메뉴 건너뛰기




Volumn 7, Issue 1, 2012, Pages

Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP

Author keywords

ALS; Cell death; FUS TLS; G3BP; Oxidative stress; Stress granules; TDP 43; TIA 1

Indexed keywords

CELL PROTEIN; G3BP PROTEIN; TAR DNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84867686875     PISSN: None     EISSN: 17501326     Source Type: Journal    
DOI: 10.1186/1750-1326-7-54     Document Type: Article
Times cited : (103)

References (49)
  • 1
    • 70350075024 scopus 로고    scopus 로고
    • Genetics of motor neuron disorders: New insights into pathogenic mechanisms
    • 19823194
    • Genetics of motor neuron disorders: new insights into pathogenic mechanisms. Dion PA, Daoud H, Rouleau GA, Nat Rev Genet 2009 10 769 782 19823194
    • (2009) Nat Rev Genet , vol.10 , pp. 769-782
    • Dion, P.A.1    Daoud, H.2    Rouleau, G.A.3
  • 4
    • 62149141328 scopus 로고    scopus 로고
    • Rethinking ALS: The FUS about TDP-43
    • 10.1016/j.cell.2009.03.006 19303844
    • Rethinking ALS: the FUS about TDP-43. Lagier-Tourenne C, Cleveland DW, Cell 2009 136 1001 1004 10.1016/j.cell.2009.03.006 19303844
    • (2009) Cell , vol.136 , pp. 1001-1004
    • Lagier-Tourenne, C.1    Cleveland, D.W.2
  • 5
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • 10.1126/science.1166066 19251627
    • 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, Russ C, et al. Science 2009 323 1205 1208 10.1126/science.1166066 19251627
    • (2009) Science , vol.323 , pp. 1205-1208
    • Kwiatkowski Jr., T.J.1    Bosco, D.A.2    Leclerc, A.L.3    Tamrazian, E.4    Vanderburg, C.R.5    Russ, C.6
  • 6
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6
    • 10.1126/science.1165942 19251628
    • 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, Sreedharan J, et al. Science 2009 323 1208 1211 10.1126/science.1165942 19251628
    • (2009) Science , vol.323 , pp. 1208-1211
    • Vance, C.1    Rogelj, B.2    Hortobagyi, T.3    De Vos, K.J.4    Nishimura, A.L.5    Sreedharan, J.6
  • 7
    • 65749119848 scopus 로고    scopus 로고
    • Stress granules
    • 10.1016/j.cub.2009.03.013 19467203
    • Stress granules. Anderson P, Kedersha N, Curr Biol 2009 19 397 R398 10.1016/j.cub.2009.03.013 19467203
    • (2009) Curr Biol , vol.19
    • Anderson, P.1    Kedersha, N.2
  • 8
    • 39949085583 scopus 로고    scopus 로고
    • Stress granules: The Tao of RNA triage
    • 10.1016/j.tibs.2007.12.003 18291657
    • Stress granules: the Tao of RNA triage. Anderson P, Kedersha N, Trends Biochem Sci 2008 33 141 150 10.1016/j.tibs.2007.12.003 18291657
    • (2008) Trends Biochem Sci , vol.33 , pp. 141-150
    • Anderson, P.1    Kedersha, N.2
  • 11
    • 0036863320 scopus 로고    scopus 로고
    • Stress granules: Sites of mRNA triage that regulate mRNA stability and translatability
    • DOI 10.1042/BST0300963
    • Stress granules: sites of mRNA triage that regulate mRNA stability and translatability. Kedersha N, Anderson P, Biochem Soc Trans 2002 30 963 969 12440955 (Pubitemid 36002389)
    • (2002) Biochemical Society Transactions , vol.30 , Issue.6 , pp. 963-969
    • Kedersha, N.1    Anderson, P.2
  • 12
    • 79952589652 scopus 로고    scopus 로고
    • TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1
    • 10.1093/hmg/ddr021 21257637
    • 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, Camu W, et al. Hum Mol Genet 2011 20 1400 1410 10.1093/hmg/ddr021 21257637
    • (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    Camu, W.6
  • 13
    • 33746516731 scopus 로고    scopus 로고
    • HnRNP A1 relocalization to the stress granules reflects a role in the stress response
    • DOI 10.1128/MCB.00224-06
    • hnRNP A1 relocalization to the stress granules reflects a role in the stress response. Guil S, Long JC, Caceres JF, Mol Cell Biol 2006 26 5744 5758 10.1128/MCB.00224-06 16847328 (Pubitemid 44134331)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.15 , pp. 5744-5758
    • Guil, S.1    Long, J.C.2    Caceres, J.F.3
  • 14
    • 79955560592 scopus 로고    scopus 로고
    • SMN deficiency reduces cellular ability to form stress granules, sensitizing cells to stress
    • 10.1007/s10571-011-9647-8 21234798
    • SMN deficiency reduces cellular ability to form stress granules, sensitizing cells to stress. Zou T, Yang X, Pan D, Huang J, Sahin M, Zhou J, Cell Mol Neurobiol 2011 31 541 550 10.1007/s10571-011-9647-8 21234798
    • (2011) Cell Mol Neurobiol , vol.31 , pp. 541-550
    • Zou, T.1    Yang, X.2    Pan, D.3    Huang, J.4    Sahin, M.5    Zhou, J.6
  • 15
    • 82355184529 scopus 로고    scopus 로고
    • Monocyte chemotactic protein-induced protein 1 (MCPIP1) suppresses stress granule formation and determines apoptosis under stress
    • 10.1074/jbc.M111.276006 21971051
    • Monocyte chemotactic protein-induced protein 1 (MCPIP1) suppresses stress granule formation and determines apoptosis under stress. Qi D, Huang S, Miao R, She ZG, Quinn T, Chang Y, et al. J Biol Chem 2011 286 41692 41700 10.1074/jbc.M111.276006 21971051
    • (2011) J Biol Chem , vol.286 , pp. 41692-41700
    • Qi, D.1    Huang, S.2    Miao, R.3    She, Z.G.4    Quinn, T.5    Chang, Y.6
  • 16
    • 63049130206 scopus 로고    scopus 로고
    • Cells lacking the fragile X mental retardation protein (FMRP) have normal RISC activity but exhibit altered stress granule assembly
    • 10.1091/mbc.E08-07-0737 19005212
    • Cells lacking the fragile X mental retardation protein (FMRP) have normal RISC activity but exhibit altered stress granule assembly. Didiot MC, Subramanian M, Flatter E, Mandel JL, Moine H, Mol Biol Cell 2009 20 428 437 10.1091/mbc.E08-07-0737 19005212
    • (2009) Mol Biol Cell , vol.20 , pp. 428-437
    • Didiot, M.C.1    Subramanian, M.2    Flatter, E.3    Mandel, J.L.4    Moine, H.5
  • 17
    • 4143097170 scopus 로고    scopus 로고
    • Survival motor neuron protein facilitates assembly of stress granules
    • DOI 10.1016/j.febslet.2004.07.010, PII S0014579304008671
    • Survival motor neuron protein facilitates assembly of stress granules. Hua Y, Zhou J, FEBS Lett 2004 572 69 74 10.1016/j.febslet.2004.07.010 15304326 (Pubitemid 39092515)
    • (2004) FEBS Letters , vol.572 , Issue.1-3 , pp. 69-74
    • Hua, Y.1    Zhou, J.2
  • 19
    • 79953200132 scopus 로고    scopus 로고
    • PolyQ Repeat Expansions in ATXN2 associated with ALS Are CAA interrupted repeats
    • 10.1371/journal.pone.0017951 21479228
    • PolyQ Repeat Expansions in ATXN2 Associated with ALS Are CAA Interrupted Repeats. Yu Z, Zhu Y, Chen-Plotkin AS, Clay-Falcone D, McCluskey L, Elman L, et al. PLoS One 2011 6 17951 10.1371/journal.pone.0017951 21479228
    • (2011) PLoS One , vol.6 , pp. 517951
    • Yu, Z.1    Zhu, Y.2    Chen-Plotkin, A.S.3    Clay-Falcone, D.4    McCluskey, L.5    Elman, L.6
  • 20
    • 79953176451 scopus 로고    scopus 로고
    • Ataxin-2 intermediate-length polyglutamine expansions in European ALS patients
    • 10.1093/hmg/ddr045 21292779
    • Ataxin-2 intermediate-length polyglutamine expansions in European ALS patients. Lee T, Li YR, Ingre C, Weber M, Grehl T, Gredal O, et al. Hum Mol Genet 2011 20 1697 1700 10.1093/hmg/ddr045 21292779
    • (2011) Hum Mol Genet , vol.20 , pp. 1697-1700
    • Lee, T.1    Li, Y.R.2    Ingre, C.3    Weber, M.4    Grehl, T.5    Gredal, O.6
  • 21
    • 77956155218 scopus 로고    scopus 로고
    • Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS
    • 10.1038/nature09320 20740007
    • Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS. Elden AC, Kim HJ, Hart MP, Chen-Plotkin AS, Johnson BS, Fang X, et al. Nature 2010 466 1069 1075 10.1038/nature09320 20740007
    • (2010) Nature , vol.466 , pp. 1069-1075
    • Elden, A.C.1    Kim, H.J.2    Hart, M.P.3    Chen-Plotkin, A.S.4    Johnson, B.S.5    Fang, X.6
  • 22
    • 79958746230 scopus 로고    scopus 로고
    • Association of Long ATXN2 CAG repeat sizes with increased risk of amyotrophic lateral sclerosis
    • 10.1001/archneurol.2011.111 21670397
    • Association of Long ATXN2 CAG Repeat Sizes With Increased Risk of Amyotrophic Lateral Sclerosis. Daoud H, Belzil V, Martins S, Sabbagh M, Provencher P, Lacomblez L, et al. Arch Neurol 2011 68 739 742 10.1001/archneurol.2011.111 21670397
    • (2011) Arch Neurol , vol.68 , pp. 739-742
    • Daoud, H.1    Belzil, V.2    Martins, S.3    Sabbagh, M.4    Provencher, P.5    Lacomblez, L.6
  • 23
    • 78149461229 scopus 로고    scopus 로고
    • Tar DNA binding protein-43 (TDP-43) associates with stress granules: Analysis of cultured cells and pathological brain tissue
    • 10.1371/journal.pone.0013250 20948999
    • Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue. Liu-Yesucevitz L, Bilgutay A, Zhang YJ, Vanderwyde T, Citro A, Mehta T, et al. PLoS One 2010 5 13250 10.1371/journal.pone.0013250 20948999
    • (2010) PLoS One , vol.5 , pp. 513250
    • Liu-Yesucevitz, L.1    Bilgutay, A.2    Zhang, Y.J.3    Vanderwyde, T.4    Citro, A.5    Mehta, T.6
  • 24
    • 79952268025 scopus 로고    scopus 로고
    • TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor
    • 21173160
    • TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor. Dewey CM, Cenik B, Sephton CF, Dries DR, Mayer P III, Good SK, et al. Mol Cell Biol 2010 31 1098 1108 21173160
    • (2010) Mol Cell Biol , vol.31 , pp. 1098-1108
    • Dewey, C.M.1    Cenik, B.2    Sephton, C.F.3    Dries, D.R.4    Iii, M.P.5    Good, S.K.6
  • 25
    • 70350135049 scopus 로고    scopus 로고
    • TDP-43 is recruited to stress granules in conditions of oxidative insult
    • 10.1111/j.1471-4159.2009.06383.x 19765185
    • TDP-43 is recruited to stress granules in conditions of oxidative insult. Colombrita C, Zennaro E, Fallini C, Weber M, Sommacal A, Buratti E, et al. J Neurochem 2009 111 1051 1061 10.1111/j.1471-4159.2009.06383.x 19765185
    • (2009) J Neurochem , vol.111 , pp. 1051-1061
    • Colombrita, C.1    Zennaro, E.2    Fallini, C.3    Weber, M.4    Sommacal, A.5    Buratti, E.6
  • 26
    • 77957875397 scopus 로고    scopus 로고
    • Nuclear localization sequence of FUS and induction of stress granules by ALS mutants
    • Nuclear localization sequence of FUS and induction of stress granules by ALS mutants. Gal J, Zhang J, Kwinter DM, Zhai J, Jia H, Jia J, et al. Neurobiol Aging 2010 32 2323.e27 2323.e40
    • (2010) Neurobiol Aging , vol.32
    • Gal, J.1    Zhang, J.2    Kwinter, D.M.3    Zhai, J.4    Jia, H.5    Jia, J.6
  • 27
    • 77957867303 scopus 로고    scopus 로고
    • Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules
    • 10.1093/hmg/ddq335 20699327
    • Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules. Bosco DA, Lemay N, Ko HK, Zhou H, Burke C, Kwiatkowski TJ Jr, et al. Hum Mol Genet 2010 19 4160 4175 10.1093/hmg/ddq335 20699327
    • (2010) Hum Mol Genet , vol.19 , pp. 4160-4175
    • Bosco, D.A.1    Lemay, N.2    Ko, H.K.3    Zhou, H.4    Burke, C.5    Kwiatkowski Jr., T.J.6
  • 28
    • 77955792022 scopus 로고    scopus 로고
    • ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import
    • 10.1038/emboj.2010.143 20606625
    • ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import. Dormann D, Rodde R, Edbauer D, Bentmann E, Fischer I, Hruscha A, et al. EMBO J 2010 29 2841 2857 10.1038/emboj.2010.143 20606625
    • (2010) EMBO J , vol.29 , pp. 2841-2857
    • Dormann, D.1    Rodde, R.2    Edbauer, D.3    Bentmann, E.4    Fischer, I.5    Hruscha, A.6
  • 29
    • 77955897545 scopus 로고    scopus 로고
    • Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations
    • 10.1212/WNL.0b013e3181ed9cde 20668261
    • Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations. Baumer D, Hilton D, Paine SM, Turner MR, Lowe J, Talbot K, et al. Neurology 2010 75 611 618 10.1212/WNL.0b013e3181ed9cde 20668261
    • (2010) Neurology , vol.75 , pp. 611-618
    • Baumer, D.1    Hilton, D.2    Paine, S.M.3    Turner, M.R.4    Lowe, J.5    Talbot, K.6
  • 30
    • 84857124994 scopus 로고    scopus 로고
    • Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates
    • 10.1016/j.neuint.2012.01.019 22306778
    • Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates. Parker SJ, Meyerowitz J, James JL, Liddell JR, Crouch PJ, Kanninen KM, et al. Neurochem Int 2012 60 415 424 10.1016/j.neuint.2012.01.019 22306778
    • (2012) Neurochem Int , vol.60 , pp. 415-424
    • Parker, S.J.1    Meyerowitz, J.2    James, J.L.3    Liddell, J.R.4    Crouch, P.J.5    Kanninen, K.M.6
  • 31
    • 84155167265 scopus 로고    scopus 로고
    • Gains or losses: Molecular mechanisms of TDP43-mediated neurodegeneration
    • Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration. Lee EB, Lee VM, Trojanowski JQ, Nat Rev Neurosci 2012 13 38 50
    • (2012) Nat Rev Neurosci , vol.13 , pp. 38-50
    • Lee, E.B.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 32
    • 80052967905 scopus 로고    scopus 로고
    • TDP-43: The relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • 10.1111/j.1742-4658.2011.08256.x 21777387
    • TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Baloh RH, FEBS J 2011 278 3539 3549 10.1111/j.1742-4658.2011. 08256.x 21777387
    • (2011) FEBS J , vol.278 , pp. 3539-3549
    • Baloh, R.H.1
  • 33
    • 79955812764 scopus 로고    scopus 로고
    • TDP-43-based animal models of neurodegeneration: New insights into ALS pathology and pathophysiology
    • 10.1159/000321547 21124004
    • TDP-43-based animal models of neurodegeneration: new insights into ALS pathology and pathophysiology. Wegorzewska I, Baloh RH, Neurodegener Dis 2011 8 262 274 10.1159/000321547 21124004
    • (2011) Neurodegener Dis , vol.8 , pp. 262-274
    • Wegorzewska, I.1    Baloh, R.H.2
  • 36
    • 40949135034 scopus 로고    scopus 로고
    • Regulation of stress granule dynamics by Grb7 and FAK signalling pathway
    • DOI 10.1038/emboj.2008.19, PII EMBOJ200819
    • Regulation of stress granule dynamics by Grb7 and FAK signalling pathway. Tsai NP, Ho PC, Wei LN, EMBO J 2008 27 715 726 10.1038/emboj.2008.19 18273060 (Pubitemid 351506682)
    • (2008) EMBO Journal , vol.27 , Issue.5 , pp. 715-726
    • Tsai, N.-P.1    Ho, P.-C.2    Wei, L.-N.3
  • 37
    • 75649135319 scopus 로고    scopus 로고
    • Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6
    • 10.1038/emboj.2009.324 19910924
    • Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6. Fiesel FC, Voigt A, Weber SS, Van den HC, Waldenmaier A, Gorner K, et al. EMBO J 2010 29 209 221 10.1038/emboj.2009.324 19910924
    • (2010) EMBO J , vol.29 , pp. 209-221
    • Fiesel, F.C.1    Voigt, A.2    Weber, S.S.3    Van Den, H.C.4    Waldenmaier, A.5    Gorner, K.6
  • 38
    • 79959869692 scopus 로고    scopus 로고
    • FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis
    • 10.1007/s13238-011-1525-0 21452073
    • FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis. Kryndushkin D, Wickner RB, Shewmaker F, Protein Cell 2011 2 223 236 10.1007/s13238-011-1525-0 21452073
    • (2011) Protein Cell , vol.2 , pp. 223-236
    • Kryndushkin, D.1    Wickner, R.B.2    Shewmaker, F.3
  • 39
    • 78449275449 scopus 로고    scopus 로고
    • ALS-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to coregulate HDAC6 mRNA
    • ALS-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to coregulate HDAC6 mRNA. Kim SH, Shanware N, Bowler MJ, Tibbetts RS, J Biol Chem 2010 286 12766 12774
    • (2010) J Biol Chem , vol.286 , pp. 12766-12774
    • Kim, S.H.1    Shanware, N.2    Bowler, M.J.3    Tibbetts, R.S.4
  • 40
    • 84857410364 scopus 로고    scopus 로고
    • Mutant TDP-43 and FUS Cause Age-Dependent Paralysis and Neurodegeneration in C. elegans
    • 10.1371/journal.pone.0031321 22363618
    • Mutant TDP-43 and FUS Cause Age-Dependent Paralysis and Neurodegeneration in C. elegans. Vaccaro A, Tauffenberger A, Aggad D, Rouleau G, Drapeau P, Parker JA, PLoS One 2012 7 31321 10.1371/journal.pone.0031321 22363618
    • (2012) PLoS One , vol.7 , pp. 531321
    • Vaccaro, A.1    Tauffenberger, A.2    Aggad, D.3    Rouleau, G.4    Drapeau, P.5    Parker, J.A.6
  • 41
    • 79953185674 scopus 로고    scopus 로고
    • Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
    • 10.1038/nn.2779 21358643
    • 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, Liang TY, et al. Nat Neurosci 2011 14 459 468 10.1038/nn.2779 21358643
    • (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    Liang, T.Y.6
  • 42
    • 35848929915 scopus 로고    scopus 로고
    • Inhibition of Cytoplasmic mRNA Stress Granule Formation by a Viral Proteinase
    • DOI 10.1016/j.chom.2007.08.006, PII S1931312807002223
    • Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase. White JP, Cardenas AM, Marissen WE, Lloyd RE, Cell Host Microbe 2007 2 295 305 10.1016/j.chom.2007.08.006 18005751 (Pubitemid 350056396)
    • (2007) Cell Host and Microbe , vol.2 , Issue.5 , pp. 295-305
    • White, J.P.1    Cardenas, A.M.2    Marissen, W.E.3    Lloyd, R.E.4
  • 43
    • 77949389673 scopus 로고    scopus 로고
    • Stable formation of compositionally unique stress granules in virus-infected cells
    • 10.1128/JVI.01320-09 20106928
    • Stable formation of compositionally unique stress granules in virus-infected cells. Piotrowska J, Hansen SJ, Park N, Jamka K, Sarnow P, Gustin KE, J Virol 2010 84 3654 3665 10.1128/JVI.01320-09 20106928
    • (2010) J Virol , vol.84 , pp. 3654-3665
    • Piotrowska, J.1    Hansen, S.J.2    Park, N.3    Jamka, K.4    Sarnow, P.5    Gustin, K.E.6
  • 44
    • 25444523445 scopus 로고    scopus 로고
    • Control of fetal growth and neonatal survival by the RasGAP-associated endoribonuclease G3BP
    • DOI 10.1128/MCB.25.19.8703-8716.2005
    • Control of fetal growth and neonatal survival by the RasGAP-associated endoribonuclease G3BP. Zekri L, Chebli K, Tourriere H, Nielsen FC, Hansen TV, Rami A, et al. Mol Cell Biol 2005 25 8703 8716 10.1128/MCB.25.19.8703-8716.2005 16166649 (Pubitemid 41369188)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.19 , pp. 8703-8716
    • Zekri, L.1    Chebli, K.2    Tourriere, H.3    Nielsen, F.C.4    Hansen, T.V.O.5    Rami, A.6    Tazi, J.7
  • 45
    • 83455162720 scopus 로고    scopus 로고
    • Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations
    • 10.1093/hmg/ddr448 21965298
    • Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations. Tradewell ML, Yu Z, Tibshirani M, Boulanger MC, Durham HD, Richard S, Hum Mol Genet 2012 21 136 149 10.1093/hmg/ddr448 21965298
    • (2012) Hum Mol Genet , vol.21 , pp. 136-149
    • Tradewell, M.L.1    Yu, Z.2    Tibshirani, M.3    Boulanger, M.C.4    Durham, H.D.5    Richard, S.6
  • 46
    • 80053625750 scopus 로고    scopus 로고
    • Translational coregulation of 5'TOP mRNAs by TIA-1 and TIAR
    • 10.1101/gad.17355911 21979918
    • Translational coregulation of 5'TOP mRNAs by TIA-1 and TIAR. Damgaard CK, Lykke-Andersen J, Genes Dev 2011 25 2057 2068 10.1101/gad.17355911 21979918
    • (2011) Genes Dev , vol.25 , pp. 2057-2068
    • Damgaard, C.K.1    Lykke-Andersen, J.2
  • 47
    • 0026091180 scopus 로고
    • A polyadenylate binding protein localized to the granules of cytolytic lymphocytes induces DNA fragmentation in target cells
    • A polyadenylate binding protein localized to the granules of cytolytic lymphocytes induces DNA fragmentation in target cells. Tian Q, Streuli M, Saito H, Schlossman SF, Anderson P, Cell 1991 67 629 639 10.1016/0092-8674(91)90536-8 1934064 (Pubitemid 121001476)
    • (1991) Cell , vol.67 , Issue.3 , pp. 629-639
    • Tian, Q.1    Streuli, M.2    Saito, H.3    Schlossman, S.F.4    Anderson, P.5
  • 48
    • 80755143679 scopus 로고    scopus 로고
    • Local RNA translation at the synapse and in disease
    • 10.1523/JNEUROSCI.4105-11.2011 22072660
    • Local RNA translation at the synapse and in disease. Liu-Yesucevitz L, Bassell GJ, Gitler AD, Hart AC, Klann E, Richter JD, et al. J Neurosci 2011 31 16086 16093 10.1523/JNEUROSCI.4105-11.2011 22072660
    • (2011) J Neurosci , vol.31 , pp. 16086-16093
    • Liu-Yesucevitz, L.1    Bassell, G.J.2    Gitler, A.D.3    Hart, A.C.4    Klann, E.5    Richter, J.D.6
  • 49
    • 60849118924 scopus 로고    scopus 로고
    • Dynein motor contributes to stress granule dynamics in primary neurons
    • 10.1016/j.neuroscience.2008.12.053 19171178
    • Dynein motor contributes to stress granule dynamics in primary neurons. Tsai NP, Tsui YC, Wei LN, Neuroscience 2009 159 647 656 10.1016/j.neuroscience. 2008.12.053 19171178
    • (2009) Neuroscience , vol.159 , pp. 647-656
    • Tsai, N.P.1    Tsui, Y.C.2    Wei, L.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.