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Volumn 289, Issue 29, 2014, Pages 20182-20191

Nuclear translocation uncovers the amyloid peptide aβ42 as a regulator of gene transcription

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEINS; HIGH RESOLUTION TRANSMISSION ELECTRON MICROSCOPY; MAMMALS; NEURODEGENERATIVE DISEASES; PEPTIDES; SCANNING ELECTRON MICROSCOPY;

EID: 84904497399     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.564690     Document Type: Article
Times cited : (69)

References (65)
  • 2
    • 79959636033 scopus 로고    scopus 로고
    • The many substrates of presenilin/γ-secretase
    • Haapasalo, A., and Kovacs, D. M. (2011) The many substrates of presenilin/γ-secretase. J. Alzheimer's Disease 25, 3-28
    • (2011) J. Alzheimer's Disease , vol.25 , pp. 3-28
    • Haapasalo, A.1    Kovacs, D.M.2
  • 3
    • 84655166492 scopus 로고    scopus 로고
    • The physiology of the β-amyloid precursor protein intracellular domain AICD
    • Pardossi-Piquard, R., and Checler, F. (2012) The physiology of the β-amyloid precursor protein intracellular domain AICD. J. Neurochem. 120, 109-124
    • (2012) J. Neurochem. , vol.120 , pp. 109-124
    • Pardossi-Piquard, R.1    Checler, F.2
  • 4
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy, J., and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 7
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • DOI 10.1126/science.1079469
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489 (Pubitemid 36444329)
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabel, C.G.7
  • 9
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., and Selkoe, D. J. (2002) Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539 (Pubitemid 34288854)
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 10
    • 34547093895 scopus 로고    scopus 로고
    • Differential regulation of basic helix-loop-helix factors Mash1 and Olig2 by β-amyloid accelerates both differentiation and death of cultured neural stem/progenitor cells
    • DOI 10.1074/jbc.M703099200
    • Uchida, Y., Nakano, S., Gomi, F., and Takahashi, H. (2007) Differential regulation of basic helix-loop-helix factors Mash1 and Olig2 by β-amyloid accelerates both differentiation and death of cultured neural stem/progenitor cells. J. Biol. Chem. 282, 19700-19709 (Pubitemid 47100101)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.27 , pp. 19700-19709
    • Uchida, Y.1    Nakano, S.-I.2    Gomi, F.3    Takahashi, H.4
  • 14
    • 0037017399 scopus 로고    scopus 로고
    • 1-42 through p53 and Bax in cultured primary human neurons
    • DOI 10.1083/jcb.200110119
    • Zhang, Y., McLaughlin, R., Goodyer, C., and LeBlanc, A. (2002) Selective cytotoxicity of intracellular amyloid β peptide 1-42 through p53 and Bax in cultured primary human neurons. J. Cell Biol. 156, 519-529 (Pubitemid 34839899)
    • (2002) Journal of Cell Biology , vol.156 , Issue.3 , pp. 519-529
    • Zhang, Y.1    McLaughlin, R.2    Goodyer, C.3    LeBlanc, A.4
  • 15
    • 0028981717 scopus 로고
    • The Alzheimer's Aβ peptide induces neurodegeneration and apoptotic cell death in transgenic mice
    • LaFerla, F. M., Tinkle, B. T., Bieberich, C. J., Haudenschild, C. C., and Jay, G. (1995) The Alzheimer's Aβ peptide induces neurodegeneration and apoptotic cell death in transgenic mice. Nat. Genet. 9, 21-30
    • (1995) Nat. Genet. , vol.9 , pp. 21-30
    • LaFerla, F.M.1    Tinkle, B.T.2    Bieberich, C.J.3    Haudenschild, C.C.4    Jay, G.5
  • 16
    • 30344448543 scopus 로고    scopus 로고
    • A dynamic relationship between intracellular and extracellular pools of Aβ
    • DOI 10.2353/ajpath.2006.050593
    • Oddo, S., Caccamo, A., Smith, I. F., Green, K. N., and LaFerla, F. M. (2006) A dynamic relationship between intracellular and extracellular pools of Aβ. Am. J. Pathol. 168, 184-194 (Pubitemid 43062572)
    • (2006) American Journal of Pathology , vol.168 , Issue.1 , pp. 184-194
    • Oddo, S.1    Caccamo, A.2    Smith, I.F.3    Green, K.N.4    LaFerla, F.M.5
  • 18
    • 37249062072 scopus 로고    scopus 로고
    • Internalization of β-amyloid peptide by primary neurons in the absence of apolipoprotein E
    • DOI 10.1074/jbc.M701823200
    • Saavedra, L., Mohamed, A., Ma, V., Kar, S., and de Chaves, E. P. (2007) Internalization of β-amyloid peptide by primary neurons in the absence of apolipoprotein E. J. Biol. Chem. 282, 35722-35732 (Pubitemid 350277136)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 35722-35732
    • Saavedra, L.1    Mohamed, A.2    Ma, V.3    Kar, S.4    De Chaves, E.P.5
  • 19
    • 0030607177 scopus 로고    scopus 로고
    • Rapid cellular uptake of Alzheimer amyloid βA4 peptide by cultured human neuroblastoma cells
    • DOI 10.1016/0014-5793(96)00948-9
    • Ida, N., Masters, C. L., and Beyreuther, K. (1996) Rapid cellular uptake of Alzheimer amyloid βA4 peptide by cultured human neuroblastoma cells. FEBS Lett. 394, 174-178 (Pubitemid 26341500)
    • (1996) FEBS Letters , vol.394 , Issue.2 , pp. 174-178
    • Ida, N.1    Masters, C.L.2    Beyreuther, K.3
  • 20
    • 68249134074 scopus 로고    scopus 로고
    • The role of apolipoprotein E in Alzheimer's disease
    • Kim, J., Basak, J. M., and Holtzman, D. M. (2009) The role of apolipoprotein E in Alzheimer's disease. Neuron 63, 287-303
    • (2009) Neuron , vol.63 , pp. 287-303
    • Kim, J.1    Basak, J.M.2    Holtzman, D.M.3
  • 21
    • 28744449206 scopus 로고    scopus 로고
    • Mitochondrial Aβ: A potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
    • DOI 10.1096/fj.05-3735fje
    • Caspersen, C., Wang, N., Yao, J., Sosunov, A., Chen, X., Lustbader, J. W., Xu, H. W., Stern, D., McKhann, G., and Yan, S. D. (2005) Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease. FASEB J. 19, 2040-2041 (Pubitemid 41759758)
    • (2005) FASEB Journal , vol.19 , Issue.14 , pp. 2040-2041
    • Caspersen, C.1    Wang, N.2    Yao, J.3    Sosunov, A.4    Chen, X.5    Lustbader, J.W.6    Xu, H.W.7    Stern, D.8    McKhann, G.9    Yan, S.D.10
  • 22
    • 79955601720 scopus 로고    scopus 로고
    • Intraneuronal amyloid β oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo
    • Umeda, T., Tomiyama, T., Sakama, N., Tanaka, S., Lambert, M. P., Klein, W. L., and Mori, H. (2011) Intraneuronal amyloid β oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo. J. Neurosci. Res. 89, 1031-1042
    • (2011) J. Neurosci. Res. , vol.89 , pp. 1031-1042
    • Umeda, T.1    Tomiyama, T.2    Sakama, N.3    Tanaka, S.4    Lambert, M.P.5    Klein, W.L.6    Mori, H.7
  • 23
    • 0035997234 scopus 로고    scopus 로고
    • The channel hypothesis of Alzheimer's disease: Current status
    • DOI 10.1016/S0196-9781(02)00067-0, PII S0196978102000670
    • Kagan, B. L., Hirakura, Y., Azimov, R., Azimova, R., and Lin, M. C. (2002) The channel hypothesis of Alzheimer's disease: current status. Peptides 23, 1311-1315 (Pubitemid 34786709)
    • (2002) Peptides , vol.23 , Issue.7 , pp. 1311-1315
    • Kagan, B.L.1    Hirakura, Y.2    Azimov, R.3    Azimova, R.4    Lin, M.-C.5
  • 24
    • 84884635054 scopus 로고    scopus 로고
    • Neuroscience. Promiscuous Alzheimer's amyloid: Yet another partner
    • Benilova, I., and De Strooper, B. (2013) Neuroscience. Promiscuous Alzheimer's amyloid: yet another partner. Science 341, 1354-1355
    • (2013) Science , vol.341 , pp. 1354-1355
    • Benilova, I.1    De Strooper, B.2
  • 25
  • 26
    • 36249023636 scopus 로고    scopus 로고
    • Pore-forming proteins share structural and functional homology with amyloid oligomers
    • DOI 10.1007/s12017-007-0003-6
    • Yoshiike, Y., Kayed, R., Milton, S. C., Takashima, A., and Glabe, C. G. (2007) Pore-forming proteins share structural and functional homology with amyloid oligomers. Neuromol. Med. 9, 270-275 (Pubitemid 350129702)
    • (2007) NeuroMolecular Medicine , vol.9 , Issue.3 , pp. 270-275
    • Yoshiike, Y.1    Kayed, R.2    Milton, S.C.3    Takashima, A.4    Glabe, C.G.5
  • 27
    • 65249143369 scopus 로고    scopus 로고
    • Subcellular localization and dimerization of APLP1 are strikingly different from APP and APLP2
    • Kaden, D., Voigt, P., Munter, L. M., Bobowski, K. D., Schaefer, M., and Multhaup, G. (2009) Subcellular localization and dimerization of APLP1 are strikingly different from APP and APLP2. J. Cell Sci. 122, 368-377
    • (2009) J. Cell Sci. , vol.122 , pp. 368-377
    • Kaden, D.1    Voigt, P.2    Munter, L.M.3    Bobowski, K.D.4    Schaefer, M.5    Multhaup, G.6
  • 28
    • 77954359268 scopus 로고    scopus 로고
    • Aberrant amyloid precursor protein (APP) processing in hereditary forms of Alzheimer disease caused by APP familial Alzheimer disease mutations can be rescued by mutations in the APP GXXXG motif
    • Munter, L. M., Botev, A., Richter, L., Hildebrand, P. W., Althoff, V., Weise, C., Kaden, D., and Multhaup, G. (2010) Aberrant amyloid precursor protein (APP) processing in hereditary forms of Alzheimer disease caused by APP familial Alzheimer disease mutations can be rescued by mutations in the APP GXXXG motif. J. Biol. Chem. 285, 21636-21643
    • (2010) J. Biol. Chem. , vol.285 , pp. 21636-21643
    • Munter, L.M.1    Botev, A.2    Richter, L.3    Hildebrand, P.W.4    Althoff, V.5    Weise, C.6    Kaden, D.7    Multhaup, G.8
  • 29
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive western blot assay
    • DOI 10.1074/jbc.271.37.22908
    • Ida, N., Hartmann, T., Pantel, J., Schröder, J., Zerfass, R., Förstl, H., Sandbrink, R., Masters, C. L., and Beyreuther, K. (1996) Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay. J. Biol. Chem. 271, 22908-22914 (Pubitemid 26304742)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.37 , pp. 22908-22914
    • Ida, N.1    Hartmann, T.2    Pantel, J.3    Schroder, J.4    Zerfass, R.5    Forstl, H.6    Sandbrink, R.7    Masters, C.L.8    Beyreuther, K.9
  • 30
    • 57349097159 scopus 로고    scopus 로고
    • Phorbol ester enhances KAI1 transcription by recruiting Tip60/Pontin complexes
    • Rowe, A., Weiske, J., Kramer, T. S., Huber, O., and Jackson, P. (2008) Phorbol ester enhances KAI1 transcription by recruiting Tip60/Pontin complexes. Neoplasia 10, 1421-1432
    • (2008) Neoplasia , vol.10 , pp. 1421-1432
    • Rowe, A.1    Weiske, J.2    Kramer, T.S.3    Huber, O.4    Jackson, P.5
  • 36
    • 5444275067 scopus 로고    scopus 로고
    • The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor
    • DOI 10.1242/jcs.01323
    • von Rotz, R. C., Kohli, B. M., Bosset, J., Meier, M., Suzuki, T., Nitsch, R. M., and Konietzko, U. (2004) The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor. J. Cell Sci. 117, 4435-4448 (Pubitemid 39360070)
    • (2004) Journal of Cell Science , vol.117 , Issue.19 , pp. 4435-4448
    • Von, R.R.C.1    Kohli, B.M.2    Bosset, J.3    Meier, M.4    Suzuki, T.5    Nitsch, R.M.6    Konietzko, U.7
  • 37
    • 84884537710 scopus 로고    scopus 로고
    • Visualization and quantification of APP intracellular domain-mediated nuclear signaling by bimolecular fluorescence complementation
    • Riese, F., Grinschgl, S., Gersbacher, M. T., Russi, N., Hock, C., Nitsch, R. M., and Konietzko, U. (2013) Visualization and quantification of APP intracellular domain-mediated nuclear signaling by bimolecular fluorescence complementation. PLoS One 8, e76094
    • (2013) PLoS One , vol.8
    • Riese, F.1    Grinschgl, S.2    Gersbacher, M.T.3    Russi, N.4    Hock, C.5    Nitsch, R.M.6    Konietzko, U.7
  • 38
    • 84880407705 scopus 로고    scopus 로고
    • Turnover of amyloid precursor protein family members determines their nuclear signaling capability
    • Gersbacher, M. T., Goodger, Z. V., Trutzel, A., Bundschuh, D., Nitsch, R. M., and Konietzko, U. (2013) Turnover of amyloid precursor protein family members determines their nuclear signaling capability. PLoS One 8, e69363
    • (2013) PLoS One , vol.8
    • Gersbacher, M.T.1    Goodger, Z.V.2    Trutzel, A.3    Bundschuh, D.4    Nitsch, R.M.5    Konietzko, U.6
  • 39
    • 34748897213 scopus 로고    scopus 로고
    • Amyloid Precursor Protein Regulates Brain Apolipoprotein E and Cholesterol Metabolism through Lipoprotein Receptor LRP1
    • DOI 10.1016/j.neuron.2007.08.008, PII S0896627307006204
    • Liu, Q., Zerbinatti, C. V., Zhang, J., Hoe, H. S., Wang, B., Cole, S. L., Herz, J., Muglia, L., and Bu, G. (2007) Amyloid precursor protein regulates brain apolipoprotein E and cholesterol metabolism through lipoprotein receptor LRP1. Neuron 56, 66-78 (Pubitemid 47484175)
    • (2007) Neuron , vol.56 , Issue.1 , pp. 66-78
    • Liu, Q.1    Zerbinatti, C.V.2    Zhang, J.3    Hoe, H.-S.4    Wang, B.5    Cole, S.L.6    Herz, J.7    Muglia, L.8    Bu, G.9
  • 40
    • 0037067655 scopus 로고    scopus 로고
    • Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-κB and β-amyloid precursor protein
    • DOI 10.1016/S0092-8674(02)00809-7
    • Baek, S. H., Ohgi, K. A., Rose, D. W., Koo, E. H., Glass, C. K., and Rosenfeld, M. G. (2002) Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-κB and β-amyloid precursor protein. Cell 110, 55-67 (Pubitemid 34874606)
    • (2002) Cell , vol.110 , Issue.1 , pp. 55-67
    • Baek, S.H.1    Ohgi, K.A.2    Rose, D.W.3    Koo, E.H.4    Glass, C.K.5    Rosenfeld, M.G.6
  • 41
    • 2642582435 scopus 로고    scopus 로고
    • Dissection of amyloid-β precursor protein-dependent transcriptional transactivation
    • DOI 10.1074/jbc.M402248200
    • Cao, X., and Südhof, T. C. (2004) Dissection of amyloid-β precursor protein-dependent transcriptional transactivation. J. Biol. Chem. 279, 24601-24611 (Pubitemid 38725327)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.23 , pp. 24601-24611
    • Cao, X.1    Sudhof, T.C.2
  • 42
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptivety active complex of APP with Fe65 and histone acetyltransferase Tip60
    • DOI 10.1126/science.1058783
    • Cao, X., and Südhof, T. C. (2001) A transcriptionally (correction of transcriptively) active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293, 115-120 (Pubitemid 32625507)
    • (2001) Science , vol.293 , Issue.5527 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 43
    • 84899571989 scopus 로고    scopus 로고
    • Intracellular accumulation of amyloid-β - A predictor for synaptic dysfunction and neuron loss in Alzheimer's disease
    • Bayer, T. A., and Wirths, O. (2010) Intracellular accumulation of amyloid-β - a predictor for synaptic dysfunction and neuron loss in Alzheimer's disease. Front. Aging Neurosci. 2, 8
    • (2010) Front. Aging Neurosci. , vol.2 , pp. 8
    • Bayer, T.A.1    Wirths, O.2
  • 46
    • 84871749175 scopus 로고    scopus 로고
    • Differential regulation of amyloid-β endocytic trafficking and lysosomal degradation by apolipoprotein E isoforms
    • Li, J., Kanekiyo, T., Shinohara, M., Zhang, Y., LaDu, M. J., Xu, H., and Bu, G. (2012) Differential regulation of amyloid-β endocytic trafficking and lysosomal degradation by apolipoprotein E isoforms. J. Biol. Chem. 287, 44593-44601
    • (2012) J. Biol. Chem. , vol.287 , pp. 44593-44601
    • Li, J.1    Kanekiyo, T.2    Shinohara, M.3    Zhang, Y.4    LaDu, M.J.5    Xu, H.6    Bu, G.7
  • 47
    • 78049374467 scopus 로고    scopus 로고
    • Novel research horizons for presenilins and γ-secretases in cell biology and disease
    • De Strooper, B., and Annaert, W. (2010) Novel research horizons for presenilins and γ-secretases in cell biology and disease. Annu. Rev. Cell Dev. Biol. 26, 235-260
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 235-260
    • De Strooper, B.1    Annaert, W.2
  • 48
    • 2342495787 scopus 로고    scopus 로고
    • Amyloid β-peptide interactions with neuronal and glial cell plasma membrane: Binding sites and implications for Alzheimer's disease
    • DOI 10.1002/psc.573
    • Verdier, Y., Zarándi, M., and Penke, B. (2004) Amyloid β-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease. J. Pept. Sci. 10, 229-248 (Pubitemid 38594184)
    • (2004) Journal of Peptide Science , vol.10 , Issue.5 , pp. 229-248
    • Verdier, Y.1    Zarandi, M.2    Penke, B.3
  • 49
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Aβ oligomer and Alzheimer's disease: An emperor in need of clothes
    • Benilova, I., Karran, E., and De Strooper, B. (2012) The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes. Nat. Neurosci. 15, 349-357
    • (2012) Nat. Neurosci. , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 50
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
    • Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., and Strittmatter, S. M. (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers. Nature 457, 1128-1132
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Laurén, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 52
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of τ misfolding from the outside to the inside of a cell
    • Frost, B., Jacks, R. L., and Diamond, M. I. (2009) Propagation of τ misfolding from the outside to the inside of a cell. J. Biol. Chem. 284, 12845-12852
    • (2009) J. Biol. Chem. , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 53
    • 84861758226 scopus 로고    scopus 로고
    • Trans-cellular propagation of τ aggregation by fibrillar species
    • Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., and Diamond, M. I. (2012) Trans-cellular propagation of τ aggregation by fibrillar species. J. Biol. Chem. 287, 19440-19451
    • (2012) J. Biol. Chem. , vol.287 , pp. 19440-19451
    • Kfoury, N.1    Holmes, B.B.2    Jiang, H.3    Holtzman, D.M.4    Diamond, M.I.5
  • 55
    • 77954375412 scopus 로고    scopus 로고
    • Astrocytic Aβ 1-42 uptake is determined by Aβ-aggregation state and the presence of amyloid-associated proteins
    • Nielsen, H. M., Mulder, S. D., Beliën, J. A., Musters, R. J., Eikelenboom, P., and Veerhuis, R. (2010) Astrocytic Aβ 1-42 uptake is determined by Aβ-aggregation state and the presence of amyloid-associated proteins. Glia 58, 1235-1246
    • (2010) Glia , vol.58 , pp. 1235-1246
    • Nielsen, H.M.1    Mulder, S.D.2    Beliën, J.A.3    Musters, R.J.4    Eikelenboom, P.5    Veerhuis, R.6
  • 56
    • 69849093363 scopus 로고    scopus 로고
    • Characterisation of the passive permeability barrier of nuclear pore complexes
    • Mohr, D., Frey, S., Fischer, T., Güttler, T., and Görlich, D. (2009) Characterisation of the passive permeability barrier of nuclear pore complexes. EMBO J. 28, 2541-2553
    • (2009) EMBO J. , vol.28 , pp. 2541-2553
    • Mohr, D.1    Frey, S.2    Fischer, T.3    Güttler, T.4    Görlich, D.5
  • 57
    • 80053384785 scopus 로고    scopus 로고
    • Functional activity of the novel Alzheimer's amyloid β-peptide interacting domain (AßID) in the APP and BACE1 promoter sequences and implications in activating apoptotic genes and in amyloidogenesis
    • Bailey, J. A., Maloney, B., Ge, Y. W., and Lahiri, D. K. (2011) Functional activity of the novel Alzheimer's amyloid β-peptide interacting domain (AßID) in the APP and BACE1 promoter sequences and implications in activating apoptotic genes and in amyloidogenesis. Gene 488, 13-22
    • (2011) Gene , vol.488 , pp. 13-22
    • Bailey, J.A.1    Maloney, B.2    Ge, Y.W.3    Lahiri, D.K.4
  • 58
    • 80053385335 scopus 로고    scopus 로고
    • The Alzheimer's amyloid β-peptide (Aβ) binds a specific DNA Aβ-interacting domain (AßID) in the APP, BACE1, and APOE promoters in a sequence-specific manner: Characterizing a new regulatory motif
    • Maloney, B., and Lahiri, D. K. (2011) The Alzheimer's amyloid β-peptide (Aβ) binds a specific DNA Aβ-interacting domain (AßID) in the APP, BACE1, and APOE promoters in a sequence-specific manner: characterizing a new regulatory motif. Gene 488, 1-12
    • (2011) Gene , vol.488 , pp. 1-12
    • Maloney, B.1    Lahiri, D.K.2
  • 60
    • 38049054918 scopus 로고    scopus 로고
    • Interaction between Alzheimer's Aβ1-42 peptide and DNA detected by surface plasmon resonance
    • Barrantes, A., Rejas, M. T., Benítez, M. J., and Jiménez, J. S. (2007) Interaction between Alzheimer's Aβ1-42 peptide and DNA detected by surface plasmon resonance. J. Alzheimer's Dis. 12, 345-355
    • (2007) J. Alzheimer's Dis. , vol.12 , pp. 345-355
    • Barrantes, A.1    Rejas, M.T.2    Benítez, M.J.3    Jiménez, J.S.4
  • 61
    • 67649488309 scopus 로고    scopus 로고
    • Aβ43 is more frequent than Aβ40 in amyloid plaque cores from Alzheimer disease brains
    • Welander, H., Frånberg, J., Graff, C., Sundström, E., Winblad, B., and Tjernberg, L. O. (2009) Aβ43 is more frequent than Aβ40 in amyloid plaque cores from Alzheimer disease brains. J. Neurochem. 110, 697-706
    • (2009) J. Neurochem. , vol.110 , pp. 697-706
    • Welander, H.1    Frånberg, J.2    Graff, C.3    Sundström, E.4    Winblad, B.5    Tjernberg, L.O.6
  • 62
    • 0035425615 scopus 로고    scopus 로고
    • Generation of aggregated β-amyloid in the rat hippocampus impairs synaptic transmission and plasticity and causes memory deficits
    • Stéphan, A., Laroche, S., and Davis, S. (2001) Generation of aggregated β-amyloid in the rat hippocampus impairs synaptic transmission and plasticity and causes memory deficits. J. Neurosci. 21, 5703-5714 (Pubitemid 32692169)
    • (2001) Journal of Neuroscience , vol.21 , Issue.15 , pp. 5703-5714
    • Stephan, A.1    Laroche, S.2    Davis, S.3
  • 64
    • 77954554036 scopus 로고    scopus 로고
    • Immunohistochemical visualization of amyloid-β protein precursor and amyloid-β in extra- and intracellular compartments in the human brain
    • Aho, L., Pikkarainen, M., Hiltunen, M., Leinonen, V., and Alafuzoff, I. (2010) Immunohistochemical visualization of amyloid-β protein precursor and amyloid-β in extra- and intracellular compartments in the human brain. J. Alzheimer's Dis. 20, 1015-1028
    • (2010) J. Alzheimer's Dis. , vol.20 , pp. 1015-1028
    • Aho, L.1    Pikkarainen, M.2    Hiltunen, M.3    Leinonen, V.4    Alafuzoff, I.5


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