메뉴 건너뛰기




Volumn 98, Issue 4, 2006, Pages 993-1006

Do axonal defects in tau and amyloid precursor protein transgenic animals model axonopathy in Alzheimer's disease?

Author keywords

Alzheimer's disease; Amyloid; Animal models; Axonal transport; Axonopathy; Tau

Indexed keywords

AMYLOID BETA PROTEIN[25-35]; AMYLOID PRECURSOR PROTEIN; PRESENILIN 1; TAU PROTEIN;

EID: 33746411112     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2006.03955.x     Document Type: Short Survey
Times cited : (109)

References (148)
  • 1
    • 0021952113 scopus 로고
    • Gliding movement of and bidirectional transport along single native microtubules from squid axoplasm: Evidence for an active role of microtubules in cytoplasmic transport
    • Allen R. D., Weiss D. G., Hayden J. H., Brown D. T., Fujiwake H. and Simpson M. (1985) Gliding movement of and bidirectional transport along single native microtubules from squid axoplasm: evidence for an active role of microtubules in cytoplasmic transport. J. Cell Biol. 100, 1736-1752.
    • (1985) J. Cell Biol. , vol.100 , pp. 1736-1752
    • Allen, R.D.1    Weiss, D.G.2    Hayden, J.H.3    Brown, D.T.4    Fujiwake, H.5    Simpson, M.6
  • 2
    • 0027267493 scopus 로고
    • Inhibition of kinesin synthesis and rapid anterograde axonal transport in vivo by an antisense oligonucleotide
    • Amaratunga A., Morin P. J., Kosik K. S. and Fine R. E. (1993) Inhibition of kinesin synthesis and rapid anterograde axonal transport in vivo by an antisense oligonucleotide. J. Biol. Chem. 268, 17 427-17 430.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17427-17430
    • Amaratunga, A.1    Morin, P.J.2    Kosik, K.S.3    Fine, R.E.4
  • 3
    • 0348108123 scopus 로고    scopus 로고
    • Synaptic plasticity and cell cycle activation in neurons are alternative effector pathways: The 'Dr. Jekyll and Mr. Hyde concept' of Alzheimer's disease or the yin and yang of neuroplasticity
    • Arendt T. (2003) Synaptic plasticity and cell cycle activation in neurons are alternative effector pathways: the 'Dr. Jekyll and Mr. Hyde concept' of Alzheimer's disease or the yin and yang of neuroplasticity. Prog. Neurobiol. 71, 83-248.
    • (2003) Prog. Neurobiol. , vol.71 , pp. 83-248
    • Arendt, T.1
  • 4
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada P. V., Growdon J. H., Hedley-Whyte E. T. and Hyman B. T. (1992) Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 42, 631-639.
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 6
    • 0042307302 scopus 로고    scopus 로고
    • Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure
    • Berriman J., Serpell L. C., Oberg K. A., Fink A. L., Goedert M. and Crowther R. A. (2003) Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure. Proc. Natl Acad. Sci. USA 100, 9034-9038.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9034-9038
    • Berriman, J.1    Serpell, L.C.2    Oberg, K.A.3    Fink, A.L.4    Goedert, M.5    Crowther, R.A.6
  • 7
    • 27444437758 scopus 로고    scopus 로고
    • Disease-related modifications in tau affect the interaction between Fyn and Tau
    • Bhaskar K., Yen S. H. and Lee G. (2005) Disease-related modifications in tau affect the interaction between Fyn and Tau. J. Biol. Chem. 280, 35 119-35 125.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35119-35125
    • Bhaskar, K.1    Yen, S.H.2    Lee, G.3
  • 10
    • 0344838686 scopus 로고    scopus 로고
    • Stereologic analysis of neurofibrillary tangle formation in prefrontal cortex area 9 in aging and Alzheimer's disease
    • Bussiere T., Gold G., Kovari E., Giannakopoulos P., Bouras C., Perl D. P., Morrison J. H. and Hof P. R. (2003) Stereologic analysis of neurofibrillary tangle formation in prefrontal cortex area 9 in aging and Alzheimer's disease. Neuroscience 117, 577-592.
    • (2003) Neuroscience , vol.117 , pp. 577-592
    • Bussiere, T.1    Gold, G.2    Kovari, E.3    Giannakopoulos, P.4    Bouras, C.5    Perl, D.P.6    Morrison, J.H.7    Hof, P.R.8
  • 11
    • 0032402095 scopus 로고    scopus 로고
    • Alzheimer amyloid protein precursor in the rat hippocampus: Transport and processing through the perforant path
    • Buxbaum J. D., Thinakaran G., Koliatsos V., O'Callahan J., Slunt H. H., Price D. L. and Sisodia S. S. (1998) Alzheimer amyloid protein precursor in the rat hippocampus: transport and processing through the perforant path. J. Neurosci. 18, 9629-9637.
    • (1998) J. Neurosci. , vol.18 , pp. 9629-9637
    • Buxbaum, J.D.1    Thinakaran, G.2    Koliatsos, V.3    O'Callahan, J.4    Slunt, H.H.5    Price, D.L.6    Sisodia, S.S.7
  • 12
    • 0035819072 scopus 로고    scopus 로고
    • UNC-16, a JNK-signaling scaffold protein, regulates vesicle transport in C. elegans
    • Byrd D. T., Kawasaki M., Walcoff M., Hisamoto N., Matsumoto K. and Jin Y. (2001) UNC-16, a JNK-signaling scaffold protein, regulates vesicle transport in C. elegans. Neuron 32, 787-800.
    • (2001) Neuron , vol.32 , pp. 787-800
    • Byrd, D.T.1    Kawasaki, M.2    Walcoff, M.3    Hisamoto, N.4    Matsumoto, K.5    Jin, Y.6
  • 13
    • 0242600546 scopus 로고    scopus 로고
    • Microtubule reduction in Alzheimer's disease and aging is independent of tau filament formation
    • Cash A. D., Aliev G., Siedlak S. L. et al. (2003) Microtubule reduction in Alzheimer's disease and aging is independent of tau filament formation. Am. J. Pathol. 162, 1623-1627.
    • (2003) Am. J. Pathol. , vol.162 , pp. 1623-1627
    • Cash, A.D.1    Aliev, G.2    Siedlak, S.L.3
  • 14
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B. and Lansbury P. T. (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267-298.
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 15
    • 27744600579 scopus 로고    scopus 로고
    • Over-expression of tau results in defective synaptic transmission in Drosophila neuromuscular junctions
    • Chee F. C., Mudher A., Cuttle M. F., Newman T. A., MacKay D., Lovestone S. and Shepherd D. (2005) Over-expression of tau results in defective synaptic transmission in Drosophila neuromuscular junctions. Neurobiol Dis. 20, 918-928.
    • (2005) Neurobiol Dis. , vol.20 , pp. 918-928
    • Chee, F.C.1    Mudher, A.2    Cuttle, M.F.3    Newman, T.A.4    MacKay, D.5    Lovestone, S.6    Shepherd, D.7
  • 17
    • 3242770404 scopus 로고    scopus 로고
    • Long-term accumulation of amyloid-beta, beta-secretase, presenilin-1, and caspase-3 in damaged axons following brain trauma
    • Chen X. H., Siman R., Iwata A., Meaney D. F., Trojanowski J. Q. and Smith D. H. (2004b) Long-term accumulation of amyloid-beta, beta-secretase, presenilin-1, and caspase-3 in damaged axons following brain trauma. Am. J. Pathol. 165, 357-371.
    • (2004) Am. J. Pathol. , vol.165 , pp. 357-371
    • Chen, X.H.1    Siman, R.2    Iwata, A.3    Meaney, D.F.4    Trojanowski, J.Q.5    Smith, D.H.6
  • 18
    • 3242770404 scopus 로고    scopus 로고
    • Long-term accumulation of amyloid-beta, beta-secretase, presenilin-1, and caspase-3 in damaged axons following brain trauma
    • Chen X. H., Siman R., Iwata A., Meaney D. F., Trojanowski J. Q. and Smith D. H. (2004c) Long-term accumulation of amyloid-beta, beta-secretase, presenilin-1, and caspase-3 in damaged axons following brain trauma. Am. J. Pathol. 165, 357-371.
    • (2004) Am. J. Pathol. , vol.165 , pp. 357-371
    • Chen, X.H.1    Siman, R.2    Iwata, A.3    Meaney, D.F.4    Trojanowski, J.Q.5    Smith, D.H.6
  • 20
    • 0031025417 scopus 로고    scopus 로고
    • Microtubule-associated protein 2c reorganizes both microtubules and microfilaments into distinct cytological structures in an actin-binding protein-280-deficient melanoma cell line
    • Cunningham C. C., Leclerc N., Flanagan L. A., Lu M., Janmey P. A. and Kosik K. S. (1997) Microtubule-associated protein 2c reorganizes both microtubules and microfilaments into distinct cytological structures in an actin-binding protein-280-deficient melanoma cell line. J. Cell Biol. 136, 845-857.
    • (1997) J. Cell Biol. , vol.136 , pp. 845-857
    • Cunningham, C.C.1    Leclerc, N.2    Flanagan, L.A.3    Lu, M.4    Janmey, P.A.5    Kosik, K.S.6
  • 21
    • 21244486781 scopus 로고    scopus 로고
    • Proteomic and functional analysis reveal a mitochondrial dysfunction in P301L tau transgenic mice
    • David D. C., Hauptmann S., Scherping I. et al. (2005a) Proteomic and functional analysis reveal a mitochondrial dysfunction in P301L tau transgenic mice. J. Biol. Chem. 280, 23 802-23 814.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23802-23814
    • David, D.C.1    Hauptmann, S.2    Scherping, I.3
  • 22
    • 25444464112 scopus 로고    scopus 로고
    • Functional genomics meets neurodegenerative disorders Part I: Transcriptomic and proteomic technology
    • David D. C., Hoerndli F. and Gotz J. (2005b) Functional genomics meets neurodegenerative disorders Part I: transcriptomic and proteomic technology. Prog. Neurobiol. 76, 153-168.
    • (2005) Prog. Neurobiol. , vol.76 , pp. 153-168
    • David, D.C.1    Hoerndli, F.2    Gotz, J.3
  • 23
    • 0142182060 scopus 로고    scopus 로고
    • The role of microtubule-associated protein 2c in the reorganization of microtubules and lamellipodia during neurite initiation
    • Dehmelt L., Smart F. M., Ozer R. S. and Halpain S. (2003) The role of microtubule-associated protein 2c in the reorganization of microtubules and lamellipodia during neurite initiation. J. Neurosci. 23, 9479-9490.
    • (2003) J. Neurosci. , vol.23 , pp. 9479-9490
    • Dehmelt, L.1    Smart, F.M.2    Ozer, R.S.3    Halpain, S.4
  • 24
    • 0032894121 scopus 로고    scopus 로고
    • The biochemical pathway of neurofibrillary degeneration in aging and Alzheimer's disease
    • Delacourte A., David J. P., Sergeant N. et al. (1999) The biochemical pathway of neurofibrillary degeneration in aging and Alzheimer's disease. Neurology 52, 1158-1165.
    • (1999) Neurology , vol.52 , pp. 1158-1165
    • Delacourte, A.1    David, J.P.2    Sergeant, N.3
  • 26
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer's disease
    • Ebneth A., Godemann R., Stamer K., Illenberger S., Trinczek B. and Mandelkow E. (1998) Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease. J. Cell Biol. 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
  • 27
    • 18844403842 scopus 로고    scopus 로고
    • Molecular mechanisms of dendritic spine development and remodeling
    • Ethell I. M. and Pasquale E. B. (2005) Molecular mechanisms of dendritic spine development and remodeling. Prog. Neurobiol. 75, 161-205.
    • (2005) Prog. Neurobiol. , vol.75 , pp. 161-205
    • Ethell, I.M.1    Pasquale, E.B.2
  • 28
    • 0141960033 scopus 로고    scopus 로고
    • Beta-amyloid induces PHF-like tau filaments in tissue culture
    • Ferrari A., Hoerndli F., Baechi T., Nitsch R. M. and Gotz J. (2003) Beta-amyloid induces PHF-like tau filaments in tissue culture. J. Biol. Chem. 278, 40 162-40 168.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40162-40168
    • Ferrari, A.1    Hoerndli, F.2    Baechi, T.3    Nitsch, R.M.4    Gotz, J.5
  • 29
    • 0026606451 scopus 로고
    • Suppression of kinesin expression in cultured hippocampal neurons using antisense oligonucleotides
    • Ferreira A., Niclas J., Vale R. D., Banker G. and Kosik K. S. (1992) Suppression of kinesin expression in cultured hippocampal neurons using antisense oligonucleotides. J. Cell Biol. 117, 595-606.
    • (1992) J. Cell Biol. , vol.117 , pp. 595-606
    • Ferreira, A.1    Niclas, J.2    Vale, R.D.3    Banker, G.4    Kosik, K.S.5
  • 30
    • 0032795884 scopus 로고    scopus 로고
    • Neurons and their dendrites in frontotemporal dementia
    • Ferrer I. (1999) Neurons and their dendrites in frontotemporal dementia. Dement. Geriatr. Cogn. Disord. 10, 55-60.
    • (1999) Dement. Geriatr. Cogn. Disord. , vol.10 , pp. 55-60
    • Ferrer, I.1
  • 31
    • 0036082812 scopus 로고    scopus 로고
    • Dendritic spine pathology: Cause or consequence of neurological disorders?
    • Fiala J. C., Spacek J. and Harris K. M. (2002) Dendritic spine pathology: cause or consequence of neurological disorders? Brain Res. Brain Res. Rev. 39, 29-54.
    • (2002) Brain Res. Brain Res. Rev. , vol.39 , pp. 29-54
    • Fiala, J.C.1    Spacek, J.2    Harris, K.M.3
  • 33
    • 0026471340 scopus 로고
    • Effects of kinesin mutations on neuronal functions
    • Gho M., McDonald K., Ganetzky B. and Saxton W. M. (1992) Effects of kinesin mutations on neuronal functions. Science 258, 313-316.
    • (1992) Science , vol.258 , pp. 313-316
    • Gho, M.1    McDonald, K.2    Ganetzky, B.3    Saxton, W.M.4
  • 36
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G. G. and Wong C. W. (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120, 885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 37
    • 0002792366 scopus 로고
    • Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: Identification as the microtubule-associated protein tau
    • Goedert M., Wischik C. M., Crowther R. A., Walker J. E. and Klug A. (1988) Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau. Proc. Natl Acad. Sci. USA 85, 4051-4055.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 38
    • 0033788787 scopus 로고    scopus 로고
    • Reduced binding of protein phosphatase 2A to tau protein with frontotemporal dementia and parkinsonism linked to chromosome 17 mutations
    • In Process Citation
    • Goedert M., Satumtira S., Jakes R., Smith M. J., Kamibayashi C., White C. L. III and Sontag E. (2000) Reduced binding of protein phosphatase 2A to tau protein with frontotemporal dementia and parkinsonism linked to chromosome 17 mutations [In Process Citation]. J. Neurochem. 75, 2155-2162.
    • (2000) J. Neurochem. , vol.75 , pp. 2155-2162
    • Goedert, M.1    Satumtira, S.2    Jakes, R.3    Smith, M.J.4    Kamibayashi, C.5    White III, C.L.6    Sontag, E.7
  • 40
    • 0034992339 scopus 로고    scopus 로고
    • Tau and transgenic animal models
    • Gotz J. (2001) Tau and transgenic animal models. Brain Res. Brain Res. Rev. 35, 266-286.
    • (2001) Brain Res. Brain Res. Rev. , vol.35 , pp. 266-286
    • Gotz, J.1
  • 41
    • 0035800219 scopus 로고    scopus 로고
    • Compartmentalized tau hyperphosphorylation and increased levels of kinases in transgenic mice
    • Gotz J. and Nitsch R. M. (2001) Compartmentalized tau hyperphosphorylation and increased levels of kinases in transgenic mice. Neuroreport 12, 2007-2016.
    • (2001) Neuroreport , vol.12 , pp. 2007-2016
    • Gotz, J.1    Nitsch, R.M.2
  • 42
    • 0028965635 scopus 로고
    • Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform
    • Gotz J., Probst A., Spillantini M. G., Schafer T., Jakes R., Burki K. and Goedert M. (1995) Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. EMBO J. 14, 1304-1313.
    • (1995) EMBO J. , vol.14 , pp. 1304-1313
    • Gotz, J.1    Probst, A.2    Spillantini, M.G.3    Schafer, T.4    Jakes, R.5    Burki, K.6    Goedert, M.7
  • 43
    • 0035808361 scopus 로고    scopus 로고
    • Tau filament formation in transgenic mice expressing P301L tau
    • Gotz J., Chen F., Barmettler R. and Nitsch R. M. (2001a) Tau filament formation in transgenic mice expressing P301L tau. J. Biol. Chem. 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
  • 44
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Abeta 42 fibrils
    • Gotz J., Chen F., van Dorpe J. and Nitsch R. M. (2001b) Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Abeta 42 fibrils. Science 293, 1491-1495.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 45
    • 4744370969 scopus 로고    scopus 로고
    • Amyloid-induced neurofibrillary tangle formation in Alzheimer's disease: Insight from transgenic mouse and tissue-culture models
    • Gotz J., Schild A., Hoerndli F. and Pennanen L. (2004a) Amyloid-induced neurofibrillary tangle formation in Alzheimer's disease: insight from transgenic mouse and tissue-culture models. Int. J. Dev. Neurosci. 22, 453-465.
    • (2004) Int. J. Dev. Neurosci. , vol.22 , pp. 453-465
    • Gotz, J.1    Schild, A.2    Hoerndli, F.3    Pennanen, L.4
  • 47
    • 0035829720 scopus 로고    scopus 로고
    • Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila
    • Gunawardena S. and Goldstein L. S. (2001) Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila. Neuron 32, 389-401.
    • (2001) Neuron , vol.32 , pp. 389-401
    • Gunawardena, S.1    Goldstein, L.S.2
  • 48
    • 3142516228 scopus 로고    scopus 로고
    • Microtubule-dependent transport in neurons: Steps towards an understanding of regulation, function and dysfunction
    • Guzik B. W. and Goldstein L. S. (2004) Microtubule-dependent transport in neurons: steps towards an understanding of regulation, function and dysfunction. Curr. Opin. Cell Biol. 16, 443-450.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 443-450
    • Guzik, B.W.1    Goldstein, L.S.2
  • 49
    • 0035341254 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in Alzheimer's disease
    • Hirai K., Aliev G., Nunomura A. et al. (2001) Mitochondrial abnormalities in Alzheimer's disease. J. Neurosci. 21, 3017-3023.
    • (2001) J. Neurosci. , vol.21 , pp. 3017-3023
    • Hirai, K.1    Aliev, G.2    Nunomura, A.3
  • 50
    • 25444467721 scopus 로고    scopus 로고
    • Functional genomics meets neurodegenerative disorders. Part II: Transcriptomic and proteomic technology
    • Hoerndli F., David D. C. and Gotz J. (2005) Functional genomics meets neurodegenerative disorders. Part II: transcriptomic and proteomic technology. Prog. Neurobiol. 76, 169-188.
    • (2005) Prog. Neurobiol. , vol.76 , pp. 169-188
    • Hoerndli, F.1    David, D.C.2    Gotz, J.3
  • 51
    • 0031914718 scopus 로고    scopus 로고
    • Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes
    • Holcomb L., Gordon M. N., McGowan E. et al. (1998) Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes. Nat. Med. 4, 97-100.
    • (1998) Nat. Med. , vol.4 , pp. 97-100
    • Holcomb, L.1    Gordon, M.N.2    McGowan, E.3
  • 52
    • 28444496758 scopus 로고    scopus 로고
    • APLIP1, a kinesin binding JIP-1/JNK scaffold protein, influences the axonal transport of both vesicles and mitochondria in Drosophila
    • Horiuchi D., Barkus R. V., Pilling A. D., Gassman A. and Saxton W. M. (2005) APLIP1, a kinesin binding JIP-1/JNK scaffold protein, influences the axonal transport of both vesicles and mitochondria in Drosophila. Curr. Biol. 15, 2137-2141.
    • (2005) Curr. Biol. , vol.15 , pp. 2137-2141
    • Horiuchi, D.1    Barkus, R.V.2    Pilling, A.D.3    Gassman, A.4    Saxton, W.M.5
  • 53
    • 0029911064 scopus 로고    scopus 로고
    • Kinesin mutations cause motor neuron disease phenotypes by disrupting fast axonal transport in Drosophila
    • Hurd D. D. and Saxton W. M. (1996) Kinesin mutations cause motor neuron disease phenotypes by disrupting fast axonal transport in Drosophila. Genetics 144, 1075-1085.
    • (1996) Genetics , vol.144 , pp. 1075-1085
    • Hurd, D.D.1    Saxton, W.M.2
  • 54
    • 0030068390 scopus 로고    scopus 로고
    • Mutation of the axonal transport motor kinesin enhances paralytic and suppresses Shaker in Drosophila
    • Hurd D. D., Stern M. and Saxton W. M. (1996) Mutation of the axonal transport motor kinesin enhances paralytic and suppresses Shaker in Drosophila. Genetics 142, 195-204.
    • (1996) Genetics , vol.142 , pp. 195-204
    • Hurd, D.D.1    Stern, M.2    Saxton, W.M.3
  • 55
    • 0034721842 scopus 로고    scopus 로고
    • Maturation and endosomal targeting of beta-site amyloid precursor protein-cleaving enzyme. The Alzheimer's disease beta-secretase
    • Huse J. T., Pijak D. S., Leslie G. J., Lee V. M. and Doms R. W. (2000) Maturation and endosomal targeting of beta-site amyloid precursor protein-cleaving enzyme. The Alzheimer's disease beta-secretase. J. Biol. Chem. 275, 33 729-33 737.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33729-33737
    • Huse, J.T.1    Pijak, D.S.2    Leslie, G.J.3    Lee, V.M.4    Doms, R.W.5
  • 56
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
    • Hutton M., Lendon C. L., Rizzu P. et al. (1998) Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 393, 702-705.
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3
  • 57
    • 11144283513 scopus 로고    scopus 로고
    • Transcriptional and conformational changes of the tau molecule in Alzheimer's disease
    • Hyman B. T., Augustinack J. C. and Ingelsson M. (2005) Transcriptional and conformational changes of the tau molecule in Alzheimer's disease. Biochim. Biophys. Acta 1739, 150-157.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 150-157
    • Hyman, B.T.1    Augustinack, J.C.2    Ingelsson, M.3
  • 58
    • 0035060129 scopus 로고    scopus 로고
    • PHF and PHF-like fibrils - Cause or consequence?
    • Ihara Y. (2001) PHF and PHF-like fibrils - cause or consequence? Neurobiol. Aging 22, 123-126.
    • (2001) Neurobiol. Aging , vol.22 , pp. 123-126
    • Ihara, Y.1
  • 59
    • 0038603918 scopus 로고    scopus 로고
    • A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1
    • Inomata H., Nakamura Y., Hayakawa A., Takata H., Suzuki T., Miyazawa K. and Kitamura N. (2003) A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1. J. Biol. Chem. 278, 22 946-22 955.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22946-22955
    • Inomata, H.1    Nakamura, Y.2    Hayakawa, A.3    Takata, H.4    Suzuki, T.5    Miyazawa, K.6    Kitamura, N.7
  • 60
    • 0033230886 scopus 로고    scopus 로고
    • Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform
    • Ishihara T., Hong M., Zhang B., Nakagawa Y., Lee M. K., Trojanowski J. Q. and Lee V. M. (1999) Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform. Neuron 24, 751-762.
    • (1999) Neuron , vol.24 , pp. 751-762
    • Ishihara, T.1    Hong, M.2    Zhang, B.3    Nakagawa, Y.4    Lee, M.K.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 61
    • 0035134081 scopus 로고    scopus 로고
    • Age-dependent induction of congophilic neurofibrillary tau inclusions in tau transgenic mice
    • Ishihara T., Zhang B., Higuchi M., Yoshiyama Y., Trojanowski J. Q. and Lee V. M. (2001) Age-dependent induction of congophilic neurofibrillary tau inclusions in tau transgenic mice. Am. J. Pathol. 158, 555-562.
    • (2001) Am. J. Pathol. , vol.158 , pp. 555-562
    • Ishihara, T.1    Zhang, B.2    Higuchi, M.3    Yoshiyama, Y.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 62
    • 0034075589 scopus 로고    scopus 로고
    • Axonal membrane proteins are transported in distinct carriers: A two-color video microscopy study in cultured hippocampal neurons
    • Kaether C., Skehel P. and Dotti C. G. (2000) Axonal membrane proteins are transported in distinct carriers: a two-color video microscopy study in cultured hippocampal neurons. Mol. Biol. Cell 11, 1213-1224.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1213-1224
    • Kaether, C.1    Skehel, P.2    Dotti, C.G.3
  • 63
    • 0033636136 scopus 로고    scopus 로고
    • Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-1
    • Kamal A., Stokin G. B., Yang Z., Xia C. H. and Goldstein L. S. (2000) Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-1. Neuron 28, 449-459.
    • (2000) Neuron , vol.28 , pp. 449-459
    • Kamal, A.1    Stokin, G.B.2    Yang, Z.3    Xia, C.H.4    Goldstein, L.S.5
  • 64
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP
    • Kamal A., Almenar-Queralt A., LeBlanc J. F., Roberts E. A. and Goldstein L. S. (2001) Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP. Nature 414, 643-648.
    • (2001) Nature , vol.414 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    LeBlanc, J.F.3    Roberts, E.A.4    Goldstein, L.S.5
  • 67
    • 26444435322 scopus 로고    scopus 로고
    • Notch interferes with the scaffold function of JNK-interacting protein 1 to inhibit the JNK signaling pathway
    • Kim J. W., Kim M. J., Kim K. J. et al. (2005) Notch interferes with the scaffold function of JNK-interacting protein 1 to inhibit the JNK signaling pathway. Proc. Natl Acad. Sci. USA 102, 14 308-14 313.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14308-14313
    • Kim, J.W.1    Kim, M.J.2    Kim, K.J.3
  • 68
    • 11844251260 scopus 로고    scopus 로고
    • Regulation of gene expression by the amyloid precursor protein: Inhibition of the JNK/c-Jun pathway
    • Kogel D., Schomburg R., Copanaki E. and Prehn J. H. (2005) Regulation of gene expression by the amyloid precursor protein: inhibition of the JNK/c-Jun pathway. Cell Death Differ. 12, 1-9.
    • (2005) Cell Death Differ. , vol.12 , pp. 1-9
    • Kogel, D.1    Schomburg, R.2    Copanaki, E.3    Prehn, J.H.4
  • 69
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • Koo E. H. and Squazzo S. L. (1994) Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J. Biol. Chem. 269, 17 386-17 389.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 71
    • 0027361281 scopus 로고
    • Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • Kopke E., Tung Y. C., Shaikh S., Alonso A. C., Iqbal K. and Grundke-Iqbal I. (1993) Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J. Biol. Chem. 268, 24 374-24 384.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24374-24384
    • Kopke, E.1    Tung, Y.C.2    Shaikh, S.3    Alonso, A.C.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 72
    • 0036955813 scopus 로고    scopus 로고
    • Neuron loss from the hippocampus of Alzheimer's disease exceeds extracellular neurofibrillary tangle formation
    • Kril J. J., Patel S., Harding A. J. and Halliday G. M. (2002) Neuron loss from the hippocampus of Alzheimer's disease exceeds extracellular neurofibrillary tangle formation. Acta Neuropathol. (Berl.) 103, 370-376.
    • (2002) Acta Neuropathol. (Berl.) , vol.103 , pp. 370-376
    • Kril, J.J.1    Patel, S.2    Harding, A.J.3    Halliday, G.M.4
  • 74
    • 0037111837 scopus 로고    scopus 로고
    • Evidence that synaptically released beta-amyloid accumulates as extracellular deposits in the hippocampus of transgenic mice
    • Lazarov O., Lee M., Peterson D. A. and Sisodia S. S. (2002) Evidence that synaptically released beta-amyloid accumulates as extracellular deposits in the hippocampus of transgenic mice. J. Neurosci. 22, 9785-9793.
    • (2002) J. Neurosci. , vol.22 , pp. 9785-9793
    • Lazarov, O.1    Lee, M.2    Peterson, D.A.3    Sisodia, S.S.4
  • 75
    • 20044396527 scopus 로고    scopus 로고
    • Axonal transport, amyloid precursor protein, kinesin-1, and the processing apparatus: Revisited
    • Lazarov O., Morfini G. A., Lee E. B. et al. (2005) Axonal transport, amyloid precursor protein, kinesin-1, and the processing apparatus: revisited. J. Neurosci. 25, 2386-2395.
    • (2005) J. Neurosci. , vol.25 , pp. 2386-2395
    • Lazarov, O.1    Morfini, G.A.2    Lee, E.B.3
  • 76
    • 0026704256 scopus 로고
    • Expression of tau protein in non-neuronal cells: Microtubule binding and stabilization
    • Lee G. and Rook S. L. (1992) Expression of tau protein in non-neuronal cells: microtubule binding and stabilization. J. Cell Sci. 102, 227-237.
    • (1992) J. Cell Sci. , vol.102 , pp. 227-237
    • Lee, G.1    Rook, S.L.2
  • 77
    • 0028326935 scopus 로고
    • Visual cortex in Alzheimer's disease: Occurrence of neuronal death and glial proliferation, and correlation with pathological hallmarks
    • Leuba G. and Kraftsik R. (1994) Visual cortex in Alzheimer's disease: occurrence of neuronal death and glial proliferation, and correlation with pathological hallmarks. Neurobiol. Aging 15, 29-43.
    • (1994) Neurobiol. Aging , vol.15 , pp. 29-43
    • Leuba, G.1    Kraftsik, R.2
  • 78
    • 0034426011 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein
    • Lewis J., McGowan E., Rockwood J. et al. (2000) Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat. Genet. 25, 402-405.
    • (2000) Nat. Genet. , vol.25 , pp. 402-405
    • Lewis, J.1    McGowan, E.2    Rockwood, J.3
  • 79
    • 28644449284 scopus 로고    scopus 로고
    • Amyloid precursor protein promotes post-developmental neunte arborization in the Drosophila brain
    • Leyssen M., Ayaz D., Hebert S. S., Reeve S., De Strooper B. and Hassan B. A. (2005) Amyloid precursor protein promotes post-developmental neunte arborization in the Drosophila brain. EMBO J. 24, 2944-2955.
    • (2005) EMBO J. , vol.24 , pp. 2944-2955
    • Leyssen, M.1    Ayaz, D.2    Hebert, S.S.3    Reeve, S.4    De Strooper, B.5    Hassan, B.A.6
  • 80
    • 0032079899 scopus 로고    scopus 로고
    • Post-translational processing and turnover kinetics of presynaptically targeted amyloid precursor superfamily proteins in the central nervous system
    • Lyckman A. W., Confaloni A. M., Thinakaran G., Sisodia S. S. and Moya K. L. (1998) Post-translational processing and turnover kinetics of presynaptically targeted amyloid precursor superfamily proteins in the central nervous system. J. Biol. Chem. 273, 11 100-11 106.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11100-11106
    • Lyckman, A.W.1    Confaloni, A.M.2    Thinakaran, G.3    Sisodia, S.S.4    Moya, K.L.5
  • 81
    • 0028803993 scopus 로고
    • Two actin binding proteins, actin-depolymerizing factor and cofilin are associated with Hirano bodies
    • Maciver S. K. and Harrington C. R. (1995) Two actin binding proteins, actin-depolymerizing factor and cofilin are associated with Hirano bodies. Neuroreport 6, 1985-1988.
    • (1995) Neuroreport , vol.6 , pp. 1985-1988
    • Maciver, S.K.1    Harrington, C.R.2
  • 82
    • 30544447666 scopus 로고    scopus 로고
    • β-Secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stree or amyloid β: A feedforward mechanism for alzheimer's disease
    • Maloney M. T., Minamide L. S., Kinley A. W., Boyle J. A. and Bamburg J. R. (2005) β-Secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stree or amyloid β: a feedforward mechanism for alzheimer's disease. J. Neurosci. 25, 11 313-11 321.
    • (2005) J. Neurosci. , vol.25 , pp. 11313-11321
    • Maloney, M.T.1    Minamide, L.S.2    Kinley, A.W.3    Boyle, J.A.4    Bamburg, J.R.5
  • 83
    • 0032741064 scopus 로고    scopus 로고
    • Cytoplasmic dynein, the dynactin complex, and kinesin are interdependent and essential for fast axonal transport
    • Martin M., Iyadurai S. J., Gassman A., Gindhart J. G. Jr, Hays T. S. and Saxton W. M. (1999) Cytoplasmic dynein, the dynactin complex, and kinesin are interdependent and essential for fast axonal transport. Mol. Biol. Cell 10, 3717-3728.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3717-3728
    • Martin, M.1    Iyadurai, S.J.2    Gassman, A.3    Gindhart Jr., J.G.4    Hays, T.S.5    Saxton, W.M.6
  • 86
    • 0141532147 scopus 로고    scopus 로고
    • Amyloid beta protein precursor (AbetaPP), but not AbetaPP-like protein 2, is bridged to the kinesin light chain by the scaffold protein JNK-interacting protein 1
    • Matsuda S., Matsuda Y. and D'Adamio L. (2003) Amyloid beta protein precursor (AbetaPP), but not AbetaPP-like protein 2, is bridged to the kinesin light chain by the scaffold protein JNK-interacting protein 1. J. Biol. Chem. 278, 38 601-38 606.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38601-38606
    • Matsuda, S.1    Matsuda, Y.2    D'Adamio, L.3
  • 87
    • 0025331812 scopus 로고
    • Spinal cord neurofibrillary tangles of Guamanian amyotrophic lateral sclerosis and parkinsonism-dementia complex: An immunohistochemical study
    • Matsumoto S., Hirano A. and Goto S. (1990) Spinal cord neurofibrillary tangles of Guamanian amyotrophic lateral sclerosis and parkinsonism-dementia complex: an immunohistochemical study. Neurology 40, 975-979.
    • (1990) Neurology , vol.40 , pp. 975-979
    • Matsumoto, S.1    Hirano, A.2    Goto, S.3
  • 88
    • 0034282106 scopus 로고    scopus 로고
    • Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function
    • Minamide L. S., Striegel A. M., Boyle J. A., Meberg P. J. and Bamburg J. R. (2000) Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat. Cell Biol. 2, 628-636.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 628-636
    • Minamide, L.S.1    Striegel, A.M.2    Boyle, J.A.3    Meberg, P.J.4    Bamburg, J.R.5
  • 89
    • 0027486263 scopus 로고
    • Interaction of the tail domain of high molecular weight subunits of neurofilaments with the COOH-terminal region of tubulin and its regulation by tau protein kinase II
    • Miyasaka H., Okabe S., Ishiguro K., Uchida T. and Hirokawa N. (1993) Interaction of the tail domain of high molecular weight subunits of neurofilaments with the COOH-terminal region of tubulin and its regulation by tau protein kinase II. J. Biol. Chem. 268, 22 695-22 702.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22695-22702
    • Miyasaka, H.1    Okabe, S.2    Ishiguro, K.3    Uchida, T.4    Hirokawa, N.5
  • 90
    • 0036469290 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility
    • Morfini G., Szebenyi G., Elluru R., Ratner N. and Brady S. T. (2002) Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility. EMBO J. 21, 281-293.
    • (2002) EMBO J. , vol.21 , pp. 281-293
    • Morfini, G.1    Szebenyi, G.2    Elluru, R.3    Ratner, N.4    Brady, S.T.5
  • 91
    • 0027254967 scopus 로고
    • Amyloid precursor protein is synthesized by retinal ganglion cells, rapidly transported to the optic nerve plasma membrane and nerve terminals, and metabolized
    • Morin P. J., Abraham C. R., Amaratunga A., Johnson R. J., Huber G., Sandell J. H. and Fine R. E. (1993) Amyloid precursor protein is synthesized by retinal ganglion cells, rapidly transported to the optic nerve plasma membrane and nerve terminals, and metabolized. J. Neurochem. 61, 464-473.
    • (1993) J. Neurochem. , vol.61 , pp. 464-473
    • Morin, P.J.1    Abraham, C.R.2    Amaratunga, A.3    Johnson, R.J.4    Huber, G.5    Sandell, J.H.6    Fine, R.E.7
  • 92
    • 0033028074 scopus 로고    scopus 로고
    • Neurons may live for decades with neurofibrillary tangles
    • Morsch R., Simon W. and Coleman P. D. (1999) Neurons may live for decades with neurofibrillary tangles. J. Neuropathol. Exp. Neurol. 58, 188-197.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 188-197
    • Morsch, R.1    Simon, W.2    Coleman, P.D.3
  • 93
    • 0027988072 scopus 로고
    • In vivo neuronal synthesis and axonal transport of Kunitz protease inhibitor (KPI)-containing forms of the amyloid precursor protein
    • Moya K. L., Confaloni A. M. and Allinquant B. (1994) In vivo neuronal synthesis and axonal transport of Kunitz protease inhibitor (KPI)-containing forms of the amyloid precursor protein. J. Neurochem. 63, 1971-1974.
    • (1994) J. Neurochem. , vol.63 , pp. 1971-1974
    • Moya, K.L.1    Confaloni, A.M.2    Allinquant, B.3
  • 94
    • 27944444156 scopus 로고    scopus 로고
    • 2-terminal kinase-interacting protein-1
    • 2-terminal kinase-interacting protein-1. J. Cell Biol. 171, 615-625.
    • (2005) J. Cell Biol. , vol.171 , pp. 615-625
    • Muresan, Z.1    Muresan, V.2
  • 95
    • 0032472369 scopus 로고    scopus 로고
    • The MAP kinase kinase kinase MLK2 co-localizes with activated JMC along microtubules and associates with kinesin superfamily motor KIF3
    • Nagata K., Puls A., Futter C., Aspenstrom P., Schaefer E., Nakata T., Hirokawa N. and Hall A. (1998) The MAP kinase kinase kinase MLK2 co-localizes with activated JMC along microtubules and associates with kinesin superfamily motor KIF3. EMBO J. 17, 149-158.
    • (1998) EMBO J. , vol.17 , pp. 149-158
    • Nagata, K.1    Puls, A.2    Futter, C.3    Aspenstrom, P.4    Schaefer, E.5    Nakata, T.6    Hirokawa, N.7    Hall, A.8
  • 96
    • 0030061020 scopus 로고    scopus 로고
    • Hippocampal pathology reflects memory deficit and brain imaging measurements in Alzheimer's disease: Clinicopathologic correlations using three sets of pathologic diagnostic criteria
    • Nagy Z., Jobst K. A., Esiri M. M., Morris J. H., King E. M., MacDonald B., Litchfield S., Barnetson L. and Smith A. D. (1996) Hippocampal pathology reflects memory deficit and brain imaging measurements in Alzheimer's disease: clinicopathologic correlations using three sets of pathologic diagnostic criteria. Dementia 7, 76-81.
    • (1996) Dementia , vol.7 , pp. 76-81
    • Nagy, Z.1    Jobst, K.A.2    Esiri, M.M.3    Morris, J.H.4    King, E.M.5    MacDonald, B.6    Litchfield, S.7    Barnetson, L.8    Smith, A.D.9
  • 97
    • 0028641560 scopus 로고
    • KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria
    • Nangaku M., Sato-Yoshitake R., Okada Y., Noda Y., Takemura R., Yamazaki H. and Hirokawa N. (1994) KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria. Cell 79, 1209-1220.
    • (1994) Cell , vol.79 , pp. 1209-1220
    • Nangaku, M.1    Sato-Yoshitake, R.2    Okada, Y.3    Noda, Y.4    Takemura, R.5    Yamazaki, H.6    Hirokawa, N.7
  • 98
    • 27144469504 scopus 로고    scopus 로고
    • Different tau epitopes define Abeta(42)-mediated tau insolubility
    • Pennanen L. and Gotz J. (2005) Different tau epitopes define Abeta(42)-mediated tau insolubility. Biochem. Biophys. Res. Commun. 337, 1097-1101.
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 1097-1101
    • Pennanen, L.1    Gotz, J.2
  • 99
    • 33646759268 scopus 로고    scopus 로고
    • Kinesin-1 and dynein are the primary motors for fast transport of mitochondria in Drosophila motor axons
    • Pilling A. D., Horiuchi D., Lively C. M. and Saxton W. M. (2006) Kinesin-1 and dynein are the primary motors for fast transport of mitochondria in Drosophila motor axons. Mol. Biol. Cell 17, 2057-2068.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2057-2068
    • Pilling, A.D.1    Horiuchi, D.2    Lively, C.M.3    Saxton, W.M.4
  • 101
    • 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 M. A., Richey P. L., Vinters H. V. and 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
  • 102
    • 0342803685 scopus 로고    scopus 로고
    • Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein
    • Probst A., Gotz J., Wiederhold K. H. et al. (2000) Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein. Acta Neuropathol. (Berl.) 99, 469-481.
    • (2000) Acta Neuropathol. (Berl.) , vol.99 , pp. 469-481
    • Probst, A.1    Gotz, J.2    Wiederhold, K.H.3
  • 103
    • 0037417899 scopus 로고    scopus 로고
    • Dentate gyrus volume is reduced before onset of plaque formation in PDAPP mice: A magnetic resonance microscopy and stereologic analysis
    • Redwine J. M., Kosofsky B., Jacobs R. E., Games D., Reilly J. F., Morrison J. H., Young W. G. and Bloom F. E. (2003) Dentate gyrus volume is reduced before onset of plaque formation in PDAPP mice: a magnetic resonance microscopy and stereologic analysis. Proc. Natl Acad. Sci. USA 100, 1381-1386.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1381-1386
    • Redwine, J.M.1    Kosofsky, B.2    Jacobs, R.E.3    Games, D.4    Reilly, J.F.5    Morrison, J.H.6    Young, W.G.7    Bloom, F.E.8
  • 104
    • 28644437291 scopus 로고    scopus 로고
    • The amyloid-beta precursor protein: Integrating structure with biological function
    • Reinhard C., Hebert S. S. and De Strooper B. (2005) The amyloid-beta precursor protein: integrating structure with biological function. EMBO J. 24, 3996-4006.
    • (2005) EMBO J. , vol.24 , pp. 3996-4006
    • Reinhard, C.1    Hebert, S.S.2    De Strooper, B.3
  • 105
    • 1842432582 scopus 로고    scopus 로고
    • MAP2c but not tau binds and bundles F-actin via its microtubule binding domain
    • Roger B., Al Bassam J., Dehmelt L., Milligan R. A. and Halpain S. (2004) MAP2c but not tau binds and bundles F-actin via its microtubule binding domain. Curr. Biol. 14, 363-371.
    • (2004) Curr. Biol. , vol.14 , pp. 363-371
    • Roger, B.1    Al Bassam, J.2    Dehmelt, L.3    Milligan, R.A.4    Halpain, S.5
  • 106
    • 18544386562 scopus 로고    scopus 로고
    • Increased a beta peptides and reduced cholesterol and myelin proteins characterize white matter degeneration in Alzheimer's disease
    • Roher A. E., Weiss N., Kokjohn T. A., et al. (2002) Increased A beta peptides and reduced cholesterol and myelin proteins characterize white matter degeneration in Alzheimer's disease. Biochemistry 41, 11 080-11 090.
    • (2002) Biochemistry , vol.41 , pp. 11080-11090
    • Roher, A.E.1    Weiss, N.2    Kokjohn, T.A.3
  • 109
    • 12844277941 scopus 로고    scopus 로고
    • The Caenorhabditis elegans UNC-14 RUN domain protein binds to the kinesin-1 and UNC-16 complex and regulates synaptic vesicle localization
    • Sakamoto R., Byrd D. T., Brown H. M., Hisamoto N., Matsumoto K. and Jin Y. (2005) The Caenorhabditis elegans UNC-14 RUN domain protein binds to the kinesin-1 and UNC-16 complex and regulates synaptic vesicle localization. Mol. Biol. Cell 16, 483-496.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 483-496
    • Sakamoto, R.1    Byrd, D.T.2    Brown, H.M.3    Hisamoto, N.4    Matsumoto, K.5    Jin, Y.6
  • 110
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • Santacruz K., Lewis J., Spires T. et al. (2005) Tau suppression in a neurodegenerative mouse model improves memory function. Science 309, 476-481.
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1    Lewis, J.2    Spires, T.3
  • 111
    • 0026096809 scopus 로고
    • Kinesin heavy chain is essential for viability and neuromuscular functions in Drosophila, but mutants show no defects in mitosis
    • Saxton W. M., Hicks J., Goldstein L. S. and Raff E. C. (1991) Kinesin heavy chain is essential for viability and neuromuscular functions in Drosophila, but mutants show no defects in mitosis. Cell 64, 1093-1102.
    • (1991) Cell , vol.64 , pp. 1093-1102
    • Saxton, W.M.1    Hicks, J.2    Goldstein, L.S.3    Raff, E.C.4
  • 112
    • 0025217385 scopus 로고
    • Quantitative assessment of cortical synaptic density in Alzheimer's disease
    • Scheff S. W., DeKosky S. T. and Price D. A. (1990) Quantitative assessment of cortical synaptic density in Alzheimer's disease. Neurobiol. Aging 11, 29-37.
    • (1990) Neurobiol. Aging , vol.11 , pp. 29-37
    • Scheff, S.W.1    DeKosky, S.T.2    Price, D.A.3
  • 113
    • 0034626853 scopus 로고    scopus 로고
    • Tau epitopes in spinal cord neurofibrillary lesions in Chamorros of Guam
    • Schmidt M. L., Garruto R., Chen J., Lee V. M. and Trojanowski J. Q. (2000) Tau epitopes in spinal cord neurofibrillary lesions in Chamorros of Guam. Neuroreport 11, 3427-3430.
    • (2000) Neuroreport , vol.11 , pp. 3427-3430
    • Schmidt, M.L.1    Garruto, R.2    Chen, J.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 114
    • 0037119947 scopus 로고    scopus 로고
    • Single-molecule investigation of the interference between kinesin, tau and MAP2c
    • Seitz A., Kojima H., Oiwa K., Mandelkow E. M., Song Y. H. and Mandelkow E. (2002) Single-molecule investigation of the interference between kinesin, tau and MAP2c. EMBO J. 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
  • 115
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe D. J. (2001) Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81, 741-766.
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 116
    • 0842320909 scopus 로고    scopus 로고
    • The beta-amyloid-related proteins presenilin 1 and BACE1 are axonally transported to nerve terminals in the brain
    • Sheng J. G., Price D. L. and Koliatsos V. E. (2003) The beta-amyloid-related proteins presenilin 1 and BACE1 are axonally transported to nerve terminals in the brain. Exp. Neurol. 184, 1053-1057.
    • (2003) Exp. Neurol. , vol.184 , pp. 1053-1057
    • Sheng, J.G.1    Price, D.L.2    Koliatsos, V.E.3
  • 117
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • Sherrington R., Rogaev E. I., Liang Y. et al. (1995) Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 375, 754-760.
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3
  • 119
    • 0028988649 scopus 로고
    • Intracellular routing of human amyloid protein precursor: Axonal delivery followed by transport to the dendrites
    • Simons M., Ikonen E., Tienari P. J., Cid-Arregui A., Monning U., Beyreuther K. and Dotti C. G. (1995) Intracellular routing of human amyloid protein precursor: axonal delivery followed by transport to the dendrites. J. Neurosci. Res. 41, 121-128.
    • (1995) J. Neurosci. Res. , vol.41 , pp. 121-128
    • Simons, M.1    Ikonen, E.2    Tienari, P.J.3    Cid-Arregui, A.4    Monning, U.5    Beyreuther, K.6    Dotti, C.G.7
  • 120
    • 0027212769 scopus 로고
    • Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system
    • Sisodia S. S., Koo E. H., Hoffman P. N., Perry G. and Price D. L. (1993) Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system. J. Neurosci. 13, 3136-3142.
    • (1993) J. Neurosci. , vol.13 , pp. 3136-3142
    • Sisodia, S.S.1    Koo, E.H.2    Hoffman, P.N.3    Perry, G.4    Price, D.L.5
  • 121
    • 0034723418 scopus 로고    scopus 로고
    • Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network
    • Skovronsky D. M., Moore D. B., Milla M. E., Doms R. W. and Lee V. M. (2000) Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network. J. Biol. Chem. 275, 2568-2575.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2568-2575
    • Skovronsky, D.M.1    Moore, D.B.2    Milla, M.E.3    Doms, R.W.4    Lee, V.M.5
  • 122
    • 0037404532 scopus 로고    scopus 로고
    • Amyloid beta accumulation in axons after traumatic brain injury in humans
    • Smith D. H., Chen X. H., Iwata A. and Graham D. I. (2003) Amyloid beta accumulation in axons after traumatic brain injury in humans. J. Neurosurg. 98, 1072-1077.
    • (2003) J. Neurosurg. , vol.98 , pp. 1072-1077
    • Smith, D.H.1    Chen, X.H.2    Iwata, A.3    Graham, D.I.4
  • 124
    • 23444448170 scopus 로고    scopus 로고
    • Dendritic spine abnormalities in amyloid precursor protein transgenic mice demonstrated by gene transfer and intravital multiphoton microscopy
    • Spires T. L., Meyer-Luehmann M., Stern E. A., McLean P. J., Skoch J., Nguyen P. T., Bacskai B. J. and Hyman B. T. (2005) Dendritic spine abnormalities in amyloid precursor protein transgenic mice demonstrated by gene transfer and intravital multiphoton microscopy. J. Neurosci. 25, 7278-7287.
    • (2005) J. Neurosci. , vol.25 , pp. 7278-7287
    • Spires, T.L.1    Meyer-Luehmann, M.2    Stern, E.A.3    McLean, P.J.4    Skoch, J.5    Nguyen, P.T.6    Bacskai, B.J.7    Hyman, B.T.8
  • 125
    • 0032786370 scopus 로고    scopus 로고
    • Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein
    • Spittaels K., Van den Haute C., Van Dorpe J. et al. (1999) Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein. Am. J. Pathol. 155, 2153-2165.
    • (1999) Am. J. Pathol. , vol.155 , pp. 2153-2165
    • Spittaels, K.1    Van Den Haute, C.2    Van Dorpe, J.3
  • 126
    • 0034731461 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta phosphorylates protein tau and rescues the axonopathy in the central nervous system of human four-repeat tau transgenic mice
    • Spittaels K., Van Den Haute C., Van Dorpe J. et al. (2000) Glycogen synthase kinase-3beta phosphorylates protein tau and rescues the axonopathy in the central nervous system of human four-repeat tau transgenic mice. J. Biol. Chem. 275, 41 340-41 349.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41340-41349
    • Spittaels, K.1    Van Den Haute, C.2    Van Dorpe, J.3
  • 127
    • 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. and Mandelkow E. M. (2002) Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J. Cell Biol. 156, 1051-1063.
    • (2002) J. Cell Biol. , vol.156 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 128
    • 20044385920 scopus 로고    scopus 로고
    • Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease
    • Stokin G. B., Lillo C., Falzone T. L. et al. (2005) Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease. Science 307, 1282-1288.
    • (2005) Science , vol.307 , pp. 1282-1288
    • Stokin, G.B.1    Lillo, C.2    Falzone, T.L.3
  • 129
    • 0034698233 scopus 로고    scopus 로고
    • Antibodies to the C-terminus of the beta-amyloid precursor protein (APP): A site specific marker for the detection of traumatic axonal injury
    • Stone J. R., Singleton R. H. and Povlishock J. T. (2000) Antibodies to the C-terminus of the beta-amyloid precursor protein (APP): a site specific marker for the detection of traumatic axonal injury. Brain Res. 871, 288-302.
    • (2000) Brain Res. , vol.871 , pp. 288-302
    • Stone, J.R.1    Singleton, R.H.2    Povlishock, J.T.3
  • 130
    • 0014193263 scopus 로고
    • Fine structural localization of acid phosphatase in senile plaques in Alzheimer's presenile dementia
    • Suzuki K. and Terry R. D. (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
  • 131
    • 32344435520 scopus 로고    scopus 로고
    • Molecular mechanisms of dendritic spine morphogenesis
    • Tada T. and Sheng M. (2006) Molecular mechanisms of dendritic spine morphogenesis. Curr. Opin. Neurobiol. 16, 95-101.
    • (2006) Curr. Opin. Neurobiol. , vol.16 , pp. 95-101
    • Tada, T.1    Sheng, M.2
  • 132
    • 0029788486 scopus 로고    scopus 로고
    • Differential axonal transport of soluble and insoluble tau in the rat sciatic nerve
    • Tashiro T., Sun X., Tsuda M. and Komiya Y. (1996) Differential axonal transport of soluble and insoluble tau in the rat sciatic nerve. J. Neurochem. 67, 1566-1574.
    • (1996) J. Neurochem. , vol.67 , pp. 1566-1574
    • Tashiro, T.1    Sun, X.2    Tsuda, M.3    Komiya, Y.4
  • 133
    • 0029795197 scopus 로고    scopus 로고
    • The pathogenesis of Alzheimer disease: An alternative to the amyloid hypothesis
    • Terry R. D. (1996) The pathogenesis of Alzheimer disease: an alternative to the amyloid hypothesis. J. Neuropathol. Exp. Neurol. 55, 1023-1025.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 1023-1025
    • Terry, R.D.1
  • 134
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry R. D., Masliah E., Salmon D. P., Butters N., DeTeresa R., Hill R., Hansen L. A. and Katzman R. (1991) Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol. 30, 572-580.
    • (1991) Ann. Neurol. , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    DeTeresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 135
    • 10144263284 scopus 로고    scopus 로고
    • The beta-amyloid domain is essential for axonal sorting of amyloid precursor protein
    • Tienari P. J., De Strooper B., Ikonen E. et al. (1996) The beta-amyloid domain is essential for axonal sorting of amyloid precursor protein. EMBO J. 15, 5218-5229.
    • (1996) EMBO J. , vol.15 , pp. 5218-5229
    • Tienari, P.J.1    De Strooper, B.2    Ikonen, E.3
  • 136
    • 0033529031 scopus 로고    scopus 로고
    • Neuronal overexpression of APPL, the Drosophila homologue of the amyloid precursor protein (APP), disrupts axonal transport
    • Torroja L., Chu H., Kotovsky I. and White K. (1999) Neuronal overexpression of APPL, the Drosophila homologue of the amyloid precursor protein (APP), disrupts axonal transport. Curr. Biol. 9, 489-492.
    • (1999) Curr. Biol. , vol.9 , pp. 489-492
    • Torroja, L.1    Chu, H.2    Kotovsky, I.3    White, K.4
  • 138
    • 0032799381 scopus 로고    scopus 로고
    • Tau regulates the attachment/detachment but not the speed of motors in microtubule-dependent transport of single vesicles and organelles
    • Trinczek B., Ebneth A., Mandelkow E. M. and Mandelkow E. (1999) Tau regulates the attachment/detachment but not the speed of motors in microtubule-dependent transport of single vesicles and organelles. J. Cell Sci. 112, 2355-2367.
    • (1999) J. Cell Sci. , vol.112 , pp. 2355-2367
    • Trinczek, B.1    Ebneth, A.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 140
    • 0021849732 scopus 로고
    • Organelle, bead, and microtubule translocations promoted by soluble factors from the squid giant axon
    • Vale R. D., Schnapp B. J., Reese T. S. and SheetZ. M. P. (1985) Organelle, bead, and microtubule translocations promoted by soluble factors from the squid giant axon. Cell 40, 559-569.
    • (1985) Cell , vol.40 , pp. 559-569
    • Vale, R.D.1    Schnapp, B.J.2    Reese, T.S.3    Sheet, Z.M.P.4
  • 142
    • 0033595706 scopus 로고    scopus 로고
    • Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar R., Bennett B. D., Babu-Khan S. et al. (1999) Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286, 735-741.
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3
  • 143
    • 0347930372 scopus 로고    scopus 로고
    • Genetics, lifestyle and the roles of amyloid beta and oxidative stress in Alzheimer's disease
    • Veurink G., Fuller S. J., Atwood C. S. and Martins R. N. (2003) Genetics, lifestyle and the roles of amyloid beta and oxidative stress in Alzheimer's disease. Ann. Hum. Biol. 30, 639-667.
    • (2003) Ann. Hum. Biol. , vol.30 , pp. 639-667
    • Veurink, G.1    Fuller, S.J.2    Atwood, C.S.3    Martins, R.N.4
  • 145
    • 0033675163 scopus 로고    scopus 로고
    • Dissecting the behaviour of transgenic mice: Is it the mutation, the genetic background, or the environment?
    • Wolfer D. P. and Lipp H. P. (2000) Dissecting the behaviour of transgenic mice: is it the mutation, the genetic background, or the environment? Exp. Physiol. 85, 627-634.
    • (2000) Exp. Physiol. , vol.85 , pp. 627-634
    • Wolfer, D.P.1    Lipp, H.P.2
  • 146
    • 0030825372 scopus 로고    scopus 로고
    • Amyloid precursor protein accumulates in white matter at the margin of a focal ischaemic lesion
    • Yam P. S., Takasago T., Dewar D., Graham D. I. and McCulloch J. (1997) Amyloid precursor protein accumulates in white matter at the margin of a focal ischaemic lesion. Brain Res. 760, 150-157.
    • (1997) Brain Res. , vol.760 , pp. 150-157
    • Yam, P.S.1    Takasago, T.2    Dewar, D.3    Graham, D.I.4    McCulloch, J.5
  • 147
    • 0028913471 scopus 로고
    • Trafficking of cell surface beta-amyloid precursor protein: Retrograde and transcytotic transport in cultured neurons
    • Yamazaki T., Selkoe D. J. and Koo E. H. (1995) Trafficking of cell surface beta-amyloid precursor protein: retrograde and transcytotic transport in cultured neurons. J. Cell Biol. 129, 431-442.
    • (1995) J. Cell Biol. , vol.129 , pp. 431-442
    • Yamazaki, T.1    Selkoe, D.J.2    Koo, E.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.