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Volumn 6, Issue 11, 2004, Pages 1048-1053

RNA and microRNAs in fragile X mental retardation

Author keywords

[No Author keywords available]

Indexed keywords

FRAGILE X MENTAL RETARDATION PROTEIN; LIGAND; MESSENGER RNA; MICRORNA;

EID: 7944232720     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1104-1048     Document Type: Review
Times cited : (283)

References (73)
  • 2
    • 0025905795 scopus 로고
    • Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting length variation in fragile X syndrome
    • Verkerk, A. J. et al. Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting length variation in fragile X syndrome. Cell 65, 905-914 (1991).
    • (1991) Cell , vol.65 , pp. 905-914
    • Verkerk, A.J.1
  • 3
    • 0025800165 scopus 로고
    • Mapping of DNA instability at the fragile X to a trinucleotide repeat sequence p(CCG)n
    • Kremer, E. J. et al. Mapping of DNA instability at the fragile X to a trinucleotide repeat sequence p(CCG)n. Science 252, 1711-1714 (1991).
    • (1991) Science , vol.252 , pp. 1711-1714
    • Kremer, E.J.1
  • 4
    • 0026345716 scopus 로고
    • Variation of the CGG repeat atthe fragile X site results in genetic instability: Resolution of the Sherman paradox
    • Fu, Y. H. et al. Variation of the CGG repeat atthe fragile X site results in genetic instability: resolution of the Sherman paradox. Cell 67, 1047-1058 (1991).
    • (1991) Cell , vol.67 , pp. 1047-1058
    • Fu, Y.H.1
  • 5
    • 0026339303 scopus 로고
    • Instability of a 550-base pair DNA segment and abnormal methylation in fragile X syndrome
    • Oberle, I. et al. Instability of a 550-base pair DNA segment and abnormal methylation in fragile X syndrome. Science 252, 1097-1102 (1991).
    • (1991) Science , vol.252 , pp. 1097-1102
    • Oberle, I.1
  • 6
    • 0034640011 scopus 로고    scopus 로고
    • Fourteen and counting: Unraveling trinucleotide repeat diseases
    • Cummings, C. J. & Zoghbi, H. Y. Fourteen and counting: unraveling trinucleotide repeat diseases. Hum. Mol. Genet. 9, 909-916 (2000).
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 909-916
    • Cummings, C.J.1    Zoghbi, H.Y.2
  • 7
    • 0031045874 scopus 로고    scopus 로고
    • Characterization of the full fragile X syndrome mutation in fetal gametes
    • Malter, H. E. et al. Characterization of the full fragile X syndrome mutation in fetal gametes. Nature Genet. 15, 165-169 (1997).
    • (1997) Nature Genet. , vol.15 , pp. 165-169
    • Malter, H.E.1
  • 8
    • 0041880131 scopus 로고    scopus 로고
    • RNA-mediated neurodegeneration caused by the fragile X premutation rCGG repeats in Drosophila
    • Jin, P. et al. RNA-mediated neurodegeneration caused by the fragile X premutation rCGG repeats in Drosophila. Neuron 39, 739-747 (2003).
    • (2003) Neuron , vol.39 , pp. 739-747
    • Jin, P.1
  • 9
    • 2342635196 scopus 로고    scopus 로고
    • The fragile-X premutation: A maturing perspective
    • Hagerman, P. J. & Hagerman, R. J. The fragile-X premutation: a maturing perspective. Am. J. Hum. Genet. 74, 805-816 (2004).
    • (2004) Am. J. Hum. Genet. , vol.74 , pp. 805-816
    • Hagerman, P.J.1    Hagerman, R.J.2
  • 10
    • 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. & Mandel, J. L. The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation. Nature Genet. 4, 335-340 (1993).
    • (1993) Nature Genet. , vol.4 , pp. 335-340
    • Devys, D.1    Lutz, Y.2    Rouyer, N.3    Bellocq, J.P.4    Mandel, J.L.5
  • 11
    • 0029069223 scopus 로고
    • FXR1, an autosomal homolog of the fragile X mental retardation gene
    • Siomi, M. C. et al. FXR1, an autosomal homolog of the fragile X mental retardation gene. EMBO J. 14, 2401-2408 (1995).
    • (1995) EMBO J. , vol.14 , pp. 2401-2408
    • Siomi, M.C.1
  • 12
    • 0028971722 scopus 로고
    • The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2
    • Zhang, Y. et al. The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2. EMBO J. 14, 5358-5366 (1995).
    • (1995) EMBO J. , vol.14 , pp. 5358-5366
    • Zhang, Y.1
  • 13
    • 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. & Dreyfuss, G. Characterization of dFMR1, a drosophila melanogaster homolog of the fragile X mental retardation protein. Mol. Cell. Biol. 20, 8536-8547 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8536-8547
    • Wan, L.1    Dockendorff, T.C.2    Jongens, T.A.3    Dreyfuss, G.4
  • 14
    • 0027377580 scopus 로고
    • FMR1 protein: Conserved RNP family domains and selective RNA binding
    • Ashley, C. T., Jr., Wilkinson, K. D., Reines, D. & Warren, S. T. FMR1 protein: conserved RNP family domains and selective RNA binding. Science 262, 563-566 (1993).
    • (1993) Science , vol.262 , pp. 563-566
    • Ashley Jr., C.T.1    Wilkinson, K.D.2    Reines, D.3    Warren, S.T.4
  • 15
    • 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. et al. 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).
    • (1997) Mol. Cell , vol.1 , pp. 109-118
    • Feng, Y.1
  • 16
  • 17
    • 0035368955 scopus 로고    scopus 로고
    • The fragile X mental retardation protein inhibits translation via interacting with mRNA
    • Li Z. et al. The fragile X mental retardation protein inhibits translation via interacting with mRNA. Nucleic Acids Res. 29, 2276-2283 (2001).
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2276-2283
    • Li, Z.1
  • 18
    • 0029816723 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals
    • Eberhart, D. E., Malter, H. E., Fang, Y. & Warren, S. T. The fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals. Hum. Mol. Genet. 5, 1083-1091 (1996).
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1083-1091
    • Eberhart, D.E.1    Malter, H.E.2    Fang, Y.3    Warren, S.T.4
  • 19
    • 0030986183 scopus 로고    scopus 로고
    • Abnormal dendritic spines in fragile X-knockout mice: Maturation and pruning deficits
    • Comery, T. A. et al. Abnormal dendritic spines in fragile X-knockout mice: maturation and pruning deficits. Proc. Natl Acad. Sci. USA 94, 5401-5404 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5401-5404
    • Comery, T.A.1
  • 20
    • 0025720084 scopus 로고
    • Analysis of neocortex in three males with the fragile X syndrome
    • Hinton, V. J., Brown, W. T., Wisniewski, K. & Rudelli, R. D. Analysis of neocortex in three males with the fragile X syndrome. Am. J. Med. Genet. 41, 289-294 (1991).
    • (1991) Am. J. Med. Genet. , vol.41 , pp. 289-294
    • Hinton, V.J.1    Brown, W.T.2    Wisniewski, K.3    Rudelli, R.D.4
  • 21
    • 0035879180 scopus 로고    scopus 로고
    • Abnormal development of dendritic spines in FMR1 knock-out mice
    • Nimchinsky, E. A., Oberlander, A. M. & Svoboda, K. Abnormal development of dendritic spines in FMR1 knock-out mice. J. Neurosci. 21, 5139-5146 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 5139-5146
    • Nimchinsky, E.A.1    Oberlander, A.M.2    Svoboda, K.3
  • 22
    • 0031046778 scopus 로고    scopus 로고
    • Fragile X mental retardation protein: Nucleocytoplasmic shuttling and association with somatodendritic ribosomes
    • Feng, Y. et al. Fragile X mental retardation protein: nucleocytoplasmic shuttling and association with somatodendritic ribosomes. J. Neurosci. 17, 1539-1547 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 1539-1547
    • Feng, Y.1
  • 23
    • 18044379515 scopus 로고    scopus 로고
    • Microarray identification of FMRP-associated brain mRNAs and altered mRNA translational profiles in fragile X syndrome
    • Brown, V. et al. Microarray identification of FMRP-associated brain mRNAs and altered mRNA translational profiles in fragile X syndrome. Cell 107, 477-487 (2001).
    • (2001) Cell , vol.107 , pp. 477-487
    • Brown, V.1
  • 24
    • 0035900649 scopus 로고    scopus 로고
    • Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function
    • Darnell, J. C. et al. Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function. Cell 107, 489-499 (2001).
    • (2001) Cell , vol.107 , pp. 489-499
    • Darnell, J.C.1
  • 25
    • 0035801393 scopus 로고    scopus 로고
    • The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif
    • Schaeffer, C. et al. The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif. EMBO J. 20, 4803-4813 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4803-4813
    • Schaeffer, C.1
  • 26
    • 0037421721 scopus 로고    scopus 로고
    • RNA cargoes associating with FMRP reveal deficits in cellular functioning in Fmr1 null mice
    • Miyashiro, K. Y. et al. RNA cargoes associating with FMRP reveal deficits in cellular functioning in Fmr1 null mice. Neuron 37, 417-431 (2003).
    • (2003) Neuron , vol.37 , pp. 417-431
    • Miyashiro, K.Y.1
  • 27
    • 0035902466 scopus 로고    scopus 로고
    • A highly conserved protein family interacting with the fragile X mental retardation protein (FMRP) and displaying selective interactions with FMRP-related proteins FXR1P and FXR2P
    • Schenck, A., Bardoni, B., Moro, A., Bagni, C. & Mandel, J. L. A highly conserved protein family interacting with the fragile X mental retardation protein (FMRP) and displaying selective interactions with FMRP-related proteins FXR1P and FXR2P. Proc. Natl Acad. Sci. USA 98, 8844-8849 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8844-8849
    • Schenck, A.1    Bardoni, B.2    Moro, A.3    Bagni, C.4    Mandel, J.L.5
  • 28
    • 0026705442 scopus 로고
    • Concerted activities of the RNA recognition and the glycine-rich C-terminal domains of nucleolin are required for efficient complex formation with pre-ribosomal RNA
    • Ghisolfi, L., Kharrat, A., Joseph, G., Amalric, F. & Erard, M. Concerted activities of the RNA recognition and the glycine-rich C-terminal domains of nucleolin are required for efficient complex formation with pre-ribosomal RNA. Eur. J. Biochem. 209, 541-548 (1992).
    • (1992) Eur. J. Biochem. , vol.209 , pp. 541-548
    • Ghisolfi, L.1    Kharrat, A.2    Joseph, G.3    Amalric, F.4    Erard, M.5
  • 29
    • 0035977134 scopus 로고    scopus 로고
    • Drosophila fragile X-related gene regulates the MAP1B homolog Futsch to control synaptic structure and function
    • Zhang, Y. Q. et al. Drosophila fragile X-related gene regulates the MAP1B homolog Futsch to control synaptic structure and function. Cell 107, 591-603 (2001).
    • (2001) Cell , vol.107 , pp. 591-603
    • Zhang, Y.Q.1
  • 30
    • 2942715357 scopus 로고    scopus 로고
    • The fragile X-related gene affects the crawling behavior of Drosophila larvae by regulating the mRNA level of the DEG/ENaC protein pickpocket1
    • Xu, K. et al. The fragile X-related gene affects the crawling behavior of Drosophila larvae by regulating the mRNA level of the DEG/ENaC protein pickpocket1. Curr Biol. 14, 1025-1034 (2004).
    • (2004) Curr. Biol. , vol.14 , pp. 1025-1034
    • Xu, K.1
  • 31
    • 0345308602 scopus 로고    scopus 로고
    • Control of dendritic development by the Drosophila fragile X-related gene involves the small GTPase Rac1
    • Lee, A. et al. Control of dendritic development by the Drosophila fragile X-related gene involves the small GTPase Rac1. Development 130, 5543-5552 (2003).
    • (2003) Development , vol.130 , pp. 5543-5552
    • Lee, A.1
  • 32
    • 0033499661 scopus 로고    scopus 로고
    • Isolation of an FMRP-associated messenger ribonucleoprotein particle and identification of nucleolin and the fragile X-related proteins as components of the complex
    • Ceman, S., Brown, V. & Warren, S. T. Isolation of an FMRP-associated messenger ribonucleoprotein particle and identification of nucleolin and the fragile X-related proteins as components of the complex. Mol. Cell. Biol. 19, 7925-7932 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7925-7932
    • Ceman, S.1    Brown, V.2    Warren, S.T.3
  • 33
    • 0034731497 scopus 로고    scopus 로고
    • Identification of mouse YB1/p50 as a component of the FMRP-associated mRNP particle
    • Ceman, S., Nelson, R. & Warren, S. T. Identification of mouse YB1/p50 as a component of the FMRP-associated mRNP particle. Biochem. Blophys. Res. Commun. 279, 904-908 (2000).
    • (2000) Biochem. Blophys. Res. Commun. , vol.279 , pp. 904-908
    • Ceman, S.1    Nelson, R.2    Warren, S.T.3
  • 34
    • 0037020098 scopus 로고    scopus 로고
    • Identification of mRNA/protein (mRNP) complexes containing Purα, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motor
    • Ohashi, S. et al. Identification of mRNA/protein (mRNP) complexes containing Purα, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motor. J. Biol. Chem. 277, 37804-37810 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 37804-37810
    • Ohashi, S.1
  • 35
    • 0035079990 scopus 로고    scopus 로고
    • Pur alpha protein implicated in dendritic RNA transport interacts with ribosomes in neuronal cytoplasm
    • Li, Y. et al. Pur alpha protein implicated in dendritic RNA transport interacts with ribosomes in neuronal cytoplasm. Biol. Pharm. Bull. 24, 231-235 (2001).
    • (2001) Biol. Pharm. Bull. , vol.24 , pp. 231-235
    • Li, Y.1
  • 36
    • 0032952380 scopus 로고    scopus 로고
    • The mammalian staufen protein localizes to the somatodendritic domain of cultured hippocampal neurons: Implications for its involvement in mRNA transport
    • Kiebler, M. A. et al. The mammalian staufen protein localizes to the somatodendritic domain of cultured hippocampal neurons: implications for its involvement in mRNA transport. J. Neurosci. 19, 288-297 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 288-297
    • Kiebler, M.A.1
  • 37
    • 0036889389 scopus 로고    scopus 로고
    • Transport of fragile X mental retardation protein via granules in neurites of PC12 cells
    • De Diego Otero, Y. et al. Transport of fragile X mental retardation protein via granules in neurites of PC12 cells. Mol. Cell. Biol. 22, 8332-8341 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8332-8341
    • De Diego Otero, Y.1
  • 38
    • 4444285375 scopus 로고    scopus 로고
    • Visualization of RNA-protein interactions in living cells: FMRP and IMP1 interact on mRNAs
    • Rackham, O. & Brown, C. M. Visualization of RNA-protein interactions in living cells: FMRP and IMP1 interact on mRNAs. EMBO J. 23, 3346-3355 (2004).
    • (2004) EMBO J. , vol.23 , pp. 3346-3355
    • Rackham, O.1    Brown, C.M.2
  • 39
    • 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. & 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, 2648-2655 (2004).
    • (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
  • 40
    • 4143088149 scopus 로고    scopus 로고
    • Kinesin transports RNA: Isolation and characterization of an RNA-transporting granule
    • Kanai, Y., Dohmae, N. & Hirokawa, N. Kinesin transports RNA: isolation and characterization of an RNA-transporting granule. Neuron 43, 513-525 (2004).
    • (2004) Neuron , vol.43 , pp. 513-525
    • Kanai, Y.1    Dohmae, N.2    Hirokawa, N.3
  • 41
    • 0030760613 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is associated with poly(A)+ mRNA in actively translating polyribosomes
    • Corbin, F. et al. The fragile X mental retardation protein is associated with poly(A)+ mRNA in actively translating polyribosomes. Hum. Mol. Genet. 6, 1465-1472 (1997).
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1465-1472
    • Corbin, F.1
  • 42
    • 0030059545 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is associated with ribosomes
    • Khandjian, E. W., Corbin, F., Woerly, S. & Rousseau, F. The fragile X mental retardation protein is associated with ribosomes. Nature Genet. 12, 91-93 (1996).
    • (1996) Nature Genet. , vol.12 , pp. 91-93
    • Khandjian, E.W.1    Corbin, F.2    Woerly, S.3    Rousseau, F.4
  • 43
    • 4444238669 scopus 로고    scopus 로고
    • Biochemical evidence for the association of fragile X mental retardation protein with brain polyribosomal ribonucleoparticles
    • Khandjian, E. W. et al. Biochemical evidence for the association of fragile X mental retardation protein with brain polyribosomal ribonucleoparticles. Proc. Natl Acad. Sci. USA 101, 13357-13362 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13357-13362
    • Khandjian, E.W.1
  • 44
    • 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. & Darnell, R. B. Fragile X mental retardation protein is associated with translating polyribosomes in neuronal cells. J. Neurosci. 24, 9272-9276 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 9272-9276
    • Stefani, G.1    Fraser, C.E.2    Darnell, J.C.3    Darnell, R.B.4
  • 45
    • 7944238178 scopus 로고    scopus 로고
    • The Fragile X Protein Controls MAP1B Translation and Microtubule Stability in Brain Neuron Development
    • (in the press)
    • Lu, R. et al. The Fragile X Protein Controls MAP1B Translation and Microtubule Stability in Brain Neuron Development. Proc. Natl Acad. Sci. USA (in the press).
    • Proc. Natl. Acad. Sci. USA
    • Lu, R.1
  • 46
    • 0345492360 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is required for type-1 metabotropic glutamate receptor-dependent translation of PSD-95
    • Todd, P. K., Mack, K. J. & Malter, J. S. The fragile X mental retardation protein is required for type-1 metabotropic glutamate receptor-dependent translation of PSD-95. Proc. Natl Acad. Sci. USA 100, 14374-14378 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14374-14378
    • Todd, P.K.1    Mack, K.J.2    Malter, J.S.3
  • 47
    • 0347382502 scopus 로고    scopus 로고
    • Phosphorylation influences the translation state of FMRP-associated polyribosomes
    • Ceman, S. et al. Phosphorylation influences the translation state of FMRP-associated polyribosomes. Hum. Mol. Genet. 12, 3295-3305 (2003).
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3295-3305
    • Ceman, S.1
  • 48
    • 0036892046 scopus 로고    scopus 로고
    • Casein kinase II phosphorylates the fragile X mental retardation protein and modulates its biological properties
    • Siomi, M. C., Higashijima, K., Ishizuka, A. & Siomi, H. Casein kinase II phosphorylates the fragile X mental retardation protein and modulates its biological properties. Mol. Cell. Biol. 22, 8438-8447 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8438-8447
    • Siomi, M.C.1    Higashijima, K.2    Ishizuka, A.3    Siomi, H.4
  • 49
    • 0036792769 scopus 로고    scopus 로고
    • Fragile X-related protein and VIG associate with the RNA interference machinery
    • Caudy, A. A., Myers, M., Hannon, G. J. & Hammond, S. M. Fragile X-related protein and VIG associate with the RNA interference machinery. Genes Dev. 16, 2491-2496 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 2491-2496
    • Caudy, A.A.1    Myers, M.2    Hannon, G.J.3    Hammond, S.M.4
  • 50
    • 0036791671 scopus 로고    scopus 로고
    • A Drosophila fragile X protein interacts with components of RNAi and ribosomal proteins
    • Ishizuka, A., Siomi, M. C. & Siomi, H. A Drosophila fragile X protein interacts with components of RNAi and ribosomal proteins. Genes Dev. 16, 2497-2508 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 2497-2508
    • Ishizuka, A.1    Siomi, M.C.2    Siomi, H.3
  • 51
    • 3142615372 scopus 로고    scopus 로고
    • The RNAi revolution
    • Novina, C. D. & Sharp, P. A. The RNAi revolution. Nature 430, 161-164 (2004).
    • (2004) Nature , vol.430 , pp. 161-164
    • Novina, C.D.1    Sharp, P.A.2
  • 52
    • 0347444723 scopus 로고    scopus 로고
    • MicroRNAs: Genomics, biogenesis, mechanism, and function
    • Bartel, D. P. MicroRNAs: genomics, biogenesis, mechanism, and function. Cell 116, 281-297 (2004).
    • (2004) Cell , vol.116 , pp. 281-297
    • Bartel, D.P.1
  • 53
    • 3142729150 scopus 로고    scopus 로고
    • Distinct roles for Argonaute proteins in small RNA-directed RNA cleavage pathways
    • Okamura, K., Ishizuka, A., Siomi, H. & Siomi, M. C. Distinct roles for Argonaute proteins in small RNA-directed RNA cleavage pathways. Genes Dev. 18, 1655-1666 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 1655-1666
    • Okamura, K.1    Ishizuka, A.2    Siomi, H.3    Siomi, M.C.4
  • 54
    • 1642540373 scopus 로고    scopus 로고
    • Biochemical and genetic interaction between the fragile X mental retardation protein and the microRNA pathway
    • Jin, P. et al. Biochemical and genetic interaction between the fragile X mental retardation protein and the microRNA pathway. Nature Neurosci. 7, 113-117 (2004).
    • (2004) Nature Neurosci. , vol.7 , pp. 113-117
    • Jin, P.1
  • 55
    • 0037071888 scopus 로고    scopus 로고
    • Drosophila fragile X protein, DFXR, regulates neuronal morphology and function in the brain
    • Morales, J. et al. Drosophila fragile X protein, DFXR, regulates neuronal morphology and function in the brain. Neuron 34, 961-972 (2002).
    • (2002) Neuron , vol.34 , pp. 961-972
    • Morales, J.1
  • 56
    • 0037071905 scopus 로고    scopus 로고
    • Drosophila lacking dfmr1 activity show defects in circadian output and fail to maintain courtship interest
    • Dockendorff, T. C. et al. Drosophila lacking dfmr1 activity show defects in circadian output and fail to maintain courtship interest. Neuron 34, 973-984 (2002).
    • (2002) Neuron , vol.34 , pp. 973-984
    • Dockendorff, T.C.1
  • 57
    • 3042735950 scopus 로고    scopus 로고
    • Defective neuronal development in the mushroom bodies of Drosophila fragile X mental retardation 1 mutants
    • Michel, C. I., Kraft, R. & Restifo, L. L. Defective neuronal development in the mushroom bodies of Drosophila fragile X mental retardation 1 mutants. J. Neurosci. 24, 5798-5809 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 5798-5809
    • Michel, C.I.1    Kraft, R.2    Restifo, L.L.3
  • 58
    • 2942532624 scopus 로고    scopus 로고
    • The Drosophila fragile X-related gene regulates axoneme differentiation during spermatogenesis
    • Zhang, Y. Q. et al. The Drosophila fragile X-related gene regulates axoneme differentiation during spermatogenesis. Dev. Biol. 270, 290-307 (2004).
    • (2004) Dev. Biol. , vol.270 , pp. 290-307
    • Zhang, Y.Q.1
  • 59
    • 0034685813 scopus 로고    scopus 로고
    • Role for rapid dendritic protein synthesis in hippocampal mGluR-dependent long-term depression
    • Huber, K. M., Kayser, M. S. & Bear, M. F. Role for rapid dendritic protein synthesis in hippocampal mGluR-dependent long-term depression. Science 288, 1254-1257 (2000).
    • (2000) Science , vol.288 , pp. 1254-1257
    • Huber, K.M.1    Kayser, M.S.2    Bear, M.F.3
  • 60
    • 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. & Bear, M. F. Altered synaptic plasticity in a mouse model of fragile X mental retardation. Proc. Natl Acad. Sci. USA 99, 7746-7750 (2002 ).
    • (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
  • 61
    • 0037022346 scopus 로고    scopus 로고
    • Dendritic spines elongate after stimulation of group 1 metabotropic glutamate receptors in cultured hippocampal neurons
    • Vanderklish, P. W. & Edelman, G. M. Dendritic spines elongate after stimulation of group 1 metabotropic glutamate receptors in cultured hippocampal neurons. Proc. Natl Acad. Sci. USA 99, 1639-1644 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1639-1644
    • Vanderklish, P.W.1    Edelman, G.M.2
  • 62
    • 3042647610 scopus 로고    scopus 로고
    • The mGluR theory of fragile X mental retardation
    • Bear, M. F., Huber, K. M. & Warren, S. T. The mGluR theory of fragile X mental retardation. Trends Neurosci. 27, 370-377 (2004).
    • (2004) Trends Neurosci. , vol.27 , pp. 370-377
    • Bear, M.F.1    Huber, K.M.2    Warren, S.T.3
  • 63
    • 0032741429 scopus 로고    scopus 로고
    • Synergistic effect of histone hyperacetylation and DNA demethylation in the reactivation of the FMR1 gene
    • Chiurazzi, P. et al. Synergistic effect of histone hyperacetylation and DNA demethylation in the reactivation of the FMR1 gene. Hum. Mol. Genet. 8, 2317-2323 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2317-2323
    • Chiurazzi, P.1
  • 64
    • 0032905253 scopus 로고    scopus 로고
    • Acetylated histones are associated with FMR1 in normal but not fragile X-syndrome cells
    • Coffee, B., Zhang, F., Warren, S. T. & Reines, D. Acetylated histones are associated with FMR1 in normal but not fragile X-syndrome cells. Nature Genet. 22, 98-101 (1999).
    • (1999) Nature Genet. , vol.22 , pp. 98-101
    • Coffee, B.1    Zhang, F.2    Warren, S.T.3    Reines, D.4
  • 65
    • 2342517250 scopus 로고    scopus 로고
    • Regulation of heterochromatin by histone methylation and small RNAs
    • Grewal, S. I. & Rice, J. C. Regulation of heterochromatin by histone methylation and small RNAs. Curr. Opin. Cell Biol. 16, 230-238 (2004).
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 230-238
    • Grewal, S.I.1    Rice, J.C.2
  • 66
    • 0037009520 scopus 로고    scopus 로고
    • Two classes of short interfering RNA in RNA silencing
    • Hamilton, A., Voinnet, O., Chappell, L. & Baulcombe, D. Two classes of short interfering RNA in RNA silencing. EMBO J. 21, 4671-4679 (2002).
    • (2002) EMBO J. , vol.21 , pp. 4671-4679
    • Hamilton, A.1    Voinnet, O.2    Chappell, L.3    Baulcombe, D.4
  • 67
    • 0037474126 scopus 로고    scopus 로고
    • ARGONAUTE4 control of locus-specific siRNA accumulation and DNA and histone methylation
    • Zilberman, D., Cao, X. & Jacobsen, S. E. ARGONAUTE4 control of locus-specific siRNA accumulation and DNA and histone methylation. Science 299, 716-719 (2003).
    • (2003) Science , vol.299 , pp. 716-719
    • Zilberman, D.1    Cao, X.2    Jacobsen, S.E.3
  • 68
    • 0037183856 scopus 로고    scopus 로고
    • Establishment and maintenance of a heterochromatin domain
    • Hall, I. M. et al. Establishment and maintenance of a heterochromatin domain. Science 297, 2232-2237 (2002).
    • (2002) Science , vol.297 , pp. 2232-2237
    • Hall, I.M.1
  • 69
    • 0037072661 scopus 로고    scopus 로고
    • Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi
    • Volpe, T. A. et al. Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi. Science 297, 1833-1837 (2002).
    • (2002) Science , vol.297 , pp. 1833-1837
    • Volpe, T.A.1
  • 70
    • 0942279615 scopus 로고    scopus 로고
    • Heterochromatic silencing and HP1 localization in Drosophila are dependent on the RNAi machinery
    • Pal-Bhadra, M. et al. Heterochromatic silencing and HP1 localization in Drosophila are dependent on the RNAi machinery. Science 303, 669-672 (2004).
    • (2004) Science , vol.303 , pp. 669-672
    • Pal-Bhadra, M.1
  • 71
    • 0037072660 scopus 로고    scopus 로고
    • Small RNAs correspond to centromere heterochromatic repeats
    • Reinhart, B. J. & Bartel, D. P. Small RNAs correspond to centromere heterochromatic repeats. Science 297, 1831 (2002).
    • (2002) Science , vol.297 , pp. 1831
    • Reinhart, B.J.1    Bartel, D.P.2
  • 72
    • 0942279635 scopus 로고    scopus 로고
    • RNAi-mediated targeting of heterochromatin by the RITS complex
    • Verdel, A. et al. RNAi-mediated targeting of heterochromatin by the RITS complex. Science 303, 672-676 (2004).
    • (2004) Science , vol.303 , pp. 672-676
    • Verdel, A.1
  • 73
    • 0344442391 scopus 로고    scopus 로고
    • The fragile X syndrome repeats form RNA hairpins that do not activate the interferon-inducible protein kinase, PKR, but are cut by Dicer
    • Handa, V., Saha, T. & Usdin, K. The fragile X syndrome repeats form RNA hairpins that do not activate the interferon-inducible protein kinase, PKR, but are cut by Dicer. Nucleic Acids Res. 31, 6243-6248 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6243-6248
    • Handa, V.1    Saha, T.2    Usdin, K.3


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