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Volumn 72, Issue 1-3, 2008, Pages 39-45

Decreased level of ferredoxin I in Tobacco mosaic virus-infected tobacco is associated with development of the mosaic symptom

Author keywords

Chlorosis induction; Ferredoxin I; Nicotiana benthamiana; Nicotiana tabacum; Virus infection

Indexed keywords

NICOTIANA BENTHAMIANA; NICOTIANA TABACUM; TOBACCO MOSAIC VIRUS;

EID: 51349135380     PISSN: 08855765     EISSN: 10961178     Source Type: Journal    
DOI: 10.1016/j.pmpp.2008.05.004     Document Type: Article
Times cited : (31)

References (52)
  • 2
    • 3042761274 scopus 로고    scopus 로고
    • Roles for host factors in plant viral pathogenicity
    • Whitham S.A., and Wang Y.Z. Roles for host factors in plant viral pathogenicity. Curr Opin Plant Biol 7 (2004) 365-371
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 365-371
    • Whitham, S.A.1    Wang, Y.Z.2
  • 3
    • 0041766197 scopus 로고    scopus 로고
    • Tobacco mosaic virus induced alterations in the gene expression profile of Arabidopsis thaliana
    • Golem S., and Culver J.N. Tobacco mosaic virus induced alterations in the gene expression profile of Arabidopsis thaliana. Mol Plant-Microbe Interact 16 (2003) 681-688
    • (2003) Mol Plant-Microbe Interact , vol.16 , pp. 681-688
    • Golem, S.1    Culver, J.N.2
  • 4
    • 33750208007 scopus 로고    scopus 로고
    • Alterations of NADPH: protochlorophyllide oxidoreductase quantity and lipid composition in etiolated barley seedlings infected by Barley stripe mosaic virus (BSMV)
    • Harsányi A., Ryberg M., Andersson M.X., Bóka K., László L., Botond G., et al. Alterations of NADPH: protochlorophyllide oxidoreductase quantity and lipid composition in etiolated barley seedlings infected by Barley stripe mosaic virus (BSMV). Mol Plant Pathol 7 (2006) 533-541
    • (2006) Mol Plant Pathol , vol.7 , pp. 533-541
    • Harsányi, A.1    Ryberg, M.2    Andersson, M.X.3    Bóka, K.4    László, L.5    Botond, G.6
  • 5
    • 0344495387 scopus 로고    scopus 로고
    • Depletion of the photosystem II core complex in mature tobacco leaves infected by the flavum strain of Tobacco mosaic virus
    • Lehto K., Tikkanen M., Hiriart J.B., Paakkarinen V., and Aro E.M. Depletion of the photosystem II core complex in mature tobacco leaves infected by the flavum strain of Tobacco mosaic virus. Mol Plant-Microbe Interact 16 (2003) 1135-1144
    • (2003) Mol Plant-Microbe Interact , vol.16 , pp. 1135-1144
    • Lehto, K.1    Tikkanen, M.2    Hiriart, J.B.3    Paakkarinen, V.4    Aro, E.M.5
  • 6
    • 33750295363 scopus 로고    scopus 로고
    • Cloning of cDNAs encoding the three subunits of oxygen evolving complex in Nicotiana benthamiana and gene expression changes in tobacco leaves infected with Tobacco mosaic virus
    • Sui C., Fan Z.F., Wong S.M., and Li H.F. Cloning of cDNAs encoding the three subunits of oxygen evolving complex in Nicotiana benthamiana and gene expression changes in tobacco leaves infected with Tobacco mosaic virus. Physiol Mol Plant Pathol 68 (2006) 61-68
    • (2006) Physiol Mol Plant Pathol , vol.68 , pp. 61-68
    • Sui, C.1    Fan, Z.F.2    Wong, S.M.3    Li, H.F.4
  • 7
    • 0023858197 scopus 로고
    • The discovery of ferredoxins: the photosynthetic path
    • Arnon D.I. The discovery of ferredoxins: the photosynthetic path. Trends Biochem Sci 13 (1988) 30-33
    • (1988) Trends Biochem Sci , vol.13 , pp. 30-33
    • Arnon, D.I.1
  • 8
    • 85051496696 scopus 로고    scopus 로고
    • Primary photosynthate production: physiology and metabolism
    • Zamski E., and Schaffer A.A. (Eds), Marcel Dekker, New York
    • Leegood R.C. Primary photosynthate production: physiology and metabolism. In: Zamski E., and Schaffer A.A. (Eds). Photoassimilate distribution in plants and crops. Source-link relationships (1996), Marcel Dekker, New York 21-41
    • (1996) Photoassimilate distribution in plants and crops. Source-link relationships , pp. 21-41
    • Leegood, R.C.1
  • 9
    • 0026097297 scopus 로고
    • Ferredoxin-dependent Chloroplast enzymes
    • Knaff D.B., and Hirasawa M. Ferredoxin-dependent Chloroplast enzymes. Biochim Biophys Acta 1056 (1991) 93-125
    • (1991) Biochim Biophys Acta , vol.1056 , pp. 93-125
    • Knaff, D.B.1    Hirasawa, M.2
  • 10
    • 0001038547 scopus 로고    scopus 로고
    • Ferredoxin and ferredoxin-dependent enzymes
    • Ort D.R., and Yochem C.F. (Eds), Kluwer Academic Publishers, Dordrecht
    • Knaff D.B. Ferredoxin and ferredoxin-dependent enzymes. In: Ort D.R., and Yochem C.F. (Eds). Oxygenic photosynthesis: the light reactions (1996), Kluwer Academic Publishers, Dordrecht 333-361
    • (1996) Oxygenic photosynthesis: the light reactions , pp. 333-361
    • Knaff, D.B.1
  • 11
    • 0001391899 scopus 로고
    • Concerning a dual function of coupled cyclic electron transport in leaves
    • Heber U., and Walker D. Concerning a dual function of coupled cyclic electron transport in leaves. Plant Physiol 100 (1992) 1621-1626
    • (1992) Plant Physiol , vol.100 , pp. 1621-1626
    • Heber, U.1    Walker, D.2
  • 12
    • 2942537759 scopus 로고    scopus 로고
    • Cyclic electron flow around photosystem I is essential for photosynthesis
    • Munekage Y., Hashimoto M., Miyake C., Tomizawa K.I., Endo T., Tasaka M., et al. Cyclic electron flow around photosystem I is essential for photosynthesis. Nature 429 (2004) 579-582
    • (2004) Nature , vol.429 , pp. 579-582
    • Munekage, Y.1    Hashimoto, M.2    Miyake, C.3    Tomizawa, K.I.4    Endo, T.5    Tasaka, M.6
  • 14
    • 0031444519 scopus 로고    scopus 로고
    • Thioredoxins: structure and function in plant cells
    • Jacquot J.P., Lancelin J.M., and Meyer Y. Thioredoxins: structure and function in plant cells. New Phytol 136 (1997) 543-570
    • (1997) New Phytol , vol.136 , pp. 543-570
    • Jacquot, J.P.1    Lancelin, J.M.2    Meyer, Y.3
  • 15
    • 0019878627 scopus 로고
    • Dark modulation of NADP-dependent malate dehydrogenase and glucose-6-phosphate dehydrogenase in the chloroplast
    • Scheibe R., and Anderson L.E. Dark modulation of NADP-dependent malate dehydrogenase and glucose-6-phosphate dehydrogenase in the chloroplast. Biochim Biophys Acta 636 (1981) 58-64
    • (1981) Biochim Biophys Acta , vol.636 , pp. 58-64
    • Scheibe, R.1    Anderson, L.E.2
  • 16
    • 0842264043 scopus 로고    scopus 로고
    • A post genomic characterization of Arabidopsis ferredoxins
    • Hanke G.T., Kimata-Ariga Y., Taniguchi I., and Hase T. A post genomic characterization of Arabidopsis ferredoxins. Plant Physiol 134 (2004) 255-264
    • (2004) Plant Physiol , vol.134 , pp. 255-264
    • Hanke, G.T.1    Kimata-Ariga, Y.2    Taniguchi, I.3    Hase, T.4
  • 17
    • 0000439105 scopus 로고
    • cis-acting elements for light regulation of pea ferredoxin I gene expression are located within transcribed sequences
    • Elliott R.C., Dickey L.F., White M.J., and Thompson W.F. cis-acting elements for light regulation of pea ferredoxin I gene expression are located within transcribed sequences. Plant Cell 1 (1989) 691-698
    • (1989) Plant Cell , vol.1 , pp. 691-698
    • Elliott, R.C.1    Dickey, L.F.2    White, M.J.3    Thompson, W.F.4
  • 18
    • 0026845980 scopus 로고
    • Both internal and external regulatory elements control expression of the pea Fed-1 gene in transgenic tobacco seedlings
    • Gallo-Meagher M., Sowinski D.A., Elliott R.C., and Thompson W.F. Both internal and external regulatory elements control expression of the pea Fed-1 gene in transgenic tobacco seedlings. Plant Cell 4 (1992) 389-395
    • (1992) Plant Cell , vol.4 , pp. 389-395
    • Gallo-Meagher, M.1    Sowinski, D.A.2    Elliott, R.C.3    Thompson, W.F.4
  • 19
    • 33747488135 scopus 로고    scopus 로고
    • Functional replacement of ferredoxin by a cyanobacterial flavodoxin in tobacco confers broad-range stress tolerance
    • Tognetti V.B., Palatnik J.F., Fillat M.F., Melzer M., Hajirezaei M.R., Valle E.M., et al. Functional replacement of ferredoxin by a cyanobacterial flavodoxin in tobacco confers broad-range stress tolerance. Plant Cell 18 (2006) 2035-2050
    • (2006) Plant Cell , vol.18 , pp. 2035-2050
    • Tognetti, V.B.1    Palatnik, J.F.2    Fillat, M.F.3    Melzer, M.4    Hajirezaei, M.R.5    Valle, E.M.6
  • 20
    • 26944444678 scopus 로고    scopus 로고
    • Expression profiling soybean response to Pseudomonas syringae reveals new defense-related genes and rapid HR-specific down regulation of photosynthesis
    • Zou J., Rodriguez-Zas S., Aldea M., Li M., Zhu J., Gonzalez D.O., et al. Expression profiling soybean response to Pseudomonas syringae reveals new defense-related genes and rapid HR-specific down regulation of photosynthesis. Mol Plant-Microbe Interact 18 (2005) 1161-1174
    • (2005) Mol Plant-Microbe Interact , vol.18 , pp. 1161-1174
    • Zou, J.1    Rodriguez-Zas, S.2    Aldea, M.3    Li, M.4    Zhu, J.5    Gonzalez, D.O.6
  • 21
    • 33846094906 scopus 로고    scopus 로고
    • Disease resistance to bacterial pathogens affected by the amount of ferredoxin-I protein in plants
    • Huang H.E., Ger M.J., Chen C.Y., Pandey A.K., Yip M.K., Chou H.W., et al. Disease resistance to bacterial pathogens affected by the amount of ferredoxin-I protein in plants. Mol Plant Pathol 8 (2007) 129-137
    • (2007) Mol Plant Pathol , vol.8 , pp. 129-137
    • Huang, H.E.1    Ger, M.J.2    Chen, C.Y.3    Pandey, A.K.4    Yip, M.K.5    Chou, H.W.6
  • 22
    • 33344465235 scopus 로고    scopus 로고
    • Comparative microarray analysis of programmed cell death induced by proteasome malfunction and hypersensitive response in plants
    • Kim M., Lee S., Park K., Jeong E.J., Ryu C.M., Choi D., et al. Comparative microarray analysis of programmed cell death induced by proteasome malfunction and hypersensitive response in plants. Biochem Biophys Res Commun 342 (2006) 514-521
    • (2006) Biochem Biophys Res Commun , vol.342 , pp. 514-521
    • Kim, M.1    Lee, S.2    Park, K.3    Jeong, E.J.4    Ryu, C.M.5    Choi, D.6
  • 23
    • 6344284936 scopus 로고    scopus 로고
    • A hypersensitive response was induced by virulent bacteria in transgenic tobacco plants overexpressing a plant ferredoxin-like protein (PFLP)
    • Huang H.E., Ger M.J., Yip M.K., Chen C.Y., Pandey A.K., and Feng T.Y. A hypersensitive response was induced by virulent bacteria in transgenic tobacco plants overexpressing a plant ferredoxin-like protein (PFLP). Physiol Mol Plant Pathol 64 (2004) 103-110
    • (2004) Physiol Mol Plant Pathol , vol.64 , pp. 103-110
    • Huang, H.E.1    Ger, M.J.2    Yip, M.K.3    Chen, C.Y.4    Pandey, A.K.5    Feng, T.Y.6
  • 24
    • 0035058257 scopus 로고    scopus 로고
    • Transgenic rice plants expressing the ferredoxin-like protein (AP1) from sweet pepper show enhanced resistance to Xanthomonas oryzae pv. oryzae
    • Tang K.X., Sun X.F., Hu Q.N., Wu A.Z., Lin C.H., Lin H.J., et al. Transgenic rice plants expressing the ferredoxin-like protein (AP1) from sweet pepper show enhanced resistance to Xanthomonas oryzae pv. oryzae. Plant Sci 160 (2001) 1035-1042
    • (2001) Plant Sci , vol.160 , pp. 1035-1042
    • Tang, K.X.1    Sun, X.F.2    Hu, Q.N.3    Wu, A.Z.4    Lin, C.H.5    Lin, H.J.6
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0034870335 scopus 로고    scopus 로고
    • Gene C2 of the monopartite geminivirus Tomato yellow leaf curl virus-China encodes a pathogenicity determinant that is localized in the nucleus
    • van Wezel R., Liu H., Tien P., Stanley J., and Hong Y. Gene C2 of the monopartite geminivirus Tomato yellow leaf curl virus-China encodes a pathogenicity determinant that is localized in the nucleus. Mol Plant-Microbe Interact 14 (2001) 1125-1128
    • (2001) Mol Plant-Microbe Interact , vol.14 , pp. 1125-1128
    • van Wezel, R.1    Liu, H.2    Tien, P.3    Stanley, J.4    Hong, Y.5
  • 27
    • 0026892978 scopus 로고
    • Potato virus X as a vector for gene expression in plants
    • Chapman S., Kavanaph T., and Baulcombe D. Potato virus X as a vector for gene expression in plants. Plant J 2 (1992) 549-557
    • (1992) Plant J , vol.2 , pp. 549-557
    • Chapman, S.1    Kavanaph, T.2    Baulcombe, D.3
  • 28
    • 0033057163 scopus 로고    scopus 로고
    • Hydrogen peroxide is generated systemically in plant leaves by wounding and systemin via the octadecanoid pathway
    • Orozco-Cárdenas M.L., and Ryan C. Hydrogen peroxide is generated systemically in plant leaves by wounding and systemin via the octadecanoid pathway. Proc Natl Acad Sci USA 96 (1999) 6553-6557
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6553-6557
    • Orozco-Cárdenas, M.L.1    Ryan, C.2
  • 29
    • 0030748530 scopus 로고    scopus 로고
    • 2 accumulation in papillae and hypersensitive response during the barley-powdery mildew interaction
    • 2 accumulation in papillae and hypersensitive response during the barley-powdery mildew interaction. Plant J 11 (1997) 1187-1194
    • (1997) Plant J , vol.11 , pp. 1187-1194
    • Thordal-Christensen, H.1    Zhang, Z.2    Wei, Y.3    Collinge, D.B.4
  • 30
    • 0027012738 scopus 로고
    • A versatile binary vector system with a T-DNA organisational structure conducive to efficient integration of cloned DNA into the plant genome
    • Gleave A.P. A versatile binary vector system with a T-DNA organisational structure conducive to efficient integration of cloned DNA into the plant genome. Plant Mol Biol 20 (1992) 1203-1207
    • (1992) Plant Mol Biol , vol.20 , pp. 1203-1207
    • Gleave, A.P.1
  • 31
    • 0033050334 scopus 로고    scopus 로고
    • An efficient Agrobacterium tumefaciens-mediated transformation and regeneration system for cotyledons of spinach (Spinacia oleracea L.)
    • Zhang H.X., and Zeevaart J.A.D. An efficient Agrobacterium tumefaciens-mediated transformation and regeneration system for cotyledons of spinach (Spinacia oleracea L.). Plant Cell Rep 18 (1999) 640-645
    • (1999) Plant Cell Rep , vol.18 , pp. 640-645
    • Zhang, H.X.1    Zeevaart, J.A.D.2
  • 33
    • 0002093629 scopus 로고
    • In vitro import of protein into chloroplasts
    • Gelvin S.B., and Schilperoort R.B. (Eds), Kluwer Academic Publishers, Boston
    • Bruce B.D., Perry S., Froehlich J., and Keegstra K. In vitro import of protein into chloroplasts. In: Gelvin S.B., and Schilperoort R.B. (Eds). Plant Molecular Biology Manual Vol J1 (1994), Kluwer Academic Publishers, Boston 1-15
    • (1994) Plant Molecular Biology Manual , vol.J1 , pp. 1-15
    • Bruce, B.D.1    Perry, S.2    Froehlich, J.3    Keegstra, K.4
  • 34
    • 0028950296 scopus 로고
    • A single nucleotide change in the coat protein gene of Tobacco mosaic virus is involved in the induction of severe chlorosis
    • Banerjee N., Wang J.Y., and Zaitlin M. A single nucleotide change in the coat protein gene of Tobacco mosaic virus is involved in the induction of severe chlorosis. Virology 207 (1995) 234-239
    • (1995) Virology , vol.207 , pp. 234-239
    • Banerjee, N.1    Wang, J.Y.2    Zaitlin, M.3
  • 36
    • 0027613997 scopus 로고
    • Light-regulated expression of the Arabidopsis thaliana ferredoxin. A gene involves both transcriptional and post-transcriptional processes
    • Vorst O., van Dam F., Weisbeek P., and Smeekens S. Light-regulated expression of the Arabidopsis thaliana ferredoxin. A gene involves both transcriptional and post-transcriptional processes. Plant J 3 (1993) 793-803
    • (1993) Plant J , vol.3 , pp. 793-803
    • Vorst, O.1    van Dam, F.2    Weisbeek, P.3    Smeekens, S.4
  • 37
    • 0029138945 scopus 로고
    • Dissection of oxidative stress tolerance using transgenic plants
    • Allen R.D. Dissection of oxidative stress tolerance using transgenic plants. Plant Physiol 107 (1995) 1049-1054
    • (1995) Plant Physiol , vol.107 , pp. 1049-1054
    • Allen, R.D.1
  • 38
    • 3242715114 scopus 로고    scopus 로고
    • Reactive oxygen species: metabolism, oxidative stress, and signal transduction
    • Apel K., and Hirt H. Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Annu Rev Plant Biol 55 (2004) 373-399
    • (2004) Annu Rev Plant Biol , vol.55 , pp. 373-399
    • Apel, K.1    Hirt, H.2
  • 41
    • 0032532127 scopus 로고    scopus 로고
    • HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status
    • Wells D.R., Tanguay R.L., Le H., and Gallie D.R. HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status. Genes Dev 12 (1998) 3236-3251
    • (1998) Genes Dev , vol.12 , pp. 3236-3251
    • Wells, D.R.1    Tanguay, R.L.2    Le, H.3    Gallie, D.R.4
  • 42
    • 0033877118 scopus 로고    scopus 로고
    • Heat shock protein HSP101 binds to the Fed-1 internal light regulatory element and mediates its high translational activity
    • Ling J., Wells D.R., Tanguay R.L., Dickey L.F., Thompson W.F., and Gallie D.R. Heat shock protein HSP101 binds to the Fed-1 internal light regulatory element and mediates its high translational activity. Plant Cell 12 (2000) 1213-1227
    • (2000) Plant Cell , vol.12 , pp. 1213-1227
    • Ling, J.1    Wells, D.R.2    Tanguay, R.L.3    Dickey, L.F.4    Thompson, W.F.5    Gallie, D.R.6
  • 43
    • 0033768589 scopus 로고    scopus 로고
    • Complex spatial responses to Cucumber mosaic virus infection in susceptible Cucurbita pepo cotyledons
    • Havelda Z., and Maule A.J. Complex spatial responses to Cucumber mosaic virus infection in susceptible Cucurbita pepo cotyledons. Plant Cell 12 (2000) 1975-1985
    • (2000) Plant Cell , vol.12 , pp. 1975-1985
    • Havelda, Z.1    Maule, A.J.2
  • 44
    • 0000207280 scopus 로고
    • Superinfection by strains of Tobacco mosaic virus
    • Fulton R.W. Superinfection by strains of Tobacco mosaic virus. Phytopathology 41 (1951) 579-592
    • (1951) Phytopathology , vol.41 , pp. 579-592
    • Fulton, R.W.1
  • 45
    • 20044385057 scopus 로고    scopus 로고
    • Redox regulation of carbon storage and partitioning in response to light and sugars
    • Geigenberger P., Kolbe A., and Tiessen A. Redox regulation of carbon storage and partitioning in response to light and sugars. J Exp Bot 56 (2005) 1469-1479
    • (2005) J Exp Bot , vol.56 , pp. 1469-1479
    • Geigenberger, P.1    Kolbe, A.2    Tiessen, A.3
  • 46
    • 0035976815 scopus 로고    scopus 로고
    • Ferredoxins of the third kind
    • Meyer J. Ferredoxins of the third kind. FEBS Lett 509 (2001) 1-5
    • (2001) FEBS Lett , vol.509 , pp. 1-5
    • Meyer, J.1
  • 47
    • 0346420991 scopus 로고    scopus 로고
    • Decreased content of leaf ferredoxin changes electron distribution and limits photosynthesis in transgenic potato plants
    • Holtgrefe S., Bader K.P., Horton P., Scheibe R., von Schaewen A., and Backhausen J.E. Decreased content of leaf ferredoxin changes electron distribution and limits photosynthesis in transgenic potato plants. Plant Physiol 133 (2003) 1768-1778
    • (2003) Plant Physiol , vol.133 , pp. 1768-1778
    • Holtgrefe, S.1    Bader, K.P.2    Horton, P.3    Scheibe, R.4    von Schaewen, A.5    Backhausen, J.E.6
  • 48
    • 0025417932 scopus 로고
    • Wound-inducible potato inhibitor II genes: enhancement of expression by sucrose
    • Johnson R., and Ryan C.A. Wound-inducible potato inhibitor II genes: enhancement of expression by sucrose. Plant Mol Biol 14 (1990) 527-536
    • (1990) Plant Mol Biol , vol.14 , pp. 527-536
    • Johnson, R.1    Ryan, C.A.2
  • 49
    • 0000236996 scopus 로고
    • Sugar-dependent expression of the CHS-A gene for chalcone synthase from petunia in transgenic Arabidopsis
    • Tsukaya H., Oshima T., Naito S., Chino M., and Komeda Y. Sugar-dependent expression of the CHS-A gene for chalcone synthase from petunia in transgenic Arabidopsis. Plant Physiol 97 (1991) 1414-1421
    • (1991) Plant Physiol , vol.97 , pp. 1414-1421
    • Tsukaya, H.1    Oshima, T.2    Naito, S.3    Chino, M.4    Komeda, Y.5
  • 50
    • 0033819994 scopus 로고    scopus 로고
    • Inhibition of photosynthesis by viral infection: Effect on PSII structure and function
    • Rahoutei J., García-Luque I., and Barón M. Inhibition of photosynthesis by viral infection: Effect on PSII structure and function. Physiol Plantarum 110 (2000) 286-292
    • (2000) Physiol Plantarum , vol.110 , pp. 286-292
    • Rahoutei, J.1    García-Luque, I.2    Barón, M.3
  • 51
    • 0036065973 scopus 로고    scopus 로고
    • Silencing of a gene encoding a protein component of the oxygen-evolving complex of photosystem II enhances virus replication in plants
    • Abbink T.E., Peart J.R., Mos T.N., Baulcombe D.C., Bol J.F., and Linthorst H.J. Silencing of a gene encoding a protein component of the oxygen-evolving complex of photosystem II enhances virus replication in plants. Virology 295 (2002) 307-319
    • (2002) Virology , vol.295 , pp. 307-319
    • Abbink, T.E.1    Peart, J.R.2    Mos, T.N.3    Baulcombe, D.C.4    Bol, J.F.5    Linthorst, H.J.6
  • 52
    • 33144489725 scopus 로고    scopus 로고
    • Identification of a Plum pox virus CI-interacting protein from chloroplast that has a negative effect in virus infection
    • Jiménez I., López L., Alamillo J.M., Valli A., and García J.A. Identification of a Plum pox virus CI-interacting protein from chloroplast that has a negative effect in virus infection. Mol Plant-Microbe Interact 19 (2006) 350-358
    • (2006) Mol Plant-Microbe Interact , vol.19 , pp. 350-358
    • Jiménez, I.1    López, L.2    Alamillo, J.M.3    Valli, A.4    García, J.A.5


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