메뉴 건너뛰기




Volumn 288, Issue 42, 2013, Pages 30236-30245

Increased expression of reticulon 3 in neurons leads to reduced axonal transport of β site amyloid precursor protein-cleaving enzyme

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID DEPOSITION; AXONAL TRANSPORTS; COLOCALIZATION; OVER-EXPRESSION; SYNAPTIC LOCALIZATION; SYNAPTOPHYSIN;

EID: 84886892404     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.480079     Document Type: Article
Times cited : (40)

References (64)
  • 2
    • 0036548070 scopus 로고    scopus 로고
    • β-Secretase, Notch, Aβ and Alzheimer's disease. Where do the presenilins fit in?
    • Sisodia, S. S., and St George-Hyslop, P. H. (2002) β-Secretase, Notch, Aβ and Alzheimer's disease. Where do the presenilins fit in? Nat. Rev. Neurosci. 3, 281-290
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 281-290
    • Sisodia, S.S.1    St George-Hyslop, P.H.2
  • 3
    • 1442264828 scopus 로고    scopus 로고
    • Take five. BACE and the β-secretase quartet conduct Alzheimer's amyloid β-peptide generation
    • Haass, C. (2004) Take five. BACE and the β-secretase quartet conduct Alzheimer's amyloid β-peptide generation. EMBO J. 23, 483-488
    • (2004) EMBO J. , vol.23 , pp. 483-488
    • Haass, C.1
  • 8
    • 0034652309 scopus 로고    scopus 로고
    • Human aspartic protease memapsin 2 cleaves the β-secretase site of β-amyloid precursor protein
    • Lin, X., Koelsch, G., Wu, S., Downs, D., Dashti, A., and Tang, J. (2000) Human aspartic protease memapsin 2 cleaves the β-secretase site of β-amyloid precursor protein. Proc. Natl. Acad. Sci. U.S.A. 97, 1456-1460
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 1456-1460
    • Lin, X.1    Koelsch, G.2    Wu, S.3    Downs, D.4    Dashti, A.5    Tang, J.6
  • 10
    • 84866291339 scopus 로고    scopus 로고
    • The membrane-bound aspartyl protease BACE1. Molecular and functional properties in Alzheimer's disease and beyond
    • Dislich, B., and Lichtenthaler, S. F. (2012) The membrane-bound aspartyl protease BACE1. Molecular and functional properties in Alzheimer's disease and beyond. Front. Physiol. 3, 8
    • (2012) Front. Physiol. , vol.3 , pp. 8
    • Dislich, B.1    Lichtenthaler, S.F.2
  • 11
    • 77956048697 scopus 로고    scopus 로고
    • Inhibition of BACE1 for therapeutic use in Alzheimer's disease
    • Luo, X., and Yan, R. (2010) Inhibition of BACE1 for therapeutic use in Alzheimer's disease. Int. J. Clin. Exp. Pathol. 3, 618-628
    • (2010) Int. J. Clin. Exp. Pathol. , vol.3 , pp. 618-628
    • Luo, X.1    Yan, R.2
  • 12
    • 84655162702 scopus 로고    scopus 로고
    • Developing β-secretase inhibitors for treatment of Alzheimer's disease
    • Ghosh, A. K., Brindisi, M., and Tang, J. (2012) Developing β-secretase inhibitors for treatment of Alzheimer's disease. J. Neurochem. 120, 71-83
    • (2012) J. Neurochem. , vol.120 , pp. 71-83
    • Ghosh, A.K.1    Brindisi, M.2    Tang, J.3
  • 13
    • 70350455062 scopus 로고    scopus 로고
    • The β-secretase enzyme BACE in health and Alzheimer's disease. Regulation, cell biology, function, and therapeutic potential
    • Vassar, R., Kovacs, D. M., Yan, R., and Wong, P. C. (2009) The β-secretase enzyme BACE in health and Alzheimer's disease. Regulation, cell biology, function, and therapeutic potential. J. Neurosci. 29, 12787-12794
    • (2009) J. Neurosci. , vol.29 , pp. 12787-12794
    • Vassar, R.1    Kovacs, D.M.2    Yan, R.3    Wong, P.C.4
  • 14
    • 84857914247 scopus 로고    scopus 로고
    • B-site APP-cleaving enzyme 1 trafficking and Alzheimer's disease pathogenesis
    • Tan, J., and Evin, G. (2012) B-site APP-cleaving enzyme 1 trafficking and Alzheimer's disease pathogenesis. J. Neurochem. 120, 869-880
    • (2012) J. Neurochem. , vol.120 , pp. 869-880
    • Tan, J.1    Evin, G.2
  • 16
    • 79953297068 scopus 로고    scopus 로고
    • BACE1 retrograde trafficking is uniquely regulated by the cytoplasmic domain of sortilin
    • Finan, G. M., Okada, H., and Kim, T. W. (2011) BACE1 retrograde trafficking is uniquely regulated by the cytoplasmic domain of sortilin. J. Biol. Chem. 286, 12602-12616
    • (2011) J. Biol. Chem. , vol.286 , pp. 12602-12616
    • Finan, G.M.1    Okada, H.2    Kim, T.W.3
  • 19
  • 20
    • 15744380393 scopus 로고    scopus 로고
    • GGA proteins mediate the recycling pathway of memapsin 2 (BACE)
    • He, X., Li, F., Chang, W. P., and Tang, J. (2005) GGA proteins mediate the recycling pathway of memapsin 2 (BACE). J. Biol. Chem. 280, 11696 -11703
    • (2005) J. Biol. Chem. , vol.280 , pp. 11696-11703
    • He, X.1    Li, F.2    Chang, W.P.3    Tang, J.4
  • 21
    • 20444377260 scopus 로고    scopus 로고
    • GGA proteins regulate retrograde transport of BACE1 from endosomes to the trans-Golgi network
    • Wahle, T., Prager, K., Raffler, N., Haass, C., Famulok, M., and Walter, J. (2005) GGA proteins regulate retrograde transport of BACE1 from endosomes to the trans-Golgi network. Mol. Cell Neurosci. 29, 453-461
    • (2005) Mol. Cell Neurosci. , vol.29 , pp. 453-461
    • Wahle, T.1    Prager, K.2    Raffler, N.3    Haass, C.4    Famulok, M.5    Walter, J.6
  • 22
    • 79955944449 scopus 로고    scopus 로고
    • Decreased expression of GGA3 protein in Alzheimer's disease frontal cortex and increased codistribution of BACE with the amyloid precursor protein
    • Santosa, C., Rasche, S., Barakat, A., Bellingham, S. A., Ho, M., Tan, J., Hill, A. F., Masters, C. L., McLean, C., and Evin, G. (2011) Decreased expression of GGA3 protein in Alzheimer's disease frontal cortex and increased codistribution of BACE with the amyloid precursor protein. Neurobiol. Dis. 43, 176-183
    • (2011) Neurobiol. Dis. , vol.43 , pp. 176-183
    • Santosa, C.1    Rasche, S.2    Barakat, A.3    Bellingham, S.A.4    Ho, M.5    Tan, J.6    Hill, A.F.7    Masters, C.L.8    McLean, C.9    Evin, G.10
  • 23
    • 4644357534 scopus 로고    scopus 로고
    • Reticulon family members modulate BACE1 activity and amyloid- peptide generation
    • He, W., Lu, Y., Qahwash, I., Hu, X. Y., Chang, A., and Yan, R. (2004) Reticulon family members modulate BACE1 activity and amyloid- peptide generation. Nat. Med. 10, 959-965
    • (2004) Nat. Med. , vol.10 , pp. 959-965
    • He, W.1    Lu, Y.2    Qahwash, I.3    Hu, X.Y.4    Chang, A.5    Yan, R.6
  • 24
    • 33748755837 scopus 로고    scopus 로고
    • Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its ability to produce amyloid β-protein
    • Murayama, K. S., Kametani, F., Saito, S., Kume, H., Akiyama, H., and Araki, W. (2006) Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its ability to produce amyloid β-protein. Eur. J. Neurosci. 24, 1237-1244
    • (2006) Eur. J. Neurosci. , vol.24 , pp. 1237-1244
    • Murayama, K.S.1    Kametani, F.2    Saito, S.3    Kume, H.4    Akiyama, H.5    Araki, W.6
  • 25
    • 67651154309 scopus 로고    scopus 로고
    • Reduced amyloid deposition in mice overexpressing RTN3 is adversely affected by preformed dystrophic neurites
    • Shi, Q., Prior, M., He, W., Tang, X., Hu, X., and Yan, R. (2009) Reduced amyloid deposition in mice overexpressing RTN3 is adversely affected by preformed dystrophic neurites. J. Neurosci. 29, 9163-9173
    • (2009) J. Neurosci. , vol.29 , pp. 9163-9173
    • Shi, Q.1    Prior, M.2    He, W.3    Tang, X.4    Hu, X.5    Yan, R.6
  • 26
    • 33646577429 scopus 로고    scopus 로고
    • Reticulon proteins. Emerging players in neurodegenerative diseases
    • Yan, R., Shi, Q., Hu, X., and Zhou, X. (2006) Reticulon proteins. Emerging players in neurodegenerative diseases. Cell Mol. Life Sci. 63, 877-889
    • (2006) Cell Mol. Life Sci. , vol.63 , pp. 877-889
    • Yan, R.1    Shi, Q.2    Hu, X.3    Zhou, X.4
  • 27
    • 40449124075 scopus 로고    scopus 로고
    • The reticulons. A family of proteins with diverse functions
    • Yang, Y. S., and Strittmatter, S. M. (2007) The reticulons. A family of proteins with diverse functions. Genome Biol. 8, 234
    • (2007) Genome Biol. , vol.8 , pp. 234
    • Yang, Y.S.1    Strittmatter, S.M.2
  • 28
    • 0038799728 scopus 로고    scopus 로고
    • A reticular rhapsody. Phylogenic evolution and nomenclature of the RTN/Nogo gene family
    • Oertle, T., Klinger, M., Stuermer, C. A., and Schwab, M. E. (2003) A reticular rhapsody. Phylogenic evolution and nomenclature of the RTN/Nogo gene family. FASEB J. 17, 1238-1247
    • (2003) FASEB J. , vol.17 , pp. 1238-1247
    • Oertle, T.1    Klinger, M.2    Stuermer, C.A.3    Schwab, M.E.4
  • 29
    • 14044257857 scopus 로고    scopus 로고
    • Nogo signaling and non-physical injuryinduced nervous system pathology
    • Teng, F. Y., and Tang, B. L. (2005) Nogo signaling and non-physical injuryinduced nervous system pathology. J. Neurosci. Res. 79, 273-278
    • (2005) J. Neurosci. Res. , vol.79 , pp. 273-278
    • Teng, F.Y.1    Tang, B.L.2
  • 30
    • 33847164931 scopus 로고    scopus 로고
    • Two hydrophobic segments of the RTN1 family determine the ER localization and retention
    • Iwahashi, J., Hamada, N., and Watanabe, H. (2007) Two hydrophobic segments of the RTN1 family determine the ER localization and retention. Biochem. Biophys. Res. Commun. 355, 508-512
    • (2007) Biochem. Biophys. Res. Commun. , vol.355 , pp. 508-512
    • Iwahashi, J.1    Hamada, N.2    Watanabe, H.3
  • 31
    • 32044445021 scopus 로고    scopus 로고
    • A class of membrane proteins shaping the tubular endoplasmic reticulum
    • Voeltz, G. K., Prinz, W. A., Shibata, Y., Rist, J. M., and Rapoport, T. A. (2006) A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 124, 573-586
    • (2006) Cell , vol.124 , pp. 573-586
    • Voeltz, G.K.1    Prinz, W.A.2    Shibata, Y.3    Rist, J.M.4    Rapoport, T.A.5
  • 32
    • 35748960521 scopus 로고    scopus 로고
    • The membrane topology of RTN3 and its effect on binding of RTN3 to BACE1
    • He, W., Shi, Q., Hu, X., and Yan, R. (2007) The membrane topology of RTN3 and its effect on binding of RTN3 to BACE1. J. Biol. Chem. 282, 29144-29151
    • (2007) J. Biol. Chem. , vol.282 , pp. 29144-29151
    • He, W.1    Shi, Q.2    Hu, X.3    Yan, R.4
  • 33
    • 33749246089 scopus 로고    scopus 로고
    • Mapping of interaction domains mediating binding between BACE1 and RTN/Nogo proteins
    • He, W., Hu, X., Shi, Q., Zhou, X., Lu, Y., Fisher, C., and Yan, R. (2006) Mapping of interaction domains mediating binding between BACE1 and RTN/Nogo proteins. J. Mol. Biol. 363, 625-634
    • (2006) J. Mol. Biol. , vol.363 , pp. 625-634
    • He, W.1    Hu, X.2    Shi, Q.3    Zhou, X.4    Lu, Y.5    Fisher, C.6    Yan, R.7
  • 34
    • 70449379429 scopus 로고    scopus 로고
    • The two-hydrophobic domain tertiary structure of reticulon proteins is critical for modulation of β-secretase BACE1
    • Kume, H., Murayama, K. S., and Araki, W. (2009) The two-hydrophobic domain tertiary structure of reticulon proteins is critical for modulation of β-secretase BACE1. J. Neurosci. Res. 87, 2963-2972
    • (2009) J. Neurosci. Res. , vol.87 , pp. 2963-2972
    • Kume, H.1    Murayama, K.S.2    Araki, W.3
  • 35
    • 65549143774 scopus 로고    scopus 로고
    • The occurrence of aging-dependent reticulon 3 immunoreactive dystrophic neurites decreases cognitive function
    • Shi, Q., Hu, X., Prior, M., and Yan, R. (2009) The occurrence of aging-dependent reticulon 3 immunoreactive dystrophic neurites decreases cognitive function. J. Neurosci. 29, 5108-5115
    • (2009) J. Neurosci. , vol.29 , pp. 5108-5115
    • Shi, Q.1    Hu, X.2    Prior, M.3    Yan, R.4
  • 37
    • 34948899795 scopus 로고    scopus 로고
    • NOGO is increased and binds to BACE1 in sporadic inclusion-body myositis and in A PP-overexpressing cultured human muscle fibers
    • Wojcik, S., Engel, W. K., Yan, R., McFerrin, J., and Askanas, V. (2007) NOGO is increased and binds to BACE1 in sporadic inclusion-body myositis and in A PP-overexpressing cultured human muscle fibers. Acta Neuropathol. 114, 517-526
    • (2007) Acta Neuropathol. , vol.114 , pp. 517-526
    • Wojcik, S.1    Engel, W.K.2    Yan, R.3    McFerrin, J.4    Askanas, V.5
  • 38
    • 84878388997 scopus 로고    scopus 로고
    • Diabetes-induced central neuritic dystrophy and cognitive deficits are associated with the formation of oligomeric reticulon-3 via oxidative stress
    • Zhao, B., Pan, B. S., Shen, S. W., Sun, X., Hou, Z. Z., Yan, R., and Sun, F. Y. (2013) Diabetes-induced central neuritic dystrophy and cognitive deficits are associated with the formation of oligomeric reticulon-3 via oxidative stress. J. Biol. Chem. 288, 15590-15599
    • (2013) J. Biol. Chem. , vol.288 , pp. 15590-15599
    • Zhao, B.1    Pan, B.S.2    Shen, S.W.3    Sun, X.4    Hou, Z.Z.5    Yan, R.6    Sun, F.Y.7
  • 40
    • 34250019939 scopus 로고    scopus 로고
    • Transgenic mice overexpressing reticulon 3 develop neuritic abnormalities
    • Hu, X., Shi, Q., Zhou, X., He, W., Yi, H., Yin, X., Gearing, M., Levey, A., and Yan, R. (2007) Transgenic mice overexpressing reticulon 3 develop neuritic abnormalities. EMBO J. 26, 2755-2767
    • (2007) EMBO J. , vol.26 , pp. 2755-2767
    • Hu, X.1    Shi, Q.2    Zhou, X.3    He, W.4    Yi, H.5    Yin, X.6    Gearing, M.7    Levey, A.8    Yan, R.9
  • 41
    • 80455143668 scopus 로고    scopus 로고
    • Optic atrophy 1 is an A-kinase anchoring protein on lipid droplets that mediates adrenergic control of lipolysis
    • Pidoux, G., Witczak, O., Jarnæss, E., Myrvold, L., Urlaub, H., Stokka, A. J., Küntziger, T., and Taskén, K. (2011) Optic atrophy 1 is an A-kinase anchoring protein on lipid droplets that mediates adrenergic control of lipolysis. EMBO J. 30, 4371-4386
    • (2011) EMBO J. , vol.30 , pp. 4371-4386
    • Pidoux, G.1    Witczak, O.2    Jarnæss, E.3    Myrvold, L.4    Urlaub, H.5    Stokka, A.J.6    Küntziger, T.7    Taskén, K.8
  • 42
    • 49649084487 scopus 로고    scopus 로고
    • The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum
    • Shibata, Y., Voss, C., Rist, J. M., Hu, J., Rapoport, T. A., Prinz, W. A., and Voeltz, G. K. (2008) The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum. J. Biol. Chem. 283, 18892-18904
    • (2008) J. Biol. Chem. , vol.283 , pp. 18892-18904
    • Shibata, Y.1    Voss, C.2    Rist, J.M.3    Hu, J.4    Rapoport, T.A.5    Prinz, W.A.6    Voeltz, G.K.7
  • 44
    • 84883462681 scopus 로고    scopus 로고
    • The Alzheimer's β-secretase BACE1 localizes to normal presynaptic terminals and to dystrophic presynaptic terminals surrounding amyloid plaques
    • Kandalepas, P. C., Sadleir, K. R., Eimer, W. A., Zhao, J., Nicholson, D. A., and Vassar, R. (2013) The Alzheimer's β-secretase BACE1 localizes to normal presynaptic terminals and to dystrophic presynaptic terminals surrounding amyloid plaques. Acta Neuropathol. 126, 329-352
    • (2013) Acta Neuropathol. , vol.126 , pp. 329-352
    • Kandalepas, P.C.1    Sadleir, K.R.2    Eimer, W.A.3    Zhao, J.4    Nicholson, D.A.5    Vassar, R.6
  • 45
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing β-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 β-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
  • 46
    • 13844265969 scopus 로고    scopus 로고
    • BACE overexpression alters the subcellular processing of APP and inhibits A deposition in vivo
    • Lee, E. B., Zhang, B., Liu, K., Greenbaum, E. A., Doms, R. W., Trojanowski, J. Q., and Lee, V. M. (2005) BACE overexpression alters the subcellular processing of APP and inhibits A deposition in vivo. J. Cell Biol. 168, 291-302
    • (2005) J. Cell Biol. , vol.168 , pp. 291-302
    • Lee, E.B.1    Zhang, B.2    Liu, K.3    Greenbaum, E.A.4    Doms, R.W.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 47
    • 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
  • 48
    • 63849105306 scopus 로고    scopus 로고
    • The cleavage products of amyloid-β 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-β 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
  • 51
    • 0035800545 scopus 로고    scopus 로고
    • Presenilin-1 and its N-terminal and C-terminal fragments are transported in the sciatic nerve of rat
    • Kasa, P., Papp, H., and Pakaski, M. (2001) Presenilin-1 and its N-terminal and C-terminal fragments are transported in the sciatic nerve of rat. Brain Res. 909, 159-169
    • (2001) Brain Res. , vol.909 , pp. 159-169
    • Kasa, P.1    Papp, H.2    Pakaski, M.3
  • 52
    • 84964915731 scopus 로고    scopus 로고
    • Calsyntenin-1 shelters APP from proteolytic processing during anterograde axonal transport
    • Steuble, M., Diep, T. M., Schätzle, P., Ludwig, A., Tagaya, M., Kunz, B., and Sonderegger, P. (2012) Calsyntenin-1 shelters APP from proteolytic processing during anterograde axonal transport. Biol. Open. 1, 761-774
    • (2012) Biol. Open. , vol.1 , pp. 761-774
    • Steuble, M.1    Diep, T.M.2    Schätzle, P.3    Ludwig, A.4    Tagaya, M.5    Kunz, B.6    Sonderegger, P.7
  • 53
    • 84863518335 scopus 로고    scopus 로고
    • Calsyntenin-1 mediates axonal transport of the amyloid precursor protein and regulatesAβ production
    • Vagnoni, A., Perkinton, M. S., Gray, E. H., Francis, P. T., Noble, W., and Miller, C. C. (2012) Calsyntenin-1 mediates axonal transport of the amyloid precursor protein and regulatesAβ production. Hum. Mol. Genet. 21, 2845-2854
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2845-2854
    • Vagnoni, A.1    Perkinton, M.S.2    Gray, E.H.3    Francis, P.T.4    Noble, W.5    Miller, C.C.6
  • 54
    • 29144490203 scopus 로고    scopus 로고
    • To think or not to think. Synaptic activity and A release
    • Schroeder, B. E., and Koo, E. H. (2005) To think or not to think. Synaptic activity and A release. Neuron 48, 873-875
    • (2005) Neuron , vol.48 , pp. 873-875
    • Schroeder, B.E.1    Koo, E.H.2
  • 55
    • 84863263718 scopus 로고    scopus 로고
    • Role of APP and A in synaptic physiology
    • Wang, Z., Yang, L., and Zheng, H. (2012) Role of APP and A in synaptic physiology. Curr. Alzheimer Res. 9, 217-226
    • (2012) Curr. Alzheimer Res. , vol.9 , pp. 217-226
    • Wang, Z.1    Yang, L.2    Zheng, H.3
  • 56
    • 84877919955 scopus 로고    scopus 로고
    • VPS35 regulates developing mouse hippocampal neuronal morphogenesis by promoting retrograde trafficking of BACE1
    • Wang, C. L., Tang, F. L., Peng, Y., Shen, C. Y., Mei, L., and Xiong, W. C. (2012) VPS35 regulates developing mouse hippocampal neuronal morphogenesis by promoting retrograde trafficking of BACE1. Biol. Open. 1, 1248-1257
    • (2012) Biol. Open. , vol.1 , pp. 1248-1257
    • Wang, C.L.1    Tang, F.L.2    Peng, Y.3    Shen, C.Y.4    Mei, L.5    Xiong, W.C.6
  • 57
    • 84873617529 scopus 로고    scopus 로고
    • Preventing formation of reticulon 3 immunoreactive dystrophic neurites improves cognitive function in mice
    • Shi, Q., Prior, M., Zhou, X., Tang, X., He, W., Hu, X., and Yan, R. (2013) Preventing formation of reticulon 3 immunoreactive dystrophic neurites improves cognitive function in mice. J. Neurosci. 33, 3059-3066
    • (2013) J. Neurosci. , vol.33 , pp. 3059-3066
    • Shi, Q.1    Prior, M.2    Zhou, X.3    Tang, X.4    He, W.5    Hu, X.6    Yan, R.7
  • 59
    • 61649114950 scopus 로고    scopus 로고
    • Site amyloid precursor protein cleaving enzyme 1 (BACE1) as a biological candidate marker of Alzheimer's disease
    • Hampel, H., and Shen, Y. (2009)-Site amyloid precursor protein cleaving enzyme 1 (BACE1) as a biological candidate marker of Alzheimer's disease. Scand. J. Clin. Lab. Invest. 69, 8-12
    • (2009) Scand. J. Clin. Lab. Invest. , vol.69 , pp. 8-12
    • Hampel, H.1    Shen, Y.2
  • 60
    • 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
  • 61
    • 79958785727 scopus 로고    scopus 로고
    • APP heterozygosity averts memory deficit in knockin mice expressing the Danish dementia BRI2 mutant
    • Tamayev, R., Matsuda, S., Giliberto, L., Arancio, O., and D'Adamio, L. (2011) APP heterozygosity averts memory deficit in knockin mice expressing the Danish dementia BRI2 mutant. EMBO J. 30, 2501-2509
    • (2011) EMBO J. , vol.30 , pp. 2501-2509
    • Tamayev, R.1    Matsuda, S.2    Giliberto, L.3    Arancio, O.4    D'adamio, L.5
  • 62
    • 78049506839 scopus 로고    scopus 로고
    • Danish dementia mice suggest that loss of function and not the amyloid cascade causes synaptic plasticity and memory deficits
    • Tamayev, R., Matsuda, S., Fà, M., Arancio, O., and D'Adamio, L. (2010) Danish dementia mice suggest that loss of function and not the amyloid cascade causes synaptic plasticity and memory deficits. Proc. Natl. Acad. Sci. U.S.A. 107, 20822-20827
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 20822-20827
    • Tamayev, R.1    Matsuda, S.2    Fà, M.3    Arancio, O.4    D'adamio, L.5
  • 63
    • 84858123000 scopus 로고    scopus 로고
    • But not β-secretase proteolysis of APP causes synaptic and memory deficits in a mouse model of dementia
    • Tamayev, R., Matsuda, S., Arancio, O., and D'Adamio, L. (2012)- but not β-secretase proteolysis of APP causes synaptic and memory deficits in a mouse model of dementia. EMBO Mol. Med. 4, 171-179
    • (2012) EMBO Mol. Med. , vol.4 , pp. 171-179
    • Tamayev, R.1    Matsuda, S.2    Arancio, O.3    D'adamio, L.4
  • 64
    • 84867766569 scopus 로고    scopus 로고
    • Enhanced β-secretase processing alters APP axonal transport and leads to axonal defects
    • Rodrigues, E. M., Weissmiller, A. M., and Goldstein, L. S. (2012) Enhanced β-secretase processing alters APP axonal transport and leads to axonal defects. Hum. Mol. Genet. 21, 4587-4601
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 4587-4601
    • Rodrigues, E.M.1    Weissmiller, A.M.2    Goldstein, L.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.