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Volumn 18, Issue 17, 2009, Pages 3164-3177

Discrimination of common and unique RNA-binding activities among Fragile X mental retardation protein paralogs

Author keywords

[No Author keywords available]

Indexed keywords

FRAGILE X MENTAL RETARDATION PROTEIN; FRAGILE X MENTAL RETARDATION PROTEIN 1; FRAGILE X MENTAL RETARDATION PROTEIN 2; FRAGILE X MENTAL RETARDATION PROTEIN 2 KH2; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 68749103452     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddp255     Document Type: Article
Times cited : (90)

References (85)
  • 1
    • 53849110899 scopus 로고    scopus 로고
    • Fragile X syndrome: Loss of local mRNA regulation alters synaptic development and function
    • Bassell, G.J. and Warren, S.T. (2008) Fragile X syndrome: Loss of local mRNA regulation alters synaptic development and function. Neuron, 60, 201-214.
    • (2008) Neuron , vol.60 , pp. 201-214
    • Bassell, G.J.1    Warren, S.T.2
  • 2
    • 0027260844 scopus 로고
    • KH domains within the FMR1 sequence suggest that fragile X syndrome stems from a defect in RNA metabolism
    • Gibson, T.J., Rice, P.M., Thompson, J.D. and Heringa, J. (1993) KH domains within the FMR1 sequence suggest that fragile X syndrome stems from a defect in RNA metabolism. Trends Biochem. Sci., 18, 331-333.
    • (1993) Trends Biochem. Sci , vol.18 , pp. 331-333
    • Gibson, T.J.1    Rice, P.M.2    Thompson, J.D.3    Heringa, J.4
  • 3
    • 0027377580 scopus 로고
    • FMR-1 protein: Conserved RNP family domains and selective RNA binding
    • Ashley, C.T., Wilkinson, K.D., Reines, D. and Warren, S.T. (1993) FMR-1 protein: Conserved RNP family domains and selective RNA binding. Science, 262, 563-566.
    • (1993) Science , vol.262 , pp. 563-566
    • Ashley, C.T.1    Wilkinson, K.D.2    Reines, D.3    Warren, S.T.4
  • 4
    • 0027327486 scopus 로고
    • The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein
    • Siomi, H., Siomi, M.C., Nussbaum, R.L. and 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
  • 6
    • 0037371441 scopus 로고    scopus 로고
    • The role of a clinically important mutation in the fold and RNA-binding properties of KH motifs
    • Ramos, A., Hollingworth, D. and Pastore, A. (2003) The role of a clinically important mutation in the fold and RNA-binding properties of KH motifs. RNA, 9, 293-298.
    • (2003) RNA , vol.9 , pp. 293-298
    • Ramos, A.1    Hollingworth, D.2    Pastore, A.3
  • 7
    • 43549124851 scopus 로고    scopus 로고
    • Structure and function of KH domains
    • Valverde, R., Edwards, L. and Regan, L. (2008) Structure and function of KH domains. FEBS J., 275, 2712-2726.
    • (2008) FEBS J , vol.275 , pp. 2712-2726
    • Valverde, R.1    Edwards, L.2    Regan, L.3
  • 8
    • 0034603208 scopus 로고    scopus 로고
    • Sequence-specific RNA binding by a Nova KH domain: Implications for paraneoplastic disease and the fragile X syndrome
    • Lewis, H.A., Musunuru, K., Jensen, K.B., Edo, C., Chen, H., Darnell, R.B. and Burley, S.K. (2000) Sequence-specific RNA binding by a Nova KH domain: Implications for paraneoplastic disease and the fragile X syndrome. Cell, 100, 323-332.
    • (2000) Cell , vol.100 , pp. 323-332
    • Lewis, H.A.1    Musunuru, K.2    Jensen, K.B.3    Edo, C.4    Chen, H.5    Darnell, R.B.6    Burley, S.K.7
  • 10
    • 0028971722 scopus 로고
    • The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2
    • Zhang, Y., O'Conner, J.P., Siomi, M.C., Srinivasan, S., Dutra, A., Nussbaum, R.L. and Dreyfuss, G. (1995) The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2. EMBO J. 14, 5358-5366.
    • (1995) EMBO J , vol.14 , pp. 5358-5366
    • Zhang, Y.1    O'Conner, J.P.2    Siomi, M.C.3    Srinivasan, S.4    Dutra, A.5    Nussbaum, R.L.6    Dreyfuss, G.7
  • 11
    • 0035885862 scopus 로고    scopus 로고
    • Comparative genomic sequence analysis of the FXR gene family: FMR1, FXR1 and FXR2
    • Kirkpatrick, L.L., McIlwain, K.A. and Nelson, D.L. (2001) Comparative genomic sequence analysis of the FXR gene family: FMR1, FXR1 and FXR2. Genomics, 78, 169-177.
    • (2001) Genomics , vol.78 , pp. 169-177
    • Kirkpatrick, L.L.1    McIlwain, K.A.2    Nelson, D.L.3
  • 12
    • 0033761489 scopus 로고    scopus 로고
    • Characterization of dFMR1, a Drosophila melanogaster homolog of the fragile X mental retardation protein
    • Wan, L., Dockendorff, T.C., Jongens, T.A. and Dreyfuss, G. (2000) Characterization of dFMR1, a Drosophila melanogaster homolog of the fragile X mental retardation protein. Mol. Cell Biol., 20 8536-8547.
    • (2000) Mol. Cell Biol , vol.20 , pp. 8536-8547
    • Wan, L.1    Dockendorff, T.C.2    Jongens, T.A.3    Dreyfuss, G.4
  • 14
    • 0030760613 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is associated with poly(A)+ mRNA in actively translating polyribosomes
    • Corbin, F., Bouillon, M., Fortin, A., Morin, S., Rousseau, F. and Khandjian, E.W. (1997) The fragile X mental retardation protein is associated with poly(A)+ mRNA in actively translating polyribosomes. Hum. Mol. Genet., 6, 1465-1472.
    • (1997) Hum. Mol. Genet , vol.6 , pp. 1465-1472
    • Corbin, F.1    Bouillon, M.2    Fortin, A.3    Morin, S.4    Rousseau, F.5    Khandjian, E.W.6
  • 16
    • 0030059545 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is associated with ribosomes
    • Khandjian, E.W., Corbin, F., Woerly, S. and Rousseau, F. (1996) The fragile X mental retardation protein is associated with ribosomes. Nat. Genet., 12, 91-93.
    • (1996) Nat. Genet , vol.12 , pp. 91-93
    • Khandjian, E.W.1    Corbin, F.2    Woerly, S.3    Rousseau, F.4
  • 17
    • 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
  • 18
    • 0029972935 scopus 로고    scopus 로고
    • Specific sequences in the fragile X syndrome protein FMR1 and the FXR proteins mediate their binding to 60S ribosomal subunits and the interactions among them
    • Siomi, M.C., Zhang, Y., Siomi, H. and Dreyfuss, G. (1996) Specific sequences in the fragile X syndrome protein FMR1 and the FXR proteins mediate their binding to 60S ribosomal subunits and the interactions among them. Mol. Cell Biol., 16, 3825-3832.
    • (1996) Mol. Cell Biol , vol.16 , pp. 3825-3832
    • Siomi, M.C.1    Zhang, Y.2    Siomi, H.3    Dreyfuss, G.4
  • 20
    • 4444238669 scopus 로고    scopus 로고
    • Biochemical evidence for the association of fragile X mental retardation protein with brain polyribosomal ribonucleoparticles
    • Khandjian, E.W., Huot, M.E., Tremblay, S., Davidovic, L., Mazroui, R. and Bardoni, B. (2004) Biochemical evidence for the association of fragile X mental retardation protein with brain polyribosomal ribonucleoparticles. Proc. Natl Acad. Sci. USA, 101, 13357-13362.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 13357-13362
    • Khandjian, E.W.1    Huot, M.E.2    Tremblay, S.3    Davidovic, L.4    Mazroui, R.5    Bardoni, B.6
  • 21
    • 7244224871 scopus 로고    scopus 로고
    • Fragile X mental retardation protein is associated with translating polyribosomes in neuronal cells
    • Stefani, G., Fraser, C.E., Darnell, J.C. and Darnell, R.B. (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
  • 22
    • 0031310667 scopus 로고    scopus 로고
    • FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association
    • Feng, Y., Absher, D., Eberhart, D.E., Brown, V., Malter, H.E. and Warren, S.T. (1997) FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association. Mol. Cell, 1, 109-118.
    • (1997) Mol. Cell , vol.1 , pp. 109-118
    • Feng, Y.1    Absher, D.2    Eberhart, D.E.3    Brown, V.4    Malter, H.E.5    Warren, S.T.6
  • 24
    • 0033231022 scopus 로고    scopus 로고
    • Oligomerization properties of fragile-X mental-retardation protein (FMRP) and the fragile-X-related proteins FXR1P and FXR2P
    • Tamanini, F., Van Unen, L., Bakker, C., Sacchi, N., Galjaard, H., Oostra, B.A. and Hoogeveen, A.T. (1999) Oligomerization properties of fragile-X mental-retardation protein (FMRP) and the fragile-X-related proteins FXR1P and FXR2P. Biochem. J., 343, 517-523.
    • (1999) Biochem. J , vol.343 , pp. 517-523
    • Tamanini, F.1    Van Unen, L.2    Bakker, C.3    Sacchi, N.4    Galjaard, H.5    Oostra, B.A.6    Hoogeveen, A.T.7
  • 26
    • 0030023275 scopus 로고    scopus 로고
    • The chicken FMR1 gene is highly conserved with a CCT 5′-untranslated repeat and encodes an RNA-binding protein
    • Price, D.K., Zhang, F., Ashley, C.T.J. and Warren, S.T. (1996) The chicken FMR1 gene is highly conserved with a CCT 5′-untranslated repeat and encodes an RNA-binding protein. Genomics, 31, 3-12.
    • (1996) Genomics , vol.31 , pp. 3-12
    • Price, D.K.1    Zhang, F.2    Ashley, C.T.J.3    Warren, S.T.4
  • 27
    • 23044512658 scopus 로고    scopus 로고
    • Two members of the Fxr gene family, Fmr1 and Fxr1, are differentially expressed in Xenopus tropicalis
    • Blonden, L., van't Padje, S., Severijnen, L.A., Destree, O., Oostra, B.A. and Willemsen, R. (2005) Two members of the Fxr gene family, Fmr1 and Fxr1, are differentially expressed in Xenopus tropicalis. Int. J. Dev. Biol., 49, 437-441.
    • (2005) Int. J. Dev. Biol , vol.49 , pp. 437-441
    • Blonden, L.1    van't Padje, S.2    Severijnen, L.A.3    Destree, O.4    Oostra, B.A.5    Willemsen, R.6
  • 28
    • 0027265596 scopus 로고
    • Human and murine FMR-1: Alternative splicing and translational initiation downstream of the CGG-repeat
    • Ashley, C.T., Sutcliffe, J.S., Kunst, C.B., Leiner, H.A., Eichler, E.E., Nelson, D.L. and Warren, S.T. (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    Nelson, D.L.6    Warren, S.T.7
  • 34
    • 0028880051 scopus 로고
    • Highly conserved 3′-UTR and expression pattern of FXR1 points to a divergent gene regulation of FXR1 and FMR1
    • Coy, J.F., Sedlacek, Z., Bachner, D., Hameister, H., Joos, S., Lichter, P., Delius, H. and Poustka, A. (1995) Highly conserved 3′-UTR and expression pattern of FXR1 points to a divergent gene regulation of FXR1 and FMR1. Hum. Mol. Genet., 4, 2209-2218.
    • (1995) Hum. Mol. Genet , vol.4 , pp. 2209-2218
    • Coy, J.F.1    Sedlacek, Z.2    Bachner, D.3    Hameister, H.4    Joos, S.5    Lichter, P.6    Delius, H.7    Poustka, A.8
  • 35
    • 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. and Mandel, J. (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.4    Mandel, J.5
  • 36
    • 2942591953 scopus 로고    scopus 로고
    • Muscle specific fragile X related protein 1 isoforms are sequestered in the nucleus of undifferentiated myoblast
    • Dube, M., Huot, M.E. and Khandjian, E.W. (2000) Muscle specific fragile X related protein 1 isoforms are sequestered in the nucleus of undifferentiated myoblast. BMC Genet., 1, 4.
    • (2000) BMC Genet , vol.1 , pp. 4
    • Dube, M.1    Huot, M.E.2    Khandjian, E.W.3
  • 38
    • 0033566226 scopus 로고    scopus 로고
    • Alternative splicing in the murine and human FXR1 genes
    • Kirkpatrick, L.L., McIlwain, K.A. and Nelson, D.L. (1999) Alternative splicing in the murine and human FXR1 genes. Genomics, 59, 193-202.
    • (1999) Genomics , vol.59 , pp. 193-202
    • Kirkpatrick, L.L.1    McIlwain, K.A.2    Nelson, D.L.3
  • 39
    • 59649126241 scopus 로고    scopus 로고
    • The FXG: A presynaptic fragile X granule expressed in a subset of developing brain circuits
    • Christie, S.B., Akins, M.R., Schwob, J.E. and Fallon, J.R. (2009) The FXG: A presynaptic fragile X granule expressed in a subset of developing brain circuits. J. Neurosci., 29, 1514-1524.
    • (2009) J. Neurosci , vol.29 , pp. 1514-1524
    • Christie, S.B.1    Akins, M.R.2    Schwob, J.E.3    Fallon, J.R.4
  • 40
    • 17444384228 scopus 로고    scopus 로고
    • Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes
    • Darnell, J.C., Fraser, C.E., Mostovetsky, O., Stefani, G., Jones, T.A., Eddy, S.R. and Darnell, R.B. (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    Eddy, S.R.6    Darnell, R.B.7
  • 41
    • 0035900649 scopus 로고    scopus 로고
    • Fragile X mental retardation protein targets G Quartet mRNAs important for neuronal function
    • Darnell, J.C., Jensen, K.B., Jin, P., Brown, V., Warren, S.T. and Darnell, R.B. (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    Darnell, R.B.6
  • 42
    • 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. and 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
  • 43
    • 0029988528 scopus 로고    scopus 로고
    • Three-dimensional structure and stability of the KH domain: Molecular insights into the Fragile X syndrome
    • Musco, G., Stier, G., Joseph, C., Morelli, M.A.C., Nilges, M., Gibson, T. and Pastore, A. (1996) Three-dimensional structure and stability of the KH domain: Molecular insights into the Fragile X syndrome. Cell 85, 237-245.
    • (1996) Cell , vol.85 , pp. 237-245
    • Musco, G.1    Stier, G.2    Joseph, C.3    Morelli, M.A.C.4    Nilges, M.5    Gibson, T.6    Pastore, A.7
  • 45
    • 0034705034 scopus 로고    scopus 로고
    • The tetranucleotide UCAY directs the specific recognition of RNA by the Nova K-homology 3 domain
    • Jensen, K.B., Musunuru, K., Lewis, H.A., Burley, S.K. and Darnell, R.B. (2000) The tetranucleotide UCAY directs the specific recognition of RNA by the Nova K-homology 3 domain. Proc. Natl Acad. Sci. USA, 97 5740-5745.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5740-5745
    • Jensen, K.B.1    Musunuru, K.2    Lewis, H.A.3    Burley, S.K.4    Darnell, R.B.5
  • 46
    • 0038382977 scopus 로고    scopus 로고
    • Nova regulates GABA(A) receptor gamma2 alternative splicing via a distal downstream UCAU-rich intronic splicing enhancer
    • Dredge, B.K. and Darnell, R.B. (2003) Nova regulates GABA(A) receptor gamma2 alternative splicing via a distal downstream UCAU-rich intronic splicing enhancer. Mol. Cell. Biol., 23, 4687-4700.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 4687-4700
    • Dredge, B.K.1    Darnell, R.B.2
  • 47
    • 0035907317 scopus 로고    scopus 로고
    • Optimized RNA targets of two closely related triple KH domain proteins, heterogeneous nuclear ribonucleoprotein K and alpha CP-2KL, suggest distinct modes of RNA recognition
    • Thisted, T., Lyakhov, D.L. and Liebhaber, S.A. (2001) Optimized RNA targets of two closely related triple KH domain proteins, heterogeneous nuclear ribonucleoprotein K and alpha CP-2KL, suggest distinct modes of RNA recognition. J. Biol. Chem., 276, 17484-17496.
    • (2001) J. Biol. Chem , vol.276 , pp. 17484-17496
    • Thisted, T.1    Lyakhov, D.L.2    Liebhaber, S.A.3
  • 48
    • 0032521186 scopus 로고    scopus 로고
    • A cooperative interaction between U2AF65 and mBBP/SF1 facilitates branchpoint region recognition
    • Berglund, J.A., Abovich, N. and Rosbash, M. (1998) A cooperative interaction between U2AF65 and mBBP/SF1 facilitates branchpoint region recognition. Genes Dev., 12, 858-867.
    • (1998) Genes Dev , vol.12 , pp. 858-867
    • Berglund, J.A.1    Abovich, N.2    Rosbash, M.3
  • 49
    • 0030929165 scopus 로고    scopus 로고
    • Localization of Xenopus Vg1 mRNA by Vera protein and the endoplasmic reticulum
    • Deshler, J.O., Highett, M.I. and Schnapp, B.J. (1997) Localization of Xenopus Vg1 mRNA by Vera protein and the endoplasmic reticulum. Science, 276, 1128-1131.
    • (1997) Science , vol.276 , pp. 1128-1131
    • Deshler, J.O.1    Highett, M.I.2    Schnapp, B.J.3
  • 51
    • 0036792844 scopus 로고    scopus 로고
    • The KH domains of Xenopus Vg1RBP mediate RNA binding and self-association
    • Git, A. and Standart, N. (2002) The KH domains of Xenopus Vg1RBP mediate RNA binding and self-association. RNA, 8, 1319-1333.
    • (2002) RNA , vol.8 , pp. 1319-1333
    • Git, A.1    Standart, N.2
  • 52
    • 0032560007 scopus 로고    scopus 로고
    • A highly conserved RNA-binding protein for cytoplasmic mRNA localization in vertebrates
    • Deshler, J.O., Highett, M.I., Abramson, T. and Schnapp, B.J. (1998) A highly conserved RNA-binding protein for cytoplasmic mRNA localization in vertebrates. Curr. Biol., 8, 489-496.
    • (1998) Curr. Biol , vol.8 , pp. 489-496
    • Deshler, J.O.1    Highett, M.I.2    Abramson, T.3    Schnapp, B.J.4
  • 53
    • 8644255888 scopus 로고    scopus 로고
    • Expression of three zebrafish orthologs of human FMR1-related genes and their phylogenetic relationships
    • Tucker, B., Richards, R. and Lardelli, M. (2004) Expression of three zebrafish orthologs of human FMR1-related genes and their phylogenetic relationships. Dev. Genes Evol., 214, 567-574.
    • (2004) Dev. Genes Evol , vol.214 , pp. 567-574
    • Tucker, B.1    Richards, R.2    Lardelli, M.3
  • 55
    • 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. (2006) Exaggerated behavioral phenotypes in Fmr1/ Fxr2 double knockout mice reveal a functional genetic interaction between Fragile X-related proteins. Hum. Mol. Genet., 15, 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
  • 57
    • 65649083055 scopus 로고    scopus 로고
    • Altered hippocampal synaptic plasticity in the Fmr1 gene family knockout mouse models
    • Zhang, J., Hou, L., Klann, E. and Nelson, D.L.N. (2009) Altered hippocampal synaptic plasticity in the Fmr1 gene family knockout mouse models. J. Neurophysiol., 101, 2572-2580.
    • (2009) J. Neurophysiol , vol.101 , pp. 2572-2580
    • Zhang, J.1    Hou, L.2    Klann, E.3    Nelson, D.L.N.4
  • 58
    • 0037188502 scopus 로고    scopus 로고
    • Altered synaptic plasticity 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 plasticity 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
  • 59
    • 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. (2006) Dynamic translational and proteasomal regulation of fragile X mental retardation protein controls mGluR-dependent long-term depression. Neuron, 51, 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
  • 60
    • 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, E.D. and Huber, K.M. (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
  • 61
    • 20144369806 scopus 로고    scopus 로고
    • Highly prevalent putative quadruplex sequence motifs in human DNA
    • Todd, A.K., Johnston, M. and Neidle, S. (2005) Highly prevalent putative quadruplex sequence motifs in human DNA. Nucleic Acids Res., 33 2901-2907.
    • (2005) Nucleic Acids Res , vol.33 , pp. 2901-2907
    • Todd, A.K.1    Johnston, M.2    Neidle, S.3
  • 62
    • 20144364292 scopus 로고    scopus 로고
    • Prevalence of quadruplexes in the human genome
    • Huppert, J.L. and Balasubramanian, S. (2005) Prevalence of quadruplexes in the human genome. Nucleic Acids Res., 33, 2908-2916.
    • (2005) Nucleic Acids Res , vol.33 , pp. 2908-2916
    • Huppert, J.L.1    Balasubramanian, S.2
  • 63
    • 33644877945 scopus 로고    scopus 로고
    • GRSDB: A database of quadruplex forming G-rich sequences in alternatively processed mammalian pre-mRNA sequences
    • Kostadinov, R., Malhotra, N., Viotti, M., Shine, R., D'Antonio, L. and Bagga, P. (2006) GRSDB: A database of quadruplex forming G-rich sequences in alternatively processed mammalian pre-mRNA sequences. Nucleic Acids Res., 34, D119-D124.
    • (2006) Nucleic Acids Res , vol.34
    • Kostadinov, R.1    Malhotra, N.2    Viotti, M.3    Shine, R.4    D'Antonio, L.5    Bagga, P.6
  • 64
    • 33947310727 scopus 로고    scopus 로고
    • An RNA G-quadruplex in the 5′-UTR of the NRAS proto-oncogene modulates translation
    • Kumari, S., Bugaut, A., Huppert, J.L. and Balasubramanian, S. (2007) An RNA G-quadruplex in the 5′-UTR of the NRAS proto-oncogene modulates translation. Nat. Chem. Biol., 3, 218-221.
    • (2007) Nat. Chem. Biol , vol.3 , pp. 218-221
    • Kumari, S.1    Bugaut, A.2    Huppert, J.L.3    Balasubramanian, S.4
  • 65
    • 58049200140 scopus 로고    scopus 로고
    • G4 resolvase 1 binds both DNA and RNA tetramolecular quadruplex with high affinity and is the major source of tetramolecular quadruplex G4-DNA and G4-RNA resolving activity in HeLa cell lysates
    • Creacy, S.D., Routh, E.D., Iwamoto, F., Nagamine, Y., Akman, S.A. and Vaughn, J.P. (2008) G4 resolvase 1 binds both DNA and RNA tetramolecular quadruplex with high affinity and is the major source of tetramolecular quadruplex G4-DNA and G4-RNA resolving activity in HeLa cell lysates. J. Biol. Chem., 283, 34626-34634.
    • (2008) J. Biol. Chem , vol.283 , pp. 34626-34634
    • Creacy, S.D.1    Routh, E.D.2    Iwamoto, F.3    Nagamine, Y.4    Akman, S.A.5    Vaughn, J.P.6
  • 66
    • 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. (2003) The fragile X mental retardation protein is required for type-I metabotropic glutamate receptor-dependent translation of PSD-95. Proc. Natl Acad. Sci. USA 100, 14374-14378.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 14374-14378
    • Todd, P.K.1    Mack, K.J.2    Malter, J.S.3
  • 67
    • 33947195786 scopus 로고    scopus 로고
    • FMRP mediates mGluR5-dependent translation of amyloid precursor protein
    • Westmark, C.J. and Malter, J.S. (2007) FMRP mediates mGluR5-dependent translation of amyloid precursor protein. PLoS Biol., 5, e52.
    • (2007) PLoS Biol , vol.5
    • Westmark, C.J.1    Malter, J.S.2
  • 69
    • 0141631894 scopus 로고    scopus 로고
    • G-quartet-dependent recognition between the FMRP RGG box and RNA
    • Ramos, A., Hollingworth, D. and Pastore, A. (2003) G-quartet-dependent recognition between the FMRP RGG box and RNA. RNA, 9, 1198-1207.
    • (2003) RNA , vol.9 , pp. 1198-1207
    • Ramos, A.1    Hollingworth, D.2    Pastore, A.3
  • 70
    • 47949115691 scopus 로고    scopus 로고
    • Fragile X mental retardation protein interactions with the microtubule associated protein 1B RNA
    • Menon, L., Mader, S.A. and Mihailescu, M.R. (2008) Fragile X mental retardation protein interactions with the microtubule associated protein 1B RNA. RNA, 14, 1644-1655.
    • (2008) RNA , vol.14 , pp. 1644-1655
    • Menon, L.1    Mader, S.A.2    Mihailescu, M.R.3
  • 71
    • 34548726219 scopus 로고    scopus 로고
    • Interactions of the G quartet forming semaphorin 3F RNA with the RGG box domain of the fragile X protein family
    • Menon, L. and Mihailescu, M.R. (2007) Interactions of the G quartet forming semaphorin 3F RNA with the RGG box domain of the fragile X protein family. Nucleic Acids Res., 35, 5379-5392.
    • (2007) Nucleic Acids Res , vol.35 , pp. 5379-5392
    • Menon, L.1    Mihailescu, M.R.2
  • 72
    • 33745858693 scopus 로고    scopus 로고
    • Thermodynamics of the fragile X mental retardation protein RGG box interactions with G quartet forming RNA
    • Zanotti, K.J., Lackey, P.E., Evans, G.L. and Mihailescu, M.R. (2006) Thermodynamics of the fragile X mental retardation protein RGG box interactions with G quartet forming RNA. Biochemistry, 45, 8319-8330.
    • (2006) Biochemistry , vol.45 , pp. 8319-8330
    • Zanotti, K.J.1    Lackey, P.E.2    Evans, G.L.3    Mihailescu, M.R.4
  • 73
    • 0026740718 scopus 로고
    • Primary structure and binding activity of the hnRNP U protein: Binding RNA through RGG box
    • Kiledjian, M. and Dreyfuss, G. (1992) Primary structure and binding activity of the hnRNP U protein: Binding RNA through RGG box. EMBO J. 11, 2655-2664.
    • (1992) EMBO J , vol.11 , pp. 2655-2664
    • Kiledjian, M.1    Dreyfuss, G.2
  • 74
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd, C.G. and Dreyfuss, G. (1994) Conserved structures and diversity of functions of RNA-binding proteins. Science, 265, 615-621.
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 75
    • 0344237280 scopus 로고    scopus 로고
    • Fragile X mental retardation protein determinants required for its association with polyribosomal mRNPs
    • Mazroui, R., Huot, M.E., Tremblay, S., Boilard, N., Labelle, Y. and Khandjian, E.W. (2003) Fragile X mental retardation protein determinants required for its association with polyribosomal mRNPs. Hum. Mol. Genet., 12, 3087-3096.
    • (2003) Hum. Mol. Genet , vol.12 , pp. 3087-3096
    • Mazroui, R.1    Huot, M.E.2    Tremblay, S.3    Boilard, N.4    Labelle, Y.5    Khandjian, E.W.6
  • 77
    • 33947537457 scopus 로고    scopus 로고
    • Fragile X mental retardation protein induces synapse loss through acute postsynaptic translational regulation
    • Pfeiffer, B.E. and Huber, K.M. (2007) Fragile X mental retardation protein induces synapse loss through acute postsynaptic translational regulation. J. Neurosci., 27, 3120-3130.
    • (2007) J. Neurosci , vol.27 , pp. 3120-3130
    • Pfeiffer, B.E.1    Huber, K.M.2
  • 78
    • 39949085583 scopus 로고    scopus 로고
    • Stress granules: The Tao of RNA triage
    • Anderson, P. and Kedersha, N. (2008) Stress granules: The Tao of RNA triage. Trends Biochem. Sci., 33, 141-150.
    • (2008) Trends Biochem. Sci , vol.33 , pp. 141-150
    • Anderson, P.1    Kedersha, N.2
  • 79
    • 34247524717 scopus 로고    scopus 로고
    • Irreversible translation arrest in the reperfused brain
    • DeGracia, D.J. and Hu, B.R. (2007) Irreversible translation arrest in the reperfused brain. J. Cereb. Blood Flow Metab., 27, 875-893.
    • (2007) J. Cereb. Blood Flow Metab , vol.27 , pp. 875-893
    • DeGracia, D.J.1    Hu, B.R.2
  • 80
    • 3242699557 scopus 로고    scopus 로고
    • Global mRNA stabilization preferentially linked to translational repression during the endoplasmic reticulum stress response
    • Kawai, T., Fan, J., Mazan-Mamczarz, K. and Gorospe, M. (2004) Global mRNA stabilization preferentially linked to translational repression during the endoplasmic reticulum stress response. Mol. Cell. Biol. 24, 6773-6787.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 6773-6787
    • Kawai, T.1    Fan, J.2    Mazan-Mamczarz, K.3    Gorospe, M.4
  • 81
    • 0037112805 scopus 로고    scopus 로고
    • Trapping of messenger RNA by Fragile X mental retardation protein into cytoplasmic granules induces translation repression
    • Mazroui, R., Huot, M.E., Tremblay, S., Filion, C., Labelle, Y. and Khandjian, E.W. (2002) Trapping of messenger RNA by Fragile X mental retardation protein into cytoplasmic granules induces translation repression. Hum. Mol. Genet., 11, 3007-3017.
    • (2002) Hum. Mol. Genet , vol.11 , pp. 3007-3017
    • Mazroui, R.1    Huot, M.E.2    Tremblay, S.3    Filion, C.4    Labelle, Y.5    Khandjian, E.W.6
  • 82
    • 33749493493 scopus 로고    scopus 로고
    • Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2alpha phosphorylation
    • Mazroui, R., Sukarieh, R., Bordeleau, M.E., Kaufman, R.J., Northcote, P., Tanaka, J., Gallouzi, I. and Pelletier, J. (2006) Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2alpha phosphorylation. Mol. Biol. Cell 17, 4212-4219.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4212-4219
    • Mazroui, R.1    Sukarieh, R.2    Bordeleau, M.E.3    Kaufman, R.J.4    Northcote, P.5    Tanaka, J.6    Gallouzi, I.7    Pelletier, J.8
  • 83
    • 33645643381 scopus 로고    scopus 로고
    • Fragile X mental retardation protein shifts between polyribosomes and stress granules after neuronal injury by arsenite stress or in vivo hippocampal electrode insertion
    • Kim, S.H., Dong, W.K., Weiler, I.J. and Greenough, W.T. (2006) Fragile X mental retardation protein shifts between polyribosomes and stress granules after neuronal injury by arsenite stress or in vivo hippocampal electrode insertion. J. Neurosci., 26, 2413-2418.
    • (2006) J. Neurosci , vol.26 , pp. 2413-2418
    • Kim, S.H.1    Dong, W.K.2    Weiler, I.J.3    Greenough, W.T.4
  • 84
    • 33846665074 scopus 로고    scopus 로고
    • Fragile X related protein 1 isoforms differentially modulate the affinity of fragile X mental retardation protein for G-quartet RNA structure
    • Bechara, E., Davidovic, L., Melko, M., Bensaid, M., Tremblay, S., Grosgeorge, J., Khandjian, E.W., Lalli, E. and Bardoni, B. (2007) Fragile X related protein 1 isoforms differentially modulate the affinity of fragile X mental retardation protein for G-quartet RNA structure. Nucleic Acids Res., 35, 299-306.
    • (2007) Nucleic Acids Res , vol.35 , pp. 299-306
    • Bechara, E.1    Davidovic, L.2    Melko, M.3    Bensaid, M.4    Tremblay, S.5    Grosgeorge, J.6    Khandjian, E.W.7    Lalli, E.8    Bardoni, B.9
  • 85
    • 0029875911 scopus 로고    scopus 로고
    • The onconeural antigen Nova-1 is a neuron-specific RNA-binding protein, the activity of which is inhibited by paraneoplastic antibodies
    • Buckanovich, R.J., Yang, Y.Y. and Darnell, R.B. (1996) The onconeural antigen Nova-1 is a neuron-specific RNA-binding protein, the activity of which is inhibited by paraneoplastic antibodies. J. Neurosci., 16, 1114-1122.
    • (1996) J. Neurosci , vol.16 , pp. 1114-1122
    • Buckanovich, R.J.1    Yang, Y.Y.2    Darnell, R.B.3


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