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Volumn 166, Issue 5, 2005, Pages 1499-1514

Fragmentation of the Golgi apparatus induced by the overexpression of wild-type and mutant human tau forms in neurons

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; MUTANT PROTEIN; TAU PROTEIN;

EID: 17844387375     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0002-9440(10)62366-8     Document Type: Article
Times cited : (59)

References (80)
  • 1
    • 0026309310 scopus 로고
    • Tau protein and the establishment of an axonal morphology
    • Kosik KS. Caceres A: Tau protein and the establishment of an axonal morphology. J Cell Sci Suppl 1991, 15:69-74
    • (1991) J Cell Sci Suppl , vol.15 , pp. 69-74
    • Kosik, K.S.1    Caceres, A.2
  • 2
    • 0024498630 scopus 로고
    • Structure of the bovine tau gene: Alternatively spliced transcripts generate a protein family
    • Himmler A: Structure of the bovine tau gene: alternatively spliced transcripts generate a protein family. Mol Cell Biol 1989, 9:1389-1396
    • (1989) Mol Cell Biol , vol.9 , pp. 1389-1396
    • Himmler, A.1
  • 3
    • 0024387161 scopus 로고
    • Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain
    • Goedert M, Spillantini MG, Potier MC, Ulrich J, Crowther RA: Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain. EMBO J 1989, 8:393-399
    • (1989) EMBO J , vol.8 , pp. 393-399
    • Goedert, M.1    Spillantini, M.G.2    Potier, M.C.3    Ulrich, J.4    Crowther, R.A.5
  • 5
    • 0037010285 scopus 로고    scopus 로고
    • Alzheimer's disease: Beta-amyloid protein and tau
    • Morishima-Kawashima M, Ihara Y: Alzheimer's disease: beta-amyloid protein and tau. J Neurosci Res 2002, 70:392-401
    • (2002) J Neurosci Res , vol.70 , pp. 392-401
    • Morishima-Kawashima, M.1    Ihara, Y.2
  • 7
    • 0036892302 scopus 로고    scopus 로고
    • Tau gene mutations: Dissecting the pathogenesis of FTDP-17
    • Ingram EM, Spillantini MG: Tau gene mutations: dissecting the pathogenesis of FTDP-17. Trends Mol Med 2002, 8:555-562
    • (2002) Trends Mol Med , vol.8 , pp. 555-562
    • Ingram, E.M.1    Spillantini, M.G.2
  • 9
    • 0035808361 scopus 로고    scopus 로고
    • Tau filament formation in transgenic mice expressing P301L tau
    • Gotz J, Chen F, Barmettler R, Nitsch RM: Tau filament formation in transgenic mice expressing P301L tau. J Biol Chem 2001, 276:529-534
    • (2001) J Biol Chem , vol.276 , pp. 529-534
    • Gotz, J.1    Chen, F.2    Barmettler, R.3    Nitsch, R.M.4
  • 12
    • 0345276565 scopus 로고    scopus 로고
    • Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses
    • Mandelkow EM, Stamer K, Vogel R, Thies E, Mandelkow E: Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses. Neurobiol Aging 2003, 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
  • 13
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Aizheimer's disease
    • Ebneth A, Godemann R, Stamer K, Illenberger S, Trinczek B, Mandelkow E: Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Aizheimer's disease. J Cell Biol 1998, 143:777-794
    • (1998) J Cell Biol , vol.143 , pp. 777-794
    • Ebneth, A.1    Godemann, R.2    Stamer, K.3    Illenberger, S.4    Trinczek, B.5    Mandelkow, E.6
  • 14
    • 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: Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J Cell Biol 2002, 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
  • 15
    • 0037119947 scopus 로고    scopus 로고
    • Single-molecule investigation of the interference between kinesin, tau and MAP2c
    • Seitz A, Kojima H, Oiwa K, Mandelkow EM, Song YH, Mandelkow E: Single-molecule investigation of the interference between kinesin, tau and MAP2c. EMBO J 2002, 21:4896-4905
    • (2002) EMBO J , vol.21 , pp. 4896-4905
    • Seitz, A.1    Kojima, H.2    Oiwa, K.3    Mandelkow, E.M.4    Song, Y.H.5    Mandelkow, E.6
  • 16
    • 0028989895 scopus 로고
    • Neurons bearing neurofibrillary tangles are responsible for selected synaptic deficits in Alzheimer's disease
    • Callahan LM, Coleman PD: Neurons bearing neurofibrillary tangles are responsible for selected synaptic deficits in Alzheimer's disease. Neurobiol Aging 1995, 16:311-314
    • (1995) Neurobiol Aging , vol.16 , pp. 311-314
    • Callahan, L.M.1    Coleman, P.D.2
  • 17
    • 0030043292 scopus 로고    scopus 로고
    • In Alzheimer's disease the Golgi apparatus of a population of neurons without neurofibrillary tangles is fragmented and atrophic
    • Stieber A, Mourelatos Z, Gonatas NK: In Alzheimer's disease the Golgi apparatus of a population of neurons without neurofibrillary tangles is fragmented and atrophic. Am J Pathol 1996, 148:415-426
    • (1996) Am J Pathol , vol.148 , pp. 415-426
    • Stieber, A.1    Mourelatos, Z.2    Gonatas, N.K.3
  • 19
    • 0031837890 scopus 로고    scopus 로고
    • The involvement of the Golgi apparatus in the pathogenesis of amyotrophic lateral sclerosis, Alzheimer's disease, and ricin intoxication
    • Gonatas NK, Gonatas JO, Stieber A: The involvement of the Golgi apparatus in the pathogenesis of amyotrophic lateral sclerosis, Alzheimer's disease, and ricin intoxication. Histochem Cell Biol 1998, 109:591-600
    • (1998) Histochem Cell Biol , vol.109 , pp. 591-600
    • Gonatas, N.K.1    Gonatas, J.O.2    Stieber, A.3
  • 21
    • 0033939401 scopus 로고    scopus 로고
    • Fragmentation of the Golgi apparatus of the ballooned neurons in patients with corticobasal degeneration and Creutzfeldt-Jakob disease
    • Sakurai A, Okamoto K, Fujita Y, Nakazato Y. Wakabayashi K, Takahashi H, Gonalas NK: Fragmentation of the Golgi apparatus of the ballooned neurons in patients with corticobasal degeneration and Creutzfeldt-Jakob disease, Acta Neuropathol 2000, 100:270-274
    • (2000) Acta Neuropathol , vol.100 , pp. 270-274
    • Sakurai, A.1    Okamoto, K.2    Fujita, Y.3    Nakazato, Y.4    Wakabayashi, K.5    Takahashi, H.6    Gonalas, N.K.7
  • 23
    • 0028950267 scopus 로고
    • Organization of organelles and membrane traffic by microtubules
    • Cole NB, Lippincott-Schwartz J: Organization of organelles and membrane traffic by microtubules. Curr Opin Cell Biol 1995, 1:55-64
    • (1995) Curr Opin Cell Biol , vol.1 , pp. 55-64
    • Cole, N.B.1    Lippincott-Schwartz, J.2
  • 25
    • 0023441953 scopus 로고
    • Fragmentation and partitioning of the Golgi apparatus during mitosis in HeLa cells
    • Lucocq JM, Warren G: Fragmentation and partitioning of the Golgi apparatus during mitosis in HeLa cells. EMBO J 1987, 6:3239-3246
    • (1987) EMBO J , vol.6 , pp. 3239-3246
    • Lucocq, J.M.1    Warren, G.2
  • 26
    • 0037175389 scopus 로고    scopus 로고
    • A caspase cleavage fragment of p115 induces fragmentation of the Golgi apparatus and apoptosis
    • Chiu R, Novikov L, Mukherjee S, Shields D: A caspase cleavage fragment of p115 induces fragmentation of the Golgi apparatus and apoptosis. J Cell Biol 2002, 159:637-648
    • (2002) J Cell Biol , vol.159 , pp. 637-648
    • Chiu, R.1    Novikov, L.2    Mukherjee, S.3    Shields, D.4
  • 29
    • 0029823784 scopus 로고    scopus 로고
    • Okadaic acid disrupts Golgi structure and impairs enzyme synthesis and secretion in the rat pancreas
    • Waschulewski IH, Kruse ML, Agricola B. Kern HF, Schmidt WE: Okadaic acid disrupts Golgi structure and impairs enzyme synthesis and secretion in the rat pancreas Am J Physiol 1996, 270:G939-G947
    • (1996) Am J Physiol , vol.270
    • Waschulewski, I.H.1    Kruse, M.L.2    Agricola, B.3    Kern, H.F.4    Schmidt, W.E.5
  • 30
    • 0029972823 scopus 로고    scopus 로고
    • Golgi dispersal during microtubule disruption: Regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites
    • Cole NB, Sciaky N, Marotta A: Song J, Lippincott-Schwartz J: Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites. Mol Biol Cell 1996, 7:631-650
    • (1996) Mol Biol Cell , vol.7 , pp. 631-650
    • Cole, N.B.1    Sciaky, N.2    Marotta, A.3    Song, J.4    Lippincott-Schwartz, J.5
  • 31
    • 0020034982 scopus 로고
    • Microtubules and beta cell function: Effect of colchicine on microtubules and insulin secretion in vitro by mouse beta cells
    • Boyd AE, Bolton WE, Brinkley BR: Microtubules and beta cell function: effect of colchicine on microtubules and insulin secretion in vitro by mouse beta cells. J Cell Biol 1982, 92:425-434
    • (1982) J Cell Biol , vol.92 , pp. 425-434
    • Boyd, A.E.1    Bolton, W.E.2    Brinkley, B.R.3
  • 32
    • 0021189557 scopus 로고
    • Effect of microtubule assembly status on the intracellular processing and surface expression of an integral protein of the plasma membrane
    • Rogalski AA, Bergmann JE, Singer SJ: Effect of microtubule assembly status on the intracellular processing and surface expression of an integral protein of the plasma membrane. J Cell Biol 1984, 99:1101-1109
    • (1984) J Cell Biol , vol.99 , pp. 1101-1109
    • Rogalski, A.A.1    Bergmann, J.E.2    Singer, S.J.3
  • 33
    • 0031887308 scopus 로고    scopus 로고
    • The fragmented neuronal Golgi apparatus in amyotrophic lateral sclerosis includes the trans-Golgi-network: Functional implications
    • Stieber A, Chen Y, Wei S, Mourelatos Z, Gonatas J, Okamoto K, Gonatas NK: The fragmented neuronal Golgi apparatus in amyotrophic lateral sclerosis includes the trans-Golgi-network: functional implications. Acta Neuropathol (Berl) 1998, 95:245-253
    • (1998) Acta Neuropathol (Berl) , vol.95 , pp. 245-253
    • Stieber, A.1    Chen, Y.2    Wei, S.3    Mourelatos, Z.4    Gonatas, J.5    Okamoto, K.6    Gonatas, N.K.7
  • 34
    • 0344874553 scopus 로고    scopus 로고
    • Reduction of detyrosinated microtubules and Golgi fragmentation are linked to tau-induced degeneration in astrocytes
    • Yoshiyama Y, Zhang B, Bruce J, Trojanowski JQ, Lee VM: Reduction of detyrosinated microtubules and Golgi fragmentation are linked to tau-induced degeneration in astrocytes. J Neurosci 2003, 23:10662-10671
    • (2003) J Neurosci , vol.23 , pp. 10662-10671
    • Yoshiyama, Y.1    Zhang, B.2    Bruce, J.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 36
    • 0035939659 scopus 로고    scopus 로고
    • Regulation of presynaptic phosphatidylinositol 4,5-biphosphate by neuronal activity
    • Micheva KD, Holz RW, Smith SJ: Regulation of presynaptic phosphatidylinositol 4,5-biphosphate by neuronal activity. J Cell Biol 2001, 154:355-368
    • (2001) J Cell Biol , vol.154 , pp. 355-368
    • Micheva, K.D.1    Holz, R.W.2    Smith, S.J.3
  • 37
    • 0035181835 scopus 로고    scopus 로고
    • Competition for microtubule-binding with dual expression of tau missense and splice isoforms
    • Lu M, Kosik KS: Competition for microtubule-binding with dual expression of tau missense and splice isoforms. Mol Biol Cell 2001, 12:171-184
    • (2001) Mol Biol Cell , vol.12 , pp. 171-184
    • Lu, M.1    Kosik, K.S.2
  • 38
    • 0029835019 scopus 로고    scopus 로고
    • A spatial gradient of tau protein phosphorylation in nascent axons
    • Mandell JW, Banker GA: A spatial gradient of tau protein phosphorylation in nascent axons. J Neurosci 1996, 16:5727-5740
    • (1996) J Neurosci , vol.16 , pp. 5727-5740
    • Mandell, J.W.1    Banker, G.A.2
  • 39
    • 0036538023 scopus 로고    scopus 로고
    • The projection domain of MAP2b regulates microtubule protrusion and process formation in Sf9 cells
    • Belanger D, Farah CA, Nguyen MD, Lauzon M, Cornibert S, Ledere N: The projection domain of MAP2b regulates microtubule protrusion and process formation in Sf9 cells. J Cell Sci 2002, 115:1523-1539
    • (2002) J Cell Sci , vol.115 , pp. 1523-1539
    • Belanger, D.1    Farah, C.A.2    Nguyen, M.D.3    Lauzon, M.4    Cornibert, S.5    Ledere, N.6
  • 40
    • 0023905661 scopus 로고
    • The establishment of polarity by hippocampal neurons in culture
    • Dotti CG, Sullivan CA, Banker GA: The establishment of polarity by hippocampal neurons in culture. J Neurosci 1988, 8:1454-1468
    • (1988) J Neurosci , vol.8 , pp. 1454-1468
    • Dotti, C.G.1    Sullivan, C.A.2    Banker, G.A.3
  • 41
    • 0021629684 scopus 로고
    • An electron microscopic study of the development of axons and dendrites by hippocampal neurons in culture. I. Cells which develop without intercellular contacts
    • Bartlett WP, Banker GA: An electron microscopic study of the development of axons and dendrites by hippocampal neurons in culture. I. Cells which develop without intercellular contacts. J Neurosci 1984, 4:1944-1953
    • (1984) J Neurosci , vol.4 , pp. 1944-1953
    • Bartlett, W.P.1    Banker, G.A.2
  • 42
    • 0023627237 scopus 로고
    • The expression and distribution of the microtubule-associated proteins tau and microtubule-associated protein 2 in hippocampal neurons in the rat in situ and in cell culture
    • Dotti CG, Banker GA, Binder Ll: The expression and distribution of the microtubule-associated proteins tau and microtubule-associated protein 2 in hippocampal neurons in the rat in situ and in cell culture. Neuroscience 1987, 23:121-130
    • (1987) Neuroscience , vol.23 , pp. 121-130
    • Dotti, C.G.1    Banker, G.A.2    Binder, L.I.3
  • 43
    • 0029812945 scopus 로고    scopus 로고
    • Tau binds to the distal axon early in development of polarity in a microtubule-and microfilament-dependent manner
    • Kempf M, Clement A, Faissner A, Lee G, Brandt R: Tau binds to the distal axon early in development of polarity in a microtubule-and microfilament- dependent manner. J Neurosci 1996, 16: 5583-5592
    • (1996) J Neurosci , vol.16 , pp. 5583-5592
    • Kempf, M.1    Clement, A.2    Faissner, A.3    Lee, G.4    Brandt, R.5
  • 44
    • 0028167602 scopus 로고
    • Polarized distribution of the trans-Golgi network marker TGN38 during the in vitro development of neocortical neurons: Effects of nocodazole and brefeldin A
    • Lowenstein PR, Morrison EE, Bain D, Shering AF, Banting G, Douglas P, Castro MG: Polarized distribution of the trans-Golgi network marker TGN38 during the in vitro development of neocortical neurons: effects of nocodazole and brefeldin A. Eur J Neurosci 1994, 6:1453-1465
    • (1994) Eur J Neurosci , vol.6 , pp. 1453-1465
    • Lowenstein, P.R.1    Morrison, E.E.2    Bain, D.3    Shering, A.F.4    Banting, G.5    Douglas, P.6    Castro, M.G.7
  • 45
    • 0035254160 scopus 로고    scopus 로고
    • Mutated tau binds less avidly to microtubules than wildtype tau in living cells
    • Naglec EW, Sampson KE, Abraham I: Mutated tau binds less avidly to microtubules than wildtype tau in living cells. J Neurosci Res 2001, 63:268-275
    • (2001) J Neurosci Res , vol.63 , pp. 268-275
    • Naglec, E.W.1    Sampson, K.E.2    Abraham, I.3
  • 46
    • 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, Mutton M. Yen SH: Accelerated filament formation from tau protein with specific FTDP-17 missense mutations. FEBS Lett 1999, 447:195-1999
    • (1999) FEBS Lett , vol.447 , pp. 195-1999
    • Nacharaju, P.1    Lewis, J.2    Easson, C.3    Yen, S.4    Hackett, J.5    Mutton, M.6    Yen, S.H.7
  • 48
    • 0028593606 scopus 로고
    • Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404
    • Otvos Jr L, Feiner L, Lang E, Szendrei GI, Goedert M, Lee VM: Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404. J Neurosci Res 1994, 39:669-673
    • (1994) J Neurosci Res , vol.39 , pp. 669-673
    • Otvos Jr., L.1    Feiner, L.2    Lang, E.3    Szendrei, G.I.4    Goedert, M.5    Lee, V.M.6
  • 50
    • 0037017405 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis
    • Lane JD, Lucocq J, Pryde J, Barr FA, Woodman PG, Allan VJ, Lowe M: Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis. J Cell Biol 2002, 156:495-509
    • (2002) J Cell Biol , vol.156 , pp. 495-509
    • Lane, J.D.1    Lucocq, J.2    Pryde, J.3    Barr, F.A.4    Woodman, P.G.5    Allan, V.J.6    Lowe, M.7
  • 51
    • 1842426969 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of syntaxin 5 and giantin accompanies inhibition of secretory traffic during apoptosis
    • Lowe M, Lane JD, Woodman PG, Allan VJ: Caspase-mediated cleavage of syntaxin 5 and giantin accompanies inhibition of secretory traffic during apoptosis. J Cell Sci 2004, 117:1139-1150
    • (2004) J Cell Sci , vol.117 , pp. 1139-1150
    • Lowe, M.1    Lane, J.D.2    Woodman, P.G.3    Allan, V.J.4
  • 53
    • 3442884830 scopus 로고    scopus 로고
    • Ultrastructural neuronal pathology in transgenic mice expressing mutant (P301L) human tau
    • Lin WL, Lewis J, Yen SH, Mutton M, Dickson DW: Ultrastructural neuronal pathology in transgenic mice expressing mutant (P301L) human tau. J Neurocytol 2003, 32:1091-1105
    • (2003) J Neurocytol , vol.32 , pp. 1091-1105
    • Lin, W.L.1    Lewis, J.2    Yen, S.H.3    Mutton, M.4    Dickson, D.W.5
  • 54
    • 0029890685 scopus 로고    scopus 로고
    • The Golgi apparatus of spinal cord motor neurons in transgenic mice expressing mutant Cu, Zn superoxide dismutase becomes fragmented in early, preclinical stages of the disease
    • Mourelatos NKG, Stieber A, Gurney ME, Dal Canto MC: The Golgi apparatus of spinal cord motor neurons in transgenic mice expressing mutant Cu, Zn superoxide dismutase becomes fragmented in early, preclinical stages of the disease. Proc Natl Acad Sci USA 1996, 93:5472-5477
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5472-5477
    • Mourelatos, N.K.G.1    Stieber, A.2    Gurney, M.E.3    Dal Canto, M.C.4
  • 55
    • 0033962285 scopus 로고    scopus 로고
    • Aggregation of ubiquitin and a mutant ALS-linked SOD1 protein correlate with disease progression and fragmentation of the Golgi apparatus
    • Stieber A, Gonatas JO, Gonatas NK: Aggregation of ubiquitin and a mutant ALS-linked SOD1 protein correlate with disease progression and fragmentation of the Golgi apparatus. J Neural Sci 2000, 173:53-62
    • (2000) J Neural Sci , vol.173 , pp. 53-62
    • Stieber, A.1    Gonatas, J.O.2    Gonatas, N.K.3
  • 56
    • 0033972489 scopus 로고    scopus 로고
    • The neuronal Golgi apparatus is fragmented in transgenic mice expressing a mutant human SOD1, but not in mice expressing the human NF-H gene
    • Stieber A, Gonatas JO, Collard J, Meier J, Julien J, Schweitzer P, Gonatas NK: The neuronal Golgi apparatus is fragmented in transgenic mice expressing a mutant human SOD1, but not in mice expressing the human NF-H gene. J Neural Sci 2000, 173:63-72
    • (2000) J Neural Sci , vol.173 , pp. 63-72
    • Stieber, A.1    Gonatas, J.O.2    Collard, J.3    Meier, J.4    Julien, J.5    Schweitzer, P.6    Gonatas, N.K.7
  • 57
    • 0032491408 scopus 로고    scopus 로고
    • Genetic classification of primary neurodegenerative disease
    • Hardy J, Gwinn-Hardy K: Genetic classification of primary neurodegenerative disease. Science 1998, 282:1075-1079
    • (1998) Science , vol.282 , pp. 1075-1079
    • Hardy, J.1    Gwinn-Hardy, K.2
  • 58
    • 0031762949 scopus 로고    scopus 로고
    • Fatal attractions: Abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia
    • Trojanowski JQ, Goedert M, Iwatsubo T, Lee VM: Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia. Cell Death Differ 1998, 5:832-837
    • (1998) Cell Death Differ , vol.5 , pp. 832-837
    • Trojanowski, J.Q.1    Goedert, M.2    Iwatsubo, T.3    Lee, V.M.4
  • 59
    • 0037073748 scopus 로고    scopus 로고
    • Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion
    • Gosavi N, Lee HJ, Lee JS, Patel S, Lee SJ: Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion. J Biol Chem 2002, 277:48984-48992
    • (2002) J Biol Chem , vol.277 , pp. 48984-48992
    • Gosavi, N.1    Lee, H.J.2    Lee, J.S.3    Patel, S.4    Lee, S.J.5
  • 60
    • 0032144774 scopus 로고    scopus 로고
    • Mechanisms of trafficking in axons and dendrites: Implications for development and neurodegeneration
    • Sheetz MP, Pfister KK, Bulinski JC, Cotman CW: Mechanisms of trafficking in axons and dendrites: implications for development and neurodegeneration. Prog Neurobiol 1998, 55:577-594
    • (1998) Prog Neurobiol , vol.55 , pp. 577-594
    • Sheetz, M.P.1    Pfister, K.K.2    Bulinski, J.C.3    Cotman, C.W.4
  • 61
    • 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 TL, Cleveland DW: Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons. Nat Neurosci 1999, 2:50-56
    • (1999) Nat Neurosci , vol.2 , pp. 50-56
    • Williamson, T.L.1    Cleveland, D.W.2
  • 63
    • 0038632271 scopus 로고    scopus 로고
    • Defective neurofilament transport in mouse models of amyotrophic lateral sclerosis: A review
    • Rao MV, Nixon RA: Defective neurofilament transport in mouse models of amyotrophic lateral sclerosis: a review. Neurochem Res 2003, 28:1041-1047
    • (2003) Neurochem Res , vol.28 , pp. 1041-1047
    • Rao, M.V.1    Nixon, R.A.2
  • 64
    • 0024237306 scopus 로고
    • Brefeldin a causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum
    • Fujiwara T, Oda K, Yokota S, Takatsuki A, Ikehara Y: Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum. J Biol Chem 1988, 263:18545-18552
    • (1988) J Biol Chem , vol.263 , pp. 18545-18552
    • Fujiwara, T.1    Oda, K.2    Yokota, S.3    Takatsuki, A.4    Ikehara, Y.5
  • 65
    • 0034697285 scopus 로고    scopus 로고
    • Inhibition of phosphatidic acid synthesis alters the structure of the Golgi apparatus and inhibits secretion in endocrine cells
    • Siddhanta A, Backer JM, Shields D: Inhibition of phosphatidic acid synthesis alters the structure of the Golgi apparatus and inhibits secretion in endocrine cells. J Biol Chem 2000, 275:12023-12031
    • (2000) J Biol Chem , vol.275 , pp. 12023-12031
    • Siddhanta, A.1    Backer, J.M.2    Shields, D.3
  • 66
    • 0034920481 scopus 로고    scopus 로고
    • Cytoskeletal mechanisms of neuronal degeneration
    • Brandt R: Cytoskeletal mechanisms of neuronal degeneration. Cell Tissue Res 2001, 305:255-265
    • (2001) Cell Tissue Res , vol.305 , pp. 255-265
    • Brandt, R.1
  • 67
    • 0021135281 scopus 로고
    • Associations of elements of the Golgi apparatus with microtubules
    • Rogalski AA, Singer SJ: Associations of elements of the Golgi apparatus with microtubules. J Cell Biol 1984, 99:1092-1100
    • (1984) J Cell Biol , vol.99 , pp. 1092-1100
    • Rogalski, A.A.1    Singer, S.J.2
  • 69
  • 70
    • 0037449756 scopus 로고    scopus 로고
    • Fragmentation of the Golgi apparatus. A role for beta III spectrin and synthesis of phosphatidylinositol 4,5-bisphosphate
    • Siddhanta A, Radulescu A, Stankewich MC, Morrow JS, Shields D: Fragmentation of the Golgi apparatus. A role for beta III spectrin and synthesis of phosphatidylinositol 4,5-bisphosphate. J Biol Chem 2003, 278:1957-1965
    • (2003) J Biol Chem , vol.278 , pp. 1957-1965
    • Siddhanta, A.1    Radulescu, A.2    Stankewich, M.C.3    Morrow, J.S.4    Shields, D.5
  • 71
    • 0033937941 scopus 로고    scopus 로고
    • Regulators and effectors of the ARF GTPases
    • Donaldson JG, Jackson CL: Regulators and effectors of the ARF GTPases. Curr Opin Cell Biol 2000, 12:475-482
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 475-482
    • Donaldson, J.G.1    Jackson, C.L.2
  • 72
    • 0036312496 scopus 로고    scopus 로고
    • Involvement of glycogen synthase kinase-3beta and tau phosphorylation in neuronal Golgi disassembly
    • Elyaman W, Yardin C, Hugon J: Involvement of glycogen synthase kinase-3beta and tau phosphorylation in neuronal Golgi disassembly. J Neurochem 2002, 81:870-880
    • (2002) J Neurochem , vol.81 , pp. 870-880
    • Elyaman, W.1    Yardin, C.2    Hugon, J.3
  • 73
    • 0036769733 scopus 로고    scopus 로고
    • GSKSbeta signalling: Casting a wide net in Alzheimer's disease
    • Bhat RV, Budd SL: GSKSbeta signalling: casting a wide net in Alzheimer's disease. Neurosignals 2002, 11:251-261
    • (2002) Neurosignals , vol.11 , pp. 251-261
    • Bhat, R.V.1    Budd, S.L.2
  • 78
    • 1642528556 scopus 로고    scopus 로고
    • Disruption of the structure of the Golgi apparatus and the function of the secretory pathway by mutants G93A and G85R of Cu, Zn superoxide dismutase (SOD1) of familial amyotrophic lateral sclerosis
    • Stieber A, Gonatas JO, Moore JS, Bantly A, Yim HS, Yim MB, Gonatas NK: Disruption of the structure of the Golgi apparatus and the function of the secretory pathway by mutants G93A and G85R of Cu, Zn superoxide dismutase (SOD1) of familial amyotrophic lateral sclerosis. J Neurol Sci 2004, 219:45-53
    • (2004) J Neurol Sci , vol.219 , pp. 45-53
    • Stieber, A.1    Gonatas, J.O.2    Moore, J.S.3    Bantly, A.4    Yim, H.S.5    Yim, M.B.6    Gonatas, N.K.7
  • 79
    • 0024454714 scopus 로고
    • Microtubules are involved in the secretion of proteins at the apical cell surface of the polarized epithelial cell, Madin-Darby canine kidney
    • Parczyk K, Haase W, Kondor-Koch C: Microtubules are involved in the secretion of proteins at the apical cell surface of the polarized epithelial cell, Madin-Darby canine kidney. J Biol Chem 1939, 264:16837-16846
    • (1939) J Biol Chem , vol.264 , pp. 16837-16846
    • Parczyk, K.1    Haase, W.2    Kondor-Koch, C.3
  • 80
    • 0025865353 scopus 로고
    • Disruption of microtubules alters polarity of basement membrane proteoglycan secretion in epithelial cells
    • De Almeida JB, Stow JL: Disruption of microtubules alters polarity of basement membrane proteoglycan secretion in epithelial cells. Am J Physiol 1991, 261:C691-C700
    • (1991) Am J Physiol , vol.261
    • De Almeida, J.B.1    Stow, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.