메뉴 건너뛰기




Volumn 8, Issue 3, 2013, Pages

Fmr1 Transcript Isoforms: Association with Polyribosomes; Regional and Developmental Expression in Mouse Brain

Author keywords

[No Author keywords available]

Indexed keywords

FRAGILE X MENTAL RETARDATION 1 PROTEIN; MEMBRANE PROTEIN; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84874695859     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0058296     Document Type: Article
Times cited : (43)

References (59)
  • 1
    • 23944473342 scopus 로고    scopus 로고
    • Structural and functional diversity generated by alternative mRNA splicing
    • Stetefeld J, Ruegg MA, (2005) Structural and functional diversity generated by alternative mRNA splicing. Trends Biochem Sci 30: 515-521.
    • (2005) Trends Biochem Sci , vol.30 , pp. 515-521
    • Stetefeld, J.1    Ruegg, M.A.2
  • 2
    • 20444368053 scopus 로고    scopus 로고
    • Neuronal proteins custom designed by alternative splicing
    • Lipscombe D, (2005) Neuronal proteins custom designed by alternative splicing. Curr Opin Neurobiol 15: 358-363.
    • (2005) Curr Opin Neurobiol , vol.15 , pp. 358-363
    • Lipscombe, D.1
  • 3
    • 8544273283 scopus 로고    scopus 로고
    • Expression of alternatively spliced sodium channel alpha-subunit genes. Unique splicing patterns are observed in dorsal root ganglia
    • Raymond CK, Castle J, Garrett-Engele P, Armour CD, Kan Z, et al. (2004) Expression of alternatively spliced sodium channel alpha-subunit genes. Unique splicing patterns are observed in dorsal root ganglia. J Biol Chem 279: 46234-46241.
    • (2004) J Biol Chem , vol.279 , pp. 46234-46241
    • Raymond, C.K.1    Castle, J.2    Garrett-Engele, P.3    Armour, C.D.4    Kan, Z.5
  • 4
    • 32344440041 scopus 로고    scopus 로고
    • RNA binding proteins and the regulation of neuronal synaptic plasticity
    • Ule J, Darnell RB, (2006) RNA binding proteins and the regulation of neuronal synaptic plasticity. Curr Opin Neurobiol 16: 102-110.
    • (2006) Curr Opin Neurobiol , vol.16 , pp. 102-110
    • Ule, J.1    Darnell, R.B.2
  • 5
    • 0036703649 scopus 로고    scopus 로고
    • Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms
    • Chetkovich DM, Bunn RC, Kuo SH, Kawasaki Y, Kohwi M, et al. (2002) Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms. J Neurosci 22: 6415-6425.
    • (2002) J Neurosci , vol.22 , pp. 6415-6425
    • Chetkovich, D.M.1    Bunn, R.C.2    Kuo, S.H.3    Kawasaki, Y.4    Kohwi, M.5
  • 6
    • 0038794104 scopus 로고    scopus 로고
    • Synapse-associated protein-97 isoform-specific regulation of surface AMPA receptors and synaptic function in cultured neurons
    • Rumbaugh G, Sia GM, Garner CC, Huganir RL, (2003) Synapse-associated protein-97 isoform-specific regulation of surface AMPA receptors and synaptic function in cultured neurons. J Neurosci 23: 4567-4576.
    • (2003) J Neurosci , vol.23 , pp. 4567-4576
    • Rumbaugh, G.1    Sia, G.M.2    Garner, C.C.3    Huganir, R.L.4
  • 7
    • 33748924690 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors
    • Ferraguti F, Shigemoto R, (2006) Metabotropic glutamate receptors. Cell Tissue Res 326: 483-504.
    • (2006) Cell Tissue Res , vol.326 , pp. 483-504
    • Ferraguti, F.1    Shigemoto, R.2
  • 8
    • 33847198227 scopus 로고    scopus 로고
    • Alternative splicing controls G protein-dependent inhibition of N-type calcium channels in nociceptors
    • Raingo J, Castiglioni AJ, Lipscombe D, (2007) Alternative splicing controls G protein-dependent inhibition of N-type calcium channels in nociceptors. Nat Neurosci 10: 285-292.
    • (2007) Nat Neurosci , vol.10 , pp. 285-292
    • Raingo, J.1    Castiglioni, A.J.2    Lipscombe, D.3
  • 12
    • 0030051618 scopus 로고    scopus 로고
    • Alternative splicing of exon 14 determines nuclear or cytoplasmic localisation of FMR1 protein isoforms
    • Sittler A, Devys D, Weber C, Mandel JL, (1996) Alternative splicing of exon 14 determines nuclear or cytoplasmic localisation of FMR1 protein isoforms. Hum Mol Genet 5: 95-102.
    • (1996) Hum Mol Genet , vol.5 , pp. 95-102
    • Sittler, A.1    Devys, D.2    Weber, C.3    Mandel, J.L.4
  • 13
    • 33748664178 scopus 로고    scopus 로고
    • Alternative splicing modulates protein arginine methyltransferase-dependent methylation of fragile X syndrome mental retardation protein
    • Dolzhanskaya N, Merz G, Denman RB, (2006) Alternative splicing modulates protein arginine methyltransferase-dependent methylation of fragile X syndrome mental retardation protein. Biochemistry 45: 10385-10393.
    • (2006) Biochemistry , vol.45 , pp. 10385-10393
    • Dolzhanskaya, N.1    Merz, G.2    Denman, R.B.3
  • 14
    • 4043055114 scopus 로고    scopus 로고
    • Regulating a translational regulator: mechanisms cells use to control the activity of the fragile X mental retardation protein
    • Denman RB, Dolzhanskaya N, Sung YJ, (2004) Regulating a translational regulator: mechanisms cells use to control the activity of the fragile X mental retardation protein. Cell Mol Life Sci 61: 1714-1728.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1714-1728
    • Denman, R.B.1    Dolzhanskaya, N.2    Sung, Y.J.3
  • 15
    • 0032546976 scopus 로고    scopus 로고
    • Purified recombinant FMRP exhibits selective RNA binding as an intrinsic property of the fragile X mental retardation protein
    • Brown V, Small K, Lakkis L, Feng Y, Gunter C, et al. (1998) Purified recombinant FMRP exhibits selective RNA binding as an intrinsic property of the fragile X mental retardation protein. J Biol Chem 273: 15521-15527.
    • (1998) J Biol Chem , vol.273 , pp. 15521-15527
    • Brown, V.1    Small, K.2    Lakkis, L.3    Feng, Y.4    Gunter, C.5
  • 16
    • 0027327486 scopus 로고
    • The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein
    • Siomi H, Siomi MC, Nussbaum RL, Dreyfuss G, (1993) The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein. Cell 74: 291-298.
    • (1993) Cell , vol.74 , pp. 291-298
    • Siomi, H.1    Siomi, M.C.2    Nussbaum, R.L.3    Dreyfuss, G.4
  • 17
    • 0029816723 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals
    • Eberhart DE, Malter HE, Feng Y, Warren ST, (1996) The fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals. Hum Mol Genet 5: 1083-1091.
    • (1996) Hum Mol Genet , vol.5 , pp. 1083-1091
    • Eberhart, D.E.1    Malter, H.E.2    Feng, Y.3    Warren, S.T.4
  • 18
    • 0347382502 scopus 로고    scopus 로고
    • Phosphorylation influences the translation state of FMRP-associated polyribosomes
    • Ceman S, O'Donnell WT, Reed M, Patton S, Pohl J, et al. (2003) Phosphorylation influences the translation state of FMRP-associated polyribosomes. Hum Mol Genet 12: 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
  • 19
    • 49749153117 scopus 로고    scopus 로고
    • Chemical and structural probing of the N-terminal residues encoded by FMR1 exon 15 and their effect on downstream arginine methylation
    • Dolzhanskaya N, Bolton DC, Denman RB, (2008) Chemical and structural probing of the N-terminal residues encoded by FMR1 exon 15 and their effect on downstream arginine methylation. Biochemistry 47: 8491-8503.
    • (2008) Biochemistry , vol.47 , pp. 8491-8503
    • Dolzhanskaya, N.1    Bolton, D.C.2    Denman, R.B.3
  • 20
    • 34548430484 scopus 로고    scopus 로고
    • Fragile X Mental Retardation Syndrome: Structure of the KH1-KH2 Domains of Fragile X Mental Retardation Protein
    • Valverde R, Pozdnyakova I, Kajander T, Venkatraman J, Regan L, (2007) Fragile X Mental Retardation Syndrome: Structure of the KH1-KH2 Domains of Fragile X Mental Retardation Protein. Structure 15: 1090-1098.
    • (2007) Structure , vol.15 , pp. 1090-1098
    • Valverde, R.1    Pozdnyakova, I.2    Kajander, T.3    Venkatraman, J.4    Regan, L.5
  • 21
    • 17444384228 scopus 로고    scopus 로고
    • Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes
    • Darnell JC, Fraser CE, Mostovetsky O, Stefani G, Jones TA, et al. (2005) Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes. Genes Dev 19: 903-918.
    • (2005) Genes Dev , vol.19 , pp. 903-918
    • Darnell, J.C.1    Fraser, C.E.2    Mostovetsky, O.3    Stefani, G.4    Jones, T.A.5
  • 22
    • 43549124851 scopus 로고    scopus 로고
    • Structure and function of KH domains
    • Valverde R, Edwards L, Regan L, (2008) Structure and function of KH domains. FEBS J (275) (): 2712-2726.
    • (2008) FEBS , vol.J , Issue.275 , pp. 2712-2726
    • Valverde, R.1    Edwards, L.2    Regan, L.3
  • 23
    • 68749103452 scopus 로고    scopus 로고
    • Discrimination of common and unique RNA-binding activities among Fragile X mental retardation protein paralogs
    • Darnell JC, Fraser CE, Mostovetsky O, Darnell RB, (2009) Discrimination of common and unique RNA-binding activities among Fragile X mental retardation protein paralogs. Hum Mol Genet 18: 3164-3177.
    • (2009) Hum Mol Genet , vol.18 , pp. 3164-3177
    • Darnell, J.C.1    Fraser, C.E.2    Mostovetsky, O.3    Darnell, R.B.4
  • 24
    • 67349246221 scopus 로고    scopus 로고
    • Tissue and developmental regulation of fragile X mental retardation 1 Exon 12 and 15 isoforms
    • Xie W, Dolzhanskaya N, Lafauci G, Dobkin C, Denman RB, (2009) Tissue and developmental regulation of fragile X mental retardation 1 Exon 12 and 15 isoforms. Neurobiol Dis 35: 52-62.
    • (2009) Neurobiol Dis , vol.35 , pp. 52-62
    • Xie, W.1    Dolzhanskaya, N.2    Lafauci, G.3    Dobkin, C.4    Denman, R.B.5
  • 25
    • 0035900649 scopus 로고    scopus 로고
    • Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function
    • Darnell JC, Jensen KB, Jin P, Brown V, Warren ST, et al. (2001) Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function. Cell 107: 489-499.
    • (2001) Cell , vol.107 , pp. 489-499
    • Darnell, J.C.1    Jensen, K.B.2    Jin, P.3    Brown, V.4    Warren, S.T.5
  • 27
    • 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 JP, Mandel JL, (1993) The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation. Nat Genet 4: 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
  • 28
    • 3142615272 scopus 로고    scopus 로고
    • Validation of housekeeping genes for normalizing RNA expression in real-time PCR
    • Dheda K, Huggett JF, Bustin SA, Johnson MA, Rook G, et al. (2004) Validation of housekeeping genes for normalizing RNA expression in real-time PCR. Biotechniques 37: 112-119.
    • (2004) Biotechniques , vol.37 , pp. 112-119
    • Dheda, K.1    Huggett, J.F.2    Bustin, S.A.3    Johnson, M.A.4    Rook, G.5
  • 29
    • 33847650029 scopus 로고    scopus 로고
    • Usefulness of the 5′ region of the cDNA encoding acidic ribosomal phosphoprotein P0 conserved among rats, mice, and humans as a standard probe for gene expression analysis in different tissues and animal species
    • Akamine R, Yamamoto T, Watanabe M, Yamazaki N, Kataoka M, et al. (2007) Usefulness of the 5′ region of the cDNA encoding acidic ribosomal phosphoprotein P0 conserved among rats, mice, and humans as a standard probe for gene expression analysis in different tissues and animal species. J Biochem Biophys Methods 70: 481-486.
    • (2007) J Biochem Biophys Methods , vol.70 , pp. 481-486
    • Akamine, R.1    Yamamoto, T.2    Watanabe, M.3    Yamazaki, N.4    Kataoka, M.5
  • 30
    • 0027265596 scopus 로고
    • Human and murine FMR-1: alternative splicing and translational initiation downstream of the CGG-repeat
    • Ashley CT, Sutcliffe JS, Kunst CB, Leiner HA, Eichler EE, et al. (1993) Human and murine FMR-1: alternative splicing and translational initiation downstream of the CGG-repeat. Nat Genet 4: 244-251.
    • (1993) Nat Genet , vol.4 , pp. 244-251
    • Ashley, C.T.1    Sutcliffe, J.S.2    Kunst, C.B.3    Leiner, H.A.4    Eichler, E.E.5
  • 31
    • 0003020465 scopus 로고    scopus 로고
    • Analysis of ribosome loading onto mRNA species: implications for translational control
    • In: Richter JD, editors. New York: Academic Press
    • Ruan HJ, Brown CY, Morris DR (1997) Analysis of ribosome loading onto mRNA species: implications for translational control. In: Richter JD, editors. Analysis of mRNA formation and function. New York: Academic Press. 305-321.
    • (1997) Analysis of mRNA formation and function , pp. 305-321
    • Ruan, H.J.1    Brown, C.Y.2    Morris, D.R.3
  • 32
    • 14944342993 scopus 로고    scopus 로고
    • Isotropic fractionator: a simple, rapid method for the quantification of total cell and neuron numbers in the brain
    • Herculano-Houzel S, Lent R, (2005) Isotropic fractionator: a simple, rapid method for the quantification of total cell and neuron numbers in the brain. J Neurosci 25: 2518-2521.
    • (2005) J Neurosci , vol.25 , pp. 2518-2521
    • Herculano-Houzel, S.1    Lent, R.2
  • 34
    • 64549116740 scopus 로고    scopus 로고
    • Equal numbers of neuronal and nonneuronal cells make the human brain an isometrically scaled-up primate brain
    • Azevedo FA, Carvalho LR, Grinberg LT, Farfel JM, Ferretti RE, et al. (2009) Equal numbers of neuronal and nonneuronal cells make the human brain an isometrically scaled-up primate brain. J Comp Neurol 513: 532-541.
    • (2009) J Comp Neurol , vol.513 , pp. 532-541
    • Azevedo, F.A.1    Carvalho, L.R.2    Grinberg, L.T.3    Farfel, J.M.4    Ferretti, R.E.5
  • 35
    • 35048886071 scopus 로고    scopus 로고
    • Developmental expression of FMRP in the astrocyte lineage: Implications for fragile X syndrome
    • Pacey LK, Doering LC, (2007) Developmental expression of FMRP in the astrocyte lineage: Implications for fragile X syndrome. Glia 55: 1601-1609.
    • (2007) Glia , vol.55 , pp. 1601-1609
    • Pacey, L.K.1    Doering, L.C.2
  • 36
    • 77957922784 scopus 로고    scopus 로고
    • Fragile X astrocytes induce developmental delays in dendrite maturation and synaptic protein expression
    • Jacobs S, Nathwani M, Doering LC, (2010) Fragile X astrocytes induce developmental delays in dendrite maturation and synaptic protein expression. BMC Neurosci 11: 132.
    • (2010) BMC Neurosci , vol.11 , pp. 132
    • Jacobs, S.1    Nathwani, M.2    Doering, L.C.3
  • 37
    • 77949835797 scopus 로고    scopus 로고
    • Astrocytes prevent abnormal neuronal development in the fragile x mouse
    • Jacobs S, Doering LC, (2010) Astrocytes prevent abnormal neuronal development in the fragile x mouse. J Neurosci 30: 4508-4514.
    • (2010) J Neurosci , vol.30 , pp. 4508-4514
    • Jacobs, S.1    Doering, L.C.2
  • 38
    • 84872027700 scopus 로고    scopus 로고
    • Excessive astrocyte-derived neurotrophin-3 contributes to the abnormal neuronal dendritic development in a mouse model of fragile x syndrome
    • Yang Q, Feng B, Zhang K, Guo YY, Liu SB, et al. (2012) Excessive astrocyte-derived neurotrophin-3 contributes to the abnormal neuronal dendritic development in a mouse model of fragile x syndrome. PLoS Genet 8: e1003172.
    • (2012) PLoS Genet , vol.8
    • Yang, Q.1    Feng, B.2    Zhang, K.3    Guo, Y.Y.4    Liu, S.B.5
  • 39
    • 69549113277 scopus 로고    scopus 로고
    • Cell-type-specific isolation of ribosome-associated mRNA from complex tissues
    • Sanz E, Yang L, Su T, Morris DR, McKnight GS, et al. (2009) Cell-type-specific isolation of ribosome-associated mRNA from complex tissues. Proc Natl Acad Sci U S A 106: 13939-13944.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13939-13944
    • Sanz, E.1    Yang, L.2    Su, T.3    Morris, D.R.4    McKnight, G.S.5
  • 40
    • 0034701295 scopus 로고    scopus 로고
    • Nuclear targeting defect of SMN lacking the C-terminus in a mouse model of spinal muscular atrophy
    • Frugier T, Tiziano FD, Cifuentes-Diaz C, Miniou P, Roblot N, et al. (2000) Nuclear targeting defect of SMN lacking the C-terminus in a mouse model of spinal muscular atrophy. Hum Mol Genet 9: 849-858.
    • (2000) Hum Mol Genet , vol.9 , pp. 849-858
    • Frugier, T.1    Tiziano, F.D.2    Cifuentes-Diaz, C.3    Miniou, P.4    Roblot, N.5
  • 41
    • 0027397928 scopus 로고
    • Tissue specific expression of FMR-1 provides evidence for a functional role in fragile X syndrome
    • Hinds HL, Ashley CT, Sutcliffe JS, Nelson DL, Warren ST, et al. (1993) Tissue specific expression of FMR-1 provides evidence for a functional role in fragile X syndrome. Nat Genet 3: 36-43.
    • (1993) Nat Genet , vol.3 , pp. 36-43
    • Hinds, H.L.1    Ashley, C.T.2    Sutcliffe, J.S.3    Nelson, D.L.4    Warren, S.T.5
  • 43
    • 33750475626 scopus 로고    scopus 로고
    • Quantitative real-time RT-PCR data analysis: current concepts and the novel "gene expression's CT difference" formula
    • Schefe JH, Lehmann KE, Buschmann IR, Unger T, Funke-Kaiser H, (2006) Quantitative real-time RT-PCR data analysis: current concepts and the novel "gene expression's CT difference" formula. J Mol Med (Berl) 84: 901-910.
    • (2006) J Mol Med (Berl) , vol.84 , pp. 901-910
    • Schefe, J.H.1    Lehmann, K.E.2    Buschmann, I.R.3    Unger, T.4    Funke-Kaiser, H.5
  • 44
    • 33750961666 scopus 로고    scopus 로고
    • [Real-time PCR: approaches to data analysis (a review)]
    • Rebrikov DV, Trofimov DI, (2006) [Real-time PCR: approaches to data analysis (a review)]. Prikl Biokhim Mikrobiol 42: 520-528.
    • (2006) Prikl Biokhim Mikrobiol , vol.42 , pp. 520-528
    • Rebrikov, D.V.1    Trofimov, D.I.2
  • 45
    • 2642566765 scopus 로고    scopus 로고
    • Gene expression analyzed by high-resolution state array analysis and quantitative proteomics: response of yeast to mating pheromone
    • MacKay VL, Li X, Flory MR, Turcott E, Law GL, et al. (2004) Gene expression analyzed by high-resolution state array analysis and quantitative proteomics: response of yeast to mating pheromone. Mol Cell Proteomics 3: 478-489.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 478-489
    • MacKay, V.L.1    Li, X.2    Flory, M.R.3    Turcott, E.4    Law, G.L.5
  • 46
    • 23244458855 scopus 로고    scopus 로고
    • Adult neurogenesis in the mammalian central nervous system
    • Ming GL, Song H, (2005) Adult neurogenesis in the mammalian central nervous system. Annu Rev Neurosci 28 223-50: 223-250.
    • (2005) Annu Rev Neurosci , vol.28 , pp. 223-250
    • Ming, G.L.1    Song, H.2
  • 47
    • 13844264520 scopus 로고    scopus 로고
    • Young and excitable: the function of new neurons in the adult mammalian brain
    • Doetsch F, Hen R, (2005) Young and excitable: the function of new neurons in the adult mammalian brain. Curr Opin Neurobiol 15: 121-128.
    • (2005) Curr Opin Neurobiol , vol.15 , pp. 121-128
    • Doetsch, F.1    Hen, R.2
  • 49
    • 0036892046 scopus 로고    scopus 로고
    • Casein kinase II phosphorylates the fragile X mental retardation protein and modulates its biological properties
    • Siomi MC, Higashijima K, Ishizuka A, Siomi H, (2002) Casein kinase II phosphorylates the fragile X mental retardation protein and modulates its biological properties. Mol Cell Biol 22: 8438-8447.
    • (2002) Mol Cell Biol , vol.22 , pp. 8438-8447
    • Siomi, M.C.1    Higashijima, K.2    Ishizuka, A.3    Siomi, H.4
  • 50
    • 10644270727 scopus 로고    scopus 로고
    • Fragile X mental retardation protein is necessary for neurotransmitter-activated protein translation at synapses
    • Weiler IJ, Spangler CC, Klintsova AY, Grossman AW, Kim SH, et al. (2004) Fragile X mental retardation protein is necessary for neurotransmitter-activated protein translation at synapses. Proc Natl Acad Sci U S A 101: 17504-17509.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17504-17509
    • Weiler, I.J.1    Spangler, C.C.2    Klintsova, A.Y.3    Grossman, A.W.4    Kim, S.H.5
  • 51
    • 4444238669 scopus 로고    scopus 로고
    • Biochemical evidence for the association of fragile X mental retardation protein with brain polyribosomal ribonucleoparticles
    • Khandjian EW, Huot ME, Tremblay S, Davidovic L, Mazroui R, et al. (2004) Biochemical evidence for the association of fragile X mental retardation protein with brain polyribosomal ribonucleoparticles. Proc Natl Acad Sci U S A 101: 13357-13362.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 13357-13362
    • Khandjian, E.W.1    Huot, M.E.2    Tremblay, S.3    Davidovic, L.4    Mazroui, R.5
  • 52
    • 7244224871 scopus 로고    scopus 로고
    • Fragile X mental retardation protein is associated with translating polyribosomes in neuronal cells
    • Stefani G, Fraser CE, Darnell JC, Darnell RB, (2004) Fragile X mental retardation protein is associated with translating polyribosomes in neuronal cells. J Neurosci 24: 7272-7276.
    • (2004) J Neurosci , vol.24 , pp. 7272-7276
    • Stefani, G.1    Fraser, C.E.2    Darnell, J.C.3    Darnell, R.B.4
  • 54
    • 23944520830 scopus 로고    scopus 로고
    • Differential translation and fragile X syndrome
    • Vanderklish PW, Edelman GM, (2005) Differential translation and fragile X syndrome. Genes Brain Behav 4: 360-384.
    • (2005) Genes Brain Behav , vol.4 , pp. 360-384
    • Vanderklish, P.W.1    Edelman, G.M.2
  • 55
    • 33646194363 scopus 로고    scopus 로고
    • Metabotropic receptor-dependent long-term depression persists in the absence of protein synthesis in the mouse model of fragile X syndrome
    • Nosyreva ED, Huber KM, (2006) Metabotropic receptor-dependent long-term depression persists in the absence of protein synthesis in the mouse model of fragile X syndrome. J Neurophysiol 95: 3291-3295.
    • (2006) J Neurophysiol , vol.95 , pp. 3291-3295
    • Nosyreva, E.D.1    Huber, K.M.2
  • 56
    • 3042647610 scopus 로고    scopus 로고
    • The mGluR theory of fragile X mental retardation
    • Bear MF, Huber KM, Warren ST, (2004) The mGluR theory of fragile X mental retardation. Trends Neurosci 27: 370-377.
    • (2004) Trends Neurosci , vol.27 , pp. 370-377
    • Bear, M.F.1    Huber, K.M.2    Warren, S.T.3
  • 57
    • 36749011299 scopus 로고    scopus 로고
    • Adult spinal cord progenitor cells are repelled by netrin-1 in the embryonic and injured adult spinal cord
    • Petit A, Sellers DL, Liebl DJ, Tessier-Lavigne M, Kennedy TE, et al. (2007) Adult spinal cord progenitor cells are repelled by netrin-1 in the embryonic and injured adult spinal cord. Proc Natl Acad Sci U S A 104: 17837-17842.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 17837-17842
    • Petit, A.1    Sellers, D.L.2    Liebl, D.J.3    Tessier-Lavigne, M.4    Kennedy, T.E.5
  • 58
    • 85010247792 scopus 로고
    • Cerebral protein synthesis. I. Physical properties of cerebral ribosomes and polyribosomes
    • Zomzely CE, Roberts S, Brown DM, Provost C, (1966) Cerebral protein synthesis. I. Physical properties of cerebral ribosomes and polyribosomes. J Mol Biol 19: 455-468.
    • (1966) J Mol Biol , vol.19 , pp. 455-468
    • Zomzely, C.E.1    Roberts, S.2    Brown, D.M.3    Provost, C.4
  • 59
    • 0014430120 scopus 로고
    • Cerebral protein synthesis. II. Instability of cerebral messenger ribonucleic acid-ribosome complexes
    • Zomzely CE, Roberts S, Gruber CP, Brown DM, (1968) Cerebral protein synthesis. II. Instability of cerebral messenger ribonucleic acid-ribosome complexes. J Biol Chem 243: 5396-5409.
    • (1968) J Biol Chem , vol.243 , pp. 5396-5409
    • Zomzely, C.E.1    Roberts, S.2    Gruber, C.P.3    Brown, D.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.