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Volumn 7, Issue 11, 2012, Pages

The Effect of PRMT1-Mediated Arginine Methylation on the Subcellular Localization, Stress Granules, and Detergent-Insoluble Aggregates of FUS/TLS

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; FUSED IN SARCOMA PROTEIN; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE 1; UNCLASSIFIED DRUG;

EID: 84869005887     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0049267     Document Type: Article
Times cited : (87)

References (59)
  • 1
    • 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-R64.
    • (2010) Hum Mol Genet , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 2
    • 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
  • 3
    • 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: 1208-1211.
    • (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
  • 4
    • 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: 1205-1208.
    • (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
  • 5
    • 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: 1001-1004.
    • (2009) Cell , vol.136 , pp. 1001-1004
    • Lagier-Tourenne, C.1    Cleveland, D.W.2
  • 6
    • 84155167265 scopus 로고    scopus 로고
    • Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration Nature Reviews Neuroscience
    • Edward B Lee, Virginia M.-Y.Lee & John Q Trojanowski, (2011) Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration Nature Reviews Neuroscience. 13: 38-50.
    • (2011) , vol.13 , pp. 38-50
    • Edward, B.L.1    Virginia, M.-Y.L.2    John, Q.T.3
  • 7
    • 79952843316 scopus 로고    scopus 로고
    • RNA-binding proteins and RNA metabolism: a new scenario in the pathogenesis of Amyotrophic lateral sclerosis
    • Colombrita C, Onesto E, Tiloca C, Ticozzi N, Silani V, et al. (2011) RNA-binding proteins and RNA metabolism: a new scenario in the pathogenesis of Amyotrophic lateral sclerosis. Arch Ital Biol 149: 83-99.
    • (2011) Arch Ital Biol , vol.149 , pp. 83-99
    • Colombrita, C.1    Onesto, E.2    Tiloca, C.3    Ticozzi, N.4    Silani, V.5
  • 8
  • 9
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, et al. (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun 351: 602-611.
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3    Ikeda, K.4    Nonaka, T.5
  • 10
    • 70350673956 scopus 로고    scopus 로고
    • A new subtype of frontotemporal lobar degeneration with FUS pathology
    • Neumann M, Rademakers R, Roeber S, Baker M, Kretzschmar HA, et al. (2009) A new subtype of frontotemporal lobar degeneration with FUS pathology. Brain 132: 2922-2931.
    • (2009) Brain , vol.132 , pp. 2922-2931
    • Neumann, M.1    Rademakers, R.2    Roeber, S.3    Baker, M.4    Kretzschmar, H.A.5
  • 11
    • 34547663747 scopus 로고    scopus 로고
    • TDP-43 in familial and sporadic frontotemporal lobar degeneration with ubiquitin inclusions
    • Cairns NJ, Neumann M, Bigio EH, Holm IE, Troost D, et al. (2007) TDP-43 in familial and sporadic frontotemporal lobar degeneration with ubiquitin inclusions. Am J Pathol 171: 227-240.
    • (2007) Am J Pathol , vol.171 , pp. 227-240
    • Cairns, N.J.1    Neumann, M.2    Bigio, E.H.3    Holm, I.E.4    Troost, D.5
  • 13
    • 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) 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. EMBO J 15: 5022-5031.
    • (1996) EMBO J , vol.15 , pp. 5022-5031
    • Bertolotti, A.1    Lutz, Y.2    Heard, D.J.3    Chambon, P.4    Tora, L.5
  • 14
    • 77955792022 scopus 로고    scopus 로고
    • ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import
    • Dormann D, Rodde R, Edbauer D, Bentmann E, Fischer I, et al. (2010) ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import. EMBO J 29: 2841-2857.
    • (2010) EMBO J , vol.29 , pp. 2841-2857
    • Dormann, D.1    Rodde, R.2    Edbauer, D.3    Bentmann, E.4    Fischer, I.5
  • 15
    • 0032561190 scopus 로고    scopus 로고
    • Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing
    • Yang L, Embree LJ, Tsai S, Hickstein DD, (1998) Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing. J Biol Chem 273: 27761-27764.
    • (1998) J Biol Chem , vol.273 , pp. 27761-27764
    • Yang, L.1    Embree, L.J.2    Tsai, S.3    Hickstein, D.D.4
  • 16
    • 0033607753 scopus 로고    scopus 로고
    • Human 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formation
    • Baechtold H, Kuroda M, Sok J, Ron D, Lopez BS, et al. (1999) Human 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formation. J Biol Chem 274: 34337-34342.
    • (1999) J Biol Chem , vol.274 , pp. 34337-34342
    • Baechtold, H.1    Kuroda, M.2    Sok, J.3    Ron, D.4    Lopez, B.S.5
  • 17
    • 0027948152 scopus 로고
    • TLS/FUS fusion domain of TLS/FUS-erg chimeric protein resulting from the t(16;21) chromosomal translocation in human myeloid leukemia functions as a transcriptional activation domain
    • Prasad DD, Ouchida M, Lee L, Rao VN, Reddy ES, (1994) TLS/FUS fusion domain of TLS/FUS-erg chimeric protein resulting from the t(16;21) chromosomal translocation in human myeloid leukemia functions as a transcriptional activation domain. Oncogene 9: 3717-3729.
    • (1994) Oncogene , vol.9 , pp. 3717-3729
    • Prasad, D.D.1    Ouchida, M.2    Lee, L.3    Rao, V.N.4    Reddy, E.S.5
  • 18
    • 0033527059 scopus 로고    scopus 로고
    • Human POMp75 is identified as the pro-oncoprotein TLS/FUS: both POMp75 and POMp100 DNA homologous pairing activities are associated to cell proliferation
    • Bertrand P, Akhmedov AT, Delacote F, Durrbach A, Lopez BS, (1999) Human POMp75 is identified as the pro-oncoprotein TLS/FUS: both POMp75 and POMp100 DNA homologous pairing activities are associated to cell proliferation. Oncogene 18: 4515-4521.
    • (1999) Oncogene , vol.18 , pp. 4515-4521
    • Bertrand, P.1    Akhmedov, A.T.2    Delacote, F.3    Durrbach, A.4    Lopez, B.S.5
  • 19
    • 15744378126 scopus 로고    scopus 로고
    • The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology
    • Fujii R, Okabe S, Urushido T, Inoue K, Yoshimura A, et al. (2005) The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology. Curr Biol 15: 587-593.
    • (2005) Curr Biol , vol.15 , pp. 587-593
    • Fujii, R.1    Okabe, S.2    Urushido, T.3    Inoue, K.4    Yoshimura, A.5
  • 20
    • 0017337454 scopus 로고    scopus 로고
    • S-adenosylmethionine: protein-arginine methyltransferase. Purification and mechanism of the enzyme
    • Lee HW, Kim S, Paik WK, (1997) S-adenosylmethionine: protein-arginine methyltransferase. Purification and mechanism of the enzyme. Biochemistry 16: 78-85.
    • (1997) Biochemistry , vol.16 , pp. 78-85
    • Lee, H.W.1    Kim, S.2    Paik, W.K.3
  • 21
    • 70350084477 scopus 로고    scopus 로고
    • The physiological and pathophysiological role of PRMT1-mediated protein arginine methylation Pharmacological Research
    • Nicholson TB, Chen T, Richard S, (2009) The physiological and pathophysiological role of PRMT1-mediated protein arginine methylation Pharmacological Research. 60: 466-474.
    • (2009) , vol.60 , pp. 466-474
    • Nicholson, T.B.1    Chen, T.2    Richard, S.3
  • 22
    • 10344243548 scopus 로고    scopus 로고
    • Arginine methylation of scaffold attachment factor A by heterogeneous nuclear ribonucleoprotein particle-associated PRMT1
    • Herrmann F, Bossert M, Schwander A, Akgun E, Fackelmayer FO, (2004) Arginine methylation of scaffold attachment factor A by heterogeneous nuclear ribonucleoprotein particle-associated PRMT1. J Biol Chem 279: 48774-48779.
    • (2004) J Biol Chem , vol.279 , pp. 48774-48779
    • Herrmann, F.1    Bossert, M.2    Schwander, A.3    Akgun, E.4    Fackelmayer, F.O.5
  • 23
    • 38449123517 scopus 로고    scopus 로고
    • Mammalian stress granules and processing bodies
    • Kedersha N, Anderson P, (2007) Mammalian stress granules and processing bodies. Methods Enzymol 431: 61-81.
    • (2007) Methods Enzymol , vol.431 , pp. 61-81
    • Kedersha, N.1    Anderson, P.2
  • 24
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: the ins and outs of translation
    • Buchan JR, Parker R, (2009) Eukaryotic stress granules: the ins and outs of translation. Mol Cell 36: 932-941.
    • (2009) Mol Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 25
    • 33847069660 scopus 로고    scopus 로고
    • Stress granules: RNP-containing cytoplasmic bodies arising in stress: Structure and mechanism of organization Mol Biol (Mosk). 40(6): 937-44
    • Ivanov PA, Nadezhdina ES, (2006) Stress granules: RNP-containing cytoplasmic bodies arising in stress: Structure and mechanism of organization Mol Biol (Mosk). 40(6): 937-44. Molecular Biology 40: 937-44.
    • (2006) Molecular Biology , vol.40 , pp. 937-944
    • Ivanov, P.A.1    Nadezhdina, E.S.2
  • 26
    • 79952268025 scopus 로고    scopus 로고
    • 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 3rd, et al (2011) TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor. Mol Cell Biol 31: 1098-1108.
    • (2011) Mol Cell Biol , vol.31 , pp. 1098-1108
    • Dewey, C.M.1    Cenik, B.2    Sephton, C.F.3    Dries, D.R.4    Mayer 3rd, P.5
  • 27
    • 78149461229 scopus 로고    scopus 로고
    • 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, Vanderweyde T, Citro A, et al. (2010) Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue. PLoS One 5: e13250.
    • (2010) PLoS One , vol.5
    • Liu-Yesucevitz, L.1    Bilgutay, A.2    Zhang, Y.J.3    Vanderweyde, T.4    Citro, A.5
  • 28
    • 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 , pp. 27-40
    • Gal, J.1    Zhang, J.2    Kwinter, D.M.3    Zhai, J.4    Jia, H.5
  • 29
    • 77957867303 scopus 로고    scopus 로고
    • Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules
    • Bosco DA, Lemay N, Ko HK, Zhou H, Burke C, et al. (2010) Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules. Hum Mol Genet 19: 4160-4175.
    • (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
  • 30
    • 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
  • 32
    • 84856011109 scopus 로고    scopus 로고
    • Over-expression of map kinase phosphatase-1 (MKP-1) suppresses neuronal death through regulating JNK signaling in hypoxia/re-oxygenation
    • Koga S, Kojima S, Kishimoto T, Kuwabara S, Yamaguchi A, (2012) Over-expression of map kinase phosphatase-1 (MKP-1) suppresses neuronal death through regulating JNK signaling in hypoxia/re-oxygenation. Brain Res 1436: 137-146.
    • (2012) Brain Res , vol.1436 , pp. 137-146
    • Koga, S.1    Kojima, S.2    Kishimoto, T.3    Kuwabara, S.4    Yamaguchi, A.5
  • 33
    • 63349098780 scopus 로고    scopus 로고
    • A feedback regulatory loop between methyltransferase PRMT1 and orphan receptor TR3
    • Lei NZ, Zhang XY, Chen HZ, Wang Y, Zhan YY, et al. (2009) A feedback regulatory loop between methyltransferase PRMT1 and orphan receptor TR3. Nucleic Acids Res 37: 832-848.
    • (2009) Nucleic Acids Res , vol.37 , pp. 832-848
    • Lei, N.Z.1    Zhang, X.Y.2    Chen, H.Z.3    Wang, Y.4    Zhan, Y.Y.5
  • 34
    • 34250305530 scopus 로고    scopus 로고
    • LIM kinase and slingshot are critical for neurite extension
    • Endo M, Ohashi K, Mizuno K, (2007) LIM kinase and slingshot are critical for neurite extension. J Biol Chem 282: 13692-13702.
    • (2007) J Biol Chem , vol.282 , pp. 13692-13702
    • Endo, M.1    Ohashi, K.2    Mizuno, K.3
  • 35
    • 77949505299 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble proteins in ALS indicates a causal link between nitrative stress and aggregation in pathogenesis
    • Basso M, Samengo G, Nardo G, Massignan T, D'Alessandro G, et al. (2009) Characterization of detergent-insoluble proteins in ALS indicates a causal link between nitrative stress and aggregation in pathogenesis. PLoS One 4: e8130.
    • (2009) PLoS One , vol.4
    • Basso, M.1    Samengo, G.2    Nardo, G.3    Massignan, T.4    D'Alessandro, G.5
  • 36
    • 36348969300 scopus 로고    scopus 로고
    • Alternative splicing yields protein arginine methyltransferase 1 isoforms with distinct activity, substrate specificity, and subcellular localization
    • Goulet I, Gauvin G, Boisvenue S, Cote J, (2007) Alternative splicing yields protein arginine methyltransferase 1 isoforms with distinct activity, substrate specificity, and subcellular localization. J Biol Chem 282: 33009-33021.
    • (2007) J Biol Chem , vol.282 , pp. 33009-33021
    • Goulet, I.1    Gauvin, G.2    Boisvenue, S.3    Cote, J.4
  • 37
    • 79151471350 scopus 로고    scopus 로고
    • TLS and PRMT1 synergistically coactivate transcription at the survivin promoter through TLS arginine methylation
    • Du K, Arai S, Kawamura T, Matsushita A, Kurokawa R, (2011) TLS and PRMT1 synergistically coactivate transcription at the survivin promoter through TLS arginine methylation. Biochem Biophys Res Commun 404: 991-996.
    • (2011) Biochem Biophys Res Commun , vol.404 , pp. 991-996
    • Du, K.1    Arai, S.2    Kawamura, T.3    Matsushita, A.4    Kurokawa, R.5
  • 38
    • 0037135695 scopus 로고    scopus 로고
    • Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy
    • Wada K, Inoue K, Hagiwara M, (2002) Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy. Biochim Biophys Acta 1591: 1-10.
    • (2002) Biochim Biophys Acta , vol.1591 , pp. 1-10
    • Wada, K.1    Inoue, K.2    Hagiwara, M.3
  • 40
    • 0034306113 scopus 로고    scopus 로고
    • The molecular interaction of 4′-iodo-4′-deoxydoxorubicin with Leu-55Pro transthyretin "amyloid-like" oligomer leading to disaggregation
    • Sebastiano MP, Merlini G, Saraiva MJ, Damas AM (2000) The molecular interaction of 4′-iodo-4′-deoxydoxorubicin with Leu-55Pro transthyretin "amyloid-like" oligomer leading to disaggregation. Biochem. J. 351, 273-279.
    • (2000) Biochem. J. , vol.351 , pp. 273-279
    • Sebastiano, M.P.1    Merlini, G.2    Saraiva, M.J.3    Damas, A.M.4
  • 41
    • 83455162720 scopus 로고    scopus 로고
    • 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, et al. (2012) Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations. Hum Mol Genet 21: 136-149.
    • (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
  • 42
    • 51349117212 scopus 로고    scopus 로고
    • Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state
    • Pahlich S, Zakaryan RP, Gehring H, (2008) Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state. Proteins 72: 1125-1137.
    • (2008) Proteins , vol.72 , pp. 1125-1137
    • Pahlich, S.1    Zakaryan, R.P.2    Gehring, H.3
  • 43
    • 9144219612 scopus 로고    scopus 로고
    • Effects of adenosine dialdehyde treatment on in vitro and in vivo stable protein methylation in HeLa cells
    • Chen DH, Wu KT, Hung CJ, Hsieh M, Li C, (2004) Effects of adenosine dialdehyde treatment on in vitro and in vivo stable protein methylation in HeLa cells. J Biochem 136: 371-376.
    • (2004) J Biochem , vol.136 , pp. 371-376
    • Chen, D.H.1    Wu, K.T.2    Hung, C.J.3    Hsieh, M.4    Li, C.5
  • 44
    • 84869237956 scopus 로고    scopus 로고
    • Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS
    • 2012 Sep 11. doi: 10.1038/emboj.2012.261. [Epub ahead of print]
    • Dormann D, Madl T, Valori CF, Bentmann E, Tahirovic S, et al. (2012) Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS. EMBO J. 2012 Sep 11. doi: 10.1038/emboj.2012.261. [Epub ahead of print].
    • (2012) EMBO J
    • Dormann, D.1    Madl, T.2    Valori, C.F.3    Bentmann, E.4    Tahirovic, S.5
  • 45
    • 68949200962 scopus 로고    scopus 로고
    • Proteomic analysis of methylarginine-containing proteins in HeLa cells by two-dimensional gel electrophoresis and immunoblotting with a methylarginine-specific antibody
    • Hung CJ, Lee YJ, Chen DH, Li C, (2009) Proteomic analysis of methylarginine-containing proteins in HeLa cells by two-dimensional gel electrophoresis and immunoblotting with a methylarginine-specific antibody. Protein J 28: 139-147.
    • (2009) Protein J , vol.28 , pp. 139-147
    • Hung, C.J.1    Lee, Y.J.2    Chen, D.H.3    Li, C.4
  • 46
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong SE, Mittler G, Mann M, (2004) Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nat Methods 1: 119-126.
    • (2004) Nat Methods , vol.1 , pp. 119-126
    • Ong, S.E.1    Mittler, G.2    Mann, M.3
  • 47
    • 0030979290 scopus 로고    scopus 로고
    • Identification of N(G)-methylarginine residues in human heterogeneous RNP protein A1: Phe/Gly-Gly-Gly-Arg-Gly-Gly-Gly/Phe is a preferred recognition motif
    • Kim S, Merrill BM, Rajpurohit R, Kumar A, Stone KL, et al. (1997) Identification of N(G)-methylarginine residues in human heterogeneous RNP protein A1: Phe/Gly-Gly-Gly-Arg-Gly-Gly-Gly/Phe is a preferred recognition motif. Biochemistry 36: 5185-5192.
    • (1997) Biochemistry , vol.36 , pp. 5185-5192
    • Kim, S.1    Merrill, B.M.2    Rajpurohit, R.3    Kumar, A.4    Stone, K.L.5
  • 49
    • 0037244282 scopus 로고    scopus 로고
    • Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1
    • Cote J, Boisvert FM, Boulanger MC, Bedford MT, Richard S, (2003) Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1. Mol. Biol. Cell 14: 274-287.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 274-287
    • Cote, J.1    Boisvert, F.M.2    Boulanger, M.C.3    Bedford, M.T.4    Richard, S.5
  • 50
    • 33744516148 scopus 로고    scopus 로고
    • Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP
    • Dolzhanskaya N, Merz G, Aletta JM, Denman RB, (2006) Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP. J Cell Sci 119: 1933-1946.
    • (2006) J Cell Sci , vol.119 , pp. 1933-1946
    • Dolzhanskaya, N.1    Merz, G.2    Aletta, J.M.3    Denman, R.B.4
  • 51
    • 77952539696 scopus 로고    scopus 로고
    • Arginines of the RGG box regulate FMRP association with polyribosomes and mRNA
    • Blackwell E, Zhang X, Ceman S, (2010) Arginines of the RGG box regulate FMRP association with polyribosomes and mRNA. Hum Mol Genet 19: 1314-1323.
    • (2010) Hum Mol Genet , vol.19 , pp. 1314-1323
    • Blackwell, E.1    Zhang, X.2    Ceman, S.3
  • 52
    • 10044237933 scopus 로고    scopus 로고
    • Nuclear export of hnRNP Hrp1p and nuclear export of hnRNP Npl3p are linked and influenced by the methylation state of Npl3p
    • Xu C, Henry MF, (2004) Nuclear export of hnRNP Hrp1p and nuclear export of hnRNP Npl3p are linked and influenced by the methylation state of Npl3p. Mol Cell Biol 24: 10742-10756.
    • (2004) Mol Cell Biol , vol.24 , pp. 10742-10756
    • Xu, C.1    Henry, M.F.2
  • 54
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • Shorter J, Lindquist S, (2005) Prions as adaptive conduits of memory and inheritance. Nat Rev Genet 6: 435-450.
    • (2005) Nat Rev Genet , vol.6 , pp. 435-450
    • Shorter, J.1    Lindquist, S.2
  • 55
    • 77951183978 scopus 로고    scopus 로고
    • Prion-like disorders: blurring the divide between transmissibility and infectivity
    • Cushman M, Johnson BS, King OD, Gitler AD, Shorter J, (2010) Prion-like disorders: blurring the divide between transmissibility and infectivity. J Cell Sci 123: 1191-1201.
    • (2010) J Cell Sci , vol.123 , pp. 1191-1201
    • Cushman, M.1    Johnson, B.S.2    King, O.D.3    Gitler, A.D.4    Shorter, J.5
  • 56
    • 78651394950 scopus 로고    scopus 로고
    • Implications of the prion-related Q/N domains in TDP-43 and FUS
    • Udan M, Baloh RH, (2011) Implications of the prion-related Q/N domains in TDP-43 and FUS. Prion 5: 1-5.
    • (2011) Prion , vol.5 , pp. 1-5
    • Udan, M.1    Baloh, R.H.2
  • 57
    • 9444279617 scopus 로고    scopus 로고
    • Stress granule assembly is mediated by prion-like aggregation of TIA-1
    • Gilks N, Kedersha N, Ayodele M, Shen L, Stoecklin G, et al. (2004) Stress granule assembly is mediated by prion-like aggregation of TIA-1. Mol Biol Cell 15: 5383-5398.
    • (2004) Mol Biol Cell , vol.15 , pp. 5383-5398
    • Gilks, N.1    Kedersha, N.2    Ayodele, M.3    Shen, L.4    Stoecklin, G.5
  • 58
    • 84857750899 scopus 로고    scopus 로고
    • The role of posttranslational modifications in the assembly of stress granules
    • Ohn T, Anderson P, (2010) The role of posttranslational modifications in the assembly of stress granules. Wiley Interdiscip Rev RNA 1: 486-493.
    • (2010) Wiley Interdiscip Rev RNA , vol.1 , pp. 486-493
    • Ohn, T.1    Anderson, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.