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Volumn 19, Issue 4, 2010, Pages 1339-1357

Co-localization of reelin and proteolytic aβpp fragments in hippocampal plaques in aged wild-type mice

Author keywords

Amyloid plaques; A PP; Electron microscopy; Hippocampus; Immunohistochemistry; Mus musculus; Non transgenic; Pepsin treatment; Pre fibrillary oligomers; Sporadic Alzheimer's disease; Stratum lacunosum moleculare; Ultrastructure

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; REELIN;

EID: 77950363927     PISSN: 13872877     EISSN: None     Source Type: Journal    
DOI: 10.3233/JAD-2010-1333     Document Type: Article
Times cited : (39)

References (84)
  • 1
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW (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
  • 2
    • 36248971777 scopus 로고    scopus 로고
    • Mechanisms of amyloid plaque pathogenesis
    • Fiala JC (2007) Mechanisms of amyloid plaque pathogenesis. Acta Neuropathol 114, 551-571.
    • (2007) Acta Neuropathol , vol.114 , pp. 551-571
    • Fiala, J.C.1
  • 4
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 5
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe CG (2008) Structural classification of toxic amyloid oligomers. J Biol Chem 283, 29639-29643.
    • (2008) J Biol Chem , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 7
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability
    • Dahlgren KN, Manelli AM, Stine WB, Jr., Baker LK, Krafft GA, LaDu MJ (2002) Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J Biol Chem 277, 32046-32053.
    • (2002) J Biol Chem , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine Jr., W.B.3    Baker, L.K.4    Krafft, G.A.5    Ladu, M.J.6
  • 8
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley DM, Walsh DM, Ye CP, Diehl T, Vasquez S, Vassilev PM, Teplow DB, Selkoe DJ (1999) Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J Neurosci 19, 8876-8884.
    • (1999) J Neurosci , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 10
    • 0037017399 scopus 로고    scopus 로고
    • Selective cytotoxicity of intracellular amyloid beta peptide1-42 through p53 and Bax in cultured primary human neurons
    • Zhang Y, McLaughlin R, Goodyer C, LeBlanc A (2002) Selective cytotoxicity of intracellular amyloid beta peptide1-42 through p53 and Bax in cultured primary human neurons. J Cell Biol 156, 519-529.
    • (2002) J Cell Biol , vol.156 , pp. 519-529
    • Zhang, Y.1    McLaughlin, R.2    Goodyer, C.3    Le Blanc, A.4
  • 13
    • 34447564164 scopus 로고    scopus 로고
    • Intracellular Abeta and cognitive deficits precede beta-amyloid deposition in transgenic arcAbeta mice
    • Knobloch M, Konietzko U, Krebs DC, Nitsch RM (2007) Intracellular Abeta and cognitive deficits precede beta-amyloid deposition in transgenic arcAbeta mice. Neurobiol Aging 28, 1297-1306.
    • (2007) Neurobiol Aging , vol.28 , pp. 1297-1306
    • Knobloch, M.1    Konietzko, U.2    Krebs, D.C.3    Nitsch, R.M.4
  • 14
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, Rowan MJ, Selkoe DJ (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539.
    • (2002) Nature , vol.416 , 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
  • 15
    • 34447649563 scopus 로고    scopus 로고
    • Abeta oligomer-mediated long-term potentiation impairment involves protein phosphatase 1-dependent mechanisms
    • Knobloch M, Farinelli M, Konietzko U, Nitsch RM, Mansuy IM (2007) Abeta oligomer-mediated long-term potentiation impairment involves protein phosphatase 1-dependent mechanisms. J Neurosci 27, 7648-7653.
    • (2007) J Neurosci , vol.27 , pp. 7648-7653
    • Knobloch, M.1    Farinelli, M.2    Konietzko, U.3    Nitsch, R.M.4    Mansuy, I.M.5
  • 16
    • 34548547281 scopus 로고    scopus 로고
    • Mitochondrial degeneration in dystrophic neurites of senile plaques may lead to extracellular deposition of fine filaments
    • Fiala JC, FeinbergM, Peters A, Barbas H (2007) Mitochondrial degeneration in dystrophic neurites of senile plaques may lead to extracellular deposition of fine filaments. Brain Struct Funct 212, 195-207.
    • (2007) Brain Struct Funct , vol.212 , pp. 195-207
    • Fiala, J.C.1    Feinbergm Peters, A.2    Barbas, H.3
  • 17
    • 0030780381 scopus 로고    scopus 로고
    • Cerebral cortex pathology in aging and Alzheimer's disease: A quantitative survey of large hospital-based geriatric and psychiatric cohorts
    • Giannakopoulos P, Hof PR, Michel JP, Guimon J, Bouras C (1997) Cerebral cortex pathology in aging and Alzheimer's disease: a quantitative survey of large hospital-based geriatric and psychiatric cohorts. Brain Res Brain Res Rev 25, 217-245.
    • (1997) Brain Res Brain Res Rev , vol.25 , pp. 217-245
    • Giannakopoulos, P.1    Hof, P.R.2    Michel, J.P.3    Guimon, J.4    Bouras, C.5
  • 18
    • 0036454716 scopus 로고    scopus 로고
    • Structural changes in the normally aging cerebral cortex of primates
    • Peters A (2002) Structural changes in the normally aging cerebral cortex of primates. Prog Brain Res 136, 455-465.
    • (2002) Prog Brain Res , vol.136 , pp. 455-465
    • Peters, A.1
  • 20
    • 0024158565 scopus 로고
    • Morphologic alterations of cholinergic processes in the neocortex of aged rats
    • Armstrong DM, Hersh LB, Gage FH (1988) Morphologic alterations of cholinergic processes in the neocortex of aged rats. Neurobiol Aging 9, 199-205.
    • (1988) Neurobiol Aging , vol.9 , pp. 199-205
    • Armstrong, D.M.1    Hersh, L.B.2    Gage, F.H.3
  • 21
    • 0031056869 scopus 로고    scopus 로고
    • Murine models of brain aging and age-related neurodegenerative diseases
    • Jucker M, Ingram DK (1997) Murine models of brain aging and age-related neurodegenerative diseases. Behav Brain Res 85, 1-26.
    • (1997) Behav Brain Res , vol.85 , pp. 1-26
    • Jucker, M.1    Ingram, D.K.2
  • 22
    • 0028490884 scopus 로고
    • Agerelated fibrillar deposits in brains of C57BL/6 mice. A review of localization, staining characteristics, and strain specificity
    • Jucker M,Walker LC,KuoH, Tian M, IngramDK(1994) Agerelated fibrillar deposits in brains of C57BL/6 mice. A review of localization, staining characteristics, and strain specificity. Mol Neurobiol 9, 125-133.
    • (1994) Mol Neurobiol , vol.9 , pp. 125-133
    • Jucker, M.1    Walker, L.C.2    Kuo, H.3    Tian, M.4    Ingram, D.K.5
  • 24
    • 0024600330 scopus 로고
    • Cerebral aging: A quantitative study of gliosis in old nude mice
    • Mandybur TI, Ormsby I, Zemlan FP (1989) Cerebral aging: a quantitative study of gliosis in old nude mice. Acta Neuropathol (Berl) 77, 507-513.
    • (1989) Acta Neuropathol (Berl) , vol.77 , pp. 507-513
    • Mandybur, T.I.1    Ormsby, I.2    Zemlan, F.P.3
  • 25
    • 0019732719 scopus 로고
    • The structure of neuritic plaque in the cerebral cortex of aged rats
    • Vaughan DW, Peters A (1981) The structure of neuritic plaque in the cerebral cortex of aged rats. J Neuropathol Exp Neurol 40, 472-487.
    • (1981) J Neuropathol Exp Neurol , vol.40 , pp. 472-487
    • Vaughan, D.W.1    Peters, A.2
  • 27
    • 0034932938 scopus 로고    scopus 로고
    • Role of the reelin signaling pathway in central nervous system development
    • Rice DS, Curran T (2001) Role of the reelin signaling pathway in central nervous system development. Annu Rev Neurosci 24, 1005-1039.
    • (2001) Annu Rev Neurosci , vol.24 , pp. 1005-1039
    • Rice, D.S.1    Curran, T.2
  • 28
    • 0028940096 scopus 로고
    • A protein related to extracellular matrix proteins deleted in the mouse mutant reeler
    • D'Arcangelo G, Miao GG, Chen SC, Soares HD, Morgan JI, Curran T (1995) A protein related to extracellular matrix proteins deleted in the mouse mutant reeler. Nature 374, 719-723.
    • (1995) Nature , vol.374 , pp. 719-723
    • D'Arcangelo, G.1    Miao, G.G.2    Chen, S.C.3    Soares, H.D.4    Morgan, J.I.5    Curran, T.6
  • 31
    • 34547115035 scopus 로고    scopus 로고
    • The extremely conserved C-terminal region of Reelin is not necessary for secretion but is required for efficient activation of downstream signaling
    • Nakano Y, Kohno T, Hibi T, Kohno S, Baba A, Mikoshiba K, Nakajima K, Hattori M (2007) The extremely conserved C-terminal region of Reelin is not necessary for secretion but is required for efficient activation of downstream signaling. J Biol Chem 282, 20544-20552.
    • (2007) J Biol Chem , vol.282 , pp. 20544-20552
    • Nakano, Y.1    Kohno, T.2    Hibi, T.3    Kohno, S.4    Baba, A.5    Mikoshiba, K.6    Nakajima, K.7    Hattori, M.8
  • 32
    • 0001025605 scopus 로고    scopus 로고
    • Reelin, the extracellular matrix protein deficient in reeler mutant mice, is processed by a metalloproteinase
    • Lambert de Rouvroit C, de Bergeyck V, Cortvrindt C, Bar I, Eeckhout Y, Goffinet AM (1999) Reelin, the extracellular matrix protein deficient in reeler mutant mice, is processed by a metalloproteinase. Exp Neurol 156, 214-217.
    • (1999) Exp Neurol , vol.156 , pp. 214-217
    • Lambert De Rouvroit, C.1    De Bergeyck, V.2    Cortvrindt, C.3    Bar, I.4    Eeckhout, Y.5    Goffinet, A.M.6
  • 33
    • 33750333569 scopus 로고    scopus 로고
    • Reelin, lipoprotein receptors and synaptic plasticity
    • Herz J, ChenY(2006) Reelin, lipoprotein receptors and synaptic plasticity. Nat Rev Neurosci 7, 850-859.
    • (2006) Nat Rev Neurosci , vol.7 , pp. 850-859
    • Herz, J.1    Chen, Y.2
  • 34
    • 33644512817 scopus 로고    scopus 로고
    • Functional dissection of Reelin signaling by site-directed disruption of Disabled-1 adaptor binding to apolipoprotein e receptor 2: Distinct roles in development and synaptic plasticity
    • Beffert U, Durudas A,Weeber EJ, Stolt PC, Giehl KM, Sweatt JD, Hammer RE, Herz J (2006) Functional dissection of Reelin signaling by site-directed disruption of Disabled-1 adaptor binding to apolipoprotein E receptor 2: distinct roles in development and synaptic plasticity. J Neurosci 26, 2041-2052.
    • (2006) J Neurosci , vol.26 , pp. 2041-2052
    • Beffert, U.1    Durudas, A.2    Weeber, E.J.3    Stolt, P.C.4    Giehl, K.M.5    Sweatt, J.D.6    Hammer, R.E.7    Herz, J.8
  • 38
    • 33845925306 scopus 로고    scopus 로고
    • Dab1 and Reelin effects on APP and ApoEr2 trafficking and processing
    • Hoe HS, Tran TS, Matsuoka Y, Howell BW, Rebeck GW (2006) Dab1 and Reelin effects on APP and ApoEr2 trafficking and processing. J Biol Chem 281, 35176-35185.
    • (2006) J Biol Chem , vol.281 , pp. 35176-35185
    • Hoe, H.S.1    Tran, T.S.2    Matsuoka, Y.3    Howell, B.W.4    Rebeck, G.W.5
  • 39
    • 1442300201 scopus 로고    scopus 로고
    • Reelin and cyclin-dependent kinase 5-dependent signals cooperate in regulating neuronal migration and synaptic transmission
    • Beffert U, Weeber EJ, Morfini G, Ko J, Brady ST, Tsai LH, Sweatt JD, Herz J (2004) Reelin and cyclin-dependent kinase 5-dependent signals cooperate in regulating neuronal migration and synaptic transmission. J Neurosci 24, 1897-1906.
    • (2004) J Neurosci , vol.24 , pp. 1897-1906
    • Beffert, U.1    Weeber, E.J.2    Morfini, G.3    Ko, J.4    Brady, S.T.5    Tsai, L.H.6    Sweatt, J.D.7    Herz, J.8
  • 40
    • 0033213319 scopus 로고    scopus 로고
    • Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation
    • Hiesberger T, TrommsdorffM, Howell BW, Goffinet A, Mumby MC, Cooper JA, Herz J (1999) Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation. Neuron 24, 481-489.
    • (1999) Neuron , vol.24 , pp. 481-489
    • Hiesberger, T.1    Trommsdorff, M.2    Howell, B.W.3    Goffinet, A.4    Mumby, M.C.5    Cooper, J.A.6    Herz, J.7
  • 48
    • 33751216748 scopus 로고    scopus 로고
    • Differential expression of PSD proteins in age-related spatial learning impairments
    • Nyffeler M, Zhang WN, Feldon J, Knuesel I (2007) Differential expression of PSD proteins in age-related spatial learning impairments. Neurobiol Aging 28, 143-155.
    • (2007) Neurobiol Aging , vol.28 , pp. 143-155
    • Nyffeler, M.1    Zhang, W.N.2    Feldon, J.3    Knuesel, I.4
  • 49
    • 33947320450 scopus 로고    scopus 로고
    • Reelin depletion in the entorhinal cortex of human amyloid precursor protein transgenic mice and humans with Alzheimer's disease
    • Chin J, Massaro CM, Palop JJ, Thwin MT, Yu GQ, Bien-Ly N, Bender A, Mucke L (2007) Reelin depletion in the entorhinal cortex of human amyloid precursor protein transgenic mice and humans with Alzheimer's disease. J Neurosci 27, 2727-2733.
    • (2007) J Neurosci , vol.27 , pp. 2727-2733
    • Chin, J.1    Massaro, C.M.2    Palop, J.J.3    Thwin, M.T.4    Yu, G.Q.5    Bien-Ly, N.6    Bender, A.7    Mucke, L.8
  • 50
    • 25144462642 scopus 로고    scopus 로고
    • Reelin-immunoreactivity in the hippocampal formation of 9-month-old wildtype mouse: Effects of APP/PS1 genotype and ovariectomy
    • Miettinen R, Riedel A, Kalesnykas G, Kettunen HP, Puolivali J, Soininen H, Arendt T (2005) Reelin-immunoreactivity in the hippocampal formation of 9-month-old wildtype mouse: effects of APP/PS1 genotype and ovariectomy. J Chem Neuroanat 30, 105-118.
    • (2005) J Chem Neuroanat , vol.30 , pp. 105-118
    • Miettinen, R.1    Riedel, A.2    Kalesnykas, G.3    Kettunen, H.P.4    Puolivali, J.5    Soininen, H.6    Arendt, T.7
  • 51
    • 33644961448 scopus 로고    scopus 로고
    • Extracellular matrix molecules and synaptic plasticity: Immunomapping of intracellular and secreted Reelin in the adult rat brain
    • Ramos-Moreno T, Galazo MJ, Porrero C, Martinez-Cerdeno V, Clasca F (2006) Extracellular matrix molecules and synaptic plasticity: immunomapping of intracellular and secreted Reelin in the adult rat brain. Eur J Neurosci 23, 401-422.
    • (2006) Eur J Neurosci , vol.23 , pp. 401-422
    • Ramos-Moreno, T.1    Galazo, M.J.2    Porrero, C.3    Martinez-Cerdeno, V.4    Clasca, F.5
  • 52
    • 0344197998 scopus 로고    scopus 로고
    • Immunocytochemical localization of reelin in the olfactory bulb of the heterozygous reeler mouse: An animal model for schizophrenia
    • Pappas GD, Kriho V, Liu WS, Tremolizzo L, Lugli G, Larson J (2003) Immunocytochemical localization of reelin in the olfactory bulb of the heterozygous reeler mouse: an animal model for schizophrenia. Neurol Res 25, 819-830.
    • (2003) Neurol Res , vol.25 , pp. 819-830
    • Pappas, G.D.1    Kriho, V.2    Liu, W.S.3    Tremolizzo, L.4    Lugli, G.5    Larson, J.6
  • 53
    • 0035739009 scopus 로고    scopus 로고
    • Reelin in the extracellular matrix and dendritic spines of the cortex and hippocampus: A comparison between wild type and heterozygous reeler mice by immunoelectron microscopy
    • Pappas GD, Kriho V, Pesold C (2001) Reelin in the extracellular matrix and dendritic spines of the cortex and hippocampus: a comparison between wild type and heterozygous reeler mice by immunoelectron microscopy. J Neurocytol 30, 413-425.
    • (2001) J Neurocytol , vol.30 , pp. 413-425
    • Pappas, G.D.1    Kriho, V.2    Pesold, C.3
  • 54
    • 30344478220 scopus 로고    scopus 로고
    • Neuronal or glial expression of human apolipoprotein e4 affects parenchymal and vascular amyloid pathology differentially in different brain regions of double- and tripletransgenic mice
    • Van Dooren T, Muyllaert D, Borghgraef P, Cresens A, Devijver H, Van der Auwera I, Wera S, Dewachter I, Van Leuven F (2006) Neuronal or glial expression of human apolipoprotein e4 affects parenchymal and vascular amyloid pathology differentially in different brain regions of double- and tripletransgenic mice. Am J Pathol 168, 245-260.
    • (2006) Am J Pathol , vol.168 , pp. 245-260
    • Van Dooren, T.1    Muyllaert, D.2    Borghgraef, P.3    Cresens, A.4    Devijver, H.5    Van Der Auwera, I.6    Wera, S.7    Dewachter, I.8    Van Leuven, F.9
  • 56
    • 0027439062 scopus 로고
    • Amyloid-like properties of peptides flanking the epitope of amyloid precursor protein-specific monoclonal antibody 22C11
    • Hilbich C, Monning U, Grund C, Masters CL, Beyreuther K (1993) Amyloid-like properties of peptides flanking the epitope of amyloid precursor protein-specific monoclonal antibody 22C11. J Biol Chem 268, 26571-26577.
    • (1993) J Biol Chem , vol.268 , pp. 26571-26577
    • Hilbich, C.1    Monning, U.2    Grund, C.3    Masters, C.L.4    Beyreuther, K.5
  • 57
    • 0026775078 scopus 로고
    • Antibody to beta-amyloid precursor protein recognizes an intermediate filament-associated protein in Alzheimer's and control fibroblasts
    • Dooley NP, Gauthier S, Durham HD (1992) Antibody to beta-amyloid precursor protein recognizes an intermediate filament-associated protein in Alzheimer's and control fibroblasts. J Neurosci Res 33, 60-67.
    • (1992) J Neurosci Res , vol.33 , pp. 60-67
    • Dooley, N.P.1    Gauthier, S.2    Durham, H.D.3
  • 58
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev A, McLaughlin T, O'Leary DD, 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
  • 59
    • 1542359477 scopus 로고    scopus 로고
    • A phosphorylated, carboxyterminal fragment of beta-amyloid precursor protein localizes to the splicing factor compartment
    • Muresan Z, Muresan V (2004) A phosphorylated, carboxyterminal fragment of beta-amyloid precursor protein localizes to the splicing factor compartment. Hum Mol Genet 13, 475-488.
    • (2004) Hum Mol Genet , vol.13 , pp. 475-488
    • Muresan, Z.1    Muresan, V.2
  • 61
    • 12944325316 scopus 로고    scopus 로고
    • Molecular heterogeneity of the dystrophin-associated protein complex in the mouse kidney nephron: Differential alterations in the absence of utrophin and dystrophin
    • Haenggi T, Schaub MC, Fritschy JM (2005) Molecular heterogeneity of the dystrophin-associated protein complex in the mouse kidney nephron: differential alterations in the absence of utrophin and dystrophin. Cell Tissue Res 319, 299-313.
    • (2005) Cell Tissue Res , vol.319 , pp. 299-313
    • Haenggi, T.1    Schaub, M.C.2    Fritschy, J.M.3
  • 62
    • 33747383933 scopus 로고    scopus 로고
    • Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue
    • Haenggi T, Fritschy JM (2006) Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue. Cell Mol Life Sci 63, 1614-1631.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1614-1631
    • Haenggi, T.1    Fritschy, J.M.2
  • 63
    • 0027941064 scopus 로고
    • Glycinergic synapses in the rod pathway of the rat retina: Cone bipolar cells express the alpha 1 subunit of the glycine receptor
    • Sassoe-Pognetto M, Wassle H, Grunert U (1994) Glycinergic synapses in the rod pathway of the rat retina: cone bipolar cells express the alpha 1 subunit of the glycine receptor. J Neurosci 14, 5131-5146.
    • (1994) J Neurosci , vol.14 , pp. 5131-5146
    • Sassoe-Pognetto, M.1    Wassle, H.2    Grunert, U.3
  • 65
    • 0025734549 scopus 로고
    • Human and rodent sequence analogs of Alzheimer's amyloid beta A4 share similar properties and can be solubilized in buffers of pH 7.4
    • Hilbich C, Kisters-Woike B, Reed J, Masters CL, Beyreuther K (1991) Human and rodent sequence analogs of Alzheimer's amyloid beta A4 share similar properties and can be solubilized in buffers of pH 7.4. Eur J Biochem 201, 61-69.
    • (1991) Eur J Biochem , vol.201 , pp. 61-69
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 66
    • 0031842886 scopus 로고    scopus 로고
    • Selective scarcity of NMDA receptor channel subunits in the stratum lucidum (mossy fibre-recipient layer) of the mouse hippocampal CA3 subfield
    • Watanabe M, Fukaya M, Sakimura K, Manabe T, Mishina M, Inoue Y (1998) Selective scarcity of NMDA receptor channel subunits in the stratum lucidum (mossy fibre-recipient layer) of the mouse hippocampal CA3 subfield. Eur J Neurosci 10, 478-487.
    • (1998) Eur J Neurosci , vol.10 , pp. 478-487
    • Watanabe, M.1    Fukaya, M.2    Sakimura, K.3    Manabe, T.4    Mishina, M.5    Inoue, Y.6
  • 68
    • 0024005801 scopus 로고
    • Alzheimer's disease amyloidogenic glycoprotein: Expression pattern in rat brain suggests a role in cell contact
    • Shivers BD, Hilbich C, Multhaup G, Salbaum M, Beyreuther K, Seeburg PH (1988) Alzheimer's disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact. EMBO J 7, 1365-1370.
    • (1988) EMBO J , vol.7 , pp. 1365-1370
    • Shivers, B.D.1    Hilbich, C.2    Multhaup, G.3    Salbaum, M.4    Beyreuther, K.5    Seeburg, P.H.6
  • 70
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT, Jr. (1993) Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 71
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid beta A4 peptides of Alzheimer's disease
    • Hilbich C, Kisters-Woike B, Reed J, Masters CL, Beyreuther K (1991) Aggregation and secondary structure of synthetic amyloid beta A4 peptides of Alzheimer's disease. J Mol Biol 218, 149-163.
    • (1991) J Mol Biol , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 72
    • 0018460806 scopus 로고
    • The specificity of some pig and human pepsins towards synthetic peptide substrates
    • Ryle AP, Auffret CA (1979) The specificity of some pig and human pepsins towards synthetic peptide substrates. Biochem J 179, 247-249.
    • (1979) Biochem J , vol.179 , pp. 247-249
    • Ryle, A.P.1    Auffret, C.A.2
  • 73
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • Dunn BM (2002) Structure and mechanism of the pepsin-like family of aspartic peptidases. Chem Rev 102, 4431-4458.
    • (2002) Chem Rev , vol.102 , pp. 4431-4458
    • Dunn, B.M.1
  • 74
    • 11244262612 scopus 로고    scopus 로고
    • Ultrastructural localization of reelin in the cortex in post-mortem human brain
    • Roberts RC, Xu L, Roche JK, Kirkpatrick B (2005) Ultrastructural localization of reelin in the cortex in post-mortem human brain. J Comp Neurol 482, 294-308.
    • (2005) J Comp Neurol , vol.482 , pp. 294-308
    • Roberts, R.C.1    Xu, L.2    Roche, J.K.3    Kirkpatrick, B.4
  • 75
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT (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
  • 76
    • 0036312590 scopus 로고    scopus 로고
    • Secreted Reelin molecules form homodimers
    • Kubo K, Mikoshiba K, Nakajima K (2002) Secreted Reelin molecules form homodimers. Neurosci Res 43, 381-388.
    • (2002) Neurosci Res , vol.43 , pp. 381-388
    • Kubo, K.1    Mikoshiba, K.2    Nakajima, K.3
  • 77
    • 0034662978 scopus 로고    scopus 로고
    • Reelin molecules assemble together to form a large protein complex, which is inhibited by the function-blocking CR-50 antibody
    • Utsunomiya-Tate N, Kubo K, Tate S, Kainosho M, Katayama E, Nakajima K, Mikoshiba K (2000) Reelin molecules assemble together to form a large protein complex, which is inhibited by the function-blocking CR-50 antibody. Proc Natl Acad Sci U S A 97, 9729-9734.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 9729-9734
    • Utsunomiya-Tate, N.1    Kubo, K.2    Tate, S.3    Kainosho, M.4    Katayama, E.5    Nakajima, K.6    Mikoshiba, K.7
  • 79
    • 34547173322 scopus 로고    scopus 로고
    • Structure of a receptor-binding fragment of reelin and mutational analysis reveal a recognition mechanism similar to endocytic receptors
    • Yasui N, Nogi T, Kitao T, Nakano Y, Hattori M, Takagi J (2007) Structure of a receptor-binding fragment of reelin and mutational analysis reveal a recognition mechanism similar to endocytic receptors. Proc Natl Acad Sci US A 104, 9988-9993.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 9988-9993
    • Yasui, N.1    Nogi, T.2    Kitao, T.3    Nakano, Y.4    Hattori, M.5    Takagi, J.6
  • 82
    • 21644480134 scopus 로고    scopus 로고
    • Morphological and morphometric alterations of Cajal-Retzius cells in early cases of Alzheimer's disease: A Golgi and electron microscope study
    • Baloyannis SJ (2005) Morphological and morphometric alterations of Cajal-Retzius cells in early cases of Alzheimer's disease: a Golgi and electron microscope study. Int J Neurosci 115, 965-980.
    • (2005) Int J Neurosci , vol.115 , pp. 965-980
    • Baloyannis, S.J.1
  • 84
    • 0344643466 scopus 로고    scopus 로고
    • Altered levels of cerebrospinal fluid reelin in frontotemporal dementia and Alzheimer's disease
    • Saez-Valero J, Costell M, Sjogren M, Andreasen N, Blennow K, Luque JM (2003) Altered levels of cerebrospinal fluid reelin in frontotemporal dementia and Alzheimer's disease. J Neurosci Res 72, 132-136.
    • (2003) J Neurosci Res , vol.72 , pp. 132-136
    • Saez-Valero, J.1    Costell, M.2    Sjogren, M.3    Andreasen, N.4    Blennow, K.5    Luque, J.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.