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Volumn 8, Issue 8, 2012, Pages

Loss of Axonal Mitochondria Promotes Tau-Mediated Neurodegeneration and Alzheimer's Disease-Related Tau Phosphorylation Via PAR-1

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; MICRORNA; MILTON PROTEIN; MIRO PROTEIN; PARTITIONING DEFECTIVE 1 PROTEIN; PHOSPHOTRANSFERASE; SERINE; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 84866150232     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1002918     Document Type: Article
Times cited : (116)

References (62)
  • 1
    • 58149091896 scopus 로고    scopus 로고
    • The mechanism of Ca2+ -dependent regulation of kinesin-mediated mitochondrial motility
    • Wang X, Schwarz TL, (2009) The mechanism of Ca2+-dependent regulation of kinesin-mediated mitochondrial motility. Cell 136: 163-174.
    • (2009) Cell , vol.136 , pp. 163-174
    • Wang, X.1    Schwarz, T.L.2
  • 2
    • 33749398995 scopus 로고    scopus 로고
    • The genetics of axonal transport and axonal transport disorders
    • Duncan JE, Goldstein LS, (2006) The genetics of axonal transport and axonal transport disorders. PLoS Genet 2: e124 doi:10.1371/journal.pgen.0020124.
    • (2006) PLoS Genet , vol.2
    • Duncan, J.E.1    Goldstein, L.S.2
  • 3
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fission and fusion in Alzheimer's disease
    • Wang X, Su B, Lee HG, Li X, Perry G, et al. (2009) Impaired balance of mitochondrial fission and fusion in Alzheimer's disease. J Neurosci 29: 9090-9103.
    • (2009) J Neurosci , vol.29 , pp. 9090-9103
    • Wang, X.1    Su, B.2    Lee, H.G.3    Li, X.4    Perry, G.5
  • 4
    • 20044385920 scopus 로고    scopus 로고
    • Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease
    • Stokin GB, Lillo C, Falzone TL, Brusch RG, Rockenstein E, et al. (2005) Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease. Science 307: 1282-1288.
    • (2005) Science , vol.307 , pp. 1282-1288
    • Stokin, G.B.1    Lillo, C.2    Falzone, T.L.3    Brusch, R.G.4    Rockenstein, E.5
  • 5
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury
    • Cho DH, Nakamura T, Fang J, Cieplak P, Godzik A, et al. (2009) S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury. Science 324: 102-105.
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3    Cieplak, P.4    Godzik, A.5
  • 6
    • 75349092711 scopus 로고    scopus 로고
    • Expression of beta-amyloid Induced age-dependent presynaptic and axonal changes in Drosophila
    • Zhao XL, Wang WA, Tan JX, Huang JK, Zhang X, et al. (2010) Expression of beta-amyloid Induced age-dependent presynaptic and axonal changes in Drosophila. J Neurosci 30: 1512-1522.
    • (2010) J Neurosci , vol.30 , pp. 1512-1522
    • Zhao, X.L.1    Wang, W.A.2    Tan, J.X.3    Huang, J.K.4    Zhang, X.5
  • 7
    • 77949505741 scopus 로고    scopus 로고
    • Mitochondrial Mislocalization Underlies Aβ42-Induced Neuronal Dysfunction in a Drosophila Model of Alzheimer's Disease
    • Iijima-Ando K, Hearn SA, Shenton C, Gatt A, Zhao L, et al. (2009) Mitochondrial Mislocalization Underlies Aβ42-Induced Neuronal Dysfunction in a Drosophila Model of Alzheimer's Disease. PLoS ONE 4: e8310 doi:10.1371/journal.pone.0008310.
    • (2009) PLoS ONE , vol.4
    • Iijima-Ando, K.1    Hearn, S.A.2    Shenton, C.3    Gatt, A.4    Zhao, L.5
  • 8
    • 33749854516 scopus 로고    scopus 로고
    • Acute impairment of mitochondrial trafficking by beta-amyloid peptides in hippocampal neurons
    • Rui Y, Tiwari P, Xie Z, Zheng JQ, (2006) Acute impairment of mitochondrial trafficking by beta-amyloid peptides in hippocampal neurons. J Neurosci 26: 10480-10487.
    • (2006) J Neurosci , vol.26 , pp. 10480-10487
    • Rui, Y.1    Tiwari, P.2    Xie, Z.3    Zheng, J.Q.4
  • 9
    • 77957737750 scopus 로고    scopus 로고
    • Tau reduction prevents Abeta-induced defects in axonal transport
    • Vossel KA, Zhang K, Brodbeck J, Daub AC, Sharma P, et al. (2010) Tau reduction prevents Abeta-induced defects in axonal transport. Science 330: 198.
    • (2010) Science , vol.330 , pp. 198
    • Vossel, K.A.1    Zhang, K.2    Brodbeck, J.3    Daub, A.C.4    Sharma, P.5
  • 10
    • 77956587739 scopus 로고    scopus 로고
    • Abeta oligomers cause localized Ca(2+) elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines
    • Zempel H, Thies E, Mandelkow E, Mandelkow EM, (2010) Abeta oligomers cause localized Ca(2+) elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines. J Neurosci 30: 11938-11950.
    • (2010) J Neurosci , vol.30 , pp. 11938-11950
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3    Mandelkow, E.M.4
  • 11
    • 70349319844 scopus 로고    scopus 로고
    • Differential effect of three-repeat and four-repeat tau on mitochondrial axonal transport
    • Stoothoff W, Jones PB, Spires-Jones TL, Joyner D, Chhabra E, et al. (2009) Differential effect of three-repeat and four-repeat tau on mitochondrial axonal transport. J Neurochem 111: 417-427.
    • (2009) J Neurochem , vol.111 , pp. 417-427
    • Stoothoff, W.1    Jones, P.B.2    Spires-Jones, T.L.3    Joyner, D.4    Chhabra, E.5
  • 12
    • 27744600579 scopus 로고    scopus 로고
    • Over-expression of tau results in defective synaptic transmission in Drosophila neuromuscular junctions
    • Chee FC, Mudher A, Cuttle MF, Newman TA, MacKay D, et al. (2005) Over-expression of tau results in defective synaptic transmission in Drosophila neuromuscular junctions. Neurobiol Dis 20: 918-928.
    • (2005) Neurobiol Dis , vol.20 , pp. 918-928
    • Chee, F.C.1    Mudher, A.2    Cuttle, M.F.3    Newman, T.A.4    MacKay, D.5
  • 13
    • 39449138356 scopus 로고    scopus 로고
    • Tau inhibits anterograde axonal transport and perturbs stability in growing axonal neurites in part by displacing kinesin cargo: neurofilaments attenuate tau-mediated neurite instability
    • Dubey M, Chaudhury P, Kabiru H, Shea TB, (2008) Tau inhibits anterograde axonal transport and perturbs stability in growing axonal neurites in part by displacing kinesin cargo: neurofilaments attenuate tau-mediated neurite instability. Cell Motil Cytoskeleton 65: 89-99.
    • (2008) Cell Motil Cytoskeleton , vol.65 , pp. 89-99
    • Dubey, M.1    Chaudhury, P.2    Kabiru, H.3    Shea, T.B.4
  • 14
    • 67650556426 scopus 로고    scopus 로고
    • Caspase-cleaved tau expression induces mitochondrial dysfunction in immortalized cortical neurons: implications for the pathogenesis of Alzheimer disease
    • Quintanilla RA, Matthews-Roberson TA, Dolan PJ, Johnson GV, (2009) Caspase-cleaved tau expression induces mitochondrial dysfunction in immortalized cortical neurons: implications for the pathogenesis of Alzheimer disease. J Biol Chem 284: 18754-18766.
    • (2009) J Biol Chem , vol.284 , pp. 18754-18766
    • Quintanilla, R.A.1    Matthews-Roberson, T.A.2    Dolan, P.J.3    Johnson, G.V.4
  • 16
    • 0036937699 scopus 로고    scopus 로고
    • Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease
    • Augustinack JC, Schneider A, Mandelkow EM, Hyman BT, (2002) Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease. Acta Neuropathol 103: 26-35.
    • (2002) Acta Neuropathol , vol.103 , pp. 26-35
    • Augustinack, J.C.1    Schneider, A.2    Mandelkow, E.M.3    Hyman, B.T.4
  • 17
    • 30544452263 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Hollenbeck PJ, Saxton WM, (2005) The axonal transport of mitochondria. J Cell Sci 118: 5411-5419.
    • (2005) J Cell Sci , vol.118 , pp. 5411-5419
    • Hollenbeck, P.J.1    Saxton, W.M.2
  • 18
    • 23044432581 scopus 로고    scopus 로고
    • The GTPase dMiro is required for axonal transport of mitochondria to Drosophila synapses
    • Guo X, Macleod GT, Wellington A, Hu F, Panchumarthi S, et al. (2005) The GTPase dMiro is required for axonal transport of mitochondria to Drosophila synapses. Neuron 47: 379-393.
    • (2005) Neuron , vol.47 , pp. 379-393
    • Guo, X.1    Macleod, G.T.2    Wellington, A.3    Hu, F.4    Panchumarthi, S.5
  • 19
    • 33646768127 scopus 로고    scopus 로고
    • Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent
    • Glater EE, Megeath LJ, Stowers RS, Schwarz TL, (2006) Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent. J Cell Biol 173: 545-557.
    • (2006) J Cell Biol , vol.173 , pp. 545-557
    • Glater, E.E.1    Megeath, L.J.2    Stowers, R.S.3    Schwarz, T.L.4
  • 20
    • 33646117742 scopus 로고    scopus 로고
    • The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking
    • Fransson S, Ruusala A, Aspenstrom P, (2006) The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking. Biochem Biophys Res Commun 344: 500-510.
    • (2006) Biochem Biophys Res Commun , vol.344 , pp. 500-510
    • Fransson, S.1    Ruusala, A.2    Aspenstrom, P.3
  • 22
    • 0035958642 scopus 로고    scopus 로고
    • Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles
    • Wittmann CW, Wszolek MF, Shulman JM, Salvaterra PM, Lewis J, et al. (2001) Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles. Science 293: 711-714.
    • (2001) Science , vol.293 , pp. 711-714
    • Wittmann, C.W.1    Wszolek, M.F.2    Shulman, J.M.3    Salvaterra, P.M.4    Lewis, J.5
  • 23
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand AH, Perrimon N, (1993) Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118: 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 24
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress
    • Stamer K, Vogel R, Thies E, Mandelkow E, Mandelkow EM, (2002) Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J Cell Biol 156: 1051-1063.
    • (2002) J Cell Biol , vol.156 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 25
    • 20244363461 scopus 로고    scopus 로고
    • Mitochondria are redistributed in Drosophila photoreceptors lacking milton, a kinesin-associated protein
    • Gorska-Andrzejak J, Stowers RS, Borycz J, Kostyleva R, Schwarz TL, et al. (2003) Mitochondria are redistributed in Drosophila photoreceptors lacking milton, a kinesin-associated protein. J Comp Neurol 463: 372-388.
    • (2003) J Comp Neurol , vol.463 , pp. 372-388
    • Gorska-Andrzejak, J.1    Stowers, R.S.2    Borycz, J.3    Kostyleva, R.4    Schwarz, T.L.5
  • 26
    • 84859237566 scopus 로고    scopus 로고
    • Parkinson's Disease-Associated Kinase PINK1 Regulates Miro Protein Level and Axonal Transport of Mitochondria
    • Liu S, Sawada T, Lee S, Yu W, Silverio G, et al. (2012) Parkinson's Disease-Associated Kinase PINK1 Regulates Miro Protein Level and Axonal Transport of Mitochondria. PLoS Genet 8: e1002537 doi:10.1371/journal.pgen.1002537.
    • (2012) PLoS Genet , vol.8
    • Liu, S.1    Sawada, T.2    Lee, S.3    Yu, W.4    Silverio, G.5
  • 27
    • 0037118247 scopus 로고    scopus 로고
    • Human Wild-Type Tau Interacts with wingless Pathway Components and Produces Neurofibrillary Pathology in Drosophila
    • Jackson GR, Wiedau-Pazos M, Sang T-K, Wagle N, Brown CA, et al. (2002) Human Wild-Type Tau Interacts with wingless Pathway Components and Produces Neurofibrillary Pathology in Drosophila. Neuron 34: 509-519.
    • (2002) Neuron , vol.34 , pp. 509-519
    • Jackson, G.R.1    Wiedau-Pazos, M.2    Sang, T.-K.3    Wagle, N.4    Brown, C.A.5
  • 28
    • 0346361872 scopus 로고    scopus 로고
    • Genetic modifiers of tauopathy in Drosophila
    • Shulman JM, Feany MB, (2003) Genetic modifiers of tauopathy in Drosophila. Genetics 165: 1233-1242.
    • (2003) Genetics , vol.165 , pp. 1233-1242
    • Shulman, J.M.1    Feany, M.B.2
  • 29
    • 34047106848 scopus 로고    scopus 로고
    • Cytoskeleton proteins are modulators of mutant tau-induced neurodegeneration in Drosophila
    • Blard O, Feuillette S, Bou J, Chaumette B, Frebourg T, et al. (2007) Cytoskeleton proteins are modulators of mutant tau-induced neurodegeneration in Drosophila. Hum Mol Genet 16: 555-566.
    • (2007) Hum Mol Genet , vol.16 , pp. 555-566
    • Blard, O.1    Feuillette, S.2    Bou, J.3    Chaumette, B.4    Frebourg, T.5
  • 30
    • 81855172495 scopus 로고    scopus 로고
    • Functional Genomic Screen and Network Analysis Reveal Novel Modifiers of Tauopathy Dissociated from Tau Phosphorylation
    • Ambegaokar SS, Jackson GR, (2011) Functional Genomic Screen and Network Analysis Reveal Novel Modifiers of Tauopathy Dissociated from Tau Phosphorylation. Hum Mol Genet 20: 4947-4977.
    • (2011) Hum Mol Genet , vol.20 , pp. 4947-4977
    • Ambegaokar, S.S.1    Jackson, G.R.2
  • 32
    • 0027338266 scopus 로고
    • Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding
    • Biernat J, Gustke N, Drewes G, Mandelkow EM, Mandelkow E, (1993) Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron 11: 153-163.
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 33
    • 0028937631 scopus 로고
    • Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262
    • Drewes G, Trinczek B, Illenberger S, Biernat J, Schmitt-Ulms G, et al. (1995) Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262. J Biol Chem 270: 7679-7688.
    • (1995) J Biol Chem , vol.270 , pp. 7679-7688
    • Drewes, G.1    Trinczek, B.2    Illenberger, S.3    Biernat, J.4    Schmitt-Ulms, G.5
  • 34
    • 77953510471 scopus 로고    scopus 로고
    • Structure and function of polarity-inducing kinase family MARK/Par-1 within the branch of AMPK/Snf1-related kinases
    • Marx A, Nugoor C, Panneerselvam S, Mandelkow E, (2010) Structure and function of polarity-inducing kinase family MARK/Par-1 within the branch of AMPK/Snf1-related kinases. FASEB J 24: 1637-1648.
    • (2010) FASEB J , vol.24 , pp. 1637-1648
    • Marx, A.1    Nugoor, C.2    Panneerselvam, S.3    Mandelkow, E.4
  • 35
    • 1542358895 scopus 로고    scopus 로고
    • PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila
    • Nishimura I, Yang Y, Lu B, (2004) PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila. Cell 116: 671-682.
    • (2004) Cell , vol.116 , pp. 671-682
    • Nishimura, I.1    Yang, Y.2    Lu, B.3
  • 36
    • 77952482205 scopus 로고    scopus 로고
    • A DNA damage-activated checkpoint kinase phosphorylates tau and enhances tau-induced neurodegeneration
    • Iijima-Ando K, Zhao L, Gatt A, Shenton C, Iijima K, (2010) A DNA damage-activated checkpoint kinase phosphorylates tau and enhances tau-induced neurodegeneration. Hum Mol Genet 19: 1930-1938.
    • (2010) Hum Mol Genet , vol.19 , pp. 1930-1938
    • Iijima-Ando, K.1    Zhao, L.2    Gatt, A.3    Shenton, C.4    Iijima, K.5
  • 37
    • 33846448743 scopus 로고    scopus 로고
    • Activation of PAR-1 kinase and stimulation of tau phosphorylation by diverse signals require the tumor suppressor protein LKB1
    • Wang JW, Imai Y, Lu B, (2007) Activation of PAR-1 kinase and stimulation of tau phosphorylation by diverse signals require the tumor suppressor protein LKB1. J Neurosci 27: 574-581.
    • (2007) J Neurosci , vol.27 , pp. 574-581
    • Wang, J.W.1    Imai, Y.2    Lu, B.3
  • 38
    • 84859624394 scopus 로고    scopus 로고
    • A Novel Drosophila Model of Nerve Injury Reveals an Essential Role of Nmnat in Maintaining Axonal Integrity
    • Fang Y, Soares L, Teng X, Geary M, Bonini NM, (2012) A Novel Drosophila Model of Nerve Injury Reveals an Essential Role of Nmnat in Maintaining Axonal Integrity. Curr Biol 10.1016/j.cub.2012.01.065.
    • (2012) Curr Biol
    • Fang, Y.1    Soares, L.2    Teng, X.3    Geary, M.4    Bonini, N.M.5
  • 39
    • 0034814018 scopus 로고    scopus 로고
    • Identification and characterization of the Drosophila tau homolog
    • Heidary G, Fortini ME, (2001) Identification and characterization of the Drosophila tau homolog. Mech Dev 108: 171-178.
    • (2001) Mech Dev , vol.108 , pp. 171-178
    • Heidary, G.1    Fortini, M.E.2
  • 40
    • 78049427560 scopus 로고    scopus 로고
    • Inhibition of GSK-3 ameliorates Abeta pathology in an adult-onset Drosophila model of Alzheimer's disease
    • Sofola O, Kerr F, Rogers I, Killick R, Augustin H, et al. (2010) Inhibition of GSK-3 ameliorates Abeta pathology in an adult-onset Drosophila model of Alzheimer's disease. PLoS Genet 6: e1001087 doi:10.1371/journal.pgen.1001087.
    • (2010) PLoS Genet , vol.6
    • Sofola, O.1    Kerr, F.2    Rogers, I.3    Killick, R.4    Augustin, H.5
  • 41
    • 2542590202 scopus 로고    scopus 로고
    • Learning and memory deficits upon TAU accumulation in Drosophila mushroom body neurons
    • Mershin A, Pavlopoulos E, Fitch O, Braden BC, Nanopoulos DV, et al. (2004) Learning and memory deficits upon TAU accumulation in Drosophila mushroom body neurons. Learn Mem 11: 277-287.
    • (2004) Learn Mem , vol.11 , pp. 277-287
    • Mershin, A.1    Pavlopoulos, E.2    Fitch, O.3    Braden, B.C.4    Nanopoulos, D.V.5
  • 42
    • 34548317186 scopus 로고    scopus 로고
    • A comparison of the neuronal dysfunction caused by Drosophila tau and human tau in a Drosophila model of tauopathies
    • Ubhi KK, Shaibah H, Newman TA, Shepherd D, Mudher A, (2007) A comparison of the neuronal dysfunction caused by Drosophila tau and human tau in a Drosophila model of tauopathies. Invert Neurosci 7: 165-171.
    • (2007) Invert Neurosci , vol.7 , pp. 165-171
    • Ubhi, K.K.1    Shaibah, H.2    Newman, T.A.3    Shepherd, D.4    Mudher, A.5
  • 43
    • 34247615021 scopus 로고    scopus 로고
    • Study of tauopathies by comparing Drosophila and human tau in Drosophila
    • Chen X, Li Y, Huang J, Cao D, Yang G, et al. (2007) Study of tauopathies by comparing Drosophila and human tau in Drosophila. Cell Tissue Res 329: 169-178.
    • (2007) Cell Tissue Res , vol.329 , pp. 169-178
    • Chen, X.1    Li, Y.2    Huang, J.3    Cao, D.4    Yang, G.5
  • 44
    • 0037393454 scopus 로고    scopus 로고
    • Neuropathology of human Alzheimer disease after immunization with amyloid-beta peptide: a case report
    • Nicoll JA, Wilkinson D, Holmes C, Steart P, Markham H, et al. (2003) Neuropathology of human Alzheimer disease after immunization with amyloid-beta peptide: a case report. Nat Med 9: 448-452.
    • (2003) Nat Med , vol.9 , pp. 448-452
    • Nicoll, J.A.1    Wilkinson, D.2    Holmes, C.3    Steart, P.4    Markham, H.5
  • 45
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J, Dickson DW, Lin WL, Chisholm L, Corral A, et al. (2001) Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 293: 1487-1491.
    • (2001) Science , vol.293 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.L.3    Chisholm, L.4    Corral, A.5
  • 46
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils
    • Gotz J, Chen F, van Dorpe J, Nitsch RM, (2001) Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils. Science 293: 1491-1495.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    van Dorpe, J.3    Nitsch, R.M.4
  • 47
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Abeta and synaptic dysfunction
    • Oddo S, Caccamo A, Shepherd JD, Murphy MP, Golde TE, et al. (2003) Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Abeta and synaptic dysfunction. Neuron 39: 409-421.
    • (2003) Neuron , vol.39 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5
  • 48
    • 4043167747 scopus 로고    scopus 로고
    • Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • Oddo S, Billings L, Kesslak JP, Cribbs DH, LaFerla FM, (2004) Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 43: 321-332.
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 50
    • 33751218015 scopus 로고    scopus 로고
    • Tau-dependent microtubule disassembly initiated by prefibrillar beta-amyloid
    • King ME, Kan HM, Baas PW, Erisir A, Glabe CG, et al. (2006) Tau-dependent microtubule disassembly initiated by prefibrillar beta-amyloid. J Cell Biol 175: 541-546.
    • (2006) J Cell Biol , vol.175 , pp. 541-546
    • King, M.E.1    Kan, H.M.2    Baas, P.W.3    Erisir, A.4    Glabe, C.G.5
  • 51
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model
    • Roberson ED, Scearce-Levie K, Palop JJ, Yan F, Cheng IH, et al. (2007) Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model. Science 316: 750-754.
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5
  • 52
    • 33947286683 scopus 로고    scopus 로고
    • Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo
    • Fulga TA, Elson-Schwab I, Khurana V, Steinhilb ML, Spires TL, et al. (2007) Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo. Nat Cell Biol 9: 139-148.
    • (2007) Nat Cell Biol , vol.9 , pp. 139-148
    • Fulga, T.A.1    Elson-Schwab, I.2    Khurana, V.3    Steinhilb, M.L.4    Spires, T.L.5
  • 53
    • 77957254409 scopus 로고    scopus 로고
    • Tau Ser262 phosphorylation is critical for Abeta42-induced tau toxicity in a transgenic Drosophila model of Alzheimer's disease
    • Iijima K, Gatt A, Iijima-Ando K, (2010) Tau Ser262 phosphorylation is critical for Abeta42-induced tau toxicity in a transgenic Drosophila model of Alzheimer's disease. Hum Mol Genet 19: 2947-2957.
    • (2010) Hum Mol Genet , vol.19 , pp. 2947-2957
    • Iijima, K.1    Gatt, A.2    Iijima-Ando, K.3
  • 54
    • 33947307791 scopus 로고    scopus 로고
    • Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1
    • Thies E, Mandelkow EM, (2007) Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1. J Neurosci 27: 2896-2907.
    • (2007) J Neurosci , vol.27 , pp. 2896-2907
    • Thies, E.1    Mandelkow, E.M.2
  • 55
    • 5444273804 scopus 로고    scopus 로고
    • MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons
    • Mandelkow EM, Thies E, Trinczek B, Biernat J, Mandelkow E, (2004) MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons. J Cell Biol 167: 99-110.
    • (2004) J Cell Biol , vol.167 , pp. 99-110
    • Mandelkow, E.M.1    Thies, E.2    Trinczek, B.3    Biernat, J.4    Mandelkow, E.5
  • 56
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore C, Lee VM, Trojanowski JQ, (2007) Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat Rev Neurosci 8: 663-672.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 57
    • 77952215397 scopus 로고    scopus 로고
    • Bazooka is required for polarisation of the Drosophila anterior-posterior axis
    • Doerflinger H, Vogt N, Torres IL, Mirouse V, Koch I, et al. (2003) Bazooka is required for polarisation of the Drosophila anterior-posterior axis. Development 137: 1765-1773.
    • (2003) Development , vol.137 , pp. 1765-1773
    • Doerflinger, H.1    Vogt, N.2    Torres, I.L.3    Mirouse, V.4    Koch, I.5
  • 58
    • 80051790291 scopus 로고    scopus 로고
    • DAPK activates MARK1/2 to regulate microtubule assembly, neuronal differentiation, and tau toxicity
    • Wu PR, Tsai PI, Chen GC, Chou HJ, Huang YP, et al. (2011) DAPK activates MARK1/2 to regulate microtubule assembly, neuronal differentiation, and tau toxicity. Cell Death Differ 18: 1507-1520.
    • (2011) Cell Death Differ , vol.18 , pp. 1507-1520
    • Wu, P.R.1    Tsai, P.I.2    Chen, G.C.3    Chou, H.J.4    Huang, Y.P.5
  • 59
    • 80052154328 scopus 로고    scopus 로고
    • Drosophila adducin regulates Dlg phosphorylation and targeting of Dlg to the synapse and epithelial membrane
    • Wang S, Yang J, Tsai A, Kuca T, Sanny J, et al. (2011) Drosophila adducin regulates Dlg phosphorylation and targeting of Dlg to the synapse and epithelial membrane. Dev Biol 357: 392-403.
    • (2011) Dev Biol , vol.357 , pp. 392-403
    • Wang, S.1    Yang, J.2    Tsai, A.3    Kuca, T.4    Sanny, J.5
  • 60
    • 79959305691 scopus 로고    scopus 로고
    • Mitochondria: the next (neurode)generation
    • Schon EA, Przedborski S, (2011) Mitochondria: the next (neurode)generation. Neuron 70: 1033-1053.
    • (2011) Neuron , vol.70 , pp. 1033-1053
    • Schon, E.A.1    Przedborski, S.2
  • 61
    • 34447530305 scopus 로고    scopus 로고
    • A genome-wide transgenic RNAi library for conditional gene inactivation in Drosophila
    • Dietzl G, Chen D, Schnorrer F, Su KC, Barinova Y, et al. (2007) A genome-wide transgenic RNAi library for conditional gene inactivation in Drosophila. Nature 448: 151-156.
    • (2007) Nature , vol.448 , pp. 151-156
    • Dietzl, G.1    Chen, D.2    Schnorrer, F.3    Su, K.C.4    Barinova, Y.5
  • 62
    • 77950940279 scopus 로고    scopus 로고
    • Drosophila models of human tauopathies indicate that Tau protein toxicity in vivo is mediated by soluble cytosolic phosphorylated forms of the protein
    • Feuillette S, Miguel L, Frebourg T, Campion D, Lecourtois M, (2010) Drosophila models of human tauopathies indicate that Tau protein toxicity in vivo is mediated by soluble cytosolic phosphorylated forms of the protein. J Neurochem 113: 895-903.
    • (2010) J Neurochem , vol.113 , pp. 895-903
    • Feuillette, S.1    Miguel, L.2    Frebourg, T.3    Campion, D.4    Lecourtois, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.