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Volumn 379, Issue 2, 2008, Pages 231-242

Enhancement of Transactivation Activity of Rta of Epstein-Barr Virus by RanBPM

Author keywords

Epstein Barr virus; RanBPM; Rta

Indexed keywords

AMINO ACID; BMLF1 PROTEIN; GLUTATHIONE TRANSFERASE; PROTEIN; PROTEIN DERIVATIVE; PROTEIN P21; PROTEIN UBC9; RANBPM PROTEIN; RTA PROTEIN; VIRUS PROTEIN;

EID: 43049127401     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.04.011     Document Type: Article
Times cited : (36)

References (51)
  • 1
    • 0000942113 scopus 로고    scopus 로고
    • Epstein-Barr virus and its replication
    • E. Kieff Epstein-Barr virus and its replication B.N. Fields D.M. Knipe P.M. Howley Fields' Virology 3rd edit. 1996 Lippincott-Raven Philadelphia, PA
    • (1996)
    • Kieff, E.1
  • 2
    • 0030760456 scopus 로고    scopus 로고
    • Reactivation of Epstein-Barr virus: regulation and function of the BZLF1 gene
    • S.H. Speck T. Chatila E. Flemington Reactivation of Epstein-Barr virus: regulation and function of the BZLF1 gene Trends Microbiol. 5 1997 399 405
    • (1997) Trends Microbiol. , vol.5 , pp. 399-405
    • Speck, S.H.1    Chatila, T.2    Flemington, E.3
  • 3
    • 0038678667 scopus 로고    scopus 로고
    • Synergistic autoactivation of the Epstein-Barr virus immediate-early BRLF1 promoter by Rta and Zta
    • P. Liu S.H. Speck Synergistic autoactivation of the Epstein-Barr virus immediate-early BRLF1 promoter by Rta and Zta Virology 310 2003 199 206
    • (2003) Virology , vol.310 , pp. 199-206
    • Liu, P.1    Speck, S.H.2
  • 4
    • 0025307412 scopus 로고
    • The Epstein-Barr virus (EBV) BMRF1 promoter for early antigen (EA-D) is regulated by the EBV transactivators, BRLF1 and BZLF1, in a cell-specific manner
    • E.A. Holley-Guthrie E.B. Quinlivan E.C. Mar S. Kenney The Epstein-Barr virus (EBV) BMRF1 promoter for early antigen (EA-D) is regulated by the EBV transactivators, BRLF1 and BZLF1, in a cell-specific manner J. Virol. 64 1990 3753 3759
    • (1990) J. Virol. , vol.64 , pp. 3753-3759
    • Holley-Guthrie, E.A.1    Quinlivan, E.B.2    Mar, E.C.3    Kenney, S.4
  • 5
    • 0026541305 scopus 로고
    • Characterization of an R-binding site mediating the R-induced activation of the Epstein-Barr virus BMLF1 promoter
    • H. Gruffat N. Duran M. Buisson F. Wild R. Buckland A. Sergeant Characterization of an R-binding site mediating the R-induced activation of the Epstein-Barr virus BMLF1 promoter J. Virol. 66 1992 46 52
    • (1992) J. Virol. , vol.66 , pp. 46-52
    • Gruffat, H.1    Duran, N.2    Buisson, M.3    Wild, F.4    Buckland, R.5    Sergeant, A.6
  • 6
    • 0034660443 scopus 로고    scopus 로고
    • The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators
    • R. Feederle M. Kost M. Baumann A. Janz E. Drouet W. Hammerschmidt H.J. Delecluse The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators EMBO J. 19 2000 3080 3089
    • (2000) EMBO J. , vol.19 , pp. 3080-3089
    • Feederle, R.1    Kost, M.2    Baumann, M.3    Janz, A.4    Drouet, E.5    Hammerschmidt, W.6    Delecluse, H.J.7
  • 7
    • 0025666546 scopus 로고
    • The enhancer factor R of Epstein-Barr virus (EBV) is a sequence-specific DNA binding protein
    • H. Gruffat E. Manet A. Rigolet A. Sergeant The enhancer factor R of Epstein-Barr virus (EBV) is a sequence-specific DNA binding protein Nucleic Acids Res. 18 1990 6835 6843
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6835-6843
    • Gruffat, H.1    Manet, E.2    Rigolet, A.3    Sergeant, A.4
  • 9
    • 0034979367 scopus 로고    scopus 로고
    • Epstein-Barr virus immediate-early protein BRLF1 interacts with CBP, promoting enhanced BRLF1 transactivation
    • J.J. Swenson E. Holley-Guthrie S.C. Kenney Epstein-Barr virus immediate-early protein BRLF1 interacts with CBP, promoting enhanced BRLF1 transactivation J. Virol. 75 2001 6228 6234
    • (2001) J. Virol. , vol.75 , pp. 6228-6234
    • Swenson, J.J.1    Holley-Guthrie, E.2    Kenney, S.C.3
  • 10
    • 0031714557 scopus 로고    scopus 로고
    • The Epstein-Barr virus immediate-early gene product, BRLF1, interacts with the retinoblastoma protein during the viral lytic cycle
    • V.L. Zacny J. Wilson J.S. Pagano The Epstein-Barr virus immediate-early gene product, BRLF1, interacts with the retinoblastoma protein during the viral lytic cycle J. Virol. 72 1998 8043 8051
    • (1998) J. Virol. , vol.72 , pp. 8043-8051
    • Zacny, V.L.1    Wilson, J.2    Pagano, J.S.3
  • 11
    • 0032775437 scopus 로고    scopus 로고
    • The Epstein-Barr virus protein BRLF1 activates S phase entry through E2F1 induction
    • J.J. Swenson A.E. Mauser W.K. Kaufmann S.C. Kenney The Epstein-Barr virus protein BRLF1 activates S phase entry through E2F1 induction J. Virol. 73 1999 6540 6550
    • (1999) J. Virol. , vol.73 , pp. 6540-6550
    • Swenson, J.J.1    Mauser, A.E.2    Kaufmann, W.K.3    Kenney, S.C.4
  • 12
    • 29144521749 scopus 로고    scopus 로고
    • Activation of Sp1-mediated transcription by Rta of Epstein-Barr virus via an interaction with MCAF1
    • L.K. Chang J.Y. Chung Y.R. Hong T. Ichimura M. Nakao S.T. Liu Activation of Sp1-mediated transcription by Rta of Epstein-Barr virus via an interaction with MCAF1 Nucleic Acids Res. 33 2005 6528 6539
    • (2005) Nucleic Acids Res. , vol.33 , pp. 6528-6539
    • Chang, L.K.1    Chung, J.Y.2    Hong, Y.R.3    Ichimura, T.4    Nakao, M.5    Liu, S.T.6
  • 13
    • 0033982336 scopus 로고    scopus 로고
    • Epstein-Barr virus immediate-early proteins BZLF1 and BRLF1 activate the ATF2 transcription factor by increasing the levels of phosphorylated p38 and c-Jun N-terminal kinases
    • A.L. Adamson D. Darr E. Holley-Guthrie R.A. Johnson A. Mauser J. Swenson S. Kenney Epstein-Barr virus immediate-early proteins BZLF1 and BRLF1 activate the ATF2 transcription factor by increasing the levels of phosphorylated p38 and c-Jun N-terminal kinases J. Virol. 74 2000 1224 1233
    • (2000) J. Virol. , vol.74 , pp. 1224-1233
    • Adamson, A.L.1    Darr, D.2    Holley-Guthrie, E.3    Johnson, R.A.4    Mauser, A.5    Swenson, J.6    Kenney, S.7
  • 14
    • 33847243278 scopus 로고    scopus 로고
    • Role of the TSG101 gene in Epstein-Barr virus late gene transcription
    • H.H. Chua H.H. Lee S.S. Chang C.C. Lu T.H. Yeh T.Y. Hsu Role of the TSG101 gene in Epstein-Barr virus late gene transcription J. Virol. 81 2007 2459 2471
    • (2007) J. Virol. , vol.81 , pp. 2459-2471
    • Chua, H.H.1    Lee, H.H.2    Chang, S.S.3    Lu, C.C.4    Yeh, T.H.5    Hsu, T.Y.6
  • 15
    • 0032538999 scopus 로고    scopus 로고
    • When overexpressed, a novel centrosomal protein, RanBPM, causes ectopic microtubule nucleation similar to gamma-tubulin
    • M. Nakamura H. Masuda J. Horii K. Kuma N. Yokoyama T. Ohba When overexpressed, a novel centrosomal protein, RanBPM, causes ectopic microtubule nucleation similar to gamma-tubulin J. Cell Biol. 143 1998 1041 1052
    • (1998) J. Cell Biol. , vol.143 , pp. 1041-1052
    • Nakamura, M.1    Masuda, H.2    Horii, J.3    Kuma, K.4    Yokoyama, N.5    Ohba, T.6
  • 16
    • 0035845013 scopus 로고    scopus 로고
    • Full-sized RanBPM cDNA encodes a protein possessing a long stretch of proline and glutamine within the N-terminal region, comprising a large protein complex
    • H. Nishitani E. Hirose Y. Uchimura M. Nakamura M. Umeda K. Nishii Full-sized RanBPM cDNA encodes a protein possessing a long stretch of proline and glutamine within the N-terminal region, comprising a large protein complex Gene 272 2001 25 33
    • (2001) Gene , vol.272 , pp. 25-33
    • Nishitani, H.1    Hirose, E.2    Uchimura, Y.3    Nakamura, M.4    Umeda, M.5    Nishii, K.6
  • 18
  • 19
    • 23844476742 scopus 로고    scopus 로고
    • RanBPM is an L1-interacting protein that regulates L1-mediated mitogen-activated protein kinase activation
    • L. Cheng S. Lemmon V. Lemmon RanBPM is an L1-interacting protein that regulates L1-mediated mitogen-activated protein kinase activation J. Neurochem. 94 2005 1102 1110
    • (2005) J. Neurochem. , vol.94 , pp. 1102-1110
    • Cheng, L.1    Lemmon, S.2    Lemmon, V.3
  • 20
    • 23944496040 scopus 로고    scopus 로고
    • The Ran binding protein RanBPM interacts with Axl and Sky receptor tyrosine kinases
    • S. Hafizi A. Gustafsson J. Stenhoff B. Dahlback The Ran binding protein RanBPM interacts with Axl and Sky receptor tyrosine kinases Int. J. Biochem. Cell. Biol. 37 2005 2344 2356
    • (2005) Int. J. Biochem. Cell. Biol. , vol.37 , pp. 2344-2356
    • Hafizi, S.1    Gustafsson, A.2    Stenhoff, J.3    Dahlback, B.4
  • 21
    • 2242481119 scopus 로고    scopus 로고
    • RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor
    • M.A. Rao H. Cheng A.N. Quayle H. Nishitani C.C. Nelson P.S. Rennie RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor J. Biol. Chem. 277 2002 48020 48027
    • (2002) J. Biol. Chem. , vol.277 , pp. 48020-48027
    • Rao, M.A.1    Cheng, H.2    Quayle, A.N.3    Nishitani, H.4    Nelson, C.C.5    Rennie, P.S.6
  • 22
    • 33646128733 scopus 로고    scopus 로고
    • Identification and characterization of RanBPM, a novel coactivator of thyroid hormone receptors
    • M.B. Poirier L. Laflamme M.F. Langlois Identification and characterization of RanBPM, a novel coactivator of thyroid hormone receptors J. Mol. Endocrinol. 36 2006 313 325
    • (2006) J. Mol. Endocrinol. , vol.36 , pp. 313-325
    • Poirier, M.B.1    Laflamme, L.2    Langlois, M.F.3
  • 23
    • 0037183982 scopus 로고    scopus 로고
    • Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM
    • D. Wang Z. Li E.M. Messing G. Wu Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM J. Biol. Chem. 277 2002 36216 36222
    • (2002) J. Biol. Chem. , vol.277 , pp. 36216-36222
    • Wang, D.1    Li, Z.2    Messing, E.M.3    Wu, G.4
  • 24
    • 1842477207 scopus 로고    scopus 로고
    • RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1
    • S. Denti A. Sirri A. Cheli L. Rogge G. Innamorati S. Putignano RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1 J. Biol. Chem. 279 2004 13027 13034
    • (2004) J. Biol. Chem. , vol.279 , pp. 13027-13034
    • Denti, S.1    Sirri, A.2    Cheli, A.3    Rogge, L.4    Innamorati, G.5    Putignano, S.6
  • 26
    • 13444257491 scopus 로고    scopus 로고
    • Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells
    • S. Kramer T. Ozaki K. Miyazaki C. Kato T. Hanamoto A. Nakagawara Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells Oncogene 24 2005 938 944
    • (2005) Oncogene , vol.24 , pp. 938-944
    • Kramer, S.1    Ozaki, T.2    Miyazaki, K.3    Kato, C.4    Hanamoto, T.5    Nakagawara, A.6
  • 27
    • 33646807840 scopus 로고    scopus 로고
    • Sumoylation of Rta of Epstein-Barr virus is preferentially enhanced by PIASxbeta
    • S.T. Liu W.H. Wang Y.R. Hong J.Y. Chuang P.J. Lu L.K. Chang Sumoylation of Rta of Epstein-Barr virus is preferentially enhanced by PIASxbeta Virus Res. 119 2006 163 170
    • (2006) Virus Res. , vol.119 , pp. 163-170
    • Liu, S.T.1    Wang, W.H.2    Hong, Y.R.3    Chuang, J.Y.4    Lu, P.J.5    Chang, L.K.6
  • 28
    • 0030974256 scopus 로고    scopus 로고
    • SPRY domains in ryanodine receptors (Ca(2+)-release channels)
    • C. Ponting J. Schultz P. Bork SPRY domains in ryanodine receptors (Ca(2+)-release channels) Trends Biochem. Sci. 22 1997 193 194
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 193-194
    • Ponting, C.1    Schultz, J.2    Bork, P.3
  • 29
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • H. Poukka U. Karvonen O.A. Janne J.J. Palvimo Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1) Proc. Natl Acad. Sci. USA 97 2000 14145 14150
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 30
    • 0036721526 scopus 로고    scopus 로고
    • Potentiation of glucocorticoid receptor transcriptional activity by sumoylation
    • Y. Le Drean N. Mincheneau P. Le Goff D. Michel Potentiation of glucocorticoid receptor transcriptional activity by sumoylation Endocrinology 143 2002 3482 3489
    • (2002) Endocrinology , vol.143 , pp. 3482-3489
    • Le Drean, Y.1    Mincheneau, N.2    Le Goff, P.3    Michel, D.4
  • 31
    • 0036847208 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor
    • S. Tian H. Poukka J.J. Palvimo O.A. Janne Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor Biochem. J. 367 2002 907 911
    • (2002) Biochem. J. , vol.367 , pp. 907-911
    • Tian, S.1    Poukka, H.2    Palvimo, J.J.3    Janne, O.A.4
  • 32
    • 0347790260 scopus 로고    scopus 로고
    • Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1
    • Y.H. Kim C.Y. Choi Y. Kim Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1 Proc. Natl Acad. Sci. USA 96 1999 12350 12355
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12350-12355
    • Kim, Y.H.1    Choi, C.Y.2    Kim, Y.3
  • 33
    • 0034680441 scopus 로고    scopus 로고
    • Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif
    • A. Minty X. Dumont M. Kaghad D. Caput Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif J. Biol. Chem. 275 2000 36316 36323
    • (2000) J. Biol. Chem. , vol.275 , pp. 36316-36323
    • Minty, A.1    Dumont, X.2    Kaghad, M.3    Caput, D.4
  • 34
    • 29144473320 scopus 로고    scopus 로고
    • Comparison of the SUMO1 and ubiquitin conjugation pathways during the inhibition of proteasome activity with evidence of SUMO1 recycling
    • D. Bailey P. O'Hare Comparison of the SUMO1 and ubiquitin conjugation pathways during the inhibition of proteasome activity with evidence of SUMO1 recycling Biochem. J. 392 2005 271 281
    • (2005) Biochem. J. , vol.392 , pp. 271-281
    • Bailey, D.1    O'Hare, P.2
  • 35
    • 41149144090 scopus 로고    scopus 로고
    • Identification of a new site of sumoylation on Tel (ETV6) uncovers a PIAS-dependent mode of regulating Tel function
    • M.G. Roukens M. Alloul-Ramdhani A.C. Vertegaal Z. Anvarian C.I. Balog A.M. Deelder Identification of a new site of sumoylation on Tel (ETV6) uncovers a PIAS-dependent mode of regulating Tel function Mol. Cell. Biol. 28 2008 2342 2357
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 2342-2357
    • Roukens, M.G.1    Alloul-Ramdhani, M.2    Vertegaal, A.C.3    Anvarian, Z.4    Balog, C.I.5    Deelder, A.M.6
  • 36
    • 0023235414 scopus 로고
    • Epstein-Barr virus gene expression in P3HR1-superinfected Raji cells
    • M. Biggin M. Bodescot M. Perricaudet P. Farrell Epstein-Barr virus gene expression in P3HR1-superinfected Raji cells J. Virol. 61 1987 3120 3132
    • (1987) J. Virol. , vol.61 , pp. 3120-3132
    • Biggin, M.1    Bodescot, M.2    Perricaudet, M.3    Farrell, P.4
  • 37
    • 0024590981 scopus 로고
    • Synchronous and sequential activation of latently infected Epstein-Barr virus genomes
    • K. Takada Y. Ono Synchronous and sequential activation of latently infected Epstein-Barr virus genomes J. Virol. 63 1989 445 449
    • (1989) J. Virol. , vol.63 , pp. 445-449
    • Takada, K.1    Ono, Y.2
  • 38
    • 0024464255 scopus 로고
    • The Epstein-Barr virus (EBV) early protein EB2 is a posttranscriptional activator expressed under the control of EBV transcription factors EB1 and R
    • M. Buisson E. Manet M.C. Trescol-Biemont H. Gruffat B. Durand A. Sergeant The Epstein-Barr virus (EBV) early protein EB2 is a posttranscriptional activator expressed under the control of EBV transcription factors EB1 and R J. Virol. 63 1989 5276 5284
    • (1989) J. Virol. , vol.63 , pp. 5276-5284
    • Buisson, M.1    Manet, E.2    Trescol-Biemont, M.C.3    Gruffat, H.4    Durand, B.5    Sergeant, A.6
  • 39
    • 0025177308 scopus 로고
    • An enhancer within the divergent promoter of Epstein-Barr virus responds synergistically to the R and Z transactivators
    • M.A. Cox J. Leahy J.M. Hardwick An enhancer within the divergent promoter of Epstein-Barr virus responds synergistically to the R and Z transactivators J. Virol. 64 1990 313 321
    • (1990) J. Virol. , vol.64 , pp. 313-321
    • Cox, M.A.1    Leahy, J.2    Hardwick, J.M.3
  • 40
    • 0024381654 scopus 로고
    • The Epstein-Barr virus BMLF1 promoter contains an enhancer element that is responsive to the BZLF1 and BRLF1 transactivators
    • S. Kenney E. Holley-Guthrie E.C. Mar M. Smith The Epstein-Barr virus BMLF1 promoter contains an enhancer element that is responsive to the BZLF1 and BRLF1 transactivators J. Virol. 63 1989 3878 3883
    • (1989) J. Virol. , vol.63 , pp. 3878-3883
    • Kenney, S.1    Holley-Guthrie, E.2    Mar, E.C.3    Smith, M.4
  • 41
    • 0024550905 scopus 로고
    • The Epstein-Barr virus (EBV) BZLF1 immediate-early gene product differentially affects latent versus productive EBV promoters
    • S. Kenney J. Kamine E. Holley-Guthrie J.C. Lin E.C. Mar J. Pagano The Epstein-Barr virus (EBV) BZLF1 immediate-early gene product differentially affects latent versus productive EBV promoters J. Virol. 63 1989 1729 1736
    • (1989) J. Virol. , vol.63 , pp. 1729-1736
    • Kenney, S.1    Kamine, J.2    Holley-Guthrie, E.3    Lin, J.C.4    Mar, E.C.5    Pagano, J.6
  • 42
    • 0037418829 scopus 로고    scopus 로고
    • The polycomb protein Pc2 Is a SUMO E3
    • M.H. Kagey T.A. Melhuish D. Wotton The polycomb protein Pc2 Is a SUMO E3 Cell 113 2003 127 137
    • (2003) Cell , vol.113 , pp. 127-137
    • Kagey, M.H.1    Melhuish, T.A.2    Wotton, D.3
  • 43
    • 33846298844 scopus 로고    scopus 로고
    • Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation
    • Z. Ji C. Degerny N. Vintonenko J. Deheuninck B. Foveau C. Leroy Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation Oncogene 26 2007 395 406
    • (2007) Oncogene , vol.26 , pp. 395-406
    • Ji, Z.1    Degerny, C.2    Vintonenko, N.3    Deheuninck, J.4    Foveau, B.5    Leroy, C.6
  • 44
    • 0035798613 scopus 로고    scopus 로고
    • The Mdm-2 amino terminus is required for Mdm2 binding and SUMO-1 conjugation by the E2 SUMO-1 conjugating enzyme Ubc9
    • T. Buschmann D. Lerner C.G. Lee Z. Ronai The Mdm-2 amino terminus is required for Mdm2 binding and SUMO-1 conjugation by the E2 SUMO-1 conjugating enzyme Ubc9 J. Biol. Chem. 276 2001 40389 40395
    • (2001) J. Biol. Chem. , vol.276 , pp. 40389-40395
    • Buschmann, T.1    Lerner, D.2    Lee, C.G.3    Ronai, Z.4
  • 46
    • 0041353442 scopus 로고    scopus 로고
    • MDM2-ARF complex regulates p53 sumoylation
    • L. Chen J. Chen MDM2-ARF complex regulates p53 sumoylation Oncogene 22 2003 5348 5357
    • (2003) Oncogene , vol.22 , pp. 5348-5357
    • Chen, L.1    Chen, J.2
  • 47
    • 0018384722 scopus 로고
    • Induction of the Epstein-Barr virus (EBV) cycle in latently infected cells by n-butyrate
    • J. Luka B. Kallin G. Klein Induction of the Epstein-Barr virus (EBV) cycle in latently infected cells by n-butyrate Virology 94 1979 228 231
    • (1979) Virology , vol.94 , pp. 228-231
    • Luka, J.1    Kallin, B.2    Klein, G.3
  • 48
    • 0025837283 scopus 로고
    • Induction of Epstein-Barr virus lytic cycle by tumor-promoting and non-tumor-promoting phorbol esters requires active protein kinase C
    • A.H. Davies R.J. Grand F.J. Evans A.B. Rickinson Induction of Epstein-Barr virus lytic cycle by tumor-promoting and non-tumor-promoting phorbol esters requires active protein kinase C J. Virol. 65 1991 6838 6844
    • (1991) J. Virol. , vol.65 , pp. 6838-6844
    • Davies, A.H.1    Grand, R.J.2    Evans, F.J.3    Rickinson, A.B.4
  • 49
    • 13644269953 scopus 로고    scopus 로고
    • Reactivation of Epstein-Barr virus can be triggered by an Rta protein mutated at the nuclear localization signal
    • T.Y. Hsu Y. Chang P.W. Wang M.Y. Liu M.R. Chen J.Y. Chen C.H. Tsai Reactivation of Epstein-Barr virus can be triggered by an Rta protein mutated at the nuclear localization signal J. Gen. Virol. 86 2005 317 322
    • (2005) J. Gen. Virol. , vol.86 , pp. 317-322
    • Hsu, T.Y.1    Chang, Y.2    Wang, P.W.3    Liu, M.Y.4    Chen, M.R.5    Chen, J.Y.6    Tsai, C.H.7
  • 50
    • 0031902921 scopus 로고    scopus 로고
    • Role of Rta in the translation of bicistronic BZLF1 of Epstein-Barr virus
    • P.J. Chang Y.S. Chang S.T. Liu Role of Rta in the translation of bicistronic BZLF1 of Epstein-Barr virus J. Virol. 72 1998 5128 5136
    • (1998) J. Virol. , vol.72 , pp. 5128-5136
    • Chang, P.J.1    Chang, Y.S.2    Liu, S.T.3


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