    • (1999) Ann. Neurol , vol.46 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3    Fuller, S.J.4    Smith, M.J.5    Beyreuther, K.6
  • 97
    • 0036092524 scopus 로고    scopus 로고
    • Mitochondrial Ca(2+) buffering regulates synaptic transmission between retinal amacrine cells
    • Medler, K., and Gleason, E. L. (2002). Mitochondrial Ca(2+) buffering regulates synaptic transmission between retinal amacrine cells. J. Neurophysiol. 87, 1426-1439. doi: 10.1152/jn.00627.2001
    • (2002) J. Neurophysiol , vol.87 , pp. 1426-1439
    • Medler, K.1    Gleason, E.L.2
  • 99
    • 65449182366 scopus 로고    scopus 로고
    • Drug development targeting the glycogen synthase kinase-3β (GSK-3β)-mediated signal transduction pathway: Role of GSK-3β in myocardial protection against ischemia/reperfusion injury
    • Miura, T., Nishihara, M., and Miki, T. (2009). Drug development targeting the glycogen synthase kinase-3β (GSK-3β)-mediated signal transduction pathway: role of GSK-3β in myocardial protection against ischemia/reperfusion injury. J. Pharmacol. Sci. 109, 162-167. doi: 10.1254/jphs.08r27fm
    • (2009) J. Pharmacol. Sci , vol.109 , pp. 162-167
    • Miura, T.1    Nishihara, M.2    Miki, T.3
  • 100
    • 78149361469 scopus 로고    scopus 로고
    • Mitochondria and GSK-3β in cardioprotection against ischemia/reperfusion injury
    • Miura, T., and Tanno, M. (2010). Mitochondria and GSK-3β in cardioprotection against ischemia/reperfusion injury. Cardiovasc. Drugs Ther. 24, 255-263. doi: 10.1007/s10557-010-6234-z
    • (2010) Cardiovasc. Drugs Ther , vol.24 , pp. 255-263
    • Miura, T.1    Tanno, M.2
  • 101
    • 39449114808 scopus 로고    scopus 로고
    • Akt mediates mitochondrial protection in cardiomyocytes through phosphorylation of mitochondrial hexokinase-II
    • Miyamoto, S., Murphy, A. N., and Brown, J. H. (2008). Akt mediates mitochondrial protection in cardiomyocytes through phosphorylation of mitochondrial hexokinase-II. Cell Death Differ. 15, 521-529. doi: 10.1038/sj.cdd.4402285
    • (2008) Cell Death Differ , vol.15 , pp. 521-529
    • Miyamoto, S.1    Murphy, A.N.2    Brown, J.H.3
  • 102
    • 0035780141 scopus 로고    scopus 로고
    • Amyloid β-peptide promotes permeability transition pore in brain mitochondria
    • Moreira, P. I., Santos, M. S., Moreno, A., and Oliveira, C. (2001). Amyloid β-peptide promotes permeability transition pore in brain mitochondria. Biosci. Rep. 21, 789-800. doi: 10.1023/A1015536808304
    • (2001) Biosci. Rep , vol.21 , pp. 789-800
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.3    Oliveira, C.4
  • 103
    • 0037100213 scopus 로고    scopus 로고
    • Effect of amyloid beta-peptide on permeability transition pore: A comparative study
    • Moreira, P. I., Santos, M. S., Moreno, A., Rego, A. C., and Oliveira, C. (2002). Effect of amyloid beta-peptide on permeability transition pore: a comparative study. J. Neurosci. Res. 69, 257-267. doi: 10.1002/jnr.10282
    • (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
  • 104
    • 34648831384 scopus 로고    scopus 로고
    • Alzheimer’s disease: A lesson from mitochondrial dysfunction
    • Moreira, P. I., Santos, M. S., and Oliveira, C. R. (2007). Alzheimer’s disease: a lesson from mitochondrial dysfunction. Antioxid. Redox Signal. 9, 1621-1630. doi: 10.1089/ars.2007.1703
    • (2007) Antioxid. Redox Signal , vol.9 , pp. 1621-1630
    • Moreira, P.I.1    Santos, M.S.2    Oliveira, C.R.3
  • 105
    • 11844260044 scopus 로고    scopus 로고
    • Structure and function of amyloid in Alzheimer’s disease
    • Morgan, C., Colombres, M., Nuñez, M. T., and Inestrosa, N. C. (2004). Structure and function of amyloid in Alzheimer’s disease. Prog. Neurobiol. 74, 323-349. doi: 10.1016/j.pneurobio.2004.10.004
    • (2004) Prog. Neurobiol , vol.74 , pp. 323-349
    • Morgan, C.1    Colombres, M.2    Nuñez, M.T.3    Inestrosa, N.C.4
  • 106
    • 0027210387 scopus 로고
    • The regulation of bidirectional mitochondrial transport is coordinated with axonal outgrowth
    • Morris, R. L., and Hollenbeck, P. J. (1993). The regulation of bidirectional mitochondrial transport is coordinated with axonal outgrowth. J. Cell Sci. 104(Pt. 3), 917-927.
    • (1993) J. Cell Sci , vol.104 , pp. 917-927
    • Morris, R.L.1    Hollenbeck, P.J.2
  • 107
    • 17844364259 scopus 로고    scopus 로고
    • Brain glucose metabolism in the early and specific diagnosis of Alzheimer’s disease. FDG-PET studies in MCI and AD
    • Mosconi, L. (2005). Brain glucose metabolism in the early and specific diagnosis of Alzheimer’s disease. FDG-PET studies in MCI and AD. Eur. J. Nucl. Med. Mol. Imaging 32, 486-510.doi: 10.1007/s00259-005-1762-7
    • (2005) Eur. J. Nucl. Med. Mol. Imaging , vol.32 , pp. 486-510
    • Mosconi, L.1
  • 108
    • 77951931900 scopus 로고    scopus 로고
    • The consequences of mitochondrial amyloid beta-peptide in Alzheimer’s disease
    • Muirhead, K. E. A., Borger, E., Aitken, L., Conway, S. J., and Gunn-Moore, F. J. (2010). The consequences of mitochondrial amyloid beta-peptide in Alzheimer’s disease. Biochem. J. 426, 255-270. doi: 10.1042/BJ20091941
    • (2010) Biochem. J , vol.426 , pp. 255-270
    • Muirhead, K.1    Borger, E.2    Aitken, L.3    Conway, S.J.4    Gunn-Moore, F.J.5
  • 109
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • Newmeyer, D. D., and Ferguson-Miller, S. (2003). Mitochondria: releasing power for life and unleashing the machineries of death. Cell 112, 481-490. doi: 10.1016/S0092-8674(03)00116-8
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 110
    • 35348988663 scopus 로고    scopus 로고
    • Modulation of the mitochondrial permeability transition pore complex in GSK-3β-mediated myocardial protection
    • Nishihara, M., Miura, T., Miki, T., Tanno, M., Yano, T., Naitoh, K., et al. (2007). Modulation of the mitochondrial permeability transition pore complex in GSK-3β-mediated myocardial protection. J. Mol. Cell. Cardiol. 43, 564-570. doi: 10.1016/j.yjmcc.2007.08.010
    • (2007) J. Mol. Cell. Cardiol , vol.43 , pp. 564-570
    • Nishihara, M.1    Miura, T.2    Miki, T.3    Tanno, M.4    Yano, T.5    Naitoh, K.6
  • 111
    • 84889684938 scopus 로고    scopus 로고
    • Wnts in adult brain: From synaptic plasticity to cognitive deficiencies
    • Oliva, C. A., Vargas, J. Y., and Inestrosa, N. C. (2013). Wnts in adult brain: from synaptic plasticity to cognitive deficiencies. Front. Cell. Neurosci. 7:224. doi: 10.3389/fncel.2013.00224
    • (2013) Front. Cell. Neurosci , vol.7 , pp. 224
    • Oliva, C.A.1    Vargas, J.Y.2    Inestrosa, N.C.3
  • 112
    • 79952417232 scopus 로고    scopus 로고
    • Amyloid β-peptide oligomers stimulate RyR-mediated Ca2+ release inducing mitochondrial fragmentation in hippocampal neurons and prevent RyR-mediated dendritic spine remodeling produced by BDNF
    • Paula-Lima, A. C., Adasme, T., SanMartín, C., Sebollela, A., Hetz, C., Carrasco, M. A., et al. (2011). Amyloid β-peptide oligomers stimulate RyR-mediated Ca2+ release inducing mitochondrial fragmentation in hippocampal neurons and prevent RyR-mediated dendritic spine remodeling produced by BDNF. Antioxid. Redox Signal. 14, 1209-1223. doi: 10.1089/ars.2010.3287
    • (2011) Antioxid. Redox Signal , vol.14 , pp. 1209-1223
    • Paula-Lima, A.C.1    Adasme, T.2    Sanmartín, C.3    Sebollela, A.4    Hetz, C.5    Carrasco, M.A.6
  • 113
    • 0035853721 scopus 로고    scopus 로고
    • The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ
    • Petronilli, V., Penzo, D., Scorrano, L., Bernardi, P., and Di Lisa, F. (2001). The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ. J. Biol. Chem. 276, 12030-12034. doi: 10.1074/jbc.m010604200
    • (2001) J. Biol. Chem , vol.276 , pp. 12030-12034
    • Petronilli, V.1    Penzo, D.2    Scorrano, L.3    Bernardi, P.4    Di Lisa, F.5
  • 114
    • 78751470559 scopus 로고    scopus 로고
    • Aberrant mitochondrial fission in neurons induced by protein kinase Cdelta under oxidative stress conditions in vivo
    • Qi, X., Disatnik, M.-H., Shen, N., Sobel, R. A., and Mochly-Rosen, D. (2011). Aberrant mitochondrial fission in neurons induced by protein kinase Cdelta under oxidative stress conditions in vivo. Mol. Biol. Cell 22, 256-265. doi: 10.1091/mbc.E10-06-0551
    • (2011) Mol. Biol. Cell , vol.22 , pp. 256-265
    • Qi, X.1    Disatnik, M.-H.2    Shen, N.3    Sobel, R.A.4    Mochly-Rosen, D.5
  • 115
    • 15744368753 scopus 로고    scopus 로고
    • Trolox and 17beta-estradiol protect against amyloid beta-peptide neurotoxicity by a mechanism that involves modulation of the Wnt signaling pathway
    • Quintanilla, R. A., Muñoz, F. J., Metcalfe, M. J., Hitschfeld, M., Olivares, G., Godoy, J. A., et al. (2005). Trolox and 17beta-estradiol protect against amyloid beta-peptide neurotoxicity by a mechanism that involves modulation of the Wnt signaling pathway. J. Biol. Chem. 280, 11615-11625. doi: 10.1074/jbc.m411936200
    • (2005) J. Biol. Chem , vol.280 , pp. 11615-11625
    • Quintanilla, R.A.1    Muñoz, F.J.2    Metcalfe, M.J.3    Hitschfeld, M.4    Olivares, G.5    Godoy, J.A.6
  • 116
    • 84903161777 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore is a potential drug target for neurodegeneration. Biochim
    • Rao, V. K., Carlson, E. A., and Yan, S. S. (2014). Mitochondrial permeability transition pore is a potential drug target for neurodegeneration. Biochim. Biophys. Acta 1842, 1267-1272. doi: 10.1016/j.bbadis.2013.09.003
    • (2014) Biophys. Acta , vol.1842 , pp. 1267-1272
    • Rao, V.K.1    Carlson, E.A.2    Yan, S.S.3
  • 117
    • 76249084726 scopus 로고    scopus 로고
    • Activation of mitochondrial ERK protects cancer cells from death through inhibition of the permeability transition
    • Rasola, A., Sciacovelli, M., Chiara, F., Pantic, B., Brusilow, W. S., and Bernardi, P. (2010a). Activation of mitochondrial ERK protects cancer cells from death through inhibition of the permeability transition. Proc. Natl. Acad. Sci. U S A 107, 726-731. doi: 10.1073/pnas.0912742107
    • (2010) Proc. Natl. Acad. Sci. U S A , vol.107 , pp. 726-731
    • Rasola, A.1    Sciacovelli, M.2    Chiara, F.3    Pantic, B.4    Brusilow, W.S.5    Bernardi, P.6
  • 118
    • 77952671613 scopus 로고    scopus 로고
    • Signal transduction to the permeability transition pore
    • Rasola, A., Sciacovelli, M., Pantic, B., and Bernardi, P. (2010b). Signal transduction to the permeability transition pore. FEBS Lett. 584, 1989-1996. doi: 10.1016/j.febslet.2010.02.022
    • (2010) FEBS Lett , vol.584 , pp. 1989-1996
    • Rasola, A.1    Sciacovelli, M.2    Pantic, B.3    Bernardi, P.4
  • 119
    • 33644845279 scopus 로고    scopus 로고
    • Amyloid precursor protein-mediated free radicals and oxidative damage: Implications for the development and progression of Alzheimer’s disease
    • Reddy, P. H. (2006). Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer’s disease. J. Neurochem. 96, 1-13. doi: 10.1111/j.1471-4159.2005.03530.x
    • (2006) J. Neurochem , vol.96 , pp. 1-13
    • Reddy, P.H.1
  • 120
    • 67649803186 scopus 로고    scopus 로고
    • Amyloid beta, mitochondrial structural and functional dynamics in Alzheimer’s disease
    • Reddy, P. H. (2009). Amyloid beta, mitochondrial structural and functional dynamics in Alzheimer’s disease. Exp. Neurol. 218, 286-292. doi: 10.1016/j.expneurol.2009.03.042
    • (2009) Exp. Neurol , vol.218 , pp. 286-292
    • Reddy, P.H.1
  • 121
    • 84882738357 scopus 로고    scopus 로고
    • Amyloid β-induced glycogen synthase kinase 3β phosphorylated VDAC1 in Alzheimer’s disease: Implications for synaptic dysfunction and neuronal damage
    • Reddy, P. H. (2013). Amyloid β-induced glycogen synthase kinase 3β phosphorylated VDAC1 in Alzheimer’s disease: implications for synaptic dysfunction and neuronal damage. Biochim. Biophys. Acta 1832, 1913-1921. doi: 10.1016/j.bbadis.2013.06.012
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 1913-1921
    • Reddy, P.H.1
  • 122
    • 33746927077 scopus 로고    scopus 로고
    • Mitochondrial hexokinases, novel mediators of the antiapoptotic effects of growth factors and Akt
    • Robey, R. B., and Hay, N. (2006). Mitochondrial hexokinases, novel mediators of the antiapoptotic effects of growth factors and Akt. Oncogene 25, 4683-4696. doi: 10.1038/sj.onc.1209595
    • (2006) Oncogene , vol.25 , pp. 4683-4696
    • Robey, R.B.1    Hay, N.2
  • 123
    • 0037089084 scopus 로고    scopus 로고
    • Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo
    • Rojo, M., Legros, F., Chateau, D., and Lombès, A. (2002). Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo. J. Cell Sci. 115, 1663-1674.
    • (2002) J. Cell Sci , vol.115 , pp. 1663-1674
    • Rojo, M.1    Legros, F.2    Chateau, D.3    Lombès, A.4
  • 124
    • 27644596641 scopus 로고    scopus 로고
    • Opinion: What is the role of protein aggregation in neurodegeneration
    • Ross, C. A., and Poirier, M. A. (2005). Opinion: what is the role of protein aggregation in neurodegeneration? Nat. Rev. Mol. Cell Biol. 6, 891-898. doi: 10.1038/nrm1742
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 125
    • 84879153349 scopus 로고    scopus 로고
    • WNT signaling in neuronal maturation and synaptogenesis
    • Rosso, S. B., and Inestrosa, N. C. (2013). WNT signaling in neuronal maturation and synaptogenesis. Front. Cell. Neurosci. 7:103. doi: 10.3389/fncel.2013.00103
    • (2013) Front. Cell. Neurosci , vol.7 , pp. 103
    • Rosso, S.B.1    Inestrosa, N.C.2
  • 126
    • 16644381829 scopus 로고    scopus 로고
    • Wnt signaling through Dishevelled, Rac and JNK regulates dendritic development
    • Rosso, S. B., Sussman, D., Wynshaw-Boris, A., and Salinas, P. C. (2005). Wnt signaling through Dishevelled, Rac and JNK regulates dendritic development. Nat. Neurosci. 8, 34-42. doi: 10.1038/nn1374
    • (2005) Nat. Neurosci , vol.8 , pp. 34-42
    • Rosso, S.B.1    Sussman, D.2    Wynshaw-Boris, A.3    Salinas, P.C.4
  • 127
    • 0141792787 scopus 로고    scopus 로고
    • Response of mitochondrial traffic to axon determination and differential branch growth
    • Ruthel, G., and Hollenbeck, P. J. (2003). Response of mitochondrial traffic to axon determination and differential branch growth. J. Neurosci. 23, 8618-8624.
    • (2003) J. Neurosci , vol.23 , pp. 8618-8624
    • Ruthel, G.1    Hollenbeck, P.J.2
  • 128
    • 77749308402 scopus 로고    scopus 로고
    • Amyloid oligomers: Formation and toxicity of Aβ oligomers
    • Sakono, M., and Zako, T. (2010). Amyloid oligomers: formation and toxicity of Aβ oligomers. FEBS J. 277, 1348-1358. doi: 10.1111/j.1742-4658.2010.07568.x
    • (2010) FEBS J , vol.277 , pp. 1348-1358
    • Sakono, M.1    Zako, T.2
  • 129
    • 48249110960 scopus 로고    scopus 로고
    • Wnt signaling in neural circuit assembly
    • Salinas, P. C., and Zou, Y. (2008). Wnt signaling in neural circuit assembly. Annu. Rev. Neurosci. 31, 339-358. doi: 10.1146/annurev.neuro.31.060407.125649
    • (2008) Annu. Rev. Neurosci , vol.31 , pp. 339-358
    • Salinas, P.C.1    Zou, Y.2
  • 130
    • 84860224686 scopus 로고    scopus 로고
    • The antioxidant N-acetylcysteine prevents the mitochondrial fragmentation induced by soluble amyloid-β peptide oligomers
    • Sanmartin, C. D., Adasme, T., Hidalgo, C., and Paula-Lima, A. C. (2012). The antioxidant N-acetylcysteine prevents the mitochondrial fragmentation induced by soluble amyloid-β peptide oligomers. Neurodegener. Dis. 10, 34-37. doi: 10.1159/000334901
    • (2012) Neurodegener. Dis , vol.10 , pp. 34-37
    • Sanmartin, C.D.1    Adasme, T.2    Hidalgo, C.3    Paula-Lima, A.C.4
  • 132
    • 24744460273 scopus 로고    scopus 로고
    • Cyclophilin D is a component of mitochondrial permeability transition and mediates neuronal cell death after focal cerebral ischemia
    • Schinzel, A. C., Takeuchi, O., Huang, Z., Fisher, J. K., Zhou, Z., Rubens, J., et al. (2005). Cyclophilin D is a component of mitochondrial permeability transition and mediates neuronal cell death after focal cerebral ischemia. Proc. Natl. Acad. Sci. U S A 102, 12005-12010.doi: 10.1073/pnas.0505294102
    • (2005) Proc. Natl. Acad. Sci. U S A , vol.102 , pp. 12005-12010
    • Schinzel, A.C.1    Takeuchi, O.2    Huang, Z.3    Fisher, J.K.4    Zhou, Z.5    Rubens, J.6
  • 133
    • 79959305691 scopus 로고    scopus 로고
    • Mitochondria: The next (neurode)generation
    • Schon, E. A., and Przedborski, S. (2011). Mitochondria: the next (neurode)generation. Neuron 70, 1033-1053. doi: 10.1016/j.neuron.2011.06.003
    • (2011) Neuron , vol.70 , pp. 1033-1053
    • Schon, E.A.1    Przedborski, S.2
  • 134
    • 84856056846 scopus 로고    scopus 로고
    • Mitochondrial transport in neurons: Impact on synaptic homeostasis and neurodegeneration
    • Sheng, Z.-H., and Cai, Q. (2012). Mitochondrial transport in neurons: impact on synaptic homeostasis and neurodegeneration. Nat. Rev. Neurosci. 13, 77-93. doi: 10.1038/nrn3156
    • (2012) Nat. Rev. Neurosci , vol.13 , pp. 77-93
    • Sheng, Z.-H.1    Cai, Q.2
  • 135
    • 77952886494 scopus 로고    scopus 로고
    • VDAC, a multi-functional mitochondrial protein regulating cell life and death
    • Shoshan-Barmatz, V., De Pinto, V., Zweckstetter, M., Raviv, Z., Keinan, N., and Arbel, N. (2010). VDAC, a multi-functional mitochondrial protein regulating cell life and death. Mol. Aspects Med. 31, 227-285. doi: 10.1016/j.mam.2010.03.002
    • (2010) Mol. Aspects Med , vol.31 , pp. 227-285
    • Shoshan-Barmatz, V.1    De Pinto, V.2    Zweckstetter, M.3    Raviv, Z.4    Keinan, N.5    Arbel, N.6
  • 136
    • 84878740033 scopus 로고    scopus 로고
    • Canonical Wnt signaling protects hippocampal neurons from Aβ oligomers: Role of non-canonical Wnt-5a/Ca(2+) in mitochondrial dynamics
    • Silva-Alvarez, C., Arrázola, M. S., Godoy, J. A., Ordenes, D., and Inestrosa, N. C. (2013). Canonical Wnt signaling protects hippocampal neurons from Aβ oligomers: role of non-canonical Wnt-5a/Ca(2+) in mitochondrial dynamics. Front. Cell. Neurosci. 7:97. doi: 10.3389/fncel.2013.00097
    • (2013) Front. Cell. Neurosci , vol.7 , pp. 97
    • Silva-Alvarez, C.1    Arrázola, M.S.2    Godoy, J.A.3    Ordenes, D.4    Inestrosa, N.C.5
  • 137
    • 77953562457 scopus 로고    scopus 로고
    • Possible role of amyloid-beta, adenine nucleotide translocase and cyclophilin-D interaction in mitochondrial dysfunction of Alzheimer’s disease
    • Singh, P., Suman, S., Chandna, S., and Das, T. K. (2009). Possible role of amyloid-beta, adenine nucleotide translocase and cyclophilin-D interaction in mitochondrial dysfunction of Alzheimer’s disease. Bioinformation 3, 440-445. doi: 10.6026/97320630003440
    • (2009) Bioinformation , vol.3 , pp. 440-445
    • Singh, P.1    Suman, S.2    Chandna, S.3    Das, T.K.4
  • 138
    • 0035166814 scopus 로고    scopus 로고
    • Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells
    • Smirnova, E., Griparic, L., Shurland, D. L., and van der Bliek, A. M. (2001). Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol. Biol. Cell 12, 2245-2256. doi: 10.1091/mbc.12.8.2245
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2245-2256
    • Smirnova, E.1    Griparic, L.2    Shurland, D.L.3    Van Der Bliek, A.M.4
  • 139
    • 68149103297 scopus 로고    scopus 로고
    • Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion
    • Song, Z., Ghochani, M., McCaffery, J. M., Frey, T. G., and Chan, D. C. (2009). Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion. Mol. Biol. Cell 20, 3525-3532. doi: 10.1091/mbc.E09-03-0252
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3525-3532
    • Song, Z.1    Ghochani, M.2    McCaffery, J.M.3    Frey, T.G.4    Chan, D.C.5
  • 140
    • 44749089373 scopus 로고    scopus 로고
    • High-and low-calcium-dependent mechanisms of mitochondrial calcium signalling
    • Spät, A., Szanda, G., Csordás, G., and Hajnóczky, G. (2008). High-and low-calcium-dependent mechanisms of mitochondrial calcium signalling. Cell Calcium 44, 51-63. doi: 10.1016/j.ceca.2007.11.015
    • (2008) Cell Calcium , vol.44 , pp. 51-63
    • Spät, A.1    Szanda, G.2    Csordás, G.3    Hajnóczky, G.4
  • 141
    • 0027960448 scopus 로고
    • Mitogen inactivation of glycogen synthase kinase-3 β in intact cells via serine 9 phosphorylation
    • Stambolic, V., and Woodgett, J. R. (1994). Mitogen inactivation of glycogen synthase kinase-3 β in intact cells via serine 9 phosphorylation. Biochem. J. 303(Pt. 3), 701-704.
    • (1994) Biochem. J , vol.303 , pp. 701-704
    • Stambolic, V.1    Woodgett, J.R.2
  • 142
    • 34247621471 scopus 로고    scopus 로고
    • Enhanced ryanodine-mediated calcium release in mutant PS1-expressing Alzheimer’s mouse models
    • Stutzmann, G. E., Smith, I., Caccamo, A., Oddo, S., Parker, I., and Laferla, F. (2007). Enhanced ryanodine-mediated calcium release in mutant PS1-expressing Alzheimer’s mouse models. Ann. N Y Acad. Sci. 1097, 265-277. doi: 10.1196/annals.1379.025
    • (2007) Ann. N Y Acad. Sci , vol.1097 , pp. 265-277
    • Stutzmann, G.E.1    Smith, I.2    Caccamo, A.3    Oddo, S.4    Parker, I.5    Laferla, F.6
  • 143
    • 71849083948 scopus 로고
    • (2010). Abnormal mitochondrial dynamics and neurodegenerative diseases
    • Su, B., Wang, X., Zheng, L., Perry, G., Smith, M. A., and Zhu, X. (2010). Abnormal mitochondrial dynamics and neurodegenerative diseases. Biochim. Biophys. Acta 1802, 135-142. doi: 10.1016/j.bbadis.2009.09.013
    • (1802) Biochim. Biophys. Acta , pp. 135-142
    • Su, B.1    Wang, X.2    Zheng, L.3    Perry, G.4    Smith, M.A.5    Zhu, X.6
  • 144
    • 77956220629 scopus 로고    scopus 로고
    • Neuronal calcium signaling, mitochondrial dysfunction and Alzheimer’s disease
    • Supnet, C., and Bezprozvanny, I. (2010). Neuronal calcium signaling, mitochondrial dysfunction and Alzheimer’s disease. J. Alzheimers Dis. 20(Suppl. 2), S487-S498. doi: 10.3233/JAD-2010-100306
    • (2010) J. Alzheimers Dis , vol.20 , pp. 487-498
    • Supnet, C.1    Bezprozvanny, I.2
  • 145
    • 77956224679 scopus 로고    scopus 로고
    • The Alzheimer’s disease mitochondrial cascade hypothesis
    • Swerdlow, R. H., Burns, J. M., and Khan, S. M. (2010). The Alzheimer’s disease mitochondrial cascade hypothesis. J. Alzheimers Dis. 20(Suppl. 2), S265-S279. doi: 10.3233/JAD-2010-100339
    • (2010) J. Alzheimers Dis , vol.20 , pp. 265-279
    • Swerdlow, R.H.1    Burns, J.M.2    Khan, S.M.3
  • 146
    • 0033570890 scopus 로고    scopus 로고
    • Apoptosis driven by IP(3)-linked mitochondrial calcium signals
    • Szalai, G., Krishnamurthy, R., and Hajnóczky, G. (1999). Apoptosis driven by IP(3)-linked mitochondrial calcium signals. EMBO J. 18, 6349-6361. doi: 10.1093/emboj/18.22.6349
    • (1999) EMBO J , vol.18 , pp. 6349-6361
    • Szalai, G.1    Krishnamurthy, R.2    Hajnóczky, G.3
  • 147
    • 34249689057 scopus 로고    scopus 로고
    • Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission
    • Taguchi, N., Ishihara, N., Jofuku, A., Oka, T., and Mihara, K. (2007). Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission. J. Biol. Chem. 282, 11521-11529. doi: 10.1074/jbc.m607279200
    • (2007) J. Biol. Chem , vol.282 , pp. 11521-11529
    • Taguchi, N.1    Ishihara, N.2    Jofuku, A.3    Oka, T.4    Mihara, K.5
  • 148
    • 79959632321 scopus 로고    scopus 로고
    • SnapShot: Mitochondrial dynamics
    • Tamura, Y., Itoh, K., and Sesaki, H. (2011). SnapShot: mitochondrial dynamics. Cell 145, 1158-1158.e1. doi: 10.1016/j.cell.2011.06.018
    • (2011) Cell 145 , vol.145 , pp. 1158
    • Tamura, Y.1    Itoh, K.2    Sesaki, H.3
  • 149
    • 84908042347 scopus 로고    scopus 로고
    • Translocation of glycogen synthase kinase-3β (GSK-3β), a trigger of permeability transition, is kinase activity-dependent and mediated by interaction with voltage-dependent anion channel 2 (VDAC2)
    • Tanno, M., Kuno, A., Ishikawa, S., Miki, T., Kouzu, H., Yano, T., et al. (2014). Translocation of glycogen synthase kinase-3β (GSK-3β), a trigger of permeability transition, is kinase activity-dependent and mediated by interaction with voltage-dependent anion channel 2 (VDAC2). J. Biol. Chem. 289, 29285-29296. doi: 10.1074/jbc.M114.563924
    • (2014) J. Biol. Chem , vol.289 , pp. 29285-29296
    • Tanno, M.1    Kuno, A.2    Ishikawa, S.3    Miki, T.4    Kouzu, H.5    Yano, T.6
  • 150
    • 77249109792 scopus 로고    scopus 로고
    • Activation of Wnt signaling by lithium and rosiglitazone reduced spatial memory impairment and neurodegeneration in brains of an APPswe/PSEN1DeltaE9 mouse model of Alzheimer’s disease
    • Toledo, E. M., and Inestrosa, N. C. (2010). Activation of Wnt signaling by lithium and rosiglitazone reduced spatial memory impairment and neurodegeneration in brains of an APPswe/PSEN1DeltaE9 mouse model of Alzheimer’s disease. Mol. Psychiatry 15, 272-285,. doi: 10.1038/mp.2009.72
    • (2010) Mol. Psychiatry , vol.15 , pp. 272-285
    • Toledo, E.M.1    Inestrosa, N.C.2
  • 151
    • 34247485841 scopus 로고    scopus 로고
    • Role of the mitochondrial membrane permeability transition in cell death
    • Tsujimoto, Y., and Shimizu, S. (2007). Role of the mitochondrial membrane permeability transition in cell death. Apoptosis 12, 835-840. doi: 10.1007/s10495-006-0525-7
    • (2007) Apoptosis , vol.12 , pp. 835-840
    • Tsujimoto, Y.1    Shimizu, S.2
  • 152
    • 78650506425 scopus 로고    scopus 로고
    • Wingless-type family member 5A (Wnt-5a) stimulates synaptic differentiation and function of glutamatergic synapses
    • Varela-Nallar, L., Alfaro, I. E., Serrano, F. G., Parodi, J., and Inestrosa, N. C. (2010). Wingless-type family member 5A (Wnt-5a) stimulates synaptic differentiation and function of glutamatergic synapses. Proc. Natl. Acad. Sci. U S A 107, 21164-21169. doi: 10.1073/pnas.1010011107
    • (2010) Proc. Natl. Acad. Sci. U S A , vol.107 , pp. 21164-21169
    • Varela-Nallar, L.1    Alfaro, I.E.2    Serrano, F.G.3    Parodi, J.4    Inestrosa, N.C.5
  • 153
    • 84878987004 scopus 로고    scopus 로고
    • Wnt signaling in the regulation of adult hippocampal neurogenesis
    • Varela-Nallar, L., and Inestrosa, N. C. (2013). Wnt signaling in the regulation of adult hippocampal neurogenesis. Front. Cell. Neurosci. 7:100. doi: 10.3389/fncel.2013.00100
    • (2013) Front. Cell. Neurosci , vol.7 , pp. 100
    • Varela-Nallar, L.1    Inestrosa, N.C.2
  • 154
    • 84893494679 scopus 로고    scopus 로고
    • In vivo activation of Wnt signaling pathway enhances cognitive function of adult mice and reverses cognitive deficits in an Alzheimer’s disease model
    • Vargas, J. Y., Fuenzalida, M., and Inestrosa, N. C. (2014). In vivo activation of Wnt signaling pathway enhances cognitive function of adult mice and reverses cognitive deficits in an Alzheimer’s disease model. J. Neurosci. 34, 2191-2202. doi: 10.1523/jneurosci.0862-13.2014
    • (2014) J. Neurosci , vol.34 , pp. 2191-2202
    • Vargas, J.Y.1    Fuenzalida, M.2    Inestrosa, N.C.3
  • 155
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., et al. (2002). Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539. doi: 10.1038/416535a
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6
  • 156
    • 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., Tian, W., Yue, W., Liu, M., et al. (2011). Parkin ubiquitinates Drp1 for proteasome-dependent degradation: implication of dysregulated mitochondrial dynamics in Parkinson disease. J. Biol. Chem. 286, 11649-11658. doi: 10.1074/jbc.m110.144238
    • (2011) J. Biol. Chem , vol.286 , pp. 11649-11658
    • Wang, H.1    Song, P.2    Du, L.3    Tian, W.4    Yue, W.5    Liu, M.6
  • 157
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fission and fusion in Alzheimer’s disease
    • Wang, X., Su, B., Lee, H., Li, X., Perry, G., Smith, M. A., et al. (2009). Impaired balance of mitochondrial fission and fusion in Alzheimer’s disease. J. Neurosci. 29, 9090-9103. doi: 10.1523/JNEUROSCI.1357-09.2009
    • (2009) J. Neurosci , vol.29 , pp. 9090-9103
    • Wang, X.1    Su, B.2    Lee, H.3    Li, X.4    Perry, G.5    Smith, M.A.6
  • 158
    • 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, S. L., Moreira, P. I., Fujioka, H., Wang, Y., et al. (2008). Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins. Proc. Natl. Acad. Sci. U S A 105, 19318-19323. doi: 10.1073/pnas.0804871105
    • (2008) Proc. Natl. Acad. Sci. U S A , vol.105 , pp. 19318-19323
    • Wang, X.1    Su, B.2    Siedlak, S.L.3    Moreira, P.I.4    Fujioka, H.5    Wang, Y.6
  • 159
    • 84859259002 scopus 로고    scopus 로고
    • LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1
    • Wang, X., Yan, M. H., Fujioka, H., Liu, J., Wilson-delfosse, A., Chen, S. G., et al. (2012). LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1. Hum. Mol. Genet. 21, 1931-1944. doi: 10.1093/hmg/dds003
    • (2012) Hum. Mol. Genet , vol.21 , pp. 1931-1944
    • Wang, X.1    Yan, M.H.2    Fujioka, H.3    Liu, J.4    Wilson-Delfosse, A.5    Chen, S.G.6
  • 160
    • 78649413837 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in cell life and death
    • Westermann, B. (2010). Mitochondrial fusion and fission in cell life and death. Nat. Rev. Mol. Cell Biol. 11, 872-884. doi: 10.1038/nrm3013
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 872-884
    • Westermann, B.1
  • 162
    • 84872686195 scopus 로고    scopus 로고
    • Cell signaling and mitochondrial dynamics: Implications for neuronal function and neurodegenerative disease
    • Wilson, T. J., Slupe, A. M., and Strack, S. (2013). Cell signaling and mitochondrial dynamics: implications for neuronal function and neurodegenerative disease. Neurobiol. Dis. 51, 13-26. doi: 10.1016/j.nbd.2012.01.009
    • (2013) Neurobiol. Dis , vol.51 , pp. 13-26
    • Wilson, T.J.1    Slupe, A.M.2    Strack, S.3
  • 163
    • 0035933279 scopus 로고    scopus 로고
    • Intraneuronal Aβ accumulation precedes plaque formation in beta-amyloid precursor protein and presenilin-1 double-transgenic mice
    • Wirths, O., Multhaup, G., Czech, C., Blanchard, V., Moussaoui, S., Tremp, G., et al. (2001). Intraneuronal Aβ accumulation precedes plaque formation in beta-amyloid precursor protein and presenilin-1 double-transgenic mice. Neurosci. Lett. 306, 116-120. doi: 10.1016/s0304-3940(01)01876-6
    • (2001) Neurosci. Lett , vol.306 , pp. 116-120
    • Wirths, O.1    Multhaup, G.2    Czech, C.3    Blanchard, V.4    Moussaoui, S.5    Tremp, G.6
  • 164
    • 84863325404 scopus 로고    scopus 로고
    • Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson’s disease
    • Xie, W., and Chung, K. K. K. (2012). Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson’s disease. J. Neurochem. 122, 404-414. doi: 10.1111/j.1471-4159.2012.07769.x
    • (2012) J. Neurochem , vol.122 , pp. 404-414
    • Xie, W.1    Chung, K.2
  • 165
    • 84884879594 scopus 로고    scopus 로고
    • Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease
    • Yan, M. H., Wang, X., and Zhu, X. (2013). Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease. Free Radic. Biol. Med. 62, 90-101. doi: 10.1016/j.freeradbiomed.2012.11.014
    • (2013) Free Radic. Biol. Med , vol.62 , pp. 90-101
    • Yan, M.H.1    Wang, X.2    Zhu, X.3
  • 166
    • 70149093436 scopus 로고    scopus 로고
    • Mitochondrial bioenergetic deficit precedes Alzheimer’s pathology in female mouse model of Alzheimer’s disease
    • Yao, J., Irwin, R. W., Zhao, L., Nilsen, J., Hamilton, R. T., and Brinton, R. D. (2009). Mitochondrial bioenergetic deficit precedes Alzheimer’s pathology in female mouse model of Alzheimer’s disease. Proc. Natl. Acad. Sci. U S A 106, 14670-14675. doi: 10.1073/pnas.0903563106
    • (2009) Proc. Natl. Acad. Sci. U S A , vol.106 , pp. 14670-14675
    • Yao, J.1    Irwin, R.W.2    Zhao, L.3    Nilsen, J.4    Hamilton, R.T.5    Brinton, R.D.6
  • 167
  • 168
    • 84865544952 scopus 로고    scopus 로고
    • Mitochondrial fission, fusion and stress
    • Youle, R. J., and van der Bliek, A. M. (2012). Mitochondrial fission, fusion and stress. Science 337, 1062-1065. doi: 10.1126/science.1219855
    • (2012) Science , vol.337 , pp. 1062-1065
    • Youle, R.J.1    Van Der Bliek, A.M.2
  • 169
    • 77952163354 scopus 로고    scopus 로고
    • Endocytic pathways mediating oligomeric Aβ42 neurotoxicity
    • Yu, C., Nwabuisi-Heath, E., Laxton, K., and Ladu, M. J. (2010). Endocytic pathways mediating oligomeric Aβ42 neurotoxicity. Mol. Neurodegener. 5:19. doi: 10.1186/1750-1326-5-19
    • (2010) Mol. Neurodegener , vol.5 , pp. 19
    • Yu, C.1    Nwabuisi-Heath, E.2    Laxton, K.3    Ladu, M.J.4
  • 170
    • 67650245365 scopus 로고    scopus 로고
    • Regulation and pharmacology of the mitochondrial permeability transition pore
    • Zorov, D. B., Juhaszova, M., Yaniv, Y., Nuss, H. B., Wang, S., and Sollott, S. J. (2009). Regulation and pharmacology of the mitochondrial permeability transition pore. Cardiovasc. Res. 83, 213-225. doi: 10.1093/cvr/cvp151
    • (2009) Cardiovasc. Res , vol.83 , pp. 213-225
    • Zorov, D.B.1    Juhaszova, M.2    Yaniv, Y.3    Nuss, H.B.4    Wang, S.5    Sollott, S.J.6


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