메뉴 건너뛰기




Volumn 7, Issue 8, 2012, Pages

Binding of the heterogeneous ribonucleoprotein K (hnRNP K) to the epstein-barr virus nuclear antigen 2 (EBNA2) enhances viral LMP2A expression

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; EPSTEIN BARR VIRUS ANTIGEN 2; GLYCINE; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K; LATENT MEMBRANE PROTEIN 2;

EID: 84864560763     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0042106     Document Type: Article
Times cited : (20)

References (82)
  • 1
    • 0035967425 scopus 로고    scopus 로고
    • Biology and disease associations of Epstein-Barr virus
    • Crawford DH, (2001) Biology and disease associations of Epstein-Barr virus. Philos Trans R Soc Lond B Biol Sci 356: 461-473.
    • (2001) Philos Trans R Soc Lond B Biol Sci , vol.356 , pp. 461-473
    • Crawford, D.H.1
  • 4
    • 0027476250 scopus 로고
    • The Epstein-Barr virus nuclear antigen 2 interacts with an EBNA2 responsive cis-element of the terminal protein 1 gene promoter
    • Zimber Strobl U, Kremmer E, Grässer F, Marschall G, Laux G, et al. (1993) The Epstein-Barr virus nuclear antigen 2 interacts with an EBNA2 responsive cis-element of the terminal protein 1 gene promoter. EMBO J 12: 167-175.
    • (1993) EMBO J , vol.12 , pp. 167-175
    • Zimber Strobl, U.1    Kremmer, E.2    Grässer, F.3    Marschall, G.4    Laux, G.5
  • 5
    • 0028855281 scopus 로고
    • Contribution of conserved amino acids in mediating the interaction between EBNA2 and CBF1/RBPJk
    • Ling PD, Hayward SD, (1995) Contribution of conserved amino acids in mediating the interaction between EBNA2 and CBF1/RBPJk. J Virol 69: 1944-1950.
    • (1995) J Virol , vol.69 , pp. 1944-1950
    • Ling, P.D.1    Hayward, S.D.2
  • 6
    • 0028133036 scopus 로고
    • Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa
    • Henkel T, Ling PD, Hayward SD, Peterson MG, (1994) Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa. Science 265: 92-95.
    • (1994) Science , vol.265 , pp. 92-95
    • Henkel, T.1    Ling, P.D.2    Hayward, S.D.3    Peterson, M.G.4
  • 7
    • 0035200379 scopus 로고    scopus 로고
    • EBNA2 and Notch signalling in Epstein-Barr virus mediated immortalization of B lymphocytes
    • Zimber Strobl U, Strobl LJ, (2001) EBNA2 and Notch signalling in Epstein-Barr virus mediated immortalization of B lymphocytes. Semin Cancer Biol 11: 423-434.
    • (2001) Semin Cancer Biol , vol.11 , pp. 423-434
    • Zimber Strobl, U.1    Strobl, L.J.2
  • 8
    • 0025834279 scopus 로고
    • Epstein-Barr virus nuclear protein 2 mutations define essential domains for transformation and transactivation
    • Cohen JI, Wang F, Kieff E, (1991) Epstein-Barr virus nuclear protein 2 mutations define essential domains for transformation and transactivation. J Virol 65: 2545-2554.
    • (1991) J Virol , vol.65 , pp. 2545-2554
    • Cohen, J.I.1    Wang, F.2    Kieff, E.3
  • 9
    • 0033516645 scopus 로고    scopus 로고
    • Characterization of DP103, a novel DEAD box protein that binds to the Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C
    • Grundhoff AT, Kremmer E, Tureci O, Glieden A, Gindorf C, et al. (1999) Characterization of DP103, a novel DEAD box protein that binds to the Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C. J Biol Chem 274: 19136-19144.
    • (1999) J Biol Chem , vol.274 , pp. 19136-19144
    • Grundhoff, A.T.1    Kremmer, E.2    Tureci, O.3    Glieden, A.4    Gindorf, C.5
  • 10
    • 0345269990 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 2 binds via its methylated Arginine- glycine repeat to the survival motor neuron protein
    • Barth S, Liss M, Voss MD, Dobner T, Fischer U, et al. (2003) Epstein-Barr virus nuclear antigen 2 binds via its methylated Arginine- glycine repeat to the survival motor neuron protein. J Virol 77: 5008-5013.
    • (2003) J Virol , vol.77 , pp. 5008-5013
    • Barth, S.1    Liss, M.2    Voss, M.D.3    Dobner, T.4    Fischer, U.5
  • 11
    • 0035158971 scopus 로고    scopus 로고
    • Functional cooperation of Epstein-Barr virus nuclear antigen 2 and the survival motor neuron protein in transactivation of the viral LMP1 promoter
    • Voss MD, Hille A, Barth S, Spurk A, Hennrich F, et al. (2001) Functional cooperation of Epstein-Barr virus nuclear antigen 2 and the survival motor neuron protein in transactivation of the viral LMP1 promoter. J Virol 75: 11781-11790.
    • (2001) J Virol , vol.75 , pp. 11781-11790
    • Voss, M.D.1    Hille, A.2    Barth, S.3    Spurk, A.4    Hennrich, F.5
  • 12
    • 0028232496 scopus 로고
    • Epstein-Barr virus nuclear protein 2A forms oligomers in vitro and in vivo through a region required for B-cell transformation
    • Tsui S, Schubach WH, (1994) Epstein-Barr virus nuclear protein 2A forms oligomers in vitro and in vivo through a region required for B-cell transformation. J Virol 68: 4287-4294.
    • (1994) J Virol , vol.68 , pp. 4287-4294
    • Tsui, S.1    Schubach, W.H.2
  • 13
    • 0033798412 scopus 로고    scopus 로고
    • Promotor-specific targeting of human SWi-SNF complex by Epstein-Barr virus nuclear protein 2
    • Wu DY, Krumm A, Schubach WH, (2000) Promotor-specific targeting of human SWi-SNF complex by Epstein-Barr virus nuclear protein 2. J Virol 74: 8893-8903.
    • (2000) J Virol , vol.74 , pp. 8893-8903
    • Wu, D.Y.1    Krumm, A.2    Schubach, W.H.3
  • 14
    • 0025816554 scopus 로고
    • Biochemical characterization of Epstein-Barr virus nuclear antigen 2A
    • Grässer FA, Haiss P, Göttel S, Mueller Lantzsch N, (1991) Biochemical characterization of Epstein-Barr virus nuclear antigen 2A. J Virol 65: 3779-3788.
    • (1991) J Virol , vol.65 , pp. 3779-3788
    • Grässer, F.A.1    Haiss, P.2    Göttel, S.3    Mueller Lantzsch, N.4
  • 15
    • 75949101284 scopus 로고    scopus 로고
    • Asymmetric Arginine dimethylation of Epstein-Barr virus nuclear antigen 2 promotes DNA targeting
    • Gross H, Barth S, Palermo RD, Mamiani A, Hennard C, et al. (2010) Asymmetric Arginine dimethylation of Epstein-Barr virus nuclear antigen 2 promotes DNA targeting. Virology 397: 299-310.
    • (2010) Virology , vol.397 , pp. 299-310
    • Gross, H.1    Barth, S.2    Palermo, R.D.3    Mamiani, A.4    Hennard, C.5
  • 16
    • 0028016452 scopus 로고
    • The EBNA-2 Arginine-glycine domain is critical but not essential for B-lymphocyte growth transformation; the rest of region 3 lacks essential interactive domains
    • Tong X, Yalamanchili R, Harada S, Kieff E, (1994) The EBNA-2 Arginine-glycine domain is critical but not essential for B-lymphocyte growth transformation; the rest of region 3 lacks essential interactive domains. J Virol 68: 6188-6197.
    • (1994) J Virol , vol.68 , pp. 6188-6197
    • Tong, X.1    Yalamanchili, R.2    Harada, S.3    Kieff, E.4
  • 17
    • 0023188723 scopus 로고
    • Influence of the Epstein-Barr virus nuclear antigen EBNA 2 on the growth phenotype of virus-transformed B cells
    • Rickinson AB, Young LS, Rowe M, (1987) Influence of the Epstein-Barr virus nuclear antigen EBNA 2 on the growth phenotype of virus-transformed B cells. J Virol 61: 1310-1317.
    • (1987) J Virol , vol.61 , pp. 1310-1317
    • Rickinson, A.B.1    Young, L.S.2    Rowe, M.3
  • 18
    • 79960943612 scopus 로고    scopus 로고
    • C-Terminal Region of EBNA-2 Determines the Superior Transforming Ability of Type 1 Epstein-Barr Virus by Enhanced Gene Regulation of LMP-1 and CXCR7
    • Cancian L, Bosshard R, Lucchesi W, Karstegl CE, Farrell PJ, (2011) C-Terminal Region of EBNA-2 Determines the Superior Transforming Ability of Type 1 Epstein-Barr Virus by Enhanced Gene Regulation of LMP-1 and CXCR7. PLoS Pathog 7: e1002164.
    • (2011) PLoS Pathog , vol.7
    • Cancian, L.1    Bosshard, R.2    Lucchesi, W.3    Karstegl, C.E.4    Farrell, P.J.5
  • 19
    • 0031603283 scopus 로고    scopus 로고
    • RNA and protein interactions modulated by protein Arginine methylation
    • Gary JD, Clarke S, (1998) RNA and protein interactions modulated by protein Arginine methylation. Prog Nucleic Acid Res Mol Biol 61: 65-131.
    • (1998) Prog Nucleic Acid Res Mol Biol , vol.61 , pp. 65-131
    • Gary, J.D.1    Clarke, S.2
  • 20
    • 0014200317 scopus 로고
    • Enzymatic methylation of protein fractions from calf thymus nuclei
    • Paik WK, Kim S, (1967) Enzymatic methylation of protein fractions from calf thymus nuclei. Biochem Biophys Res Commun 29: 14-20.
    • (1967) Biochem Biophys Res Commun , vol.29 , pp. 14-20
    • Paik, W.K.1    Kim, S.2
  • 21
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation an emerging regulator of protein function
    • Bedford MT, Richard S, (2005) Arginine methylation an emerging regulator of protein function. Mol Cell 18: 263-272.
    • (2005) Mol Cell , vol.18 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 22
    • 33344475410 scopus 로고    scopus 로고
    • FBXO11/PRMT9, a new protein Arginine methyltransferase, symmetrically dimethylates Arginine residues
    • Cook JR, Lee JH, Yang ZH, Krause CD, Herth N, et al. (2006) FBXO11/PRMT9, a new protein Arginine methyltransferase, symmetrically dimethylates Arginine residues. Biochem Biophys Res Commun 342: 472-481.
    • (2006) Biochem Biophys Res Commun , vol.342 , pp. 472-481
    • Cook, J.R.1    Lee, J.H.2    Yang, Z.H.3    Krause, C.D.4    Herth, N.5
  • 23
    • 25444463928 scopus 로고    scopus 로고
    • PRMT8, a new membrane-bound tissue-specific member of the protein Arginine methyltransferase family
    • Lee J, Sayegh J, Daniel J, Clarke S, Bedford MT, (2005) PRMT8, a new membrane-bound tissue-specific member of the protein Arginine methyltransferase family. J Biol Chem 280: 32890-32896.
    • (2005) J Biol Chem , vol.280 , pp. 32890-32896
    • Lee, J.1    Sayegh, J.2    Daniel, J.3    Clarke, S.4    Bedford, M.T.5
  • 24
    • 0024009108 scopus 로고
    • Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities
    • Swanson MS, Dreyfuss G, (1988) Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities. Mol Cell Biol 8: 2237-2241.
    • (1988) Mol Cell Biol , vol.8 , pp. 2237-2241
    • Swanson, M.S.1    Dreyfuss, G.2
  • 25
    • 2942623743 scopus 로고    scopus 로고
    • hnRNP K: one protein multiple processes
    • Bomsztyk K, Denisenko O, Ostrowski J, (2004) hnRNP K: one protein multiple processes. Bioessays 26: 629-638.
    • (2004) Bioessays , vol.26 , pp. 629-638
    • Bomsztyk, K.1    Denisenko, O.2    Ostrowski, J.3
  • 26
    • 4344575965 scopus 로고    scopus 로고
    • Control of mRNA translation and stability in haematopoietic cells: the function of hnRNPs K and E1/E2
    • Ostareck-Lederer A, Ostareck DH, (2004) Control of mRNA translation and stability in haematopoietic cells: the function of hnRNPs K and E1/E2. Biol Cell 96: 407-411.
    • (2004) Biol Cell , vol.96 , pp. 407-411
    • Ostareck-Lederer, A.1    Ostareck, D.H.2
  • 27
    • 79955632672 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K and nucleolin as transcriptional activators of the vascular endothelial growth factor promoter through interaction with secondary DNA structures
    • Uribe DJ, Guo K, Shin YJ, Sun D, (2011) Heterogeneous nuclear ribonucleoprotein K and nucleolin as transcriptional activators of the vascular endothelial growth factor promoter through interaction with secondary DNA structures. Biochemistry 50: 3796-3806.
    • (2011) Biochemistry , vol.50 , pp. 3796-3806
    • Uribe, D.J.1    Guo, K.2    Shin, Y.J.3    Sun, D.4
  • 28
    • 0031795447 scopus 로고    scopus 로고
    • Cytoplasmic regulatory functions of the KH-domain proteins hnRNPs K and E1/E2
    • Ostareck-Lederer A, Ostareck DH, Hentze MW, (1998) Cytoplasmic regulatory functions of the KH-domain proteins hnRNPs K and E1/E2. Trends Biochem Sci 23: 409-411.
    • (1998) Trends Biochem Sci , vol.23 , pp. 409-411
    • Ostareck-Lederer, A.1    Ostareck, D.H.2    Hentze, M.W.3
  • 29
    • 33744948703 scopus 로고    scopus 로고
    • Asymmetric Arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-Arginine methyltransferase 1 inhibits its interaction with c-Src
    • Ostareck-Lederer A, Ostareck DH, Rucknagel KP, Schierhorn A, Moritz B, et al. (2006) Asymmetric Arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-Arginine methyltransferase 1 inhibits its interaction with c-Src. J Biol Chem 281: 11115-11125.
    • (2006) J Biol Chem , vol.281 , pp. 11115-11125
    • Ostareck-Lederer, A.1    Ostareck, D.H.2    Rucknagel, K.P.3    Schierhorn, A.4    Moritz, B.5
  • 30
    • 49649117795 scopus 로고    scopus 로고
    • mRNA silencing in human erythroid cell maturation: heterogeneous nuclear ribonucleoprotein K controls the expression of its regulator c-Src
    • Naarmann IS, Harnisch C, Flach N, Kremmer E, Kuhn H, et al. (2008) mRNA silencing in human erythroid cell maturation: heterogeneous nuclear ribonucleoprotein K controls the expression of its regulator c-Src. J Biol Chem 283: 18461-18472.
    • (2008) J Biol Chem , vol.283 , pp. 18461-18472
    • Naarmann, I.S.1    Harnisch, C.2    Flach, N.3    Kremmer, E.4    Kuhn, H.5
  • 31
    • 78149287243 scopus 로고    scopus 로고
    • DDX6 recruits translational silenced human reticulocyte 15-lipoxygenase mRNA to RNP granules
    • Naarmann IS, Harnisch C, Muller-Newen G, Urlaub H, Ostareck-Lederer A, et al. (2010) DDX6 recruits translational silenced human reticulocyte 15-lipoxygenase mRNA to RNP granules. Rna 16: 2189-2204.
    • (2010) Rna , vol.16 , pp. 2189-2204
    • Naarmann, I.S.1    Harnisch, C.2    Muller-Newen, G.3    Urlaub, H.4    Ostareck-Lederer, A.5
  • 32
    • 79959743514 scopus 로고    scopus 로고
    • The NP9 protein encoded by the human endogenous retrovirus HERV-K(HML-2) negatively regulates gene activation of the Epstein-Barr virus nuclear antigen 2 (EBNA2)
    • Gross H, Barth S, Pfuhl T, Willnecker V, Spurk A, et al. (2011) The NP9 protein encoded by the human endogenous retrovirus HERV-K(HML-2) negatively regulates gene activation of the Epstein-Barr virus nuclear antigen 2 (EBNA2). Int J Cancer 129: 1105-1115.
    • (2011) Int J Cancer , vol.129 , pp. 1105-1115
    • Gross, H.1    Barth, S.2    Pfuhl, T.3    Willnecker, V.4    Spurk, A.5
  • 33
    • 0035846546 scopus 로고    scopus 로고
    • Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln
    • Meister G, Eggert C, Buhler D, Brahms H, Kambach C, et al. (2001) Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. Curr Biol 11: 1990-1994.
    • (2001) Curr Biol , vol.11 , pp. 1990-1994
    • Meister, G.1    Eggert, C.2    Buhler, D.3    Brahms, H.4    Kambach, C.5
  • 34
    • 0035947239 scopus 로고    scopus 로고
    • SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylArginine-containing protein targets
    • Friesen WJ, Massenet S, Paushkin S, Wyce A, Dreyfuss G, (2001) SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylArginine-containing protein targets. Mol Cell 7: 1111-1117.
    • (2001) Mol Cell , vol.7 , pp. 1111-1117
    • Friesen, W.J.1    Massenet, S.2    Paushkin, S.3    Wyce, A.4    Dreyfuss, G.5
  • 35
    • 0034714380 scopus 로고    scopus 로고
    • Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN)
    • Friesen WJ, Dreyfuss G, (2000) Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN). J Biol Chem 275: 26370-26375.
    • (2000) J Biol Chem , vol.275 , pp. 26370-26375
    • Friesen, W.J.1    Dreyfuss, G.2
  • 36
    • 33746903582 scopus 로고    scopus 로고
    • The antibody 2B4 directed against the Epstein-Barr virus (EBV)-encoded nuclear antigen 1 (EBNA1) detects MAGE-4: implications for studies on the EBV association of human cancers
    • Hennard C, Pfuhl T, Buettner M, Becker KF, Knofel T, et al. (2006) The antibody 2B4 directed against the Epstein-Barr virus (EBV)-encoded nuclear antigen 1 (EBNA1) detects MAGE-4: implications for studies on the EBV association of human cancers. J Pathol 209: 430-435.
    • (2006) J Pathol , vol.209 , pp. 430-435
    • Hennard, C.1    Pfuhl, T.2    Buettner, M.3    Becker, K.F.4    Knofel, T.5
  • 37
    • 0035735484 scopus 로고    scopus 로고
    • A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs
    • Meister G, Buhler D, Pillai R, Lottspeich F, Fischer U, (2001) A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs. Nat Cell Biol 3: 945-949.
    • (2001) Nat Cell Biol , vol.3 , pp. 945-949
    • Meister, G.1    Buhler, D.2    Pillai, R.3    Lottspeich, F.4    Fischer, U.5
  • 38
    • 0030931727 scopus 로고    scopus 로고
    • The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins
    • Liu Q, Fischer U, Wang F, Dreyfuss G, (1997) The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins. Cell 90: 1013-1021.
    • (1997) Cell , vol.90 , pp. 1013-1021
    • Liu, Q.1    Fischer, U.2    Wang, F.3    Dreyfuss, G.4
  • 39
    • 0028899270 scopus 로고
    • Rat monoclonal antibodies differentiating between the Epstein-Barr virus nuclear antigens 2A (EBNA2A) and 2B (EBNA2B)
    • Kremmer E, Kranz B, Hille A, Klein K, Eulitz M, et al. (1995) Rat monoclonal antibodies differentiating between the Epstein-Barr virus nuclear antigens 2A (EBNA2A) and 2B (EBNA2B). Virology 208: 336-342.
    • (1995) Virology , vol.208 , pp. 336-342
    • Kremmer, E.1    Kranz, B.2    Hille, A.3    Klein, K.4    Eulitz, M.5
  • 40
    • 58249097456 scopus 로고    scopus 로고
    • Physical and functional interactions between hnRNP K and PRMT family proteins
    • Chan JY, Hsieh TY, Liu ST, Chou WY, Chung MH, et al. (2009) Physical and functional interactions between hnRNP K and PRMT family proteins. FEBS Lett 583: 281-286.
    • (2009) FEBS Lett , vol.583 , pp. 281-286
    • Chan, J.Y.1    Hsieh, T.Y.2    Liu, S.T.3    Chou, W.Y.4    Chung, M.H.5
  • 41
    • 77952892684 scopus 로고    scopus 로고
    • Identification of heterogeneous nuclear ribonucleoprotein K as a transactivator for human low density lipoprotein receptor gene transcription
    • Li H, Liu J, (2010) Identification of heterogeneous nuclear ribonucleoprotein K as a transactivator for human low density lipoprotein receptor gene transcription. J Biol Chem 285: 17789-17797.
    • (2010) J Biol Chem , vol.285 , pp. 17789-17797
    • Li, H.1    Liu, J.2
  • 42
    • 0037336890 scopus 로고    scopus 로고
    • Identification of the SRC pyrimidine-binding protein (SPy) as hnRNP K: implications in the regulation of SRC1A transcription
    • Ritchie SA, Pasha MK, Batten DJ, Sharma RK, Olson DJ, et al. (2003) Identification of the SRC pyrimidine-binding protein (SPy) as hnRNP K: implications in the regulation of SRC1A transcription. Nucleic Acids Res 31: 1502-1513.
    • (2003) Nucleic Acids Res , vol.31 , pp. 1502-1513
    • Ritchie, S.A.1    Pasha, M.K.2    Batten, D.J.3    Sharma, R.K.4    Olson, D.J.5
  • 43
    • 0027182876 scopus 로고
    • Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter, in vitro
    • Takimoto M, Tomonaga T, Matunis M, Avigan M, Krutzsch H, et al. (1993) Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter, in vitro. J Biol Chem 268: 18249-18258.
    • (1993) J Biol Chem , vol.268 , pp. 18249-18258
    • Takimoto, M.1    Tomonaga, T.2    Matunis, M.3    Avigan, M.4    Krutzsch, H.5
  • 44
    • 0029998428 scopus 로고    scopus 로고
    • Multiple single-stranded cis elements are associated with activated chromatin of the human c-myc gene in vivo
    • Michelotti GA, Michelotti EF, Pullner A, Duncan RC, Eick D, et al. (1996) Multiple single-stranded cis elements are associated with activated chromatin of the human c-myc gene in vivo. Mol Cell Biol 16: 2656-2669.
    • (1996) Mol Cell Biol , vol.16 , pp. 2656-2669
    • Michelotti, G.A.1    Michelotti, E.F.2    Pullner, A.3    Duncan, R.C.4    Eick, D.5
  • 45
    • 0032504223 scopus 로고    scopus 로고
    • Hepatitis C virus core protein interacts with heterogeneous nuclear ribonucleoprotein K
    • Hsieh TY, Matsumoto M, Chou HC, Schneider R, Hwang SB, et al. (1998) Hepatitis C virus core protein interacts with heterogeneous nuclear ribonucleoprotein K. J Biol Chem. 273: 17651-17659.
    • (1998) J Biol Chem , vol.273 , pp. 17651-17659
    • Hsieh, T.Y.1    Matsumoto, M.2    Chou, H.C.3    Schneider, R.4    Hwang, S.B.5
  • 46
    • 0034618358 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoproteins as regulators of gene expression through interactions with the human thymidine kinase promoter
    • Lau JS, Baumeister P, Kim E, Roy B, Hsieh TY, et al. (2000) Heterogeneous nuclear ribonucleoproteins as regulators of gene expression through interactions with the human thymidine kinase promoter. J Cell Biochem 79: 395-406.
    • (2000) J Cell Biochem , vol.79 , pp. 395-406
    • Lau, J.S.1    Baumeister, P.2    Kim, E.3    Roy, B.4    Hsieh, T.Y.5
  • 47
    • 0028063483 scopus 로고
    • Epstein-Barr virus nuclear antigen 2 exerts its transactivating function through interaction with recombination signal binding protein RBP-J kappa, the homologue of Drosophila Suppressor of Hairless
    • Zimber Strobl U, Strobl LJ, Meitinger C, Hinrichs R, Sakai T, et al. (1994) Epstein-Barr virus nuclear antigen 2 exerts its transactivating function through interaction with recombination signal binding protein RBP-J kappa, the homologue of Drosophila Suppressor of Hairless. EMBO J 13: 4973-4982.
    • (1994) EMBO J , vol.13 , pp. 4973-4982
    • Zimber Strobl, U.1    Strobl, L.J.2    Meitinger, C.3    Hinrichs, R.4    Sakai, T.5
  • 48
    • 9244252472 scopus 로고    scopus 로고
    • Mutational analysis of the Epstein-Barr virus nuclear antigen 2 by far-Western blotting and DNA-binding studies
    • Sauder C, Götzinger N, Schubach WH, Horvath GC, Kremmer E, et al. (1996) Mutational analysis of the Epstein-Barr virus nuclear antigen 2 by far-Western blotting and DNA-binding studies. J Gen Virol 77: 991-996.
    • (1996) J Gen Virol , vol.77 , pp. 991-996
    • Sauder, C.1    Götzinger, N.2    Schubach, W.H.3    Horvath, G.C.4    Kremmer, E.5
  • 49
    • 0035200379 scopus 로고    scopus 로고
    • EBNA2 and Notch signalling in Epstein-Barr virus mediated immortalization of B lymphocytes
    • Zimber-Strobl U, Strobl LJ, (2001) EBNA2 and Notch signalling in Epstein-Barr virus mediated immortalization of B lymphocytes. Semin Cancer Biol 11: 423-434.
    • (2001) Semin Cancer Biol , vol.11 , pp. 423-434
    • Zimber-Strobl, U.1    Strobl, L.J.2
  • 50
    • 13544262935 scopus 로고    scopus 로고
    • PRMT7: A new protein Arginine methyltransferase that synthesizes symmetric dimethylArginine
    • Lee JH, Cook JR, Yang ZH, Mirochnitchenko O, Gunderson S, et al. (2004) PRMT7: A new protein Arginine methyltransferase that synthesizes symmetric dimethylArginine. J Biol Chem 19: 19.
    • (2004) J Biol Chem , vol.19 , pp. 19
    • Lee, J.H.1    Cook, J.R.2    Yang, Z.H.3    Mirochnitchenko, O.4    Gunderson, S.5
  • 51
    • 0034595798 scopus 로고    scopus 로고
    • The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylArginines, which form a major B-cell epitope for anti-Sm autoantibodies
    • Brahms H, Raymackers J, Union A, de Keyser F, Meheus L, et al. (2000) The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylArginines, which form a major B-cell epitope for anti-Sm autoantibodies. J Biol Chem 275: 17122-17129.
    • (2000) J Biol Chem , vol.275 , pp. 17122-17129
    • Brahms, H.1    Raymackers, J.2    Union, A.3    de Keyser, F.4    Meheus, L.5
  • 52
    • 0042671357 scopus 로고    scopus 로고
    • Pre-mRNA splicing: awash in a sea of proteins
    • Jurica MS, Moore MJ, (2003) Pre-mRNA splicing: awash in a sea of proteins. Mol Cell 12: 5-14.
    • (2003) Mol Cell , vol.12 , pp. 5-14
    • Jurica, M.S.1    Moore, M.J.2
  • 53
    • 79955560592 scopus 로고    scopus 로고
    • SMN deficiency reduces cellular ability to form stress granules, sensitizing cells to stress
    • Zou T, Yang X, Pan D, Huang J, Sahin M, et al. (2011) SMN deficiency reduces cellular ability to form stress granules, sensitizing cells to stress. Cell Mol Neurobiol 31: 541-550.
    • (2011) Cell Mol Neurobiol , vol.31 , pp. 541-550
    • Zou, T.1    Yang, X.2    Pan, D.3    Huang, J.4    Sahin, M.5
  • 54
    • 4143097170 scopus 로고    scopus 로고
    • Survival motor neuron protein facilitates assembly of stress granules
    • Hua Y, Zhou J, (2004) Survival motor neuron protein facilitates assembly of stress granules. FEBS Lett 572: 69-74.
    • (2004) FEBS Lett , vol.572 , pp. 69-74
    • Hua, Y.1    Zhou, J.2
  • 55
    • 0028213927 scopus 로고
    • A cellular factor is required for transcription of vaccinia viral intermediate-stage genes
    • Rosales R, Sutter G, Moss B, (1994) A cellular factor is required for transcription of vaccinia viral intermediate-stage genes. Proc Natl Acad Sci U S A 91: 3794-3798.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3794-3798
    • Rosales, R.1    Sutter, G.2    Moss, B.3
  • 56
    • 2542476990 scopus 로고    scopus 로고
    • Arginine methylation of RNA helicase a determines its subcellular localization
    • Smith WA, Schurter BT, Wong-Staal F, David M, (2004) Arginine methylation of RNA helicase a determines its subcellular localization. J Biol Chem 279: 22795-22798.
    • (2004) J Biol Chem , vol.279 , pp. 22795-22798
    • Smith, W.A.1    Schurter, B.T.2    Wong-Staal, F.3    David, M.4
  • 57
    • 49849094556 scopus 로고    scopus 로고
    • Identification of intracellular proteins associated with the EBV-encoded nuclear antigen 5 using an efficient TAP procedure and FT-ICR mass spectrometry
    • Forsman A, Ruetschi U, Ekholm J, Rymo L, (2008) Identification of intracellular proteins associated with the EBV-encoded nuclear antigen 5 using an efficient TAP procedure and FT-ICR mass spectrometry. J Proteome Res 7: 2309-2319.
    • (2008) J Proteome Res , vol.7 , pp. 2309-2319
    • Forsman, A.1    Ruetschi, U.2    Ekholm, J.3    Rymo, L.4
  • 58
    • 79953216685 scopus 로고    scopus 로고
    • Direct recruitment of ERK cascade components to inducible genes is regulated by heterogeneous nuclear ribonucleoprotein (hnRNP) K
    • Mikula M, Bomsztyk K, (2011) Direct recruitment of ERK cascade components to inducible genes is regulated by heterogeneous nuclear ribonucleoprotein (hnRNP) K. J Biol Chem. 286: 9763-9775.
    • (2011) J Biol Chem , vol.286 , pp. 9763-9775
    • Mikula, M.1    Bomsztyk, K.2
  • 59
    • 33748752047 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K modulates angiotensinogen gene expression in kidney cells
    • Wei CC, Zhang SL, Chen YW, Guo DF, Ingelfinger JR, et al. (2006) Heterogeneous nuclear ribonucleoprotein K modulates angiotensinogen gene expression in kidney cells. J Biol Chem 281: 25344-25355.
    • (2006) J Biol Chem , vol.281 , pp. 25344-25355
    • Wei, C.C.1    Zhang, S.L.2    Chen, Y.W.3    Guo, D.F.4    Ingelfinger, J.R.5
  • 60
    • 33847222136 scopus 로고    scopus 로고
    • Deciphering the cross talk between hnRNP K and c-Src: the c-Src activation domain in hnRNP K is distinct from a second interaction site
    • Adolph D, Flach N, Mueller K, Ostareck DH, Ostareck-Lederer A, (2007) Deciphering the cross talk between hnRNP K and c-Src: the c-Src activation domain in hnRNP K is distinct from a second interaction site. Mol Cell Biol 27: 1758-1770.
    • (2007) Mol Cell Biol , vol.27 , pp. 1758-1770
    • Adolph, D.1    Flach, N.2    Mueller, K.3    Ostareck, D.H.4    Ostareck-Lederer, A.5
  • 61
    • 79954475530 scopus 로고    scopus 로고
    • Identification of protein partners of the human immunodeficiency virus 1 tat/rev exon 3 leads to the discovery of a new HIV-1 splicing regulator, protein hnRNP K
    • Marchand V, Santerre M, Aigueperse C, Fouillen L, Saliou JM, et al. (2011) Identification of protein partners of the human immunodeficiency virus 1 tat/rev exon 3 leads to the discovery of a new HIV-1 splicing regulator, protein hnRNP K. RNA Biol. 8: 325-342.
    • (2011) RNA Biol , vol.8 , pp. 325-342
    • Marchand, V.1    Santerre, M.2    Aigueperse, C.3    Fouillen, L.4    Saliou, J.M.5
  • 63
    • 79952284178 scopus 로고    scopus 로고
    • Monoclonal antibody that recognizes a domain on heterogeneous nuclear ribonucleoprotein K and PTB-associated splicing factor
    • Garcia-Jurado G, Llanes D, Moreno A, Soria B, Tejedo JR, (2011) Monoclonal antibody that recognizes a domain on heterogeneous nuclear ribonucleoprotein K and PTB-associated splicing factor. Hybridoma (Larchmt) 30: 53-59.
    • (2011) Hybridoma (Larchmt) , vol.30 , pp. 53-59
    • Garcia-Jurado, G.1    Llanes, D.2    Moreno, A.3    Soria, B.4    Tejedo, J.R.5
  • 64
    • 0033887512 scopus 로고    scopus 로고
    • Regulation of the Epstein-Barr virus C promoter by AUF1 and the cyclic AMP/protein kinase A signaling pathway
    • Fuentes Panana EM, Peng R, Brewer G, Tan J, Ling PD, (2000) Regulation of the Epstein-Barr virus C promoter by AUF1 and the cyclic AMP/protein kinase A signaling pathway. J Virol 74: 8166-8175.
    • (2000) J Virol , vol.74 , pp. 8166-8175
    • Fuentes Panana, E.M.1    Peng, R.2    Brewer, G.3    Tan, J.4    Ling, P.D.5
  • 65
    • 0343593691 scopus 로고    scopus 로고
    • Nuclear pre-mRNA compartmentalization: trafficking of released transcripts to splicing factor reservoirs
    • Melcak I, Cermanova S, Jirsova K, Koberna K, Malinsky J, et al. (2000) Nuclear pre-mRNA compartmentalization: trafficking of released transcripts to splicing factor reservoirs. Mol Biol Cell 11: 497-510.
    • (2000) Mol Biol Cell , vol.11 , pp. 497-510
    • Melcak, I.1    Cermanova, S.2    Jirsova, K.3    Koberna, K.4    Malinsky, J.5
  • 66
    • 0030728698 scopus 로고    scopus 로고
    • Pre-mRNA processing and the CTD of RNA polymerase II: the tail that wags the dog?
    • Steinmetz EJ, (1997) Pre-mRNA processing and the CTD of RNA polymerase II: the tail that wags the dog? Cell 89: 491-494.
    • (1997) Cell , vol.89 , pp. 491-494
    • Steinmetz, E.J.1
  • 67
    • 0030959371 scopus 로고    scopus 로고
    • Distribution of pre-mRNA splicing factors at sites of RNA polymerase II transcription
    • Neugebauer KM, Roth MB, (1997) Distribution of pre-mRNA splicing factors at sites of RNA polymerase II transcription. Genes Dev 11: 1148-1159.
    • (1997) Genes Dev , vol.11 , pp. 1148-1159
    • Neugebauer, K.M.1    Roth, M.B.2
  • 68
    • 0032923696 scopus 로고    scopus 로고
    • The proto-oncogene c-myc is a direct target gene of Epstein-Barr virus nuclear antigen 2
    • Kaiser C, Laux G, Eick D, Jochner N, Bornkamm GW, et al. (1999) The proto-oncogene c-myc is a direct target gene of Epstein-Barr virus nuclear antigen 2. J Virol 73: 4481-4484.
    • (1999) J Virol , vol.73 , pp. 4481-4484
    • Kaiser, C.1    Laux, G.2    Eick, D.3    Jochner, N.4    Bornkamm, G.W.5
  • 69
    • 0025890062 scopus 로고
    • Early events in Epstein-Barr virus infection of human B lymphocytes
    • Alfieri C, Birkenbach M, Kieff E, (1991) Early events in Epstein-Barr virus infection of human B lymphocytes. Virology 181: 595-608.
    • (1991) Virology , vol.181 , pp. 595-608
    • Alfieri, C.1    Birkenbach, M.2    Kieff, E.3
  • 70
    • 0029671095 scopus 로고    scopus 로고
    • trans-Activation by the hnRNP K protein involves an increase in RNA synthesis from the reporter genes
    • Lee MH, Mori S, Raychaudhuri P, (1996) trans-Activation by the hnRNP K protein involves an increase in RNA synthesis from the reporter genes. J Biol Chem 271: 3420-3427.
    • (1996) J Biol Chem , vol.271 , pp. 3420-3427
    • Lee, M.H.1    Mori, S.2    Raychaudhuri, P.3
  • 71
    • 0017329178 scopus 로고
    • Establishment in continuous culture of a new type of lymphocyte from a "Burkitt like" malignant lymphoma (line D.G.-75)
    • Ben-Bassat H, Goldblum N, Mitrani S, Goldblum T, Yoffey JM, et al. (1977) Establishment in continuous culture of a new type of lymphocyte from a "Burkitt like" malignant lymphoma (line D.G.-75). Int J Cancer 19: 27-33.
    • (1977) Int J Cancer , vol.19 , pp. 27-33
    • Ben-Bassat, H.1    Goldblum, N.2    Mitrani, S.3    Goldblum, T.4    Yoffey, J.M.5
  • 72
    • 39149129648 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoded microRNA miR-BART2 down-regulates the viral DNA polymerase BALF5
    • Barth S, Pfuhl T, Mamiani A, Ehses C, Roemer K, et al. (2008) Epstein-Barr virus-encoded microRNA miR-BART2 down-regulates the viral DNA polymerase BALF5. Nucleic Acids Res 36: 666-675.
    • (2008) Nucleic Acids Res , vol.36 , pp. 666-675
    • Barth, S.1    Pfuhl, T.2    Mamiani, A.3    Ehses, C.4    Roemer, K.5
  • 73
    • 0037904754 scopus 로고    scopus 로고
    • Structure of the predominant protein Arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides
    • Zhang X, Cheng X, (2003) Structure of the predominant protein Arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides. Structure 11: 509-520.
    • (2003) Structure , vol.11 , pp. 509-520
    • Zhang, X.1    Cheng, X.2
  • 74
    • 0035951373 scopus 로고    scopus 로고
    • Lipoxygenase mRNA silencing in erythroid differentiation: The 3′UTR regulatory complex controls 60S ribosomal subunit joining
    • Ostareck DH, Ostareck-Lederer A, Shatsky IN, Hentze MW, (2001) Lipoxygenase mRNA silencing in erythroid differentiation: The 3′UTR regulatory complex controls 60S ribosomal subunit joining. Cell 104: 281-290.
    • (2001) Cell , vol.104 , pp. 281-290
    • Ostareck, D.H.1    Ostareck-Lederer, A.2    Shatsky, I.N.3    Hentze, M.W.4
  • 75
    • 79959188574 scopus 로고    scopus 로고
    • Downregulation of Sec23A Protein by miRNA-375 in Prostate Carcinoma
    • Szczyrba J, Nolte E, Wach S, Kremmer E, Stohr R, et al. (2011) Downregulation of Sec23A Protein by miRNA-375 in Prostate Carcinoma. Mol Cancer Res 9: 791-800.
    • (2011) Mol Cancer Res , vol.9 , pp. 791-800
    • Szczyrba, J.1    Nolte, E.2    Wach, S.3    Kremmer, E.4    Stohr, R.5
  • 77
    • 57049168200 scopus 로고    scopus 로고
    • A fluorescent two-hybrid assay for direct visualization of protein interactions in living cells
    • Zolghadr K, Mortusewicz O, Rothbauer U, Kleinhans R, Goehler H, et al. (2008) A fluorescent two-hybrid assay for direct visualization of protein interactions in living cells. Mol Cell Proteomics 7: 2279-2287.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2279-2287
    • Zolghadr, K.1    Mortusewicz, O.2    Rothbauer, U.3    Kleinhans, R.4    Goehler, H.5
  • 79
    • 84860201576 scopus 로고    scopus 로고
    • CENP-C facilitates the recruitment of M18BP1 to centromeric chromatin
    • Dambacher S, Deng W, Hahn M, Sadic D, Frohlich J, et al. (2012) CENP-C facilitates the recruitment of M18BP1 to centromeric chromatin. Nucleus 3.
    • (2012) Nucleus , vol.3
    • Dambacher, S.1    Deng, W.2    Hahn, M.3    Sadic, D.4    Frohlich, J.5
  • 80
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam JD, Lebovitz RM, Roeder RG, (1983) Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res 11: 1475-1489.
    • (1983) Nucleic Acids Res , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 81
    • 0028130679 scopus 로고
    • DNA-binding studies of the Epstein-Barr virus nuclear antigen 2 (EBNA-2): evidence for complex formation by latent membrane protein gene promoter-binding proteins in EBNA-2-positive cell lines
    • Sauder C, Haiss P, Grässer FA, Zimber Strobl U, Mueller Lantzsch N, (1994) DNA-binding studies of the Epstein-Barr virus nuclear antigen 2 (EBNA-2): evidence for complex formation by latent membrane protein gene promoter-binding proteins in EBNA-2-positive cell lines. J Gen Virol 75: 3067-3079.
    • (1994) J Gen Virol , vol.75 , pp. 3067-3079
    • Sauder, C.1    Haiss, P.2    Grässer, F.A.3    Zimber Strobl, U.4    Mueller Lantzsch, N.5
  • 82
    • 21644471586 scopus 로고    scopus 로고
    • A somatic knockout of CBF1 in a human B-cell line reveals that induction of CD21 and CCR7 by EBNA-2 is strictly CBF1 dependent and that downregulation of immunoglobulin M is partially CBF1 independent
    • Maier S, Santak M, Mantik A, Grabusic K, Kremmer E, et al. (2005) A somatic knockout of CBF1 in a human B-cell line reveals that induction of CD21 and CCR7 by EBNA-2 is strictly CBF1 dependent and that downregulation of immunoglobulin M is partially CBF1 independent. J Virol 79: 8784-8792.
    • (2005) J Virol , vol.79 , pp. 8784-8792
    • Maier, S.1    Santak, M.2    Mantik, A.3    Grabusic, K.4    Kremmer, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.