메뉴 건너뛰기




Volumn 2, Issue 7, 2012, Pages 789-802

Comparison of parallel high-throughput RNA sequencing between knockout of TDP-43 and its overexpression reveals primarily nonreciprocal and nonoverlapping gene expression changes in the central nervous system of drosophila

Author keywords

Invertebrate; Models of human disease; Neurodegeneration; Neuropathy; RNA binding protein genomics; TARDBP

Indexed keywords

DNA BINDING PROTEIN; DROSOPHILA PROTEIN; PROTEIN TDP-43; TAR DNA BINDING PROTEIN;

EID: 84883348833     PISSN: None     EISSN: 21601836     Source Type: Journal    
DOI: 10.1534/g3.112.002998     Document Type: Article
Times cited : (51)

References (64)
  • 1
    • 37549025044 scopus 로고    scopus 로고
    • A novel CpG-free vertebrate insulator silences the testis-specific SP-10 gene in somatic tissues
    • Abhyankar, M. M., C. Urekar, and P. P. Reddi, 2007 A novel CpG-free vertebrate insulator silences the testis-specific SP-10 gene in somatic tissues. J. Biol. Chem. 282: 36143-36154.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36143-36154
    • Abhyankar, M.M.1    Urekar, C.2    Reddi, P.P.3
  • 3
    • 32344435621 scopus 로고    scopus 로고
    • TDP43 depletion rescues aberrant CFTR exon 9 skipping
    • Ayala, Y. M., F. Pagani, and F. E. Baralle, 2006 TDP43 depletion rescues aberrant CFTR exon 9 skipping. FEBS Lett. 580: 1339-1344.
    • (2006) FEBS Lett. , vol.580 , pp. 1339-1344
    • Ayala, Y.M.1    Pagani, F.2    Baralle, F.E.3
  • 4
    • 59549094064 scopus 로고    scopus 로고
    • Structural determinants of the cellular localization and shuttling of TDP-43
    • Ayala, Y. M., P. Zago, A. D'Ambrogio, Y.-F. Xu, L. Petrucelli et al., 2008a Structural determinants of the cellular localization and shuttling of TDP-43. J. Cell Sci. 121: 3778-3785.
    • (2008) J. Cell Sci. , vol.121 , pp. 3778-3785
    • Ayala, Y.M.1    Zago, P.2    D'Ambrogio, A.3    Xu, Y.-F.4    Petrucelli, L.5
  • 5
    • 41649106307 scopus 로고    scopus 로고
    • TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression
    • Ayala, Y. M., T. Misteli, and F. E. Baralle, 2008b TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression. Proc. Natl. Acad. Sci. USA 105: 3785-3789.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3785-3789
    • Ayala, Y.M.1    Misteli, T.2    Baralle, F.E.3
  • 7
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: a practical and powerful approach to multiple testing
    • Benjamini, Y., and Y. Hochberg, 1995 Controlling the false discovery rate: a practical and powerful approach to multiple testing. J. R. Stat. Soc., B 57 (1): 289-300.
    • (1995) J. R. Stat. Soc., B , vol.57 , Issue.1 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 8
    • 0000064419 scopus 로고
    • Behavioral mutants of Drosophila isolated by countercurrent distribution
    • Benzer, S., 1967 Behavioral mutants of Drosophila isolated by countercurrent distribution. Proc. Natl. Acad. Sci. USA 58: 1112-1119.
    • (1967) Proc. Natl. Acad. Sci. USA , vol.58 , pp. 1112-1119
    • Benzer, S.1
  • 9
    • 57649174592 scopus 로고    scopus 로고
    • TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing
    • Bose, J. K., I.-F. Wang, L. Hung, W.-Y Tarn, and C.-K. James Shen, 2008 TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing. J. Biol. Chem. 283: 28852-28859.
    • (2008) J. Biol. Chem. , vol.283 , pp. 28852-28859
    • Bose, J.K.1    Wang, I.-F.2    Hung, L.3    Tarn, W.-Y.4    James Shen, C.-K.5
  • 10
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A. H., and N. Perrimon, 1993 Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118: 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 11
    • 84857768992 scopus 로고    scopus 로고
    • Cellular model of TAR DNA-binding protein 43 (TDP-43) aggregation based on its C-terminal Gln/Asn-rich region
    • Budini, M., E. Buratti, C. Stuani, C. Garnaccia, V. Romano, et al. 2012 Cellular model of TAR DNA-binding protein 43 (TDP-43) aggregation based on its C-terminal Gln/Asn-rich region. J. Biol. Chem. 287: 7512-7525.
    • (2012) J. Biol. Chem. , vol.287 , pp. 7512-7525
    • Budini, M.1    Buratti, E.2    Stuani, C.3    Garnaccia, C.4    Romano, V.5
  • 12
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, novel splicing regulator of CFTR exon 9
    • Buratti, E., and F. E. Baralle, 2001 Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, novel splicing regulator of CFTR exon 9. J. Biol. Chem. 276: 36337-36343.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 13
    • 0035794665 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
    • Buratti, E., T. Dork, E. Zuccato, F. Pagani, M. Romano, et al. 2001 Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. EMBO J. 20: 1774-1784.
    • (2001) EMBO J. , vol.20 , pp. 1774-1784
    • Buratti, E.1    Dork, T.2    Zuccato, E.3    Pagani, F.4    Romano, M.5
  • 14
    • 77951700391 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 can affect selected microRNA levels
    • Buratti, E., L. De Conti, C. Stuani, M. Romano, M. Baralle, et al. 2010 Nuclear factor TDP-43 can affect selected microRNA levels. FEBS J. 277: 2268-2281.
    • (2010) FEBS J. , vol.277 , pp. 2268-2281
    • Buratti, E.1    De Conti, L.2    Stuani, C.3    Romano, M.4    Baralle, M.5
  • 15
    • 32544447773 scopus 로고    scopus 로고
    • Overexpression of tau results in defective synaptic transmission in Drosophila neuromuscular junctions
    • Chee, F., A. Mudher, T. A. Newman, M. Cuttle, S. Lovestone, et al. 2006 Overexpression of tau results in defective synaptic transmission in Drosophila neuromuscular junctions. Biochem. Soc. Trans. 34: 88-90.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 88-90
    • Chee, F.1    Mudher, A.2    Newman, T.A.3    Cuttle, M.4    Lovestone, S.5
  • 16
    • 34247615021 scopus 로고    scopus 로고
    • Study of tauopathies by comparing Drosophila and human tau in Drosophila
    • Chen, X., Y. Li, J. Huang, D. Cao, G. Yang, et al. 2007 Study of tauopathies by comparing Drosophila and human tau in Drosophila. Cell Tissue Res. 329: 169-178.
    • (2007) Cell Tissue Res. , vol.329 , pp. 169-178
    • Chen, X.1    Li, Y.2    Huang, J.3    Cao, D.4    Yang, G.5
  • 17
    • 0036081081 scopus 로고    scopus 로고
    • Homophila: human disease gene cognates in Drosophila
    • Chien, S., L. T. Reiter, E. Bier, and M. Gribskov, 2002 Homophila: human disease gene cognates in Drosophila. Nuc Ac Res 30: 149-151.
    • (2002) Nuc Ac Res , vol.30 , pp. 149-151
    • Chien, S.1    Reiter, L.T.2    Bier, E.3    Gribskov, M.4
  • 18
    • 34249804498 scopus 로고    scopus 로고
    • Using FlyAtlas to identify better Drosophila melanogaster models of human disease
    • Chintapalli, V. R., J. Wang, and J. A. T. Dow, 2007 Using FlyAtlas to identify better Drosophila melanogaster models of human disease. Nat. Genet. 39: 715-720.
    • (2007) Nat. Genet. , vol.39 , pp. 715-720
    • Chintapalli, V.R.1    Wang, J.2    Dow, J.A.T.3
  • 19
    • 33846854871 scopus 로고    scopus 로고
    • Synaptic development: insights from Drosophila
    • Collins, C. A., and A. DiAntonio, 2007 Synaptic development: insights from Drosophila. Curr. Opin. Neurobiol. 17: 35-42.
    • (2007) Curr. Opin. Neurobiol. , vol.17 , pp. 35-42
    • Collins, C.A.1    DiAntonio, A.2
  • 21
    • 79957488875 scopus 로고    scopus 로고
    • Wild-type and A315T mutant TDP-43 exert differential neurotoxicity in a Drosophila model of ALS
    • Estes, P. S., A. Boehringer, R. Zwick, J. E. Tang, B. Grigsby, et al. 2010 Wild-type and A315T mutant TDP-43 exert differential neurotoxicity in a Drosophila model of ALS. Hum. Mol. Genet. 20: 2308-2321.
    • (2010) Hum. Mol. Genet. , vol.20 , pp. 2308-2321
    • Estes, P.S.1    Boehringer, A.2    Zwick, R.3    Tang, J.E.4    Grigsby, B.5
  • 22
    • 67349271683 scopus 로고    scopus 로고
    • Depletion of TDP-43 affects Drosophila motoneurons terminal synapsis and locomotive behavior
    • Feiguin, F., V. K. Godena, G. Romano, A. D'Ambrogio, R. Klima, et al. 2009 Depletion of TDP-43 affects Drosophila motoneurons terminal synapsis and locomotive behavior. FEBS Lett. 583: 1586-1592.
    • (2009) FEBS Lett. , vol.583 , pp. 1586-1592
    • Feiguin, F.1    Godena, V.K.2    Romano, G.3    D'Ambrogio, A.4    Klima, R.5
  • 24
    • 0027429729 scopus 로고    scopus 로고
    • Striatal L-DOPA decarboxylase activity in Parkinson's disease in vivo: implications for the regulation of dopamine synthesis
    • Gjedde, A., G. C. Léger, P. Cumming, Y. Yasuhara, A. C. Evans, et al. 2006 Striatal L-DOPA decarboxylase activity in Parkinson's disease in vivo: implications for the regulation of dopamine synthesis. J. Neurochem. 61: 1538-1541.
    • (2006) J. Neurochem. , vol.61 , pp. 1538-1541
    • Gjedde, A.1    Léger, G.C.2    Cumming, P.3    Yasuhara, Y.4    Evans, A.C.5
  • 25
    • 79952585752 scopus 로고    scopus 로고
    • TDP-43 regulates Drosophila neuromuscular junctions growth by modulating futsch/MAP1B levels and synaptic microtubules organization
    • Godena, V. K., G. Romano, M. Romano, C. Appocher, R. Klima, et al. 2011 TDP-43 regulates Drosophila neuromuscular junctions growth by modulating futsch/MAP1B levels and synaptic microtubules organization. PLoS ONE 6: e17808.
    • (2011) PLoS ONE , vol.6
    • Godena, V.K.1    Romano, G.2    Romano, M.3    Appocher, C.4    Klima, R.5
  • 26
    • 0004241854 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Greenspan, R. J., 2004 Fly Pushing, Ed. 2. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2004) Fly Pushing, Ed. 2
    • Greenspan, R.J.1
  • 27
    • 77951236534 scopus 로고    scopus 로고
    • Ubiquilin modifies TDP-43 toxicity in a Drosophila model of amyotrophic lateral sclerosis (ALS)
    • Hanson, K. A., S. H. Kim, D. A. Wassarman, and R. S. Tibbets, 2010 Ubiquilin modifies TDP-43 toxicity in a Drosophila model of amyotrophic lateral sclerosis (ALS). J. Biol. Chem. 285: 11068-11072.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11068-11072
    • Hanson, K.A.1    Kim, S.H.2    Wassarman, D.A.3    Tibbets, R.S.4
  • 28
    • 0034814018 scopus 로고    scopus 로고
    • Identification and characterization of the Drosophila tau homolog
    • Heidary, G., and M. E. Fortini, 2001 Identification and characterization of the Drosophila tau homolog. Mech. Dev. 108: 171-178.
    • (2001) Mech. Dev. , vol.108 , pp. 171-178
    • Heidary, G.1    Fortini, M.E.2
  • 29
    • 79551610291 scopus 로고    scopus 로고
    • Genome-wide analysis of promoter architecture in Drosophila melanogaster
    • Hoskins, R. A., J. M. Landolin, J. B. Brown, J. E. Sandler, H. Takahashi, et al. 2011 Genome-wide analysis of promoter architecture in Drosophila melanogaster. Genome Res. 21: 182-192.
    • (2011) Genome Res. , vol.21 , pp. 182-192
    • Hoskins, R.A.1    Landolin, J.M.2    Brown, J.B.3    Sandler, J.E.4    Takahashi, H.5
  • 30
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID Bioinformatics Resources
    • Huang, D. W., B. T. Sherman, and R. A. Lempicki, 2009a Systematic and integrative analysis of large gene lists using DAVID Bioinformatics Resources. Nature Protoc. 4: 44-57.
    • (2009) Nature Protoc. , vol.4 , pp. 44-57
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 31
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists
    • Huang, D. W., B. T. Sherman, and R. A. Lempicki, 2009b Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res. 37: 1-13.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1-13
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 32
    • 0037118247 scopus 로고    scopus 로고
    • Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila
    • Jackson, G. R., M. Wiedau-Pazos, T. K. Sang, N. Wagle, C. A. Brown, et al. 2002 Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila. Neuron 34: 509-519.
    • (2002) Neuron , vol.34 , pp. 509-519
    • Jackson, G.R.1    Wiedau-Pazos, M.2    Sang, T.K.3    Wagle, N.4    Brown, C.A.5
  • 33
    • 84873751778 scopus 로고
    • An invariant form for the prior probability in estimation problems
    • Jeffreys, H., 1946 An invariant form for the prior probability in estimation problems. Proc. R. Soc. Lond. 186: 453-461.
    • (1946) Proc. R. Soc. Lond. , vol.186 , pp. 453-461
    • Jeffreys, H.1
  • 34
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • Johnson, B. S., D. Snead, J. J. Lee, J. M. McCaffery, J. Shorter, et al. 2009 TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J. Biol. Chem. 284: 20329-20339.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20329-20339
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3    McCaffery, J.M.4    Shorter, J.5
  • 35
    • 79953060951 scopus 로고    scopus 로고
    • Comprehensive analysis of the chromatin landscape in Drosophila melanogaster
    • Kharchenko, P. V., A. A. Alekseyenko, Y. B. Schwartz, A. Minoda, N. C. Riddle, et al. 2010 Comprehensive analysis of the chromatin landscape in Drosophila melanogaster. Nature 471: 480-485.
    • (2010) Nature , vol.471 , pp. 480-485
    • Kharchenko, P.V.1    Alekseyenko, A.A.2    Schwartz, Y.B.3    Minoda, A.4    Riddle, N.C.5
  • 36
    • 2942592798 scopus 로고    scopus 로고
    • Wnt-3a and Dvl induce neurite retraction by activating rho-associated kinase
    • Kishida, S., H. Yamamoto, and A. Kikuchi, 2004 Wnt-3a and Dvl induce neurite retraction by activating rho-associated kinase. Mol. Cell. Biol. 24: 4487-4501.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4487-4501
    • Kishida, S.1    Yamamoto, H.2    Kikuchi, A.3
  • 37
    • 59049089760 scopus 로고    scopus 로고
    • Syndapin is dispensable for synaptic vesicle endocytosis at the Drosophila larval neuromuscular junction
    • Kumar, V., S. R. Alla, K. S. Krishnan, and M. Ramaswami, 2009 Syndapin is dispensable for synaptic vesicle endocytosis at the Drosophila larval neuromuscular junction. Mol. Cell. Neurosci. 40: 234-241.
    • (2009) Mol. Cell. Neurosci. , vol.40 , pp. 234-241
    • Kumar, V.1    Alla, S.R.2    Krishnan, K.S.3    Ramaswami, M.4
  • 38
    • 84155167265 scopus 로고    scopus 로고
    • Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
    • Lee, E. B., V. M.-Y. Lee, and J. Q. Trojanowski, 2012 Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration. Nat Neurosci Rev 13: 38-50.
    • (2012) Nat Neurosci Rev , vol.13 , pp. 38-50
    • Lee, E.B.1    Lee, V.M.-Y.2    Trojanowski, J.Q.3
  • 39
    • 0023823645 scopus 로고
    • Ubiquitin deposits in anterior horn cells in motor neurone disease
    • Leigh, P. N., B. H. Anderton, A. Dodson, J. M. Gallo, and M. Swash, 1988 Ubiquitin deposits in anterior horn cells in motor neurone disease. Neurosci. Lett. 93: 197-203.
    • (1988) Neurosci. Lett. , vol.93 , pp. 197-203
    • Leigh, P.N.1    Anderton, B.H.2    Dodson, A.3    Gallo, J.M.4    Swash, M.5
  • 42
    • 77954563918 scopus 로고    scopus 로고
    • A genomic response to the yeast transcription factor GAL4 in Drosophila
    • Liu, Y., and M. Lehmann, 2008 A genomic response to the yeast transcription factor GAL4 in Drosophila. Fly (Austin) 2: 92-98.
    • (2008) Fly (Austin) , vol.2 , pp. 92-98
    • Liu, Y.1    Lehmann, M.2
  • 43
    • 0014941986 scopus 로고
    • Parkinson's disease: activity of L-Dopa decarboxylase in discrete brain regions
    • Lloyd, K., and O. Hornykiewicz, 1970 Parkinson's disease: activity of L-Dopa decarboxylase in discrete brain regions. Science 170: 1212-1213.
    • (1970) Science , vol.170 , pp. 1212-1213
    • Lloyd, K.1    Hornykiewicz, O.2
  • 44
    • 0023738162 scopus 로고
    • A filamentous inclusion body within anterior horn neurones in motor neurone disease defined by immunocytochemical localisation of ubiquitin
    • Lowe, J., G. Lennox, D. Jefferson, K. Morrell, D. McQuire, et al. 1988 A filamentous inclusion body within anterior horn neurones in motor neurone disease defined by immunocytochemical localisation of ubiquitin. Neurosci. Lett. 94: 203-210.
    • (1988) Neurosci. Lett. , vol.94 , pp. 203-210
    • Lowe, J.1    Lennox, G.2    Jefferson, D.3    Morrell, K.4    McQuire, D.5
  • 45
    • 70350356317 scopus 로고    scopus 로고
    • Frontotemporal dementia and amyotrophic lateral sclerosis-associated disease protein TDP-43 promotes dendritic branching
    • Lu, Y., J. Ferris, and F.-B. Gao, 2009 Frontotemporal dementia and amyotrophic lateral sclerosis-associated disease protein TDP-43 promotes dendritic branching. Mol. Brain 2: 30.
    • (2009) Mol. Brain , vol.2 , pp. 30
    • Lu, Y.1    Ferris, J.2    Gao, F.-B.3
  • 46
    • 0344442656 scopus 로고    scopus 로고
    • Drosophila amphiphysin functions during synaptic Fasciclin II membrane cycling
    • Mathew, D., A. Popescu, and V. Budnik, 2003 Drosophila amphiphysin functions during synaptic Fasciclin II membrane cycling. J. Neurosci. 23: 10710-10716.
    • (2003) J. Neurosci. , vol.23 , pp. 10710-10716
    • Mathew, D.1    Popescu, A.2    Budnik, V.3
  • 47
    • 27744554553 scopus 로고    scopus 로고
    • Depletion of TDP43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene
    • Mercado, P. A., Y. M. Ayala, M. Romano, E. Buratti, and F. E. Baralle, 2005 Depletion of TDP43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene. Nuc Ac Res 33: 6000-6010.
    • (2005) Nuc Ac Res , vol.33 , pp. 6000-6010
    • Mercado, P.A.1    Ayala, Y.M.2    Romano, M.3    Buratti, E.4    Baralle, F.E.5
  • 48
    • 0025332899 scopus 로고
    • Ubiquitiniated filamentous inclusions in spinal cord of patients with motor neuron disease
    • Migheli, A., L. Autilio-Gambetti, P. Gambetti, C. Mocellini, M. C. Vigliani, et al. 1990 Ubiquitiniated filamentous inclusions in spinal cord of patients with motor neuron disease. Neurosci. Lett. 114: 5-10.
    • (1990) Neurosci. Lett. , vol.114 , pp. 5-10
    • Migheli, A.1    Autilio-Gambetti, L.2    Gambetti, P.3    Mocellini, C.4    Vigliani, M.C.5
  • 51
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann, M., D. M. Sampathu, L. K. Kwong, A. C. Truax, M. C. Micsenyi, et al. 2006 Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314: 130-133.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3    Truax, A.C.4    Micsenyi, M.C.5
  • 52
    • 0029066110 scopus 로고
    • Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs
    • Ou, S. H., F. Wu, D. Harrich, L. F. Garcia-Martinez, and R. B. Gaynor, 1995 Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J. Virol. 69: 3584-3596.
    • (1995) J. Virol. , vol.69 , pp. 3584-3596
    • Ou, S.H.1    Wu, F.2    Harrich, D.3    Garcia-Martinez, L.F.4    Gaynor, R.B.5
  • 53
    • 70449711243 scopus 로고    scopus 로고
    • Computation for ChIP-seq and RNA-seq studies
    • Pepke, S., B. Wold, and A. Mortazavi, 2009 Computation for ChIP-seq and RNA-seq studies. Nat. Methods 6: S22-S32.
    • (2009) Nat. Methods , vol.6
    • Pepke, S.1    Wold, B.2    Mortazavi, A.3
  • 55
    • 79953185674 scopus 로고    scopus 로고
    • Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
    • Polymenidou, M., C. Lagieer-Tourenne, K. Hutt, S. C. Huelga, J. Moran, et al. 2011 Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43. Nat. Neurosci. 14: 459-468.
    • (2011) Nat. Neurosci. , vol.14 , pp. 459-468
    • Polymenidou, M.1    Lagieer-Tourenne, C.2    Hutt, K.3    Huelga, S.C.4    Moran, J.5
  • 56
    • 77953194507 scopus 로고    scopus 로고
    • TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97
    • Ritson, G. P., S. K. Custer, B. D. Freibaum, J. B. Guinto, D. Geffel, et al. 2010 TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97. J. Neurosci. 30: 7729-7739.
    • (2010) J. Neurosci. , vol.30 , pp. 7729-7739
    • Ritson, G.P.1    Custer, S.K.2    Freibaum, B.D.3    Guinto, J.B.4    Geffel, D.5
  • 57
    • 78651408754 scopus 로고    scopus 로고
    • Identification of neuronal RNA targets of TDP-43-containing ribonucleoprotein complexes
    • Sephton, C. F., C. Cenik, A. Kucukural, E. B. Dammer, B. Cenik, et al. 2011 Identification of neuronal RNA targets of TDP-43-containing ribonucleoprotein complexes. J. Biol. Chem. 286: 1204-1215.
    • (2011) J. Biol. Chem. , vol.286 , pp. 1204-1215
    • Sephton, C.F.1    Cenik, C.2    Kucukural, A.3    Dammer, E.B.4    Cenik, B.5
  • 58
    • 34249751076 scopus 로고    scopus 로고
    • TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein
    • Strong, M. J., K. Volkening, R. Hammond, W. Yang, W. Strong, et al. 2007 TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein. Mol. Cell. Neurosci. 35: 320-327.
    • (2007) Mol. Cell. Neurosci. , vol.35 , pp. 320-327
    • Strong, M.J.1    Volkening, K.2    Hammond, R.3    Yang, W.4    Strong, W.5
  • 59
    • 79952467898 scopus 로고    scopus 로고
    • TDP-43 potentiates alpha-synuclein toxicity to dopaminergic neurons in transgenic mice
    • Tian, T., C. Huang, J. Tong, M. Yang, H. Zhou, et al. 2011 TDP-43 potentiates alpha-synuclein toxicity to dopaminergic neurons in transgenic mice. Int. J. Biol. Sci. 7: 234-243.
    • (2011) Int. J. Biol. Sci. , vol.7 , pp. 234-243
    • Tian, T.1    Huang, C.2    Tong, J.3    Yang, M.4    Zhou, H.5
  • 60
    • 79953180492 scopus 로고    scopus 로고
    • Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
    • Tollervey, J. R., T. Curk, B. Rogelj, M. Briese, M. Cereda, et al. 2011 Characterizing the RNA targets and position-dependent splicing regulation by TDP-43. Nat. Neurosci. 14: 452-458.
    • (2011) Nat. Neurosci. , vol.14 , pp. 452-458
    • Tollervey, J.R.1    Curk, T.2    Rogelj, B.3    Briese, M.4    Cereda, M.5
  • 61
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska, I., S. Bell, N. J. Cairns, T. M. Miller, and R. H. Baloh, 2009 TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc. Natl. Acad. Sci. USA 106: 18809-18814.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 62
    • 67449141880 scopus 로고    scopus 로고
    • RNA-Seq-quantitative measurement of expression through massively parallel RNA-sequencing
    • Wilhelm, B. T., and J.-R. Landry, 2009 RNA-Seq-quantitative measurement of expression through massively parallel RNA-sequencing. Methods 48: 249-257.
    • (2009) Methods , vol.48 , pp. 249-257
    • Wilhelm, B.T.1    Landry, J.-R.2
  • 63
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton, M. J., L. M. Igaz, M. M. Wong, L. K. Kwong, J. Q. Trojanowski, et al. 2008 Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J. Biol. Chem. 283: 13302-13309.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13302-13309
    • Winton, M.J.1    Igaz, L.M.2    Wong, M.M.3    Kwong, L.K.4    Trojanowski, J.Q.5
  • 64
    • 22544459024 scopus 로고    scopus 로고
    • Developmental consequences of neuromuscular junctions with reduced presynaptic calcium channel function
    • Xing, B., A. Long, D. A. Harrison, and R. L. Cooper, 2005 Developmental consequences of neuromuscular junctions with reduced presynaptic calcium channel function. Synapse 57: 132-147.
    • (2005) Synapse , vol.57 , pp. 132-147
    • Xing, B.1    Long, A.2    Harrison, D.A.3    Cooper, R.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.