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Volumn 23, Issue 26, 2003, Pages 8967-8977

Glutamate and amyloid β-protein rapidly inhibit fast axonal transport in cultured rat hippocampal neurons by different mechanisms

Author keywords

Actin; Amyloid protein; Axonal transport; Ca2+; Cultured hippocampal neurons; Glutamate

Indexed keywords

ACTIN; ALPHA AMINO 3 HYDROXY 5 METHYL 4 ISOXAZOLEPROPIONIC ACID; AMYLOID BETA PROTEIN; GLUTAMIC ACID; JASPAMIDE; LATRUNCULIN B; N METHYL DEXTRO ASPARTIC ACID;

EID: 0141864562     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.23-26-08967.2003     Document Type: Article
Times cited : (98)

References (88)
  • 3
    • 0037200064 scopus 로고    scopus 로고
    • (-)-Doliculide, a new macrocyclic depsipeptide enhancer of actin assembly
    • Bai R, Covell DG, Liu C, Ghosh AK, Hamel E (2002) (-)-Doliculide, a new macrocyclic depsipeptide enhancer of actin assembly. J Biol Chem 277:32165-32171.
    • (2002) J Biol Chem , vol.277 , pp. 32165-32171
    • Bai, R.1    Covell, D.G.2    Liu, C.3    Ghosh, A.K.4    Hamel, E.5
  • 4
    • 0025779179 scopus 로고
    • Solution structures of β peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow CJ, Zagorski MG (1991) Solution structures of β peptide and its constituent fragments: relation to amyloid deposition. Science 253:179-182.
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 5
    • 0005541930 scopus 로고    scopus 로고
    • Association of actin filaments with axonal microtubule tracts
    • Bearer EL, Reese TS (1999) Association of actin filaments with axonal microtubule tracts. J Neurocytol 28:85-98.
    • (1999) J Neurocytol , vol.28 , pp. 85-98
    • Bearer, E.L.1    Reese, T.S.2
  • 7
    • 0037291289 scopus 로고    scopus 로고
    • Assemblies of Alzheimer's peptides Aβ25-35 and Aβ31-35: Reverse-turn conformation and side-chain interactions revealed by X-ray diffraction
    • Bond JP, Deverin SP, Inouye H, El-Agnaf OM, Teeter MM, Kirschner DA (2003) Assemblies of Alzheimer's peptides Aβ25-35 and Aβ31-35: reverse-turn conformation and side-chain interactions revealed by X-ray diffraction. J Struct Biol 141:156-170.
    • (2003) J Struct Biol , vol.141 , pp. 156-170
    • Bond, J.P.1    Deverin, S.P.2    Inouye, H.3    El-Agnaf, O.M.4    Teeter, M.M.5    Kirschner, D.A.6
  • 8
    • 0021136122 scopus 로고
    • Gelsolin inhibition of fast axonal transport indicates a requirement for actin microfilaments
    • Brady ST, Lasek RJ, Allen RD, Yin HL, Stossel TP (1984) Gelsolin inhibition of fast axonal transport indicates a requirement for actin microfilaments. Nature 310:56-58.
    • (1984) Nature , vol.310 , pp. 56-58
    • Brady, S.T.1    Lasek, R.J.2    Allen, R.D.3    Yin, H.L.4    Stossel, T.P.5
  • 9
    • 0020461105 scopus 로고
    • Abnormalities of axonal transport: Are they a cause of peripheral nerve disease?
    • Brimijoin WS (1982) Abnormalities of axonal transport: are they a cause of peripheral nerve disease? Mayo Clin Proc 57:707-714.
    • (1982) Mayo Clin Proc , vol.57 , pp. 707-714
    • Brimijoin, W.S.1
  • 10
    • 0027429732 scopus 로고
    • β-Amyloid neurotoxicity in human cortical culture is not mediated by excitotoxins
    • Busciglio J, Yeh J, Yankner BA (1993) β-Amyloid neurotoxicity in human cortical culture is not mediated by excitotoxins. J Neurochem 61:1565-1568.
    • (1993) J Neurochem , vol.61 , pp. 1565-1568
    • Busciglio, J.1    Yeh, J.2    Yankner, B.A.3
  • 11
    • 0027324457 scopus 로고
    • 3H] MK-801 binding to rat cortical membranes in the presence of glutamate and glycine
    • 3H] MK-801 binding to rat cortical membranes in the presence of glutamate and glycine. J Neurochem 60:2297-2303.
    • (1993) J Neurochem , vol.60 , pp. 2297-2303
    • Calligaro, D.O.1    O'Malley, P.J.2    Monn, J.A.3
  • 12
    • 0031593854 scopus 로고    scopus 로고
    • Molecular modeling of the Aβ1-42 peptide from Alzheimer's disease
    • Chaney MO, Webster SD, Kuo YM, Roher AE (1998) Molecular modeling of the Aβ1-42 peptide from Alzheimer's disease. Protein Eng 11:761-767.
    • (1998) Protein Eng , vol.11 , pp. 761-767
    • Chaney, M.O.1    Webster, S.D.2    Kuo, Y.M.3    Roher, A.E.4
  • 13
    • 0032483035 scopus 로고    scopus 로고
    • Solution structure of amyloid β-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?
    • Coles M, Bicknell W, Watson AA, Fairlie DP, Craik DJ (1998) Solution structure of amyloid β-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is? Biochemistry 37:11064-11077.
    • (1998) Biochemistry , vol.37 , pp. 11064-11077
    • Coles, M.1    Bicknell, W.2    Watson, A.A.3    Fairlie, D.P.4    Craik, D.J.5
  • 15
    • 0030817292 scopus 로고    scopus 로고
    • Effects of β-amyloid-(25-35) peptides on radioligand binding to excitatory amino acid receptors and voltage-dependent calcium channels: Evidence for a selective affinity for the glutamate and glycine recognition sites of the NMDA receptor
    • Cowburn RF, Wiehager B, Trief E, Li-Li M, Sundström E (1997) Effects of β-amyloid-(25-35) peptides on radioligand binding to excitatory amino acid receptors and voltage-dependent calcium channels: evidence for a selective affinity for the glutamate and glycine recognition sites of the NMDA receptor. Neurochem Res 22:1437-1442.
    • (1997) Neurochem Res , vol.22 , pp. 1437-1442
    • Cowburn, R.F.1    Wiehager, B.2    Trief, E.3    Li-Li, M.4    Sundström, E.5
  • 16
    • 0016589417 scopus 로고
    • Role of axonal transport in maintaining central synaptic connections
    • Cull RE (1975) Role of axonal transport in maintaining central synaptic connections. Exp Brain Res 24:97-101.
    • (1975) Exp Brain Res , vol.24 , pp. 97-101
    • Cull, R.E.1
  • 17
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
    • Dahlgren KN, Manelli AM, Stine WB Jr, Baker LK, Krafft GA, LaDu MJ (2002) Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability. J Biol Chem 277:32046-32053.
    • (2002) J Biol Chem , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine W.B., Jr.3    Baker, L.K.4    Krafft, G.A.5    LaDu, M.J.6
  • 18
    • 0039228392 scopus 로고    scopus 로고
    • Pathogenic amyloid β-protein induces apoptosis in cultured human cerebrovascular smooth muscle cells
    • Davis J, Cribbs DH, Cotman CW, Van Nostrand WE (1999) Pathogenic amyloid β-protein induces apoptosis in cultured human cerebrovascular smooth muscle cells. Amyloid 6:157-164.
    • (1999) Amyloid , vol.6 , pp. 157-164
    • Davis, J.1    Cribbs, D.H.2    Cotman, C.W.3    Van Nostrand, W.E.4
  • 19
    • 0033153011 scopus 로고    scopus 로고
    • Alteration of actin organization by jaspamide inhibits ruffling, but not phagocytosis or oxidative burst, in HL-60 cells and human monocytes
    • Fabian I, Halperin D, Lefter S, Mittelman L, Altstock RT, Seaon O, Tsarfaty I (1999) Alteration of actin organization by jaspamide inhibits ruffling, but not phagocytosis or oxidative burst, in HL-60 cells and human monocytes. Blood 93:3994-4005.
    • (1999) Blood , vol.93 , pp. 3994-4005
    • Fabian, I.1    Halperin, D.2    Lefter, S.3    Mittelman, L.4    Altstock, R.T.5    Seaon, O.6    Tsarfaty, I.7
  • 20
    • 0027535084 scopus 로고
    • Excitatory amino acid-mediated cytotoxicity and calcium homeostasis in cultured neurons
    • Frandsen A, Schousboe A (1993) Excitatory amino acid-mediated cytotoxicity and calcium homeostasis in cultured neurons. J Neurochem 60:1202-1211.
    • (1993) J Neurochem , vol.60 , pp. 1202-1211
    • Frandsen, A.1    Schousboe, A.2
  • 22
    • 0028037404 scopus 로고
    • Amyloid β protein-induced irreversible current in rat cortical neurones
    • Furukawa K, Abe Y, Akaike N (1994) Amyloid β protein-induced irreversible current in rat cortical neurones. NeuroReport 5:2016-2018.
    • (1994) NeuroReport , vol.5 , pp. 2016-2018
    • Furukawa, K.1    Abe, Y.2    Akaike, N.3
  • 24
    • 0023132179 scopus 로고
    • Hirano body filaments contain actin and actin-associated proteins
    • Galloway PG, Perry G, Gambetti P (1987) Hirano body filaments contain actin and actin-associated proteins. J Neuropathol Exp Neurol 46:185-199.
    • (1987) J Neuropathol Exp Neurol , vol.46 , pp. 185-199
    • Galloway, P.G.1    Perry, G.2    Gambetti, P.3
  • 26
    • 0020170121 scopus 로고
    • Microinjection into an identified axon to study the mechanism of fast axonal transport
    • Goldberg DJ (1982) Microinjection into an identified axon to study the mechanism of fast axonal transport. Proc Natl Acad Sci USA 79:4818-4822.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4818-4822
    • Goldberg, D.J.1
  • 27
    • 0019274004 scopus 로고
    • Analysis of the mechanism of fast axonal transport by intracellular injection of potentially inhibitory macromolecules: Evidence for a possible role of actin filaments
    • Goldberg DJ, Harris DA, Lubit BW, Schwartz JH (1980) Analysis of the mechanism of fast axonal transport by intracellular injection of potentially inhibitory macromolecules: evidence for a possible role of actin filaments. Proc Natl Acad Sci USA 77:7448-7452.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 7448-7452
    • Goldberg, D.J.1    Harris, D.A.2    Lubit, B.W.3    Schwartz, J.H.4
  • 28
    • 0020540685 scopus 로고
    • The association of actin with Hirano bodies
    • Goldman JE (1983) The association of actin with Hirano bodies. J Neuropathol Exp Neurol 42:146-152.
    • (1983) J Neuropathol Exp Neurol , vol.42 , pp. 146-152
    • Goldman, J.E.1
  • 29
    • 0029102993 scopus 로고
    • Neurodegeneration mediated by glutamate and β-amyloid peptide: A comparison and possible interaction
    • Gray CW, Patel AJ (1995) Neurodegeneration mediated by glutamate and β-amyloid peptide: a comparison and possible interaction. Brain Res 691:169-179.
    • (1995) Brain Res , vol.691 , pp. 169-179
    • Gray, C.W.1    Patel, A.J.2
  • 32
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley DM, Walsh DM, Ye CP, Diehl T, Vasquez S, Vassilev PM, Teplow DB, Selkoe DJ (1999) Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J Neurosci 19:8876-8884.
    • (1999) J Neurosci , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 34
    • 0018885810 scopus 로고
    • Experimental approach to test the role of actin in axonal transport
    • Isenberg G, Schubert P, Kreutzberg GW (1980) Experimental approach to test the role of actin in axonal transport. Brain Res 194:588-593.
    • (1980) Brain Res , vol.194 , pp. 588-593
    • Isenberg, G.1    Schubert, P.2    Kreutzberg, G.W.3
  • 35
    • 0028169925 scopus 로고
    • Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is A beta 42(43)
    • Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y (1994) Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is A beta 42(43). Neuron 13:45-53.
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 36
    • 0026778186 scopus 로고
    • Amyloid β-protein fragment 25-35 causes activation of cytoplasmic calcium in neurons
    • Joseph R, Han E (1992) Amyloid β-protein fragment 25-35 causes activation of cytoplasmic calcium in neurons. Biochem Biophys Res Commun 184:1441-1447.
    • (1992) Biochem Biophys Res Commun , vol.184 , pp. 1441-1447
    • Joseph, R.1    Han, E.2
  • 37
    • 0033621641 scopus 로고    scopus 로고
    • Human amyloid-β1-42 applied in vivo inhibits the fast axonal transport of proteins in the sciatic nerve of rat
    • Kasa P, Papp H, Kovacs I, Forgon M, Penke B, Yamaguchi H (2000) Human amyloid-β1-42 applied in vivo inhibits the fast axonal transport of proteins in the sciatic nerve of rat. Neurosci Lett 278:117-119.
    • (2000) Neurosci Lett , vol.278 , pp. 117-119
    • Kasa, P.1    Papp, H.2    Kovacs, I.3    Forgon, M.4    Penke, B.5    Yamaguchi, H.6
  • 38
    • 0030962492 scopus 로고    scopus 로고
    • Nanomolar amyloid β protein-induced inhibition of cellular redox activity in cultured astrocytes
    • Kato M, Saito H, Abe K (1997) Nanomolar amyloid β protein-induced inhibition of cellular redox activity in cultured astrocytes. J Neurochem 68:1889-1895.
    • (1997) J Neurochem , vol.68 , pp. 1889-1895
    • Kato, M.1    Saito, H.2    Abe, K.3
  • 39
    • 0034319190 scopus 로고    scopus 로고
    • Molecular mechanism of neurodegeneration induced by Alzheimer's β-amyloid protein: Channel formation and disruption of calcium homeostasis
    • Kawahara M, Kuroda Y (2000) Molecular mechanism of neurodegeneration induced by Alzheimer's β-amyloid protein: channel formation and disruption of calcium homeostasis. Brain Res Bull 53:389-397.
    • (2000) Brain Res Bull , vol.53 , pp. 389-397
    • Kawahara, M.1    Kuroda, Y.2
  • 42
    • 0027288860 scopus 로고
    • Amyloid β-protein as a substrate interacts with extracellular matrix to promote neurite outgrowth
    • Koo EH, Park L, Selkoe DJ (1993) Amyloid β-protein as a substrate interacts with extracellular matrix to promote neurite outgrowth. Proc Natl Acad Sci USA 90:4748-4752.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4748-4752
    • Koo, E.H.1    Park, L.2    Selkoe, D.J.3
  • 43
    • 0028273013 scopus 로고
    • Beta amyloid neurotoxicity and neuronal degeneration in Alzheimer's disease
    • Kowall NW (1994) Beta amyloid neurotoxicity and neuronal degeneration in Alzheimer's disease. Neurobiol Aging 15:257-258.
    • (1994) Neurobiol Aging , vol.15 , pp. 257-258
    • Kowall, N.W.1
  • 44
    • 0026534466 scopus 로고
    • Actin-dependent organelle movement in squid axoplasm
    • Kuznetsov SA, Langford GM, Weiss DG (1992) Actin-dependent organelle movement in squid axoplasm. Nature 356:722-725.
    • (1992) Nature , vol.356 , pp. 722-725
    • Kuznetsov, S.A.1    Langford, G.M.2    Weiss, D.G.3
  • 46
    • 0031765270 scopus 로고    scopus 로고
    • Glutamate toxicity in chronic neurodegenerative disease
    • Lancelot E, Beal MF (1998) Glutamate toxicity in chronic neurodegenerative disease. Prog Brain Res 116:331-347.
    • (1998) Prog Brain Res , vol.116 , pp. 331-347
    • Lancelot, E.1    Beal, M.F.2
  • 47
    • 0029056516 scopus 로고
    • Cell death induced by β-amyloid 1-40 in MES 23.5 hybrid clone: The role of nitric oxide and NMDA-gated channel activation leading to apoptosis
    • Le WD, Colom LV, Xie WJ, Smith RG, Alexianu M, Appel SH (1995) Cell death induced by β-amyloid 1-40 in MES 23.5 hybrid clone: the role of nitric oxide and NMDA-gated channel activation leading to apoptosis. Brain Res 686:49-60.
    • (1995) Brain Res , vol.686 , pp. 49-60
    • Le, W.D.1    Colom, L.V.2    Xie, W.J.3    Smith, R.G.4    Alexianu, M.5    Appel, S.H.6
  • 48
    • 0031914182 scopus 로고    scopus 로고
    • Formation of F-actin aggregates in cells treated with actin stabilizing drugs
    • Lee E, Shelden EA, Knecht DA (1998) Formation of F-actin aggregates in cells treated with actin stabilizing drugs. Cell Motil Cytoskeleton 39:122-133.
    • (1998) Cell Motil Cytoskeleton , vol.39 , pp. 122-133
    • Lee, E.1    Shelden, E.A.2    Knecht, D.A.3
  • 50
    • 0033040551 scopus 로고    scopus 로고
    • An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments
    • Li L, Darden TA, Bartolotti L, Kominos D, Pedersen LG (1999) An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments. Biophys J 76:2871-2878.
    • (1999) Biophys J , vol.76 , pp. 2871-2878
    • Li, L.1    Darden, T.A.2    Bartolotti, L.3    Kominos, D.4    Pedersen, L.G.5
  • 51
    • 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 LA, 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
  • 52
    • 0035831137 scopus 로고    scopus 로고
    • 2+ sequestration/extrusion mechanisms following excitotoxic glutamate exposure
    • 2+ sequestration/extrusion mechanisms following excitotoxic glutamate exposure. Brain Res 894:56-67.
    • (2001) Brain Res , vol.894 , pp. 56-67
    • Limbrick D.D., Jr.1    Pal, S.2    DeLorenzo, R.J.3
  • 53
    • 0028898888 scopus 로고
    • Mechanisms of synaptic dysfunction in Alzheimer's disease
    • Masliah E (1995) Mechanisms of synaptic dysfunction in Alzheimer's disease. Histol Histopathol 10:509-519.
    • (1995) Histol Histopathol , vol.10 , pp. 509-519
    • Masliah, E.1
  • 54
    • 0024364877 scopus 로고
    • Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease
    • Masliah E, Terry RD, DeTeresa RM, Hansen LA (1989) Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease. Neurosci Lett 103:234-239.
    • (1989) Neurosci Lett , vol.103 , pp. 234-239
    • Masliah, E.1    Terry, R.D.2    DeTeresa, R.M.3    Hansen, L.A.4
  • 55
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson MP, Cheng B, Davis D, Bryant K, Lieberburg I, Rydel RE (1992) β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J Neurosci 12:376-389.
    • (1992) J Neurosci , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 56
    • 0023838603 scopus 로고
    • Progressive deficits in retrograde axon transport precede degeneration of motor axons in acrylamide neuropathy
    • Moretto A, Sabri MI (1988) Progressive deficits in retrograde axon transport precede degeneration of motor axons in acrylamide neuropathy. Brain Res 440:18-24.
    • (1988) Brain Res , vol.440 , pp. 18-24
    • Moretto, A.1    Sabri, M.I.2
  • 57
    • 0028861992 scopus 로고
    • Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons
    • Morris RL, Hollenbeck PJ (1995) Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons. J Cell Biol 131:1315-1326.
    • (1995) J Cell Biol , vol.131 , pp. 1315-1326
    • Morris, R.L.1    Hollenbeck, P.J.2
  • 58
    • 0023775466 scopus 로고
    • Immunoelectron microscopic localization of actin in neurites of cultured embryonic chick dorsal root ganglia: Actin is a component of granular, microtubule-associated cross-bridges
    • Nagele RG, Kosciuk MC, Hunter ET, Bush KT, Lee H (1988) Immunoelectron microscopic localization of actin in neurites of cultured embryonic chick dorsal root ganglia: actin is a component of granular, microtubule-associated cross-bridges. Brain Res 474:279-286.
    • (1988) Brain Res , vol.474 , pp. 279-286
    • Nagele, R.G.1    Kosciuk, M.C.2    Hunter, E.T.3    Bush, K.T.4    Lee, H.5
  • 59
    • 0021993506 scopus 로고
    • Structural effects in axoplasm of DNase I, an actin depolymerizer that blocks fast axonal transport
    • Nemhauser I, Goldberg DJ (1985) Structural effects in axoplasm of DNase I, an actin depolymerizer that blocks fast axonal transport. Brain Res 334:47-58.
    • (1985) Brain Res , vol.334 , pp. 47-58
    • Nemhauser, I.1    Goldberg, D.J.2
  • 60
    • 0034054984 scopus 로고    scopus 로고
    • Mechanism of lateral movement of filopodia and radial actin bundles across neuronal growth cones
    • Oldenbourg R, Katoh K, Danuser G (2000) Mechanism of lateral movement of filopodia and radial actin bundles across neuronal growth cones. Biophys J 78:1176-1182.
    • (2000) Biophys J , vol.78 , pp. 1176-1182
    • Oldenbourg, R.1    Katoh, K.2    Danuser, G.3
  • 62
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike CJ, Walencewicz AJ, Glabe CG, Cotman CW (1991) In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res 563:311-314.
    • (1991) Brain Res , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 63
    • 0030049915 scopus 로고    scopus 로고
    • Filament heterogeneity within the dystrophic neurites of senile plaques suggests blockage of fast axonal transport in Alzheimer's disease
    • Praprotnik D, Smith MA, Richey PL, Vinters HV, Perry G (1996) Filament heterogeneity within the dystrophic neurites of senile plaques suggests blockage of fast axonal transport in Alzheimer's disease. Acta Neuropathol (Berl) 91:226-235.
    • (1996) Acta Neuropathol (Berl) , vol.91 , pp. 226-235
    • Praprotnik, D.1    Smith, M.A.2    Richey, P.L.3    Vinters, H.V.4    Perry, G.5
  • 64
    • 0035934268 scopus 로고    scopus 로고
    • Amyloid β-protein fragment 31-35 forms ion channels in membrane patches excised from rat hippocampal neurons
    • Qi JS, Qiao JT (2001) Amyloid β-protein fragment 31-35 forms ion channels in membrane patches excised from rat hippocampal neurons. Neuroscience 105:845-852.
    • (2001) Neuroscience , vol.105 , pp. 845-852
    • Qi, J.S.1    Qiao, J.T.2
  • 65
    • 0024368871 scopus 로고
    • Accumulation of smooth endoplasmic reticulum in Alzheimer's disease: New morphological evidence of axoplasmic flow disturbances
    • Richard S, Brion JP, Couck AM, Flament-Durand J (1989) Accumulation of smooth endoplasmic reticulum in Alzheimer's disease: new morphological evidence of axoplasmic flow disturbances. J Submicrosc Cytol Pathol 21:461-467.
    • (1989) J Submicrosc Cytol Pathol , vol.21 , pp. 461-467
    • Richard, S.1    Brion, J.P.2    Couck, A.M.3    Flament-Durand, J.4
  • 66
    • 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 RK, Brady ST, Black MM (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
  • 67
    • 0031035836 scopus 로고    scopus 로고
    • Aggregates of a β-amyloid peptide are required to induce calcium currents in neuron-like human teratocarcinoma cells: Relation to Alzheimer's disease
    • Sanderson KL, Butler L, Ingram VM (1997) Aggregates of a β-amyloid peptide are required to induce calcium currents in neuron-like human teratocarcinoma cells: relation to Alzheimer's disease. Brain Res 744:7-14.
    • (1997) Brain Res , vol.744 , pp. 7-14
    • Sanderson, K.L.1    Butler, L.2    Ingram, V.M.3
  • 70
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: Structure and assembly
    • Serpell LC (2000) Alzheimer's amyloid fibrils: structure and assembly. Biochim Biophys Acta 1502:16-30.
    • (2000) Biochim Biophys Acta , vol.1502 , pp. 16-30
    • Serpell, L.C.1
  • 71
    • 0036847145 scopus 로고    scopus 로고
    • β-Amyloid peptide induces formation of actin stress fibers through p38 mitogen-activated protein kinase
    • Song C, Perides G, Wang D, Liu YF (2002) β-Amyloid peptide induces formation of actin stress fibers through p38 mitogen-activated protein kinase. J Neurochem 83:828-836.
    • (2002) J Neurochem , vol.83 , pp. 828-836
    • Song, C.1    Perides, G.2    Wang, D.3    Liu, Y.F.4
  • 72
    • 0014193263 scopus 로고
    • Fine structural localization of acid phosphatase in senile plaques in Alzheimer's presenile dementia
    • Suzuki K, Terry RD (1967) Fine structural localization of acid phosphatase in senile plaques in Alzheimer's presenile dementia. Acta Neuropathol (Berl) 8:276-284.
    • (1967) Acta Neuropathol (Berl) , vol.8 , pp. 276-284
    • Suzuki, K.1    Terry, R.D.2
  • 74
    • 0033776708 scopus 로고    scopus 로고
    • Rapid movement of axonal neurofilaments interrupted by prolonged pauses
    • Wang L, Ho CL, Sun D, Liem RK, Brown A (2000) Rapid movement of axonal neurofilaments interrupted by prolonged pauses. Nat Cell Biol 2:137-141.
    • (2000) Nat Cell Biol , vol.2 , pp. 137-141
    • Wang, L.1    Ho, C.L.2    Sun, D.3    Liem, R.K.4    Brown, A.5
  • 75
    • 0033585832 scopus 로고    scopus 로고
    • Selective impairment of fast anterograde axonal transport in the peripheral nerves of asymptomatic transgenic mice with a G93A mutant SOD1 gene
    • Warita H, Itoyama Y, Abe K (1999) Selective impairment of fast anterograde axonal transport in the peripheral nerves of asymptomatic transgenic mice with a G93A mutant SOD1 gene. Brain Res 819:120-131.
    • (1999) Brain Res , vol.819 , pp. 120-131
    • Warita, H.1    Itoyama, Y.2    Abe, K.3
  • 76
    • 0028180304 scopus 로고
    • 2+ channel blockers attenuate β-amyloid peptide toxicity to cortical neurons in culture
    • 2+ channel blockers attenuate β-amyloid peptide toxicity to cortical neurons in culture. J Neurochem 62:372-375.
    • (1994) J Neurochem , vol.62 , pp. 372-375
    • Weiss, J.H.1    Pike, C.J.2    Cotman, C.W.3
  • 77
    • 0035029801 scopus 로고    scopus 로고
    • Sublethal concentrations of prion peptide PrP106-126 or the amyloid beta peptide of Alzheimer's disease activates expression of proapoptotic markers in primary cortical neurons
    • White AR, Guirguis R, Brazier MW, Jobling MF, Hill AF, Beyreuther K, Barrow CJ, Masters CL, Collins SJ, Cappai R (2001) Sublethal concentrations of prion peptide PrP106-126 or the amyloid beta peptide of Alzheimer's disease activates expression of proapoptotic markers in primary cortical neurons. Neurobiol Dis 8:299-316.
    • (2001) Neurobiol Dis , vol.8 , pp. 299-316
    • White, A.R.1    Guirguis, R.2    Brazier, M.W.3    Jobling, M.F.4    Hill, A.F.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Collins, S.J.9    Cappai, R.10
  • 79
    • 0028981561 scopus 로고
    • Neurotoxicity of A β amyloid protein in vitro is not altered by calcium channel blockade
    • Whitson JS, Appel SH (1995) Neurotoxicity of A β amyloid protein in vitro is not altered by calcium channel blockade. Neurobiol Aging 16:5-10.
    • (1995) Neurobiol Aging , vol.16 , pp. 5-10
    • Whitson, J.S.1    Appel, S.H.2
  • 81
    • 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 (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
  • 83
    • 0015078708 scopus 로고
    • Ultrastructure and function of growth cones and axons of cultured nerve cells
    • Yamada KM, Spooner BS, Wessells NK (1971) Ultrastructure and function of growth cones and axons of cultured nerve cells. J Cell Biol 49:614-635.
    • (1971) J Cell Biol , vol.49 , pp. 614-635
    • Yamada, K.M.1    Spooner, B.S.2    Wessells, N.K.3
  • 84
    • 0033036691 scopus 로고    scopus 로고
    • β-amyloid peptide fragment 31-35 induces apoptosis in cultured cortical neurons
    • Yan XZ, Qiao JT, Dou Y, Qiao ZD (1999) β-amyloid peptide fragment 31-35 induces apoptosis in cultured cortical neurons. Neuroscience 92:177-184.
    • (1999) Neuroscience , vol.92 , pp. 177-184
    • Yan, X.Z.1    Qiao, J.T.2    Dou, Y.3    Qiao, Z.D.4
  • 85
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner BA, Duffy LK, Kirschner DA (1990) Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides. Science 250:279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.