메뉴 건너뛰기




Volumn 21, Issue 21, 2012, Pages 4587-4601

Enhanced β-secretase processing alters APP axonal transport and leads to axonal defects

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; BETA SECRETASE INHIBITOR; GAMMA SECRETASE INHIBITOR;

EID: 84867766569     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/dds297     Document Type: Article
Times cited : (44)

References (85)
  • 1
    • 0036883539 scopus 로고    scopus 로고
    • Presenilin-1 and the amyloid precursor protein are transported bidirectionally in the sciatic nerve of adult rat
    • Papp, H., Pakaski, M. and Kasa, P. (2002) Presenilin-1 and the amyloid precursor protein are transported bidirectionally in the sciatic nerve of adult rat. Neurochem. Int., 41, 429-435.
    • (2002) Neurochem. Int. , vol.41 , pp. 429-435
    • Papp, H.1    Pakaski, M.2    Kasa, P.3
  • 2
    • 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
  • 3
    • 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
  • 4
    • 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
  • 6
    • 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
  • 7
    • 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
  • 8
    • 63849105306 scopus 로고    scopus 로고
    • The cleavage products of amyloid-beta precursor protein are sorted to distinct carrier vesicles that are independently transported within neurites
    • Muresan, V., Varvel, N.H., Lamb, B.T. and Muresan, Z. (2009) The cleavage products of amyloid-beta precursor protein are sorted to distinct carrier vesicles that are independently transported within neurites. J. Neurosci., 29, 3565-3578.
    • (2009) J. Neurosci. , vol.29 , pp. 3565-3578
    • Muresan, V.1    Varvel, N.H.2    Lamb, B.T.3    Muresan, Z.4
  • 12
    • 0033549485 scopus 로고    scopus 로고
    • Drosophila roadblock and Chlamydomonas LC7: a conserved family of dynein-associated proteins involved in axonal transport, flagellar motility, and mitosis
    • Bowman, A.B., Patel-King, R.S., Benashski, S.E., McCaffery, J.M., Goldstein, L.S. and King, S.M. (1999) Drosophila roadblock and Chlamydomonas LC7: a conserved family of dynein-associated proteins involved in axonal transport, flagellar motility, and mitosis. J. Cell Biol., 146, 165-180.
    • (1999) J. Cell Biol. , vol.146 , pp. 165-180
    • Bowman, A.B.1    Patel-King, R.S.2    Benashski, S.E.3    McCaffery, J.M.4    Goldstein, L.S.5    King, S.M.6
  • 13
    • 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
  • 14
    • 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
  • 16
    • 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
  • 17
    • 0028866435 scopus 로고
    • The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway
    • Haass, C., Lemere, C.A., Capell, A., Citron, M., Seubert, P., Schenk, D., Lannfelt, L. and Selkoe, D.J. (1995) The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway. Nat. Med., 1, 1291-1296.
    • (1995) Nat. Med. , vol.1 , pp. 1291-1296
    • Haass, C.1    Lemere, C.A.2    Capell, A.3    Citron, M.4    Seubert, P.5    Schenk, D.6    Lannfelt, L.7    Selkoe, D.J.8
  • 18
    • 0242267132 scopus 로고    scopus 로고
    • Proteolytic processing of the Alzheimer's disease amyloid precursor protein in brain and platelets
    • Evin, G., Zhu, A., Holsinger, R.M., Masters, C.L. and Li, Q.X. (2003) Proteolytic processing of the Alzheimer's disease amyloid precursor protein in brain and platelets. J. Neurosci. Res., 74, 386-392.
    • (2003) J. Neurosci. Res. , vol.74 , pp. 386-392
    • Evin, G.1    Zhu, A.2    Holsinger, R.M.3    Masters, C.L.4    Li, Q.X.5
  • 20
    • 0036260892 scopus 로고    scopus 로고
    • Increased expression of the amyloid precursor beta-secretase in Alzheimer's disease
    • Holsinger, R.M., McLean, C.A., Beyreuther, K., Masters, C.L. and Evin, G. (2002) Increased expression of the amyloid precursor beta-secretase in Alzheimer's disease. Ann. Neurol., 51, 783-786.
    • (2002) Ann. Neurol. , vol.51 , pp. 783-786
    • Holsinger, R.M.1    McLean, C.A.2    Beyreuther, K.3    Masters, C.L.4    Evin, G.5
  • 22
    • 0033869715 scopus 로고    scopus 로고
    • Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations
    • Cataldo, A.M., Peterhoff, C.M., Troncoso, J.C., Gomez-Isla, T., Hyman, B.T. and Nixon, R.A. (2000) Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations. Am. J. Pathol., 157, 277-286.
    • (2000) Am. J. Pathol. , vol.157 , pp. 277-286
    • Cataldo, A.M.1    Peterhoff, C.M.2    Troncoso, J.C.3    Gomez-Isla, T.4    Hyman, B.T.5    Nixon, R.A.6
  • 23
    • 33847194657 scopus 로고    scopus 로고
    • Axonal accumulation of synaptic markers in APP transgenic Drosophila depends on the NPTY motif and is paralleled by defects in synaptic plasticity
    • Rusu, P., Jansen, A., Soba, P., Kirsch, J., Lower, A., Merdes, G., Kuan, Y.H., Jung, A., Beyreuther, K., Kjaerulff, O. et al. (2007) Axonal accumulation of synaptic markers in APP transgenic Drosophila depends on the NPTY motif and is paralleled by defects in synaptic plasticity. Eur. J. Neurosci., 25, 1079-1086.
    • (2007) Eur. J. Neurosci. , vol.25 , pp. 1079-1086
    • Rusu, P.1    Jansen, A.2    Soba, P.3    Kirsch, J.4    Lower, A.5    Merdes, G.6    Kuan, Y.H.7    Jung, A.8    Beyreuther, K.9    Kjaerulff, O.10
  • 25
    • 0033636136 scopus 로고    scopus 로고
    • Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I
    • 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-I. 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
  • 26
    • 33749854516 scopus 로고    scopus 로고
    • Acute impairment of mitochondrial trafficking by beta-amyloid peptides in hippocampal neurons
    • Rui, Y., Tiwari, P., Xie, Z. and Zheng, J.Q. (2006) Acute impairment of mitochondrial trafficking by beta-amyloid peptides in hippocampal neurons. J. Neurosci., 26, 10480-10487.
    • (2006) J. Neurosci. , vol.26 , pp. 10480-10487
    • Rui, Y.1    Tiwari, P.2    Xie, Z.3    Zheng, J.Q.4
  • 28
    • 77954466407 scopus 로고    scopus 로고
    • Amyloid-beta peptide oligomers disrupt axonal transport through an NMDA receptor-dependent mechanism that is mediated by glycogen synthase kinase 3beta in primary cultured hippocampal neurons
    • Decker, H., Lo, K.Y., Unger, S.M., Ferreira, S.T. and Silverman, M.A. (2010) Amyloid-beta peptide oligomers disrupt axonal transport through an NMDA receptor-dependent mechanism that is mediated by glycogen synthase kinase 3beta in primary cultured hippocampal neurons. J. Neurosci., 30, 9166-9171.
    • (2010) J. Neurosci. , vol.30 , pp. 9166-9171
    • Decker, H.1    Lo, K.Y.2    Unger, S.M.3    Ferreira, S.T.4    Silverman, M.A.5
  • 30
    • 0141864562 scopus 로고    scopus 로고
    • Glutamate and amyloid beta-protein rapidly inhibit fast axonal transport in cultured rat hippocampal neurons by different mechanisms
    • Hiruma, H., Katakura, T., Takahashi, S., Ichikawa, T. and Kawakami, T. (2003) Glutamate and amyloid beta-protein rapidly inhibit fast axonal transport in cultured rat hippocampal neurons by different mechanisms. J. Neurosci., 23, 8967-8977.
    • (2003) J. Neurosci. , vol.23 , pp. 8967-8977
    • Hiruma, H.1    Katakura, T.2    Takahashi, S.3    Ichikawa, T.4    Kawakami, T.5
  • 31
    • 0033621641 scopus 로고    scopus 로고
    • Human amyloid-beta1-42 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. and Yamaguchi, H. (2000) Human amyloid-beta1-42 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
  • 32
    • 79751537405 scopus 로고    scopus 로고
    • Amyloid beta impairs mitochondrial anterograde transport and degenerates synapses in Alzheimer's disease neurons
    • Calkins, M.J. and Reddy, P.H. (2011) Amyloid beta impairs mitochondrial anterograde transport and degenerates synapses in Alzheimer's disease neurons. Biochim. Biophys. Acta, 1812, 507-513.
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 507-513
    • Calkins, M.J.1    Reddy, P.H.2
  • 33
    • 0026907151 scopus 로고
    • A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid
    • Mullan, M., Crawford, F., Axelman, K., Houlden, H., Lilius, L., Winblad, B. and Lannfelt, L. (1992) A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid. Nat. Genet., 1, 345-347.
    • (1992) Nat. Genet. , vol.1 , pp. 345-347
    • Mullan, M.1    Crawford, F.2    Axelman, K.3    Houlden, H.4    Lilius, L.5    Winblad, B.6    Lannfelt, L.7
  • 34
    • 0028924248 scopus 로고
    • Generation of amyloid beta protein from its precursor is sequence specific
    • Citron, M., Teplow, D.B. and Selkoe, D.J. (1995) Generation of amyloid beta protein from its precursor is sequence specific. Neuron, 14, 661-670.
    • (1995) Neuron , vol.14 , pp. 661-670
    • Citron, M.1    Teplow, D.B.2    Selkoe, D.J.3
  • 38
    • 0028174753 scopus 로고
    • An extensive network of PHF tau-rich dystrophic neurites permeates neocortex and nearly all neuritic and diffuse amyloid plaques in Alzheimer disease
    • Schmidt, M.L., DiDario, A.G., Lee, V.M. and Trojanowski, J.Q. (1994) An extensive network of PHF tau-rich dystrophic neurites permeates neocortex and nearly all neuritic and diffuse amyloid plaques in Alzheimer disease. FEBS Lett., 344, 69-73.
    • (1994) FEBS Lett. , vol.344 , pp. 69-73
    • Schmidt, M.L.1    DiDario, A.G.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 40
    • 0024836809 scopus 로고
    • Dystrophic neuropeptidergic neurites in senile plaques of Alzheimer's disease precede formation of paired helical filaments
    • Lenders, M.B., Peers, M.C., Tramu, G., Delacourte, A., Defossez, A., Petit, H. and Mazzuca, M. (1989) Dystrophic neuropeptidergic neurites in senile plaques of Alzheimer's disease precede formation of paired helical filaments. Acta Neurol. Belg., 89, 279-285.
    • (1989) Acta Neurol. Belg. , vol.89 , pp. 279-285
    • Lenders, M.B.1    Peers, M.C.2    Tramu, G.3    Delacourte, A.4    Defossez, A.5    Petit, H.6    Mazzuca, M.7
  • 41
    • 0022595501 scopus 로고
    • Occurrence of neuropil threads in the senile human brain and in Alzheimer's disease: a third location of paired helical filaments outside of neurofibrillary tangles and neuritic plaques
    • Braak, H., Braak, E., Grundke-Iqbal, I. and Iqbal, K. (1986) Occurrence of neuropil threads in the senile human brain and in Alzheimer's disease: a third location of paired helical filaments outside of neurofibrillary tangles and neuritic plaques. Neurosci. Lett., 65, 351-355.
    • (1986) Neurosci. Lett. , vol.65 , pp. 351-355
    • Braak, H.1    Braak, E.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 42
    • 0022869529 scopus 로고
    • Altered structural proteins in plaques and tangles: what do they tell us about the biology of Alzheimer's disease?
    • Selkoe, D.J. (1986) Altered structural proteins in plaques and tangles: what do they tell us about the biology of Alzheimer's disease? Neurobiol. Aging, 7, 425-432.
    • (1986) Neurobiol. Aging , vol.7 , pp. 425-432
    • Selkoe, D.J.1
  • 43
    • 0029788661 scopus 로고    scopus 로고
    • Enhanced amyloidogenic processing of the beta-amyloid precursor protein in gene-targeted mice bearing the Swedish familial Alzheimer's disease mutations and a 'humanized' Abeta sequence
    • Reaume, A.G., Howland, D.S., Trusko, S.P., Savage, M.J., Lang, D.M., Greenberg, B.D., Siman, R. and Scott, R.W. (1996) Enhanced amyloidogenic processing of the beta-amyloid precursor protein in gene-targeted mice bearing the Swedish familial Alzheimer's disease mutations and a 'humanized' Abeta sequence. J. Biol. Chem., 271, 23380-23388.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23380-23388
    • Reaume, A.G.1    Howland, D.S.2    Trusko, S.P.3    Savage, M.J.4    Lang, D.M.5    Greenberg, B.D.6    Siman, R.7    Scott, R.W.8
  • 45
    • 34347353311 scopus 로고    scopus 로고
    • Impairments in fast axonal transport and motor neuron deficits in transgenic mice expressing familial Alzheimer's disease-linked mutant presenilin 1
    • Lazarov, O., Morfini, G.A., Pigino, G., Gadadhar, A., Chen, X., Robinson, J., Ho, H., Brady, S.T. and Sisodia, S.S. (2007) Impairments in fast axonal transport and motor neuron deficits in transgenic mice expressing familial Alzheimer's disease-linked mutant presenilin 1. J. Neurosci., 27, 7011-7020.
    • (2007) J. Neurosci. , vol.27 , pp. 7011-7020
    • Lazarov, O.1    Morfini, G.A.2    Pigino, G.3    Gadadhar, A.4    Chen, X.5    Robinson, J.6    Ho, H.7    Brady, S.T.8    Sisodia, S.S.9
  • 46
    • 0029934134 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization
    • Yamazaki, T., Koo, E.H. and Selkoe, D.J. (1996) Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization. J. Cell Sci., 109 (Pt 5), 999-1008.
    • (1996) J. Cell Sci. , vol.109 , Issue.PART 5 , pp. 999-1008
    • Yamazaki, T.1    Koo, E.H.2    Selkoe, D.J.3
  • 47
    • 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, 17386-17389.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 51
    • 0031031006 scopus 로고    scopus 로고
    • Trafficking of cell-surface beta-amyloid precursor protein: evidence that a sorting intermediate participates in synaptic vesicle recycling
    • Marquez-Sterling, N.R., Lo, A.C., Sisodia, S.S. and Koo, E.H. (1997) Trafficking of cell-surface beta-amyloid precursor protein: evidence that a sorting intermediate participates in synaptic vesicle recycling. J. Neurosci., 17, 140-151.
    • (1997) J. Neurosci. , vol.17 , pp. 140-151
    • Marquez-Sterling, N.R.1    Lo, A.C.2    Sisodia, S.S.3    Koo, E.H.4
  • 52
    • 14244261725 scopus 로고    scopus 로고
    • Axonal transport defects: a common theme in neurodegenerative diseases
    • Roy, S., Zhang, B., Lee, V.M. and Trojanowski, J.Q. (2005) Axonal transport defects: a common theme in neurodegenerative diseases. Acta Neuropathol., 109, 5-13.
    • (2005) Acta Neuropathol. , vol.109 , pp. 5-13
    • Roy, S.1    Zhang, B.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 57
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev, A., McLaughlin, T., O'Leary, D.D. and Tessier-Lavigne, M. (2009) APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature, 457, 981-989.
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'Leary, D.D.3    Tessier-Lavigne, M.4
  • 58
    • 0029257190 scopus 로고
    • Cell-surface beta-amyloid precursor protein stimulates neurite outgrowth of hippocampal neurons in an isoform-dependent manner
    • Qiu, W.Q., Ferreira, A., Miller, C., Koo, E.H. and Selkoe, D.J. (1995) Cell-surface beta-amyloid precursor protein stimulates neurite outgrowth of hippocampal neurons in an isoform-dependent manner. J. Neurosci., 15, 2157-2167.
    • (1995) J. Neurosci. , vol.15 , pp. 2157-2167
    • Qiu, W.Q.1    Ferreira, A.2    Miller, C.3    Koo, E.H.4    Selkoe, D.J.5
  • 59
  • 60
    • 25144501662 scopus 로고    scopus 로고
    • Intraneuronal Abeta accumulation and origin of plaques in Alzheimer's disease
    • Gouras, G.K., Almeida, C.G. and Takahashi, R.H. (2005) Intraneuronal Abeta accumulation and origin of plaques in Alzheimer's disease. Neurobiol. Aging, 26, 1235-1244.
    • (2005) Neurobiol. Aging , vol.26 , pp. 1235-1244
    • Gouras, G.K.1    Almeida, C.G.2    Takahashi, R.H.3
  • 62
    • 0028329090 scopus 로고
    • The amyloid precursor protein is developmentally regulated and correlated with synaptogenesis
    • Moya, K.L., Benowitz, L.I., Schneider, G.E. and Allinquant, B. (1994) The amyloid precursor protein is developmentally regulated and correlated with synaptogenesis. Dev. Biol., 161, 597-603.
    • (1994) Dev. Biol. , vol.161 , pp. 597-603
    • Moya, K.L.1    Benowitz, L.I.2    Schneider, G.E.3    Allinquant, B.4
  • 66
    • 34249696007 scopus 로고    scopus 로고
    • Rapid, concurrent alterations in pre- and postsynaptic structure induced by naturally-secreted amyloid-beta protein
    • Calabrese, B., Shaked, G.M., Tabarean, I.V., Braga, J., Koo, E.H. and Halpain, S. (2007) Rapid, concurrent alterations in pre- and postsynaptic structure induced by naturally-secreted amyloid-beta protein. Mol. Cell. Neurosci., 35, 183-193.
    • (2007) Mol. Cell. Neurosci. , vol.35 , pp. 183-193
    • Calabrese, B.1    Shaked, G.M.2    Tabarean, I.V.3    Braga, J.4    Koo, E.H.5    Halpain, S.6
  • 67
    • 68549127183 scopus 로고    scopus 로고
    • Synaptic activity reduces intraneuronal Abeta, promotes APP transport to synapses, and protects against Abeta-related synaptic alterations
    • Tampellini, D., Rahman, N., Gallo, E.F., Huang, Z., Dumont, M., Capetillo-Zarate, E., Ma, T., Zheng, R., Lu, B., Nanus, D.M. et al. (2009) Synaptic activity reduces intraneuronal Abeta, promotes APP transport to synapses, and protects against Abeta-related synaptic alterations. J. Neurosci., 29, 9704-9713.
    • (2009) J. Neurosci. , vol.29 , pp. 9704-9713
    • Tampellini, D.1    Rahman, N.2    Gallo, E.F.3    Huang, Z.4    Dumont, M.5    Capetillo-Zarate, E.6    Ma, T.7    Zheng, R.8    Lu, B.9    Nanus, D.M.10
  • 68
    • 81255190781 scopus 로고    scopus 로고
    • Impaired mitochondrial biogenesis, defective axonal transport of mitochondria, abnormal mitochondrial dynamics and synaptic degeneration in a mouse model of Alzheimer's disease
    • Calkins, M.J., Manczak, M., Mao, P., Shirendeb, U. and Reddy, P.H. (2011) Impaired mitochondrial biogenesis, defective axonal transport of mitochondria, abnormal mitochondrial dynamics and synaptic degeneration in a mouse model of Alzheimer's disease. Hum. Mol. Genet., 20, 4515-4529.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 4515-4529
    • Calkins, M.J.1    Manczak, M.2    Mao, P.3    Shirendeb, U.4    Reddy, P.H.5
  • 69
    • 70549106846 scopus 로고    scopus 로고
    • Amyloid-beta as a positive endogenous regulator of release probability at hippocampal synapses
    • Abramov, E., Dolev, I., Fogel, H., Ciccotosto, G.D., Ruff, E. and Slutsky, I. (2009) Amyloid-beta as a positive endogenous regulator of release probability at hippocampal synapses. Nat. Neurosci., 12, 1567-1576.
    • (2009) Nat. Neurosci. , vol.12 , pp. 1567-1576
    • Abramov, E.1    Dolev, I.2    Fogel, H.3    Ciccotosto, G.D.4    Ruff, E.5    Slutsky, I.6
  • 70
    • 75549092259 scopus 로고    scopus 로고
    • Amyloid beta from axons and dendrites reduces local spine number and plasticity
    • Wei, W., Nguyen, L.N., Kessels, H.W., Hagiwara, H., Sisodia, S. and Malinow, R. (2010) Amyloid beta from axons and dendrites reduces local spine number and plasticity. Nat. Neurosci., 13, 190-196.
    • (2010) Nat. Neurosci. , vol.13 , pp. 190-196
    • Wei, W.1    Nguyen, L.N.2    Kessels, H.W.3    Hagiwara, H.4    Sisodia, S.5    Malinow, R.6
  • 71
    • 0025970091 scopus 로고
    • Immunoelectron microscopic study of synaptic pathology in Alzheimer's disease
    • Masliah, E., Hansen, L., Albright, T., Mallory, M. and Terry, R.D. (1991) Immunoelectron microscopic study of synaptic pathology in Alzheimer's disease. Acta Neuropathol., 81, 428-433.
    • (1991) Acta Neuropathol. , vol.81 , pp. 428-433
    • Masliah, E.1    Hansen, L.2    Albright, T.3    Mallory, M.4    Terry, R.D.5
  • 72
    • 0026032039 scopus 로고
    • Cortical and subcortical patterns of synaptophysin-like immunoreactivity in Alzheimer's disease
    • Masliah, E., Terry, R.D., Alford, M., DeTeresa, R. and Hansen, L.A. (1991) Cortical and subcortical patterns of synaptophysin-like immunoreactivity in Alzheimer's disease. Am. J. Pathol., 138, 235-246.
    • (1991) Am. J. Pathol. , vol.138 , pp. 235-246
    • Masliah, E.1    Terry, R.D.2    Alford, M.3    DeTeresa, R.4    Hansen, L.A.5
  • 73
    • 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
  • 74
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity
    • DeKosky, S.T. and Scheff, S.W. (1990) Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity. Ann. Neurol., 27, 457-464.
    • (1990) Ann. Neurol. , vol.27 , pp. 457-464
    • DeKosky, S.T.1    Scheff, S.W.2
  • 76
    • 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. (2004) 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
  • 77
    • 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
  • 78
    • 0036898083 scopus 로고    scopus 로고
    • Long-term accumulation of amyloid-beta in axons following brain trauma without persistent upregulation of amyloid precursor protein genes
    • Iwata, A., Chen, X.H., McIntosh, T.K., Browne, K.D. and Smith, D.H. (2002) Long-term accumulation of amyloid-beta in axons following brain trauma without persistent upregulation of amyloid precursor protein genes. J. Neuropathol. Exp. Neurol., 61, 1056-1068.
    • (2002) J. Neuropathol. Exp. Neurol. , vol.61 , pp. 1056-1068
    • Iwata, A.1    Chen, X.H.2    McIntosh, T.K.3    Browne, K.D.4    Smith, D.H.5
  • 79
    • 0036264173 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of amyloid precursor protein and formation of amyloid beta peptide in traumatic axonal injury
    • Stone, J.R., Okonkwo, D.O., Singleton, R.H., Mutlu, L.K., Helm, G.A. and Povlishock, J.T. (2002) Caspase-3-mediated cleavage of amyloid precursor protein and formation of amyloid beta peptide in traumatic axonal injury. J. Neurotrauma, 19, 601-614.
    • (2002) J. Neurotrauma , vol.19 , pp. 601-614
    • Stone, J.R.1    Okonkwo, D.O.2    Singleton, R.H.3    Mutlu, L.K.4    Helm, G.A.5    Povlishock, J.T.6
  • 81
    • 77958459087 scopus 로고    scopus 로고
    • Kinesin-1 transport reductions enhance human tau hyperphosphorylation, aggregation and neurodegeneration in animal models of tauopathies
    • Falzone, T.L., Gunawardena, S., McCleary, D., Reis, G.F. and Goldstein, L.S. (2010) Kinesin-1 transport reductions enhance human tau hyperphosphorylation, aggregation and neurodegeneration in animal models of tauopathies. Hum. Mol. Genet., 19, 4399-4408.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 4399-4408
    • Falzone, T.L.1    Gunawardena, S.2    McCleary, D.3    Reis, G.F.4    Goldstein, L.S.5
  • 82
    • 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
  • 83
    • 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
  • 84
    • 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., Dotti, C.G. and Haass, C. (2006) Axonal membrane proteins are transported in distinct carriers: a two-color video microscopy study in cultured hippocampal neurons. Mol. Biol. Cell, 11, 1213-1224.
    • (2006) Mol. Biol. Cell , vol.11 , pp. 1213-1224
    • Kaether, C.1    Skehel, P.2    Dotti, C.G.3    Haass, C.4
  • 85
    • 33644862462 scopus 로고    scopus 로고
    • Amyloid precursor protein and Notch intracellular domains are generated after transport of their precursors to the cell surface
    • Kaether, C., Schmitt, S., Willem, M. and Haass, C. (2006) Amyloid precursor protein and Notch intracellular domains are generated after transport of their precursors to the cell surface. Traffic, 7, 408-415.
    • (2006) Traffic , vol.7 , pp. 408-415
    • Kaether, C.1    Schmitt, S.2    Willem, M.3    Haass, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.