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Volumn 1, Issue 1, 2010, Pages 12-29

Reelin-mediated signaling during normal and pathological forms of aging

Author keywords

Aging; Alzheimer's disease; APP processing; Cognitive impairments; In utero infection; Inflammation; Mid and late gestation; Neurodegeneration; polyriboinosinic polyribocytodilic acid; Tau phosphorylation

Indexed keywords

MUS MUSCULUS;

EID: 80755185579     PISSN: None     EISSN: 21525250     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (28)

References (137)
  • 2
    • 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, 156:214-7.
    • (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
  • 3
    • 0036312590 scopus 로고    scopus 로고
    • Secreted Reelin molecules form homodimers
    • Kubo K, Mikoshiba K, Nakajima K (2002). Secreted Reelin molecules form homodimers. Neurosci Res, 43:381-8.
    • (2002) Neurosci Res , vol.43 , pp. 381-388
    • Kubo, K.1    Mikoshiba, K.2    Nakajima, K.3
  • 4
    • 65249162798 scopus 로고    scopus 로고
    • The N-terminal region of reelin regulates postnatal dendritic maturation of cortical pyramidal neurons
    • Chameau P, Inta D, Vitalis T, Monyer H, Wadman WJ, van Hooft JA (2009). The N-terminal region of reelin regulates postnatal dendritic maturation of cortical pyramidal neurons. Proc Natl Acad Sci U S A,106:7227-32.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7227-7232
    • Chameau, P.1    Inta, D.2    Vitalis, T.3    Monyer, H.4    Wadman, W.J.5    van Hooft, J.A6
  • 5
    • 34247354614 scopus 로고    scopus 로고
    • Processing of Reelin by embryonic neurons is important for function in tissue but not in dissociated cultured neurons
    • Jossin Y, Gui L, Goffinet AM (2007). Processing of Reelin by embryonic neurons is important for function in tissue but not in dissociated cultured neurons. J Neurosci, 27:4243-52.
    • (2007) J Neurosci , vol.27 , pp. 4243-4252
    • Jossin, Y.1    Gui, L.2    Goffinet, A.M.3
  • 6
    • 1642540032 scopus 로고    scopus 로고
    • The central fragment of Reelin, generated by proteolytic processing in vivo, is critical to its function during cortical plate development
    • Jossin Y, Ignatova N, Hiesberger T, Herz J, Lambert de Rouvroit C, Goffinet AM (2004). The central fragment of Reelin, generated by proteolytic processing in vivo, is critical to its function during cortical plate development. J Neurosci, 24:514-21.
    • (2004) J Neurosci , vol.24 , pp. 514-521
    • Jossin, Y.1    Ignatova, N.2    Hiesberger, T.3    Herz, J.4    Lambert de Rouvroit, C.5    Goffinet, A.M.6
  • 9
    • 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, 282:20544-52.
    • (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
  • 11
    • 77954203843 scopus 로고    scopus 로고
    • Reelin-mediated signaling in neuropsychiatric and neurodegenerative diseases
    • Knuesel I (2010). Reelin-mediated signaling in neuropsychiatric and neurodegenerative diseases. Prog Neurobiol, 91(4):257-74.
    • (2010) Prog Neurobiol , vol.91 , Issue.4 , pp. 257-274
    • Knuesel, I.1
  • 12
  • 13
    • 39949084146 scopus 로고    scopus 로고
    • A mechanism for inside-out lamination in the neocortex
    • Cooper JA (2008). A mechanism for inside-out lamination in the neocortex. Trends Neurosci,31:113-9.
    • (2008) Trends Neurosci , vol.31 , pp. 113-119
    • Cooper, J.A1
  • 14
    • 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, 374:719-23.
    • (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
  • 16
    • 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,24:481-9.
    • (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
  • 17
    • 0033066680 scopus 로고    scopus 로고
    • The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids
    • Howell BW, Lanier LM, Frank R, Gertler FB, Cooper JA (1999). The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids. Mol Cell Biol,19:5179-88.
    • (1999) Mol Cell Biol , vol.19 , pp. 5179-5188
    • Howell, B.W.1    Lanier, L.M.2    Frank, R.3    Gertler, F.B.4    Cooper, J.A5
  • 19
    • 33845925306 scopus 로고    scopus 로고
    • DAB1 and Reelin effects on amyloid precursor protein and ApoE receptor 2 trafficking and processing
    • Hoe HS, Tran TS, Matsuoka Y, Howell BW, Rebeck GW (2006). DAB1 and Reelin effects on amyloid precursor protein and ApoE receptor 2 trafficking and processing. J Biol Chem, 281:35176-85.
    • (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
  • 20
    • 0033198295 scopus 로고    scopus 로고
    • Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1
    • Homayouni R, Rice DS, Sheldon M, Curran T (1999). Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. J Neurosci, 19:7507-15.
    • (1999) J Neurosci , vol.19 , pp. 7507-7515
    • Homayouni, R.1    Rice, D.S.2    Sheldon, M.3    Curran, T.4
  • 22
    • 0032509346 scopus 로고    scopus 로고
    • Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein
    • TrommsdorffM, Borg JP, Margolis B, Herz J (1998). Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein. J Biol Chem, 273:33556-60.
    • (1998) J Biol Chem , vol.273 , pp. 33556-33560
    • Trommsdorff, M.1    Borg, J.P.2    Margolis, B.3    Herz, J.4
  • 23
    • 0141755223 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase interacts with the adaptor protein Dab1 in response to Reelin signaling and is required for normal cortical lamination
    • Bock HH, Jossin Y, Liu P, Forster E, May P, Goffinet AM, Herz J (2003). Phosphatidylinositol 3-kinase interacts with the adaptor protein Dab1 in response to Reelin signaling and is required for normal cortical lamination. J Biol Chem, 278:38772-9.
    • (2003) J Biol Chem , vol.278 , pp. 38772-38779
    • Bock, H.H.1    Jossin, Y.2    Liu, P.3    Forster, E.4    May, P.5    Goffinet, A.M.6    Herz, J.7
  • 24
    • 0345894331 scopus 로고    scopus 로고
    • Reelin-mediated signaling locally regulates protein kinase B/Akt and glycogen synthase kinase 3beta
    • Beffert U, Morfini G, Bock HH, Reyna H, Brady ST, Herz J (2002). Reelin-mediated signaling locally regulates protein kinase B/Akt and glycogen synthase kinase 3beta. J Biol Chem, 277:49958-64.
    • (2002) J Biol Chem , vol.277 , pp. 49958-49964
    • Beffert, U.1    Morfini, G.2    Bock, H.H.3    Reyna, H.4    Brady, S.T.5    Herz, J.6
  • 25
    • 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, 24:1897-906.
    • (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
  • 26
    • 58149389019 scopus 로고    scopus 로고
    • Reelin stabilizes the actin cytoskeleton of neuronal processes by inducing n-cofilin phosphorylation at serine3
    • Chai X, Forster E, Zhao S, Bock HH, Frotscher M (2009). Reelin stabilizes the actin cytoskeleton of neuronal processes by inducing n-cofilin phosphorylation at serine3. J Neurosci,29:288-99.
    • (2009) J Neurosci , vol.29 , pp. 288-299
    • Chai, X.1    Forster, E.2    Zhao, S.3    Bock, H.H.4    Frotscher, M.5
  • 27
    • 0021168726 scopus 로고
    • Events governing organization of postmigratory neurons: studies on brain development in normal and reeler mice.
    • Goffinet AM (1984). Events governing organization of postmigratory neurons: studies on brain development in normal and reeler mice. Brain Res,319:261-96.
    • (1984) Brain Res , vol.319 , pp. 261-296
    • Goffinet, A.M1
  • 30
    • 77951167145 scopus 로고    scopus 로고
    • Differential functions of ApoER2 and very low density lipoprotein receptor in Reelin signaling depend on differential sorting of the receptors
    • Duit S, Mayer H, Blake SM, Schneider WJ, Nimpf J (2010). Differential functions of ApoER2 and very low density lipoprotein receptor in Reelin signaling depend on differential sorting of the receptors. J Biol Chem, 285:4896-908.
    • (2010) J Biol Chem , vol.285 , pp. 4896-4908
    • Duit, S.1    Mayer, H.2    Blake, S.M.3    Schneider, W.J.4    Nimpf, J.5
  • 31
    • 0344197741 scopus 로고    scopus 로고
    • Cooper JA. Regulation of protein tyrosine kinase signaling by substrate degradation during brain development.
    • Arnaud L, Ballif BA (2003), Cooper JA. Regulation of protein tyrosine kinase signaling by substrate degradation during brain development. Mol Cell Biol, 23:9293-302.
    • (2003) Mol Cell Biol , vol.23 , pp. 9293-9302
    • Arnaud, L.1    Ballif, B.A2
  • 32
    • 4043068564 scopus 로고    scopus 로고
    • Apolipoprotein E receptors are required for reelin-induced proteasomal degradation of the neuronal adaptor protein Disabled-1
    • Bock HH, Jossin Y, May P, Bergner O, Herz J (2004). Apolipoprotein E receptors are required for reelin-induced proteasomal degradation of the neuronal adaptor protein Disabled-1. J Biol Chem, 279:33471-9.
    • (2004) J Biol Chem , vol.279 , pp. 33471-33479
    • Bock, H.H.1    Jossin, Y.2    May, P.3    Bergner, O.4    Herz, J.5
  • 33
    • 20444500505 scopus 로고    scopus 로고
    • Disabled1 regulates the intracellular trafficking of reelin receptors
    • Morimura T, Hattori M, Ogawa M, Mikoshiba K (2005). Disabled1 regulates the intracellular trafficking of reelin receptors. J Biol Chem, 280:16901-8.
    • (2005) J Biol Chem , vol.280 , pp. 16901-16908
    • Morimura, T.1    Hattori, M.2    Ogawa, M.3    Mikoshiba, K.4
  • 34
    • 0032191870 scopus 로고    scopus 로고
    • Cajal-Retzius cells, Reelin, and the formation of layers
    • Frotscher M (1998). Cajal-Retzius cells, Reelin, and the formation of layers. Curr Opin Neurobiol, 8:570-5.
    • (1998) Curr Opin Neurobiol , vol.8 , pp. 570-575
    • Frotscher, M.1
  • 35
    • 0041379872 scopus 로고    scopus 로고
    • Reelin-expressing neurons in the postnatal and adult human hippocampal formation
    • Abraham H, Meyer G (2003). Reelin-expressing neurons in the postnatal and adult human hippocampal formation. Hippocampus, 13:715-27.
    • (2003) Hippocampus , vol.13 , pp. 715-727
    • Abraham, H.1    Meyer, G.2
  • 36
    • 2342522038 scopus 로고    scopus 로고
    • p73 and Reelin in Cajal-Retzius cells of the developing human hippocampal formation
    • Abraham H, Perez-Garcia CG, Meyer G (2004). p73 and Reelin in Cajal-Retzius cells of the developing human hippocampal formation. Cereb Cortex, 14:484-95.
    • (2004) Cereb Cortex , vol.14 , pp. 484-495
    • Abraham, H.1    Perez-Garcia, C.G.2    Meyer, G.3
  • 37
    • 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, 15:965-80.
    • (2005) Int J Neurosci , vol.15 , pp. 965-980
    • Baloyannis, S.J.1
  • 38
    • 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, 27:2727-33.
    • (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
  • 40
    • 0034724228 scopus 로고    scopus 로고
    • Reelin secretion from glutamatergic neurons in culture is independent from neurotransmitter regulation
    • Lacor PN, Grayson DR, Auta J, Sugaya I, Costa E, Guidotti A (2000). Reelin secretion from glutamatergic neurons in culture is independent from neurotransmitter regulation. Proc Natl Acad Sci U S A, 97:3556-61.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 3556-3561
    • Lacor, P.N.1    Grayson, D.R.2    Auta, J.3    Sugaya, I.4    Costa, E.5    Guidotti, A.6
  • 41
    • 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, 30:105-18.
    • (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
  • 42
    • 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, 25:819-30.
    • (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
  • 44
    • 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, 23:401-22.
    • (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
  • 47
    • 0038580991 scopus 로고    scopus 로고
    • Reelin controls granule cell migration in the dentate gyrus by acting on the radial glial scaffold.
    • Frotscher M, Haas CA, Forster E (2003). Reelin controls granule cell migration in the dentate gyrus by acting on the radial glial scaffold. Cereb Cortex,13:634-40.
    • (2003) Cereb Cortex , vol.13 , pp. 634-640
    • Frotscher, M.1    Haas, C.A.2    Forster, E.3
  • 48
    • 0015799240 scopus 로고
    • Long-lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path
    • Bliss TV, Lomo T (1973). Long-lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path. J Physiol, 232:331-56.
    • (1973) J Physiol , vol.232 , pp. 331-356
    • Bliss, T.V.1    Lomo, T.2
  • 50
    • 33750333569 scopus 로고    scopus 로고
    • Reelin, lipoprotein receptors and synaptic plasticity.
    • Herz J, Chen Y (2006). Reelin, lipoprotein receptors and synaptic plasticity. Nat Rev Neurosci,7:850-9.
    • (2006) Nat Rev Neurosci , vol.7 , pp. 850-859
    • Herz, J.1    Chen, Y.2
  • 52
    • 33845606845 scopus 로고    scopus 로고
    • Differential reelin-induced enhancement of NMDA and AMPA receptor activity in the adult hippocampus
    • Qiu S, Zhao LF, Korwek KM, Weeber EJ (2006). Differential reelin-induced enhancement of NMDA and AMPA receptor activity in the adult hippocampus. J Neurosci, 26:12943-55.
    • (2006) J Neurosci , vol.26 , pp. 12943-12955
    • Qiu, S.1    Zhao, L.F.2    Korwek, K.M.3    Weeber, E.J.4
  • 53
    • 0242363254 scopus 로고    scopus 로고
    • The long-term potential of LTP
    • Malenka RC (2003). The long-term potential of LTP. Nat Rev Neurosci,4:923-6.
    • (2003) Nat Rev Neurosci , vol.4 , pp. 923-926
    • Malenka, R.C1
  • 54
    • 0034682827 scopus 로고    scopus 로고
    • Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction
    • Gotthardt M, TrommsdorffM, Nevitt MF, Shelton J, Richardson JA, Stockinger W, Nimpf J, Herz J (2000). Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction. J Biol Chem, 275:25616-24.
    • (2000) J Biol Chem , vol.275 , pp. 25616-25624
    • Gotthardt, M.1    Trommsdorff, M.2    Nevitt, M.F.3    Shelton, J.4    Richardson, J.A.5    Stockinger, W.6    Nimpf, J.7    Herz, J.8
  • 56
    • 35148880174 scopus 로고    scopus 로고
    • Reelin signals through phosphatidylinositol 3-kinase and Akt to control cortical development and through mTor to regulate dendritic growth.
    • Jossin Y, Goffinet AM (2007). Reelin signals through phosphatidylinositol 3-kinase and Akt to control cortical development and through mTor to regulate dendritic growth. Mol Cell Biol,27:7113-24.
    • (2007) Mol Cell Biol , vol.27 , pp. 7113-7124
    • Jossin, Y.1    Goffinet, A.M2
  • 57
    • 46749093398 scopus 로고    scopus 로고
    • Reduction of Crk and CrkL expression blocks reelin-induced dendritogenesis
    • Matsuki T, Pramatarova A, Howell BW (2008). Reduction of Crk and CrkL expression blocks reelin-induced dendritogenesis. J Cell Sci, 121:1869-75.
    • (2008) J Cell Sci , vol.121 , pp. 1869-1875
    • Matsuki, T.1    Pramatarova, A.2    Howell, B.W.3
  • 58
    • 0347318070 scopus 로고    scopus 로고
    • Reelin promotes hippocampal dendrite development through the VLDLR/ApoER2-Dab1 pathway
    • Niu S, Renfro A, Quattrocchi CC, Sheldon M, D'Arcangelo G (2004). Reelin promotes hippocampal dendrite development through the VLDLR/ApoER2-Dab1 pathway. Neuron, 41:71-84.
    • (2004) Neuron , vol.41 , pp. 71-84
    • Niu, S.1    Renfro, A.2    Quattrocchi, C.C.3    Sheldon, M.4    D'Arcangelo, G.5
  • 59
    • 55249114701 scopus 로고    scopus 로고
    • The Reelin signaling pathway promotes dendritic spine development in hippocampal neurons
    • Niu S, Yabut O, D'Arcangelo G (2008). The Reelin signaling pathway promotes dendritic spine development in hippocampal neurons. J Neurosci, 28:10339-48.
    • (2008) J Neurosci , vol.28 , pp. 10339-10348
    • Niu, S.1    Yabut, O.2    D'Arcangelo, G.3
  • 60
    • 0018486153 scopus 로고
    • The morphology of the hippocampus and dentate gyrus in normal and reeler mice
    • Stanfield BB, Cowan WM (1979). The morphology of the hippocampus and dentate gyrus in normal and reeler mice. J Comp Neurol, 185:393-422.
    • (1979) J Comp Neurol , vol.185 , pp. 393-422
    • Stanfield, B.B.1    Cowan, W.M.2
  • 61
    • 0018757238 scopus 로고
    • The development of the hippocampus and dentate gyrus in normal and reeler mice
    • Stanfield BB, Cowan WM (1979). The development of the hippocampus and dentate gyrus in normal and reeler mice. J Comp Neurol, 185:423-59.
    • (1979) J Comp Neurol , vol.185 , pp. 423-459
    • Stanfield, B.B.1    Cowan, W.M.2
  • 63
    • 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, 30:413-25.
    • (2001) J Neurocytol , vol.30 , pp. 413-425
    • Pappas, G.D.1    Kriho, V.2    Pesold, C.3
  • 66
    • 0032551514 scopus 로고    scopus 로고
    • Prenatal development of reelin-immunoreactive neurons in the human neocortex
    • Meyer G, Goffinet AM (1998). Prenatal development of reelin-immunoreactive neurons in the human neocortex. J Comp Neurol, 397:29-40.
    • (1998) J Comp Neurol , vol.397 , pp. 29-40
    • Meyer, G.1    Goffinet, A.M.2
  • 67
    • 0029008666 scopus 로고
    • The reeler gene-associated antigen on Cajal-Retzius neurons is a crucial molecule for laminar organization of cortical neurons
    • Ogawa M, Miyata T, Nakajima K, Yagyu K, Seike M, Ikenaka K, Yamamoto H, Mikoshiba K (1995). The reeler gene-associated antigen on Cajal-Retzius neurons is a crucial molecule for laminar organization of cortical neurons. Neuron, 14:899-912.
    • (1995) Neuron , vol.14 , pp. 899-912
    • Ogawa, M.1    Miyata, T.2    Nakajima, K.3    Yagyu, K.4    Seike, M.5    Ikenaka, K.6    Yamamoto, H.7    Mikoshiba, K.8
  • 69
    • 0029124017 scopus 로고
    • Calretinin-positive Cajal-Retzius cells persist in the adult human neocortex
    • Belichenko PV, Vogt Weisenhorn DM, Myklossy J, Celio MR (1995). Calretinin-positive Cajal-Retzius cells persist in the adult human neocortex. Neuroreport, 6:1869-74.
    • (1995) Neuroreport , vol.6 , pp. 1869-1874
    • Belichenko, P.V.1    Vogt Weisenhorn, D.M.2    Myklossy, J.3    Celio, M.R.4
  • 70
    • 0032951895 scopus 로고    scopus 로고
    • Persistence of Cajal-Retzius cells in the adult human cerebral cortex. An immunohistochemical study
    • Martin R, Gutierrez A, Penafiel A, Marin-Padilla M, de la Calle A (1999). Persistence of Cajal-Retzius cells in the adult human cerebral cortex. An immunohistochemical study. Histol Histopathol, 14:487-90.
    • (1999) Histol Histopathol , vol.14 , pp. 487-490
    • Martin, R.1    Gutierrez, A.2    Penafiel, A.3    Marin-Padilla, M.4    de la Calle, A.5
  • 71
    • 0030707501 scopus 로고    scopus 로고
    • Distribution of parvalbumin-, calretinin-, and calbindin-D28k-immunoreactive neurons and fibers in the human entorhinal cortex
    • Mikkonen M, Soininen H, Pitkanen A (1997). Distribution of parvalbumin-, calretinin-, and calbindin-D28k-immunoreactive neurons and fibers in the human entorhinal cortex. J Comp Neurol, 388:64-88.
    • (1997) J Comp Neurol , vol.388 , pp. 64-88
    • Mikkonen, M.1    Soininen, H.2    Pitkanen, A.3
  • 73
    • 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
  • 74
    • 0037491843 scopus 로고    scopus 로고
    • Reelin-immunoreactive neurons, axons, and neuropil in the adult ferret brain: evidence for axonal secretion of reelin in long axonal pathways
    • Martinez-Cerdeno V, Galazo MJ, Clasca F (2003). Reelin-immunoreactive neurons, axons, and neuropil in the adult ferret brain: evidence for axonal secretion of reelin in long axonal pathways. J Comp Neurol, 463:92-116.
    • (2003) J Comp Neurol , vol.463 , pp. 92-116
    • Martinez-Cerdeno, V.1    Galazo, M.J.2    Clasca, F.3
  • 75
    • 0036891891 scopus 로고    scopus 로고
    • Reelin immunoreactivity in the adult primate brain: intracellular localization in projecting and local circuit neurons of the cerebral cortex, hippocampus and subcortical regions
    • Martinez-Cerdeno V, Galazo MJ, Cavada C, Clasca F (2002). Reelin immunoreactivity in the adult primate brain: intracellular localization in projecting and local circuit neurons of the cerebral cortex, hippocampus and subcortical regions. Cereb Cortex, 12:1298-311.
    • (2002) Cereb Cortex , vol.12 , pp. 1298-1311
    • Martinez-Cerdeno, V.1    Galazo, M.J.2    Cavada, C.3    Clasca, F.4
  • 81
    • 27644547658 scopus 로고    scopus 로고
    • Neuropsychology in Alzheimer's disease and other dementia research
    • Savla GN, Palmer BW (2005). Neuropsychology in Alzheimer's disease and other dementia research. Curr Opin Psychiatry, 18:621-7.
    • (2005) Curr Opin Psychiatry , vol.18 , pp. 621-627
    • Savla, G.N.1    Palmer, B.W.2
  • 83
    • 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, 120:885-90.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 85
    • 0026735070 scopus 로고
    • Targeting of cell-surface beta-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments
    • Haass C, Koo EH, Mellon A, Hung AY, Selkoe DJ (1992). Targeting of cell-surface beta-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature, 357:500-3.
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 86
    • 0029841562 scopus 로고    scopus 로고
    • Increased activity-regulating and neuroprotective efficacy of alpha-secretase-derived secreted amyloid precursor protein conferred by a C-terminal heparin-binding domain
    • Furukawa K, Sopher BL, Rydel RE, Begley JG, Pham DG, Martin GM, Fox M, Mattson MP (1996). Increased activity-regulating and neuroprotective efficacy of alpha-secretase-derived secreted amyloid precursor protein conferred by a C-terminal heparin-binding domain. J Neurochem, 67:1882-96.
    • (1996) J Neurochem , vol.67 , pp. 1882-1896
    • Furukawa, K.1    Sopher, B.L.2    Rydel, R.E.3    Begley, J.G.4    Pham, D.G.5    Martin, G.M.6    Fox, M.7    Mattson, M.P.8
  • 87
    • 0035909901 scopus 로고    scopus 로고
    • The gamma -secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus
    • Gao Y, Pimplikar SW (2001). The gamma -secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus. Proc Natl Acad Sci U S A, 98:14979-84.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14979-14984
    • Gao, Y.1    Pimplikar, S.W.2
  • 88
    • 5444275067 scopus 로고    scopus 로고
    • The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor
    • von Rotz RC, Kohli BM, Bosset J, Meier M, Suzuki T, Nitsch RM, Konietzko U (2004). The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor. J Cell Sci, 117:4435-48.
    • (2004) J Cell Sci , vol.117 , pp. 4435-4448
    • von Rotz, R.C.1    Kohli, B.M.2    Bosset, J.3    Meier, M.4    Suzuki, T.5    Nitsch, R.M.6    Konietzko, U.7
  • 89
    • 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, 457:981-9.
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'Leary, D.D.3    Tessier-Lavigne, M.4
  • 92
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe DJ (2002). Alzheimer's disease is a synaptic failure. Science, 298:789-91.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 93
    • 33845411954 scopus 로고    scopus 로고
    • AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss
    • Hsieh H, Boehm J, Sato C, Iwatsubo T, Tomita T, Sisodia S, Malinow R (2006). AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss. Neuron, 52:831-43.
    • (2006) Neuron , vol.52 , pp. 831-843
    • Hsieh, H.1    Boehm, J.2    Sato, C.3    Iwatsubo, T.4    Tomita, T.5    Sisodia, S.6    Malinow, R.7
  • 96
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • Shankar GM, Bloodgood BL, Townsend M, Walsh DM, Selkoe DJ, Sabatini BL (2007). Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J Neurosci, 27:2866-75.
    • (2007) J Neurosci , vol.27 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 98
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers of amyloid beta-protein on hippocampal synaptic plasticity: a potent role for trimers
    • Townsend M, Shankar GM, Mehta T, Walsh DM, Selkoe DJ (2006). Effects of secreted oligomers of amyloid beta-protein on hippocampal synaptic plasticity: a potent role for trimers. J Physiol, 572:477-92.
    • (2006) J Physiol , vol.572 , pp. 477-492
    • Townsend, M.1    Shankar, G.M.2    Mehta, T.3    Walsh, D.M.4    Selkoe, D.J.5
  • 99
    • 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, 416:535-9.
    • (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
  • 103
  • 104
    • 64049110805 scopus 로고    scopus 로고
    • The N-terminal fragment of Reelin is generated after endocytosis and released through the pathway regulated by Rab11
    • Hibi T, Hattori M (2009). The N-terminal fragment of Reelin is generated after endocytosis and released through the pathway regulated by Rab11. FEBS Lett, 583:1299-303.
    • (2009) FEBS Lett , vol.583 , pp. 1299-1303
    • Hibi, T.1    Hattori, M.2
  • 105
    • 77950363927 scopus 로고    scopus 로고
    • Co-localization of Reelin and proteolytic AbetaPP fragments in hippocampal plaques in aged wild-type mice
    • Doehner J, Madhusudan A, Konietzko U, Fritschy JM, Knuesel I (2010). Co-localization of Reelin and proteolytic AbetaPP fragments in hippocampal plaques in aged wild-type mice. J Alzheimers Dis, 19:1339-57.
    • (2010) J Alzheimers Dis , vol.19 , pp. 1339-1357
    • Doehner, J.1    Madhusudan, A.2    Konietzko, U.3    Fritschy, J.M.4    Knuesel, I.5
  • 108
    • 70349213977 scopus 로고    scopus 로고
    • Accumulation of reelin-positive plaques is accompanied by a decline in basal forebrain projection neurons during normal aging
    • Madhusudan A, Sidler C, Knuesel I (2009). Accumulation of reelin-positive plaques is accompanied by a decline in basal forebrain projection neurons during normal aging. Eur J Neurosci, 30:1064-76.
    • (2009) Eur J Neurosci , vol.30 , pp. 1064-1076
    • Madhusudan, A.1    Sidler, C.2    Knuesel, I.3
  • 109
    • 0141522452 scopus 로고    scopus 로고
    • Acetylcholine modulation of neural systems involved in learning and memory
    • Gold PE (2003). Acetylcholine modulation of neural systems involved in learning and memory. Neurobiol Learn Mem, 80:194-210.
    • (2003) Neurobiol Learn Mem , vol.80 , pp. 194-210
    • Gold, P.E.1
  • 110
    • 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, 28:1297-306.
    • (2007) Neurobiol Aging , vol.28 , pp. 1297-1306
    • Knobloch, M.1    Konietzko, U.2    Krebs, D.C.3    Nitsch, R.M.4
  • 113
    • 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, 201:61-9.
    • (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
  • 114
    • 70349807619 scopus 로고    scopus 로고
    • Immune activation in brain aging and neurodegeneration: too much or too little?
    • Lucin KM, Wyss-Coray T (2009). Immune activation in brain aging and neurodegeneration: too much or too little? Neuron, 64:110-22.
    • (2009) Neuron , vol.64 , pp. 110-122
    • Lucin, K.M.1    Wyss-Coray, T.2
  • 116
    • 33644541112 scopus 로고    scopus 로고
    • Neuroinflammation and regeneration in the early stages of Alzheimer's disease pathology
    • Hoozemans JJ, Veerhuis R, Rozemuller JM, Eikelenboom P (2006). Neuroinflammation and regeneration in the early stages of Alzheimer's disease pathology. Int J Dev Neurosci, 24:157-65.
    • (2006) Int J Dev Neurosci , vol.24 , pp. 157-165
    • Hoozemans, J.J.1    Veerhuis, R.2    Rozemuller, J.M.3    Eikelenboom, P.4
  • 117
    • 61349088546 scopus 로고    scopus 로고
    • Inflammation in Alzheimer's disease: amyloid-beta oligomers trigger innate immunity defence via pattern recognition receptors
    • Salminen A, Ojala J, Kauppinen A, Kaarniranta K, Suuronen T (2009). Inflammation in Alzheimer's disease: amyloid-beta oligomers trigger innate immunity defence via pattern recognition receptors. Prog Neurobiol, 87:181-94.
    • (2009) Prog Neurobiol , vol.87 , pp. 181-194
    • Salminen, A.1    Ojala, J.2    Kauppinen, A.3    Kaarniranta, K.4    Suuronen, T.5
  • 118
    • 0036949091 scopus 로고    scopus 로고
    • Local neuroinflammation and the progression of Alzheimer's disease
    • McGeer PL, McGeer EG (2002). Local neuroinflammation and the progression of Alzheimer's disease. J Neurovirol, 8:529-38.
    • (2002) J Neurovirol , vol.8 , pp. 529-538
    • McGeer, P.L.1    McGeer, E.G.2
  • 119
    • 33748471099 scopus 로고    scopus 로고
    • Inflammation in Alzheimer disease: driving force, bystander or beneficial response?
    • Wyss-Coray T (2006). Inflammation in Alzheimer disease: driving force, bystander or beneficial response? Nat Med, 12:1005-1015.
    • (2006) Nat Med , vol.12 , pp. 1005-1015
    • Wyss-Coray, T.1
  • 121
    • 70349838218 scopus 로고    scopus 로고
    • Cytokines and CNS development
    • Deverman BE, Patterson PH (2009). Cytokines and CNS development. Neuron, 64:61-78.
    • (2009) Neuron , vol.64 , pp. 61-78
    • Deverman, B.E.1    Patterson, P.H.2
  • 122
    • 67749114055 scopus 로고    scopus 로고
    • Immune involvement in schizophrenia and autism: etiology, pathology and animal models
    • Patterson PH (2009). Immune involvement in schizophrenia and autism: etiology, pathology and animal models. Behav Brain Res, 204:313-21.
    • (2009) Behav Brain Res , vol.204 , pp. 313-321
    • Patterson, P.H.1
  • 123
    • 34447133469 scopus 로고    scopus 로고
    • Prenatal infectious and nutritional factors and risk of adult schizophrenia
    • Penner JD, Brown AS (2007). Prenatal infectious and nutritional factors and risk of adult schizophrenia. Expert Rev Neurother, 7:797-805.
    • (2007) Expert Rev Neurother , vol.7 , pp. 797-805
    • Penner, J.D.1    Brown, A.S.2
  • 124
    • 23244437953 scopus 로고    scopus 로고
    • Towards an immuno-precipitated neurodevelopmental animal model of schizophrenia
    • Meyer U, Feldon J, Schedlowski M, Yee BK (2005). Towards an immuno-precipitated neurodevelopmental animal model of schizophrenia. Neurosci Biobehav Rev, 29:913-47.
    • (2005) Neurosci Biobehav Rev , vol.29 , pp. 913-947
    • Meyer, U.1    Feldon, J.2    Schedlowski, M.3    Yee, B.K.4
  • 125
    • 0037218688 scopus 로고    scopus 로고
    • Maternal influenza infection causes marked behavioral and pharmacological changes in the offspring
    • Shi L, Fatemi SH, Sidwell RW, Patterson PH (2003). Maternal influenza infection causes marked behavioral and pharmacological changes in the offspring. J Neurosci, 23:297-302.
    • (2003) J Neurosci , vol.23 , pp. 297-302
    • Shi, L.1    Fatemi, S.H.2    Sidwell, R.W.3    Patterson, P.H.4
  • 126
    • 0642369566 scopus 로고    scopus 로고
    • Immune activation during pregnancy in rats leads to a postpubertal emergence of disrupted latent inhibition, dopaminergic hyperfunction, and altered limbic morphology in the offspring: a novel neurodevelopmental model of schizophrenia
    • Zuckerman L, Rehavi M, Nachman R, Weiner I (2003). Immune activation during pregnancy in rats leads to a postpubertal emergence of disrupted latent inhibition, dopaminergic hyperfunction, and altered limbic morphology in the offspring: a novel neurodevelopmental model of schizophrenia. Neuropsychopharmacology, 28:1778-89.
    • (2003) Neuropsychopharmacology , vol.28 , pp. 1778-1789
    • Zuckerman, L.1    Rehavi, M.2    Nachman, R.3    Weiner, I.4
  • 127
    • 33646926705 scopus 로고    scopus 로고
    • The time of prenatal immune challenge determines the specificity of inflammation-mediated brain and behavioral pathology
    • Meyer U, Nyffeler M, Engler A, Urwyler A, Schedlowski M, Knuesel I, Yee BK, Feldon J (2006). The time of prenatal immune challenge determines the specificity of inflammation-mediated brain and behavioral pathology. J Neurosci, 26:4752-62.
    • (2006) J Neurosci , vol.26 , pp. 4752-4762
    • Meyer, U.1    Nyffeler, M.2    Engler, A.3    Urwyler, A.4    Schedlowski, M.5    Knuesel, I.6    Yee, B.K.7    Feldon, J.8
  • 128
    • 36949028725 scopus 로고    scopus 로고
    • Relative prenatal and postnatal maternal contributions to schizophrenia-related neurochemical dysfunction after in utero immune challenge
    • Meyer U, Nyffeler M, Schwendener S, Knuesel I, Yee BK, Feldon J (2008). Relative prenatal and postnatal maternal contributions to schizophrenia-related neurochemical dysfunction after in utero immune challenge. Neuropsychopharmacology, 33:441-56.
    • (2008) Neuropsychopharmacology , vol.33 , pp. 441-456
    • Meyer, U.1    Nyffeler, M.2    Schwendener, S.3    Knuesel, I.4    Yee, B.K.5    Feldon, J.6
  • 129
    • 41349105699 scopus 로고    scopus 로고
    • Adult brain and behavioral pathological markers of prenatal immune challenge during early/middle and late fetal development in mice
    • Meyer U, Nyffeler M, Yee BK, Knuesel I, Feldon J (2008). Adult brain and behavioral pathological markers of prenatal immune challenge during early/middle and late fetal development in mice. Brain Behav Immun, 22:469-86.
    • (2008) Brain Behav Immun , vol.22 , pp. 469-486
    • Meyer, U.1    Nyffeler, M.2    Yee, B.K.3    Knuesel, I.4    Feldon, J.5
  • 130
    • 33750512968 scopus 로고    scopus 로고
    • Maternal immune activation during pregnancy increases limbic GABAA receptor immunoreactivity in the adult offspring: implications for schizophrenia
    • Nyffeler M, Meyer U, Yee BK, Feldon J, Knuesel I (2006). Maternal immune activation during pregnancy increases limbic GABAA receptor immunoreactivity in the adult offspring: implications for schizophrenia. Neuroscience, 143:51-62.
    • (2006) Neuroscience , vol.143 , pp. 51-62
    • Nyffeler, M.1    Meyer, U.2    Yee, B.K.3    Feldon, J.4    Knuesel, I.5
  • 131
    • 58149379046 scopus 로고    scopus 로고
    • Crk and Crk-like play essential overlapping roles downstream of disabled-1 in the Reelin pathway
    • Park TJ, Curran T (2008). Crk and Crk-like play essential overlapping roles downstream of disabled-1 in the Reelin pathway. J Neurosci, 28:13551-62.
    • (2008) J Neurosci , vol.28 , pp. 13551-13562
    • Park, T.J.1    Curran, T.2
  • 132
    • 9444237381 scopus 로고    scopus 로고
    • Regulation of actin cytoskeleton by mDab1 through N-WASP and ubiquitination of mDab1.
    • Mikoshiba K, Yamamoto T, Takenawa T.
    • Suetsugu S, Tezuka T, Morimura T, Hattori M (2004), Mikoshiba K, Yamamoto T, Takenawa T. Regulation of actin cytoskeleton by mDab1 through N-WASP and ubiquitination of mDab1. Biochem J, 384:1-8.
    • (2004) Biochem J , vol.384 , pp. 1-8
    • Suetsugu, S.1    Tezuka, T.2    Morimura, T.3    Hattori, M.4
  • 133
    • 33947168671 scopus 로고    scopus 로고
    • Reelin signaling facilitates maturation of CA1 glutamatergic synapses
    • Qiu S, Weeber EJ (2007). Reelin signaling facilitates maturation of CA1 glutamatergic synapses. J Neurophysiol, 97:2312-21.
    • (2007) J Neurophysiol , vol.97 , pp. 2312-2321
    • Qiu, S.1    Weeber, E.J.2


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