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Volumn 7, Issue 4, 2012, Pages

TDP-43 identified from a genome wide RNAi screen for SOD1 regulators

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; REGULATOR PROTEIN; TAR DNA BINDING PROTEIN; DNA BINDING PROTEIN; PROTEIN TDP-43; SMALL INTERFERING RNA; SUPEROXIDE DISMUTASE;

EID: 84860381354     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0035818     Document Type: Article
Times cited : (12)

References (52)
  • 1
    • 0027164824 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen DR, (1993) Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 364: 362.
    • (1993) Nature , vol.364 , pp. 362
    • Rosen, D.R.1
  • 2
    • 0032544674 scopus 로고    scopus 로고
    • Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1
    • Bruijn LI, Houseweart MK, Kato S, Anderson KL, Anderson SD, et al. (1998) Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 281: 1851-1854.
    • (1998) Science , vol.281 , pp. 1851-1854
    • Bruijn, L.I.1    Houseweart, M.K.2    Kato, S.3    Anderson, K.L.4    Anderson, S.D.5
  • 3
    • 0141642203 scopus 로고    scopus 로고
    • Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS mice
    • Clement AM, Nguyen MD, Roberts EA, Garcia ML, Boillee S, et al. (2003) Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS mice. Science 302: 113-117.
    • (2003) Science , vol.302 , pp. 113-117
    • Clement, A.M.1    Nguyen, M.D.2    Roberts, E.A.3    Garcia, M.L.4    Boillee, S.5
  • 4
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, 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
  • 5
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Sreedharan J, Blair IP, Tripathi VB, Hu X, Vance C, et al. (2008) TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319: 1668-1672.
    • (2008) Science , vol.319 , pp. 1668-1672
    • Sreedharan, J.1    Blair, I.P.2    Tripathi, V.B.3    Hu, X.4    Vance, C.5
  • 6
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord JM, Fridovich I, (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244: 6049-6055.
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 7
    • 0037168643 scopus 로고    scopus 로고
    • Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state
    • Lindberg MJ, Tibell L, Oliveberg M, (2002) Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state. Proc Natl Acad Sci U S A 99: 16607-16612.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16607-16612
    • Lindberg, M.J.1    Tibell, L.2    Oliveberg, M.3
  • 8
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne C, Polymenidou M, Cleveland DW, (2010) TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum Mol Genet 19: R46-64.
    • (2010) Hum Mol Genet , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 9
    • 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: 459-468.
    • (2011) Nat Neurosci , vol.14 , pp. 459-468
    • Polymenidou, M.1    Lagier-Tourenne, C.2    Hutt, K.R.3    Huelga, S.C.4    Moran, J.5
  • 10
    • 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, 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
  • 11
    • 0035978743 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis
    • Rowland LP, Shneider NA, (2001) Amyotrophic lateral sclerosis. N Engl J Med 344: 1688-1700.
    • (2001) N Engl J Med , vol.344 , pp. 1688-1700
    • Rowland, L.P.1    Shneider, N.A.2
  • 12
    • 34249946466 scopus 로고    scopus 로고
    • Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations
    • Mackenzie IR, Bigio EH, Ince PG, Geser F, Neumann M, et al. (2007) Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. Ann Neurol 61: 427-434.
    • (2007) Ann Neurol , vol.61 , pp. 427-434
    • Mackenzie, I.R.1    Bigio, E.H.2    Ince, P.G.3    Geser, F.4    Neumann, M.5
  • 13
    • 0035130371 scopus 로고    scopus 로고
    • Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein
    • Wigley WC, Stidham RD, Smith NM, Hunt JF, Thomas PJ, (2001) Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein. Nat Biotechnol 19: 131-136.
    • (2001) Nat Biotechnol , vol.19 , pp. 131-136
    • Wigley, W.C.1    Stidham, R.D.2    Smith, N.M.3    Hunt, J.F.4    Thomas, P.J.5
  • 14
    • 80053540457 scopus 로고    scopus 로고
    • A Screen to Identify Cellular Modulators of Soluble Levels of an Amyotrophic Lateral Sclerosis (ALS)-Causing Mutant SOD1
    • Somalinga BR, Miller GA, Malik HT, Wigley WC, Thomas PJ, (2011) A Screen to Identify Cellular Modulators of Soluble Levels of an Amyotrophic Lateral Sclerosis (ALS)-Causing Mutant SOD1. J Biomol Screen 16: 974-985.
    • (2011) J Biomol Screen , vol.16 , pp. 974-985
    • Somalinga, B.R.1    Miller, G.A.2    Malik, H.T.3    Wigley, W.C.4    Thomas, P.J.5
  • 15
    • 0014202305 scopus 로고
    • Characterization by in vitro complementation of a peptide corresponding to an operator-proximal segment of the beta-galactosidase structural gene of Escherichia coli
    • Ullmann A, Jacob F, Monod J, (1967) Characterization by in vitro complementation of a peptide corresponding to an operator-proximal segment of the beta-galactosidase structural gene of Escherichia coli. J Mol Biol 24: 339-343.
    • (1967) J Mol Biol , vol.24 , pp. 339-343
    • Ullmann, A.1    Jacob, F.2    Monod, J.3
  • 16
    • 48249099724 scopus 로고    scopus 로고
    • 50 bp deletion in the promoter for superoxide dismutase 1 (SOD1) reduces SOD1 expression in vitro and may correlate with increased age of onset of sporadic amyotrophic lateral sclerosis
    • Broom WJ, Greenway M, Sadri-Vakili G, Russ C, Auwarter KE, et al. (2008) 50 bp deletion in the promoter for superoxide dismutase 1 (SOD1) reduces SOD1 expression in vitro and may correlate with increased age of onset of sporadic amyotrophic lateral sclerosis. Amyotroph Lateral Scler 9: 229-237.
    • (2008) Amyotroph Lateral Scler , vol.9 , pp. 229-237
    • Broom, W.J.1    Greenway, M.2    Sadri-Vakili, G.3    Russ, C.4    Auwarter, K.E.5
  • 18
    • 80053524679 scopus 로고    scopus 로고
    • Engineering High-throughput protein stability assays for drug discovery
    • [MS Dissertation], University of Texas at Arlington
    • Kambuj PA, (2003) Engineering High-throughput protein stability assays for drug discovery. [MS Dissertation] University of Texas at Arlington.
    • (2003)
    • Kambuj, P.A.1
  • 19
    • 0033003760 scopus 로고    scopus 로고
    • A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays
    • Zhang JH, Chung TD, Oldenburg KR, (1999) A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays. J Biomol Screen 4: 67-73.
    • (1999) J Biomol Screen , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 20
    • 39049097168 scopus 로고    scopus 로고
    • Median absolute deviation to improve hit selection for genome-scale RNAi screens
    • Chung N, Zhang XD, Kreamer A, Locco L, Kuan PF, et al. (2008) Median absolute deviation to improve hit selection for genome-scale RNAi screens. J Biomol Screen 13: 149-158.
    • (2008) J Biomol Screen , vol.13 , pp. 149-158
    • Chung, N.1    Zhang, X.D.2    Kreamer, A.3    Locco, L.4    Kuan, P.F.5
  • 21
    • 34147198467 scopus 로고    scopus 로고
    • Synthetic lethal screen identification of chemosensitizer loci in cancer cells
    • Whitehurst AW, Bodemann BO, Cardenas J, Ferguson D, Girard L, et al. (2007) Synthetic lethal screen identification of chemosensitizer loci in cancer cells. Nature 446: 815-819.
    • (2007) Nature , vol.446 , pp. 815-819
    • Whitehurst, A.W.1    Bodemann, B.O.2    Cardenas, J.3    Ferguson, D.4    Girard, L.5
  • 22
    • 79952589652 scopus 로고    scopus 로고
    • TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1
    • McDonald KK, Aulas A, Destroismaisons L, Pickles S, Beleac E, et al. (2011) TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1. Hum Mol Genet 20: 1400-1410.
    • (2011) Hum Mol Genet , vol.20 , pp. 1400-1410
    • McDonald, K.K.1    Aulas, A.2    Destroismaisons, L.3    Pickles, S.4    Beleac, E.5
  • 23
    • 37549025044 scopus 로고    scopus 로고
    • A novel CpG-free vertebrate insulator silences the testis-specific SP-10 gene in somatic tissues: role for TDP-43 in insulator function
    • Abhyankar MM, Urekar C, Reddi PP, (2007) A novel CpG-free vertebrate insulator silences the testis-specific SP-10 gene in somatic tissues: role for TDP-43 in insulator function. 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
  • 24
    • 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: 28852-28859.
    • (2008) J Biol Chem , vol.283 , pp. 28852-28859
    • Bose, J.K.1    Wang, I.F.2    Hung, L.3    Tarn, W.Y.4    Shen, C.K.5
  • 25
    • 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: 36337-36343.
    • (2001) J Biol Chem , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 26
    • 79953174305 scopus 로고    scopus 로고
    • TDP-43 Is a Transcriptional Repressor: THE TESTIS-SPECIFIC MOUSE acrv1 GENE IS A TDP-43 TARGET IN VIVO
    • Lalmansingh AS, Urekar CJ, Reddi PP, (2011) TDP-43 Is a Transcriptional Repressor: THE TESTIS-SPECIFIC MOUSE acrv1 GENE IS A TDP-43 TARGET IN VIVO. J Biol Chem 286: 10970-10982.
    • (2011) J Biol Chem , vol.286 , pp. 10970-10982
    • Lalmansingh, A.S.1    Urekar, C.J.2    Reddi, P.P.3
  • 27
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe DJ, (2003) Folding proteins in fatal ways. Nature 426: 900-904.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 28
    • 0028856292 scopus 로고
    • Defective protein folding as a basis of human disease
    • Thomas PJ, Qu BH, Pedersen PL, (1995) Defective protein folding as a basis of human disease. Trends Biochem Sci 20: 456-459.
    • (1995) Trends Biochem Sci , vol.20 , pp. 456-459
    • Thomas, P.J.1    Qu, B.H.2    Pedersen, P.L.3
  • 29
    • 0032504710 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative diseases
    • Beal MF, (1998) Mitochondrial dysfunction in neurodegenerative diseases. Biochim Biophys Acta 1366: 211-223.
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 211-223
    • Beal, M.F.1
  • 30
    • 0033934734 scopus 로고    scopus 로고
    • Mitochondria and the pathogenesis of ALS
    • Beal MF, (2000) Mitochondria and the pathogenesis of ALS. Brain 123 (Pt 7): 1291-1292.
    • (2000) Brain , vol.123 , Issue.Pt 7 , pp. 1291-1292
    • Beal, M.F.1
  • 31
    • 0027397195 scopus 로고
    • Cell culture evidence for neuronal degeneration in amyotrophic lateral sclerosis being linked to glutamate AMPA/kainate receptors
    • Couratier P, Hugon J, Sindou P, Vallat JM, Dumas M, (1993) Cell culture evidence for neuronal degeneration in amyotrophic lateral sclerosis being linked to glutamate AMPA/kainate receptors. Lancet 341: 265-268.
    • (1993) Lancet , vol.341 , pp. 265-268
    • Couratier, P.1    Hugon, J.2    Sindou, P.3    Vallat, J.M.4    Dumas, M.5
  • 32
    • 13344286293 scopus 로고    scopus 로고
    • Knockout of glutamate transporters reveals a major role for astroglial transport in excitotoxicity and clearance of glutamate
    • Rothstein JD, Dykes-Hoberg M, Pardo CA, Bristol LA, Jin L, et al. (1996) Knockout of glutamate transporters reveals a major role for astroglial transport in excitotoxicity and clearance of glutamate. Neuron 16: 675-686.
    • (1996) Neuron , vol.16 , pp. 675-686
    • Rothstein, J.D.1    Dykes-Hoberg, M.2    Pardo, C.A.3    Bristol, L.A.4    Jin, L.5
  • 33
    • 0037734370 scopus 로고    scopus 로고
    • Mutations in dynein link motor neuron degeneration to defects in retrograde transport
    • Hafezparast M, Klocke R, Ruhrberg C, Marquardt A, Ahmad-Annuar A, et al. (2003) Mutations in dynein link motor neuron degeneration to defects in retrograde transport. Science 300: 808-812.
    • (2003) Science , vol.300 , pp. 808-812
    • Hafezparast, M.1    Klocke, R.2    Ruhrberg, C.3    Marquardt, A.4    Ahmad-Annuar, A.5
  • 34
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate, and neurodegenerative disorders
    • Coyle JT, Puttfarcken P, (1993) Oxidative stress, glutamate, and neurodegenerative disorders. Science 262: 689-695.
    • (1993) Science , vol.262 , pp. 689-695
    • Coyle, J.T.1    Puttfarcken, P.2
  • 35
    • 0032731637 scopus 로고    scopus 로고
    • ALS-linked Cu/Zn-SOD mutation increases vulnerability of motor neurons to excitotoxicity by a mechanism involving increased oxidative stress and perturbed calcium homeostasis
    • Kruman, II, Pedersen WA, Springer JE, Mattson MP, (1999) ALS-linked Cu/Zn-SOD mutation increases vulnerability of motor neurons to excitotoxicity by a mechanism involving increased oxidative stress and perturbed calcium homeostasis. Exp Neurol 160: 28-39.
    • (1999) Exp Neurol , vol.160 , pp. 28-39
    • Kruman, I.I.1    Pedersen, W.A.2    Springer, J.E.3    Mattson, M.P.4
  • 36
    • 43649100018 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis
    • Atkin JD, Farg MA, Walker AK, McLean C, Tomas D, et al. (2008) Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis. Neurobiol Dis 30: 400-407.
    • (2008) Neurobiol Dis , vol.30 , pp. 400-407
    • Atkin, J.D.1    Farg, M.A.2    Walker, A.K.3    McLean, C.4    Tomas, D.5
  • 37
    • 0030813067 scopus 로고    scopus 로고
    • Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis
    • Ferrante RJ, Browne SE, Shinobu LA, Bowling AC, Baik MJ, et al. (1997) Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis. J Neurochem 69: 2064-2074.
    • (1997) J Neurochem , vol.69 , pp. 2064-2074
    • Ferrante, R.J.1    Browne, S.E.2    Shinobu, L.A.3    Bowling, A.C.4    Baik, M.J.5
  • 38
    • 0030851761 scopus 로고    scopus 로고
    • Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis
    • Beal MF, Ferrante RJ, Browne SE, Matthews RT, Kowall NW, et al. (1997) Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis. Ann Neurol 42: 644-654.
    • (1997) Ann Neurol , vol.42 , pp. 644-654
    • Beal, M.F.1    Ferrante, R.J.2    Browne, S.E.3    Matthews, R.T.4    Kowall, N.W.5
  • 39
    • 77949910265 scopus 로고    scopus 로고
    • Review: transactive response DNA-binding protein 43 (TDP-43): mechanisms of neurodegeneration
    • Gendron TF, Josephs KA, Petrucelli L, (2010) Review: transactive response DNA-binding protein 43 (TDP-43): mechanisms of neurodegeneration. Neuropathol Appl Neurobiol 36: 97-112.
    • (2010) Neuropathol Appl Neurobiol , vol.36 , pp. 97-112
    • Gendron, T.F.1    Josephs, K.A.2    Petrucelli, L.3
  • 40
    • 42649120983 scopus 로고    scopus 로고
    • TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
    • Kabashi E, Valdmanis PN, Dion P, Spiegelman D, McConkey BJ, et al. (2008) TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat Genet 40: 572-574.
    • (2008) Nat Genet , vol.40 , pp. 572-574
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3    Spiegelman, D.4    McConkey, B.J.5
  • 41
    • 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, et al. (2010) Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis. J Neurosci 30: 639-649.
    • (2010) J Neurosci , vol.30 , pp. 639-649
    • Barmada, S.J.1    Skibinski, G.2    Korb, E.3    Rao, E.J.4    Wu, J.Y.5
  • 42
    • 34249313704 scopus 로고    scopus 로고
    • Lack of TDP-43 abnormalities in mutant SOD1 transgenic mice shows disparity with ALS
    • Robertson J, Sanelli T, Xiao S, Yang W, Horne P, et al. (2007) Lack of TDP-43 abnormalities in mutant SOD1 transgenic mice shows disparity with ALS. Neurosci Lett 420: 128-132.
    • (2007) Neurosci Lett , vol.420 , pp. 128-132
    • Robertson, J.1    Sanelli, T.2    Xiao, S.3    Yang, W.4    Horne, P.5
  • 43
    • 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: 1104-1120.
    • (2010) J Proteome Res , vol.9 , pp. 1104-1120
    • Freibaum, B.D.1    Chitta, R.K.2    High, A.A.3    Taylor, J.P.4
  • 44
    • 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
    • Buratti E, Brindisi A, Giombi M, Tisminetzky S, Ayala YM, et al. (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: 37572-37584.
    • (2005) J Biol Chem , vol.280 , pp. 37572-37584
    • Buratti, E.1    Brindisi, A.2    Giombi, M.3    Tisminetzky, S.4    Ayala, Y.M.5
  • 45
  • 46
    • 25144498379 scopus 로고    scopus 로고
    • A human protein-protein interaction network: a resource for annotating the proteome
    • Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, et al. (2005) A human protein-protein interaction network: a resource for annotating the proteome. Cell 122: 957-968.
    • (2005) Cell , vol.122 , pp. 957-968
    • Stelzl, U.1    Worm, U.2    Lalowski, M.3    Haenig, C.4    Brembeck, F.H.5
  • 47
    • 41649106307 scopus 로고    scopus 로고
    • TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression
    • Ayala YM, Misteli T, Baralle FE, (2008) TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression. Proc Natl Acad Sci U S A 105: 3785-3789.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3785-3789
    • Ayala, Y.M.1    Misteli, T.2    Baralle, F.E.3
  • 48
    • 75649135319 scopus 로고    scopus 로고
    • Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6
    • Fiesel FC, Voigt A, Weber SS, Van den Haute C, Waldenmaier A, et al. (2009) Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6. EMBO J 29: 209-221.
    • (2009) EMBO J , vol.29 , pp. 209-221
    • Fiesel, F.C.1    Voigt, A.2    Weber, S.S.3    van den Haute, C.4    Waldenmaier, A.5
  • 49
    • 0036618178 scopus 로고    scopus 로고
    • Preferential transformation of human neuronal cells by human adenoviruses and the origin of HEK 293 cells
    • Shaw G, Morse S, Ararat M, Graham FL, (2002) Preferential transformation of human neuronal cells by human adenoviruses and the origin of HEK 293 cells. FASEB J 16: 869-871.
    • (2002) FASEB J , vol.16 , pp. 869-871
    • Shaw, G.1    Morse, S.2    Ararat, M.3    Graham, F.L.4
  • 50
    • 0037080819 scopus 로고    scopus 로고
    • A masked NES in INI1/hSNF5 mediates hCRM1-dependent nuclear export: implications for tumorigenesis
    • Craig E, Zhang ZK, Davies KP, Kalpana GV, (2002) A masked NES in INI1/hSNF5 mediates hCRM1-dependent nuclear export: implications for tumorigenesis. EMBO J 21: 31-42.
    • (2002) EMBO J , vol.21 , pp. 31-42
    • Craig, E.1    Zhang, Z.K.2    Davies, K.P.3    Kalpana, G.V.4
  • 51
    • 68349112682 scopus 로고    scopus 로고
    • Statistical methods for analysis of high-throughput RNA interference screens
    • Birmingham A, Selfors LM, Forster T, Wrobel D, Kennedy CJ, et al. (2009) Statistical methods for analysis of high-throughput RNA interference screens. Nat Methods 6: 569-575.
    • (2009) Nat Methods , vol.6 , pp. 569-575
    • Birmingham, A.1    Selfors, L.M.2    Forster, T.3    Wrobel, D.4    Kennedy, C.J.5
  • 52
    • 11144337833 scopus 로고    scopus 로고
    • Quantitative real-time PCR protocol for analysis of nuclear receptor signaling pathways
    • Bookout AL, Mangelsdorf DJ, (2003) Quantitative real-time PCR protocol for analysis of nuclear receptor signaling pathways. Nucl Recept Signal 1: e012.
    • (2003) Nucl Recept Signal , vol.1
    • Bookout, A.L.1    Mangelsdorf, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.