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Volumn 24, Issue 13, 2015, Pages 3623-3637

Impaired retrograde transport by the Dynein/Dynactin complex contributes to Tau-induced toxicity

Author keywords

[No Author keywords available]

Indexed keywords

DYNACTIN; DYNEIN ADENOSINE TRIPHOSPHATASE; DYNEIN DYNACTIN COMPLEX; GLUTAMINE; MESSENGER RNA; TAR DNA BINDING PROTEIN; TAU PROTEIN; TUBULIN; UNCLASSIFIED DRUG; DROSOPHILA PROTEIN; MICROTUBULE ASSOCIATED PROTEIN; TAU PROTEIN, DROSOPHILA;

EID: 84936748562     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddv107     Document Type: Article
Times cited : (57)

References (80)
  • 1
    • 0031738468 scopus 로고    scopus 로고
    • Tau pathology in two Dutch families with mutations in the microtubule-binding region of tau
    • Spillantini, M.G., Crowther, R.A., Kamphorst, W., Heutink, P. and van Swieten, J.C. (1998) Tau pathology in two Dutch families with mutations in the microtubule-binding region of tau. Am. J. Pathol., 153, 1359-1363.
    • (1998) Am. J. Pathol , vol.153 , pp. 1359-1363
    • Spillantini, M.G.1    Crowther, R.A.2    Kamphorst, W.3    Heutink, P.4    van Swieten, J.C.5
  • 4
    • 0033011181 scopus 로고    scopus 로고
    • Accelerated filament formation from tau protein with specific FTDP-17 missense mutations
    • Nacharaju, P., Lewis, J., Easson, C., Yen, S., Hackett, J., Hutton, M. and Yen, S.H. (1999) Accelerated filament formation from tau protein with specific FTDP-17 missense mutations. FEBS Lett., 447, 195-199.
    • (1999) FEBS Lett , vol.447 , pp. 195-199
    • Nacharaju, P.1    Lewis, J.2    Easson, C.3    Yen, S.4    Hackett, J.5    Hutton, M.6    Yen, S.H.7
  • 5
    • 0002792366 scopus 로고
    • Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau
    • Goedert, M., Wischik, C.M., Crowther, R.A., Walker, J.E. and Klug, A. (1988) Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau. Proc. Natl Acad. Sci. USA, 85, 4051-4055.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 6
    • 0024109663 scopus 로고
    • The carboxyl third of tau is tightly bound to paired helical filaments
    • Kondo, J., Honda, T., Mori, H., Hamada, Y., Miura, R., Ogawara, M. and Ihara, Y. (1988) The carboxyl third of tau is tightly bound to paired helical filaments. Neuron, 1, 827-834.
    • (1988) Neuron , vol.1 , pp. 827-834
    • Kondo, J.1    Honda, T.2    Mori, H.3    Hamada, Y.4    Miura, R.5    Ogawara, M.6    Ihara, Y.7
  • 7
    • 0024109687 scopus 로고
    • Epitopes that span the tau molecule are shared with paired helical filaments
    • Kosik, K.S., Orecchio, L.D., Binder, L., Trojanowski, J.Q., Lee, V. M. and Lee, G. (1988) Epitopes that span the tau molecule are shared with paired helical filaments. Neuron, 1, 817-825.
    • (1988) Neuron , vol.1 , pp. 817-825
    • Kosik, K.S.1    Orecchio, L.D.2    Binder, L.3    Trojanowski, J.Q.4    Lee, V.M.5    Lee, G.6
  • 9
    • 0025904444 scopus 로고
    • A68: a major subunit of paired helical filaments and derivatized forms of normal Tau
    • Lee, V.M., Balin, B.J., Otvos, L. Jr. and Trojanowski, J.Q. (1991) A68: a major subunit of paired helical filaments and derivatized forms of normal Tau. Science, 251, 675-678.
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.1    Balin, B.J.2    Otvos, L.3    Trojanowski, J.Q.4
  • 11
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel, D.N., Hyman, A.A., Cobb, M.H. and Kirschner, M.W. (1992) Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell, 3, 1141-1154.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 13
    • 0028820411 scopus 로고
    • Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules
    • Trinczek, B., Biernat, J., Baumann, K., Mandelkow, E.M. and Mandelkow, E. (1995) Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules. Mol. Biol. Cell, 6, 1887-1902.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1887-1902
    • Trinczek, B.1    Biernat, J.2    Baumann, K.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 14
    • 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, E.M. and 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
  • 15
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • Lindwall, G. and Cole, R.D. (1984) Phosphorylation affects the ability of tau protein to promote microtubule assembly. J. Biol. Chem., 259, 5301-5305.
    • (1984) J. Biol. Chem , vol.259 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 16
    • 0033850080 scopus 로고    scopus 로고
    • Abnormal tau-containing filaments in neurodegenerative diseases
    • Crowther, R.A. and Goedert, M. (2000) Abnormal tau-containing filaments in neurodegenerative diseases. J. Struct. Biol., 130, 271-279.
    • (2000) J. Struct. Biol , vol.130 , pp. 271-279
    • Crowther, R.A.1    Goedert, M.2
  • 18
    • 0025863618 scopus 로고
    • Neuropathological staging of Alzheimer-related changes
    • Braak, H. and Braak, E. (1991) Neuropathological staging of Alzheimer-related changes. Acta Neuropathol., 82, 239-259.
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 21
    • 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.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 23
    • 0037111833 scopus 로고    scopus 로고
    • Tau-mediated cytotoxicity in a pseudohyperphosphorylation model of Alzheimer's disease
    • Fath, T., Eidenmuller, J. and Brandt, R. (2002) Tau-mediated cytotoxicity in a pseudohyperphosphorylation model of Alzheimer's disease. J. Neurosci., 22, 9733-9741.
    • (2002) J. Neurosci , vol.22 , pp. 9733-9741
    • Fath, T.1    Eidenmuller, J.2    Brandt, R.3
  • 25
    • 2342444942 scopus 로고    scopus 로고
    • Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival
    • Shimura, H., Miura-Shimura, Y. and Kosik, K.S. (2004) Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival. J. Biol. Chem., 279, 17957-17962.
    • (2004) J. Biol. Chem , vol.279 , pp. 17957-17962
    • Shimura, H.1    Miura-Shimura, Y.2    Kosik, K.S.3
  • 27
    • 84925883347 scopus 로고    scopus 로고
    • Microtubule-stabilizing agents as potential therapeutics for neurodegenerative disease
    • Brunden, K.R., Trojanowski, J.Q., Smith, A.B. III, Lee, V.M. and Ballatore, C. (2014) Microtubule-stabilizing agents as potential therapeutics for neurodegenerative disease. Bioorg. Med. Chem., 22, 5040-5049.
    • (2014) Bioorg. Med. Chem , vol.22 , pp. 5040-5049
    • Brunden, K.R.1    Trojanowski, J.Q.2    Smith, A.B.3    Lee, V.M.4    Ballatore, C.5
  • 28
    • 84863230105 scopus 로고    scopus 로고
    • The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice
    • Zhang, B., Carroll, J., Trojanowski, J.Q., Yao, Y., Iba, M., Potuzak, J.S., Hogan, A.M., Xie, S.X., Ballatore, C., Smith, A.B. III et al. (2012) The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice. J. Neurosci., 32, 3601-3611.
    • (2012) J. Neurosci , vol.32 , pp. 3601-3611
    • Zhang, B.1    Carroll, J.2    Trojanowski, J.Q.3    Yao, Y.4    Iba, M.5    Potuzak, J.S.6    Hogan, A.M.7    Xie, S.X.8    Ballatore, C.9    Smith, A.B.10
  • 29
    • 78149411188 scopus 로고    scopus 로고
    • Soluble hyper-phosphorylated tau causes microtubule breakdown and functionally compromises normal tau in vivo
    • Cowan, C.M., Bossing, T., Page, A., Shepherd, D. and Mudher, A. (2010) Soluble hyper-phosphorylated tau causes microtubule breakdown and functionally compromises normal tau in vivo. Acta Neuropathol., 120, 593-604.
    • (2010) Acta Neuropathol , vol.120 , pp. 593-604
    • Cowan, C.M.1    Bossing, T.2    Page, A.3    Shepherd, D.4    Mudher, A.5
  • 31
    • 79960284291 scopus 로고    scopus 로고
    • The power and richness of modelling tauopathies in Drosophila
    • Papanikolopoulou, K. and Skoulakis, E.M. (2011) The power and richness of modelling tauopathies in Drosophila. Mol. Neurobiol., 44, 122-133.
    • (2011) Mol. Neurobiol , vol.44 , pp. 122-133
    • Papanikolopoulou, K.1    Skoulakis, E.M.2
  • 32
    • 33749242234 scopus 로고    scopus 로고
    • Drosophila in the study of neurodegenerative disease
    • Marsh, J.L. and Thompson, L.M. (2006) Drosophila in the study of neurodegenerative disease. Neuron, 52, 169-178.
    • (2006) Neuron , vol.52 , pp. 169-178
    • Marsh, J.L.1    Thompson, L.M.2
  • 33
    • 84887065883 scopus 로고    scopus 로고
    • Drosophila as a screening tool to study human neurodegenerative diseases
    • Lenz, S., Karsten, P., Schulz, J.B. and Voigt, A. (2013) Drosophila as a screening tool to study human neurodegenerative diseases. J. Neurochem., 127, 453-460.
    • (2013) J. Neurochem , vol.127 , pp. 453-460
    • Lenz, S.1    Karsten, P.2    Schulz, J.B.3    Voigt, A.4
  • 34
    • 84887869663 scopus 로고    scopus 로고
    • Drosophila melanogaster as a model organism for Alzheimer's disease
    • Prüssing, K., Voigt, A. and Schulz, J.B. (2013) Drosophila melanogaster as a model organism for Alzheimer's disease. Mol. Neurodegener., 8, 35.
    • (2013) Mol. Neurodegener , vol.8 , pp. 35
    • Prüssing, K.1    Voigt, A.2    Schulz, J.B.3
  • 36
    • 5444234179 scopus 로고    scopus 로고
    • RNA interference: from model organisms towards therapy for neural and neuromuscular disorders
    • Buckingham, S.D., Esmaeili, B., Wood, M. and Sattelle, D.B. (2004) RNA interference: from model organisms towards therapy for neural and neuromuscular disorders. Hum. Mol. Genet., 13(Spec No. 2), R275-R288.
    • (2004) Hum. Mol. Genet , vol.13 , pp. R275-R288
    • Buckingham, S.D.1    Esmaeili, B.2    Wood, M.3    Sattelle, D.B.4
  • 37
    • 1842715778 scopus 로고    scopus 로고
    • Dicers at RISC: the mechanism of RNAi
    • Tijsterman, M. and Plasterk, R.H. (2004) Dicers at RISC: the mechanism of RNAi. Cell, 117, 1-3.
    • (2004) Cell , vol.117 , pp. 1-3
    • Tijsterman, M.1    Plasterk, R.H.2
  • 38
    • 0346361872 scopus 로고    scopus 로고
    • Genetic modifiers of tauopathy in Drosophila
    • Shulman, J.M. and Feany, M.B. (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
  • 39
    • 81855172495 scopus 로고    scopus 로고
    • Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation
    • Ambegaokar, S.S. and Jackson, G.R. (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
  • 41
    • 0034629073 scopus 로고    scopus 로고
    • Genetic suppression of polyglutamine toxicity in Drosophila
    • Kazemi-Esfarjani, P. and Benzer, S. (2000) Genetic suppression of polyglutamine toxicity in Drosophila. Science, 287, 1837-1840.
    • (2000) Science , vol.287 , pp. 1837-1840
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 42
    • 35949001344 scopus 로고    scopus 로고
    • Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila
    • Bilen, J. and Bonini, N.M. (2007) Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila. PLoS Genet., 3, 1950-1964.
    • (2007) PLoS Genet , vol.3 , pp. 1950-1964
    • Bilen, J.1    Bonini, N.M.2
  • 43
    • 40149101562 scopus 로고    scopus 로고
    • Polyglutamine genes interact to modulate the severity and progression of neurodegeneration in Drosophila
    • Lessing, D. and Bonini, N.M. (2008) Polyglutamine genes interact to modulate the severity and progression of neurodegeneration in Drosophila. PLoS Biol., 6, e29.
    • (2008) PLoS Biol , vol.6
    • Lessing, D.1    Bonini, N.M.2
  • 44
    • 33847660443 scopus 로고    scopus 로고
    • An optimized transgenesis system for Drosophila using germ-line-specific phiC31 integrases
    • Bischof, J., Maeda, R.K., Hediger, M., Karch, F. and Basler, K. (2007) An optimized transgenesis system for Drosophila using germ-line-specific phiC31 integrases. Proc. Natl Acad. Sci. USA, 104, 3312-3317.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 3312-3317
    • Bischof, J.1    Maeda, R.K.2    Hediger, M.3    Karch, F.4    Basler, K.5
  • 45
    • 0033004145 scopus 로고    scopus 로고
    • Cytoplasmic dynein and dynactin in cell division and intracellular transport
    • Karki, S. and Holzbaur, E.L. (1999) Cytoplasmic dynein and dynactin in cell division and intracellular transport. Curr. Opin. Cell Biol., 11, 45-53.
    • (1999) Curr. Opin. Cell Biol , vol.11 , pp. 45-53
    • Karki, S.1    Holzbaur, E.L.2
  • 46
    • 70450228589 scopus 로고    scopus 로고
    • Regulators of the cytoplasmic dynein motor
    • Kardon, J.R. and Vale, R.D. (2009) Regulators of the cytoplasmic dynein motor. Nat. Rev. Mol. Cell Biol., 10, 854-865.
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 854-865
    • Kardon, J.R.1    Vale, R.D.2
  • 47
    • 0029911064 scopus 로고    scopus 로고
    • Kinesin mutations cause motor neuron disease phenotypes by disrupting fast axonal transport in Drosophila
    • Hurd, D.D. and Saxton, W.M. (1996) Kinesin mutations cause motor neuron disease phenotypes by disrupting fast axonal transport in Drosophila. Genetics, 144, 1075-1085.
    • (1996) Genetics , vol.144 , pp. 1075-1085
    • Hurd, D.D.1    Saxton, W.M.2
  • 50
    • 0033232718 scopus 로고    scopus 로고
    • Targeted expression of truncated glued disrupts giant fiber synapse formation in Drosophila
    • Allen, M.J., Shan, X., Caruccio, P., Froggett, S.J., Moffat, K.G. and Murphey, R.K. (1999) Targeted expression of truncated glued disrupts giant fiber synapse formation in Drosophila. J. Neurosci., 19, 9374-9384.
    • (1999) J. Neurosci , vol.19 , pp. 9374-9384
    • Allen, M.J.1    Shan, X.2    Caruccio, P.3    Froggett, S.J.4    Moffat, K.G.5    Murphey, R.K.6
  • 51
    • 0037198709 scopus 로고    scopus 로고
    • Dynactin is necessary for synapse stabilization
    • Eaton, B.A., Fetter, R.D. and Davis, G.W. (2002) Dynactin is necessary for synapse stabilization. Neuron, 34, 729-741.
    • (2002) Neuron , vol.34 , pp. 729-741
    • Eaton, B.A.1    Fetter, R.D.2    Davis, G.W.3
  • 52
    • 32944482206 scopus 로고    scopus 로고
    • The expression pattern of the Drosophila vesicular glutamate transporter: a marker protein for motoneurons and glutamatergic centers in the brain
    • Mahr, A. and Aberle, H. (2006) The expression pattern of the Drosophila vesicular glutamate transporter: a marker protein for motoneurons and glutamatergic centers in the brain. Gene Expr. Patterns, 6, 299-309.
    • (2006) Gene Expr. Patterns , vol.6 , pp. 299-309
    • Mahr, A.1    Aberle, H.2
  • 53
    • 0345276565 scopus 로고    scopus 로고
    • Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses
    • Mandelkow, E.M., Stamer, K., Vogel, R., Thies, E. and Mandelkow, E. (2003) Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses. Neurobiol. Aging, 24, 1079-1085.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1079-1085
    • Mandelkow, E.M.1    Stamer, K.2    Vogel, R.3    Thies, E.4    Mandelkow, E.5
  • 55
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A.H. and 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
  • 56
    • 0034716223 scopus 로고    scopus 로고
    • Tau and tau reporters disrupt central projections of sensory neurons in Drosophila
    • Williams, D.W., Tyrer, M. and Shepherd, D. (2000) Tau and tau reporters disrupt central projections of sensory neurons in Drosophila. J. Comp. Neurol., 428, 630-640.
    • (2000) J. Comp. Neurol , vol.428 , pp. 630-640
    • Williams, D.W.1    Tyrer, M.2    Shepherd, D.3
  • 58
    • 0036892302 scopus 로고    scopus 로고
    • Tau gene mutations: dissecting the pathogenesis of FTDP-17
    • Ingram, E.M. and Spillantini, M.G. (2002) Tau gene mutations: dissecting the pathogenesis of FTDP-17. Trends Mol. Med., 8, 555-562.
    • (2002) Trends Mol. Med , vol.8 , pp. 555-562
    • Ingram, E.M.1    Spillantini, M.G.2
  • 59
    • 10944241542 scopus 로고    scopus 로고
    • Tau alteration and neuronal degeneration in tauopathies: mechanisms and models
    • Brandt, R., Hundelt, M. and Shahani, N. (2005) Tau alteration and neuronal degeneration in tauopathies: mechanisms and models. Biochim. Biophys. Acta, 1739, 331-354.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 331-354
    • Brandt, R.1    Hundelt, M.2    Shahani, N.3
  • 60
    • 70350532246 scopus 로고    scopus 로고
    • Cwc25 is a novel splicing factor required after Prp2 and Yju2 to facilitate the first catalytic reaction
    • Chiu, Y.F., Liu, Y.C., Chiang, T.W., Yeh, T.C., Tseng, C.K., Wu, N.Y. and Cheng, S.C. (2009) Cwc25 is a novel splicing factor required after Prp2 and Yju2 to facilitate the first catalytic reaction. Mol. Cell. Biol., 29, 5671-5678.
    • (2009) Mol. Cell. Biol , vol.29 , pp. 5671-5678
    • Chiu, Y.F.1    Liu, Y.C.2    Chiang, T.W.3    Yeh, T.C.4    Tseng, C.K.5    Wu, N.Y.6    Cheng, S.C.7
  • 62
    • 33646133424 scopus 로고    scopus 로고
    • Molecular pathways that influence human tau-induced pathology in Caenorhabditis elegans
    • Kraemer, B.C., Burgess, J.K., Chen, J.H., Thomas, J.H. and Schellenberg, G.D. (2006) Molecular pathways that influence human tau-induced pathology in Caenorhabditis elegans. Hum. Mol. Genet., 15, 1483-1496.
    • (2006) Hum. Mol. Genet , vol.15 , pp. 1483-1496
    • Kraemer, B.C.1    Burgess, J.K.2    Chen, J.H.3    Thomas, J.H.4    Schellenberg, G.D.5
  • 63
    • 0033366384 scopus 로고    scopus 로고
    • Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons
    • Williamson, T.L. and Cleveland, D.W. (1999) Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons. Nat. Neurosci., 2, 50-56.
    • (1999) Nat. Neurosci , vol.2 , pp. 50-56
    • Williamson, T.L.1    Cleveland, D.W.2
  • 64
    • 0345599021 scopus 로고    scopus 로고
    • Smn, the spinal muscular atrophy-determining gene product, modulates axon growth and localization of beta-actin mRNA in growth cones of motoneurons
    • Rossoll, W., Jablonka, S., Andreassi, C., Kroning, A.K., Karle, K., Monani, U.R. and Sendtner, M. (2003) Smn, the spinal muscular atrophy-determining gene product, modulates axon growth and localization of beta-actin mRNA in growth cones of motoneurons. J. Cell Biol., 163, 801-812.
    • (2003) J. Cell Biol , vol.163 , pp. 801-812
    • Rossoll, W.1    Jablonka, S.2    Andreassi, C.3    Kroning, A.K.4    Karle, K.5    Monani, U.R.6    Sendtner, M.7
  • 65
    • 0037328987 scopus 로고    scopus 로고
    • Science in motion: common molecular pathological themes emerge in the hereditary spastic paraplegias
    • Reid, E. (2003) Science in motion: common molecular pathological themes emerge in the hereditary spastic paraplegias. J. Med. Genet., 40, 81-86.
    • (2003) J. Med. Genet , vol.40 , pp. 81-86
    • Reid, E.1
  • 66
    • 0033230886 scopus 로고    scopus 로고
    • Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform
    • Ishihara, T., Hong, M., Zhang, B., Nakagawa, Y., Lee, M.K., Trojanowski, J.Q. and Lee, V.M. (1999) Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform. Neuron, 24, 751-762.
    • (1999) Neuron , vol.24 , pp. 751-762
    • Ishihara, T.1    Hong, M.2    Zhang, B.3    Nakagawa, Y.4    Lee, M.K.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 69
    • 1542267796 scopus 로고    scopus 로고
    • Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease
    • Lee, W.C., Yoshihara, M. and Littleton, J.T. (2004) Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease. Proc. Natl Acad. Sci. USA, 101, 3224-3229.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 3224-3229
    • Lee, W.C.1    Yoshihara, M.2    Littleton, J.T.3
  • 70
    • 33646136884 scopus 로고    scopus 로고
    • Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons
    • Chang, D.T., Rintoul, G.L., Pandipati, S. and Reynolds, I.J. (2006) Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons. Neurobiol. Dis., 22, 388-400.
    • (2006) Neurobiol. Dis , vol.22 , pp. 388-400
    • Chang, D.T.1    Rintoul, G.L.2    Pandipati, S.3    Reynolds, I.J.4
  • 73
    • 33846224191 scopus 로고    scopus 로고
    • Altered axonal mitochondrial transport in the pathogenesis of Charcot-Marie-Tooth disease from mitofusin 2 mutations
    • Baloh, R.H., Schmidt, R.E., Pestronk, A. and Milbrandt, J. (2007) Altered axonal mitochondrial transport in the pathogenesis of Charcot-Marie-Tooth disease from mitofusin 2 mutations. J. Neurosci., 27, 422-430.
    • (2007) J. Neurosci , vol.27 , pp. 422-430
    • Baloh, R.H.1    Schmidt, R.E.2    Pestronk, A.3    Milbrandt, J.4
  • 74
    • 0025438055 scopus 로고
    • Altered slowaxonal transport and regeneration in a myelin-deficient mutant mouse: the trembler as an in vivo model for Schwann cell-axon interactions
    • deWaegh, S. and Brady, S.T. (1990) Altered slowaxonal transport and regeneration in a myelin-deficient mutant mouse: the trembler as an in vivo model for Schwann cell-axon interactions. J. Neurosci., 10, 1855-1865.
    • (1990) J. Neurosci , vol.10 , pp. 1855-1865
    • deWaegh, S.1    Brady, S.T.2
  • 75
    • 39749165656 scopus 로고    scopus 로고
    • Differential regulation of dynein and kinesin motor proteins by tau
    • Dixit, R., Ross, J.L., Goldman, Y.E. and Holzbaur, E.L. (2008) Differential regulation of dynein and kinesin motor proteins by tau. Science, 319, 1086-1089.
    • (2008) Science , vol.319 , pp. 1086-1089
    • Dixit, R.1    Ross, J.L.2    Goldman, Y.E.3    Holzbaur, E.L.4
  • 76
    • 40449093880 scopus 로고    scopus 로고
    • Tau-induced traffic jams reflect organelles accumulation at points of microtubule polar mismatching
    • Shemesh, O.A., Erez, H., Ginzburg, I. and Spira, M.E. (2008) Tau-induced traffic jams reflect organelles accumulation at points of microtubule polar mismatching. Traffic, 9, 458-471.
    • (2008) Traffic , vol.9 , pp. 458-471
    • Shemesh, O.A.1    Erez, H.2    Ginzburg, I.3    Spira, M.E.4
  • 77
    • 16244410446 scopus 로고    scopus 로고
    • Four different subunits are essential for expressing the synaptic glutamate receptor at neuromuscular junctions of Drosophila
    • Qin, G., Schwarz, T., Kittel, R.J., Schmid, A., Rasse, T.M., Kappei, D., Ponimaskin, E., Heckmann, M. and Sigrist, S.J. (2005) Four different subunits are essential for expressing the synaptic glutamate receptor at neuromuscular junctions of Drosophila. J. Neurosci., 25, 3209-3218.
    • (2005) J. Neurosci , vol.25 , pp. 3209-3218
    • Qin, G.1    Schwarz, T.2    Kittel, R.J.3    Schmid, A.4    Rasse, T.M.5    Kappei, D.6    Ponimaskin, E.7    Heckmann, M.8    Sigrist, S.J.9
  • 78
    • 39149116364 scopus 로고    scopus 로고
    • Live imaging of synapse development and measuring protein dynamics using two-color fluorescence recovery after photo-bleaching at Drosophila synapses
    • Fuger, P., Behrends, L.B., Mertel, S., Sigrist, S.J. and Rasse, T.M. (2007) Live imaging of synapse development and measuring protein dynamics using two-color fluorescence recovery after photo-bleaching at Drosophila synapses. Nat. Protoc., 2, 3285-3298.
    • (2007) Nat. Protoc , vol.2 , pp. 3285-3298
    • Fuger, P.1    Behrends, L.B.2    Mertel, S.3    Sigrist, S.J.4    Rasse, T.M.5
  • 79
    • 80355142001 scopus 로고    scopus 로고
    • In vivo imaging of intact Drosophila larvae at sub-cellular resolution
    • Zhang, Y., Fuger, P., Hannan, S.B., Kern, J.V., Lasky, B. and Rasse, T.M. (2010) In vivo imaging of intact Drosophila larvae at sub-cellular resolution. J. Vis. Exp., 43, 2249.
    • (2010) J. Vis. Exp , vol.43 , pp. 2249
    • Zhang, Y.1    Fuger, P.2    Hannan, S.B.3    Kern, J.V.4    Lasky, B.5    Rasse, T.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.