메뉴 건너뛰기




Volumn 103, Issue 2, 2011, Pages 87-107

Dysregulation of axonal transport and motorneuron diseases

Author keywords

Axonal transport; Cell death; Dysregulation; Motorneuron disease; Neurodegenerative disease

Indexed keywords

ANGIOGENIN; DYNEIN ADENOSINE TRIPHOSPHATASE; HEAT SHOCK PROTEIN 60; KINESIN; TAR DNA BINDING PROTEIN;

EID: 78651499280     PISSN: 02484900     EISSN: 1768322X     Source Type: Journal    
DOI: 10.1042/BC20100093     Document Type: Review
Times cited : (32)

References (189)
  • 2
    • 27744494043 scopus 로고    scopus 로고
    • Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival
    • Allen, E., Ding, J., Wang,W., Pramanik, S., Chou, J., Yau, V. and Yang, Y. (2005) Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival. Nature 438, 224-228
    • (2005) Nature , vol.438 , pp. 224-228
    • Allen, E.1    Ding, J.2    Wang, W.3    Pramanik, S.4    Chou, J.5    Yau, V.6    Yang, Y.7
  • 4
    • 0036798495 scopus 로고    scopus 로고
    • Visualization of translated tau protein in the axons of neuronal P19 cells and characterization of tau RNP granules
    • Aronov, S., Aranda, G., Behar, L. and Ginzburg, I. (2002) Visualization of translated tau protein in the axons of neuronal P19 cells and characterization of tau RNP granules. J. Cell Sci. 115, 3817-3827
    • (2002) J. Cell Sci. , vol.115 , pp. 3817-3827
    • Aronov, S.1    Aranda, G.2    Behar, L.3    Ginzburg, I.4
  • 5
    • 33745373359 scopus 로고    scopus 로고
    • Autosomal recessive ataxia with peripheral neuropathy and elevated AFP: Novel mutations in SETX
    • Asaka, T., Yokoji, H., Ito, J., Yamaguchi, K. and Matsushima, A. (2006) Autosomal recessive ataxia with peripheral neuropathy and elevated AFP: novel mutations in SETX. Neurology 66, 1580-1581
    • (2006) Neurology , vol.66 , pp. 1580-1581
    • Asaka, T.1    Yokoji, H.2    Ito, J.3    Yamaguchi, K.4    Matsushima, A.5
  • 6
    • 0038744272 scopus 로고    scopus 로고
    • Mutations in MTMR13, a new pseudophosphatase homologue of MTMR2 and Sbf1, in two families with an autosomal recessive demyelinating form of Charcot-Marie-Tooth disease associated with early-onset glaucoma
    • Azzedine, H., Bolino, A., Taieb, T., Birouk, N., Di Duca, M., Bouhouche, A., Benamou, S., Mrabet, A., Hammadouche, T., Chkili, T. et al. (2003) Mutations in MTMR13, a new pseudophosphatase homologue of MTMR2 and Sbf1, in two families with an autosomal recessive demyelinating form of Charcot-Marie-Tooth disease associated with early-onset glaucoma. Am. J. Hum. Genet. 72, 1141-1153
    • (2003) Am. J. Hum. Genet. , vol.72 , pp. 1141-1153
    • Azzedine, H.1    Bolino, A.2    Taieb, T.3    Birouk, N.4    Di Duca, M.5    Bouhouche, A.6    Benamou, S.7    Mrabet, A.8    Hammadouche, T.9    Chkili, T.10
  • 7
    • 0033166528 scopus 로고    scopus 로고
    • Identification and characterization of AFG3L2, a novel paraplegin- Related gene
    • DOI 10.1006/geno.1999.5818
    • Banfi, S., Bassi, M.T., Andolfi, G., Marchitiello, A., Zanotta, S., Ballabio, A., Casari, G. and Franco, B. (1999) Identification and characterization of AFG3L2, a novel paraplegin-related gene. Genomics 59, 51-58 (Pubitemid 29339872)
    • (1999) Genomics , vol.59 , Issue.1 , pp. 51-58
    • Banfi, S.1    Bassi, M.T.2    Andolfi, G.3    Marchitiello, A.4    Zanotta, S.5    Ballabio, A.6    Casari, G.7    Franco, B.8
  • 10
    • 56749096054 scopus 로고    scopus 로고
    • Translational control of localized mRNAs: Restricting protein synthesis in space and time
    • Besse, F. and Ephrussi, A. (2008) Translational control of localized mRNAs: restricting protein synthesis in space and time. Nat. Rev. Mol. Cell Biol. 9, 971-980
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 971-980
    • Besse, F.1    Ephrussi, A.2
  • 11
    • 0041353619 scopus 로고    scopus 로고
    • Mouse kappa-opioid receptor mRNA differential transport in neurons
    • Bi, J., Hu, X., Loh, H.H. and Wei, L.N. (2003) Mouse kappa-opioid receptor mRNA differential transport in neurons. Mol. Pharmacol. 64, 594-599
    • (2003) Mol. Pharmacol. , vol.64 , pp. 594-599
    • Bi, J.1    Hu, X.2    Loh, H.H.3    Wei, L.N.4
  • 14
    • 0021808444 scopus 로고
    • A novel brain ATPase with properties expected for the fast axonal transport motor
    • *Brady, S.T. (1985) A novel brain ATPase with properties expected for the fast axonal transport motor. Nature 317, 73-75
    • (1985) Nature , vol.317 , pp. 73-75
    • Brady, S.T.1
  • 17
    • 38449102667 scopus 로고    scopus 로고
    • Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
    • Buratti, E. and Baralle, F.E. (2008) Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease. Front. Biosci. 13, 867-878
    • (2008) Front. Biosci. , vol.13 , pp. 867-878
    • Buratti, E.1    Baralle, F.E.2
  • 18
    • 38349014354 scopus 로고    scopus 로고
    • Dynamin 2 mediates fluid-phase micropinocytosis in epithelial cells
    • Cao, H., Chen, J., Awoniyi, M., Henley, J.R. and McNiven, M.A. (2007) Dynamin 2 mediates fluid-phase micropinocytosis in epithelial cells. J. Cell Sci. 120, 4167-4177
    • (2007) J. Cell Sci. , vol.120 , pp. 4167-4177
    • Cao, H.1    Chen, J.2    Awoniyi, M.3    Henley, J.R.4    McNiven, M.A.5
  • 20
    • 77951096150 scopus 로고    scopus 로고
    • Mitochondrial dynamics - Fusion, fission, movement, and mitophagy - in neurodegenerative diseases
    • *Chen, H. and Chan, D.C. (2009) Mitochondrial dynamics - fusion, fission, movement, and mitophagy - in neurodegenerative diseases. Hum. Mol. Genet. 18, R169-R176
    • (2009) Hum. Mol. Genet. , vol.18
    • Chen, H.1    Chan, D.C.2
  • 21
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen, H., Detmer, S.A., Ewald, A.J., Griffin, E.E., Fraser, S.E. and Chan, D.C. (2003) Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 160, 189-200
    • (2003) J. Cell Biol. , vol.160 , pp. 189-200
    • Chen, H.1    Detmer, S.A.2    Ewald, A.J.3    Griffin, E.E.4    Fraser, S.E.5    Chan, D.C.6
  • 23
    • 37549068958 scopus 로고    scopus 로고
    • Proprioceptive sensory neuropathy in mice with a mutation in the cytoplasmic Dynein heavy chain 1 gene
    • Chen, X.J., Levedakou, E.N., Millen, K.J., Wollmann, R.L., Soliven, B. and Popko, B. (2007) Proprioceptive sensory neuropathy in mice with a mutation in the cytoplasmic Dynein heavy chain 1 gene. J. Neurosci. 27, 14515-14524
    • (2007) J. Neurosci. , vol.27 , pp. 14515-14524
    • Chen, X.J.1    Levedakou, E.N.2    Millen, K.J.3    Wollmann, R.L.4    Soliven, B.5    Popko, B.6
  • 24
    • 33751020569 scopus 로고    scopus 로고
    • Axonal transport and neurodegenerative disease
    • *Chevalier-Larsen, E. and Holzbaur, E.L. (2006) Axonal transport and neurodegenerative disease. Biochim. Biophys. Acta 1762, 1094-1108
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 1094-1108
    • Chevalier-Larsen, E.1    Holzbaur, E.L.2
  • 26
    • 64549164076 scopus 로고    scopus 로고
    • Gigaxonin controls vimentin organization through a tubulin chaperone-independent pathway
    • Cleveland, D.W., Yamanaka, K. and Bomont, P. (2009) Gigaxonin controls vimentin organization through a tubulin chaperone-independent pathway. Hum. Mol. Genet. 18, 1384-1394
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 1384-1394
    • Cleveland, D.W.1    Yamanaka, K.2    Bomont, P.3
  • 28
    • 27644591304 scopus 로고    scopus 로고
    • Axon degeneration mechanisms: Commonality amid diversity
    • Coleman, M. (2005) Axon degeneration mechanisms: commonality amid diversity. Nat. Rev. Neurosci. 6, 889-898
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 889-898
    • Coleman, M.1
  • 30
    • 0036844683 scopus 로고    scopus 로고
    • Is the transportation highway the right road for hereditary spastic paraplegia?
    • Crosby, A.H. and Proukakis, C. (2002) Is the transportation highway the right road for hereditary spastic paraplegia? Am. J. Hum. Genet. 71, 1009-1016
    • (2002) Am. J. Hum. Genet. , vol.71 , pp. 1009-1016
    • Crosby, A.H.1    Proukakis, C.2
  • 34
    • 55749090654 scopus 로고    scopus 로고
    • The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila
    • Deng, H., Dodson, M.W., Huang, H. and Guo, M. (2008) The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc. Natl. Acad. Sci. U.S.A. 105, 14503-14508
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 14503-14508
    • Deng, H.1    Dodson, M.W.2    Huang, H.3    Guo, M.4
  • 35
    • 33646140347 scopus 로고    scopus 로고
    • Gene targeting of GAN in mouse causes a toxic accumulation of microtubule-associated protein 8 and impaired retrograde axonal transport
    • Ding, J., Allen, E., Wang, W., Valle, A., Wu, C., Nardine, T., Cui, B., Yi, J., Taylor, A., Jeon, N.L. et al. (2006) Gene targeting of GAN in mouse causes a toxic accumulation of microtubule-associated protein 8 and impaired retrograde axonal transport. Hum. Mol. Genet. 15, 1451-1463
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1451-1463
    • Ding, J.1    Allen, E.2    Wang, W.3    Valle, A.4    Wu, C.5    Nardine, T.6    Cui, B.7    Yi, J.8    Taylor, A.9    Jeon, N.L.10
  • 36
    • 74949142875 scopus 로고    scopus 로고
    • Collapsin response mediator protein 4a (CRMP4a) is upregulated in motoneurons of mutant SOD1 mice and can trigger motoneuron axonal degeneration and cell death
    • Duplan, L., Bernard, N., Casseron, W., Dudley, K., Thouvenot, E., Honnorat, J., Rogemond, V., De Bovis, B., Aebischer, P., Marin, P. et al. (2010) Collapsin response mediator protein 4a (CRMP4a) is upregulated in motoneurons of mutant SOD1 mice and can trigger motoneuron axonal degeneration and cell death. J. Neurosci. 30, 785-796
    • (2010) J. Neurosci. , vol.30 , pp. 785-796
    • Duplan, L.1    Bernard, N.2    Casseron, W.3    Dudley, K.4    Thouvenot, E.5    Honnorat, J.6    Rogemond, V.7    De Bovis, B.8    Aebischer, P.9    Marin, P.10
  • 37
    • 0014301112 scopus 로고
    • Lower motor and primary sensory neuron diseases with peroneal muscular atrophy. II. Neurologic, genetic, and electrophysiologic findings in various neuronal degenerations
    • Dyck, P.J. and Lambert, E.H. (1968) Lower motor and primary sensory neuron diseases with peroneal muscular atrophy. II. Neurologic, genetic, and electrophysiologic findings in various neuronal degenerations. Arch. Neurol. 18, 619-625
    • (1968) Arch. Neurol. , vol.18 , pp. 619-625
    • Dyck, P.J.1    Lambert, E.H.2
  • 41
    • 77952308995 scopus 로고    scopus 로고
    • A VAPB mutant linked to amyotrophic lateral sclerosis generates a novel form of organized smooth endoplasmic reticulum
    • Fasana, E., Fossati, M., Ruggiano, A., Brambillasca, S., Hoogenraad, C.C., Navone, F., Francolini, M. and Borgese, N. (2009) A VAPB mutant linked to amyotrophic lateral sclerosis generates a novel form of organized smooth endoplasmic reticulum. FASEB J. 24, 1419-1430
    • (2009) FASEB J. , vol.24 , pp. 1419-1430
    • Fasana, E.1    Fossati, M.2    Ruggiano, A.3    Brambillasca, S.4    Hoogenraad, C.C.5    Navone, F.6    Francolini, M.7    Borgese, N.8
  • 44
    • 0031922119 scopus 로고    scopus 로고
    • The ephrins and Eph receptors in neural development
    • Flanagan, J.G. and Vanderhaeghen, P. (1998) The ephrins and Eph receptors in neural development. Annu. Rev. Neurosci. 21, 309-345
    • (1998) Annu. Rev. Neurosci. , vol.21 , pp. 309-345
    • Flanagan, J.G.1    Vanderhaeghen, P.2
  • 45
    • 33845600705 scopus 로고    scopus 로고
    • Abnormal small heat shock protein interactions involving neuropathy-associated HSP22 (HSPB8) mutants
    • Fontaine, J.M., Sun, X., Hoppe, A.D., Simon, S., Vicart, P., Welsh, M.J. and Benndorf, R. (2006) Abnormal small heat shock protein interactions involving neuropathy-associated HSP22 (HSPB8) mutants. FASEB J. 20, 2168-2170
    • (2006) FASEB J. , vol.20 , pp. 2168-2170
    • Fontaine, J.M.1    Sun, X.2    Hoppe, A.D.3    Simon, S.4    Vicart, P.5    Welsh, M.J.6    Benndorf, R.7
  • 46
    • 0034209034 scopus 로고    scopus 로고
    • A functional role for VAP-33 in insulin-stimulated GLUT4 traffic
    • Foster, L.J., Weir, M.L., Lim, D.Y., Liu, Z., Trimble, W.S. and Klip, A. (2000) A functional role for VAP-33 in insulin-stimulated GLUT4 traffic. Traffic 1, 512-521
    • (2000) Traffic , vol.1 , pp. 512-521
    • Foster, L.J.1    Weir, M.L.2    Lim, D.Y.3    Liu, Z.4    Trimble, W.S.5    Klip, A.6
  • 47
    • 30544448358 scopus 로고    scopus 로고
    • TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines
    • Fujii, R. and Takumi, T. (2005) TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines. J. Cell Sci. 118, 5755-5765
    • (2005) J. Cell Sci. , vol.118 , pp. 5755-5765
    • Fujii, R.1    Takumi, T.2
  • 48
    • 44649129342 scopus 로고    scopus 로고
    • The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells
    • Gandre-Babbe, S. and van der Bliek, A.M. (2008) The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells. Mol. Biol. Cell 19, 2402-2412
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2402-2412
    • Gandre-Babbe, S.1    Van Der Bliek, A.M.2
  • 49
    • 47549106881 scopus 로고    scopus 로고
    • Mechanisms of action of angiogenin
    • Shanghai
    • Gao, X. and Xu, Z. (2008) Mechanisms of action of angiogenin. Acta Biochim. Biophys. Sin. (Shanghai) 40, 619-624
    • (2008) Acta Biochim. Biophys. Sin. , vol.40 , pp. 619-624
    • Gao, X.1    Xu, Z.2
  • 50
    • 38649105800 scopus 로고    scopus 로고
    • Identification of new ANG gene mutations in a large cohort of Italian patients with amyotrophic lateral sclerosis
    • Gellera, C., Colombrita, C., Ticozzi, N., Castellotti, B., Bragato, C., Ratti, A., Taroni, F. and Silani, V. (2008) Identification of new ANG gene mutations in a large cohort of Italian patients with amyotrophic lateral sclerosis. Neurogenetics 9, 33-40
    • (2008) Neurogenetics , vol.9 , pp. 33-40
    • Gellera, C.1    Colombrita, C.2    Ticozzi, N.3    Castellotti, B.4    Bragato, C.5    Ratti, A.6    Taroni, F.7    Silani, V.8
  • 52
    • 0141987864 scopus 로고    scopus 로고
    • Do disorders of movement cause movement disorders and dementia?
    • Goldstein, L.S. (2003) Do disorders of movement cause movement disorders and dementia? Neuron 40, 415-425
    • (2003) Neuron , vol.40 , pp. 415-425
    • Goldstein, L.S.1
  • 55
    • 0842269058 scopus 로고    scopus 로고
    • Cargo-carrying motor vehicles on the neuronal highway: Transport pathways and neurodegenerative disease
    • *Gunawardena, S. and Goldstein, L.S.B. (2004) Cargo-carrying motor vehicles on the neuronal highway: transport pathways and neurodegenerative disease. J. Neurobiol. 58, 258-271
    • (2004) J. Neurobiol. , vol.58 , pp. 258-271
    • Gunawardena, S.1    Goldstein, L.S.B.2
  • 60
    • 33746196575 scopus 로고    scopus 로고
    • MRNA transport in dendrites: RNA granules, motors, and tracks
    • Hirokawa, N. (2006) mRNA transport in dendrites: RNA granules, motors, and tracks. J. Neurosci. 26, 7139-7142
    • (2006) J. Neurosci. , vol.26 , pp. 7139-7142
    • Hirokawa, N.1
  • 61
    • 70450270783 scopus 로고    scopus 로고
    • The mechanisms of kinesin motor motility: Lessons from the monomeric motor KIF1A
    • Hirokawa, N., Nitta, R. and Okada, Y. (2009) The mechanisms of kinesin motor motility: lessons from the monomeric motor KIF1A. Nat. Rev. Mol. Cell Biol. 10, 877-884
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 877-884
    • Hirokawa, N.1    Nitta, R.2    Okada, Y.3
  • 62
    • 23044503665 scopus 로고    scopus 로고
    • Mitochondria and neurotransmission: Evacuating the synapse
    • Hollenbeck, P.J. (2005) Mitochondria and neurotransmission: evacuating the synapse. Neuron 47, 331-333
    • (2005) Neuron , vol.47 , pp. 331-333
    • Hollenbeck, P.J.1
  • 64
    • 0842290736 scopus 로고    scopus 로고
    • Axonal defects in mouse models of motoneuron disease
    • Jablonka, S., Wiese, S. and Sendtner, M. (2004) Axonal defects in mouse models of motoneuron disease. J. Neurobiol. 58, 272-286
    • (2004) J. Neurobiol. , vol.58 , pp. 272-286
    • Jablonka, S.1    Wiese, S.2    Sendtner, M.3
  • 66
    • 27744476574 scopus 로고    scopus 로고
    • The high and middle molecular weight neurofilament subunits regulate the association of neurofilaments with kinesin: Inhibition by phosphorylation of the high molecular weight subunit
    • Jung, C., Lee, S., Ortiz, D., Zhu, Q., Julien, J.P. and Shea, T.B. (2005) The high and middle molecular weight neurofilament subunits regulate the association of neurofilaments with kinesin: inhibition by phosphorylation of the high molecular weight subunit. Mol. Brain Res. 141, 151-155
    • (2005) Mol. Brain Res. , vol.141 , pp. 151-155
    • Jung, C.1    Lee, S.2    Ortiz, D.3    Zhu, Q.4    Julien, J.P.5    Shea, T.B.6
  • 67
    • 0036468983 scopus 로고    scopus 로고
    • Principles of cargo attachment to cytoplasmic motor proteins
    • Kamal, A. and Goldstein, L.S. (2002) Principles of cargo attachment to cytoplasmic motor proteins. Curr. Opin. Cell Biol. 14, 63-68
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 63-68
    • Kamal, A.1    Goldstein, L.S.2
  • 68
    • 4143088149 scopus 로고    scopus 로고
    • Kinesin transports RNA: Isolation and characterization of an RNA-transporting granule
    • *Kanai, Y., Dohmae, N. and Hirokawa, N. (2004) Kinesin transports RNA: isolation and characterization of an RNA-transporting granule. Neuron 43, 513-525
    • (2004) Neuron , vol.43 , pp. 513-525
    • Kanai, Y.1    Dohmae, N.2    Hirokawa, N.3
  • 69
    • 0038714285 scopus 로고    scopus 로고
    • Leuprorelin rescues polyglutamine-dependent phenotypes in a transgenic mouse model of spinal and bulbar muscular atrophy
    • Katsuno, M., Adachi, H., Doyu, M., Minamiyama, M., Sang, C., Kobayashi, Y., Inukai, A. and Sobue, G. (2003) Leuprorelin rescues polyglutamine-dependent phenotypes in a transgenic mouse model of spinal and bulbar muscular atrophy. Nat. Med. 9, 768-773
    • (2003) Nat. Med. , vol.9 , pp. 768-773
    • Katsuno, M.1    Adachi, H.2    Doyu, M.3    Minamiyama, M.4    Sang, C.5    Kobayashi, Y.6    Inukai, A.7    Sobue, G.8
  • 70
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Kawaguchi, Y., Kovacs, J.J., McLaurin, A., Vance, J.M., Ito, A. and Yao, T.P. (2003) The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 115, 727-738
    • (2003) Cell , vol.115 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.P.6
  • 71
    • 33748526877 scopus 로고    scopus 로고
    • Neuronal RNA granules: Movers and makers
    • *Kiebler, M.A. and Bassell, G.J. (2006) Neuronal RNA granules: movers and makers. Neuron 51, 685-690
    • (2006) Neuron , vol.51 , pp. 685-690
    • Kiebler, M.A.1    Bassell, G.J.2
  • 74
    • 77952107065 scopus 로고    scopus 로고
    • Occurrence of basophilic inclusions and FUS-immunoreactive neuronal and glial inclusions in a case of familial amyotrophic lateral sclerosis
    • Kobayashi, Z., Tsuchiya, K., Arai, T., Aoki, M., Hasegawa, M., Ishizu, H., Akiyama, H. and Mizusawa, H. (2010) Occurrence of basophilic inclusions and FUS-immunoreactive neuronal and glial inclusions in a case of familial amyotrophic lateral sclerosis. J. Neurol. Sci. 293, 6-11
    • (2010) J. Neurol. Sci. , vol.293 , pp. 6-11
    • Kobayashi, Z.1    Tsuchiya, K.2    Arai, T.3    Aoki, M.4    Hasegawa, M.5    Ishizu, H.6    Akiyama, H.7    Mizusawa, H.8
  • 76
    • 73949149584 scopus 로고    scopus 로고
    • RNA processing defects associated with diseases of the motor neuron
    • *Kolb, S.J., Sutton, S. and Schoenberg, D.R. (2010b) RNA processing defects associated with diseases of the motor neuron. Muscle Nerve 41, 5-17
    • (2010) Muscle Nerve , vol.41 , pp. 5-17
    • Kolb, S.J.1    Sutton, S.2    Schoenberg, D.R.3
  • 78
    • 0035923735 scopus 로고    scopus 로고
    • Neuronal RNA granules: A link between RNA localization and stimulation-dependent translation
    • *Krichevsky, A.M. and Kosik, K.S. (2001) Neuronal RNA granules: a link between RNA localization and stimulation-dependent translation. Neuron 32, 683-696
    • (2001) Neuron , vol.32 , pp. 683-696
    • Krichevsky, A.M.1    Kosik, K.S.2
  • 80
    • 0025800526 scopus 로고
    • Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy
    • *La Spada, A.R., Wilson, E.M., Lubahn, D.B., Harding, A.E. and Fischbeck, K.H. (1991) Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature 352, 77-79
    • (1991) Nature , vol.352 , pp. 77-79
    • La Spada, A.R.1    Wilson, E.M.2    Lubahn, D.B.3    Harding, A.E.4    Fischbeck, K.H.5
  • 81
    • 77956147372 scopus 로고    scopus 로고
    • Neurodegeneration: An expansion in ALS genetics
    • Lagier-Tourenne, C. and Cleveland, D.W. (2010) Neurodegeneration: an expansion in ALS genetics. Nature 466, 1052-1053
    • (2010) Nature , vol.466 , pp. 1052-1053
    • Lagier-Tourenne, C.1    Cleveland, D.W.2
  • 82
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: Emerging roles in RNA processing and neurodegeneration
    • *Lagier-Tourenne, C., Polymenidou, M. and Cleveland, D.W. (2010) TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum. Mol. Genet. 19, 46-64
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 46-64
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 86
    • 0242550967 scopus 로고    scopus 로고
    • Organization and translation of mRNA in sympathetic axons
    • *Lee, S.K. and Hollenbeck, P.J. (2003) Organization and translation of mRNA in sympathetic axons. J. Cell Sci. 116, 4467-4478
    • (2003) J. Cell Sci. , vol.116 , pp. 4467-4478
    • Lee, S.K.1    Hollenbeck, P.J.2
  • 89
    • 0034694152 scopus 로고    scopus 로고
    • Role of microtubules and actin filaments in the movement of mitochondria in the axons and dendrites of cultured hippocampal neurons
    • Ligon, L.A. and Steward, O. (2000) Role of microtubules and actin filaments in the movement of mitochondria in the axons and dendrites of cultured hippocampal neurons. J. Comp. Neurol. 427, 351-361
    • (2000) J. Comp. Neurol. , vol.427 , pp. 351-361
    • Ligon, L.A.1    Steward, O.2
  • 90
    • 2342640469 scopus 로고    scopus 로고
    • A direct interaction between cytoplasmic dynein and kinesin I may coordinate motor activity
    • Ligon, L.A., Tokito, M., Finklestein, J.M., Grossman, F.E. and Holzbaur, E.L. (2004) A direct interaction between cytoplasmic dynein and kinesin I may coordinate motor activity. J. Biol. Chem. 279, 19201-19208
    • (2004) J. Biol. Chem. , vol.279 , pp. 19201-19208
    • Ligon, L.A.1    Tokito, M.2    Finklestein, J.M.3    Grossman, F.E.4    Holzbaur, E.L.5
  • 91
    • 33748043331 scopus 로고    scopus 로고
    • The hereditary spastic paraplegia protein spartin localises to mitochondria
    • Lu, J., Rashid, F. and Byrne, P.C. (2006) The hereditary spastic paraplegia protein spartin localises to mitochondria. J. Neurochem. 98, 1908-1919
    • (2006) J. Neurochem. , vol.98 , pp. 1908-1919
    • Lu, J.1    Rashid, F.2    Byrne, P.C.3
  • 92
    • 66749104344 scopus 로고    scopus 로고
    • Mitochondrial function, morphology, and axonal transport in amyotrophic lateral sclerosis
    • *Magrane, J. and Manfredi, G. (2009) Mitochondrial function, morphology, and axonal transport in amyotrophic lateral sclerosis. Antioxid. Redox Signalling 11, 1615-1626
    • (2009) Antioxid. Redox Signalling , vol.11 , pp. 1615-1626
    • Magrane, J.1    Manfredi, G.2
  • 95
    • 0030711565 scopus 로고    scopus 로고
    • Hormonally induced neuronal plasticity in the adult motoneurons
    • Matsumoto, A. (1997) Hormonally induced neuronal plasticity in the adult motoneurons. Brain Res. Bull. 44, 539-547
    • (1997) Brain Res. Bull. , vol.44 , pp. 539-547
    • Matsumoto, A.1
  • 96
    • 15044358735 scopus 로고    scopus 로고
    • Dynamin in disease
    • *McNiven, M.A. (2005) Dynamin in disease. Nat. Genet. 37, 215-216
    • (2005) Nat. Genet. , vol.37 , pp. 215-216
    • McNiven, M.A.1
  • 97
    • 24344465919 scopus 로고    scopus 로고
    • Analysis of the kinesin superfamily: Insights into structure and function
    • *Miki, H., Okada, Y. and Hirokawa, N. (2005) Analysis of the kinesin superfamily: insights into structure and function. Trends Cell Biol. 15, 467-476
    • (2005) Trends Cell Biol. , vol.15 , pp. 467-476
    • Miki, H.1    Okada, Y.2    Hirokawa, N.3
  • 98
    • 3242875557 scopus 로고    scopus 로고
    • Axonal mitochondrial transport and potential are correlated
    • Miller, K.E. and Sheetz, M.P. (2004) Axonal mitochondrial transport and potential are correlated. J. Cell Sci. 117, 2791-2804
    • (2004) J. Cell Sci. , vol.117 , pp. 2791-2804
    • Miller, K.E.1    Sheetz, M.P.2
  • 100
    • 58049221032 scopus 로고    scopus 로고
    • Divergent patterns of cytosolic TDP-43 and neuronal progranulin expression following axotomy: Implications for TDP-43 in the physiological response to neuronal injury
    • Moisse, K., Volkening, K., Leystra-Lantz, C., Welch, I., Hill, T. and Strong, M.J. (2009) Divergent patterns of cytosolic TDP-43 and neuronal progranulin expression following axotomy: implications for TDP-43 in the physiological response to neuronal injury. Brain Res. 1249, 202-211
    • (2009) Brain Res. , vol.1249 , pp. 202-211
    • Moisse, K.1    Volkening, K.2    Leystra-Lantz, C.3    Welch, I.4    Hill, T.5    Strong, M.J.6
  • 101
    • 65249126818 scopus 로고    scopus 로고
    • Neurodegeneration mutations in dynactin impair dynein-dependent nuclear migration
    • Moore, J.K., Sept, D. and Cooper, J.A. (2009) Neurodegeneration mutations in dynactin impair dynein-dependent nuclear migration. Proc. Natl. Acad. Sci. U.S.A. 106, 5147-5152
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 5147-5152
    • Moore, J.K.1    Sept, D.2    Cooper, J.A.3
  • 102
    • 24644502657 scopus 로고    scopus 로고
    • From birth to death: The complex lives of eukaryotic mRNAs
    • Moore, M.J. (2005) From birth to death: the complex lives of eukaryotic mRNAs. Science 309, 1514-1518
    • (2005) Science , vol.309 , pp. 1514-1518
    • Moore, M.J.1
  • 103
    • 33745520772 scopus 로고    scopus 로고
    • JNK mediates pathogenic effects of polyglutamine-expanded androgen receptor on fast axonal transport
    • Morfini, G., Pigino, G., Szebenyi, G., You, Y., Pollema, S. and Brady, S.T. (2006) JNK mediates pathogenic effects of polyglutamine-expanded androgen receptor on fast axonal transport. Nat. Neurosci. 9, 907-916
    • (2006) Nat. Neurosci. , vol.9 , pp. 907-916
    • Morfini, G.1    Pigino, G.2    Szebenyi, G.3    You, Y.4    Pollema, S.5    Brady, S.T.6
  • 106
    • 0035839187 scopus 로고    scopus 로고
    • Impaired retrograde axonal transport of adenovirus-mediated E. coli LacZ gene in the mice carrying mutant SOD1 gene
    • Murakami, T., Nagano, I., Hayashi, T., Manabe, Y., Shoji, M., Setoguchi, Y. and Abe, K. (2001) Impaired retrograde axonal transport of adenovirus-mediated E. coli LacZ gene in the mice carrying mutant SOD1 gene. Neurosci. Lett. 308, 149-152
    • (2001) Neurosci. Lett. , vol.308 , pp. 149-152
    • Murakami, T.1    Nagano, I.2    Hayashi, T.3    Manabe, Y.4    Shoji, M.5    Setoguchi, Y.6    Abe, K.7
  • 108
    • 33745268197 scopus 로고    scopus 로고
    • Pathomechanisms of mutant proteins in Charcot-Marie-Tooth disease
    • Niemann, A., Berger, P. and Suter, U. (2006) Pathomechanisms of mutant proteins in Charcot-Marie-Tooth disease. Neuromol. Med. 8, 217-242
    • (2006) Neuromol. Med. , vol.8 , pp. 217-242
    • Niemann, A.1    Berger, P.2    Suter, U.3
  • 109
    • 25444514731 scopus 로고    scopus 로고
    • Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network: New implications for Charcot-Marie-Tooth disease
    • Niemann, A., Ruegg, M., La Padula, V., Schenone, A. and Suter, U. (2005) Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network: new implications for Charcot-Marie-Tooth disease. J. Cell. Biol. 170, 1067-1078
    • (2005) J. Cell. Biol. , vol.170 , pp. 1067-1078
    • Niemann, A.1    Ruegg, M.2    La Padula, V.3    Schenone, A.4    Suter, U.5
  • 112
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto, K. and Shaw, J.M. (2005) Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu. Rev. Genet. 39, 503-536
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 113
    • 0037223126 scopus 로고    scopus 로고
    • Dynamin at the actin-membrane interface
    • Orth, J.D. and McNiven, M.A. (2003) Dynamin at the actin-membrane interface. Curr. Opin. Cell Biol. 15, 31-39
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 31-39
    • Orth, J.D.1    McNiven, M.A.2
  • 117
    • 67649390851 scopus 로고    scopus 로고
    • Diagnosis, natural history, and management of Charcot-Marie-Tooth disease
    • *Pareyson, D. and Marchesi, C. (2009) Diagnosis, natural history, and management of Charcot-Marie-Tooth disease. Lancet Neurol. 8, 654-667
    • (2009) Lancet Neurol. , vol.8 , pp. 654-667
    • Pareyson, D.1    Marchesi, C.2
  • 118
  • 119
    • 77951172861 scopus 로고    scopus 로고
    • Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network
    • Park, S.H., Zhu, P.P., Parker, R.L. and Blackstone, C. (2010) Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network. J. Clin. Invest. 120, 1097-1110
    • (2010) J. Clin. Invest. , vol.120 , pp. 1097-1110
    • Park, S.H.1    Zhu, P.P.2    Parker, R.L.3    Blackstone, C.4
  • 120
    • 0023658669 scopus 로고
    • Isolated flagellar outer arm dynein translocates brain microtubules in vitro
    • Paschal, B.M., King, S.M., Moss, A.G., Collins, C.A., Vallee, R.B. and Witman, G.B. (1987) Isolated flagellar outer arm dynein translocates brain microtubules in vitro. Nature 330, 672-674
    • (1987) Nature , vol.330 , pp. 672-674
    • Paschal, B.M.1    King, S.M.2    Moss, A.G.3    Collins, C.A.4    Vallee, R.B.5    Witman, G.B.6
  • 121
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: Insights from genetics
    • Pasinelli, P. and Brown, R.H. (2006) Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat. Rev. Neurosci. 7, 710-723
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 123
    • 63149139630 scopus 로고    scopus 로고
    • Post-translational modifications of expanded polyglutamine proteins: Impact on neurotoxicity
    • Pennuto, M., Palazzolo, I. and Poletti, A. (2009) Post-translational modifications of expanded polyglutamine proteins: impact on neurotoxicity. Hum. Mol. Genet. 18, R40-R47
    • (2009) Hum. Mol. Genet. , vol.18
    • Pennuto, M.1    Palazzolo, I.2    Poletti, A.3
  • 125
    • 14644404885 scopus 로고    scopus 로고
    • Vimentin-dependent spatial translocation of an activated MAP kinase in injured nerve
    • Perlson, E., Hanz, S., Ben-Yaakov, K., Segal-Ruder, Y., Seger, R. and Fainzilber, M. (2005) Vimentin-dependent spatial translocation of an activated MAP kinase in injured nerve. Neuron 45, 715-726
    • (2005) Neuron , vol.45 , pp. 715-726
    • Perlson, E.1    Hanz, S.2    Ben-Yaakov, K.3    Segal-Ruder, Y.4    Seger, R.5    Fainzilber, M.6
  • 127
    • 70349482318 scopus 로고    scopus 로고
    • Neuronal intermediate filaments and neurodegenerative disorders
    • *Perrot, R. and Eyer, J. (2009) Neuronal intermediate filaments and neurodegenerative disorders. Brain Res. Bull. 80, 282-295
    • (2009) Brain Res. Bull. , vol.80 , pp. 282-295
    • Perrot, R.1    Eyer, J.2
  • 128
    • 0036716277 scopus 로고    scopus 로고
    • Androgen receptor with elongated polyglutamine tract forms aggregates that alter axonal trafficking and mitochondrial distribution in motor neuronal processes
    • *Piccioni, F., Pinton, P., Simeoni, S., Pozzi, P., Fascio, U., Vismara, G., Martini, L., Rizzuto, R. and Poletti, A. (2002) Androgen receptor with elongated polyglutamine tract forms aggregates that alter axonal trafficking and mitochondrial distribution in motor neuronal processes. FASEB J. 160, 1418-1420
    • (2002) FASEB J. , vol.160 , pp. 1418-1420
    • Piccioni, F.1    Pinton, P.2    Simeoni, S.3    Pozzi, P.4    Fascio, U.5    Vismara, G.6    Martini, L.7    Rizzuto, R.8    Poletti, A.9
  • 129
    • 2942588983 scopus 로고    scopus 로고
    • The polyglutamine tract of androgen receptor: From functions to dysfunctions in motor neurons
    • *Poletti, A. (2004) The polyglutamine tract of androgen receptor: from functions to dysfunctions in motor neurons. Front. Neuroendocrinol. 25, 1-26
    • (2004) Front. Neuroendocrinol. , vol.25 , pp. 1-26
    • Poletti, A.1
  • 132
    • 0142122897 scopus 로고    scopus 로고
    • NIPA1 gene mutations cause autosomal dominant hereditary spastic paraplegia (SPG6)
    • Rainier, S., Chai, J.H., Tokarz, D., Nicholls, R.D. and Fink, J.K. (2003) NIPA1 gene mutations cause autosomal dominant hereditary spastic paraplegia (SPG6). Am. J. Hum. Genet. 73, 967-971
    • (2003) Am. J. Hum. Genet. , vol.73 , pp. 967-971
    • Rainier, S.1    Chai, J.H.2    Tokarz, D.3    Nicholls, R.D.4    Fink, J.K.5
  • 133
    • 77950860161 scopus 로고    scopus 로고
    • Retrograde signaling in axonal regeneration
    • *Rishal, I. and Fainzilber, M. (2010) Retrograde signaling in axonal regeneration. Exp. Neurol. 223, 5-10
    • (2010) Exp. Neurol. , vol.223 , pp. 5-10
    • Rishal, I.1    Fainzilber, M.2
  • 136
    • 70249095607 scopus 로고    scopus 로고
    • Spinal muscular atrophy and a model for survival of motor neuron protein function in axonal ribonucleoprotein complexes
    • Rossoll, W. and Bassell, G.J. (2009) Spinal muscular atrophy and a model for survival of motor neuron protein function in axonal ribonucleoprotein complexes. Results Probl. Cell Differ. 48, 289-326
    • (2009) Results Probl. Cell Differ. , vol.48 , pp. 289-326
    • Rossoll, W.1    Bassell, G.J.2
  • 137
    • 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
  • 138
    • 0034666282 scopus 로고    scopus 로고
    • Neurofilaments are transported rapidly but intermittently in axons: Implications for slow axonal transport
    • Roy, S., Coffee, P., Smith, G., Liem, R.K., Brady, S.T. and Black, M.M. (2000) Neurofilaments are transported rapidly but intermittently in axons: implications for slow axonal transport. J. Neurosci. 20, 6849-6861
    • (2000) J. Neurosci. , vol.20 , pp. 6849-6861
    • Roy, S.1    Coffee, P.2    Smith, G.3    Liem, R.K.4    Brady, S.T.5    Black, M.M.6
  • 141
    • 35348827324 scopus 로고    scopus 로고
    • That which does not kill me makes me stronger: Adapting to chronic ER stress
    • Rutkowski, D.T. and Kaufman, R.J. (2007) That which does not kill me makes me stronger: adapting to chronic ER stress. Trends Biochem. Sci. 32, 469-476
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 469-476
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 143
    • 55549094109 scopus 로고    scopus 로고
    • Hereditary spastic paraplegia: Clinical features and pathogenetic mechanisms
    • Salinas, S., Proukakis, C., Crosby, A. and Warner, T.T. (2008) Hereditary spastic paraplegia: clinical features and pathogenetic mechanisms. Lancet Neurol. 7, 1127-1138
    • (2008) Lancet Neurol. , vol.7 , pp. 1127-1138
    • Salinas, S.1    Proukakis, C.2    Crosby, A.3    Warner, T.T.4
  • 144
    • 0030034385 scopus 로고    scopus 로고
    • Dendritic synapses of anterior horn neurons in amyotrophic lateral sclerosis: An ultrastructural study
    • DOI 10.1007/s004010050426
    • Sasaki, S. and Iwata, M. (1996) Dendritic synapses of anterior horn neurons in amyotrophic lateral sclerosis: an ultrastructural study. Acta Neuropathol. 91, 278-283 (Pubitemid 26042220)
    • (1996) Acta Neuropathologica , vol.91 , Issue.3 , pp. 278-283
    • Sasaki, S.1    Iwata, M.2
  • 145
    • 33846087291 scopus 로고    scopus 로고
    • Mitochondrial alterations in the spinal cord of patients with sporadic amyotrophic lateral sclerosis
    • Sasaki, S. and Iwata, M. (2007) Mitochondrial alterations in the spinal cord of patients with sporadic amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 66, 10-16
    • (2007) J. Neuropathol. Exp. Neurol. , vol.66 , pp. 10-16
    • Sasaki, S.1    Iwata, M.2
  • 149
    • 33846930562 scopus 로고    scopus 로고
    • Axonal-SMN (a-SMN), a protein isoform of the survival motor neuron gene, is specifically involved in axonogenesis
    • Setola, V., Terao, M., Locatelli, D., Bassanini, S., Garattini, E. and Battaglia, G. (2007) Axonal-SMN (a-SMN), a protein isoform of the survival motor neuron gene, is specifically involved in axonogenesis. Proc. Natl. Acad. Sci. U.S.A. 104, 1959-1964
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 1959-1964
    • Setola, V.1    Terao, M.2    Locatelli, D.3    Bassanini, S.4    Garattini, E.5    Battaglia, G.6
  • 151
    • 0034098057 scopus 로고    scopus 로고
    • Motoneuronal cell death is not correlated with aggregate formation of androgen receptors containing an elongated polyglutamine tract
    • Simeoni, S., Mancini, M.A., Stenoien, D.L., Marcelli, M., Weigel, N.L., Zanisi, M., Martini, L. and Poletti, A. (2000) Motoneuronal cell death is not correlated with aggregate formation of androgen receptors containing an elongated polyglutamine tract. Hum. Mol. Genet. 9, 133-144
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 133-144
    • Simeoni, S.1    Mancini, M.A.2    Stenoien, D.L.3    Marcelli, M.4    Weigel, N.L.5    Zanisi, M.6    Martini, L.7    Poletti, A.8
  • 152
    • 0033967492 scopus 로고    scopus 로고
    • Mouse VAP33 is associated with the endoplasmic reticulum and microtubules
    • Skehel, P.A., Fabian-Fine, R. and Kandel, E.R. (2000) Mouse VAP33 is associated with the endoplasmic reticulum and microtubules. Proc. Nat. Acad. Sci. U.S.A. 97, 1101-1106
    • (2000) Proc. Nat. Acad. Sci. U.S.A. , vol.97 , pp. 1101-1106
    • Skehel, P.A.1    Fabian-Fine, R.2    Kandel, E.R.3
  • 155
    • 71049166754 scopus 로고    scopus 로고
    • The evidence for altered RNA metabolism in amyotrophic lateral sclerosis (ALS)
    • Strong, M.J. (2010) The evidence for altered RNA metabolism in
    • (2010) J. Neurol. Sci. , vol.288 , pp. 1-12
    • Strong, M.J.1
  • 157
    • 37549019664 scopus 로고    scopus 로고
    • Human angiogenin is a neuroprotective factor and amyotrophic lateral sclerosis associated angiogenin variants affect neurite extension/pathfinding and survival of motor neurons
    • Subramanian, V., Crabtree, B. and Acharya, K.R. (2008) Human angiogenin is a neuroprotective factor and amyotrophic lateral sclerosis associated angiogenin variants affect neurite extension/pathfinding and survival of motor neurons. Hum. Mol. Genet. 17, 130-149
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 130-149
    • Subramanian, V.1    Crabtree, B.2    Acharya, K.R.3
  • 158
    • 58549088349 scopus 로고    scopus 로고
    • ALS-linked P56S-VAPB, an aggregated loss-of-function mutant of VAPB, predisposes motor neurons to ER stress-related death by inducing aggregation of co-expressed wild-type VAPB
    • Suzuki, H., Kanekura, K., Levine, T.P., Kohno, K., Olkkonen, V.M., Aiso, S. and Matsuoka, M. (2009) ALS-linked P56S-VAPB, an aggregated loss-of-function mutant of VAPB, predisposes motor neurons to ER stress-related death by inducing aggregation of co-expressed wild-type VAPB. J. Neurochem. 108, 973-985
    • (2009) J. Neurochem. , vol.108 , pp. 973-985
    • Suzuki, H.1    Kanekura, K.2    Levine, T.P.3    Kohno, K.4    Olkkonen, V.M.5    Aiso, S.6    Matsuoka, M.7
  • 160
    • 33845353014 scopus 로고    scopus 로고
    • A mutation of spastin is responsible for swellings and impairment of transport in a region of axon characterized by changes in microtubule composition
    • Tarrade, A., Fassier, C., Courageot, S., Charvin, D., Vitte, J., Peris, L., Thorel, A., Mouisel, E., Fonknechten, N., Roblot, N. et al. (2006) A mutation of spastin is responsible for swellings and impairment of transport in a region of axon characterized by changes in microtubule composition. Hum. Mol. Genet. 15, 3544-3558
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 3544-3558
    • Tarrade, A.1    Fassier, C.2    Courageot, S.3    Charvin, D.4    Vitte, J.5    Peris, L.6    Thorel, A.7    Mouisel, E.8    Fonknechten, N.9    Roblot, N.10
  • 162
    • 33744770333 scopus 로고    scopus 로고
    • Pharmacologic and genetic inhibition of hsp90-dependent trafficking reduces aggregation and promotes degradation of the expanded glutamine androgen receptor without stress protein induction
    • Thomas, M., Harrell, J.M., Morishima, Y., Peng, H.M., Pratt, W.B. and Lieberman, A.P. (2006) Pharmacologic and genetic inhibition of hsp90-dependent trafficking reduces aggregation and promotes degradation of the expanded glutamine androgen receptor without stress protein induction. Hum. Mol. Genet. 15, 1876-1883
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1876-1883
    • Thomas, M.1    Harrell, J.M.2    Morishima, Y.3    Peng, H.M.4    Pratt, W.B.5    Lieberman, A.P.6
  • 163
    • 2642536202 scopus 로고    scopus 로고
    • Alsin is a Rab5 and Rac1 guanine nucleotide exchange factor
    • Topp, J.D., Gray, N.W., Gerard, R.D. and Horazdovsky, B.F. (2004) Alsin is a Rab5 and Rac1 guanine nucleotide exchange factor. J. Biol. Chem. 279, 24612-24623
    • (2004) J. Biol. Chem. , vol.279 , pp. 24612-24623
    • Topp, J.D.1    Gray, N.W.2    Gerard, R.D.3    Horazdovsky, B.F.4
  • 165
    • 43449099127 scopus 로고    scopus 로고
    • The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors
    • Tsuda, H., Han, S.M., Yang, Y., Tong, C., Lin, Y.Q., Mohan, K., Haueter, C., Zoghbi, A., Harati, Y., Kwan, J. et al. (2008) The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors. Cell 133, 963-977
    • (2008) Cell , vol.133 , pp. 963-977
    • Tsuda, H.1    Han, S.M.2    Yang, Y.3    Tong, C.4    Lin, Y.Q.5    Mohan, K.6    Haueter, C.7    Zoghbi, A.8    Harati, Y.9    Kwan, J.10
  • 166
    • 77951298381 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis mutant vesicle-associated membrane protein-associated protein-B transgenic mice develop TAR-DNA-binding protein-43 pathology
    • Tudor, E.L., Galtrey, C.M., Perkinton, M.S., Lau, K.F., De Vos, K.J., Mitchell, J.C., Ackerley, S., Hortobagyi, T., Vamos, E., Leigh, P.N. et al. (2010) Amyotrophic lateral sclerosis mutant vesicle-associated membrane protein-associated protein-B transgenic mice develop TAR-DNA-binding protein-43 pathology. Neuroscience 167, 774-785
    • (2010) Neuroscience , vol.167 , pp. 774-785
    • Tudor, E.L.1    Galtrey, C.M.2    Perkinton, M.S.3    Lau, K.F.4    De Vos, K.J.5    Mitchell, J.C.6    Ackerley, S.7    Hortobagyi, T.8    Vamos, E.9    Leigh, P.N.10
  • 168
    • 61649101716 scopus 로고    scopus 로고
    • The proportion of mutations predicted to have a deleterious effect differs between gain and loss of function genes in neurodegenerative disease
    • Valdmanis, P.N., Verlaan, D.J. and Rouleau, G.A. (2009) The proportion of mutations predicted to have a deleterious effect differs between gain and loss of function genes in neurodegenerative disease. Hum. Mutat. 30, E481-E489
    • (2009) Hum. Mutat. , vol.30
    • Valdmanis, P.N.1    Verlaan, D.J.2    Rouleau, G.A.3
  • 169
    • 0021910658 scopus 로고
    • Movement of organelles along filaments dissociated from the axoplasm of the squid giant axon
    • Vale, R.D., Schnapp, B.J., Reese, T.S. and Sheetz, M.P. (1985) Movement of organelles along filaments dissociated from the axoplasm of the squid giant axon. Cell 40, 449-454
    • (1985) Cell , vol.40 , pp. 449-454
    • Vale, R.D.1    Schnapp, B.J.2    Reese, T.S.3    Sheetz, M.P.4
  • 172
    • 22744447453 scopus 로고    scopus 로고
    • Rab7 associates with early endosomes to mediate sorting and transport of Semliki forest virus to late endosomes
    • Vonderheit, A. and Helenius, A. (2005) Rab7 associates with early endosomes to mediate sorting and transport of Semliki forest virus to late endosomes. PLoS Biol. 3, e233
    • (2005) PLoS Biol. , vol.3
    • Vonderheit, A.1    Helenius, A.2
  • 173
    • 42449163952 scopus 로고    scopus 로고
    • TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor
    • Wang, I.F., Wu, L.S., Chang, H.Y. and Shen, C.K. (2008) TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor. J. Neurochem. 105, 797-806
    • (2008) J. Neurochem. , vol.105 , pp. 797-806
    • Wang, I.F.1    Wu, L.S.2    Chang, H.Y.3    Shen, C.K.4
  • 174
    • 27844560722 scopus 로고    scopus 로고
    • Gigaxonin interacts with tubulin folding cofactor B and controls its degradation through the ubiquitin-proteasome pathway
    • Wang, W., Ding, J., Allen, E., Zhu, P., Zhang, L., Vogel, H. and Yang, Y. (2005) Gigaxonin interacts with tubulin folding cofactor B and controls its degradation through the ubiquitin-proteasome pathway. Curr. Biol. 15, 2050-2055
    • (2005) Curr. Biol. , vol.15 , pp. 2050-2055
    • Wang, W.1    Ding, J.2    Allen, E.3    Zhu, P.4    Zhang, L.5    Vogel, H.6    Yang, Y.7
  • 177
    • 77951848688 scopus 로고    scopus 로고
    • Regulation of protein levels in subcellular domains through mRNA transport and localized translation
    • Willis, D.E. and Twiss, J.L. (2010) Regulation of protein levels in subcellular domains through mRNA transport and localized translation. Mol. Cell. Proteom. 9, 952-962
    • (2010) Mol. Cell. Proteom. , vol.9 , pp. 952-962
    • Willis, D.E.1    Twiss, J.L.2
  • 178
    • 0036899518 scopus 로고    scopus 로고
    • PTEN and myotubularin phosphatases: From 3-phosphoinositide dephosphorylation to disease
    • Wishart, M.J. and Dixon, J.E. (2002) PTEN and myotubularin phosphatases: from 3-phosphoinositide dephosphorylation to disease. Trends Cell Biol. 12, 579-585
    • (2002) Trends Cell Biol. , vol.12 , pp. 579-585
    • Wishart, M.J.1    Dixon, J.E.2
  • 179
    • 0034785509 scopus 로고    scopus 로고
    • The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis
    • Yang, Y., Hentati, A., Deng, H.X., Dabbagh, O., Sasaki, T., Hirano, M., Hung, W.Y., Ouahchi, K., Yan, J., Azim, A.C. et al. (2001) The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis. Nat. Genet. 29, 160-165
    • (2001) Nat. Genet. , vol.29 , pp. 160-165
    • Yang, Y.1    Hentati, A.2    Deng, H.X.3    Dabbagh, O.4    Sasaki, T.5    Hirano, M.6    Hung, W.Y.7    Ouahchi, K.8    Yan, J.9    Azim, A.C.10
  • 180
  • 181
    • 30344458745 scopus 로고    scopus 로고
    • Abnormalities of germ cell maturation and sertoli cell cytoskeleton in androgen receptor 113 CAG knock-in mice reveal toxic effects of the mutant protein
    • Yu, Z., Dadgar, N., Albertelli, M., Scheller, A., Albin, R.L., Robins, D.M. and Lieberman, A.P. (2006) Abnormalities of germ cell maturation and sertoli cell cytoskeleton in androgen receptor 113 CAG knock-in mice reveal toxic effects of the mutant protein. Am. J. Pathol. 168, 195-204
    • (2006) Am. J. Pathol. , vol.168 , pp. 195-204
    • Yu, Z.1    Dadgar, N.2    Albertelli, M.3    Scheller, A.4    Albin, R.L.5    Robins, D.M.6    Lieberman, A.P.7
  • 182
    • 66149101014 scopus 로고    scopus 로고
    • Ran on tracks - Cytoplasmic roles for a nuclear regulator
    • Yudin, D. and Fainzilber, M. (2009) Ran on tracks - cytoplasmic roles for a nuclear regulator. J. Cell Sci. 122, 587-593
    • (2009) J. Cell Sci. , vol.122 , pp. 587-593
    • Yudin, D.1    Fainzilber, M.2
  • 183
    • 34447550238 scopus 로고    scopus 로고
    • Interaction between familial amyotrophic lateral sclerosis (ALS)-linked SOD1 mutants and the dynein complex
    • Zhang, F., Strom, A.-L., Fukada, K., Lee, S., Hayward, L.J. and Zhu, H. (2007) Interaction between familial amyotrophic lateral sclerosis (ALS)-linked SOD1 mutants and the dynein complex. J. Biol. Chem. 282, 16691-16699
    • (2007) J. Biol. Chem. , vol.282 , pp. 16691-16699
    • Zhang, F.1    Strom, A.-L.2    Fukada, K.3    Lee, S.4    Hayward, L.J.5    Zhu, H.6
  • 184
    • 0035797518 scopus 로고    scopus 로고
    • Neurotrophin-induced transport of a beta-actin mRNP complex increases beta-actin levels and stimulates growth cone motility
    • Zhang, H.L., Eom, T., Oleynikov, Y., Shenoy, S.M., Liebelt, D.A., Dictenberg, J.B., Singer, R.H. and Bassell, G.J. (2001) Neurotrophin-induced transport of a beta-actin mRNP complex increases beta-actin levels and stimulates growth cone motility. Neuron 31, 261-275
    • (2001) Neuron , vol.31 , pp. 261-275
    • Zhang, H.L.1    Eom, T.2    Oleynikov, Y.3    Shenoy, S.M.4    Liebelt, D.A.5    Dictenberg, J.B.6    Singer, R.H.7    Bassell, G.J.8
  • 185
    • 0042202619 scopus 로고    scopus 로고
    • Active transport of the survival motor neuron protein and the role of exon-7 in cytoplasmic localization
    • Zhang, H.L., Pan, F., Hong, D., Shenoy, S.M., Singer, R.H. and Bassell, G.J. (2003) Active transport of the survival motor neuron protein and the role of exon-7 in cytoplasmic localization. J. Neurosci. 23, 6627-6637
    • (2003) J. Neurosci. , vol.23 , pp. 6627-6637
    • Zhang, H.L.1    Pan, F.2    Hong, D.3    Shenoy, S.M.4    Singer, R.H.5    Bassell, G.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.