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Volumn 153, Issue 1, 2010, Pages 50-57

Inhibitory effect on the tobacco mosaic virus infection by a plant RING finger protein

Author keywords

RING finger protein; RNA dependent RNA polymerase; Tobacco mosaic virus; Ubiquitin ligase; Yeast two hybrid

Indexed keywords

RING FINGER PROTEIN; RNA DIRECTED RNA POLYMERASE;

EID: 77956227853     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2010.07.005     Document Type: Article
Times cited : (11)

References (53)
  • 1
    • 0037771203 scopus 로고    scopus 로고
    • Host factors in positive-strand RNA virus genome replication
    • Ahlquist P., Noueiry A.O., Lee W.M., Kushner D.B., Dye B.T. Host factors in positive-strand RNA virus genome replication. J. Virol. 2003, 77(15):8181-8186.
    • (2003) J. Virol. , vol.77 , Issue.15 , pp. 8181-8186
    • Ahlquist, P.1    Noueiry, A.O.2    Lee, W.M.3    Kushner, D.B.4    Dye, B.T.5
  • 2
    • 70350320561 scopus 로고    scopus 로고
    • The Nedd4-type Rsp5p ubiquitin ligase inhibits tombusvirus replication by regulating degradation of the p92 replication protein and decreasing the activity of the tombusvirus replicase
    • Barajas D., Li Z., Nagy P.D. The Nedd4-type Rsp5p ubiquitin ligase inhibits tombusvirus replication by regulating degradation of the p92 replication protein and decreasing the activity of the tombusvirus replicase. J. Virol. 2009, 83(22):11751-11764.
    • (2009) J. Virol. , vol.83 , Issue.22 , pp. 11751-11764
    • Barajas, D.1    Li, Z.2    Nagy, P.D.3
  • 3
    • 35148827341 scopus 로고    scopus 로고
    • Elicitors, effectors, and R genes: the new paradigm and a lifetime supply of questions
    • Bent A.F., Mackey D. Elicitors, effectors, and R genes: the new paradigm and a lifetime supply of questions. Annu. Rev. Phytopathol. 2007, 45(1):399-436.
    • (2007) Annu. Rev. Phytopathol. , vol.45 , Issue.1 , pp. 399-436
    • Bent, A.F.1    Mackey, D.2
  • 4
    • 0030332528 scopus 로고    scopus 로고
    • Comparison of the replication of positive-stranded RNA viruses of plants and animals
    • Buck K.W. Comparison of the replication of positive-stranded RNA viruses of plants and animals. Adv. Virus Res. 1996, 47(1):159-251.
    • (1996) Adv. Virus Res. , vol.47 , Issue.1 , pp. 159-251
    • Buck, K.W.1
  • 6
    • 0042572096 scopus 로고    scopus 로고
    • Role of ubiquitination in the regulation of plant defence against pathogens
    • Devoto A., Muskett P.R., Shirasu K. Role of ubiquitination in the regulation of plant defence against pathogens. Curr. Opin. Plant Biol. 2003, 6(4):307-311.
    • (2003) Curr. Opin. Plant Biol. , vol.6 , Issue.4 , pp. 307-311
    • Devoto, A.1    Muskett, P.R.2    Shirasu, K.3
  • 7
    • 0036936858 scopus 로고    scopus 로고
    • Stability in vitro of the 69K movement protein of Turnip yellow mosaic virus is regulated by the ubiquitin-mediated proteasome pathway
    • Drugeon G., Jupin I. Stability in vitro of the 69K movement protein of Turnip yellow mosaic virus is regulated by the ubiquitin-mediated proteasome pathway. J. Gen. Virol. 2002, 83(Pt 12):3187-3197.
    • (2002) J. Gen. Virol. , vol.83 , Issue.PART 12 , pp. 3187-3197
    • Drugeon, G.1    Jupin, I.2
  • 8
    • 0024041480 scopus 로고
    • Tobacco mosaic virus particles contain ubiquitinated coat protein subunits
    • Dunigan D.D., Dietzgen R.G., Schoelz J.E., Zaitlin M. Tobacco mosaic virus particles contain ubiquitinated coat protein subunits. Virology 1988, 165(1):310-312.
    • (1988) Virology , vol.165 , Issue.1 , pp. 310-312
    • Dunigan, D.D.1    Dietzgen, R.G.2    Schoelz, J.E.3    Zaitlin, M.4
  • 9
    • 0346864044 scopus 로고
    • In vivo localization of ubiquitin in tobacco mosaic virus infected and uninfected tobacco cells
    • Gaspar J.O., Dunigan M.D., Zaitlin M. In vivo localization of ubiquitin in tobacco mosaic virus infected and uninfected tobacco cells. Mol. Plant Microbe Interact. 1990, 3(1):182-187.
    • (1990) Mol. Plant Microbe Interact. , vol.3 , Issue.1 , pp. 182-187
    • Gaspar, J.O.1    Dunigan, M.D.2    Zaitlin, M.3
  • 10
    • 33745479207 scopus 로고    scopus 로고
    • The U-box protein CMPG1 is required for efficient activation of defense mechanisms triggered by multiple resistance genes in tobacco and tomato
    • González-Lamothe R., Tsitsigiannis D.I., Ludwig A.A., Panicot M., Shirasu K., Jones J.D. The U-box protein CMPG1 is required for efficient activation of defense mechanisms triggered by multiple resistance genes in tobacco and tomato. Plant Cell 2006, 18(4):1067-1083.
    • (2006) Plant Cell , vol.18 , Issue.4 , pp. 1067-1083
    • González-Lamothe, R.1    Tsitsigiannis, D.I.2    Ludwig, A.A.3    Panicot, M.4    Shirasu, K.5    Jones, J.D.6
  • 11
    • 11144248172 scopus 로고    scopus 로고
    • Loss and gain of elicitor function of soybean mosaic virus G7 provoking Rsv1-mediated lethal systemic hypersensitive response maps to P3
    • Hajimorad M.R., Eggenberger A.L., Hill J.H. Loss and gain of elicitor function of soybean mosaic virus G7 provoking Rsv1-mediated lethal systemic hypersensitive response maps to P3. J. Virol. 2005, 79(2):1215-1222.
    • (2005) J. Virol. , vol.79 , Issue.2 , pp. 1215-1222
    • Hajimorad, M.R.1    Eggenberger, A.L.2    Hill, J.H.3
  • 12
  • 13
    • 0025289848 scopus 로고
    • Ubiquitinated conjugates are found in preparations of several plant viruses
    • Hazelwood D., Zaitlin M. Ubiquitinated conjugates are found in preparations of several plant viruses. Virology 1990, 177(1):352-356.
    • (1990) Virology , vol.177 , Issue.1 , pp. 352-356
    • Hazelwood, D.1    Zaitlin, M.2
  • 14
    • 0029549778 scopus 로고
    • Interaction of tobamovirus movement proteins with the plant cytoskeleton
    • Heinlein M., Epel B.L., Padgett H.S., Beachy R.N. Interaction of tobamovirus movement proteins with the plant cytoskeleton. Science 1995, 270(5244):1983-1985.
    • (1995) Science , vol.270 , Issue.5244 , pp. 1983-1985
    • Heinlein, M.1    Epel, B.L.2    Padgett, H.S.3    Beachy, R.N.4
  • 15
    • 0037008512 scopus 로고    scopus 로고
    • Plant development: regulation by protein degradation
    • Hellmann H., Estelle M. Plant development: regulation by protein degradation. Science 2002, 297(5582):793-797.
    • (2002) Science , vol.297 , Issue.5582 , pp. 793-797
    • Hellmann, H.1    Estelle, M.2
  • 16
    • 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
    • Héricourt F., Blanc S., Redeker V., Jupin I. 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. 2000, 349(Pt 2):417-425.
    • (2000) Biochem. J. , vol.349 , Issue.PART 2 , pp. 417-425
    • Héricourt, F.1    Blanc, S.2    Redeker, V.3    Jupin, I.4
  • 18
    • 33847066702 scopus 로고    scopus 로고
    • Plasmodesmata and intercellular transport of viral RNA
    • Hofmann C., Sambade A., Heinlein M. Plasmodesmata and intercellular transport of viral RNA. Biochem. Soc. Trans. 2007, 35(Pt 1):142-145.
    • (2007) Biochem. Soc. Trans. , vol.35 , Issue.PART 1 , pp. 142-145
    • Hofmann, C.1    Sambade, A.2    Heinlein, M.3
  • 19
    • 33845632472 scopus 로고    scopus 로고
    • The LeATL6-associated ubiquitin/proteasome system may contribute to fungal elicitor-activated defense response via the jasmonic acid-dependent signaling pathway in tomato
    • Hondo D., Hase S., Kanayama Y., Yoshikawa N., Takenaka S., Takahashi H. The LeATL6-associated ubiquitin/proteasome system may contribute to fungal elicitor-activated defense response via the jasmonic acid-dependent signaling pathway in tomato. Mol. Plant Microbe Interact. 2007, 20(1):72-81.
    • (2007) Mol. Plant Microbe Interact. , vol.20 , Issue.1 , pp. 72-81
    • Hondo, D.1    Hase, S.2    Kanayama, Y.3    Yoshikawa, N.4    Takenaka, S.5    Takahashi, H.6
  • 20
    • 35348850024 scopus 로고    scopus 로고
    • An inhibitor of viral RNA replication is encoded by a plant resistance gene
    • Ishibashi K., Masuda K., Naito S., Meshi T., Ishikawa M. An inhibitor of viral RNA replication is encoded by a plant resistance gene. Proc. Natl. Acad. Sci. U.S.A. 2007, 104(34):13833-13838.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , Issue.34 , pp. 13833-13838
    • Ishibashi, K.1    Masuda, K.2    Naito, S.3    Meshi, T.4    Ishikawa, M.5
  • 21
    • 66649102111 scopus 로고    scopus 로고
    • An inhibitory interaction between viral and cellular proteins underlies the resistance of tomato to nonadapted tobamoviruses
    • Ishibashi K., Naito S., Meshi T., Ishikawa M. An inhibitory interaction between viral and cellular proteins underlies the resistance of tomato to nonadapted tobamoviruses. Proc. Natl. Acad. Sci. U.S.A. 2009, 106(21):8778-8783.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , Issue.21 , pp. 8778-8783
    • Ishibashi, K.1    Naito, S.2    Meshi, T.3    Ishikawa, M.4
  • 22
    • 0038540537 scopus 로고    scopus 로고
    • Misfolded plant virus proteins: elicitors and targets of ubiquitylation
    • Jockusch H., Wiegand C. Misfolded plant virus proteins: elicitors and targets of ubiquitylation. FEBS Lett. 2003, 545(2-3):229-232.
    • (2003) FEBS Lett. , vol.545 , Issue.2-3 , pp. 229-232
    • Jockusch, H.1    Wiegand, C.2
  • 23
    • 33746310969 scopus 로고    scopus 로고
    • Plant signal transduction and defense against viral pathogens
    • Kachroo P., Chandra-Shekara A.C., Klessig D.F. Plant signal transduction and defense against viral pathogens. Adv. Virus Res. 2006, 66:161-191.
    • (2006) Adv. Virus Res. , vol.66 , pp. 161-191
    • Kachroo, P.1    Chandra-Shekara, A.C.2    Klessig, D.F.3
  • 24
    • 18944380045 scopus 로고    scopus 로고
    • Characterization of a prokaryotic haemerythrin from the methanotrophic bacterium Methylococcus capsulatus (Bath)
    • Karlsen O.A., Ramsevik L., Bruseth L.J., Larsen Ø., Brenner A., Berven F.S., Jensen H.B., Lillehaug J.R. Characterization of a prokaryotic haemerythrin from the methanotrophic bacterium Methylococcus capsulatus (Bath). FEBS J. 2005, 272(10):2428-2440.
    • (2005) FEBS J. , vol.272 , Issue.10 , pp. 2428-2440
    • Karlsen, O.A.1    Ramsevik, L.2    Bruseth, L.J.3    Larsen, Ø.4    Brenner, A.5    Berven, F.S.6    Jensen, H.B.7    Lillehaug, J.R.8
  • 25
    • 33644805023 scopus 로고    scopus 로고
    • A duplicated pair of Arabidopsis RING-finger E3 ligases contribute to the RPM1- and RPS2-mediated hypersensitive response
    • Kawasaki T., Nam J., Boyes D.C., Holt B.F., Hubert D.A., Wiig A., Dangl J.L. A duplicated pair of Arabidopsis RING-finger E3 ligases contribute to the RPM1- and RPS2-mediated hypersensitive response. Plant J. 2005, 44(2):258-270.
    • (2005) Plant J. , vol.44 , Issue.2 , pp. 258-270
    • Kawasaki, T.1    Nam, J.2    Boyes, D.C.3    Holt, B.F.4    Hubert, D.A.5    Wiig, A.6    Dangl, J.L.7
  • 26
    • 0030957090 scopus 로고    scopus 로고
    • The plant defense response to cucumber mosaic virus in cowpea is elicited by the viral polymerase gene and affects virus accumulation in single cells
    • Kim C.H., Palukaitis P. The plant defense response to cucumber mosaic virus in cowpea is elicited by the viral polymerase gene and affects virus accumulation in single cells. EMBO J. 1997, 16(13):4060-4068.
    • (1997) EMBO J. , vol.16 , Issue.13 , pp. 4060-4068
    • Kim, C.H.1    Palukaitis, P.2
  • 27
    • 33644993733 scopus 로고    scopus 로고
    • Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis
    • Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.S., Deng X.W., Callis J. Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis. Plant Physiol. 2005, 139(4):1597-1611.
    • (2005) Plant Physiol. , vol.139 , Issue.4 , pp. 1597-1611
    • Kraft, E.1    Stone, S.L.2    Ma, L.3    Su, N.4    Gao, Y.5    Lau, O.S.6    Deng, X.W.7    Callis, J.8
  • 28
    • 77249163190 scopus 로고    scopus 로고
    • Arabidopsis synaptotagmin SYTA regulates endocytosis and virus movement protein cell-to-cell transport
    • Lewis J.D., Lazarowitz S.G. Arabidopsis synaptotagmin SYTA regulates endocytosis and virus movement protein cell-to-cell transport. Proc. Natl. Acad. Sci. U.S.A. 2010, 107(6):2491-2496.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , Issue.6 , pp. 2491-2496
    • Lewis, J.D.1    Lazarowitz, S.G.2
  • 30
    • 47049126717 scopus 로고    scopus 로고
    • Cdc34p ubiquitin-conjugating enzyme is a component of the tombusvirus replicase complex and ubiquitinates p33 replication protein
    • Li Z., Barajas D., Panavas T., Herbst D.A., Nagy P.D. Cdc34p ubiquitin-conjugating enzyme is a component of the tombusvirus replicase complex and ubiquitinates p33 replication protein. J. Virol. 2008, 82(14):6911-6926.
    • (2008) J. Virol. , vol.82 , Issue.14 , pp. 6911-6926
    • Li, Z.1    Barajas, D.2    Panavas, T.3    Herbst, D.A.4    Nagy, P.D.5
  • 31
    • 33644693303 scopus 로고    scopus 로고
    • The tobacco mosaic virus 126-kilodalton protein, a constituent of the virus replication complex, alone or within the complex aligns with and traffics along microfilaments
    • Liu J.Z., Blancaflor E.B., Nelson R.S. The tobacco mosaic virus 126-kilodalton protein, a constituent of the virus replication complex, alone or within the complex aligns with and traffics along microfilaments. Plant Physiol. 2005, 138(4):1853-1865.
    • (2005) Plant Physiol. , vol.138 , Issue.4 , pp. 1853-1865
    • Liu, J.Z.1    Blancaflor, E.B.2    Nelson, R.S.3
  • 32
    • 0029556710 scopus 로고
    • Tobacco mosaic virus movement protein associates with the cytoskeleton in tobacco cells
    • McLean B.G., Zupan J., Zambryski P.C. Tobacco mosaic virus movement protein associates with the cytoskeleton in tobacco cells. Plant Cell 1995, 7(12):2101-2114.
    • (1995) Plant Cell , vol.7 , Issue.12 , pp. 2101-2114
    • McLean, B.G.1    Zupan, J.2    Zambryski, P.C.3
  • 33
    • 17444420139 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and plant development
    • Moon J., Parry G., Estelle M. The ubiquitin-proteasome pathway and plant development. Plant Cell 2004, 16(12):3181-3195.
    • (2004) Plant Cell , vol.16 , Issue.12 , pp. 3181-3195
    • Moon, J.1    Parry, G.2    Estelle, M.3
  • 34
    • 51849139963 scopus 로고    scopus 로고
    • Yeast as a model host to explore plant virus-host interactions
    • Nagy P.D. Yeast as a model host to explore plant virus-host interactions. Annu. Rev. Phytopathol. 2008, 46:217-242.
    • (2008) Annu. Rev. Phytopathol. , vol.46 , pp. 217-242
    • Nagy, P.D.1
  • 35
    • 0034099838 scopus 로고    scopus 로고
    • Degradation of tobacco mosaic virus movement protein by the 26S proteasome
    • Reichel C., Beachy R.N. Degradation of tobacco mosaic virus movement protein by the 26S proteasome. J. Virol. 2000, 74(7):3330-3337.
    • (2000) J. Virol. , vol.74 , Issue.7 , pp. 3330-3337
    • Reichel, C.1    Beachy, R.N.2
  • 37
    • 67349191497 scopus 로고    scopus 로고
    • Identification of a novel tobacco DnaJ-like protein that interacts with the movement protein of tobacco mosaic virus
    • Shimizu T., Yoshii A., Sakurai K., Hamada K., Yamaji Y., Suzuki M., Namba S., Hibi T. Identification of a novel tobacco DnaJ-like protein that interacts with the movement protein of tobacco mosaic virus. Arch. Virol. 2009, 154(6):959-967.
    • (2009) Arch. Virol. , vol.154 , Issue.6 , pp. 959-967
    • Shimizu, T.1    Yoshii, A.2    Sakurai, K.3    Hamada, K.4    Yamaji, Y.5    Suzuki, M.6    Namba, S.7    Hibi, T.8
  • 38
    • 33845276321 scopus 로고    scopus 로고
    • LjnsRING, a novel RING finger protein, is required for symbiotic interactions between Mesorhizobium loti and Lotus japonicus
    • Shimomura K., Nomura M., Tajima S., Kouchi H. LjnsRING, a novel RING finger protein, is required for symbiotic interactions between Mesorhizobium loti and Lotus japonicus. Plant Cell Physiol. 2006, 47(11):1572-1581.
    • (2006) Plant Cell Physiol. , vol.47 , Issue.11 , pp. 1572-1581
    • Shimomura, K.1    Nomura, M.2    Tajima, S.3    Kouchi, H.4
  • 39
    • 0038607608 scopus 로고    scopus 로고
    • Complex formation, promiscuity and multi-functionality: protein interactions in disease-resistance pathways
    • Shirasu K., Schulze-Lefert P. Complex formation, promiscuity and multi-functionality: protein interactions in disease-resistance pathways. Trends Plant Sci. 2003, 8(6):252-258.
    • (2003) Trends Plant Sci. , vol.8 , Issue.6 , pp. 252-258
    • Shirasu, K.1    Schulze-Lefert, P.2
  • 40
    • 0033558735 scopus 로고    scopus 로고
    • Heterologous sequences greatly affect foreign gene expression in tobacco mosaic virus-based vectors
    • Shivprasad S., Pogue G.P., Lewandowski D.J., Hidalgo J., Donson J., Grill L.K., Dawson W.O. Heterologous sequences greatly affect foreign gene expression in tobacco mosaic virus-based vectors. Virology 1999, 255(2):312-323.
    • (1999) Virology , vol.255 , Issue.2 , pp. 312-323
    • Shivprasad, S.1    Pogue, G.P.2    Lewandowski, D.J.3    Hidalgo, J.4    Donson, J.5    Grill, L.K.6    Dawson, W.O.7
  • 42
    • 0036015057 scopus 로고    scopus 로고
    • EL5, a rice N-acetylchitooligosaccharide elicitor-responsive RING-H2 finger protein, is a ubiquitin ligase which functions in vitro in co-operation with an elicitor-responsive ubiquitin-conjugating enzyme, OsUBC5b
    • Takai R., Matsuda N., Nakano A., Hasegawa K., Akimoto C., Shibuya N., Minami E. EL5, a rice N-acetylchitooligosaccharide elicitor-responsive RING-H2 finger protein, is a ubiquitin ligase which functions in vitro in co-operation with an elicitor-responsive ubiquitin-conjugating enzyme, OsUBC5b. Plant J. 2002, 30(4):447-455.
    • (2002) Plant J. , vol.30 , Issue.4 , pp. 447-455
    • Takai, R.1    Matsuda, N.2    Nakano, A.3    Hasegawa, K.4    Akimoto, C.5    Shibuya, N.6    Minami, E.7
  • 43
    • 26044454390 scopus 로고    scopus 로고
    • The tobacco ubiquitin-activating enzymes NtE1A and NtE1B are induced by tobacco mosaic virus, wounding and stress hormones
    • Takizawa M., Goto A., Watanabe Y. The tobacco ubiquitin-activating enzymes NtE1A and NtE1B are induced by tobacco mosaic virus, wounding and stress hormones. Mol Cells 2005, 19(2):228-231.
    • (2005) Mol Cells , vol.19 , Issue.2 , pp. 228-231
    • Takizawa, M.1    Goto, A.2    Watanabe, Y.3
  • 44
    • 52049119002 scopus 로고    scopus 로고
    • Negative regulation of PAMP-triggered immunity by an E3 ubiquitin ligase triplet in Arabidopsis
    • Trujillo M., Ichimura K., Casais C., Shirasu K. Negative regulation of PAMP-triggered immunity by an E3 ubiquitin ligase triplet in Arabidopsis. Curr. Biol. 2008, 18(18):1396-1401.
    • (2008) Curr. Biol. , vol.18 , Issue.18 , pp. 1396-1401
    • Trujillo, M.1    Ichimura, K.2    Casais, C.3    Shirasu, K.4
  • 45
    • 0037439086 scopus 로고    scopus 로고
    • Arabidopsis TOBAMOVIRUS MULTIPLICATION (TOM) 2 locus encodes a transmembrane protein that interacts with TOM1
    • Tsujimoto Y., Numaga T., Ohshima K., Yano M.A., Ohsawa R., Goto D.B., Naito S., Ishikawa M. Arabidopsis TOBAMOVIRUS MULTIPLICATION (TOM) 2 locus encodes a transmembrane protein that interacts with TOM1. EMBO J. 2003, 22(2):335-343.
    • (2003) EMBO J. , vol.22 , Issue.2 , pp. 335-343
    • Tsujimoto, Y.1    Numaga, T.2    Ohshima, K.3    Yano, M.A.4    Ohsawa, R.5    Goto, D.B.6    Naito, S.7    Ishikawa, M.8
  • 46
    • 48249105163 scopus 로고    scopus 로고
    • The F-box protein ACRE189/ACIF1 regulates cell death and defense responses activated during pathogen recognition in tobacco and tomato
    • Van den Burg H.A., Tsitsigiannis D.I., Rowland O., Lo J., Rallapalli G., Maclean D., Takken F.L., Jones J.D. The F-box protein ACRE189/ACIF1 regulates cell death and defense responses activated during pathogen recognition in tobacco and tomato. Plant Cell 2008, 20(3):697-719.
    • (2008) Plant Cell , vol.20 , Issue.3 , pp. 697-719
    • Van den Burg, H.A.1    Tsitsigiannis, D.I.2    Rowland, O.3    Lo, J.4    Rallapalli, G.5    Maclean, D.6    Takken, F.L.7    Jones, J.D.8
  • 47
    • 33645028151 scopus 로고    scopus 로고
    • In vivo interaction between Tobacco mosaic virus RNA-dependent RNA polymerase and host translation elongation factor 1A
    • Yamaji Y., Kobayashi T., Hamada K., Sakurai K., Yoshii A., Suzuki M., Namba S., Hibi T. In vivo interaction between Tobacco mosaic virus RNA-dependent RNA polymerase and host translation elongation factor 1A. Virology 2006, 347(1):100-108.
    • (2006) Virology , vol.347 , Issue.1 , pp. 100-108
    • Yamaji, Y.1    Kobayashi, T.2    Hamada, K.3    Sakurai, K.4    Yoshii, A.5    Suzuki, M.6    Namba, S.7    Hibi, T.8
  • 49
    • 0034730162 scopus 로고    scopus 로고
    • TOM1, an Arabidopsis gene required for efficient multiplication of a tobamovirus, encodes a putative transmembrane protein
    • Yamanaka T., Ohta T., Takahashi M., Meshi T., Schmidt R., Dean C., Naito S., Ishikawa M. TOM1, an Arabidopsis gene required for efficient multiplication of a tobamovirus, encodes a putative transmembrane protein. Proc. Natl. Acad. Sci. U.S.A. 2000, 97(18):10107-10112.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , Issue.18 , pp. 10107-10112
    • Yamanaka, T.1    Ohta, T.2    Takahashi, M.3    Meshi, T.4    Schmidt, R.5    Dean, C.6    Naito, S.7    Ishikawa, M.8
  • 50
    • 33745449581 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase activity of arabidopsis PLANT U-BOX17 and its functional tobacco homolog ACRE276 are required for cell death and defense
    • Yang C.W., González-Lamothe R., Ewan R.A., Rowland O., Yoshioka H., Shenton M., Ye H., O'Donnell E., Jones J.D., Sadanandom A. The E3 ubiquitin ligase activity of arabidopsis PLANT U-BOX17 and its functional tobacco homolog ACRE276 are required for cell death and defense. Plant Cell 2006, 18(4):1084-1098.
    • (2006) Plant Cell , vol.18 , Issue.4 , pp. 1084-1098
    • Yang, C.W.1    González-Lamothe, R.2    Ewan, R.A.3    Rowland, O.4    Yoshioka, H.5    Shenton, M.6    Ye, H.7    O'Donnell, E.8    Jones, J.D.9    Sadanandom, A.10
  • 52
    • 0036098489 scopus 로고    scopus 로고
    • Eukaryotic elongation factor 1A interacts with the upstream pseudoknot domain in the 3' untranslated region of tobacco mosaic virus RNA
    • Zeenko V.V., Ryabova L.A., Spirin A.S., Rothnie H.M., Hess D., Browning K.S., Hohn T. Eukaryotic elongation factor 1A interacts with the upstream pseudoknot domain in the 3' untranslated region of tobacco mosaic virus RNA. J. Virol. 2002, 76(11):5678-5691.
    • (2002) J. Virol. , vol.76 , Issue.11 , pp. 5678-5691
    • Zeenko, V.V.1    Ryabova, L.A.2    Spirin, A.S.3    Rothnie, H.M.4    Hess, D.5    Browning, K.S.6    Hohn, T.7
  • 53
    • 14644422554 scopus 로고    scopus 로고
    • Spotted leaf11, a negative regulator of plant cell death and defense, encodes a U-box/armadillo repeat protein endowed with E3 ubiquitin ligase activity
    • Zeng L.R., Qu S., Bordeos A., Yang C., Baraoidan M., Yan H., Xie Q., Nahm B.H., Leung H., Wang G.L. Spotted leaf11, a negative regulator of plant cell death and defense, encodes a U-box/armadillo repeat protein endowed with E3 ubiquitin ligase activity. Plant Cell 2004, 16(10):2795-2808.
    • (2004) Plant Cell , vol.16 , Issue.10 , pp. 2795-2808
    • Zeng, L.R.1    Qu, S.2    Bordeos, A.3    Yang, C.4    Baraoidan, M.5    Yan, H.6    Xie, Q.7    Nahm, B.H.8    Leung, H.9    Wang, G.L.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.