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Volumn , Issue , 2008, Pages 27-50

To the nucleus with proteomics

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[No Author keywords available]

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EID: 67649401575     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-0-387-73609-9_2     Document Type: Chapter
Times cited : (3)

References (149)
  • 1
    • 0035889083 scopus 로고    scopus 로고
    • Regulation of nucleocytoplasmic trafficking by cell adhesion receptors and the cytoskeleton
    • Aplin, A. E., and Juliano, R. L. (2001) Regulation of nucleocytoplasmic trafficking by cell adhesion receptors and the cytoskeleton. J. Cell Biol. 155, 187-191.
    • (2001) J. Cell Biol. , vol.155 , pp. 187-191
    • Aplin, A.E.1    Juliano, R.L.2
  • 3
    • 0034595219 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 and an interacting tran scription factor regulate ErbB-2 expression
    • Balda, M. S., andMatter, K. (2000) The tight junction protein ZO-1 and an interacting tran scription factor regulate ErbB-2 expression. EMBO J. 19, 2024-2033.
    • (2000) EMBO J. , vol.19 , pp. 2024-2033
    • Balda, M.S.1    AndMatter, K.2
  • 4
    • 0016289176 scopus 로고
    • Proteins of the postsynaptic density
    • Banker, G., Churchill, L., and Cotman, C. W. (1974) Proteins of the postsynaptic density. J. Cell Biol. 63, 456-465.
    • (1974) J. Cell Biol. , vol.63 , pp. 456-465
    • Banker, G.1    Churchill, L.2    Cotman, C.W.3
  • 5
    • 0028897761 scopus 로고
    • N-cadherin is a major glycoprotein component of isolated rat forebrain postsynaptic densities
    • Beesley, P.W., Mummery, R., and Tibaldi, J. (1995) N-cadherin is a major glycoprotein component of isolated rat forebrain postsynaptic densities. J. Neurochem. 64, 2288-2294.
    • (1995) J. Neurochem , vol.64 , pp. 2288-2294
    • Beesley, P.W.1    Mummery, R.2    Tibaldi, J.3
  • 7
    • 0034611731 scopus 로고    scopus 로고
    • Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity
    • Bianchi, E., Denti, S., Granata, A., Bossi, G., Geginat, J., Villa, A., Rogge, L., and Pardi, R. (2000) Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity. Nature 404, 617-621.
    • (2000) Nature , vol.404 , pp. 617-621
    • Bianchi, E.1    Denti, S.2    Granata, A.3    Bossi, G.4    Geginat, J.5    Villa, A.6    Rogge, L.7    Pardi, R.8
  • 8
    • 33747845027 scopus 로고    scopus 로고
    • Splicing bioinformatics to biology
    • Black, D. L., and Graveley, B. R. (2006) Splicing bioinformatics to biology. Genome Biol. 7, 317.
    • (2006) Genome Biol. , vol.7 , pp. 317
    • Black, D.L.1    Graveley, B.R.2
  • 10
    • 0028126769 scopus 로고
    • Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion
    • Butz, S., and Kemler, R. (1994) Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion. FEBS Lett. 355, 195-200.
    • (1994) FEBS Lett. , vol.355 , pp. 195-200
    • Butz, S.1    Kemler, R.2
  • 11
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao, X., and Sudhof, T. C. (2001) A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293, 115-120.
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 12
    • 0019134836 scopus 로고
    • Isolation and characteriza tion of postsynaptic densities from various brain regions: Enrichment of different types of postsynaptic densities
    • Carlin, R. K., Grab, D. J., Cohen, R. S., and Siekevitz, P. (1980) Isolation and characteriza tion of postsynaptic densities from various brain regions: enrichment of different types of postsynaptic densities. J. Cell Biol. 86, 831-845.
    • (1980) J. Cell Biol. , vol.86 , pp. 831-845
    • Carlin, R.K.1    Grab, D.J.2    Cohen, R.S.3    Siekevitz, P.4
  • 13
    • 33845958654 scopus 로고    scopus 로고
    • α-Actinin 4 Potentiates Myocyte Enhancer Factor-2 Transcription Activ ity by Antagonizing Histone Deacetylase 7
    • Chakraborty, S., Reineke, E. L., Lam, M., Li, X., Liu, Y., Gao, C., Khurana, S., and Kao, H. Y. (2006) α-Actinin 4 Potentiates Myocyte Enhancer Factor-2 Transcription Activ ity by Antagonizing Histone Deacetylase 7. J. Biol. Chem. 281, 35070-35080.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35070-35080
    • Chakraborty, S.1    Reineke, E.L.2    Lam, M.3    Li, X.4    Liu, Y.5    Gao, C.6    Khurana, S.7    Kao, H.Y.8
  • 14
    • 0042125569 scopus 로고    scopus 로고
    • Integrin require ment for hippocampal synaptic plasticity and spatial memory
    • Chan, C. S., Weeber, E. J., Kurup, S., Sweatt, J. D., and Davis, R. L. (2003) Integrin require ment for hippocampal synaptic plasticity and spatial memory. J. Neurosci. 23, 7107-7116.
    • (2003) J. Neurosci. , vol.23 , pp. 7107-7116
    • Chan, C.S.1    Weeber, E.J.2    Kurup, S.3    Sweatt, J.D.4    Davis, R.L.5
  • 15
    • 0037379709 scopus 로고    scopus 로고
    • Neuronal activ itydependent nucleocytoplasmic shuttling of HDAC4 and HDAC5
    • Chawla, S., Vanhoutte, P., Arnold, F. J., Huang, C. L., and Bading, H. (2003) Neuronal activ itydependent nucleocytoplasmic shuttling of HDAC4 and HDAC5. J. Neurochem. 85, 151-159.
    • (2003) J. Neurochem. , vol.85 , pp. 151-159
    • Chawla, S.1    Vanhoutte, P.2    Arnold, F.J.3    Huang, C.L.4    Bading, H.5
  • 16
    • 17444394481 scopus 로고    scopus 로고
    • Im paired long-term potentiation in c-Jun N-terminal kinase 2-deficient mice
    • Chen, J. T., Lu, D. H., Chia, C. P., Ruan, D. Y., Sabapathy, K., and Xiao, Z. C. (2005) Im paired long-term potentiation in c-Jun N-terminal kinase 2-deficient mice. J. Neurochem. 93, 463-473.
    • (2005) J. Neurochem. , vol.93 , pp. 463-473
    • Chen, J.T.1    Lu, D.H.2    Chia, C.P.3    Ruan, D.Y.4    Sabapathy, K.5    Xiao, Z.C.6
  • 17
    • 33745994650 scopus 로고    scopus 로고
    • Alternative splicing controls selective trans- synaptic interactions of the neuroligin-neurexin complex
    • Chih, B., Gollan, L., and Scheiffele, P. (2006) Alternative splicing controls selective trans- synaptic interactions of the neuroligin-neurexin complex. Neuron 51, 171-178.
    • (2006) Neuron , vol.51 , pp. 171-178
    • Chih, B.1    Gollan, L.2    Scheiffele, P.3
  • 18
    • 0034307444 scopus 로고    scopus 로고
    • Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domaincontaining proteins
    • Chung, H. J., Xia, J., Scannevin, R. H., Zhang, X., and Huganir, R. L. (2000) Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domaincontaining proteins. J. Neurosci. 20, 7258-7267.
    • (2000) J. Neurosci. , vol.20 , pp. 7258-7267
    • Chung, H.J.1    Xia, J.2    Scannevin, R.H.3    Zhang, X.4    Huganir, R.L.5
  • 19
    • 28444456713 scopus 로고    scopus 로고
    • CAJAL BODIES: A long history of discovery
    • Cioce, M., and Lamond, A. I. (2005) CAJAL BODIES: A Long History of Discovery. Annu. Rev. Cell Dev. Biol. 21, 105-131.
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 105-131
    • Cioce, M.1    Lamond, A.I.2
  • 20
    • 0017396421 scopus 로고
    • The structure of postsynap tic densities isolated from dog cerebral cortex. I. Overall morphology and protein com position
    • Cohen, R. S., Blomberg, F., Berzins, K., and Siekevitz, P. (1977) The structure of postsynap tic densities isolated from dog cerebral cortex. I. Overall morphology and protein com position. J. Cell Biol. 74, 181-203.
    • (1977) J. Cell Biol. , vol.74 , pp. 181-203
    • Cohen, R.S.1    Blomberg, F.2    Berzins, K.3    Siekevitz, P.4
  • 21
    • 33646823604 scopus 로고    scopus 로고
    • Molecular characterization and comparison of the components and multiprotein complexes in the postsynaptic proteome
    • Collins, M. O., Husi, H., Yu, L., Brandon, J. M., Anderson, C. N., Blackstock, W. P., Choudhary, J. S., and Grant, S. G. (2006) Molecular characterization and comparison of the components and multiprotein complexes in the postsynaptic proteome. J. Neurochem. 97 Suppl 1, 16-23.
    • (2006) J. Neurochem. , vol.97 , pp. 16-23
    • Collins, M.O.1    Husi, H.2    Yu, L.3    Brandon, J.M.4    Anderson, C.N.5    Blackstock, W.P.6    Choudhary, J.S.7    Grant, S.G.8
  • 22
    • 7244245762 scopus 로고    scopus 로고
    • Finishing the euchromatic sequence of the human genome
    • Consortium, I. H. G. S. (2004) Finishing the euchromatic sequence of the human genome. Nature 431, 931-945.
    • (2004) Nature , vol.431 , pp. 931-945
    • Consortium, I.H.G.S.1
  • 23
    • 0035877590 scopus 로고    scopus 로고
    • Regulation of nuclear localization during signaling
    • Cyert, M. S. (2001) Regulation of nuclear localization during signaling. J. Biol. Chem. 276, 20805-20808.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20805-20808
    • Cyert, M.S.1
  • 24
    • 0028940096 scopus 로고
    • A rotein related to extracellular matrix proteins deleted in the mouse mutant reeler
    • D'Arcangelo, G., Miao, G. G., Chen, S. C., Soares, H. D., Morgan, J. I., and Curran, T. (1995) A rotein 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
  • 25
  • 26
    • 28444459973 scopus 로고    scopus 로고
    • Preparation of postsynaptic density fraction from hippocampal slices and proteomic analysis
    • Dosemeci, A., Tao-Cheng, J. H., Vinade, L., and Jaffe, H. (2006) Preparation of postsynaptic density fraction from hippocampal slices and proteomic analysis. Biochem. Biophys. Res. Commun. 339, 687-694.
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 687-694
    • Dosemeci, A.1    Tao-Cheng, J.H.2    Vinade, L.3    Jaffe, H.4
  • 27
    • 0035242433 scopus 로고    scopus 로고
    • An RNA recognition motif (RRM) is required for the localization of PTB-associated splicing factor (PSF) to subnuclear speckles
    • Dye, B. T., and Patton, J. G. (2001) An RNA recognition motif (RRM) is required for the localization of PTB-associated splicing factor (PSF) to subnuclear speckles. Exp. Cell Res. 263, 131-144.
    • (2001) Exp. Cell Res. , vol.263 , pp. 131-144
    • Dye, B.T.1    Patton, J.G.2
  • 28
    • 0029915306 scopus 로고    scopus 로고
    • Binding to cadherins antagonizes the signaling activity of beta-catenin during axis formation in Xenopus
    • Fagotto, F., Funayama, N., Gluck, U., and Gumbiner, B. M. (1996) Binding to cadherins antagonizes the signaling activity of beta-catenin during axis formation in Xenopus. J. Cell Biol. 132, 1105-1114.
    • (1996) J. Cell Biol. , vol.132 , pp. 1105-1114
    • Fagotto, F.1    Funayama, N.2    Gluck, U.3    Gumbiner, B.M.4
  • 29
    • 0031046778 scopus 로고    scopus 로고
    • Fragile X mental retardation protein: Nucleocytoplasmic shuttling and association with somatodendritic ribosomes
    • Feng, Y., Gutekunst, C. A., Eberhart, D. E., Yi, H., Warren, S. T., and Hersch, S. M. (1997) Fragile X mental retardation protein: nucleocytoplasmic shuttling and association with somatodendritic ribosomes. J. Neurosci. 17, 1539-1547.
    • (1997) J. Neurosci. , vol.17 , pp. 1539-1547
    • Feng, Y.1    Gutekunst, C.A.2    Eberhart, D.E.3    Yi, H.4    Warren, S.T.5    Hersch, S.M.6
  • 31
    • 0033517367 scopus 로고    scopus 로고
    • EB-1, a tyrosine kinase signal transduction gene, is transcriptionally activated in the t(1;19) subset of pre-B ALL, which express oncoprotein E2a-Pbx1
    • Fu, X., McGrath, S., Pasillas, M., Nakazawa, S., and Kamps, M. P. (1999) EB-1, a tyrosine kinase signal transduction gene, is transcriptionally activated in the t(1;19) subset of pre-B ALL, which express oncoprotein E2a-Pbx1. Oncogene 18, 4920-4929.
    • (1999) Oncogene , vol.18 , pp. 4920-4929
    • Fu, X.1    McGrath, S.2    Pasillas, M.3    Nakazawa, S.4    Kamps, M.P.5
  • 32
  • 33
    • 30544448358 scopus 로고    scopus 로고
    • TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines
    • Fujii, R., and Takumi, T. (2005) TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines. J. Cell Sci. 118, 5755-5765.
    • (2005) J. Cell Sci. , vol.118 , pp. 5755-5765
    • Fujii, R.1    Takumi, T.2
  • 34
    • 0345169047 scopus 로고    scopus 로고
    • The centennial of the Cajal body
    • Gall, J. G. (2003) The centennial of the Cajal body. Nat. Rev. Mol. Cell Biol. 4, 975-980.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 975-980
    • Gall, J.G.1
  • 36
    • 0029934811 scopus 로고    scopus 로고
    • The human hnRNP-M proteins: Structure and relation with early heat shock- induced splicing arrest and chromosome mapping
    • Gattoni, R., Mahe, D., Mahl, P., Fischer, N., Mattei, M. G., Stevenin, J., and Fuchs, J. P. (1996) The human hnRNP-M proteins: Structure and relation with early heat shock- induced splicing arrest and chromosome mapping. Nucleic Acids Res. 24, 2535-2542.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2535-2542
    • Gattoni, R.1    Mahe, D.2    Mahl, P.3    Fischer, N.4    Mattei, M.G.5    Stevenin, J.6    Fuchs, J.P.7
  • 37
    • 33744535466 scopus 로고    scopus 로고
    • Cell adhesion molecules at the synapse
    • Gerrow, K., and El-Husseini, A. (2006) Cell adhesion molecules at the synapse. Front. Biosci. 11, 2400-2419.
    • (2006) Front. Biosci. , vol.11 , pp. 2400-2419
    • Gerrow, K.1    El-Husseini, A.2
  • 38
    • 10344247703 scopus 로고    scopus 로고
    • Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner
    • Ghersi, E., Noviello, C., and D'Adamio, L. (2004) Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner. J. Biol. Chem. 279, 49105-49112.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49105-49112
    • Ghersi, E.1    Noviello, C.2    D'Adamio, L.3
  • 39
    • 33747339465 scopus 로고    scopus 로고
    • Wnt signaling: Multiple pathways, multiple receptors, and multiple transcription factors
    • Gordon, M. D., and Nusse, R. (2006) Wnt signaling: multiple pathways, multiple receptors, and multiple transcription factors. J. Biol. Chem. 281, 22429-22433.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22429-22433
    • Gordon, M.D.1    Nusse, R.2
  • 40
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich, D., and Kutay, U. (1999) Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 15, 607-660.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 41
    • 0029744106 scopus 로고    scopus 로고
    • The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts
    • Gottardi, C. J., Arpin, M., Fanning, A. S., and Louvard, D. (1996) The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts. Proc. Natl. Acad. Sci. USA 93, 10779-10784.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10779-10784
    • Gottardi, C.J.1    Arpin, M.2    Fanning, A.S.3    Louvard, D.4
  • 43
    • 0034213297 scopus 로고    scopus 로고
    • Inhibition of activity-dependent arc protein expression in the rat hippocampus impairs the maintenance of long-term potentiation and the consolidation of longterm memory
    • Guzowski, J. F., Lyford, G. L., Stevenson, G. D., Houston, F. P., McGaugh, J. L., Worley, P. F., and Barnes, C. A. (2000) Inhibition of activity-dependent arc protein expression in the rat hippocampus impairs the maintenance of long-term potentiation and the consolidation of longterm memory. J. Neurosci. 20, 3993-4001.
    • (2000) J. Neurosci. , vol.20 , pp. 3993-4001
    • Guzowski, J.F.1    Lyford, G.L.2    Stevenson, G.D.3    Houston, F.P.4    McGaugh, J.L.5    Worley, P.F.6    Barnes, C.A.7
  • 44
    • 0032570707 scopus 로고    scopus 로고
    • The transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLS
    • Hallier, M., Lerga, A., Barnache, S., Tavitian, A., and Moreau-Gachelin, F. (1998) The transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLS. J. Biol. Chem. 273, 4838-4842.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4838-4842
    • Hallier, M.1    Lerga, A.2    Barnache, S.3    Tavitian, A.4    Moreau-Gachelin, F.5
  • 45
    • 0035116275 scopus 로고    scopus 로고
    • Nuclear calcium signaling controls CREBmediated gene expression triggered by synaptic activity
    • Hardingham, G. E., Arnold, F. J., and Bading, H. (2001) Nuclear calcium signaling controls CREBmediated gene expression triggered by synaptic activity. Nat. Neurosci. 4, 261-267.
    • (2001) Nat. Neurosci. , vol.4 , pp. 261-267
    • Hardingham, G.E.1    Arnold, F.J.2    Bading, H.3
  • 46
    • 14844340468 scopus 로고    scopus 로고
    • The p120 family of cell adhesion molecules
    • Hatzfeld, M. (2005) The p120 family of cell adhesion molecules. Eur J. Cell Biol. 84, 205-214.
    • (2005) Eur J. Cell Biol. , vol.84 , pp. 205-214
    • Hatzfeld, M.1
  • 47
    • 0038345674 scopus 로고    scopus 로고
    • Bursts of highfrequency stimulation trigger rapid delivery of pre-existing alpha-CaMKII mRNA to synapses: A mechanism in dendritic protein synthesis during long-term potentiation in adult awake rats
    • Havik, B., Rokke, H., Bardsen, K., Davanger, S., and Bramham, C. R. (2003) Bursts of highfrequency stimulation trigger rapid delivery of pre-existing alpha-CaMKII mRNA to synapses: A mechanism in dendritic protein synthesis during long-term potentiation in adult awake rats. Eur J. Neurosci. 17, 2679-2689.
    • (2003) Eur J. Neurosci. , vol.17 , pp. 2679-2689
    • Havik, B.1    Rokke, H.2    Bardsen, K.3    Davanger, S.4    Bramham, C.R.5
  • 49
    • 0033198190 scopus 로고    scopus 로고
    • Regulated expression and subcellular localization of syndecan heparan sulfate proteoglycans and the syndecan-binding protein CASK/LIN-2 during rat brain development
    • Hsueh, Y. P., and Sheng, M. (1999) Regulated expression and subcellular localization of syndecan heparan sulfate proteoglycans and the syndecan-binding protein CASK/LIN-2 during rat brain development. J. Neurosci. 19, 7415-7425.
    • (1999) J. Neurosci. , vol.19 , pp. 7415-7425
    • Hsueh, Y.P.1    Sheng, M.2
  • 50
    • 0034673760 scopus 로고    scopus 로고
    • Nuclear translocation and tran scription regulation by the membrane-associated guanylate kinase CASK/LIN-2
    • Hsueh, Y. P., Wang, T. F., Yang, F. C., and Sheng, M. (2000) Nuclear translocation and tran scription regulation by the membrane-associated guanylate kinase CASK/LIN-2. Nature 404, 298-302.
    • (2000) Nature , vol.404 , pp. 298-302
    • Hsueh, Y.P.1    Wang, T.F.2    Yang, F.C.3    Sheng, M.4
  • 51
    • 0037188502 scopus 로고    scopus 로고
    • Altered synaptic plas ticity in a mouse model of fragile X mental retardation
    • Huber, K. M., Gallagher, S. M., Warren, S. T., and Bear, M. F. (2002) Altered synaptic plas ticity in a mouse model of fragile X mental retardation. Proc. Natl. Acad. Sci. USA 99, 7746-7750.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7746-7750
    • Huber, K.M.1    Gallagher, S.M.2    Warren, S.T.3    Bear, M.F.4
  • 52
    • 0345343608 scopus 로고    scopus 로고
    • Nuclear localization of beta-catenin by interaction with transcription factor LEF-1
    • Huber, O., Korn, R., McLaughlin, J., Ohsugi, M., Herrmann, B. G., and Kemler, R. (1996) Nuclear localization of beta-catenin by interaction with transcription factor LEF-1. Mech. Dev. 59, 3-10.
    • (1996) Mech. Dev. , vol.59 , pp. 3-10
    • Huber, O.1    Korn, R.2    McLaughlin, J.3    Ohsugi, M.4    Herrmann, B.G.5    Kemler, R.6
  • 53
    • 0034899717 scopus 로고    scopus 로고
    • Roles of cytoskeletal and junctional plaque proteins in nuclear signaling
    • Hubner, S., Jans, D. A., and Drenckhahn, D. (2001) Roles of cytoskeletal and junctional plaque proteins in nuclear signaling. Int. Rev. Cytol. 208, 207-265.
    • (2001) Int. Rev. Cytol. , vol.208 , pp. 207-265
    • Hubner, S.1    Jans, D.A.2    Drenckhahn, D.3
  • 54
    • 0028572556 scopus 로고
    • E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton
    • Hulsken, J., Birchmeier, W., and Behrens, J. (1994) E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton. J. Cell Biol. 127, 2061-2069.
    • (1994) J. Cell Biol. , vol.127 , pp. 2061-2069
    • Hulsken, J.1    Birchmeier, W.2    Behrens, J.3
  • 55
    • 0033946468 scopus 로고    scopus 로고
    • Proteo mic analysis of NMDA receptor-adhesion protein signaling complexes
    • Husi, H., Ward, M. A., Choudhary, J. S., Blackstock, W. P., and Grant, S. G. (2000) Proteo mic analysis of NMDA receptor-adhesion protein signaling complexes. Nat. Neurosci. 3, 661-669.
    • (2000) Nat. Neurosci. , vol.3 , pp. 661-669
    • Husi, H.1    Ward, M.A.2    Choudhary, J.S.3    Blackstock, W.P.4    Grant, S.G.5
  • 56
    • 0028850777 scopus 로고
    • Activity-dependent regulation of a ribosomal RNA epitope in the chick cochlear nucleus
    • Hyson, R. L., and Rubel, E. W. (1995) Activity-dependent regulation of a ribosomal RNA epitope in the chick cochlear nucleus. Brain Res. 672, 196-204.
    • (1995) Brain Res. , vol.672 , pp. 196-204
    • Hyson, R.L.1    Rubel, E.W.2
  • 58
    • 30544449081 scopus 로고    scopus 로고
    • A quantitative protein interaction network for the ErbB receptors using protein microarrays
    • Jones, R. B., Gordus, A., Krall, J. A., and MacBeath, G. (2006) A quantitative protein interaction network for the ErbB receptors using protein microarrays. Nature 439, 168-174.
    • (2006) Nature , vol.439 , pp. 168-174
    • Jones, R.B.1    Gordus, A.2    Krall, J.A.3    MacBeath, G.4
  • 61
    • 33947679342 scopus 로고    scopus 로고
    • Activity-dependent AIDA-1 nuclear signaling regulates nucleolar numbers and protein synthesis in neurons
    • Jordan, B. A., Fernholz, B. D., Khatri, L., Ziff, E. B. (2007) Activity-dependent AIDA-1 nuclear signaling regulates nucleolar numbers and protein synthesis in neurons. Nat. Neurosci. 10, 427-35.
    • (2007) Nat. Neurosci. , vol.10 , pp. 427-435
    • Jordan, B.A.1    Fernholz, B.D.2    Khatri, L.3    Ziff, E.B.4
  • 62
    • 0028889739 scopus 로고
    • Stimulation of ionotropic gluta mate receptors activates transcription factor NF-kappa B in primary neurons
    • Kaltschmidt, C., Kaltschmidt, B., and Baeuerle, P. A. (1995) Stimulation of ionotropic gluta mate receptors activates transcription factor NF-kappa B in primary neurons. Proc. Natl. Acad. Sci. USA 92, 9618-9622.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9618-9622
    • Kaltschmidt, C.1    Kaltschmidt, B.2    Baeuerle, P.A.3
  • 63
    • 2442435550 scopus 로고    scopus 로고
    • P54(nrb) associates with the 5' splice site within large transcription/splicing complexes
    • Kameoka, S., Duque, P., and Konarska, M. M. (2004) p54(nrb) associates with the 5' splice site within large transcription/splicing complexes. EMBO J. 23, 1782-1791.
    • (2004) EMBO J. , vol.23 , pp. 1782-1791
    • Kameoka, S.1    Duque, P.2    Konarska, M.M.3
  • 64
    • 0035798238 scopus 로고    scopus 로고
    • The molecular biology of memory storage: A dialogue between genes and synapses
    • Kandel, E. R. (2001) The molecular biology of memory storage: A dialogue between genes and synapses. Science 294, 1030-1038.
    • (2001) Science , vol.294 , pp. 1030-1038
    • Kandel, E.R.1
  • 65
    • 0033542725 scopus 로고    scopus 로고
    • Identi fication of a 55-kDa ezrin-related protein that induces cytoskeletal changes and localizes to the nucleolus
    • Kaul, S. C., Kawai, R., Nomura, H., Mitsui, Y., Reddel, R. R., and Wadhwa, R. (1999) Identi fication of a 55-kDa ezrin-related protein that induces cytoskeletal changes and localizes to the nucleolus. Exp. Cell Res. 250, 51-61.
    • (1999) Exp. Cell Res. , vol.250 , pp. 51-61
    • Kaul, S.C.1    Kawai, R.2    Nomura, H.3    Mitsui, Y.4    Reddel, R.R.5    Wadhwa, R.6
  • 66
    • 9444277252 scopus 로고    scopus 로고
    • Association of ARVCF with zonula occludens (ZO)-1 and ZO-2: Binding to PDZ-domain proteins and cell-cell adhesion regulate plasma membrane and nuclear localization of ARVCF
    • Kausalya, P. J., Phua, D. C., and Hunziker, W. (2004) Association of ARVCF with zonula occludens (ZO)-1 and ZO-2: binding to PDZ-domain proteins and cell-cell adhesion regulate plasma membrane and nuclear localization of ARVCF. Mol. Biol. Cell 15, 5503-5515.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5503-5515
    • Kausalya, P.J.1    Phua, D.C.2    Hunziker, W.3
  • 67
    • 33846136942 scopus 로고    scopus 로고
    • Functional interaction between the ZO-1-interacting transcription factor ZONAB/DbpA and the RNA processing factor symplekin
    • Kavanagh, E., Buchert, M., Tsapara, A., Choquet, A., Balda, M. S., Hollande, F., and Matter, K. (2006) Functional interaction between the ZO-1-interacting transcription factor ZONAB/DbpA and the RNA processing factor symplekin. J. Cell Sci. 119, 5098-5105.
    • (2006) J. Cell Sci. , vol.119 , pp. 5098-5105
    • Kavanagh, E.1    Buchert, M.2    Tsapara, A.3    Choquet, A.4    Balda, M.S.5    Hollande, F.6    Matter, K.7
  • 68
    • 1342322145 scopus 로고    scopus 로고
    • Trans lational control by MAPK signaling in long-term synaptic plasticity and memory
    • Kelleher, R. J. 3rd, Govindarajan, A., Jung, H. Y., Kang, H., and Tonegawa, S. (2004) Trans lational control by MAPK signaling in long-term synaptic plasticity and memory. Cell 116, 467-479.
    • (2004) Cell , vol.116 , pp. 467-479
    • Kelleher, R.J.1    Govindarajan, A.2    Jung, H.Y.3    Kang, H.4    Tonegawa, S.5
  • 69
    • 3242885068 scopus 로고    scopus 로고
    • NLS-dependent nuclear localization of p120ctn is necessary to relieve Kaiso-mediated transcriptional repression
    • Kelly, K. F., Spring, C. M., Otchere, A. A., and Daniel, J. M. (2004) NLS-dependent nuclear localization of p120ctn is necessary to relieve Kaiso-mediated transcriptional repression. J. Cell Sci. 117, 2675-2686.
    • (2004) J. Cell Sci. , vol.117 , pp. 2675-2686
    • Kelly, K.F.1    Spring, C.M.2    Otchere, A.A.3    Daniel, J.M.4
  • 70
    • 0027487859 scopus 로고
    • The postsynaptic density
    • Kennedy, M. B. (1993) The postsynaptic density. Curr Opin Neurobiol 3, 732-737.
    • (1993) Curr Opin Neurobiol , vol.3 , pp. 732-737
    • Kennedy, M.B.1
  • 71
    • 0035985054 scopus 로고    scopus 로고
    • The SH3, HOOK and guanylate kinase-like domains of hDLG are important for its cytoplasmic localization
    • Kohu, K., Ogawa, F., and Akiyama, T. (2002) The SH3, HOOK and guanylate kinase-like domains of hDLG are important for its cytoplasmic localization. Genes Cells 7, 707-715.
    • (2002) Genes Cells , vol.7 , pp. 707-715
    • Kohu, K.1    Ogawa, F.2    Akiyama, T.3
  • 72
    • 2142827074 scopus 로고    scopus 로고
    • Nuclear RNP complex assembly initiates cytoplasmic RNA localization
    • Kress, T. L., Yoon, Y. J., and Mowry, K. L. (2004) Nuclear RNP complex assembly initiates cytoplasmic RNA localization. J. Cell Biol. 165, 203-211.
    • (2004) J. Cell Biol. , vol.165 , pp. 203-211
    • Kress, T.L.1    Yoon, Y.J.2    Mowry, K.L.3
  • 73
    • 0028965387 scopus 로고
    • Number of nucleoli and coiled bodies and distribution of fibrillar centres in differentiating Purkinje neurons of chick and rat cerebellum
    • Berl
    • Lafarga, M., Andres, M. A., Fernandez-Viadero, C., Villegas, J., and Berciano, M. T. (1995) Number of nucleoli and coiled bodies and distribution of fibrillar centres in differentiating Purkinje neurons of chick and rat cerebellum. Anat. Embryol. (Berl) 191, 359-367.
    • (1995) Anat. Embryol. , vol.191 , pp. 359-367
    • Lafarga, M.1    Andres, M.A.2    Fernandez-Viadero, C.3    Villegas, J.4    Berciano, M.T.5
  • 75
    • 0031846441 scopus 로고    scopus 로고
    • Functional association of nuclear protein 4.1 with pre-mRNA splicing factors
    • Lallena, M. J., Martinez, C., Valcarcel, J., and Correas, I. (1998) Functional association of nuclear protein 4.1 with pre-mRNA splicing factors. J. Cell Sci. 111 (Pt 14), 1963-1971.
    • (1998) J. Cell Sci. , vol.111 , pp. 1963-1971
    • Lallena, M.J.1    Martinez, C.2    Valcarcel, J.3    Correas, I.4
  • 76
    • 0037422575 scopus 로고    scopus 로고
    • Evidence for the widespread coupling of alternative splicing and nonsense-mediated mRNA decay in humans
    • Lewis, B. P., Green, R. E., and Brenner, S. E. (2003) Evidence for the widespread coupling of alternative splicing and nonsense-mediated mRNA decay in humans. Proc. Natl. Acad. Sci. USA 100, 189-192.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 189-192
    • Lewis, B.P.1    Green, R.E.2    Brenner, S.E.3
  • 77
    • 20844455428 scopus 로고    scopus 로고
    • Organelle proteomics of rat synaptic proteins: Correlation-profiling by isotope- coded affinity tagging in conjunction with liquid chromatography-tandem mass spectrometry to reveal post-synaptic density specific proteins
    • Li, K., Hornshaw, M. P., van Minnen, J., Smalla, K. H., Gundelfinger, E. D., and Smit, A. B. (2005) Organelle proteomics of rat synaptic proteins: correlation-profiling by isotope- coded affinity tagging in conjunction with liquid chromatography-tandem mass spectrometry to reveal post-synaptic density specific proteins. J. Proteome Res. 4, 725-733.
    • (2005) J. Proteome Res. , vol.4 , pp. 725-733
    • Li, K.1    Hornshaw, M.P.2    Van Minnen, J.3    Smalla, K.H.4    Gundelfinger, E.D.5    Smit, A.B.6
  • 79
    • 0041828907 scopus 로고    scopus 로고
    • Heregulin targets gamma-catenin to the nucleolus by a mechanism dependent on the DF3/MUC1 oncoprotein
    • Li, Y., Yu, W. H., Ren, J., Chen, W., Huang, L., Kharbanda, S., Loda, M., and Kufe, D. (2003) Heregulin targets gamma-catenin to the nucleolus by a mechanism dependent on the DF3/MUC1 oncoprotein. Mol. Cancer Res. 1, 765-775.
    • (2003) Mol. Cancer Res. , vol.1 , pp. 765-775
    • Li, Y.1    Yu, W.H.2    Ren, J.3    Chen, W.4    Huang, L.5    Kharbanda, S.6    Loda, M.7    Kufe, D.8
  • 80
    • 0035368955 scopus 로고    scopus 로고
    • The fragile X mental retardation protein inhibits translation via interacting with mRNA
    • Li, Z., Zhang, Y., Ku, L., Wilkinson, K. D., Warren, S. T., and Feng, Y. (2001) The fragile X mental retardation protein inhibits translation via interacting with mRNA. Nucleic Acids Res. 29, 2276-2283.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2276-2283
    • Li, Z.1    Zhang, Y.2    Ku, L.3    Wilkinson, K.D.4    Warren, S.T.5    Feng, Y.6
  • 81
    • 0024038695 scopus 로고
    • Imaging of cytosolic Ca2+ transients arising from Ca2+ stores and Ca2+ channels in sympathetic neurons
    • Lipscombe, D., Madison, D. V., Poenie, M., Reuter, H., Tsien, R.W., and Tsien, R. Y. (1988) Imaging of cytosolic Ca2+ transients arising from Ca2+ stores and Ca2+ channels in sympathetic neurons. Neuron 1, 355-365.
    • (1988) Neuron , vol.1 , pp. 355-365
    • Lipscombe, D.1    Madison, D.V.2    Poenie, M.3    Reuter, H.4    Tsien, R.W.5    Tsien, R.Y.6
  • 82
    • 0030093785 scopus 로고    scopus 로고
    • Alternative splicing of the Brn-3a and Brn-3b transcription factor RNAs is regulated in neuronal cells
    • Liu, Y. Z., Dawson, S. J., and Latchman, D. S. (1996) Alternative splicing of the Brn-3a and Brn-3b transcription factor RNAs is regulated in neuronal cells. J. Mol. Neurosci. 7, 77- 85.
    • (1996) J. Mol. Neurosci. , vol.7 , pp. 77-85
    • Liu, Y.Z.1    Dawson, S.J.2    Latchman, D.S.3
  • 83
    • 3843145108 scopus 로고    scopus 로고
    • The brain-specific double-stranded RNA-binding protein Staufen2: Nucleolar accumulation and isoform-specific exportin-5-dependent export
    • Macchi, P., Brownawell, A. M., Grunewald, B., DesGroseillers, L., Macara, I. G., and Kiebler, M. A. (2004) The brain-specific double-stranded RNA-binding protein Staufen2: nucleolar accumulation and isoform-specific exportin-5-dependent export. J. Biol. Chem. 279, 31440-31444.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31440-31444
    • Macchi, P.1    Brownawell, A.M.2    Grunewald, B.3    DesGroseillers, L.4    Macara, I.G.5    Kiebler, M.A.6
  • 84
    • 0141429160 scopus 로고    scopus 로고
    • A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations
    • Marambaud, P., Wen, P. H., Dutt, A., Shioi, J., Takashima, A., Siman, R., and Robakis, N. K. (2003) A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations. Cell 114, 635-645.
    • (2003) Cell , vol.114 , pp. 635-645
    • Marambaud, P.1    Wen, P.H.2    Dutt, A.3    Shioi, J.4    Takashima, A.5    Siman, R.6    Robakis, N.K.7
  • 85
    • 30044443622 scopus 로고    scopus 로고
    • Staufen1 is imported into the nucleolus via a bipartite nuclear localization signal and several modulatory determinants
    • Martel, C., Macchi, P., Furic, L., Kiebler, M. A., and Desgroseillers, L. (2006) Staufen1 is imported into the nucleolus via a bipartite nuclear localization signal and several modulatory determinants. Biochem. J. 393, 245-254.
    • (2006) Biochem. J. , vol.393 , pp. 245-254
    • Martel, C.1    Macchi, P.2    Furic, L.3    Kiebler, M.A.4    Desgroseillers, L.5
  • 86
    • 0032823580 scopus 로고    scopus 로고
    • Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein
    • Matsuda, S., Mikawa, S., and Hirai, H. (1999) Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein. J. Neurochem. 73, 1765-1768.
    • (1999) J. Neurochem. , vol.73 , pp. 1765-1768
    • Matsuda, S.1    Mikawa, S.2    Hirai, H.3
  • 87
    • 0026543785 scopus 로고
    • Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2
    • Mayeda, A., and Krainer, A. R. (1992) Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2. Cell 68, 365-375.
    • (1992) Cell , vol.68 , pp. 365-375
    • Mayeda, A.1    Krainer, A.R.2
  • 88
    • 0033969570 scopus 로고    scopus 로고
    • Memory-A century of consolidation
    • McGaugh, J. L. (2000) Memory-a century of consolidation. Science 287, 248-251.
    • (2000) Science , vol.287 , pp. 248-251
    • McGaugh, J.L.1
  • 89
    • 0344407006 scopus 로고    scopus 로고
    • Proto- oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRm160, and SR proteins
    • Meissner, M., Lopato, S., Gotzmann, J., Sauermann, G., and Barta, A. (2003) Proto- oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRm160, and SR proteins. Exp. Cell Res. 283, 184-195.
    • (2003) Exp. Cell Res. , vol.283 , pp. 184-195
    • Meissner, M.1    Lopato, S.2    Gotzmann, J.3    Sauermann, G.4    Barta, A.5
  • 90
    • 0344688265 scopus 로고    scopus 로고
    • Activity-dependent mRNA splicing controls ER export and synaptic delivery of NMDA receptors
    • Mu, Y., Otsuka, T., Horton, A. C., Scott, D. B., and Ehlers, M. D. (2003) Activity-dependent mRNA splicing controls ER export and synaptic delivery of NMDA receptors. Neuron 40, 581-594.
    • (2003) Neuron , vol.40 , pp. 581-594
    • Mu, Y.1    Otsuka, T.2    Horton, A.C.3    Scott, D.B.4    Ehlers, M.D.5
  • 91
    • 0037014456 scopus 로고    scopus 로고
    • Depolarization drives beta-Catenin into neuronal spines promoting changes in synaptic structure and function
    • Murase, S., Mosser, E., and Schuman, E. M. (2002) Depolarization drives beta-Catenin into neuronal spines promoting changes in synaptic structure and function. Neuron 35, 91-105.
    • (2002) Neuron , vol.35 , pp. 91-105
    • Murase, S.1    Mosser, E.2    Schuman, E.M.3
  • 92
    • 0037249644 scopus 로고    scopus 로고
    • NLSdb: Database of nuclear localization signals
    • Nair, R., Carter, P., and Rost, B. (2003) NLSdb: database of nuclear localization signals. Nucleic Acids Res 31, 397-399.
    • (2003) Nucleic Acids Res , vol.31 , pp. 397-399
    • Nair, R.1    Carter, P.2    Rost, B.3
  • 93
    • 7944223219 scopus 로고    scopus 로고
    • GRIP1tau, a novel PDZ domaincontaining transcriptional activator, cooperates with the testis-specific transcription elongation factor SII-T1
    • Nakata, A., Ito, T., Nagata, M., Hori, S., and Sekimizu, K. (2004) GRIP1tau, a novel PDZ domaincontaining transcriptional activator, cooperates with the testis-specific transcription elongation factor SII-T1. Genes Cells 9, 1125-1135.
    • (2004) Genes Cells , vol.9 , pp. 1125-1135
    • Nakata, A.1    Ito, T.2    Nagata, M.3    Hori, S.4    Sekimizu, K.5
  • 94
    • 0035879180 scopus 로고    scopus 로고
    • Abnormal development of dendritic spines in FMR1 knock-out mice
    • Nimchinsky, E. A., Oberlander, A. M., and Svoboda, K. (2001) Abnormal development of dendritic spines in FMR1 knock-out mice. J. Neurosci. 21, 5139-5146.
    • (2001) J. Neurosci. , vol.21 , pp. 5139-5146
    • Nimchinsky, E.A.1    Oberlander, A.M.2    Svoboda, K.3
  • 95
  • 97
    • 0027245959 scopus 로고
    • Cloning and characterization of PSF, a novel pre-mRNA splicing factor
    • Patton, J. G., Porro, E. B., Galceran, J., Tempst, P., and Nadal-Ginard, B. (1993) Cloning and characterization of PSF, a novel pre-mRNA splicing factor. Genes Dev. 7, 393-406.
    • (1993) Genes Dev. , vol.7 , pp. 393-406
    • Patton, J.G.1    Porro, E.B.2    Galceran, J.3    Tempst, P.4    Nadal-Ginard, B.5
  • 98
    • 2442683994 scopus 로고    scopus 로고
    • Semi-quantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spec trometry
    • Peng, J., Kim, M. J., Cheng, D., Duong, D. M., Gygi, S. P., and Sheng, M. (2004) Semi-quantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spec trometry. J. Biol. Chem. 14, 21003-21011.
    • (2004) J. Biol. Chem. , vol.14 , pp. 21003-21011
    • Peng, J.1    Kim, M.J.2    Cheng, D.3    Duong, D.M.4    Gygi, S.P.5    Sheng, M.6
  • 99
    • 33746222965 scopus 로고    scopus 로고
    • Current advances in local protein synthesis and synaptic plasticity
    • Pfeiffer, B. E., and Huber, K. M. (2006) Current advances in local protein synthesis and synaptic plasticity. J. Neurosci. 26, 7147-7150.
    • (2006) J. Neurosci. , vol.26 , pp. 7147-7150
    • Pfeiffer, B.E.1    Huber, K.M.2
  • 101
    • 0026527447 scopus 로고
    • Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
    • Pinol-Roma, S., and Dreyfuss, G. (1992) Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature 355, 730-732.
    • (1992) Nature , vol.355 , pp. 730-732
    • Pinol-Roma, S.1    Dreyfuss, G.2
  • 102
    • 2942748224 scopus 로고    scopus 로고
    • Small is beautiful: What flies tell us about ERM protein function in development
    • Polesello, C., and Payre, F. (2004) Small is beautiful: What flies tell us about ERM protein function in development. Trends Cell Biol. 14, 294-302.
    • (2004) Trends Cell Biol. , vol.14 , pp. 294-302
    • Polesello, C.1    Payre, F.2
  • 103
    • 28844477891 scopus 로고    scopus 로고
    • Nucleolar biogenesis: The first small steps
    • Prieto, J. L., and McStay, B. (2005) Nucleolar biogenesis: The first small steps. Biochem. Soc. Trans. 33, 1441-1443.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1441-1443
    • Prieto, J.L.1    McStay, B.2
  • 104
    • 0029986152 scopus 로고    scopus 로고
    • STAT proteins are activated by ciliary neurotrophic factor in cells of central nervous system origin
    • Rajan, P., Symes, A. J., and Fink, J. S. (1996) STAT proteins are activated by ciliary neurotrophic factor in cells of central nervous system origin. J. Neurosci. Res 43, 403-411.
    • (1996) J. Neurosci. Res , vol.43 , pp. 403-411
    • Rajan, P.1    Symes, A.J.2    Fink, J.S.3
  • 105
    • 33748373580 scopus 로고    scopus 로고
    • RNA-mediated neuromuscular disorders
    • Ranum, L. P., and Cooper, T. A. (2006) RNA-mediated neuromuscular disorders. Annu. Rev. Neurosci. 29, 259-277.
    • (2006) Annu. Rev. Neurosci. , vol.29 , pp. 259-277
    • Ranum, L.P.1    Cooper, T.A.2
  • 106
    • 33845864415 scopus 로고    scopus 로고
    • The late maintenance of hippocampal LTP: Requirements, phases, 'synaptic tagging', 'late-associativity' and implications
    • Reymann, K. G., and Frey, J. U. (2007) The late maintenance of hippocampal LTP: Requirements, phases, 'synaptic tagging', 'late-associativity' and implications. Neuropharmacol. 52, 24-40.
    • (2007) Neuropharmacol , vol.52 , pp. 24-40
    • Reymann, K.G.1    Frey, J.U.2
  • 107
    • 0034192397 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor (BDNF) induces dendritic targeting of BDNF and tyrosine kinase B mRNAs in hippocampal neurons through a phosphatidylinositol-3 kinase-dependent pathway
    • Righi, M., Tongiorgi, E., and Cattaneo, A. (2000) Brain-derived neurotrophic factor (BDNF) induces dendritic targeting of BDNF and tyrosine kinase B mRNAs in hippocampal neurons through a phosphatidylinositol-3 kinase-dependent pathway. J. Neurosci. 20, 3165-3174.
    • (2000) J. Neurosci. , vol.20 , pp. 3165-3174
    • Righi, M.1    Tongiorgi, E.2    Cattaneo, A.3
  • 108
    • 0242382635 scopus 로고    scopus 로고
    • Regulation of p120-catenin nucleocyto plasmic shuttling activity
    • Roczniak-Ferguson, A., and Reynolds, A. B. (2003) Regulation of p120-catenin nucleocyto plasmic shuttling activity. J. Cell Sci. 116, 4201-4212.
    • (2003) J. Cell Sci. , vol.116 , pp. 4201-4212
    • Roczniak-Ferguson, A.1    Reynolds, A.B.2
  • 109
  • 110
    • 0034724337 scopus 로고    scopus 로고
    • Colocalization of integrin receptors and reelin in dendritic spine postsynaptic densities of adult nonhuman primate cortex
    • Rodriguez, M. A., Pesold, C., Liu, W. S., Kriho, V., Guidotti, A., Pappas, G. D., and Costa, E. (2000) Colocalization of integrin receptors and reelin in dendritic spine postsynaptic densities of adult nonhuman primate cortex. Proc. Natl. Acad. Sci. USA 97, 3550-3555.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3550-3555
    • Rodriguez, M.A.1    Pesold, C.2    Liu, W.S.3    Kriho, V.4    Guidotti, A.5    Pappas, G.D.6    Costa, E.7
  • 111
    • 0034257926 scopus 로고    scopus 로고
    • CaMKIIalpha 3' untranslated region-directed mRNA translocation in living neurons: Visualization by GFP linkage
    • Rook, M. S., Lu, M., and Kosik, K. S. (2000) CaMKIIalpha 3' untranslated region-directed mRNA translocation in living neurons: visualization by GFP linkage. J. Neurosci. 20, 6385-6393.
    • (2000) J. Neurosci. , vol.20 , pp. 6385-6393
    • Rook, M.S.1    Lu, M.2    Kosik, K.S.3
  • 112
    • 23844471326 scopus 로고    scopus 로고
    • HnRNP L represses exon splicing via a regulated exonic splicing silencer
    • Rothrock, C. R., House, A. E., and Lynch, K. W. (2005) HnRNP L represses exon splicing via a regulated exonic splicing silencer. EMBO J. 24, 2792-2802.
    • (2005) EMBO J , vol.24 , pp. 2792-2802
    • Rothrock, C.R.1    House, A.E.2    Lynch, K.W.3
  • 113
    • 0030856349 scopus 로고    scopus 로고
    • Regulation of beta-catenin levels and localization by overexpression of plakoglobin and inhibition of the ubiquitin-proteasome system
    • Salomon, D., Sacco, P. A., Roy, S. G., Simcha, I., Johnson, K. R., Wheelock, M. J., and Ben- Ze'ev, A. (1997) Regulation of beta-catenin levels and localization by overexpression of plakoglobin and inhibition of the ubiquitin-proteasome system. J. Cell Biol. 139, 1325-1335.
    • (1997) J. Cell Biol. , vol.139 , pp. 1325-1335
    • Salomon, D.1    Sacco, P.A.2    Roy, S.G.3    Simcha, I.4    Johnson, K.R.5    Wheelock, M.J.6    Ben- Ze'ev, A.7
  • 114
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Unamour impossible?
    • Santoni, V., Molloy, M., and Rabilloud, T. (2000) Membrane proteins and proteomics: unamour impossible? Electrophoresis 21, 1054-1070.
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 115
    • 0034625250 scopus 로고    scopus 로고
    • Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons
    • Scheiffele, P., Fan, J., Choih, J., Fetter, R., and Serafini, T. (2000) Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons. Cell 101, 657-669.
    • (2000) Cell , vol.101 , pp. 657-669
    • Scheiffele, P.1    Fan, J.2    Choih, J.3    Fetter, R.4    Serafini, T.5
  • 116
    • 33746196496 scopus 로고    scopus 로고
    • Synaptic regulation of translation of dendritic mRNAs
    • Schuman, E. M., Dynes, J. L., and Steward, O. (2006) Synaptic regulation of translation of dendritic mRNAs. J. Neurosci. 26, 7143-7146.
    • (2006) J. Neurosci. , vol.26 , pp. 7143-7146
    • Schuman, E.M.1    Dynes, J.L.2    Steward, O.3
  • 117
    • 0034332508 scopus 로고    scopus 로고
    • Regulation of AMPA receptor GluR1 subunit surface expression by a 4. 1N-linked actin cytoskeletal association
    • Shen, L., Liang, F., Walensky, L. D., and Huganir, R. L. (2000) Regulation of AMPA receptor GluR1 subunit surface expression by a 4. 1N-linked actin cytoskeletal association. J. Neurosci. 20, 7932-7940.
    • (2000) J. Neurosci. , vol.20 , pp. 7932-7940
    • Shen, L.1    Liang, F.2    Walensky, L.D.3    Huganir, R.L.4
  • 118
    • 4444272979 scopus 로고    scopus 로고
    • Cell signalling and the control of pre-mRNA splicing
    • Shin, C., and Manley, J. L. (2004) Cell signalling and the control of pre-mRNA splicing. Nat Rev Mol Cell Biol 5, 727-738.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 727-738
    • Shin, C.1    Manley, J.L.2
  • 119
    • 0346186101 scopus 로고    scopus 로고
    • A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in aplysia
    • Si, K., Giustetto, M., Etkin, A., Hsu, R., Janisiewicz, A. M., Miniaci, M. C., Kim, J. H., Zhu, H., and Kandel, E. R. (2003) A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in aplysia. Cell 115, 893-904.
    • (2003) Cell , vol.115 , pp. 893-904
    • Si, K.1    Giustetto, M.2    Etkin, A.3    Hsu, R.4    Janisiewicz, A.M.5    Miniaci, M.C.6    Kim, J.H.7    Zhu, H.8    Kandel, E.R.9
  • 120
    • 0024020782 scopus 로고
    • Excitatory amino acids activate calpain I and induce structural protein breakdown in vivo
    • Siman, R., and Noszek, J. C. (1988) Excitatory amino acids activate calpain I and induce structural protein breakdown in vivo. Neuron 1, 279-287.
    • (1988) Neuron , vol.1 , pp. 279-287
    • Siman, R.1    Noszek, J.C.2
  • 121
    • 0029917554 scopus 로고    scopus 로고
    • Suppression of tumorigenicity by plakoglobin: An augmenting effect of N-cadherin
    • Simcha, I., Geiger, B., Yehuda-Levenberg, S., Salomon, D., and Ben-Ze'ev, A. (1996) Suppression of tumorigenicity by plakoglobin: An augmenting effect of N-cadherin. J. Cell Biol. 133, 199-209.
    • (1996) J. Cell Biol. , vol.133 , pp. 199-209
    • Simcha, I.1    Geiger, B.2    Yehuda-Levenberg, S.3    Salomon, D.4    Ben-Ze'ev, A.5
  • 122
    • 3242748982 scopus 로고    scopus 로고
    • Positional changes of pericentromeric heterochromatin and nucleoli in postmitotic Purkinje cells during murine cerebellum development
    • Solovei, I., Grandi, N., Knoth, R., Volk, B., and Cremer, T. (2004) Positional changes of pericentromeric heterochromatin and nucleoli in postmitotic Purkinje cells during murine cerebellum development. Cytogenetic and Genome Research 105, 302-310.
    • (2004) Cytogenetic and Genome Research , vol.105 , pp. 302-310
    • Solovei, I.1    Grandi, N.2    Knoth, R.3    Volk, B.4    Cremer, T.5
  • 123
    • 33750993210 scopus 로고    scopus 로고
    • Intracellular trafficking of RNA in neurons
    • Sossin, W. S., and DesGroseillers, L. (2006) Intracellular trafficking of RNA in neurons. Traffic 7, 1581-1589.
    • (2006) Traffic , vol.7 , pp. 1581-1589
    • Sossin, W.S.1    DesGroseillers, L.2
  • 124
    • 0022637334 scopus 로고
    • Protein-synthetic machinery at postsynaptic sites during synaptogenesis: A quantitative study of the association between polyribosomes and developing synapses
    • Steward, O., and Falk, P. M. (1986) Protein-synthetic machinery at postsynaptic sites during synaptogenesis: A quantitative study of the association between polyribosomes and developing synapses. J. Neurosci. 6, 412-423.
    • (1986) J. Neurosci. , vol.6 , pp. 412-423
    • Steward, O.1    Falk, P.M.2
  • 125
    • 0020063563 scopus 로고
    • Preferential localization of polyribosomes under the base of dendritic spines in granule cells of the dentate gyrus
    • Steward, O., and Levy, W. B. (1982) Preferential localization of polyribosomes under the base of dendritic spines in granule cells of the dentate gyrus. J. Neurosci. 2, 284-291.
    • (1982) J. Neurosci. , vol.2 , pp. 284-291
    • Steward, O.1    Levy, W.B.2
  • 126
    • 0035912719 scopus 로고    scopus 로고
    • A cellular mechanism for targeting newly synthesized mRNAs to synaptic sites on dendrites
    • Steward, O., and Worley, P. F. (2001a) A cellular mechanism for targeting newly synthesized mRNAs to synaptic sites on dendrites. Proc. Natl. Acad. Sci. USA 98, 7062-7068.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7062-7068
    • Steward, O.1    Worley, P.F.2
  • 127
    • 0035036344 scopus 로고    scopus 로고
    • Selective targeting of newly synthesized Arc mRNA to active synapses requires NMDA receptor activation
    • Steward, O., and Worley, P. F. (2001b) Selective targeting of newly synthesized Arc mRNA to active synapses requires NMDA receptor activation. Neuron 30, 227-240.
    • (2001) Neuron , vol.30 , pp. 227-240
    • Steward, O.1    Worley, P.F.2
  • 128
    • 0035829728 scopus 로고    scopus 로고
    • A role for a rat homolog of staufen in the transport of RNA to neuronal dendrites
    • Tang, S. J., Meulemans, D., Vazquez, L., Colaco, N., and Schuman, E. (2001) A role for a rat homolog of staufen in the transport of RNA to neuronal dendrites. Neuron 32, 463-475.
    • (2001) Neuron , vol.32 , pp. 463-475
    • Tang, S.J.1    Meulemans, D.2    Vazquez, L.3    Colaco, N.4    Schuman, E.5
  • 129
    • 0028033340 scopus 로고
    • Spatial and temporal changes in signal transduction pathways during LTP
    • Thomas, K. L., Laroche, S., Errington, M. L., Bliss, T. V., and Hunt, S. P. (1994) Spatial and temporal changes in signal transduction pathways during LTP. Neuron 13, 737-745.
    • (1994) Neuron , vol.13 , pp. 737-745
    • Thomas, K.L.1    Laroche, S.2    Errington, M.L.3    Bliss, T.V.4    Hunt, S.P.5
  • 130
    • 10444251033 scopus 로고    scopus 로고
    • Synapse to nucleus signaling during long-term synaptic plasticity; a role for the classical active nuclear import pathway
    • Thompson, K. R., Otis, K. O., Chen, D. Y., Zhao, Y., O'Dell, T. J., and Martin, K. C. (2004) Synapse to nucleus signaling during long-term synaptic plasticity; a role for the classical active nuclear import pathway. Neuron 44, 997-1009.
    • (2004) Neuron , vol.44 , pp. 997-1009
    • Thompson, K.R.1    Otis, K.O.2    Chen, D.Y.3    Zhao, Y.4    O'Dell, T.J.5    Martin, K.C.6
  • 131
    • 0031439983 scopus 로고    scopus 로고
    • Activity-dependent dendritic targeting of BDNF and TrkB mRNAs in hippocampal neurons
    • Tongiorgi, E., Righi, M., and Cattaneo, A. (1997) Activity-dependent dendritic targeting of BDNF and TrkB mRNAs in hippocampal neurons. J. Neurosci. 17, 9492-9505.
    • (1997) J. Neurosci. , vol.17 , pp. 9492-9505
    • Tongiorgi, E.1    Righi, M.2    Cattaneo, A.3
  • 133
    • 0035933730 scopus 로고    scopus 로고
    • The WD motif-containing protein receptor for activated protein kinase C (RACK1) is required for recruitment and activation of signal transducer and activator of transcription 1 through the type I interferon receptor
    • Usacheva, A., Smith, R., Minshall, R., Baida, G., Seng, S., Croze, E., and Colamonici, O. (2001) The WD motif-containing protein receptor for activated protein kinase C (RACK1) is required for recruitment and activation of signal transducer and activator of transcription 1 through the type I interferon receptor. J. Biol. Chem. 276, 22948-22953.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22948-22953
    • Usacheva, A.1    Smith, R.2    Minshall, R.3    Baida, G.4    Seng, S.5    Croze, E.6    Colamonici, O.7
  • 135
    • 0034212618 scopus 로고    scopus 로고
    • Identification of Proteins in the Postsynaptic Density Fraction by Mass Spectrometry
    • Walikonis, R. S., Jensen, O. N., Mann, M., Provance, D. W. Jr, Mercer, J. A., and Kennedy, M. B. (2000) Identification of Proteins in the Postsynaptic Density Fraction by Mass Spectrometry. J. Neurosci. 20, 4069-4080.
    • (2000) J. Neurosci. , vol.20 , pp. 4069-4080
    • Walikonis, R.S.1    Jensen, O.N.2    Mann, M.3    Provance, D.W.4    Mercer, J.A.5    Kennedy, M.B.6
  • 136
    • 0026651939 scopus 로고
    • The postsynaptic density: Constituent and associated prot eins characterized by electrophoresis, immunoblotting, and peptide sequencing
    • Walsh, M. J., and Kuruc, N. (1992) The postsynaptic density: constituent and associated prot eins characterized by electrophoresis, immunoblotting, and peptide sequencing. J. Neuro chem. 59, 667-678.
    • (1992) J. Neuro Chem. , vol.59 , pp. 667-678
    • Walsh, M.J.1    Kuruc, N.2
  • 138
    • 0036884163 scopus 로고    scopus 로고
    • Regulation of transcription factors by neuronal activity
    • West, A. E., Griffith, E. C., and Greenberg, M. E. (2002) Regulation of transcription factors by neuronal activity. Nat. Rev. Neurosci. 3, 921-931.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 921-931
    • West, A.E.1    Griffith, E.C.2    Greenberg, M.E.3
  • 139
    • 8444243682 scopus 로고    scopus 로고
    • The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone
    • Williams, C. C., Allison, J. G., Vidal, G. A., Burow, M. E., Beckman, B. S., Marrero, L., and Jones, F. E. (2004) The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone. J. Cell Biol. 167, 469-478.
    • (2004) J. Cell Biol. , vol.167 , pp. 469-478
    • Williams, C.C.1    Allison, J.G.2    Vidal, G.A.3    Burow, M.E.4    Beckman, B.S.5    Marrero, L.6    Jones, F.E.7
  • 140
    • 0037155266 scopus 로고    scopus 로고
    • Paxillin associates with poly(A)-binding protein 1 at the dense endoplasmic reticulum and the leading edge of migrating cells
    • Woods, A. J., Roberts, M. S., Choudhary, J., Barry, S. T., Mazaki, Y., Sabe, H., Morley, S. J., Critchley, D. R., and Norman, J. C. (2002) Paxillin associates with poly(A)-binding protein 1 at the dense endoplasmic reticulum and the leading edge of migrating cells. J. Biol. Chem. 277, 6428-6437.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6428-6437
    • Woods, A.J.1    Roberts, M.S.2    Choudhary, J.3    Barry, S.T.4    Mazaki, Y.5    Sabe, H.6    Morley, S.J.7    Critchley, D.R.8    Norman, J.C.9
  • 141
    • 0032215079 scopus 로고    scopus 로고
    • CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of alpha-CaMKII mRNA at synapses
    • Wu, L., Wells, D., Tay, J., Mendis, D., Abbott, M. A., Barnitt, A., Quinlan, E., Heynen, A., Fallon, J. R., and Richter, J. D. (1998) CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of alpha-CaMKII mRNA at synapses. Neuron 21, 1129-1139.
    • (1998) Neuron , vol.21 , pp. 1129-1139
    • Wu, L.1    Wells, D.2    Tay, J.3    Mendis, D.4    Abbott, M.A.5    Barnitt, A.6    Quinlan, E.7    Heynen, A.8    Fallon, J.R.9    Richter, J.D.10
  • 142
    • 0031013896 scopus 로고    scopus 로고
    • Competitive binding of alpha-actinin and calmodulin to the NMDA receptor
    • Wyszynski, M., Lin, J., Rao, A., Nigh, E., Beggs, A. H., Craig, A. M., and Sheng, M. (1997) Competitive binding of alpha-actinin and calmodulin to the NMDA receptor. Nature 385, 439-442.
    • (1997) Nature , vol.385 , pp. 439-442
    • Wyszynski, M.1    Lin, J.2    Rao, A.3    Nigh, E.4    Beggs, A.H.5    Craig, A.M.6    Sheng, M.7
  • 143
    • 28344434660 scopus 로고    scopus 로고
    • A consensus CaMK IV-responsive RNA sequence mediates regulation of alternative exons in neurons
    • Xie, J., Jan, C., Stoilov, P., Park, J., and Black, D. L. (2005) A consensus CaMK IV-responsive RNA sequence mediates regulation of alternative exons in neurons. RNA 11, 1825-1834.
    • (2005) RNA , vol.11 , pp. 1825-1834
    • Xie, J.1    Jan, C.2    Stoilov, P.3    Park, J.4    Black, D.L.5
  • 144
    • 25444517097 scopus 로고    scopus 로고
    • A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body protein coilin
    • Xu, H., and Hebert, M. D. (2005) A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body protein coilin. BMC. Cell Biol. 6, 23.
    • (2005) BMC. Cell Biol. , vol.6 , pp. 23
    • Xu, H.1    Hebert, M.D.2
  • 145
    • 0942287657 scopus 로고    scopus 로고
    • Molecular constituents of the postsynaptic density fraction revealed by proteomic analysis using multidimensional liquid chromatography-tandem mass spectrometry
    • Yoshimura, Y., Yamauchi, Y., Shinkawa, T., Taoka, M., Donai, H., Takahashi, N., Isobe, T., and Yamauchi, T. (2004) Molecular constituents of the postsynaptic density fraction revealed by proteomic analysis using multidimensional liquid chromatography-tandem mass spectrometry. J. Neurochem. 88, 759-768.
    • (2004) J. Neurochem. , vol.88 , pp. 759-768
    • Yoshimura, Y.1    Yamauchi, Y.2    Shinkawa, T.3    Taoka, M.4    Donai, H.5    Takahashi, N.6    Isobe, T.7    Yamauchi, T.8
  • 146
    • 0035944532 scopus 로고    scopus 로고
    • Evidence that GRIP, a PDZ-domain protein which is expressed in the embryonic forebrain, co-activates transcription with DLX homeodomain proteins
    • Yu, G., Zerucha, T., Ekker, M., and Rubenstein, J. L. (2001) Evidence that GRIP, a PDZ-domain protein which is expressed in the embryonic forebrain, co-activates transcription with DLX homeodomain proteins. Brain Res. Dev. Brain Res. 130, 217-230.
    • (2001) Brain Res. Dev. Brain Res. , vol.130 , pp. 217-230
    • Yu, G.1    Zerucha, T.2    Ekker, M.3    Rubenstein, J.L.4
  • 147
    • 0037230155 scopus 로고    scopus 로고
    • The step-wise assembly of a functional nucleolus in preimplantation mouse embryos involves the cajal (coiled) body
    • Zatsepina, O., Baly, C., Chebrout, M., and Debey, P. (2003) The step-wise assembly of a functional nucleolus in preimplantation mouse embryos involves the cajal (coiled) body. Dev. Biol. 253, 66-83.
    • (2003) Dev. Biol. , vol.253 , pp. 66-83
    • Zatsepina, O.1    Baly, C.2    Chebrout, M.3    Debey, P.4
  • 148
    • 0031442806 scopus 로고    scopus 로고
    • Enlightening the postsynaptic density
    • Ziff, E. B. (1997) Enlightening the postsynaptic density. Neuron 19, 1163-1174.
    • (1997) Neuron , vol.19 , pp. 1163-1174
    • Ziff, E.B.1
  • 149
    • 0030746523 scopus 로고    scopus 로고
    • TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling
    • Zinszner, H., Sok, J., Immanuel, D., Yin, Y., and Ron, D. (1997) TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling. J. Cell Sci. 110, 1741-1750.
    • (1997) J. Cell Sci. , vol.110 , pp. 1741-1750
    • Zinszner, H.1    Sok, J.2    Immanuel, D.3    Yin, Y.4    Ron, D.5


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