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Volumn 126, Issue 2, 2013, Pages 155-164

Actin filaments and microtubules in dendritic spines

Author keywords

actin; dendritic spine; microtubules; synaptic plasticity

Indexed keywords

ACTIN; ACTIN DEPOLYMERIZING FACTOR; ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 2-3 COMPLEX; AMYLOID BETA PROTEIN; APOLIPOPROTEIN E; BASIC HELIX LOOP HELIX TRANSCRIPTION FACTOR; BRAIN DERIVED NEUROTROPHIC FACTOR; COFILIN; CYTOSKELETON PROTEIN; DREBRIN; FRAGILE X MENTAL RETARDATION PROTEIN; GUANOSINE TRIPHOSPHATASE; IQ MOTIF CONTAINING GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN 1; LIM KINASE 1; MEMBRANE RECEPTOR; MICROTUBULE ASSOCIATED PROTEIN 1; MICROTUBULE ASSOCIATED PROTEIN 2; MYOSIN II; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; NEUREXIN; NEUROLIGIN; OLIGOPHRENIN 1; P21 ACTIVATED KINASE 1; P21 ACTIVATED KINASE 3; RAC1 PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84879978794     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.12313     Document Type: Review
Times cited : (89)

References (106)
  • 2
    • 14644401845 scopus 로고    scopus 로고
    • Drebrin A is a postsynaptic protein that localizes in vivo to the submembranous surface of dendritic sites forming excitatory synapses
    • Aoki C., Sekino Y., Hanamura K., Fujisawa S., Mahadomrongkul V., Ren Y., and, Shirao T., (2005) Drebrin A is a postsynaptic protein that localizes in vivo to the submembranous surface of dendritic sites forming excitatory synapses. J. Comp. Neurol. 483, 383-402.
    • (2005) J. Comp. Neurol. , vol.483 , pp. 383-402
    • Aoki, C.1    Sekino, Y.2    Hanamura, K.3    Fujisawa, S.4    Mahadomrongkul, V.5    Ren, Y.6    Shirao, T.7
  • 4
    • 0033198879 scopus 로고    scopus 로고
    • Putting a new twist on actin: ADF/cofilins modulate actin dynamics
    • Bamburg J. R., McGough A., and, Ono S., (1999) Putting a new twist on actin: ADF/cofilins modulate actin dynamics. Trends Cell Biol. 9, 364-370.
    • (1999) Trends Cell Biol. , vol.9 , pp. 364-370
    • Bamburg, J.R.1    McGough, A.2    Ono, S.3
  • 5
    • 0033134860 scopus 로고    scopus 로고
    • Bridging cognition, the brain and molecular genetics: Evidence from Williams syndrome
    • Bellugi U., Lichtenberger L., Mills D., Galaburda A., and, Korenberg J. R., (1999) Bridging cognition, the brain and molecular genetics: evidence from Williams syndrome. Trends Neurosci. 22, 197-207.
    • (1999) Trends Neurosci. , vol.22 , pp. 197-207
    • Bellugi, U.1    Lichtenberger, L.2    Mills, D.3    Galaburda, A.4    Korenberg, J.R.5
  • 6
    • 0032580161 scopus 로고    scopus 로고
    • Oligophrenin-1 encodes a rhoGAP protein involved in X-linked mental retardation
    • Billuart P., Bienvenu T., Ronce N., et al,. (1998) Oligophrenin-1 encodes a rhoGAP protein involved in X-linked mental retardation. Nature 392, 923-926.
    • (1998) Nature , vol.392 , pp. 923-926
    • Billuart, P.1    Bienvenu, T.2    Ronce, N.3
  • 7
    • 0028010005 scopus 로고
    • Microtubule-associated protein 1b (MAP1b) is concentrated in the distal region of growing axons
    • Black M. M., Slaughter T., and, Fischer I., (1994) Microtubule-associated protein 1b (MAP1b) is concentrated in the distal region of growing axons. J. Neurosci. 14, 857-870.
    • (1994) J. Neurosci. , vol.14 , pp. 857-870
    • Black, M.M.1    Slaughter, T.2    Fischer, I.3
  • 8
    • 4444223956 scopus 로고    scopus 로고
    • Docosahexaenoic acid protects from dendritic pathology in an Alzheimer's disease mouse model
    • Calon F., Lim G. P., Yang F., et al,. (2004) Docosahexaenoic acid protects from dendritic pathology in an Alzheimer's disease mouse model. Neuron 43, 633-645.
    • (2004) Neuron , vol.43 , pp. 633-645
    • Calon, F.1    Lim, G.P.2    Yang, F.3
  • 9
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • Carlier M. F., Laurent V., Santolini J., Melki R., Didry D., Xia G. X., Hong Y., Chua N. H., and, Pantaloni D., (1997) Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136, 1307-1322.
    • (1997) J. Cell Biol. , vol.136 , pp. 1307-1322
    • Carlier, M.F.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.X.6    Hong, Y.7    Chua, N.H.8    Pantaloni, D.9
  • 10
    • 3543136466 scopus 로고    scopus 로고
    • Disorder-associated mutations lead to functional inactivation of neuroligins
    • Chih B., Afridi S. K., Clark L., and, Scheiffele P., (2004) Disorder-associated mutations lead to functional inactivation of neuroligins. Hum. Mol. Genet. 13, 1471-1477.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1471-1477
    • Chih, B.1    Afridi, S.K.2    Clark, L.3    Scheiffele, P.4
  • 11
    • 65249107203 scopus 로고    scopus 로고
    • Microtubule assembly, organization and dynamics in axons and dendrites
    • Conde C., and, Cáceres A., (2009) Microtubule assembly, organization and dynamics in axons and dendrites. Nat. Rev. Neurosci. 10, 319-332.
    • (2009) Nat. Rev. Neurosci. , vol.10 , pp. 319-332
    • Conde, C.1    Cáceres, A.2
  • 12
    • 33746752209 scopus 로고    scopus 로고
    • Differential expression of synaptic proteins in the frontal and temporal cortex of elderly subjects with mild cognitive impairment"
    • Counts S. E., Nadeem M., Lad S. P., Wuu J., and, Mufson E. J., (2006) Differential expression of synaptic proteins in the frontal and temporal cortex of elderly subjects with mild cognitive impairment". J. Neuropathol. Exp. Neurol. 65, 592-601.
    • (2006) J. Neuropathol. Exp. Neurol. , vol.65 , pp. 592-601
    • Counts, S.E.1    Nadeem, M.2    Lad, S.P.3    Wuu, J.4    Mufson, E.J.5
  • 13
    • 79952067607 scopus 로고    scopus 로고
    • The dynamic cytoskeleton: Backbone of dendritic spine plasticity
    • Dent E. W., Merriam E. B., and, Hu X., (2011) The dynamic cytoskeleton: backbone of dendritic spine plasticity. Curr. Opin. Neurobiol. 21, 175-181.
    • (2011) Curr. Opin. Neurobiol. , vol.21 , pp. 175-181
    • Dent, E.W.1    Merriam, E.B.2    Hu, X.3
  • 14
    • 33845889998 scopus 로고    scopus 로고
    • Mutations in the gene encoding the synaptic scaffolding protein SHANK3 are associated with autism spectrum disorders
    • Durand C. M., Betancur C., Boeckers T. M., et al,. (2007) Mutations in the gene encoding the synaptic scaffolding protein SHANK3 are associated with autism spectrum disorders. Nat. Genet. 39, 25-27.
    • (2007) Nat. Genet. , vol.39 , pp. 25-27
    • Durand, C.M.1    Betancur, C.2    Boeckers, T.M.3
  • 15
    • 0043194092 scopus 로고    scopus 로고
    • Timing of neuronal and glial ultrastructure disruption during brain slice preparation and recovery in vitro
    • Fiala J. C., Kirov S. A., Feinberg M. D., Petrak L. J., George P., Goddard C. A., and, Harris K. M., (2003) Timing of neuronal and glial ultrastructure disruption during brain slice preparation and recovery in vitro. J. Comp. Neurol. 465, 90-103.
    • (2003) J. Comp. Neurol. , vol.465 , pp. 90-103
    • Fiala, J.C.1    Kirov, S.A.2    Feinberg, M.D.3    Petrak, L.J.4    George, P.5    Goddard, C.A.6    Harris, K.M.7
  • 16
    • 0033666317 scopus 로고    scopus 로고
    • Assembly of new individual excitatory synapses: Time course and temporal order of synaptic molecule recruitment
    • Friedman H. V., Bresler T., Garner C. C., and, Ziv N. E., (2000) Assembly of new individual excitatory synapses: time course and temporal order of synaptic molecule recruitment. Neuron 27, 57-69.
    • (2000) Neuron , vol.27 , pp. 57-69
    • Friedman, H.V.1    Bresler, T.2    Garner, C.C.3    Ziv, N.E.4
  • 19
    • 53349165549 scopus 로고    scopus 로고
    • Targeting of the F-actin-binding protein drebrin by the microtubule plus-tip protein EB3 is required for neuritogenesis
    • Geraldo S., Khanzada U. K., Parsons M., Chilton J. K., and, Gordon-Weeks P. R., (2008) Targeting of the F-actin-binding protein drebrin by the microtubule plus-tip protein EB3 is required for neuritogenesis. Nat. Cell Biol. 10, 1181-1189.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1181-1189
    • Geraldo, S.1    Khanzada, U.K.2    Parsons, M.3    Chilton, J.K.4    Gordon-Weeks, P.R.5
  • 20
    • 0033809584 scopus 로고    scopus 로고
    • Molecular genetic approaches to microtubule-associated protein function
    • González-Billault C., and, Avila J., (2000) Molecular genetic approaches to microtubule-associated protein function. Histol. Histopathol. 15, 1177-1183.
    • (2000) Histol. Histopathol. , vol.15 , pp. 1177-1183
    • González-Billault, C.1    Avila, J.2
  • 21
  • 23
    • 0020463993 scopus 로고
    • Synaptic organisation and neuron microtubule distribution
    • Gray E. G., Westrum L. E., Burgoyne R. D., and, Barron J., (1982) Synaptic organisation and neuron microtubule distribution. Cell Tissue Res. 226, 579-588.
    • (1982) Cell Tissue Res. , vol.226 , pp. 579-588
    • Gray, E.G.1    Westrum, L.E.2    Burgoyne, R.D.3    Barron, J.4
  • 25
    • 58149225472 scopus 로고    scopus 로고
    • Microtubules in dendritic spine development
    • Gu J., Firestein B. L., and, Zheng J. Q., (2008) Microtubules in dendritic spine development. J. Neurosci. 28, 12120-12124.
    • (2008) J. Neurosci. , vol.28 , pp. 12120-12124
    • Gu, J.1    Firestein, B.L.2    Zheng, J.Q.3
  • 26
    • 0030025216 scopus 로고    scopus 로고
    • Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease
    • Harigaya Y., Shoji M., Shirao T., and, Hirai S., (1996) Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease. J. Neurosci. Res. 43 (1), 87-92.
    • (1996) J. Neurosci. Res. , vol.43 , Issue.1 , pp. 87-92
    • Harigaya, Y.1    Shoji, M.2    Shirao, T.3    Hirai, S.4
  • 27
    • 0033033642 scopus 로고    scopus 로고
    • Loss of proteins regulating synaptic plasticity in normal aging of the human brain and in Alzheimer disease
    • Hatanpaa K., Isaacs K. R., Shirao T., Brady D. R., and, Rapoport S. I., (1999) Loss of proteins regulating synaptic plasticity in normal aging of the human brain and in Alzheimer disease. J. Neuropathol. Exp. Neurol. 58, 637-643.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 637-643
    • Hatanpaa, K.1    Isaacs, K.R.2    Shirao, T.3    Brady, D.R.4    Rapoport, S.I.5
  • 29
    • 84871648576 scopus 로고    scopus 로고
    • The light chain 1 subunit of the microtubule-associated protein 1B (MAP1B) is responsible for Tiam1 binding and Rac1 activation in neuronal cells
    • Henríquez D. R., Bodaleo F. J., Montenegro-Venegas C., and, González-Billault C., (2012) The light chain 1 subunit of the microtubule-associated protein 1B (MAP1B) is responsible for Tiam1 binding and Rac1 activation in neuronal cells. PLoS ONE 7, e53123.
    • (2012) PLoS ONE , vol.7
    • Henríquez, D.R.1    Bodaleo, F.J.2    Montenegro-Venegas, C.3    González-Billault, C.4
  • 30
    • 33745780575 scopus 로고    scopus 로고
    • Phosphorylation of actin-depolymerizing factor/cofilin by LIM-kinase mediates amyloid beta-induced degeneration: A potential mechanism of neuronal dystrophy in Alzheimer's disease
    • Heredia L., Helguera P., de Olmos S., et al,. (2006) Phosphorylation of actin-depolymerizing factor/cofilin by LIM-kinase mediates amyloid beta-induced degeneration: a potential mechanism of neuronal dystrophy in Alzheimer's disease. J. Neurosci. 26 (24), 6533-6542.
    • (2006) J. Neurosci. , vol.26 , Issue.24 , pp. 6533-6542
    • Heredia, L.1    Helguera, P.2    De Olmos, S.3
  • 31
    • 40249097516 scopus 로고    scopus 로고
    • The subspine organization of actin fibers regulates the structure and plasticity of dendritic spines
    • Honkura N., Matsuzaki M., Noguchi J., Ellis-Davies G. C., and, Kasai H., (2008) The subspine organization of actin fibers regulates the structure and plasticity of dendritic spines. Neuron 57, 719-729.
    • (2008) Neuron , vol.57 , pp. 719-729
    • Honkura, N.1    Matsuzaki, M.2    Noguchi, J.3    Ellis-Davies, G.C.4    Kasai, H.5
  • 32
    • 65349085563 scopus 로고    scopus 로고
    • Defining mechanisms of actin polymerization and depolymerization during dendritic spine morphogenesis
    • Hotulainen P., Llano O., Smirnov S., Tanhuanpää K., Faix J., Rivera C., and, Lappalainen P., (2009) Defining mechanisms of actin polymerization and depolymerization during dendritic spine morphogenesis. J. Cell Biol. 185, 323-339.
    • (2009) J. Cell Biol. , vol.185 , pp. 323-339
    • Hotulainen, P.1    Llano, O.2    Smirnov, S.3    Tanhuanpää, K.4    Faix, J.5    Rivera, C.6    Lappalainen, P.7
  • 33
    • 58149272090 scopus 로고    scopus 로고
    • Activity-dependent dynamic microtubule invasion of dendritic spines
    • Hu X., Viesselmann C., Nam S., Merriam E., and, Dent E. W., (2008) Activity-dependent dynamic microtubule invasion of dendritic spines. J. Neurosci. 28, 13094-13105.
    • (2008) J. Neurosci. , vol.28 , pp. 13094-13105
    • Hu, X.1    Viesselmann, C.2    Nam, S.3    Merriam, E.4    Dent, E.W.5
  • 35
    • 85012414651 scopus 로고
    • Electron microscopic studies on structure of natural and synthetic protein filaments from striated muscle
    • Huxley H. E., (1963) Electron microscopic studies on structure of natural and synthetic protein filaments from striated muscle. J. Mol. Biol. 7, 281-308.
    • (1963) J. Mol. Biol. , vol.7 , pp. 281-308
    • Huxley, H.E.1
  • 36
    • 0033797832 scopus 로고    scopus 로고
    • Dendritic spine structural anomalies in fragile-X mental retardation syndrome
    • Irwin S. A., Galvez R., and, Greenough W. T., (2000) Dendritic spine structural anomalies in fragile-X mental retardation syndrome. Cereb. Cortex 10, 1038-1044.
    • (2000) Cereb. Cortex , vol.10 , pp. 1038-1044
    • Irwin, S.A.1    Galvez, R.2    Greenough, W.T.3
  • 37
    • 0014608608 scopus 로고
    • Formation of arrowhead complexes with heavy meromyosin in a variety of cell types
    • Ishikawa H., Bischoff R., and, Holtzer H., (1969) Formation of arrowhead complexes with heavy meromyosin in a variety of cell types. J. Cell Biol. 43, 312-328.
    • (1969) J. Cell Biol. , vol.43 , pp. 312-328
    • Ishikawa, H.1    Bischoff, R.2    Holtzer, H.3
  • 38
    • 0028139040 scopus 로고
    • Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments
    • Ishikawa R., Hayashi K., Shirao T., Xue Y., Takagi T., Sasaki Y., and, Kohama K., (1994) Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments. J. Biol. Chem. 269, 29928-29933.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29928-29933
    • Ishikawa, R.1    Hayashi, K.2    Shirao, T.3    Xue, Y.4    Takagi, T.5    Sasaki, Y.6    Kohama, K.7
  • 39
    • 0037656313 scopus 로고    scopus 로고
    • Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are associated with autism
    • Jamain S., Quach H., Betancur C., et al,. (2003) Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are associated with autism. Nat. Genet. 34, 27-29.
    • (2003) Nat. Genet. , vol.34 , pp. 27-29
    • Jamain, S.1    Quach, H.2    Betancur, C.3
  • 40
    • 81855196008 scopus 로고    scopus 로고
    • Post-translational regulation of the microtubule cytoskeleton: Mechanisms and functions
    • Janke C., and, Bulinski J. C., (2011) Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions. Nat. Rev. Mol. Cell Biol. 12, 773-786.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 773-786
    • Janke, C.1    Bulinski, J.C.2
  • 41
    • 84869480370 scopus 로고    scopus 로고
    • IQGAP1: A microtubule-microfilament scaffolding protein with multiple roles in nerve cell development and synaptic plasticity
    • Jausoro I., Mestres I., Remedi M., Sanchez M., and, Cáceres A., (2012) IQGAP1: a microtubule-microfilament scaffolding protein with multiple roles in nerve cell development and synaptic plasticity. Histol. Histopathol. 27, 1385-1394.
    • (2012) Histol. Histopathol. , vol.27 , pp. 1385-1394
    • Jausoro, I.1    Mestres, I.2    Remedi, M.3    Sanchez, M.4    Cáceres, A.5
  • 43
    • 58149214025 scopus 로고    scopus 로고
    • Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity
    • Jaworski J., Kapitein L. C., Gouveia S. M., et al,. (2009) Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity. Neuron 61, 85-100.
    • (2009) Neuron , vol.61 , pp. 85-100
    • Jaworski, J.1    Kapitein, L.C.2    Gouveia, S.M.3
  • 44
    • 0242403213 scopus 로고    scopus 로고
    • Apolipoprotein e isoform-specific regulation of dendritic spine morphology in apolipoprotein e transgenic mice and Alzheimer's disease patients
    • Ji Y., Gong Y., Gan W., Beach T., Holtzman D. M., and, Wisniewski T., (2003) Apolipoprotein E isoform-specific regulation of dendritic spine morphology in apolipoprotein E transgenic mice and Alzheimer's disease patients. Neuroscience 122, 305-315.
    • (2003) Neuroscience , vol.122 , pp. 305-315
    • Ji, Y.1    Gong, Y.2    Gan, W.3    Beach, T.4    Holtzman, D.M.5    Wisniewski, T.6
  • 45
    • 0035912770 scopus 로고    scopus 로고
    • Cytoskeletal microdifferentiation: A mechanism for organizing morphological plasticity in dendrites
    • Kaech S., Parmar H., Roelandse M., Bornmann C., and, Matus A., (2001) Cytoskeletal microdifferentiation: a mechanism for organizing morphological plasticity in dendrites. Proc. Natl Acad. Sci. USA 98, 7086-7092.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7086-7092
    • Kaech, S.1    Parmar, H.2    Roelandse, M.3    Bornmann, C.4    Matus, A.5
  • 47
    • 0033797735 scopus 로고    scopus 로고
    • Dendritic anomalies in disorders associated with mental retardation
    • Kaufmann W. E., and, Moser H. W., (2000) Dendritic anomalies in disorders associated with mental retardation. Cereb. Cortex 10, 981-991.
    • (2000) Cereb. Cortex , vol.10 , pp. 981-991
    • Kaufmann, W.E.1    Moser, H.W.2
  • 48
    • 34247632141 scopus 로고    scopus 로고
    • Synaptic dysfunction and disruption of postsynaptic drebrin-actin complex: A study of neurological disorders accompanied by cognitive deficits
    • Kojima N., and, Shirao T., (2007) Synaptic dysfunction and disruption of postsynaptic drebrin-actin complex: a study of neurological disorders accompanied by cognitive deficits. Neurosci. Res. 58, 1-5.
    • (2007) Neurosci. Res. , vol.58 , pp. 1-5
    • Kojima, N.1    Shirao, T.2
  • 49
    • 0023637721 scopus 로고
    • Actin polymerization and ATP hydrolysis
    • Korn E. D., Carlier M. F., and, Pantaloni D., (1987) Actin polymerization and ATP hydrolysis. Science 238, 638-644.
    • (1987) Science , vol.238 , pp. 638-644
    • Korn, E.D.1    Carlier, M.F.2    Pantaloni, D.3
  • 50
    • 75649108232 scopus 로고    scopus 로고
    • Molecular architecture of synaptic actin cytoskeleton in hippocampal neurons reveals a mechanism of dendritic spine morphogenesis
    • Korobova F., and, Svitkina T., (2010) Molecular architecture of synaptic actin cytoskeleton in hippocampal neurons reveals a mechanism of dendritic spine morphogenesis. Mol. Biol. Cell 21, 165-176.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 165-176
    • Korobova, F.1    Svitkina, T.2
  • 52
    • 33846633336 scopus 로고    scopus 로고
    • Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease
    • Lacor P. N., Buniel M. C., Furlow P. W., Clemente A. S., Velasco P. T., Wood M., Viola K. L., and, Klein W. L., (2007) Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J. Neurosci. 27, 796-807.
    • (2007) J. Neurosci. , vol.27 , pp. 796-807
    • Lacor, P.N.1    Buniel, M.C.2    Furlow, P.W.3    Clemente, A.S.4    Velasco, P.T.5    Wood, M.6    Viola, K.L.7    Klein, W.L.8
  • 53
    • 0043095312 scopus 로고    scopus 로고
    • Dendritic spine loss in the hippocampus of young PDAPP and Tg2576 mice and its prevention by the ApoE2 genotype
    • Lanz T. A., Carter D. B., and, Merchant K. M., (2003) Dendritic spine loss in the hippocampus of young PDAPP and Tg2576 mice and its prevention by the ApoE2 genotype. Neurobiol. Dis. 13, 246-253.
    • (2003) Neurobiol. Dis. , vol.13 , pp. 246-253
    • Lanz, T.A.1    Carter, D.B.2    Merchant, K.M.3
  • 54
    • 84864605119 scopus 로고    scopus 로고
    • Presenilin conditional double knockout mice exhibit decreases in drebrin A at hippocampal CA1 synapses
    • Lee D., and, Aoki C., (2012) Presenilin conditional double knockout mice exhibit decreases in drebrin A at hippocampal CA1 synapses. Synapse 66, 870-879.
    • (2012) Synapse , vol.66 , pp. 870-879
    • Lee, D.1    Aoki, C.2
  • 55
    • 0036441201 scopus 로고    scopus 로고
    • Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity
    • Luo L., (2002) Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity. Annu. Rev. Cell Dev. Biol. 18, 601-635.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 601-635
    • Luo, L.1
  • 56
    • 28844442257 scopus 로고    scopus 로고
    • Stability of the distribution of spines containing drebrin A in the sensory cortex layer i of mice expressing mutated APP and PS1 genes
    • Mahadomrongkul V., Huerta P. T., Shirao T., and, Aoki C., (2005) Stability of the distribution of spines containing drebrin A in the sensory cortex layer I of mice expressing mutated APP and PS1 genes. Brain Res. 1064, 66-74.
    • (2005) Brain Res. , vol.1064 , pp. 66-74
    • Mahadomrongkul, V.1    Huerta, P.T.2    Shirao, T.3    Aoki, C.4
  • 58
    • 84858130236 scopus 로고    scopus 로고
    • Fibrillar amyloid-β1-42 modifies actin organization affecting the cofilin phosphorylation state: A role for Rac1/cdc42 effector proteins and the slingshot phosphatase
    • Mendoza-Naranjo A., Contreras-Vallejos E., Henriquez D. R., Otth C., Bamburg J. R., Maccioni R. B., and, González-Billault C., (2012) Fibrillar amyloid-β1-42 modifies actin organization affecting the cofilin phosphorylation state: a role for Rac1/cdc42 effector proteins and the slingshot phosphatase. J. Alzheimers Dis. 29, 63-77.
    • (2012) J. Alzheimers Dis. , vol.29 , pp. 63-77
    • Mendoza-Naranjo, A.1    Contreras-Vallejos, E.2    Henriquez, D.R.3    Otth, C.4    Bamburg, J.R.5    MacCioni, R.B.6    González-Billault, C.7
  • 59
    • 18444372636 scopus 로고    scopus 로고
    • Abnormal spine morphology and enhanced LTP in LIMK-1 knockout mice
    • Meng Y., Zhang Y., Tregoubov V., et al,. (2002) Abnormal spine morphology and enhanced LTP in LIMK-1 knockout mice. Neuron 35, 121-133.
    • (2002) Neuron , vol.35 , pp. 121-133
    • Meng, Y.1    Zhang, Y.2    Tregoubov, V.3
  • 61
    • 0034282106 scopus 로고    scopus 로고
    • Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function
    • Minamide L. S., Striegl A. M., Boyle J. A., Meberg P. J., and, Bamburg J. R., (2000) Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat. Cell Biol. 2, 628-636.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 628-636
    • Minamide, L.S.1    Striegl, A.M.2    Boyle, J.A.3    Meberg, P.J.4    Bamburg, J.R.5
  • 62
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison T., and, Kirschner M., (1984) Dynamic instability of microtubule growth. Nature 312, 237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 63
    • 23644462713 scopus 로고    scopus 로고
    • Overexpression of drebrin A in immature neurons induces the accumulation of F-actin and PSD-95 into dendritic filopodia, and the formation of large abnormal protrusions
    • Mizui T., Sekino Y., Takahashi H., Yamazaki H., and, Shirao T., (2005) Overexpression of drebrin A in immature neurons induces the accumulation of F-actin and PSD-95 into dendritic filopodia, and the formation of large abnormal protrusions. Mol. Cell. Neurosci. 30, 149-157.
    • (2005) Mol. Cell. Neurosci. , vol.30 , pp. 149-157
    • Mizui, T.1    Sekino, Y.2    Takahashi, H.3    Yamazaki, H.4    Shirao, T.5
  • 65
    • 79953748494 scopus 로고    scopus 로고
    • Local, persistent activation of Rho GTPases during plasticity of single dendritic spines
    • Murakoshi H., Wang H., and, Yasuda R., (2011) Local, persistent activation of Rho GTPases during plasticity of single dendritic spines. Nature 472, 100-104.
    • (2011) Nature , vol.472 , pp. 100-104
    • Murakoshi, H.1    Wang, H.2    Yasuda, R.3
  • 66
    • 79952322355 scopus 로고    scopus 로고
    • The filamins: Organizers of cell structure and function
    • Nakamura F., Stossel T. P., and, Hartwig J. H., (2011) The filamins: organizers of cell structure and function. Cell Adh. Migr. 5, 160-169.
    • (2011) Cell Adh. Migr. , vol.5 , pp. 160-169
    • Nakamura, F.1    Stossel, T.P.2    Hartwig, J.H.3
  • 67
    • 0034661746 scopus 로고    scopus 로고
    • Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons
    • Nakayama A. Y., Harms M. B., and, Luo L., (2000) Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons. J. Neurosci. 20, 5329-5338.
    • (2000) J. Neurosci. , vol.20 , pp. 5329-5338
    • Nakayama, A.Y.1    Harms, M.B.2    Luo, L.3
  • 68
    • 20544447033 scopus 로고    scopus 로고
    • Rho GTPases, dendritic structure, and mental retardation
    • Newey S. E., Velamoor V., Govek E. E., and, Van Aelst L., (2005) Rho GTPases, dendritic structure, and mental retardation. J. Neurobiol. 64, 58-74.
    • (2005) J. Neurobiol. , vol.64 , pp. 58-74
    • Newey, S.E.1    Velamoor, V.2    Govek, E.E.3    Van Aelst, L.4
  • 69
    • 7044267351 scopus 로고    scopus 로고
    • Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity
    • Okamoto K., Nagai T., Miyawaki A., and, Hayashi Y., (2004) Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity. Nat. Neurosci. 7, 1104-1112.
    • (2004) Nat. Neurosci. , vol.7 , pp. 1104-1112
    • Okamoto, K.1    Nagai, T.2    Miyawaki, A.3    Hayashi, Y.4
  • 70
    • 0347986677 scopus 로고    scopus 로고
    • Identification of a novel basic helix-loop-helix-PAS factor, NXF, reveals a Sim2 competitive, positive regulatory role in dendritic-cytoskeleton modulator drebrin gene expression
    • Ooe N., Saito K., Mikami N., Nakatuka I., and, Kaneko H., (2004) Identification of a novel basic helix-loop-helix-PAS factor, NXF, reveals a Sim2 competitive, positive regulatory role in dendritic-cytoskeleton modulator drebrin gene expression. Mol. Cell. Biol. 24, 608-616.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 608-616
    • Ooe, N.1    Saito, K.2    Mikami, N.3    Nakatuka, I.4    Kaneko, H.5
  • 71
    • 0036909561 scopus 로고    scopus 로고
    • Structure and function of the Arp2/3 complex
    • Pollard T. D., and, Beltzner C. C., (2002) Structure and function of the Arp2/3 complex. Curr. Opin. Struct. Biol. 12, 768-774.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 768-774
    • Pollard, T.D.1    Beltzner, C.C.2
  • 72
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard T. D., and, Borisy G. G., (2003) Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 73
    • 0019495845 scopus 로고
    • Direct measurement of actin polymerization rate constants by electron microscopy actin filaments nucleated by isolated microvillus cores
    • Pollard T. D., and, Mooseker M. S., (1981) Direct measurement of actin polymerization rate constants by electron microscopy actin filaments nucleated by isolated microvillus cores. J. Cell Biol. 88, 654-659.
    • (1981) J. Cell Biol. , vol.88 , pp. 654-659
    • Pollard, T.D.1    Mooseker, M.S.2
  • 74
    • 67650490390 scopus 로고    scopus 로고
    • Different Rho GTPase-dependent signaling pathways initiate sequential steps in the consolidation of long-term potentiation
    • Rex C. S., Chen L. Y., Sharma A., Liu J., Babayan A. H., Gall C. M., and, Lynch G., (2009) Different Rho GTPase-dependent signaling pathways initiate sequential steps in the consolidation of long-term potentiation. J. Cell Biol. 186, 85-97.
    • (2009) J. Cell Biol. , vol.186 , pp. 85-97
    • Rex, C.S.1    Chen, L.Y.2    Sharma, A.3    Liu, J.4    Babayan, A.H.5    Gall, C.M.6    Lynch, G.7
  • 75
    • 84864878892 scopus 로고    scopus 로고
    • Dendritic spines: From structure to in vivo function
    • Rochefort N. L., and, Konnerth A., (2012) Dendritic spines: from structure to in vivo function. EMBO Rep. 13, 699-708.
    • (2012) EMBO Rep. , vol.13 , pp. 699-708
    • Rochefort, N.L.1    Konnerth, A.2
  • 76
  • 77
    • 0030040876 scopus 로고    scopus 로고
    • Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones
    • Sasaki Y., Hayashi K., Shirao T., Ishikawa R., and, Kohama K., (1996) Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones. J. Neurochem. 66, 980-988.
    • (1996) J. Neurochem. , vol.66 , pp. 980-988
    • Sasaki, Y.1    Hayashi, K.2    Shirao, T.3    Ishikawa, R.4    Kohama, K.5
  • 78
    • 84860739976 scopus 로고    scopus 로고
    • SHANK1 deletions in males with autism spectrum disorder
    • Sato D., Lionel A. C., Leblond C. S., et al,. (2012) SHANK1 deletions in males with autism spectrum disorder. Am. J. Hum. Genet. 90, 879-887.
    • (2012) Am. J. Hum. Genet. , vol.90 , pp. 879-887
    • Sato, D.1    Lionel, A.C.2    Leblond, C.S.3
  • 79
    • 0037523396 scopus 로고    scopus 로고
    • CYFIP/Sra-1 controls neuronal connectivity in Drosophila and links the Rac1 GTPase pathway to the fragile X protein
    • Schenck A., Bardoni B., Langmann C., Harden N., Mandel J. L., and, Giangrande A., (2003) CYFIP/Sra-1 controls neuronal connectivity in Drosophila and links the Rac1 GTPase pathway to the fragile X protein. Neuron 38, 887-898.
    • (2003) Neuron , vol.38 , pp. 887-898
    • Schenck, A.1    Bardoni, B.2    Langmann, C.3    Harden, N.4    Mandel, J.L.5    Giangrande, A.6
  • 80
    • 34548269154 scopus 로고    scopus 로고
    • N-cadherin regulates cytoskeletally associated IQGAP1/ERK signaling and memory formation
    • Schrick C., Fischer A., Srivastava D., Tronson N., Penzes P., and, Radulovic J., (2007) N-cadherin regulates cytoskeletally associated IQGAP1/ERK signaling and memory formation. Neuron 55, 786-798.
    • (2007) Neuron , vol.55 , pp. 786-798
    • Schrick, C.1    Fischer, A.2    Srivastava, D.3    Tronson, N.4    Penzes, P.5    Radulovic, J.6
  • 81
    • 33644827036 scopus 로고    scopus 로고
    • Activation of N-methyl-d-aspartate receptor induces a shift of drebrin distribution: Disappearance from dendritic spines and appearance in dendritic shafts
    • Sekino Y., Tanaka S., Hanamura K., Yamazaki H., Sasagawa Y., Xue Y., Hayashi K., and, Shirao T., (2006) Activation of N-methyl-d-aspartate receptor induces a shift of drebrin distribution: disappearance from dendritic spines and appearance in dendritic shafts. Mol. Cell. Neurosci. 31, 493-504.
    • (2006) Mol. Cell. Neurosci. , vol.31 , pp. 493-504
    • Sekino, Y.1    Tanaka, S.2    Hanamura, K.3    Yamazaki, H.4    Sasagawa, Y.5    Xue, Y.6    Hayashi, K.7    Shirao, T.8
  • 82
    • 34547488455 scopus 로고    scopus 로고
    • Role of actin cytoskeleton in dendritic spine morphogenesis
    • Sekino Y., Kojima N., and, Shirao T., (2007) Role of actin cytoskeleton in dendritic spine morphogenesis. Neurochem. Int. 51, 92-104.
    • (2007) Neurochem. Int. , vol.51 , pp. 92-104
    • Sekino, Y.1    Kojima, N.2    Shirao, T.3
  • 83
    • 79851502285 scopus 로고    scopus 로고
    • Atomic force microscopy reveals drebrin induced remodeling of f-actin with subnanometer resolution
    • Sharma S., Grintsevich E. E., Phillips M. L., Reisler E., and, Gimzewski J. K., (2011) Atomic force microscopy reveals drebrin induced remodeling of f-actin with subnanometer resolution. Nano Lett. 11, 825-827.
    • (2011) Nano Lett. , vol.11 , pp. 825-827
    • Sharma, S.1    Grintsevich, E.E.2    Phillips, M.L.3    Reisler, E.4    Gimzewski, J.K.5
  • 84
    • 84864751696 scopus 로고    scopus 로고
    • Molecular cooperativity of drebrin1-300 binding and structural remodeling of F-actin
    • Sharma S., Grintsevich E. E., Hsueh C., Reisler E., and, Gimzewski J. K., (2012) Molecular cooperativity of drebrin1-300 binding and structural remodeling of F-actin. Biophys. J. 103, 275-283.
    • (2012) Biophys. J. , vol.103 , pp. 275-283
    • Sharma, S.1    Grintsevich, E.E.2    Hsueh, C.3    Reisler, E.4    Gimzewski, J.K.5
  • 85
    • 0037166050 scopus 로고    scopus 로고
    • Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome
    • Shim K. S., and, Lubec G., (2002) Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome. Neurosci. Lett. 324, 209-212.
    • (2002) Neurosci. Lett. , vol.324 , pp. 209-212
    • Shim, K.S.1    Lubec, G.2
  • 86
    • 0026512294 scopus 로고
    • Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells
    • Shirao T., Kojima N., and, Obata K., (1992) Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells. NeuroReport 3, 109-112.
    • (1992) NeuroReport , vol.3 , pp. 109-112
    • Shirao, T.1    Kojima, N.2    Obata, K.3
  • 87
    • 0027961093 scopus 로고
    • Formation of thick, curving bundles of actin by drebrin A expressed in fibroblasts
    • Shirao T., Hayashi K., Ishikawa R., Isa K., Asada H., Ikeda K., and, Uyemura K., (1994) Formation of thick, curving bundles of actin by drebrin A expressed in fibroblasts. Exp. Cell Res. 215, 145-153.
    • (1994) Exp. Cell Res. , vol.215 , pp. 145-153
    • Shirao, T.1    Hayashi, K.2    Ishikawa, R.3    Isa, K.4    Asada, H.5    Ikeda, K.6    Uyemura, K.7
  • 88
    • 0036176244 scopus 로고    scopus 로고
    • Rapid turnover of actin in dendritic spines and its regulation by activity
    • Star E. N., Kwiatkowski D. J., and, Murthy V. N., (2002) Rapid turnover of actin in dendritic spines and its regulation by activity. Nat. Neurosci. 5, 239-246.
    • (2002) Nat. Neurosci. , vol.5 , pp. 239-246
    • Star, E.N.1    Kwiatkowski, D.J.2    Murthy, V.N.3
  • 89
    • 55049085418 scopus 로고    scopus 로고
    • Destabilization of the postsynaptic density by PSD-95 serine 73 phosphorylation inhibits spine growth and synaptic plasticity
    • Steiner P., Higley M. J., Xu W., Czervionke B. L., Malenka R. C., and, Sabatini B. L., (2008) Destabilization of the postsynaptic density by PSD-95 serine 73 phosphorylation inhibits spine growth and synaptic plasticity. Neuron 60, 788-802.
    • (2008) Neuron , vol.60 , pp. 788-802
    • Steiner, P.1    Higley, M.J.2    Xu, W.3    Czervionke, B.L.4    Malenka, R.C.5    Sabatini, B.L.6
  • 90
    • 54049091941 scopus 로고    scopus 로고
    • Neuroligins and neurexins link synaptic function to cognitive disease
    • Südhof T. C., (2008) Neuroligins and neurexins link synaptic function to cognitive disease. Nature 455, 903-911.
    • (2008) Nature , vol.455 , pp. 903-911
    • Südhof, T.C.1
  • 92
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons M., Derry J. M., Karlak B., Jiang S., Lemahieu V., Mccormick F., Francke U., and, Abo A., (1996) Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84, 723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6    Francke, U.7    Abo, A.8
  • 93
    • 32344435520 scopus 로고    scopus 로고
    • Molecular mechanisms of dendritic spine morphogenesis
    • Tada T., and, Sheng M., (2006) Molecular mechanisms of dendritic spine morphogenesis. Curr. Opin. Neurobiol. 16, 95-101.
    • (2006) Curr. Opin. Neurobiol. , vol.16 , pp. 95-101
    • Tada, T.1    Sheng, M.2
  • 94
    • 0041342023 scopus 로고    scopus 로고
    • Drebrin-dependent actin clustering in dendritic filopodia governs synaptic targeting of postsynaptic density-95 and dendritic spine morphogenesis
    • Takahashi H., Sekino Y., Tanaka S., Mizui T., Kishi S., and, Shirao T., (2003) Drebrin-dependent actin clustering in dendritic filopodia governs synaptic targeting of postsynaptic density-95 and dendritic spine morphogenesis. J. Neurosci. 23, 6586-6595.
    • (2003) J. Neurosci. , vol.23 , pp. 6586-6595
    • Takahashi, H.1    Sekino, Y.2    Tanaka, S.3    Mizui, T.4    Kishi, S.5    Shirao, T.6
  • 95
    • 66849109049 scopus 로고    scopus 로고
    • AMPA receptor inhibition causes abnormal dendritic spines by destabilizing drebrin
    • Takahashi H., Yamazaki H., Hanamura K., Sekino Y., and, Shirao T., (2009) AMPA receptor inhibition causes abnormal dendritic spines by destabilizing drebrin. J. Cell Sci. 122, 1211-1229.
    • (2009) J. Cell Sci. , vol.122 , pp. 1211-1229
    • Takahashi, H.1    Yamazaki, H.2    Hanamura, K.3    Sekino, Y.4    Shirao, T.5
  • 96
    • 0027102583 scopus 로고
    • Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau
    • Takemura R., Okabe S., Umeyama T., Kanai Y., Cowan N. J., and, Hirokawa N., (1992) Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau. J. Cell Sci. 103, 953-964.
    • (1992) J. Cell Sci. , vol.103 , pp. 953-964
    • Takemura, R.1    Okabe, S.2    Umeyama, T.3    Kanai, Y.4    Cowan, N.J.5    Hirokawa, N.6
  • 97
    • 70450184120 scopus 로고    scopus 로고
    • Investigating sub-spine actin dynamics in rat hippocampal neurons with super-resolution optical imaging
    • Tatavarty V., Kim E. J., Rodionov V., and, Yu J., (2009) Investigating sub-spine actin dynamics in rat hippocampal neurons with super-resolution optical imaging. PLoS ONE 4, e7724.
    • (2009) PLoS ONE , vol.4
    • Tatavarty, V.1    Kim, E.J.2    Rodionov, V.3    Yu, J.4
  • 100
    • 0023034195 scopus 로고
    • Reversible assembly purification of microtubules without assembly-promoting agents and further purification of tubulin, microtubule-associated proteins, and MAP fragments
    • Vallee R. B., (1986) Reversible assembly purification of microtubules without assembly-promoting agents and further purification of tubulin, microtubule-associated proteins, and MAP fragments. Methods Enzymol. 134, 89-104.
    • (1986) Methods Enzymol. , vol.134 , pp. 89-104
    • Vallee, R.B.1
  • 101
    • 70350020891 scopus 로고    scopus 로고
    • Phosphorylation of CLASP2 by GSK-3beta regulates its interaction with IQGAP1, EB1 and microtubules
    • Watanabe T., Noritake J., Kakeno M., et al,. (2009) Phosphorylation of CLASP2 by GSK-3beta regulates its interaction with IQGAP1, EB1 and microtubules. J. Cell Sci. 122, 2969-2979.
    • (2009) J. Cell Sci. , vol.122 , pp. 2969-2979
    • Watanabe, T.1    Noritake, J.2    Kakeno, M.3
  • 102
    • 0017176529 scopus 로고
    • Head to tail polymerization of actin
    • Wegner A., (1976) Head to tail polymerization of actin. J. Mol. Biol. 108, 139-150.
    • (1976) J. Mol. Biol. , vol.108 , pp. 139-150
    • Wegner, A.1
  • 103
    • 0019188788 scopus 로고
    • Microtubules, dendritic spines and spine appratuses
    • Westrum L. E., Jones D. H., Gray E. G., and, Barron J., (1980) Microtubules, dendritic spines and spine appratuses. Cell Tissue Res. 208, 171-181.
    • (1980) Cell Tissue Res. , vol.208 , pp. 171-181
    • Westrum, L.E.1    Jones, D.H.2    Gray, E.G.3    Barron, J.4
  • 105
    • 16344390935 scopus 로고    scopus 로고
    • A GIT1/PIX/Rac/PAK signaling module regulates spine morphogenesis and synapse formation through MLC
    • Zhang H., Webb D. J., Asmussen H., Niu S., and, Horwitz A. F., (2005) A GIT1/PIX/Rac/PAK signaling module regulates spine morphogenesis and synapse formation through MLC. J. Neurosci. 25, 3379-3388.
    • (2005) J. Neurosci. , vol.25 , pp. 3379-3388
    • Zhang, H.1    Webb, D.J.2    Asmussen, H.3    Niu, S.4    Horwitz, A.F.5
  • 106
    • 31544476561 scopus 로고    scopus 로고
    • Role of p21-activated kinase pathway defects in the cognitive deficits of Alzheimer disease
    • Zhao L., Ma Q. L., Calon F., et al,. (2006) Role of p21-activated kinase pathway defects in the cognitive deficits of Alzheimer disease. Nat. Neurosci. 9, 234-242.
    • (2006) Nat. Neurosci. , vol.9 , pp. 234-242
    • Zhao, L.1    Ma, Q.L.2    Calon, F.3


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