메뉴 건너뛰기




Volumn 7, Issue , 2012, Pages 323-352

RNA dysregulation in diseases of motor neurons

Author keywords

Amyotrophic lateral sclerosis; IGHMBP2; RNP; SMN; Spinal muscular atrophy; TDP 43

Indexed keywords

ANGIOGENIN; COPPER ZINC SUPEROXIDE DISMUTASE; ELONGATOR PROTEIN 3; EPIDERMAL GROWTH FACTOR RECEPTOR 3; PROTEIN; RNA; RNA BINDING PROTEIN; SENATAXIN; SMALL NUCLEAR RIBONUCLEOPROTEIN; SURVIVAL MOTOR NEURON PROTEIN 1; SURVIVAL MOTOR NEURON PROTEIN 2; TAR DNA BINDING PROTEIN; TATA BINDING PROTEIN ASSOCIATED FACTOR; UNCLASSIFIED DRUG;

EID: 84856936343     PISSN: 15534006     EISSN: 15534014     Source Type: Book Series    
DOI: 10.1146/annurev-pathol-011110-130307     Document Type: Review
Times cited : (18)

References (206)
  • 1
    • 70350075024 scopus 로고    scopus 로고
    • Genetics of motor neuron disorders: New insights into pathogenic mechanisms
    • Dion PA, Daoud H, Rouleau GA. 2009. Genetics of motor neuron disorders: new insights into pathogenic mechanisms. Nat. Rev. Genet. 10:769-82
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 769-82
    • Dion, P.A.1    Daoud, H.2    Rouleau, G.A.3
  • 2
    • 0028797783 scopus 로고
    • Identification and characterization of a spinal muscular atrophy-determining gene
    • Lefebvre S, Burglen L, Reboullet S, Clermont O, Burlet P, et al. 1995. Identification and characterization of a spinal muscular atrophy-determining gene. Cell 80:155-65
    • (1995) Cell , vol.80 , pp. 155-65
    • Lefebvre, S.1    Burglen, L.2    Reboullet, S.3    Clermont, O.4    Burlet, P.5
  • 5
    • 77649114471 scopus 로고    scopus 로고
    • A degron created by SMN2 exon 7 skipping is a principal contributor to spinal muscular atrophy severity
    • Cho S, Dreyfuss G. 2010. A degron created by SMN2 exon 7 skipping is a principal contributor to spinal muscular atrophy severity. Genes Dev. 24:438-42
    • (2010) Genes Dev. , vol.24 , pp. 438-42
    • Cho, S.1    Dreyfuss, G.2
  • 6
    • 0242683460 scopus 로고    scopus 로고
    • Essential role for the tudor domain of SMN in spliceosomal U snRNP assembly: Implications for spinal muscular atrophy
    • Buhler D, Raker V, Luhrmann R, Fischer U. 1999. Essential role for the tudor domain of SMN in spliceosomal U snRNP assembly: implications for spinal muscular atrophy. Hum. Mol. Genet. 8:2351-57
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2351-57
    • Buhler, D.1    Raker, V.2    Luhrmann, R.3    Fischer, U.4
  • 7
    • 0033552589 scopus 로고    scopus 로고
    • Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems
    • Charroux B, Pellizzoni L, Perkinson RA, Shevchenko A, Mann M, Dreyfuss G. 1999. Gemin3: a novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems. J. Cell Biol. 147:1181-94
    • (1999) J. Cell Biol. , vol.147 , pp. 1181-94
    • Charroux, B.1    Pellizzoni, L.2    Perkinson, R.A.3    Shevchenko, A.4    Mann, M.5    Dreyfuss, G.6
  • 9
    • 0035476679 scopus 로고    scopus 로고
    • SMN interacts with a novel family of hnRNP and spliceosomal proteins
    • DOI 10.1093/emboj/20.19.5443
    • Mourelatos Z, Abel L, Yong J, Kataoka N, Dreyfuss G. 2001. SMN interacts with a novel family of hnRNP and spliceosomal proteins. EMBO J. 20:5443-52 (Pubitemid 32959464)
    • (2001) EMBO Journal , vol.20 , Issue.19 , pp. 5443-5452
    • Mourelatos, Z.1    Abel, L.2    Yong, J.3    Kataoka, N.4    Dreyfuss, G.5
  • 10
    • 11344265204 scopus 로고    scopus 로고
    • Molecular and functional analysis of intragenic SMN1 mutations in patients with spinal muscular atrophy
    • DOI 10.1002/humu.20111
    • Sun Y, Grimmler M, Schwarzer V, Schoenen F, Fischer U, Wirth B. 2005. Molecular and functional analysis of intragenic SMN1 mutations in patients with spinal muscular atrophy. Hum. Mutat. 25:64-71 (Pubitemid 40075915)
    • (2005) Human Mutation , vol.25 , Issue.1 , pp. 64-71
    • Sun, Y.1    Grimmler, M.2    Schwarzer, V.3    Schoenen, F.4    Fischer, U.5    Wirth, B.6
  • 12
    • 0029954338 scopus 로고    scopus 로고
    • A novel nuclear structure containing the survival of motor neurons protein
    • Liu Q, Dreyfuss G. 1996. A novel nuclear structure containing the survival of motor neurons protein. EMBO J. 15:3555-65 (Pubitemid 26239768)
    • (1996) EMBO Journal , vol.15 , Issue.14 , pp. 3555-3565
    • Liu, Q.1    Dreyfuss, G.2
  • 13
    • 0030931727 scopus 로고    scopus 로고
    • The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins
    • DOI 10.1016/S0092-8674(00)80367-0
    • Liu Q, Fischer U, Wang F, Dreyfuss G. 1997. The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins. Cell 90:1013-21 (Pubitemid 27408515)
    • (1997) Cell , vol.90 , Issue.6 , pp. 1013-1021
    • Liu, Q.1    Fischer, U.2    Wang, F.3    Dreyfuss, G.4
  • 14
    • 0030928716 scopus 로고    scopus 로고
    • The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis
    • DOI 10.1016/S0092-8674(00)80368-2
    • Fischer U, Liu Q, Dreyfuss G. 1997. The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis. Cell 90:1023-29 (Pubitemid 27408516)
    • (1997) Cell , vol.90 , Issue.6 , pp. 1023-1029
    • Fischer, U.1    Liu, Q.2    Dreyfuss, G.3
  • 15
    • 43049168361 scopus 로고    scopus 로고
    • SMN Deficiency Causes Tissue-Specific Perturbations in the Repertoire of snRNAs and Widespread Defects in Splicing
    • DOI 10.1016/j.cell.2008.03.031, PII S0092867408004601
    • Zhang Z, Lotti F, Dittmar K, Younis I, Wan L, et al. 2008. SMN deficiency causes tissue-specific perturbations in the repertoire of snRNAs and widespread defects in splicing. Cell 133:585-600 (Pubitemid 351636302)
    • (2008) Cell , vol.133 , Issue.4 , pp. 585-600
    • Zhang, Z.1    Lotti, F.2    Dittmar, K.3    Younis, I.4    Wan, L.5    Kasim, M.6    Dreyfuss, G.7
  • 16
    • 2142819496 scopus 로고    scopus 로고
    • Why do cells need an assembly machine for RNA-protein complexes?
    • DOI 10.1016/j.tcb.2004.03.010, PII S0962892404000844
    • Yong J, Wan L, Dreyfuss G. 2004. Why do cells need an assembly machine for RNA-protein complexes? Trends Cell Biol. 14:226-32 (Pubitemid 38591326)
    • (2004) Trends in Cell Biology , vol.14 , Issue.5 , pp. 226-232
    • Yong, J.1    Wan, L.2    Dreyfuss, G.3
  • 17
    • 77952575677 scopus 로고    scopus 로고
    • Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis
    • Yong J, Kasim M, Bachorik JL, Wan L, Dreyfuss G. 2010. Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis. Mol. Cell 38:551-62
    • (2010) Mol. Cell , vol.38 , pp. 551-62
    • Yong, J.1    Kasim, M.2    Bachorik, J.L.3    Wan, L.4    Dreyfuss, G.5
  • 18
    • 2242443509 scopus 로고    scopus 로고
    • Essential role for the SMN complex in the specificity of snRNP assembly
    • DOI 10.1126/science.1074962
    • Pellizzoni L, Yong J, Dreyfuss G. 2002. Essential role for the SMN complex in the specificity of snRNP assembly. Science 298:1775-79 (Pubitemid 35404118)
    • (2002) Science , vol.298 , Issue.5599 , pp. 1775-1779
    • Pellizzoni, L.1    Yong, J.2    Dreyfuss, G.3
  • 19
    • 34047148903 scopus 로고    scopus 로고
    • Chaperoning ribonucleoprotein biogenesis in health and disease
    • DOI 10.1038/sj.embor.7400941, PII 7400941
    • Pellizzoni L. 2007. Chaperoning ribonucleoprotein biogenesis in health and disease. EMBO Rep. 8:340-45 (Pubitemid 46511034)
    • (2007) EMBO Reports , vol.8 , Issue.4 , pp. 340-345
    • Pellizzoni, L.1
  • 20
    • 54549102220 scopus 로고    scopus 로고
    • An assembly chaperone collaborates with the SMN complex to generate spliceosomal snRNPs
    • Chari A, Golas MM, Klingenhager M, Neuenkirchen N, Sander B, et al. 2008. An assembly chaperone collaborates with the SMN complex to generate spliceosomal snRNPs. Cell 135:497-509
    • (2008) Cell , vol.135 , pp. 497-509
    • Chari, A.1    Golas, M.M.2    Klingenhager, M.3    Neuenkirchen, N.4    Sander, B.5
  • 24
    • 70350754456 scopus 로고    scopus 로고
    • Zebrafish survival motor neuron mutants exhibit presynaptic neuromuscular junction defects
    • Boon KL, Xiao S, McWhorterML, Donn T, Wolf-Saxon E, et al. 2009. Zebrafish survival motor neuron mutants exhibit presynaptic neuromuscular junction defects. Hum. Mol. Genet. 18:3615-25
    • (2009) Hum. Mol. Genet , vol.18 , pp. 3615-25
    • Boon, K.L.1    Xiao, S.2    McWhorterml Donn, T.3    Wolf-Saxon, E.4
  • 25
    • 57649207934 scopus 로고    scopus 로고
    • Deletion of smn-1, the Caenorhabditis elegans ortholog of the spinalmuscular atrophy gene, results in locomotor dysfunction and reduced lifespan
    • Briese M, Esmaeili B, Fraboulet S, Burt EC, Christodoulou S, et al. 2009. Deletion of smn-1, the Caenorhabditis elegans ortholog of the spinalmuscular atrophy gene, results in locomotor dysfunction and reduced lifespan. Hum. Mol. Genet. 18:97-104
    • (2009) Hum. Mol. Genet , vol.18 , pp. 97-104
    • Briese, M.1    Esmaeili, B.2    Fraboulet, S.3    Burt, E.C.4    Christodoulou, S.5
  • 26
    • 29144463310 scopus 로고    scopus 로고
    • Spinal muscular atrophy: A deficiency in a ubiquitous protein; a motor neuron-specific disease
    • DOI 10.1016/j.neuron.2005.12.001, PII S0896627305010111
    • Monani UR. 2005. Spinal muscular atrophy: a deficiency in a ubiquitous protein; amotor neuron-specific disease. Neuron 48:885-96 (Pubitemid 41814694)
    • (2005) Neuron , vol.48 , Issue.6 , pp. 885-896
    • Monani, U.R.1
  • 27
    • 48249145306 scopus 로고    scopus 로고
    • Reduced SMN protein impairs maturation of the neuromuscular junctions in mouse models of spinal muscular atrophy
    • Kariya S, Park GH, Maeno-Hikichi Y, Leykekhman O, Lutz C, et al. 2008. Reduced SMN protein impairs maturation of the neuromuscular junctions in mouse models of spinal muscular atrophy. Hum. Mol. Genet. 17:2552-69
    • (2008) Hum. Mol. Genet , vol.17 , pp. 2552-69
    • Kariya, S.1    Park, G.H.2    Maeno-Hikichi, Y.3    Leykekhman, O.4    Lutz, C.5
  • 29
    • 41549119007 scopus 로고    scopus 로고
    • Ribonucleoprotein assembly defects correlate with spinal muscular atrophy severity and preferentially affect a subset of spliceosomal snRNPs
    • Gabanella F, Butchbach ME, Saieva L, Carissimi C, Burghes AH, Pellizzoni L. 2007. Ribonucleoprotein assembly defects correlate with spinal muscular atrophy severity and preferentially affect a subset of spliceosomal snRNPs. PLoS ONE 2:e921
    • (2007) PLoS ONE , vol.2
    • Gabanella, F.1    Butchbach, M.E.2    Saieva, L.3    Carissimi, C.4    Burghes, A.H.5    Pellizzoni, L.6
  • 32
    • 63149150048 scopus 로고    scopus 로고
    • IGHMBP2 is a ribosomeassociated helicase inactive in the neuromuscular disorder distal SMA type 1 (DSMA1)
    • Guenther UP, Handoko L, Laggerbauer B, Jablonka S, Chari A, et al. 2009. IGHMBP2 is a ribosomeassociated helicase inactive in the neuromuscular disorder distal SMA type 1 (DSMA1). Hum. Mol. Genet. 18:1288-300
    • (2009) Hum. Mol. Genet , vol.18 , pp. 1288-300
    • Guenther, U.P.1    Handoko, L.2    Laggerbauer, B.3    Jablonka, S.4    Chari, A.5
  • 33
    • 0026091768 scopus 로고
    • A recombinant cDNA derived from human brain encodes a DNA binding protein that stimulates transcription of the human neurotropic virus JCV
    • Kerr D, Khalili K. 1991. A recombinant cDNA derived from human brain encodes a DNA binding protein that stimulates transcription of the human neurotropic virus JCV. J. Biol. Chem. 266:15876-81 (Pubitemid 21907739)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.24 , pp. 15876-15881
    • Kerr, D.1    Khalili, K.2
  • 34
    • 0027236550 scopus 로고
    • The human Sμbp-2, a DNA-binding protein specific to the single-stranded guanine-rich sequence related to the immunoglobulin μ chain switch region
    • Fukita Y, Mizuta TR, Shirozu M, Ozawa K, Shimizu A, Honjo T. 1993. The human Sbp-2, a DNAbinding protein specific to the single-stranded guanine-rich sequence related to the immunoglobulin α chain switch region. J. Biol. Chem. 268:17463-70 (Pubitemid 23236989)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.23 , pp. 17463-17470
    • Fukita, Y.1    Mizuta, T.-R.2    Shirozu, M.3    Ozawa, K.4    Shimizu, A.5    Honjo, T.6
  • 38
    • 0032408306 scopus 로고    scopus 로고
    • Identification of the mouse neuromuscular degeneration gene and mapping of a second site suppressor allele
    • DOI 10.1016/S0896-6273(00)80652-2
    • Cox GA, Mahaffey CL, Frankel WN. 1998. Identification of the mouse neuromuscular degeneration gene and mapping of a second site suppressor allele. Neuron 21:1327-37 (Pubitemid 29022535)
    • (1998) Neuron , vol.21 , Issue.6 , pp. 1327-1337
    • Cox, G.A.1    Mahaffey, C.L.2    Frankel, W.N.3
  • 39
    • 2942709863 scopus 로고    scopus 로고
    • Transgenic rescue of neurogenic atrophy in the nmd mouse reveals a role for Ighmbp2 in dilated cardiomyopathy
    • DOI 10.1093/hmg/ddh129
    • Maddatu TP, Garvey SM, Schroeder DG, Hampton TG, Cox GA. 2004. Transgenic rescue of neurogenic atrophy in the nmd mouse reveals a role for Ighmbp2 in dilated cardiomyopathy. Hum. Mol. Genet. 13:1105-15 (Pubitemid 38786993)
    • (2004) Human Molecular Genetics , vol.13 , Issue.11 , pp. 1105-1115
    • Maddatu, T.P.1    Garvey, S.M.2    Schroeder, D.G.3    Hampton, T.G.4    Cox, G.A.5
  • 40
    • 0028338608 scopus 로고
    • Lethal congenital contracture syndrome: Further delineation and genetic aspects
    • Vuopala K, Herva R. 1994. Lethal congenital contracture syndrome: further delineation and genetic aspects. J. Med. Genet. 31:521-27 (Pubitemid 24226397)
    • (1994) Journal of Medical Genetics , vol.31 , Issue.7 , pp. 521-527
    • Vuopala, K.1    Herva, R.2
  • 43
    • 34548202722 scopus 로고    scopus 로고
    • Lethal congenital contractural syndrome type 2 (LCCS2) is caused by a mutation in ERBB3 (Her3), a modulator of the phosphatidylinositol-3-kinase/akt pathway
    • DOI 10.1086/520770
    • Narkis G, Ofir R, Manor E, Landau D, Elbedour K, Birk OS. 2007. Lethal congenital contractural syndrome type 2 (LCCS2) is caused by a mutation inERBB3(Her3), a modulator of the phosphatidylinositol- 3-kinase/Akt pathway. Am. J. Hum. Genet. 81:589-95 (Pubitemid 47330217)
    • (2007) American Journal of Human Genetics , vol.81 , Issue.3 , pp. 589-595
    • Narkis, G.1    Ofir, R.2    Manor, E.3    Landau, D.4    Elbedour, K.5    Birk, O.S.6
  • 45
    • 0029745374 scopus 로고    scopus 로고
    • An RNA-export mediator with an essential nuclear export signal
    • DOI 10.1038/383357a0
    • Murphy R, Wente SR. 1996. An RNA-export mediator with an essential nuclear export signal. Nature 383:357-60 (Pubitemid 26321769)
    • (1996) Nature , vol.383 , Issue.6598 , pp. 357-360
    • Murphy, R.1    Wente, S.R.2
  • 47
    • 0037417412 scopus 로고    scopus 로고
    • An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export
    • DOI 10.1083/jcb.200211081
    • Kendirgi F, Barry DM, Griffis ER, Powers MA, Wente SR. 2003. An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export. J. Cell Biol. 160:1029-40 (Pubitemid 36443872)
    • (2003) Journal of Cell Biology , vol.160 , Issue.7 , pp. 1029-1040
    • Kendirgi, F.1    Barry, D.M.2    Griffis, E.R.3    Powers, M.A.4    Wente, S.R.5
  • 48
    • 33745736445 scopus 로고    scopus 로고
    • Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export
    • Alcazar-Roman AR, Tran EJ, Guo S, Wente SR. 2006. Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export. Nat. Cell Biol. 8:711-16
    • (2006) Nat. Cell Biol , vol.8 , pp. 711-16
    • Alcazar-Roman, A.R.1    Tran, E.J.2    Guo, S.3    Wente, S.R.4
  • 49
    • 33745742173 scopus 로고    scopus 로고
    • Activation of the DExD/Hbox protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export
    • Weirich CS, Erzberger JP, Flick JS, Berger JM, Thorner J, Weis K. 2006. Activation of the DExD/Hbox protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export. Nat. Cell Biol. 8:668-76
    • (2006) Nat. Cell Biol , vol.8 , pp. 668-76
    • Weirich, C.S.1    Erzberger, J.P.2    Flick, J.S.3    Berger, J.M.4    Thorner, J.5    Weis, K.6
  • 50
    • 79954598438 scopus 로고    scopus 로고
    • Aconserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 in mRNA export
    • Montpetit B, Thomsen ND, Helmke KJ, Seeliger MA, Berger JM, Weis K. 2011.Aconserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 in mRNA export. Nature 472:238-42
    • (2011) Nature , vol.472 , pp. 238-42
    • Montpetit, B.1    Thomsen, N.D.2    Helmke, K.J.3    Ma, S.4    Berger, J.M.5    Weis, K.6
  • 51
    • 34548624258 scopus 로고    scopus 로고
    • Neural precursor cells from a fatal human motoneuron disease differentiate despite aberrant gene expression
    • Pakkasjarvi N, Kerosuo L, Nousiainen H, Gentile M, Saharinen J, et al. 2007. Neural precursor cells from a fatal human motoneuron disease differentiate despite aberrant gene expression. Dev. Neurobiol. 67:270-84
    • (2007) Dev. Neurobiol , vol.67 , pp. 270-84
    • Pakkasjarvi, N.1    Kerosuo, L.2    Nousiainen, H.3    Gentile, M.4    Saharinen, J.5
  • 52
    • 0035516124 scopus 로고    scopus 로고
    • From Charcot to Lou Gehrig: Deciphering selective motor neuron death in ALS
    • DOI 10.1038/35097565
    • Cleveland DW, Rothstein JD. 2001. From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat. Rev. Neurosci. 2:806-19 (Pubitemid 33674062)
    • (2001) Nature Reviews Neuroscience , vol.2 , Issue.11 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 53
    • 60849093466 scopus 로고    scopus 로고
    • Current hypotheses for the underlying biology of amyotrophic lateral sclerosis
    • Rothstein JD. 2009. Current hypotheses for the underlying biology of amyotrophic lateral sclerosis. Ann. Neurol. 65(Suppl. 1):3-9
    • (2009) Ann. Neurol , vol.65 , Issue.SUPPL. 1 , pp. 3-9
    • Rothstein, J.D.1
  • 54
    • 77949897022 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis and frontotemporal lobar degeneration: A spectrum of TDP-43 proteinopathies
    • Geser F, Lee VM, Trojanowski JQ. 2010. Amyotrophic lateral sclerosis and frontotemporal lobar degeneration: a spectrum of TDP-43 proteinopathies. Neuropathology 30:103-12
    • (2010) Neuropathology , vol.30 , pp. 103-12
    • Geser, F.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 55
    • 74049164709 scopus 로고    scopus 로고
    • Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond
    • Ilieva H, Polymenidou M, Cleveland DW. 2009. Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond. J. Cell Biol. 187:761-72
    • (2009) J. Cell Biol , vol.187 , pp. 761-72
    • Ilieva, H.1    Polymenidou, M.2    Cleveland, D.W.3
  • 56
    • 0027164824 scopus 로고
    • Erratum: Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis (Nature (1993) 362 (59-62))
    • RosenDR. 1993. Mutations inCu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 364:362 (Pubitemid 23265284)
    • (1993) Nature , vol.364 , Issue.6435 , pp. 362
    • Rosen, D.R.1
  • 59
    • 77957317483 scopus 로고    scopus 로고
    • Themultiple roles of TDP-43 in pre-mRNA processing and gene expression regulation
    • Buratti E, Baralle FE. 2010. Themultiple roles of TDP-43 in pre-mRNA processing and gene expression regulation. RNA Biol. 7:420-29
    • (2010) RNA Biol. , vol.7 , pp. 420-29
    • Buratti, E.1    Baralle, F.E.2
  • 61
    • 0029257498 scopus 로고
    • Neuromuscular degeneration (NMD): A mutation on mouse chromosome 19 that causes motor neuron degeneration
    • Cook SA, Johnson KR, Bronson RT, Davisson MT. 1995. Neuromuscular degeneration (NMD): a mutation on mouse chromosome 19 that causes motor neuron degeneration. Mamm. Genome 6:187-91
    • (1995) Mamm. Genome , vol.6 , pp. 187-91
    • Cook, S.A.1    Johnson, K.R.2    Bronson, R.T.3    Davisson, M.T.4
  • 62
    • 27844514227 scopus 로고    scopus 로고
    • TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: An important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
    • DOI 10.1074/jbc.M505557200
    • Buratti E, Brindisi A, Giombi M, Tisminetzky S, Ayala YM, Baralle FE. 2005. TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing. J. Biol. Chem. 280:37572-84 (Pubitemid 41642366)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.45 , pp. 37572-37584
    • Buratti, E.1    Brindisi, A.2    Giombi, M.3    Tisminetzky, S.4    Ayala, Y.M.5    Baralle, F.E.6
  • 66
    • 41949100148 scopus 로고    scopus 로고
    • TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: A genetic and histopathological analysis
    • Van Deerlin VM, Leverenz JB, Bekris LM, Bird TD, Yuan W, et al. 2008. TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis. Lancet Neurol. 7:409-16
    • (2008) Lancet Neurol , vol.7 , pp. 409-16
    • Van Deerlin, V.M.1    Leverenz, J.B.2    Bekris, L.M.3    Bird, T.D.4    Yuan, W.5
  • 67
    • 62149141328 scopus 로고    scopus 로고
    • Rethinking ALS: The FUS about TDP-43
    • Lagier-Tourenne C, Cleveland DW. 2009. Rethinking ALS: the FUS about TDP-43. Cell 136:1001-4
    • (2009) Cell , vol.136 , pp. 1001-4
    • Lagier-Tourenne, C.1    Cleveland, D.W.2
  • 68
    • 59549094064 scopus 로고    scopus 로고
    • Structural determinants of the cellular localization and shuttling of TDP-43
    • Ayala YM, Zago P, D'Ambrogio A, Xu YF, Petrucelli L, et al. 2008. Structural determinants of the cellular localization and shuttling of TDP-43. J. Cell Sci. 121:3778-85
    • (2008) J. Cell Sci , vol.121 , pp. 3778-85
    • Ayala, Y.M.1    Zago, P.2    D'ambrogio, A.3    Xu, Y.F.4    Petrucelli, L.5
  • 72
    • 47949099336 scopus 로고    scopus 로고
    • Maturation process of TDP-43- positive neuronal cytoplasmic inclusions in amyotrophic lateral sclerosis with and without dementia
    • Mori F, Tanji K, Zhang HX, Nishihira Y, Tan CF, et al. 2008. Maturation process of TDP-43- positive neuronal cytoplasmic inclusions in amyotrophic lateral sclerosis with and without dementia. Acta Neuropathol. 116:193-203
    • (2008) Acta Neuropathol , vol.116 , pp. 193-203
    • Mori, F.1    Tanji, K.2    Zhang, H.X.3    Nishihira, Y.4    Tan, C.F.5
  • 73
    • 75949105684 scopus 로고    scopus 로고
    • TDP-43 redistribution is an early event in sporadic amyotrophic lateral sclerosis
    • Giordana MT, Piccinini M, Grifoni S, De Marco G, Vercellino M, et al. 2010. TDP-43 redistribution is an early event in sporadic amyotrophic lateral sclerosis. Brain Pathol. 20:351-60
    • (2010) Brain Pathol. , vol.20 , pp. 351-60
    • Giordana, M.T.1    Piccinini, M.2    Grifoni, S.3    De Marco, G.4    Vercellino, M.5
  • 74
    • 67650432367 scopus 로고    scopus 로고
    • Proteolytic processing of TAR DNA binding protein 43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin
    • Dormann D, Capell A, Carlson AM, Shankaran SS, Rodde R, et al. 2009. Proteolytic processing of TAR DNA binding protein 43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin. J. Neurochem. 110:1082-94
    • (2009) J. Neurochem , vol.110 , pp. 1082-94
    • Dormann, D.1    Capell, A.2    Carlson, A.M.3    Shankaran, S.S.4    Rodde, R.5
  • 76
    • 79956304001 scopus 로고    scopus 로고
    • A "two hit" hypothesis for inclusion formation by carboxy terminal fragments of TDP-43 linked to RNAdepletion and impaired microtubule dependent transport
    • Pesiridis GS, Tripathy K, Tanik S, Trojanowski JQ, Lee VM. 2011. A "two hit" hypothesis for inclusion formation by carboxy terminal fragments of TDP-43 linked to RNAdepletion and impaired microtubule dependent transport. J. Biol. Chem. 286:18845-55
    • (2011) J. Biol. Chem , vol.286 , pp. 18845-55
    • Pesiridis, G.S.1    Tripathy, K.2    Tanik, S.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 77
    • 79960160835 scopus 로고    scopus 로고
    • Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing
    • Che MX, Jiang YJ, Xie YY, Jiang LL, Hu HY. 2011. Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing. FASEB J. 25:2344-53
    • (2011) FASEB J. , vol.25 , pp. 2344-53
    • Che, M.X.1    Jiang, Y.J.2    Xie, Y.Y.3    Jiang, L.L.4    Hu, H.Y.5
  • 78
    • 74949135753 scopus 로고    scopus 로고
    • Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis
    • Barmada SJ, Skibinski G, Korb E, Rao EJ, Wu JY, Finkbeiner S. 2010. Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis. J. Neurosci. 30:639-49
    • (2010) J. Neurosci. , vol.30 , pp. 639-49
    • Barmada, S.J.1    Skibinski, G.2    Korb, E.3    Rao, E.J.4    Wu, J.Y.5    Finkbeiner, S.6
  • 79
    • 79551523377 scopus 로고    scopus 로고
    • Dysregulation of the ALSassociated gene TDP-43 leads to neuronal death and degeneration in mice
    • Igaz LM, Kwong LK, Lee EB, Chen-Plotkin A, Swanson E, et al. 2011. Dysregulation of the ALSassociated gene TDP-43 leads to neuronal death and degeneration in mice. J. Clin. Investig. 121:726-38
    • (2011) J. Clin. Investig. , vol.121 , pp. 726-38
    • Igaz, L.M.1    Kwong, L.K.2    Lee, E.B.3    Chen-Plotkin, A.4    Swanson, E.5
  • 80
    • 76149120427 scopus 로고    scopus 로고
    • Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery
    • Freibaum BD, Chitta RK, High AA, Taylor JP. 2010. Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery. J. Proteome Res. 9:1104-20
    • (2010) J. Proteome Res. , vol.9 , pp. 1104-20
    • Freibaum, B.D.1    Chitta, R.K.2    High, A.A.3    Taylor, J.P.4
  • 81
    • 78651408754 scopus 로고    scopus 로고
    • Identification of neuronal RNA targets of TDP-43-containing ribonucleoprotein complexes
    • Sephton CF, Cenik C, Kucukural A, Dammer EB, Cenik B, et al. 2011. Identification of neuronal RNA targets of TDP-43-containing ribonucleoprotein complexes. J. Biol. Chem. 286:1204-15
    • (2011) J. Biol. Chem. , vol.286 , pp. 1204-15
    • Sephton, C.F.1    Cenik, C.2    Kucukural, A.3    Dammer, E.B.4    Cenik, B.5
  • 82
    • 77956155218 scopus 로고    scopus 로고
    • Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS
    • Elden AC, Kim HJ, Hart MP, Chen-Plotkin AS, Johnson BS, et al. 2010. Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS. Nature 466:1069-75
    • (2010) Nature , vol.466 , pp. 1069-75
    • Elden, A.C.1    Kim, H.J.2    Hart, M.P.3    Chen-Plotkin, A.S.4    Johnson, B.S.5
  • 83
    • 54249100481 scopus 로고    scopus 로고
    • TDP-43: An emerging new player in neurodegenerative diseases
    • Wang IF, Wu LS, Shen CK. 2008. TDP-43: an emerging new player in neurodegenerative diseases. Trends Mol. Med. 14:479-85
    • (2008) Trends Mol. Med , vol.14 , pp. 479-85
    • Wang, I.F.1    Wu, L.S.2    Shen, C.K.3
  • 84
    • 70349292075 scopus 로고    scopus 로고
    • Cytosolic TDP-43 expression following axotomy is associated with caspase 3 activation in NFL-/- mice: Support for a role for TDP-43 in the physiological response to neuronal injury
    • Moisse K, Mepham J, Volkening K, Welch I, Hill T, Strong MJ. 2009. Cytosolic TDP-43 expression following axotomy is associated with caspase 3 activation in NFL-/- mice: support for a role for TDP-43 in the physiological response to neuronal injury. Brain Res. 1296:176-86
    • (2009) Brain Res , vol.1296 , pp. 176-86
    • Moisse, K.1    Mepham, J.2    Volkening, K.3    Welch, I.4    Hill, T.5    Strong, M.J.6
  • 85
    • 70449523111 scopus 로고    scopus 로고
    • Axonal ligation induces transient redistribution of TDP-43 in brainstem motor neurons
    • Sato T, Takeuchi S, Saito A, DingW, Bamba H, et al. 2009. Axonal ligation induces transient redistribution of TDP-43 in brainstem motor neurons. Neuroscience 164:1565-78
    • (2009) Neuroscience , vol.164 , pp. 1565-78
    • Sato, T.1    Takeuchi, S.2    Saito, A.3    Ding, W.4    Bamba, H.5
  • 86
    • 73949134014 scopus 로고    scopus 로고
    • TarDNAbinding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS)
    • Volkening K, Leystra-Lantz C, Yang W, Jaffee H, Strong MJ. 2009. TarDNAbinding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS). Brain Res. 1305:168-82
    • (2009) Brain Res , vol.1305 , pp. 168-82
    • Volkening, K.1    Leystra-Lantz, C.2    Yang, W.3    Jaffee, H.4    Strong, M.J.5
  • 87
    • 71049166754 scopus 로고    scopus 로고
    • The evidence for altered RNA metabolism in amyotrophic lateral sclerosis (ALS)
    • Strong MJ. 2010. The evidence for altered RNA metabolism in amyotrophic lateral sclerosis (ALS). J. Neurol. Sci. 288:1-12
    • (2010) J. Neurol. Sci. , vol.288 , pp. 1-12
    • Strong, M.J.1
  • 88
    • 33845900214 scopus 로고    scopus 로고
    • 14-3-3 protein binds to the low molecular weight neurofilament (NFL) mRNA 3′ UTR
    • DOI 10.1016/j.mcn.2006.10.001, PII S1044743106002132
    • Ge WW, Volkening K, Leystra-Lantz C, Jaffe H, Strong MJ. 2007. 14-3-3 protein binds to the low molecular weight neurofilament (NFL) mRNA 3′ UTR. Mol. Cell. Neurosci. 34:80-87 (Pubitemid 46026930)
    • (2007) Molecular and Cellular Neuroscience , vol.34 , Issue.1 , pp. 80-87
    • Ge, W.-w.1    Volkening, K.2    Leystra-Lantz, C.3    Jaffe, H.4    Strong, M.J.5
  • 89
    • 38449102667 scopus 로고    scopus 로고
    • Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
    • DOI 10.2741/2727
    • Buratti E, Baralle FE. 2008. Multiple roles ofTDP-43 in gene expression, splicing regulation, and human disease. Front. Biosci. 13:867-78 (Pubitemid 351594732)
    • (2008) Frontiers in Bioscience , vol.13 , Issue.3 , pp. 867-878
    • Buratti, E.1    Baralle, F.E.2
  • 90
    • 0344256486 scopus 로고    scopus 로고
    • Structural diversity and functional implications of the eukaryotic TDP gene family
    • DOI 10.1016/S0888-7543(03)00214-3
    • Wang HY, Wang IF, Bose J, Shen CK. 2004. Structural diversity and functional implications of the eukaryotic TDP gene family. Genomics 83:130-39 (Pubitemid 37518267)
    • (2004) Genomics , vol.83 , Issue.1 , pp. 130-139
    • Wang, H.-Y.1    Wang, I.-F.2    Bose, J.3    Shen, C.-K.J.4
  • 92
    • 51449107580 scopus 로고    scopus 로고
    • P68 RNA helicase (DDX5) alters activity of cis- and trans-acting factors of the alternative splicing of H-Ras
    • Camats M, Guil S, Kokolo M, Bach-Elias M. 2008. P68 RNA helicase (DDX5) alters activity of cis- and trans-acting factors of the alternative splicing of H-Ras. PLoS ONE 3:e2926
    • (2008) PLoS ONE , vol.3
    • Camats, M.1    Guil, S.2    Kokolo, M.3    Bach-Elias, M.4
  • 93
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • Buratti E, Baralle FE. 2001. Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J. Biol. Chem. 276:36337-43
    • (2001) J. Biol. Chem , vol.276 , pp. 36337-43
    • Buratti, E.1    Baralle, F.E.2
  • 94
    • 27744554553 scopus 로고    scopus 로고
    • Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene
    • DOI 10.1093/nar/gki897
    • Mercado PA, Ayala YM, Romano M, Buratti E, Baralle FE. 2005. Depletion of TDP43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene. Nucleic Acids Res. 33:6000-10 (Pubitemid 41742619)
    • (2005) Nucleic Acids Research , vol.33 , Issue.18 , pp. 6000-6010
    • Mercado, P.A.1    Ayala, Y.M.2    Romano, M.3    Buratti, E.4    Baralle, F.E.5
  • 95
    • 32344435621 scopus 로고    scopus 로고
    • TDP43 depletion rescues aberrant CFTR exon 9 skipping
    • DOI 10.1016/j.febslet.2006.01.052, PII S0014579306001050
    • Ayala YM, Pagani F, Baralle FE. 2006. TDP43 depletion rescues aberrant CFTR exon 9 skipping. FEBS Lett. 580:1339-44 (Pubitemid 43221997)
    • (2006) FEBS Letters , vol.580 , Issue.5 , pp. 1339-1344
    • Ayala, Y.M.1    Pagani, F.2    Baralle, F.E.3
  • 96
    • 57649174592 scopus 로고    scopus 로고
    • TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing
    • Bose JK, Wang IF, Hung L, Tarn WY, Shen CK. 2008. TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing. J. Biol. Chem. 283:28852-59
    • (2008) J. Biol. Chem , vol.283 , pp. 28852-59
    • Bose, J.K.1    Wang, I.F.2    Hung, L.3    Tarn, W.Y.4    Shen, C.K.5
  • 98
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • Johnson BS, Snead D, Lee JJ, McCaffery JM, Shorter J, Gitler AD. 2009. TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J. Biol. Chem. 284:20329-39
    • (2009) J. Biol. Chem , vol.284 , pp. 20329-39
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3    McCaffery, J.M.4    Shorter, J.5    Gitler, A.D.6
  • 99
  • 100
    • 77649269011 scopus 로고    scopus 로고
    • TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration
    • Wils H, Kleinberger G, Janssens J, Pereson S, Joris G, et al. 2010. TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration. Proc. Natl. Acad. Sci. USA 107:3858-63
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 3858-63
    • Wils, H.1    Kleinberger, G.2    Janssens, J.3    Pereson, S.4    Joris, G.5
  • 102
    • 77957918535 scopus 로고    scopus 로고
    • TDP-43-mediated neuron loss in vivo requires RNA-binding activity
    • Voigt A, Herholz D, Fiesel FC, Kaur K, Muller D, et al. 2010. TDP-43-mediated neuron loss in vivo requires RNA-binding activity. PLoS ONE 5:e12247
    • (2010) PLoS ONE , vol.5
    • Voigt, A.1    Herholz, D.2    Fiesel, F.C.3    Kaur, K.4    Muller, D.5
  • 103
    • 77950421249 scopus 로고    scopus 로고
    • Transgenic ratmodel of neurodegeneration caused by mutation in the TDP gene
    • Zhou H, Huang C, Chen H, Wang D, Landel CP, et al. 2010. Transgenic ratmodel of neurodegeneration caused by mutation in the TDP gene. PLoS Genet. 6:e1000887
    • (2010) PLoS Genet , vol.6
    • Zhou, H.1    Huang, C.2    Chen, H.3    Wang, D.4    Landel, C.P.5
  • 104
    • 77958022745 scopus 로고    scopus 로고
    • Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice
    • Shan X, Chiang PM, Price DL, Wong PC. 2010. Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice. Proc. Natl. Acad. Sci. USA 107:16325-30
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 16325-30
    • Shan, X.1    Chiang, P.M.2    Price, D.L.3    Wong, P.C.4
  • 107
    • 67749132423 scopus 로고    scopus 로고
    • Argonaute HITS-CLIP decodes microRNA-mRNA interaction maps
    • Chi SW, Zang JB, Mele A, Darnell RB. 2009. Argonaute HITS-CLIP decodes microRNA-mRNA interaction maps. Nature 460:479-86
    • (2009) Nature , vol.460 , pp. 479-86
    • Chi, S.W.1    Zang, J.B.2    Mele, A.3    Darnell, R.B.4
  • 108
    • 0021219155 scopus 로고
    • Characterization of heterogeneous nuclear RNA-protein complexes in vivo with monoclonal antibodies
    • Dreyfuss G, Choi YD, Adam SA. 1984. Characterization of heterogeneous nuclear RNA-protein complexes in vivo with monoclonal antibodies. Mol. Cell. Biol. 4:1104-14 (Pubitemid 14050727)
    • (1984) Molecular and Cellular Biology , vol.4 , Issue.6 , pp. 1104-1114
    • Dreyfuss, G.1    Yang Do Choi2    Adam, S.A.3
  • 109
    • 0242497663 scopus 로고    scopus 로고
    • CLIP Identifies Nova-Regulated RNA Networks in the Brain
    • DOI 10.1126/science.1090095
    • Ule J, Jensen KB, Ruggiu M, Mele A, Ule A, Darnell RB. 2003. CLIP identifies Nova-regulated RNA networks in the brain. Science 302:1212-15 (Pubitemid 37421026)
    • (2003) Science , vol.302 , Issue.5648 , pp. 1212-1215
    • Ule, J.1    Jensen, K.B.2    Ruggiu, M.3    Mele, A.4    Ule, A.5    Darnell, R.B.6
  • 110
    • 57749195712 scopus 로고    scopus 로고
    • RNA-seq: A revolutionary tool for transcriptomics
    • Wang Z, Gerstein M, Snyder M. 2009. RNA-seq: a revolutionary tool for transcriptomics. Nat. Rev. Genet. 10:57-63
    • (2009) Nat. Rev. Genet , vol.10 , pp. 57-63
    • Wang, Z.1    Gerstein, M.2    Snyder, M.3
  • 111
    • 79953185674 scopus 로고    scopus 로고
    • Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
    • Polymenidou M, Lagier-Tourenne C, Hutt KR, Huelga SC, Moran J, et al. 2011. Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43. Nat. Neurosci. 14:459-68
    • (2011) Nat. Neurosci. , vol.14 , pp. 459-68
    • Polymenidou, M.1    Lagier-Tourenne, C.2    Hutt, K.R.3    Huelga, S.C.4    Moran, J.5
  • 112
    • 79953180492 scopus 로고    scopus 로고
    • Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
    • Tollervey JR, Curk T, Rogelj B, Briese M, Cereda M, et al. 2011. Characterizing the RNA targets and position-dependent splicing regulation by TDP-43. Nat. Neurosci. 14:452-58
    • (2011) Nat. Neurosci. , vol.14 , pp. 452-58
    • Tollervey, J.R.1    Curk, T.2    Rogelj, B.3    Briese, M.4    Cereda, M.5
  • 113
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • DOI 10.1016/S0092-8674(03)00939-5
    • Kawaguchi Y, Kovacs JJ, McLaurin A, Vance JM, Ito A, Yao TP. 2003. The deacetylaseHDAC6regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 115:727-38 (Pubitemid 38030301)
    • (2003) Cell , vol.115 , Issue.6 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.-P.6
  • 114
    • 77952326081 scopus 로고    scopus 로고
    • Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy
    • Lee JY, Nagano Y, Taylor JP, Lim KL, Yao TP. 2010. Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy. J. Cell Biol. 189:671-79
    • (2010) J. Cell Biol. , vol.189 , pp. 671-79
    • Lee, J.Y.1    Nagano, Y.2    Taylor, J.P.3    Lim, K.L.4    Yao, T.P.5
  • 115
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski TJ Jr, Bosco DA, Leclerc AL, Tamrazian E, Vanderburg CR, et al. 2009. Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323:1205-8
    • (2009) Science , vol.323 , pp. 1205-8
    • Kwiatkowski Jr., T.J.1    Bosco, D.A.2    Leclerc, A.L.3    Tamrazian, E.4    Vanderburg, C.R.5
  • 116
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6
    • Vance C, Rogelj B, Hortobagyi T, De Vos KJ, Nishimura AL, et al. 2009. Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 323:1208-11
    • (2009) Science , vol.323 , pp. 1208-11
    • Vance, C.1    Rogelj, B.2    Hortobagyi, T.3    De Vos, K.J.4    Nishimura, A.L.5
  • 117
    • 77951712967 scopus 로고    scopus 로고
    • FALS with FUS mutation in Japan, with early onset, rapid progress and basophilic inclusion
    • Suzuki N, Aoki M, Warita H, Kato M, Mizuno H, et al. 2010. FALS with FUS mutation in Japan, with early onset, rapid progress and basophilic inclusion. J. Hum. Genet. 55:252-54
    • (2010) J. Hum. Genet. , vol.55 , pp. 252-54
    • Suzuki, N.1    Aoki, M.2    Warita, H.3    Kato, M.4    Mizuno, H.5
  • 118
    • 77952107930 scopus 로고    scopus 로고
    • Multiple system degeneration with basophilic inclusions in Japanese ALS patients with FUS mutation
    • Tateishi T, Hokonohara T, Yamasaki R, Miura S, Kikuchi H, et al. 2010. Multiple system degeneration with basophilic inclusions in Japanese ALS patients with FUS mutation. Acta Neuropathol. 119:355-64
    • (2010) Acta Neuropathol. , vol.119 , pp. 355-64
    • Tateishi, T.1    Hokonohara, T.2    Yamasaki, R.3    Miura, S.4    Kikuchi, H.5
  • 119
    • 77952932485 scopus 로고    scopus 로고
    • FUS-immunoreactive inclusions are a common feature in sporadic and non-SOD1 familial amyotrophic lateral sclerosis
    • Deng HX, ZhaiH, Bigio EH, Yan J, Fecto F, et al. 2010. FUS-immunoreactive inclusions are a common feature in sporadic and non-SOD1 familial amyotrophic lateral sclerosis. Ann. Neurol. 67:739-48
    • (2010) Ann. Neurol. , vol.67 , pp. 739-48
    • Deng, H.X.1    Zhaih Bigio, E.H.2    Yan, J.3    Fecto, F.4
  • 122
  • 124
    • 59249085091 scopus 로고    scopus 로고
    • Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies
    • Neumann M, Kwong LK, Lee EB, Kremmer E, Flatley A, et al. 2009. Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies. Acta Neuropathol. 117:137-49
    • (2009) Acta Neuropathol , vol.117 , pp. 137-49
    • Neumann, M.1    Kwong, L.K.2    Lee, E.B.3    Kremmer, E.4    Flatley, A.5
  • 125
    • 35548940665 scopus 로고    scopus 로고
    • Neuronal regulation of alternative pre-mRNA splicing
    • DOI 10.1038/nrn2237, PII NRN2237
    • Li Q, Lee JA, Black DL. 2007. Neuronal regulation of alternative pre-mRNA splicing. Nat. Rev. Neurosci. 8:819-31 (Pubitemid 350006218)
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.11 , pp. 819-831
    • Li, Q.1    Lee, J.-A.2    Black, D.L.3
  • 126
    • 0036319256 scopus 로고    scopus 로고
    • RNA splicing mediated by YB-1 is inhibited by TLS/CHOP in human myxoid liposarcoma cells
    • DOI 10.1016/S0736-0266(02)00006-2, PII S0736026602000062
    • Rapp TB, Yang L, Conrad EU 3rd, Mandahl N, Chansky HA. 2002. RNA splicing mediated by YB-1 is inhibited by TLS/CHOP in human myxoid liposarcoma cells. J. Orthop. Res. 20:723-29 (Pubitemid 34822991)
    • (2002) Journal of Orthopaedic Research , vol.20 , Issue.4 , pp. 723-729
    • Rapp, T.B.1    Yang, L.2    Conrad III, E.U.3    Mandahl, N.4    Chansky, H.A.5
  • 127
  • 128
    • 0344407006 scopus 로고    scopus 로고
    • Proto-oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRm160, and SR proteins
    • DOI 10.1016/S0014-4827(02)00046-0
    • Meissner M, Lopato S, Gotzmann J, Sauermann G, Barta A. 2003. Proto-oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRm160, and SR proteins. Exp. Cell Res. 283:184-95 (Pubitemid 36269024)
    • (2003) Experimental Cell Research , vol.283 , Issue.2 , pp. 184-195
    • Meissner, M.1    Lopato, S.2    Gotzmann, J.3    Sauermann, G.4    Barta, A.5
  • 129
    • 0027970712 scopus 로고
    • A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP
    • Zinszner H, Albalat R, Ron D. 1994. A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP. Genes Dev. 8:2513-26 (Pubitemid 24347243)
    • (1994) Genes and Development , vol.8 , Issue.21 , pp. 2513-2526
    • Zinszner, H.1    Albalat, R.2    Ron, D.3
  • 130
    • 0036674269 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human spliceosome
    • DOI 10.1101/gr.473902
    • Rappsilber J, RyderU, Lamond AI, Mann M. 2002. Large-scale proteomic analysis of the human spliceosome. Genome Res. 12:1231-45 (Pubitemid 41264425)
    • (2002) Genome Research , vol.12 , Issue.8 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.I.3    Mann, M.4
  • 131
    • 2442435550 scopus 로고    scopus 로고
    • nrb associates with the 5′ splice site within large transcription/splicing complexes
    • DOI 10.1038/sj.emboj.7600187
    • Kameoka S, Duque P, Konarska MM. 2004. p54nrb associates with the 5′ splice site within large transcription/ splicing complexes. EMBO J. 23:1782-91 (Pubitemid 38649641)
    • (2004) EMBO Journal , vol.23 , Issue.8 , pp. 1782-1791
    • Kameoka, S.1    Duque, P.2    Konarska, M.M.3
  • 132
    • 0030855063 scopus 로고    scopus 로고
    • Identification of a human protein that recognizes the 3' splice site during the second step of pre-mRNA splicing
    • DOI 10.1093/emboj/16.14.4421
    • Wu S, Green MR. 1997. Identification of a human protein that recognizes the 3′ splice site during the second step of pre-mRNA splicing. EMBO J. 16:4421-32 (Pubitemid 27298195)
    • (1997) EMBO Journal , vol.16 , Issue.14 , pp. 4421-4432
    • Wu, S.1    Green, M.R.2
  • 134
    • 17444381645 scopus 로고    scopus 로고
    • Delocalization of the multifunctional RNA splicing factor TLS/FUS in hippocampal neurones: Exclusion from the nucleus and accumulation in dendritic granules and spine heads
    • DOI 10.1016/j.neulet.2004.12.071
    • Belly A, Moreau-Gachelin F, Sadoul R, Goldberg Y. 2005. Delocalization of the multifunctional RNA splicing factor TLS/FUS in hippocampal neurones: exclusion from the nucleus and accumulation in dendritic granules and spine heads. Neurosci. Lett. 379:152-57 (Pubitemid 40544525)
    • (2005) Neuroscience Letters , vol.379 , Issue.3 , pp. 152-157
    • Belly, A.1    Moreau-Gachelin, F.2    Sadoul, R.3    Goldberg, Y.4
  • 137
    • 58149503004 scopus 로고    scopus 로고
    • TLS interaction with NMDA R1 splice variant in retinal ganglion cell line RGC-5
    • Selamat W, Jamari I, Wang Y, Takumi T, Wong F, Fujii R. 2009. TLS interaction with NMDA R1 splice variant in retinal ganglion cell line RGC-5. Neurosci. Lett. 450:163-66
    • (2009) Neurosci. Lett , vol.450 , pp. 163-66
    • Selamat, W.1    Jamari, I.2    Wang, Y.3    Takumi, T.4    Wong, F.5    Fujii, R.6
  • 138
    • 77957867303 scopus 로고    scopus 로고
    • MutantFUSproteins that cause amyotrophic lateral sclerosis incorporate into stress granules
    • Bosco DA, Lemay N, Ko HK, Zhou H, Burke C, et al. 2010. MutantFUSproteins that cause amyotrophic lateral sclerosis incorporate into stress granules. Hum. Mol. Genet. 19:4160-75
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 4160-75
    • Bosco, D.A.1    Lemay, N.2    Ko, H.K.3    Zhou, H.4    Burke, C.5
  • 139
    • 80053646130 scopus 로고    scopus 로고
    • Nuclear localization sequence of FUS and induction of stress granules by ALS mutants
    • Gal J, Zhang J, Kwinter DM, Zhai J, Jia H, et al. 2011. Nuclear localization sequence of FUS and induction of stress granules by ALS mutants. Neurobiol. Aging 32:2323.e27-40
    • (2011) Neurobiol. Aging , vol.32
    • Gal, J.1    Zhang, J.2    Kwinter, D.M.3    Zhai, J.4    Jia, H.5
  • 140
    • 79251573834 scopus 로고    scopus 로고
    • Dr. Jekyll and Mr.Hyde: The two faces of the FUS/EWS/TAF15 protein family
    • KovarH. 2011. Dr. Jekyll and Mr.Hyde: the two faces of the FUS/EWS/TAF15 protein family. Sarcoma 2011:837474
    • (2011) Sarcoma , vol.2011 , pp. 837474
    • Kovar, H.1
  • 141
    • 48249083430 scopus 로고    scopus 로고
    • The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response
    • Andersson MK, Stahlberg A, Arvidsson Y, Olofsson A, Semb H, et al. 2008. The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response. BMC Cell Biol. 9:37
    • (2008) BMC Cell Biol , vol.9 , pp. 37
    • Andersson, M.K.1    Stahlberg, A.2    Arvidsson, Y.3    Olofsson, A.4    Semb, H.5
  • 143
    • 0029812470 scopus 로고    scopus 로고
    • HTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II
    • Bertolotti A, Lutz Y, Heard DJ, Chambon P, Tora L. 1996. hTAFII68, a novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II. EMBO J. 15:5022-31 (Pubitemid 26315812)
    • (1996) EMBO Journal , vol.15 , Issue.18 , pp. 5022-5031
    • Bertolotti, A.1    Lutz, Y.2    Heard, D.J.3    Chambon, P.4    Tora, L.5
  • 144
    • 33747881750 scopus 로고    scopus 로고
    • The general transcription machinery and general cofactors
    • Thomas MC, Chiang CM. 2006. The general transcription machinery and general cofactors. Crit. Rev. Biochem. Mol. Biol. 41:105-78
    • (2006) Crit. Rev. Biochem. Mol. Biol , vol.41 , pp. 105-78
    • Thomas, M.C.1    Chiang, C.M.2
  • 145
    • 63049100536 scopus 로고    scopus 로고
    • PRMT1mediated methylation ofTAF15 is required for its positive gene regulatory function
    • Jobert L, Argentini M, Tora L. 2009. PRMT1mediated methylation ofTAF15 is required for its positive gene regulatory function. Exp. Cell Res. 315:1273-86
    • (2009) Exp. Cell Res , vol.315 , pp. 1273-86
    • Jobert, L.1    Argentini, M.2    Tora, L.3
  • 146
    • 67349171403 scopus 로고    scopus 로고
    • Human U1 snRNA forms a new chromatin-associated snRNP with TAF15
    • Jobert L, Pinzon N, Van Herreweghe E, Jady BE, Guialis A, et al. 2009. Human U1 snRNA forms a new chromatin-associated snRNP with TAF15. EMBO Rep. 10:494-500
    • (2009) EMBO Rep , vol.10 , pp. 494-500
    • Jobert, L.1    Pinzon, N.2    Van Herreweghe, E.3    Jady, B.E.4    Guialis, A.5
  • 147
    • 33745945163 scopus 로고    scopus 로고
    • TLS, EWS and TAF15: A model for transcriptional integration of gene expression
    • DOI 10.1093/bfgp/ell015, The Comparative and Functional Genomics (BITS) Workshop
    • Law WJ, Cann KL, Hicks GG. 2006. TLS, EWS and TAF15: a model for transcriptional integration of gene expression. Brief. Funct. Genomics 5:8-14 (Pubitemid 46402988)
    • (2006) Briefings in Functional Genomics and Proteomics , vol.5 , Issue.1 , pp. 8-14
    • Law, W.J.1    Cann, K.L.2    Hicks, G.G.3
  • 149
    • 35248844678 scopus 로고    scopus 로고
    • Angiogenin loss-of-function mutations in amyotrophic lateral sclerosis
    • Wu D, Yu W, Kishikawa H, Folkerth RD, Iafrate AJ, et al. 2007. Angiogenin loss-of-function mutations in amyotrophic lateral sclerosis. Ann. Neurol. 62:609-17
    • (2007) Ann. Neurol , vol.62 , pp. 609-17
    • Wu, D.1    Yu, W.2    Kishikawa, H.3    Folkerth, R.D.4    Iafrate, A.J.5
  • 150
    • 38649105800 scopus 로고    scopus 로고
    • Identification of new ANG gene mutations in a large cohort of Italian patients with amyotrophic lateral sclerosis
    • Gellera C, Colombrita C, Ticozzi N, Castellotti B, Bragato C, et al. 2008. Identification of new ANG gene mutations in a large cohort of Italian patients with amyotrophic lateral sclerosis. Neurogenetics 9:33-40
    • (2008) Neurogenetics , vol.9 , pp. 33-40
    • Gellera, C.1    Colombrita, C.2    Ticozzi, N.3    Castellotti, B.4    Bragato, C.5
  • 151
    • 54049119245 scopus 로고    scopus 로고
    • Mutations of the ANG gene in French patients with sporadic amyotrophic lateral sclerosis
    • Paubel A, Violette J, Amy M, Praline J, Meininger V, et al. 2008. Mutations of the ANG gene in French patients with sporadic amyotrophic lateral sclerosis. Arch. Neurol. 65:1333-36
    • (2008) Arch. Neurol , vol.65 , pp. 1333-36
    • Paubel, A.1    Violette, J.2    Amy, M.3    Praline, J.4    Meininger, V.5
  • 152
    • 77955396350 scopus 로고    scopus 로고
    • SOD1, ANG, VAPB, TARDBP, and FUS mutations in familial amyotrophic lateral sclerosis: Genotype-phenotype correlations
    • Millecamps S, Salachas F, Cazeneuve C, Gordon P, Bricka B, et al. 2010. SOD1, ANG, VAPB, TARDBP, and FUS mutations in familial amyotrophic lateral sclerosis: genotype-phenotype correlations. J. Med. Genet. 47:554-60
    • (2010) J. Med. Genet. , vol.47 , pp. 554-60
    • Millecamps, S.1    Salachas, F.2    Cazeneuve Cgordon, P.3    Bricka, B.4
  • 154
    • 33644843205 scopus 로고    scopus 로고
    • Posttranscriptionalmechanisms contribute to osmotic regulation of ANG type 1 receptors in cultured rat renomedullary interstitial cells
    • Lee S, Wu Z, Sandberg K, Yoo SE, Maric C. 2006. Posttranscriptionalmechanisms contribute to osmotic regulation of ANG type 1 receptors in cultured rat renomedullary interstitial cells. Am. J. Physiol. Regul. Integr. Comp. Physiol. 290:44-49
    • (2006) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.290 , pp. 44-49
    • Lee, S.1    Wu, Z.2    Sandberg, K.3    Yoo, S.E.4    Maric, C.5
  • 155
    • 78649940361 scopus 로고    scopus 로고
    • Angiogenin-mediated rRNA transcription in cancer and neurodegeneration
    • Li S, Hu GF. 2010. Angiogenin-mediated rRNA transcription in cancer and neurodegeneration. Int. J. Biochem. Mol. Biol. 1:26-35
    • (2010) Int. J. Biochem. Mol. Biol. , vol.1 , pp. 26-35
    • Li, S.1    Hu, G.F.2
  • 156
    • 34447317537 scopus 로고    scopus 로고
    • A new role for angiogenin in neurite growth and pathfinding: Implications for amyotrophic lateral sclerosis
    • DOI 10.1093/hmg/ddm095
    • Subramanian V, Feng Y. 2007. A new role for angiogenin in neurite growth and pathfinding: implications for amyotrophic lateral sclerosis. Hum. Mol. Genet. 16:1445-53 (Pubitemid 47055116)
    • (2007) Human Molecular Genetics , vol.16 , Issue.12 , pp. 1445-1453
    • Subramanian, V.1    Feng, Y.2
  • 158
    • 65249129859 scopus 로고    scopus 로고
    • Angiogenin cleaves tRNA and promotes stress-induced translational repression
    • Yamasaki S, Ivanov P, Hu GF, Anderson P. 2009. Angiogenin cleaves tRNA and promotes stress-induced translational repression. J. Cell Biol. 185:35-42
    • (2009) J. Cell Biol , vol.185 , pp. 35-42
    • Yamasaki, S.1    Ivanov, P.2    Hu, G.F.3    Anderson, P.4
  • 161
    • 0037064145 scopus 로고    scopus 로고
    • Separable roles for rent1/hUpf1 in altered splicing and decay of nonsense transcripts
    • DOI 10.1126/science.1074428
    • Mendell JT, ap Rhys CMJ, Dietz HC. 2002. Separable roles for rent1/hUpf1 in altered splicing and decay of nonsense transcripts. Science 298:419-22 (Pubitemid 35176351)
    • (2002) Science , vol.298 , Issue.5592 , pp. 419-422
    • Mendell, J.T.1    Ap Rhys, C.M.J.2    Dietz, H.C.3
  • 163
    • 69449101422 scopus 로고    scopus 로고
    • Functional role for senataxin, defective in ataxia oculomotor apraxia type 2, in transcriptional regulation
    • Suraweera A, Lim Y, Woods R, Birrell GW, Nasim T, et al. 2009. Functional role for senataxin, defective in ataxia oculomotor apraxia type 2, in transcriptional regulation. Hum. Mol. Genet. 18:3384-96
    • (2009) Hum. Mol. Genet , vol.18 , pp. 3384-96
    • Suraweera, A.1    Lim, Y.2    Woods, R.3    Birrell, G.W.4    Nasim, T.5
  • 164
    • 62549146705 scopus 로고    scopus 로고
    • A novel mutation in the senataxin gene identified in a Chinese patient with sporadic amyotrophic lateral sclerosis
    • Zhao ZH, Chen WZ, Wu ZY, Wang N, Zhao GX, et al. 2009. A novel mutation in the senataxin gene identified in a Chinese patient with sporadic amyotrophic lateral sclerosis. Amyotroph. Lateral Scler. 10:118-22
    • (2009) Amyotroph. Lateral Scler , vol.10 , pp. 118-22
    • Zh, Z.1    Chen, W.Z.2    Wu, Z.Y.3    Wang, N.4    Zhao, G.X.5
  • 166
    • 33745131439 scopus 로고    scopus 로고
    • Senataxin, the yeast Sen1p orthologue: Characterization of a unique protein in which recessive mutations cause ataxia and dominant mutations cause motor neuron disease
    • DOI 10.1016/j.nbd.2006.02.007, PII S0969996106000362
    • Chen YZ, Hashemi SH, Anderson SK, Huang Y, Moreira MC, et al. 2006. Senataxin, the yeast Sen1p orthologue: characterization of a unique protein in which recessive mutations cause ataxia and dominant mutations cause motor neuron disease. Neurobiol. Dis. 23:97-108 (Pubitemid 43903634)
    • (2006) Neurobiology of Disease , vol.23 , Issue.1 , pp. 97-108
    • Chen, Y.-Z.1    Hashemi, S.H.2    Anderson, S.K.3    Huang, Y.4    Moreira, M.-C.5    Lynch, D.R.6    Glass, I.A.7    Chance, P.F.8    Bennett, C.L.9
  • 167
    • 58749097964 scopus 로고    scopus 로고
    • Variants of the elongator protein 3 (ELP3) gene are associated with motor neuron degeneration
    • Simpson CL, Lemmens R, Miskiewicz K, Broom WJ, Hansen VK, et al. 2009. Variants of the elongator protein 3 (ELP3) gene are associated with motor neuron degeneration. Hum. Mol. Genet. 18:472-81
    • (2009) Hum. Mol. Genet , vol.18 , pp. 472-81
    • Simpson, C.L.1    Lemmens, R.2    Miskiewicz, K.3    Broom, W.J.4    Hansen, V.K.5
  • 170
    • 15444371415 scopus 로고    scopus 로고
    • An early step in wobble uridine tRNA modification requires the Elongator complex
    • DOI 10.1261/rna.7247705
    • Huang B, JohanssonMJ, Bystrom AS. 2005. An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11:424-36 (Pubitemid 40397176)
    • (2005) RNA , vol.11 , Issue.4 , pp. 424-436
    • Huang, B.1    Johansson, M.J.O.2    Bystrom, A.S.3
  • 172
    • 38949102236 scopus 로고    scopus 로고
    • Gcn5- and Elp3-induced histone H3 acetylation regulates hsp70 gene transcription in yeast
    • DOI 10.1042/BJ20070578
    • Han Q, Lu J, Duan J, Su D, Hou X, et al. 2008. Gcn5- and Elp3-induced histoneH3 acetylation regulates hsp70 gene transcription in yeast. Biochem. J. 409:779-88 (Pubitemid 351214204)
    • (2008) Biochemical Journal , vol.409 , Issue.3 , pp. 779-788
    • Han, Q.1    Lu, J.2    Duan, J.3    Su, D.4    Hou, X.5    Li, F.6    Wang, X.7    Huang, B.8
  • 173
    • 50149098605 scopus 로고    scopus 로고
    • Induced pluripotent stem cells generated from patients with ALS can be differentiated into motor neurons
    • Dimos JT, Rodolfa KT, Niakan KK, Weisenthal LM, Mitsumoto H, et al. 2008. Induced pluripotent stem cells generated from patients with ALS can be differentiated into motor neurons. Science 321:1218-21
    • (2008) Science , vol.321 , pp. 1218-21
    • Dimos, J.T.1    Rodolfa, K.T.2    Niakan, K.K.3    Weisenthal, L.M.4    Mitsumoto, H.5
  • 174
    • 0033788228 scopus 로고    scopus 로고
    • The ends of the affair: Capping and polyadenylation
    • Shatkin AJ, Manley JL. 2000. The ends of the affair: capping and polyadenylation. Nat. Struct. Biol. 7:838-42
    • (2000) Nat. Struct. Biol , vol.7 , pp. 838-42
    • Shatkin, A.J.1    Manley, J.L.2
  • 175
    • 5044229348 scopus 로고    scopus 로고
    • Molecular mechanisms of translational control
    • DOI 10.1038/nrm1488
    • Gebauer F, Hentze MW. 2004. Molecular mechanisms of translational control. Nat. Rev. Mol. Cell Biol. 5:827-35 (Pubitemid 39336276)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.10 , pp. 827-835
    • Gebauer, F.1    Hentze, M.W.2
  • 176
    • 42449098125 scopus 로고    scopus 로고
    • Splicing regulation: From a parts list of regulatory elements to an integrated splicing code
    • DOI 10.1261/rna.876308
    • Wang Z, Burge CB. 2008. Splicing regulation: from a parts list of regulatory elements to an integrated splicing code. RNA 14:802-13 (Pubitemid 351574901)
    • (2008) RNA , vol.14 , Issue.5 , pp. 802-813
    • Wang, Z.1    Burge, C.B.2
  • 177
    • 60149110358 scopus 로고    scopus 로고
    • Pre-mRNA processing reaches back to transcription and ahead to translation
    • Moore MJ, Proudfoot NJ. 2009. Pre-mRNA processing reaches back to transcription and ahead to translation. Cell 136:688-700
    • (2009) Cell , vol.136 , pp. 688-700
    • Moore, M.J.1    Proudfoot, N.J.2
  • 178
    • 60149086205 scopus 로고    scopus 로고
    • MRNAlocalization: Gene expression in the spatial dimension
    • Martin KC, Ephrussi A. 2009.mRNAlocalization: gene expression in the spatial dimension. Cell 136:719-30
    • (2009) Cell , vol.136 , pp. 719-30
    • Martin, K.C.1    Ephrussi, A.2
  • 179
    • 78049296915 scopus 로고    scopus 로고
    • Nuclear export of mRNA
    • Stewart M. 2010. Nuclear export of mRNA. Trends Biochem. Sci. 35:609-17
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 609-17
    • Stewart, M.1
  • 180
    • 60149090021 scopus 로고    scopus 로고
    • The many pathways of RNA degradation
    • Houseley J, Tollervey D. 2009. The many pathways of RNA degradation. Cell 136:763-76
    • (2009) Cell , vol.136 , pp. 763-76
    • Houseley, J.1    Tollervey, D.2
  • 181
    • 49949105213 scopus 로고    scopus 로고
    • The multiple lives of NMD factors: Balancing roles in gene and genome regulation
    • Isken O, Maquat LE. 2008. The multiple lives of NMD factors: balancing roles in gene and genome regulation. Nat. Rev. Genet. 9:699-712
    • (2008) Nat. Rev. Genet , vol.9 , pp. 699-712
    • Isken, O.1    Maquat, L.E.2
  • 182
    • 0035801373 scopus 로고    scopus 로고
    • The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay
    • DOI 10.1093/emboj/20.17.4987
    • Le Hir H, Gatfield D, Izaurralde E, Moore MJ. 2001. The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay. EMBO J. 20:4987-97 (Pubitemid 32848650)
    • (2001) EMBO Journal , vol.20 , Issue.17 , pp. 4987-4997
    • Le Hir, H.1    Gatfield, D.2    Izaurralde, E.3    Moore, M.J.4
  • 183
    • 0037046798 scopus 로고    scopus 로고
    • Translation is required to remove Y14 from mRNAs in the cytoplasm
    • DOI 10.1016/S0960-9822(02)00902-8, PII S0960982202009028
    • Dostie J, Dreyfuss G. 2002. Translation is required to remove Y14 from mRNAs in the cytoplasm. Curr. Biol. 12:1060-67 (Pubitemid 34766927)
    • (2002) Current Biology , vol.12 , Issue.13 , pp. 1060-1067
    • Dostie, J.1    Dreyfuss, G.2
  • 184
    • 21044438900 scopus 로고    scopus 로고
    • Multiple roles of arginine/serine-rich splicing factors in RNA processing
    • DOI 10.1042/BST0330443
    • Sanford JR, Ellis J, Caceres JF. 2005. Multiple roles of arginine/serine-rich splicing factors in RNA processing. Biochem. Soc. Trans. 33:443-46 (Pubitemid 40873861)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.3 , pp. 443-446
    • Sanford, J.R.1    Ellis, J.2    Caceres, J.F.3
  • 186
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: Design principles of a dynamicRNPmachine
    • Wahl MC, Will CL, Luhrmann R. 2009. The spliceosome: design principles of a dynamicRNPmachine. Cell 136:701-18
    • (2009) Cell , vol.136 , pp. 701-18
    • Wahl, M.C.1    Will, C.L.2    Luhrmann, R.3
  • 187
    • 66049124365 scopus 로고    scopus 로고
    • The role of RNP biogenesis in spinal muscular atrophy
    • Chari A, Paknia E, Fischer U. 2009. The role of RNP biogenesis in spinal muscular atrophy. Curr. Opin. Cell Biol. 21:387-93
    • (2009) Curr. Opin. Cell Biol , vol.21 , pp. 387-93
    • Chari, A.1    Paknia, E.2    Fischer, U.3
  • 188
    • 0025276512 scopus 로고
    • The U3 small nucleolar ribonucleoprotein functions in the first step of preribosomal RNA processing
    • Kass S, Tyc K, Steitz JA, Sollner-Webb B. 1990. The U3 small nucleolar ribonucleoprotein functions in the first step of preribosomal RNA processing. Cell 60:897-908
    • (1990) Cell , vol.60 , pp. 897-908
    • Kass, S.1    Tyc, K.2    Steitz, J.A.3    Sollner-Webb, B.4
  • 189
    • 0037133942 scopus 로고    scopus 로고
    • Small nucleolar RNAs: An abundant group of noncoding RNAs with diverse cellular functions
    • DOI 10.1016/S0092-8674(02)00718-3
    • Kiss T. 2002. Small nucleolar RNAs: an abundant group of noncoding RNAs with diverse cellular functions. Cell 109:145-48 (Pubitemid 34518252)
    • (2002) Cell , vol.109 , Issue.2 , pp. 145-148
    • Kiss, T.1
  • 190
    • 0036850335 scopus 로고    scopus 로고
    • Nuclear export of ribosomal subunits
    • DOI 10.1016/S0968-0004(02)02208-9, PII S0968000402022089
    • Johnson AW, Lund E, Dahlberg J. 2002. Nuclear export of ribosomal subunits. Trends Biochem. Sci. 27:580-85 (Pubitemid 35335407)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.11 , pp. 580-585
    • Johnson, A.W.1    Lund, E.2    Dahlberg, J.3
  • 191
    • 9744222917 scopus 로고    scopus 로고
    • Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large dynamic multiprotein complex
    • DOI 10.1016/j.molcel.2004.11.012, PII S109727650400677X
    • Watkins NJ, Lemm I, Ingelfinger D, Schneider C, Hossbach M, et al. 2004. Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large dynamic multiprotein complex. Mol. Cell 16:789-98 (Pubitemid 39586536)
    • (2004) Molecular Cell , vol.16 , Issue.5 , pp. 789-798
    • Watkins, N.J.1    Lemm, I.2    Ingelfinger, D.3    Schneider, C.4    Hossbach, M.5    Urlaub, H.6    Luhrmann, R.7
  • 192
    • 77957037447 scopus 로고    scopus 로고
    • Ribosome biogenesis: From structure to dynamics
    • Cisterna B, Biggiogera M. 2010. Ribosome biogenesis: from structure to dynamics. Int. Rev. Cell Mol. Biol. 284:67-111
    • (2010) Int. Rev. Cell Mol. Biol. , vol.284 , pp. 67-111
    • Cisterna, B.1    Biggiogera, M.2
  • 193
  • 194
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba M, Soll D. 2000. Aminoacyl-tRNA synthesis. Annu. Rev. Biochem. 69:617-50
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 617-50
    • Ibba, M.1    Soll, D.2
  • 195
    • 23144460836 scopus 로고    scopus 로고
    • The tRNAscan-SE, snoscan and snoGPS Web servers for the detection of tRNAs and snoRNAs
    • Schattner P, Brooks AN, Lowe TM. 2005. The tRNAscan-SE, snoscan and snoGPS Web servers for the detection of tRNAs and snoRNAs. Nucleic Acids Res. 33:686-89
    • (2005) Nucleic Acids Res , vol.33 , pp. 686-89
    • Schattner, P.1    Brooks, A.N.2    Lowe, T.M.3
  • 196
    • 0037439213 scopus 로고    scopus 로고
    • TRNA transfers to the limelight
    • DOI 10.1101/gad.1049103
    • Hopper AK, Phizicky EM. 2003. tRNA transfers to the limelight. Genes Dev. 17:162-80 (Pubitemid 36105890)
    • (2003) Genes and Development , vol.17 , Issue.2 , pp. 162-180
    • Hopper, A.K.1    Phizicky, E.M.2
  • 197
    • 0037108150 scopus 로고    scopus 로고
    • Recruitment of RNA polymerase III to its target promoters
    • Schramm L, Hernandez N. 2002. Recruitment of RNA polymerase III to its target promoters. Genes Dev. 16:2593-620
    • (2002) Genes Dev , vol.16 , pp. 2593-620
    • Schramm, L.1    Hernandez, N.2
  • 198
    • 2042479408 scopus 로고    scopus 로고
    • Identification of a human endonuclease complex reveals a link between tRNA splicing and pre-mRNA 3′ end formation
    • DOI 10.1016/S0092-8674(04)00342-3, PII S0092867404003423
    • Paushkin SV, Patel M, Furia BS, Peltz SW, Trotta CR. 2004. Identification of a human endonuclease complex reveals a link between tRNA splicing and pre-mRNA 3′ end formation. Cell 117:311-21 (Pubitemid 38534538)
    • (2004) Cell , vol.117 , Issue.3 , pp. 311-321
    • Paushkin, S.V.1    Patel, M.2    Furia, B.S.3    Peltz, S.W.4    Trotta, C.R.5
  • 199
    • 26044435441 scopus 로고    scopus 로고
    • Recent progress of structural biology of tRNA processing and modification
    • Nakanishi K, Nureki O. 2005. Recent progress of structural biology of tRNA processing and modification. Mol. Cells 19:157-66
    • (2005) Mol. Cells , vol.19 , pp. 157-66
    • Nakanishi, K.1    Nureki, O.2
  • 200
    • 53549086938 scopus 로고    scopus 로고
    • Toward a more complete view of tRNA biology
    • Giege R. 2008. Toward a more complete view of tRNA biology. Nat. Struct. Mol. Biol. 15:1007-14
    • (2008) Nat. Struct. Mol. Biol , vol.15 , pp. 1007-14
    • Giege, R.1
  • 201
    • 79951476167 scopus 로고    scopus 로고
    • HSPC117 is the essential subunit of a human tRNA splicing ligase complex
    • Popow J, Englert M, Weitzer S, Schleiffer A, Mierzwa B, et al. 2011. HSPC117 is the essential subunit of a human tRNA splicing ligase complex. Science 331:760-64
    • (2011) Science , vol.331 , pp. 760-64
    • Popow, J.1    Englert, M.2    Weitzer, S.3    Schleiffer, A.4    Mierzwa, B.5
  • 202
    • 38349131954 scopus 로고    scopus 로고
    • MicroRNAs: Biogenesis and molecular functions
    • Liu X, Fortin K, Mourelatos Z. 2008. MicroRNAs: biogenesis and molecular functions. Brain Pathol. 18:113-21
    • (2008) Brain Pathol , vol.18 , pp. 113-21
    • Liu, X.1    Fortin, K.2    Mourelatos, Z.3
  • 203
    • 58249088751 scopus 로고    scopus 로고
    • MicroRNAs: Target recognition and regulatory functions
    • Bartel DP. 2009. MicroRNAs: target recognition and regulatory functions. Cell 136:215-33
    • (2009) Cell , vol.136 , pp. 215-33
    • Bartel, D.P.1
  • 204
    • 79551627496 scopus 로고    scopus 로고
    • A parsimonious model for gene regulation by miRNAs
    • Djuranovic S, Nahvi A, Green R. 2011. A parsimonious model for gene regulation by miRNAs. Science 331:550-53
    • (2011) Science , vol.331 , pp. 550-53
    • Djuranovic, S.1    Nahvi, A.2    Green, R.3
  • 205
    • 80054832080 scopus 로고    scopus 로고
    • Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS
    • DeJesus-Hernandez M, Mackenzie IR, Boeve BF, Boxer AL, Baker M, et al. 2011. Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS. Neuron 72:245-56
    • (2011) Neuron , vol.72 , pp. 245-56
    • Dejesus-Hernandez, M.1    MacKenzie, I.R.2    Boeve, B.F.3    Boxer, A.L.4    Baker, M.5
  • 206
    • 80054837386 scopus 로고    scopus 로고
    • A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD
    • Renton AE, Majounie E, Waite A, Siḿon-Śanchez J, Rollinson S, et al. 2011. A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron 72:257-68
    • (2011) Neuron , vol.72 , pp. 257-68
    • Renton, A.E.1    Majounie, E.2    Waite, A.3    Siḿon-Śanchez, J.4    Rollinson, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.