메뉴 건너뛰기




Volumn 343, Issue 1, 2005, Pages 79-92

Inhibition of in vitro RNA binding and replicase activity by phosphorylation of the p33 replication protein of Cucumber necrosis tombusvirus

Author keywords

In vitro replication; Phosphorylation; RNA binding; RNA synthesis; Tombusvirus

Indexed keywords

ALANINE; ARGININE; ASPARTIC ACID; PROLINE; PROTEIN P33; RNA DIRECTED RNA POLYMERASE; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS RNA;

EID: 27644467561     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2005.08.005     Document Type: Article
Times cited : (43)

References (49)
  • 1
    • 0026638841 scopus 로고
    • Phosphorylation by cellular casein kinase II is essential for transcriptional activity of vesicular stomatitis virus phosphoprotein P
    • S. Barik, and A.K. Banerjee Phosphorylation by cellular casein kinase II is essential for transcriptional activity of vesicular stomatitis virus phosphoprotein P Proc. Natl. Acad. Sci. U.S.A. 89 14 1992 6570 6574
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , Issue.14 , pp. 6570-6574
    • Barik, S.1    Banerjee, A.K.2
  • 2
    • 0030928832 scopus 로고    scopus 로고
    • The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR
    • S.R. Brand, R. Kobayashi, and M.B. Mathews The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR J. Biol. Chem. 272 13 1997 8388 8395
    • (1997) J. Biol. Chem. , vol.272 , Issue.13 , pp. 8388-8395
    • Brand, S.R.1    Kobayashi, R.2    Mathews, M.B.3
  • 3
    • 0034468075 scopus 로고    scopus 로고
    • The ORF1 products of tombusviruses play a crucial role in lethal necrosis of virus-infected plants
    • J. Burgyan, C. Hornyik, G. Szittya, D. Silhavy, and G. Bisztray The ORF1 products of tombusviruses play a crucial role in lethal necrosis of virus-infected plants J. Virol. 74 23 2000 10873 10881
    • (2000) J. Virol. , vol.74 , Issue.23 , pp. 10873-10881
    • Burgyan, J.1    Hornyik, C.2    Szittya, G.3    Silhavy, D.4    Bisztray, G.5
  • 4
    • 4444377616 scopus 로고    scopus 로고
    • Phosphorylation of hepatitis C virus nonstructural protein 5A modulates its protein interactions and viral RNA replication
    • M.J. Evans, C.M. Rice, and S.P. Goff Phosphorylation of hepatitis C virus nonstructural protein 5A modulates its protein interactions and viral RNA replication Proc. Natl. Acad. Sci. U.S.A. 101 35 2004 13038 13043
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.35 , pp. 13038-13043
    • Evans, M.J.1    Rice, C.M.2    Goff, S.P.3
  • 5
    • 0030836217 scopus 로고    scopus 로고
    • Site-specific phosphorylation of the human immunodeficiency virus type-1 Rev protein accelerates formation of an efficient RNA-binding conformation
    • D.E. Fouts, H.L. True, K.A. Cengel, and D.W. Celander Site-specific phosphorylation of the human immunodeficiency virus type-1 Rev protein accelerates formation of an efficient RNA-binding conformation Biochemistry 36 43 1997 13256 13262
    • (1997) Biochemistry , vol.36 , Issue.43 , pp. 13256-13262
    • Fouts, D.E.1    True, H.L.2    Cengel, K.A.3    Celander, D.W.4
  • 6
    • 0346034578 scopus 로고    scopus 로고
    • Structural and dynamic changes in human annexin VI induced by a phosphorylation-mimicking mutation, T356D
    • C. Freye-Minks, R.H. Kretsinger, and C.E. Creutz Structural and dynamic changes in human annexin VI induced by a phosphorylation-mimicking mutation, T356D Biochemistry 42 3 2003 620 630
    • (2003) Biochemistry , vol.42 , Issue.3 , pp. 620-630
    • Freye-Minks, C.1    Kretsinger, R.H.2    Creutz, C.E.3
  • 7
    • 0028820127 scopus 로고
    • Cooperative binding of multimeric phosphoprotein (P) of vesicular stomatitis virus to polymerase (L) and template: Pathways of assembly
    • Y. Gao, and J. Lenard Cooperative binding of multimeric phosphoprotein (P) of vesicular stomatitis virus to polymerase (L) and template: pathways of assembly J. Virol. 69 12 1995 7718 7723
    • (1995) J. Virol. , vol.69 , Issue.12 , pp. 7718-7723
    • Gao, Y.1    Lenard, J.2
  • 8
    • 0030446687 scopus 로고    scopus 로고
    • The transcriptional form of the phosphoprotein of vesicular stomatitis virus is a trimer: Structure and stability
    • Y. Gao, N.J. Greenfield, D.Z. Cleverley, and J. Lenard The transcriptional form of the phosphoprotein of vesicular stomatitis virus is a trimer: structure and stability Biochemistry 35 46 1996 14569 14573
    • (1996) Biochemistry , vol.35 , Issue.46 , pp. 14569-14573
    • Gao, Y.1    Greenfield, N.J.2    Cleverley, D.Z.3    Lenard, J.4
  • 9
    • 0031716920 scopus 로고    scopus 로고
    • RNA binding and modulation of PKR activity
    • S. Gunnery, and M.B. Mathews RNA binding and modulation of PKR activity Methods 15 3 1998 189 198
    • (1998) Methods , vol.15 , Issue.3 , pp. 189-198
    • Gunnery, S.1    Mathews, M.B.2
  • 10
    • 0034662167 scopus 로고    scopus 로고
    • Evidence for phosphorylation and ubiquitinylation of the turnip yellow mosaic virus RNA-dependent RNA polymerase domain expressed in a baculovirus-insect cell system
    • F. Hericourt, S. Blanc, V. Redeker, and I. Jupin Evidence for phosphorylation and ubiquitinylation of the turnip yellow mosaic virus RNA-dependent RNA polymerase domain expressed in a baculovirus-insect cell system Biochem. J. 349 Pt. 2 2000 417 425
    • (2000) Biochem. J. , vol.349 , Issue.PART 2 , pp. 417-425
    • Hericourt, F.1    Blanc, S.2    Redeker, V.3    Jupin, I.4
  • 11
    • 0026636883 scopus 로고
    • The regulation of transcription by phosphorylation
    • T. Hunter, and M. Karin The regulation of transcription by phosphorylation Cell 70 3 1992 375 387
    • (1992) Cell , vol.70 , Issue.3 , pp. 375-387
    • Hunter, T.1    Karin, M.2
  • 12
    • 0035957981 scopus 로고    scopus 로고
    • Phosphorylation down-regulates the RNA binding function of the coat protein of potato virus a
    • K.I. Ivanov, P. Puustinen, A. Merits, M. Saarma, and K. Makinen Phosphorylation down-regulates the RNA binding function of the coat protein of potato virus A J. Biol. Chem. 276 17 2001 13530 13540
    • (2001) J. Biol. Chem. , vol.276 , Issue.17 , pp. 13530-13540
    • Ivanov, K.I.1    Puustinen, P.2    Merits, A.3    Saarma, M.4    Makinen, K.5
  • 14
    • 0035258591 scopus 로고    scopus 로고
    • Enhancement of the antiproliferative function of p53 by phosphorylation at serine 20: An inference from site-directed mutagenesis studies
    • J.R. Jabbur, P. Huang, and W. Zhang Enhancement of the antiproliferative function of p53 by phosphorylation at serine 20: an inference from site-directed mutagenesis studies Int. J. Mol. Med. 7 2 2001 163 168
    • (2001) Int. J. Mol. Med. , vol.7 , Issue.2 , pp. 163-168
    • Jabbur, J.R.1    Huang, P.2    Zhang, W.3
  • 15
    • 11144237279 scopus 로고    scopus 로고
    • Hedgehog signalling activity of Smoothened requires phosphorylation by protein kinase a and casein kinase I
    • J. Jia, C. Tong, B. Wang, L. Luo, and J. Jiang Hedgehog signalling activity of Smoothened requires phosphorylation by protein kinase A and casein kinase I Nature 432 7020 2004 1045 1050
    • (2004) Nature , vol.432 , Issue.7020 , pp. 1045-1050
    • Jia, J.1    Tong, C.2    Wang, B.3    Luo, L.4    Jiang, J.5
  • 16
    • 0028073177 scopus 로고
    • Effect of core protein phosphorylation by protein kinase C on encapsidation of RNA within core particles of hepatitis B virus
    • M. Kann, and W.H. Gerlich Effect of core protein phosphorylation by protein kinase C on encapsidation of RNA within core particles of hepatitis B virus J. Virol. 68 12 1994 7993 8000
    • (1994) J. Virol. , vol.68 , Issue.12 , pp. 7993-8000
    • Kann, M.1    Gerlich, W.H.2
  • 17
    • 0033526096 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex
    • M. Kann, B. Sodeik, A. Vlachou, W.H. Gerlich, and A. Helenius Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex J. Cell Biol. 145 1 1999 45 55
    • (1999) J. Cell Biol. , vol.145 , Issue.1 , pp. 45-55
    • Kann, M.1    Sodeik, B.2    Vlachou, A.3    Gerlich, W.H.4    Helenius, A.5
  • 18
    • 0033567389 scopus 로고    scopus 로고
    • Phosphorylation of tobacco mosaic virus movement protein abolishes its translation repressing ability
    • O.V. Karpova, N.P. Rodionova, K.I. Ivanov, S.V. Kozlovsky, Y.L. Dorokhov, and J.G. Atabekov Phosphorylation of tobacco mosaic virus movement protein abolishes its translation repressing ability Virology 261 1 1999 20 24
    • (1999) Virology , vol.261 , Issue.1 , pp. 20-24
    • Karpova, O.V.1    Rodionova, N.P.2    Ivanov, K.I.3    Kozlovsky, S.V.4    Dorokhov, Y.L.5    Atabekov, J.G.6
  • 19
    • 0036566460 scopus 로고    scopus 로고
    • Phosphorylation of cucumber mosaic virus RNA polymerase 2a protein inhibits formation of replicase complex
    • S.H. Kim, P. Palukaitis, and Y.I. Park Phosphorylation of cucumber mosaic virus RNA polymerase 2a protein inhibits formation of replicase complex EMBO J. 21 9 2002 2292 2300
    • (2002) EMBO J. , vol.21 , Issue.9 , pp. 2292-2300
    • Kim, S.H.1    Palukaitis, P.2    Park, Y.I.3
  • 21
    • 0035006310 scopus 로고    scopus 로고
    • Phosphorylation of viral movement proteins-Regulation of cell-to-cell trafficking
    • J.Y. Lee, and W.J. Lucas Phosphorylation of viral movement proteins-Regulation of cell-to-cell trafficking Trends Microbiol. 9 1 2001 5 8 (discussion 8)
    • (2001) Trends Microbiol. , vol.9 , Issue.1 , pp. 5-8
    • Lee, J.Y.1    Lucas, W.J.2
  • 22
    • 0032870871 scopus 로고    scopus 로고
    • Host cell protein kinases in nonsegmented negative-strand virus (mononegavirales) infection
    • J. Lenard Host cell protein kinases in nonsegmented negative-strand virus (mononegavirales) infection Pharmacol. Ther. 83 1 1999 39 48
    • (1999) Pharmacol. Ther. , vol.83 , Issue.1 , pp. 39-48
    • Lenard, J.1
  • 23
    • 16244386884 scopus 로고    scopus 로고
    • The p92 polymerase coding region contains an internal RNA element required at an early step in tombusvirus genome replication
    • S. Monkewich, H.X. Lin, M.R. Fabian, W. Xu, H. Na, D. Ray, O.A. Chernysheva, P.D. Nagy, and K.A. White The p92 polymerase coding region contains an internal RNA element required at an early step in tombusvirus genome replication J. Virol. 79 8 2005 4848 4858
    • (2005) J. Virol. , vol.79 , Issue.8 , pp. 4848-4858
    • Monkewich, S.1    Lin, H.X.2    Fabian, M.R.3    Xu, W.4    Na, H.5    Ray, D.6    Chernysheva, O.A.7    Nagy, P.D.8    White, K.A.9
  • 24
    • 0034890657 scopus 로고    scopus 로고
    • Phosphorylation of two serine residues regulates human T-cell leukemia virus type 2 Rex function
    • M. Narayan, K. Kusuhara, and P.L. Green Phosphorylation of two serine residues regulates human T-cell leukemia virus type 2 Rex function J. Virol. 75 18 2001 8440 8448
    • (2001) J. Virol. , vol.75 , Issue.18 , pp. 8440-8448
    • Narayan, M.1    Kusuhara, K.2    Green, P.L.3
  • 25
    • 16544386872 scopus 로고    scopus 로고
    • Expression of the Cymbidium ringspot virus 33-kilodalton protein in Saccharomyces cerevisiae and molecular dissection of the peroxisomal targeting signal
    • B. Navarro, L. Rubino, and M. Russo Expression of the Cymbidium ringspot virus 33-kilodalton protein in Saccharomyces cerevisiae and molecular dissection of the peroxisomal targeting signal J. Virol. 78 9 2004 4744 4752
    • (2004) J. Virol. , vol.78 , Issue.9 , pp. 4744-4752
    • Navarro, B.1    Rubino, L.2    Russo, M.3
  • 26
    • 0037213878 scopus 로고    scopus 로고
    • The RNA replication enhancer element of tombusviruses contains two interchangeable hairpins that are functional during plus-strand synthesis
    • T. Panavas, and P.D. Nagy The RNA replication enhancer element of tombusviruses contains two interchangeable hairpins that are functional during plus-strand synthesis J. Virol. 77 1 2003 258 269
    • (2003) J. Virol. , vol.77 , Issue.1 , pp. 258-269
    • Panavas, T.1    Nagy, P.D.2
  • 27
    • 0141457199 scopus 로고    scopus 로고
    • Yeast as a model host to study replication and recombination of defective interfering RNA of Tomato bushy stunt virus
    • T. Panavas, and P.D. Nagy Yeast as a model host to study replication and recombination of defective interfering RNA of Tomato bushy stunt virus Virology 314 1 2003 315 325
    • (2003) Virology , vol.314 , Issue.1 , pp. 315-325
    • Panavas, T.1    Nagy, P.D.2
  • 28
    • 20644441780 scopus 로고    scopus 로고
    • The role of the p33:p33/p92 interaction domain in RNA replication and intracellular localization of p33 and p92 proteins of Cucumber necrosis tombusvirus
    • T. Panavas, C.M. Hawkins, Z. Panaviene, and P.D. Nagy The role of the p33:p33/p92 interaction domain in RNA replication and intracellular localization of p33 and p92 proteins of Cucumber necrosis tombusvirus Virology 338 1 2005 81 95
    • (2005) Virology , vol.338 , Issue.1 , pp. 81-95
    • Panavas, T.1    Hawkins, C.M.2    Panaviene, Z.3    Nagy, P.D.4
  • 29
    • 0347416788 scopus 로고    scopus 로고
    • Mutations in the RNA-binding domains of tombusvirus replicase proteins affect RNA recombination in vivo
    • Z. Panaviene, and P.D. Nagy Mutations in the RNA-binding domains of tombusvirus replicase proteins affect RNA recombination in vivo Virology 317 2 2003 359 372
    • (2003) Virology , vol.317 , Issue.2 , pp. 359-372
    • Panaviene, Z.1    Nagy, P.D.2
  • 30
    • 0037473344 scopus 로고    scopus 로고
    • The overlapping RNA-binding domains of p33 and p92 replicase proteins are essential for tombusvirus replication
    • Z. Panaviene, J.M. Baker, and P.D. Nagy The overlapping RNA-binding domains of p33 and p92 replicase proteins are essential for tombusvirus replication Virology 308 1 2003 191 205
    • (2003) Virology , vol.308 , Issue.1 , pp. 191-205
    • Panaviene, Z.1    Baker, J.M.2    Nagy, P.D.3
  • 31
    • 3242695073 scopus 로고    scopus 로고
    • Purification of the cucumber necrosis virus replicase from yeast cells: Role of coexpressed viral RNA in stimulation of replicase activity
    • Z. Panaviene, T. Panavas, S. Serva, and P.D. Nagy Purification of the cucumber necrosis virus replicase from yeast cells: role of coexpressed viral RNA in stimulation of replicase activity J. Virol. 78 15 2004 8254 8263
    • (2004) J. Virol. , vol.78 , Issue.15 , pp. 8254-8263
    • Panaviene, Z.1    Panavas, T.2    Serva, S.3    Nagy, P.D.4
  • 32
    • 23244453197 scopus 로고    scopus 로고
    • Role of an internal and two 3′-terminal RNA elements in assembly of tombusvirus replicase
    • Z. Panaviene, T. Panavas, and P.D. Nagy Role of an internal and two 3′-terminal RNA elements in assembly of tombusvirus replicase J. Virol. 79 16 2005 10608 10618
    • (2005) J. Virol. , vol.79 , Issue.16 , pp. 10608-10618
    • Panaviene, Z.1    Panavas, T.2    Nagy, P.D.3
  • 33
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • T. Pawson, and J.D. Scott Signaling through scaffold, anchoring, and adaptor proteins Science 278 5346 1997 2075 2080
    • (1997) Science , vol.278 , Issue.5346 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 34
    • 0142041877 scopus 로고    scopus 로고
    • A replication silencer element in a plus-strand RNA virus
    • J. Pogany, M.R. Fabian, K.A. White, and P.D. Nagy A replication silencer element in a plus-strand RNA virus EMBO J. 22 20 2003 5602 5611
    • (2003) EMBO J. , vol.22 , Issue.20 , pp. 5602-5611
    • Pogany, J.1    Fabian, M.R.2    White, K.A.3    Nagy, P.D.4
  • 35
    • 16244383861 scopus 로고    scopus 로고
    • Specific binding of tombusvirus replication protein p33 to an internal replication element in the viral RNA is essential for replication
    • J. Pogany, K.A. White, and P.D. Nagy Specific binding of tombusvirus replication protein p33 to an internal replication element in the viral RNA is essential for replication J. Virol. 79 8 2005 4859 4869
    • (2005) J. Virol. , vol.79 , Issue.8 , pp. 4859-4869
    • Pogany, J.1    White, K.A.2    Nagy, P.D.3
  • 36
    • 0036892620 scopus 로고    scopus 로고
    • Detection of the potyviral genome-linked protein VPg in virions and its phosphorylation by host kinases
    • P. Puustinen, M.L. Rajamaki, K.I. Ivanov, J.P. Valkonen, and K. Makinen Detection of the potyviral genome-linked protein VPg in virions and its phosphorylation by host kinases J. Virol. 76 24 2002 12703 12711
    • (2002) J. Virol. , vol.76 , Issue.24 , pp. 12703-12711
    • Puustinen, P.1    Rajamaki, M.L.2    Ivanov, K.I.3    Valkonen, J.P.4    Makinen, K.5
  • 37
    • 0042389654 scopus 로고    scopus 로고
    • Characterization of the RNA-binding domains in the replicase proteins of tomato bushy stunt virus
    • K.S. Rajendran, and P.D. Nagy Characterization of the RNA-binding domains in the replicase proteins of tomato bushy stunt virus J. Virol. 77 17 2003 9244 9258
    • (2003) J. Virol. , vol.77 , Issue.17 , pp. 9244-9258
    • Rajendran, K.S.1    Nagy, P.D.2
  • 38
    • 4043055863 scopus 로고    scopus 로고
    • Interaction between the replicase proteins of Tomato Bushy Stunt virus in vitro and in vivo
    • K.S. Rajendran, and P.D. Nagy Interaction between the replicase proteins of Tomato Bushy Stunt virus in vitro and in vivo Virology 326 2 2004 250 261
    • (2004) Virology , vol.326 , Issue.2 , pp. 250-261
    • Rajendran, K.S.1    Nagy, P.D.2
  • 39
    • 0036147983 scopus 로고    scopus 로고
    • Comparison of turnip crinkle virus RNA-dependent RNA polymerase preparations expressed in Escherichia coli or derived from infected plants
    • K.S. Rajendran, J. Pogany, and P.D. Nagy Comparison of turnip crinkle virus RNA-dependent RNA polymerase preparations expressed in Escherichia coli or derived from infected plants J. Virol. 76 4 2002 1707 1717
    • (2002) J. Virol. , vol.76 , Issue.4 , pp. 1707-1717
    • Rajendran, K.S.1    Pogany, J.2    Nagy, P.D.3
  • 41
    • 0036204740 scopus 로고    scopus 로고
    • A positive-strand RNA virus replication complex parallels form and function of retrovirus capsids
    • M. Schwartz, J. Chen, M. Janda, M. Sullivan, J. den Boon, and P. Ahlquist A positive-strand RNA virus replication complex parallels form and function of retrovirus capsids Mol. Cell 9 3 2002 505 514
    • (2002) Mol. Cell , vol.9 , Issue.3 , pp. 505-514
    • Schwartz, M.1    Chen, J.2    Janda, M.3    Sullivan, M.4    Den Boon, J.5    Ahlquist, P.6
  • 42
    • 27644531656 scopus 로고    scopus 로고
    • Phosphorylation of the p33 replication protein of Cucumber necrosis tombusvirus adjacent to the RNA binding site affects viral RNA replication
    • (doi:10.1016/j.virol.2005.08.006)
    • N. Shapka, J. Stork, and P.D. Nagy Phosphorylation of the p33 replication protein of Cucumber necrosis tombusvirus adjacent to the RNA binding site affects viral RNA replication J. Virol. 343 2005 65 78 (doi:10.1016/j.virol. 2005.08.006 )
    • (2005) J. Virol. , vol.343 , pp. 65-78
    • Shapka, N.1    Stork, J.2    Nagy, P.D.3
  • 43
    • 17044455584 scopus 로고    scopus 로고
    • The potato leafroll virus 17 K movement protein is phosphorylated by a membrane-associated protein kinase from potato with biochemical features of protein kinase C
    • M. Sokolova, D. Prufer, E. Tacke, and W. Rohde The potato leafroll virus 17 K movement protein is phosphorylated by a membrane-associated protein kinase from potato with biochemical features of protein kinase C FEBS Lett. 400 2 1997 201 205
    • (1997) FEBS Lett. , vol.400 , Issue.2 , pp. 201-205
    • Sokolova, M.1    Prufer, D.2    Tacke, E.3    Rohde, W.4
  • 44
    • 1842478144 scopus 로고    scopus 로고
    • The hepatitis C virus NS5A protein activates a phosphoinositide 3-kinase-dependent survival signaling cascade
    • A. Street, A. Macdonald, K. Crowder, and M. Harris The hepatitis C virus NS5A protein activates a phosphoinositide 3-kinase-dependent survival signaling cascade J. Biol. Chem. 279 13 2004 12232 12241
    • (2004) J. Biol. Chem. , vol.279 , Issue.13 , pp. 12232-12241
    • Street, A.1    MacDonald, A.2    Crowder, K.3    Harris, M.4
  • 45
    • 0026727599 scopus 로고
    • Phosphorylation of specific serine residues within the acidic domain of the phosphoprotein of vesicular stomatitis virus regulates transcription in vitro
    • A.M. Takacs, S. Barik, T. Das, and A.K. Banerjee Phosphorylation of specific serine residues within the acidic domain of the phosphoprotein of vesicular stomatitis virus regulates transcription in vitro J. Virol. 66 10 1992 5842 5848
    • (1992) J. Virol. , vol.66 , Issue.10 , pp. 5842-5848
    • Takacs, A.M.1    Barik, S.2    Das, T.3    Banerjee, A.K.4
  • 46
    • 13144253137 scopus 로고    scopus 로고
    • Mimicking carboxyterminal phosphorylation differentially effects subcellular distribution and cell-to-cell movement of Tobacco mosaic virus movement protein
    • K. Trutnyeva, R. Bachmaier, and E. Waigmann Mimicking carboxyterminal phosphorylation differentially effects subcellular distribution and cell-to-cell movement of Tobacco mosaic virus movement protein Virology 332 2 2005 563 577
    • (2005) Virology , vol.332 , Issue.2 , pp. 563-577
    • Trutnyeva, K.1    Bachmaier, R.2    Waigmann, E.3
  • 47
    • 0034665471 scopus 로고    scopus 로고
    • Regulation of plasmodesmal transport by phosphorylation of tobacco mosaic virus cell-to-cell movement protein
    • E. Waigmann, M.H. Chen, R. Bachmaier, S. Ghoshroy, and V. Citovsky Regulation of plasmodesmal transport by phosphorylation of tobacco mosaic virus cell-to-cell movement protein EMBO J. 19 18 2000 4875 4884
    • (2000) EMBO J. , vol.19 , Issue.18 , pp. 4875-4884
    • Waigmann, E.1    Chen, M.H.2    Bachmaier, R.3    Ghoshroy, S.4    Citovsky, V.5
  • 48
    • 4444376173 scopus 로고    scopus 로고
    • Advances in the molecular biology of tombusviruses: Gene expression, genome replication, and recombination
    • K.A. White, and P.D. Nagy Advances in the molecular biology of tombusviruses: gene expression, genome replication, and recombination Prog. Nucleic Acid Res. Mol. Biol. 78 2004 187 226
    • (2004) Prog. Nucleic Acid Res. Mol. Biol. , vol.78 , pp. 187-226
    • White, K.A.1    Nagy, P.D.2
  • 49
    • 17544368687 scopus 로고    scopus 로고
    • The human T-cell leukemia virus Rex protein
    • I. Younis, and P.L. Green The human T-cell leukemia virus Rex protein Front. Biosci. 10 2005 431 445
    • (2005) Front. Biosci. , vol.10 , pp. 431-445
    • Younis, I.1    Green, P.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.