메뉴 건너뛰기




Volumn 34, Issue 3, 2007, Pages 343-354

The fragile X mental retardation protein-RNP granules show an mGluR-dependent localization in the post-synaptic spines

Author keywords

CaMKII mRNA; BC1 RNA; CPEB; Dendritic mRNA; FMR1 mRNA; Fragile X mental retardation protein; Spines; Staufen

Indexed keywords

CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN; FRAGILE X MENTAL RETARDATION PROTEIN; POSTSYNAPTIC DENSITY PROTEIN 95; PROTEIN DERIVATIVE; PROTEIN KINASE (CALCIUM,CALMODULIN) II; RIBONUCLEOPROTEIN; RNA; SHANK PROTEIN; STAUFEN PROTEIN; UNCLASSIFIED DRUG;

EID: 33847283381     PISSN: 10447431     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mcn.2006.11.015     Document Type: Article
Times cited : (95)

References (68)
  • 2
    • 0032054473 scopus 로고    scopus 로고
    • Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors
    • Allison D.W., Gelfand V.I., Spector I., and Craig A.M. Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors. J. Neurosci. 18 (1998) 2423-2436
    • (1998) J. Neurosci. , vol.18 , pp. 2423-2436
    • Allison, D.W.1    Gelfand, V.I.2    Spector, I.3    Craig, A.M.4
  • 3
    • 1642336232 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor activation regulates fragile X mental retardation protein and FMR1 mRNA localization differentially in dendrites and at synapses
    • Antar L.N., Afroz R., Dictenberg J.B., Carroll R.C., and Bassell G.J. Metabotropic glutamate receptor activation regulates fragile X mental retardation protein and FMR1 mRNA localization differentially in dendrites and at synapses. J. Neurosci. 24 (2004) 2648-2655
    • (2004) J. Neurosci. , vol.24 , pp. 2648-2655
    • Antar, L.N.1    Afroz, R.2    Dictenberg, J.B.3    Carroll, R.C.4    Bassell, G.J.5
  • 4
    • 23944511133 scopus 로고    scopus 로고
    • Localization of FMRP-associated mRNA granules and requirement of microtubules for activity-dependent trafficking in hippocampal neurons
    • Antar L.N., Dictenberg J.B., Plociniak M., Afroz R., and Bassell G.J. Localization of FMRP-associated mRNA granules and requirement of microtubules for activity-dependent trafficking in hippocampal neurons. Genes Brain Behav. 4 (2005) 350-359
    • (2005) Genes Brain Behav. , vol.4 , pp. 350-359
    • Antar, L.N.1    Dictenberg, J.B.2    Plociniak, M.3    Afroz, R.4    Bassell, G.J.5
  • 5
    • 33744966575 scopus 로고    scopus 로고
    • Local functions for FMRP in axon growth cone motility and activity-dependent regulation of filopodia and spine synapses
    • Antar L.N., Li C., Zhang H., Carroll R.C., and Bassell G.J. Local functions for FMRP in axon growth cone motility and activity-dependent regulation of filopodia and spine synapses. Mol. Cell. Neurosci. 32 (2006) 37-48
    • (2006) Mol. Cell. Neurosci. , vol.32 , pp. 37-48
    • Antar, L.N.1    Li, C.2    Zhang, H.3    Carroll, R.C.4    Bassell, G.J.5
  • 6
    • 0036798495 scopus 로고    scopus 로고
    • Visualization of translated tau protein in the axons of neuronal P19 cells and characterization of tau RNP granules
    • Aronov S., Aranda G., Behar L., and Ginzburg I. Visualization of translated tau protein in the axons of neuronal P19 cells and characterization of tau RNP granules. J. Cell Sci. 115 (2002) 3817-3827
    • (2002) J. Cell Sci. , vol.115 , pp. 3817-3827
    • Aronov, S.1    Aranda, G.2    Behar, L.3    Ginzburg, I.4
  • 7
    • 17844372504 scopus 로고    scopus 로고
    • From mRNP trafficking to spine dysmorphogenesis: the roots of fragile X syndrome
    • Bagni C., and Greenough W.T. From mRNP trafficking to spine dysmorphogenesis: the roots of fragile X syndrome. Nat. Rev., Neurosci. 6 (2005) 376-387
    • (2005) Nat. Rev., Neurosci. , vol.6 , pp. 376-387
    • Bagni, C.1    Greenough, W.T.2
  • 9
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder L.I., Frankfurter A., and Rebhun L.I. The distribution of tau in the mammalian central nervous system. J. Cell Biol. 101 (1985) 1371-1378
    • (1985) J. Cell Biol. , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 13
    • 0347382502 scopus 로고    scopus 로고
    • Phosphorylation influences the translation state of FMRP-associated polyribosomes
    • Ceman S., O'Donnell W.T., Reed M., Patton S., Pohl J., and Warren S.T. Phosphorylation influences the translation state of FMRP-associated polyribosomes. Hum. Mol. Genet. 12 (2003) 3295-3305
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3295-3305
    • Ceman, S.1    O'Donnell, W.T.2    Reed, M.3    Patton, S.4    Pohl, J.5    Warren, S.T.6
  • 14
    • 13444279881 scopus 로고    scopus 로고
    • The Abl/Arg substrate ArgBP2/nArgBP2 coordinates the function of multiple regulatory mechanisms converging on the actin cytoskeleton
    • Cestra G., Toomre D., Chang S., and De Camilli P. The Abl/Arg substrate ArgBP2/nArgBP2 coordinates the function of multiple regulatory mechanisms converging on the actin cytoskeleton. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1731-1736
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1731-1736
    • Cestra, G.1    Toomre, D.2    Chang, S.3    De Camilli, P.4
  • 15
    • 24344445896 scopus 로고    scopus 로고
    • Prolonged epileptiform discharges induced by altered group I metabotropic glutamate receptor-mediated synaptic responses in hippocampal slices of a fragile X mouse model
    • Chuang S.C., Zhao W., Bauchwitz R., Yan Q., Bianchi R., and Wong R.K. Prolonged epileptiform discharges induced by altered group I metabotropic glutamate receptor-mediated synaptic responses in hippocampal slices of a fragile X mouse model. J. Neurosci. 25 (2005) 8048-8055
    • (2005) J. Neurosci. , vol.25 , pp. 8048-8055
    • Chuang, S.C.1    Zhao, W.2    Bauchwitz, R.3    Yan, Q.4    Bianchi, R.5    Wong, R.K.6
  • 17
    • 0027176361 scopus 로고
    • The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation
    • Devys D., Lutz Y., Rouyer N., Bellocq J.P., and Mandel J.L. The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation. Nat. Genet. 4 (1993) 335-340
    • (1993) Nat. Genet. , vol.4 , pp. 335-340
    • Devys, D.1    Lutz, Y.2    Rouyer, N.3    Bellocq, J.P.4    Mandel, J.L.5
  • 18
    • 33744516148 scopus 로고    scopus 로고
    • Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP
    • Dolzhanskaya N., Merz G., Aletta J.M., and Denman R.B. Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP. J. Cell Sci. 119 (2006) 1933-1946
    • (2006) J. Cell Sci. , vol.119 , pp. 1933-1946
    • Dolzhanskaya, N.1    Merz, G.2    Aletta, J.M.3    Denman, R.B.4
  • 19
    • 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. Fragile X mental retardation protein: nucleocytoplasmic shuttling and association with somatodendritic ribosomes. J. Neurosci. 17 (1997) 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
  • 20
    • 9344246891 scopus 로고    scopus 로고
    • Visual experience regulates transient expression and dendritic localization of fragile X mental retardation protein
    • Gabel L.A., Won S., Kawai H., McKinney M., Tartakoff A.M., and Fallon J.R. Visual experience regulates transient expression and dendritic localization of fragile X mental retardation protein. J. Neurosci. 24 (2004) 10579-10583
    • (2004) J. Neurosci. , vol.24 , pp. 10579-10583
    • Gabel, L.A.1    Won, S.2    Kawai, H.3    McKinney, M.4    Tartakoff, A.M.5    Fallon, J.R.6
  • 21
    • 2342564387 scopus 로고    scopus 로고
    • The fragile X mental retardation protein has nucleic acid chaperone properties
    • Gabus C., Mazroui R., Tremblay S., Khandjian E.W., and Darlix J.L. The fragile X mental retardation protein has nucleic acid chaperone properties. Nucleic Acids Res. 32 (2004) 2129-2137
    • (2004) Nucleic Acids Res. , vol.32 , pp. 2129-2137
    • Gabus, C.1    Mazroui, R.2    Tremblay, S.3    Khandjian, E.W.4    Darlix, J.L.5
  • 22
    • 32344434917 scopus 로고    scopus 로고
    • A preformed complex of postsynaptic proteins is involved in excitatory synapse development
    • Gerrow K., Romorini S., Nabi S.M., Colicos M.A., Sala C., and El-Husseini A. A preformed complex of postsynaptic proteins is involved in excitatory synapse development. Neuron 49 (2006) 547-562
    • (2006) Neuron , vol.49 , pp. 547-562
    • Gerrow, K.1    Romorini, S.2    Nabi, S.M.3    Colicos, M.A.4    Sala, C.5    El-Husseini, A.6
  • 23
    • 25644434915 scopus 로고    scopus 로고
    • A reduced number of metabotropic glutamate subtype 5 receptors are associated with constitutive homer proteins in a mouse model of fragile X syndrome
    • Giuffrida R., Musumeci S., D'Antoni S., Bonaccorso C.M., Giuffrida-Stella A.M., Oostra B.A., and Catania M.V. A reduced number of metabotropic glutamate subtype 5 receptors are associated with constitutive homer proteins in a mouse model of fragile X syndrome. J. Neurosci. 25 (2005) 8908-8916
    • (2005) J. Neurosci. , vol.25 , pp. 8908-8916
    • Giuffrida, R.1    Musumeci, S.2    D'Antoni, S.3    Bonaccorso, C.M.4    Giuffrida-Stella, A.M.5    Oostra, B.A.6    Catania, M.V.7
  • 24
    • 0346750742 scopus 로고    scopus 로고
    • Microtubule-associated protein 1B function during normal development, regeneration, and pathological conditions in the nervous system
    • Gonzalez-Billault C., Jimenez-Mateos E.M., Caceres A., Diaz-Nido J., Wandosell F., and Avila J. Microtubule-associated protein 1B function during normal development, regeneration, and pathological conditions in the nervous system. J. Neurobiol. 58 (2004) 48-59
    • (2004) J. Neurobiol. , vol.58 , pp. 48-59
    • Gonzalez-Billault, C.1    Jimenez-Mateos, E.M.2    Caceres, A.3    Diaz-Nido, J.4    Wandosell, F.5    Avila, J.6
  • 25
    • 33746892681 scopus 로고    scopus 로고
    • Hippocampal pyramidal cells in adult Fmr1 knockout mice exhibit an immature-appearing profile of dendritic spines
    • Grossman A.W., Elisseou N.M., McKinney B.C., and Greenough W.T. Hippocampal pyramidal cells in adult Fmr1 knockout mice exhibit an immature-appearing profile of dendritic spines. Brain Res. 1084 (2006) 158-164
    • (2006) Brain Res. , vol.1084 , pp. 158-164
    • Grossman, A.W.1    Elisseou, N.M.2    McKinney, B.C.3    Greenough, W.T.4
  • 26
    • 33746866693 scopus 로고    scopus 로고
    • Dynamic translational and proteasomal regulation of fragile X mental retardation protein controls mGluR-dependent long-term depression
    • Hou L., Antion M.D., Hu D., Spencer C.M., Paylor R., and Klann E. Dynamic translational and proteasomal regulation of fragile X mental retardation protein controls mGluR-dependent long-term depression. Neuron 51 (2006) 441-454
    • (2006) Neuron , vol.51 , pp. 441-454
    • Hou, L.1    Antion, M.D.2    Hu, D.3    Spencer, C.M.4    Paylor, R.5    Klann, E.6
  • 27
    • 0036565678 scopus 로고    scopus 로고
    • N-methyl-d-aspartate receptor signaling results in Aurora kinase-catalyzed CPEB phosphorylation and alpha CaMKII mRNA polyadenylation at synapses
    • Huang Y.S., Jung M.Y., Sarkissian M., and Richter J.D. N-methyl-d-aspartate receptor signaling results in Aurora kinase-catalyzed CPEB phosphorylation and alpha CaMKII mRNA polyadenylation at synapses. EMBO J. 21 (2002) 2139-2148
    • (2002) EMBO J. , vol.21 , pp. 2139-2148
    • Huang, Y.S.1    Jung, M.Y.2    Sarkissian, M.3    Richter, J.D.4
  • 30
    • 0033797832 scopus 로고    scopus 로고
    • Dendritic spine structural anomalies in fragile-X mental retardation syndrome
    • Irwin S.A., Galvez R., and Greenough W.T. Dendritic spine structural anomalies in fragile-X mental retardation syndrome. Cereb. Cortex 10 (2000) 1038-1044
    • (2000) Cereb. Cortex , vol.10 , pp. 1038-1044
    • Irwin, S.A.1    Galvez, R.2    Greenough, W.T.3
  • 32
    • 4143088149 scopus 로고    scopus 로고
    • Kinesin transports RNA: isolation and characterization of an RNA-transporting granule
    • Kanai Y., Dohmae N., and Hirokawa N. Kinesin transports RNA: isolation and characterization of an RNA-transporting granule. Neuron 43 (2004) 513-525
    • (2004) Neuron , vol.43 , pp. 513-525
    • Kanai, Y.1    Dohmae, N.2    Hirokawa, N.3
  • 34
    • 0034109216 scopus 로고    scopus 로고
    • Molecular insights into mRNA transport and local translation in the mammalian nervous system
    • Kiebler M.A., and DesGroseillers L. Molecular insights into mRNA transport and local translation in the mammalian nervous system. Neuron 25 (2000) 19-28
    • (2000) Neuron , vol.25 , pp. 19-28
    • Kiebler, M.A.1    DesGroseillers, L.2
  • 35
    • 0036130339 scopus 로고    scopus 로고
    • Candidate RNA-binding proteins regulating extrasomatic mRNA targeting and translation in mammalian neurons
    • Kindler S., and Monshausen M. Candidate RNA-binding proteins regulating extrasomatic mRNA targeting and translation in mammalian neurons. Mol. Neurobiol. 25 (2002) 149-165
    • (2002) Mol. Neurobiol. , vol.25 , pp. 149-165
    • Kindler, S.1    Monshausen, M.2
  • 36
    • 0036257343 scopus 로고    scopus 로고
    • Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction
    • Kioka N., Ueda K., and Amachi T. Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction. Cell Struct. Funct. 27 (2002) 1-7
    • (2002) Cell Struct. Funct. , vol.27 , pp. 1-7
    • Kioka, N.1    Ueda, K.2    Amachi, T.3
  • 37
    • 0034703607 scopus 로고    scopus 로고
    • Neural BC1 RNA associates with pur alpha, a single-stranded DNA and RNA binding protein, which is involved in the transcription of the BC1 RNA gene
    • Kobayashi S., Agui K., Kamo S., Li Y., and Anzai K. Neural BC1 RNA associates with pur alpha, a single-stranded DNA and RNA binding protein, which is involved in the transcription of the BC1 RNA gene. Biochem. Biophys. Res. Commun. 277 (2000) 341-347
    • (2000) Biochem. Biophys. Res. Commun. , vol.277 , pp. 341-347
    • Kobayashi, S.1    Agui, K.2    Kamo, S.3    Li, Y.4    Anzai, K.5
  • 38
    • 0344466778 scopus 로고    scopus 로고
    • Microtubule-dependent recruitment of Staufen-green fluorescent protein into large RNA-containing granules and subsequent dendritic transport in living hippocampal neurons
    • Kohrmann M., Luo M., Kaether C., DesGroseillers L., Dotti C.G., and Kiebler M.A. Microtubule-dependent recruitment of Staufen-green fluorescent protein into large RNA-containing granules and subsequent dendritic transport in living hippocampal neurons. Mol. Biol. Cell 10 (1999) 2945-2953
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2945-2953
    • Kohrmann, M.1    Luo, M.2    Kaether, C.3    DesGroseillers, L.4    Dotti, C.G.5    Kiebler, M.A.6
  • 39
    • 0035923735 scopus 로고    scopus 로고
    • Neuronal RNA granules: a link between RNA localization and stimulation-dependent translation
    • Krichevsky A.M., and Kosik K.S. Neuronal RNA granules: a link between RNA localization and stimulation-dependent translation. Neuron 32 (2001) 683-696
    • (2001) Neuron , vol.32 , pp. 683-696
    • Krichevsky, A.M.1    Kosik, K.S.2
  • 40
  • 41
    • 26844565093 scopus 로고    scopus 로고
    • Age-dependent and selective impairment of long-term potentiation in the anterior piriform cortex of mice lacking the fragile X mental retardation protein
    • Larson J., Jessen R.E., Kim D., Fine A.K., and du Hoffmann J. Age-dependent and selective impairment of long-term potentiation in the anterior piriform cortex of mice lacking the fragile X mental retardation protein. J. Neurosci. 25 (2005) 9460-9469
    • (2005) J. Neurosci. , vol.25 , pp. 9460-9469
    • Larson, J.1    Jessen, R.E.2    Kim, D.3    Fine, A.K.4    du Hoffmann, J.5
  • 42
    • 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. The fragile X mental retardation protein inhibits translation via interacting with mRNA. Nucleic Acids Res. 29 (2001) 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
  • 43
    • 0036198673 scopus 로고    scopus 로고
    • Reduced cortical synaptic plasticity and GluR1 expression associated with fragile X mental retardation protein deficiency
    • Li J., Pelletier M.R., Perez Velazquez J.L., and Carlen P.L. Reduced cortical synaptic plasticity and GluR1 expression associated with fragile X mental retardation protein deficiency. Mol. Cell. Neurosci. 19 (2002) 138-151
    • (2002) Mol. Cell. Neurosci. , vol.19 , pp. 138-151
    • Li, J.1    Pelletier, M.R.2    Perez Velazquez, J.L.3    Carlen, P.L.4
  • 44
    • 6344276563 scopus 로고    scopus 로고
    • The fragile X protein controls microtubule-associated protein 1B translation and microtubule stability in brain neuron development
    • Lu R., Wang H., Liang Z., Ku L., O'Donnell W T., Li W., Warren S.T., and Feng Y. The fragile X protein controls microtubule-associated protein 1B translation and microtubule stability in brain neuron development. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 15201-15206
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 15201-15206
    • Lu, R.1    Wang, H.2    Liang, Z.3    Ku, L.4    O'Donnell W, T.5    Li, W.6    Warren, S.T.7    Feng, Y.8
  • 45
    • 0037112805 scopus 로고    scopus 로고
    • Trapping of messenger RNA by Fragile X Mental Retardation protein into cytoplasmic granules induces translation repression
    • Mazroui R., Hout M.E., Tremblay S., Filion C., Labelle Y., and Khandjian E.W. Trapping of messenger RNA by Fragile X Mental Retardation protein into cytoplasmic granules induces translation repression. Hum. Mol. Genet. 11 (2002) 3007-3017
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 3007-3017
    • Mazroui, R.1    Hout, M.E.2    Tremblay, S.3    Filion, C.4    Labelle, Y.5    Khandjian, E.W.6
  • 48
    • 0033785413 scopus 로고    scopus 로고
    • The single-stranded DNA- and RNA-binding proteins pur alpha and pur beta link BC1 RNA to microtubules through binding to the dendrite-targeting RNA motifs
    • Ohashi S., Kobayashi S., Omori A., Ohara S., Omae A., Muramatsu T., Li Y., and Anzai K. The single-stranded DNA- and RNA-binding proteins pur alpha and pur beta link BC1 RNA to microtubules through binding to the dendrite-targeting RNA motifs. J. Neurochem. 75 (2000) 1781-1790
    • (2000) J. Neurochem. , vol.75 , pp. 1781-1790
    • Ohashi, S.1    Kobayashi, S.2    Omori, A.3    Ohara, S.4    Omae, A.5    Muramatsu, T.6    Li, Y.7    Anzai, K.8
  • 49
    • 0037020098 scopus 로고    scopus 로고
    • Identification of mRNA/protein (mRNP) complexes containing Puralpha, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motor
    • Ohashi S., Koike K., Omori A., Ichinose S., Ohara S., Kobayashi S., Sato T.A., and Anzai K. Identification of mRNA/protein (mRNP) complexes containing Puralpha, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motor. J. Biol. Chem. 277 (2002) 37804-37810
    • (2002) J. Biol. Chem. , vol.277 , pp. 37804-37810
    • Ohashi, S.1    Koike, K.2    Omori, A.3    Ichinose, S.4    Ohara, S.5    Kobayashi, S.6    Sato, T.A.7    Anzai, K.8
  • 50
    • 20544468497 scopus 로고    scopus 로고
    • The Drosophila fragile X mental retardation protein controls actin dynamics by directly regulating profilin in the brain
    • Reeve S.P., Bassetto L., Genova G.K., Kleyner Y., Leyssen M., Jackson F.R., and Hassan B.A. The Drosophila fragile X mental retardation protein controls actin dynamics by directly regulating profilin in the brain. Curr. Biol. 15 (2005) 1156-1163
    • (2005) Curr. Biol. , vol.15 , pp. 1156-1163
    • Reeve, S.P.1    Bassetto, L.2    Genova, G.K.3    Kleyner, Y.4    Leyssen, M.5    Jackson, F.R.6    Hassan, B.A.7
  • 52
    • 0035801393 scopus 로고    scopus 로고
    • The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif
    • Schaeffer C., Bardoni B., Mandel J.L., Ehresmann B., Ehresmann C., and Moine H. The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif. Embo J. 20 (2001) 4803-4813
    • (2001) Embo J. , vol.20 , pp. 4803-4813
    • Schaeffer, C.1    Bardoni, B.2    Mandel, J.L.3    Ehresmann, B.4    Ehresmann, C.5    Moine, H.6
  • 53
    • 7044260537 scopus 로고    scopus 로고
    • Rapid, activity-induced increase in tissue plasminogen activator is mediated by metabotropic glutamate receptor-dependent mRNA translation
    • Shin C.Y., Kundel M., and Wells D.G. Rapid, activity-induced increase in tissue plasminogen activator is mediated by metabotropic glutamate receptor-dependent mRNA translation. J. Neurosci. 24 (2004) 9425-9433
    • (2004) J. Neurosci. , vol.24 , pp. 9425-9433
    • Shin, C.Y.1    Kundel, M.2    Wells, D.G.3
  • 54
    • 33745588863 scopus 로고    scopus 로고
    • Exaggerated behavioral phenotypes in Fmr1/Fxr2 double knockout mice reveal a functional genetic interaction between fragile X-related proteins
    • Spencer C.M., Serysheva E., Yuva-Paylor L.A., Oostra B.A., Nelson D.L., and Paylor R. Exaggerated behavioral phenotypes in Fmr1/Fxr2 double knockout mice reveal a functional genetic interaction between fragile X-related proteins. Hum. Mol. Genet. 15 (2006) 1984-1994
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1984-1994
    • Spencer, C.M.1    Serysheva, E.2    Yuva-Paylor, L.A.3    Oostra, B.A.4    Nelson, D.L.5    Paylor, R.6
  • 55
    • 29644436341 scopus 로고    scopus 로고
    • Identification and characterization of the methyl arginines in the fragile X mental retardation protein Fmrp
    • Stetler A., Winograd C., Sayegh J., Cheever A., Patton E., Zhang X., Clarke S., and Ceman S. Identification and characterization of the methyl arginines in the fragile X mental retardation protein Fmrp. Hum. Mol. Genet. 15 (2006) 87-96
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 87-96
    • Stetler, A.1    Winograd, C.2    Sayegh, J.3    Cheever, A.4    Patton, E.5    Zhang, X.6    Clarke, S.7    Ceman, S.8
  • 56
    • 0141918785 scopus 로고    scopus 로고
    • Compartmentalized synthesis and degradation of proteins in neurons
    • Steward O., and Schuman E.M. Compartmentalized synthesis and degradation of proteins in neurons. Neuron 40 (2003) 347-359
    • (2003) Neuron , vol.40 , pp. 347-359
    • Steward, O.1    Schuman, E.M.2
  • 59
    • 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. A role for a rat homolog of Staufen in the transport of RNA to neuronal dendrites. Neuron 32 (2001) 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
  • 60
    • 0345492360 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is required for type-I metabotropic glutamate receptor-dependent translation of PSD-95
    • Todd P.K., Mack K.J., and Malter J.S. The fragile X mental retardation protein is required for type-I metabotropic glutamate receptor-dependent translation of PSD-95. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 14374-14378
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 14374-14378
    • Todd, P.K.1    Mack, K.J.2    Malter, J.S.3
  • 61
    • 2342487399 scopus 로고    scopus 로고
    • The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs
    • Villace P., Marion R.M., and Ortin J. The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs. Nucleic Acids Res. 32 (2004) 2411-2420
    • (2004) Nucleic Acids Res. , vol.32 , pp. 2411-2420
    • Villace, P.1    Marion, R.M.2    Ortin, J.3
  • 65
    • 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. CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of alpha-CaMKII mRNA at synapses. Neuron 21 (1998) 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
  • 66
    • 0037423293 scopus 로고    scopus 로고
    • The fragile X syndrome protein FMRP associates with BC1 RNA and regulates the translation of specific mRNAs at synapses
    • Zalfa F., Giorgi M., Primerano B., Moro A., Di Penta A., Reis S., Oostra B., and Bagni C. The fragile X syndrome protein FMRP associates with BC1 RNA and regulates the translation of specific mRNAs at synapses. Cell 112 (2003) 317-327
    • (2003) Cell , vol.112 , pp. 317-327
    • Zalfa, F.1    Giorgi, M.2    Primerano, B.3    Moro, A.4    Di Penta, A.5    Reis, S.6    Oostra, B.7    Bagni, C.8
  • 67
    • 25844513780 scopus 로고    scopus 로고
    • Fragile X mental retardation protein (FMRP) binds specifically to the brain cytoplasmic RNAs BC1/BC200 via a novel RNA-binding motif
    • Zalfa F., Adinolfi S., Napoli I., Kuhn-Holsken E., Urlaub H., Achsel T., Pastore A., and Bagni C. Fragile X mental retardation protein (FMRP) binds specifically to the brain cytoplasmic RNAs BC1/BC200 via a novel RNA-binding motif. J. Biol. Chem. 280 (2005) 33403-33410
    • (2005) J. Biol. Chem. , vol.280 , pp. 33403-33410
    • Zalfa, F.1    Adinolfi, S.2    Napoli, I.3    Kuhn-Holsken, E.4    Urlaub, H.5    Achsel, T.6    Pastore, A.7    Bagni, C.8
  • 68
    • 23744492534 scopus 로고    scopus 로고
    • Deficits in trace fear memory and long-term potentiation in a mouse model for fragile X syndrome
    • Zhao M.G., Toyoda H., Ko S.W., Ding H.K., Wu L.J., and Zhuo M. Deficits in trace fear memory and long-term potentiation in a mouse model for fragile X syndrome. J. Neurosci. 25 (2005) 7385-7392
    • (2005) J. Neurosci. , vol.25 , pp. 7385-7392
    • Zhao, M.G.1    Toyoda, H.2    Ko, S.W.3    Ding, H.K.4    Wu, L.J.5    Zhuo, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.