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Volumn 28, Issue 4, 2015, Pages 467-481

Insights into the Polerovirus-plant interactome revealed by coimmunoprecipitation and mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

AGROBACTERIUM TUMEFACIENS; HEXAPODA; LUTEOVIRIDAE; NICOTIANA BENTHAMIANA; POLEROVIRUS; POTATO LEAFROLL VIRUS;

EID: 84927629325     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI-11-14-0363-R     Document Type: Article
Times cited : (43)

References (96)
  • 1
    • 0025187346 scopus 로고
    • Expression of the genome of Potato leafroll virus: Readthrough of the coat protein termination codon in vivo
    • Bahner, I., Lamb, J., Mayo, M. A., and Hay, R. T. 1990. Expression of the genome of Potato leafroll virus: Readthrough of the coat protein termination codon in vivo. J. Gen. Virol. 71:2251-2256.
    • (1990) J. Gen. Virol. , vol.71 , pp. 2251-2256
    • Bahner, I.1    Lamb, J.2    Mayo, M.A.3    Hay, R.T.4
  • 2
    • 34548474870 scopus 로고    scopus 로고
    • The Polerovirus silencing suppressor P0 targets ARGONAUTE proteins for degradation
    • Baumberger, N., Tsai, C. H., Lie, M., Havecker, E., and Baulcombe, D. C. 2007. The Polerovirus silencing suppressor P0 targets ARGONAUTE proteins for degradation. Curr. Biol. 17:1609-1614.
    • (2007) Curr. Biol. , vol.17 , pp. 1609-1614
    • Baumberger, N.1    Tsai, C.H.2    Lie, M.3    Havecker, E.4    Baulcombe, D.C.5
  • 5
    • 84898630787 scopus 로고    scopus 로고
    • Both structural and non-structural forms of the readthrough protein of Cucurbit aphid-borne yellows virus are essential for efficient systemic infection of plants
    • Boissinot, S., Erdinger, M., Monsion, B., Ziegler-Graff, V., and Brault, V. 2014. Both structural and non-structural forms of the readthrough protein of Cucurbit aphid-borne yellows virus are essential for efficient systemic infection of plants. PLoS One 9:e93448.
    • (2014) PLoS One , vol.9 , pp. e93448
    • Boissinot, S.1    Erdinger, M.2    Monsion, B.3    Ziegler-Graff, V.4    Brault, V.5
  • 7
    • 33845970196 scopus 로고    scopus 로고
    • Proteome analysis of plant-virus interactome: Comprehensive data for virus multiplication inside their hosts
    • Brizard, J. P., Carapito, C., Delalande, F., Van Dorsselaer, A., and Brugidou, C. 2006. Proteome analysis of plant-virus interactome: Comprehensive data for virus multiplication inside their hosts. Mol. Cell. Proteomics 5:2279-2297.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2279-2297
    • Brizard, J.P.1    Carapito, C.2    Delalande, F.3    Van Dorsselaer, A.4    Brugidou, C.5
  • 10
    • 33749020281 scopus 로고    scopus 로고
    • Intronregulated expression of SUVH3, an Arabidopsis Su (var) 3-9 homologue
    • Casas-Mollano, J. A., Lao, N. T., and Kavanagh, T. A. 2006. Intronregulated expression of SUVH3, an Arabidopsis Su (var) 3-9 homologue. J. Exp. Bot. 57:3301-3311.
    • (2006) J. Exp. Bot. , vol.57 , pp. 3301-3311
    • Casas-Mollano, J.A.1    Lao, N.T.2    Kavanagh, T.A.3
  • 11
    • 79953703744 scopus 로고    scopus 로고
    • Quantification of protein-protein interactions with chemical cross-linking and mass spectrometry
    • Chavez, J. D., Liu, N. L., and Bruce, J. E. 2011. Quantification of protein-protein interactions with chemical cross-linking and mass spectrometry. J. Proteome Res. 10:1528-1537.
    • (2011) J. Proteome Res. , vol.10 , pp. 1528-1537
    • Chavez, J.D.1    Liu, N.L.2    Bruce, J.E.3
  • 12
    • 84860602175 scopus 로고    scopus 로고
    • Cross-linking measurements of the Potato leafroll virus reveal protein interaction topologies required for virion stability, aphid transmission, and virus-plant interactions
    • Chavez, J. D., Cilia, M., Weisbrod, C. R., Ju, H. J., Eng, J. K., Gray, S. M., and Bruce, J. E. 2012. Cross-linking measurements of the Potato leafroll virus reveal protein interaction topologies required for virion stability, aphid transmission, and virus-plant interactions. J. Proteome Res. 11:2968-2981.
    • (2012) J. Proteome Res. , vol.11 , pp. 2968-2981
    • Chavez, J.D.1    Cilia, M.2    Weisbrod, C.R.3    Ju, H.J.4    Eng, J.K.5    Gray, S.M.6    Bruce, J.E.7
  • 14
    • 84868357292 scopus 로고    scopus 로고
    • Analyzing protein-protein interactions from affinity purification-mass spectrometry data with SAINT
    • Choi, H., Liu, G., Mellacheruvu, D., Tyers, M., Gingras, A. C., and Nesvizhskii, A. I. 2012. Analyzing protein-protein interactions from affinity purification-mass spectrometry data with SAINT. Curr. Protoc. Bioinfor. 39:8.15.1-8.15.23.
    • (2012) Curr. Protoc. Bioinfor. , vol.39 , pp. 8151-81523
    • Choi, H.1    Liu, G.2    Mellacheruvu, D.3    Tyers, M.4    Gingras, A.C.5    Nesvizhskii, A.I.6
  • 15
    • 84868120044 scopus 로고    scopus 로고
    • Discovery and targeted LC-MS/MS of purified polerovirus reveals differences in the virus-host interactome associated with altered aphid transmission
    • Cilia, M., Peter, K. A., Bereman, M. S., Howe, K., Fish, T., Smith, D., Gildow, F., MacCoss, M. J., Thannhauser, T. W., and Gray, S. M. 2012. Discovery and targeted LC-MS/MS of purified polerovirus reveals differences in the virus-host interactome associated with altered aphid transmission. PLoS One 7:e48177.
    • (2012) PLoS One , vol.7 , pp. e48177
    • Cilia, M.1    Peter, K.A.2    Bereman, M.S.3    Howe, K.4    Fish, T.5    Smith, D.6    Gildow, F.7    MacCoss, M.J.8    Thannhauser, T.W.9    Gray, S.M.10
  • 18
    • 79957574414 scopus 로고    scopus 로고
    • Affinity purification of protein complexes
    • Cristea, I. M., and Chait, B. T. 2011. Affinity purification of protein complexes. Cold Spring Harb. Protoc. 2011(5): pdb.prot5611.
    • (2011) Cold Spring Harb. Protoc. , vol.2011 , Issue.5
    • Cristea, I.M.1    Chait, B.T.2
  • 20
    • 77954485440 scopus 로고    scopus 로고
    • Human cytomegalovirus pUL83 stimulates activity of the viral immediateearly promoter through its interaction with the cellular IFI16 protein
    • Cristea, I. M., Moorman, N. J., Terhune, S. S., Cuevas, C. D., O'Keefe, E. S., Rout, M. P., Chait, B. T., and Shenk, T. 2010. Human cytomegalovirus pUL83 stimulates activity of the viral immediateearly promoter through its interaction with the cellular IFI16 protein. J. Virol. 84:7803-7814.
    • (2010) J. Virol. , vol.84 , pp. 7803-7814
    • Cristea, I.M.1    Moorman, N.J.2    Terhune, S.S.3    Cuevas, C.D.4    O'Keefe, E.S.5    Rout, M.P.6    Chait, B.T.7    Shenk, T.8
  • 22
    • 35148834683 scopus 로고    scopus 로고
    • Virus-induced disease: Altering host physiology one interaction at a time
    • Culver, J. N., and Padmanabhan, M. S. 2007. Virus-induced disease: Altering host physiology one interaction at a time. Annu. Rev. Phytopathol. 45:221-243.
    • (2007) Annu. Rev. Phytopathol. , vol.45 , pp. 221-243
    • Culver, J.N.1    Padmanabhan, M.S.2
  • 23
    • 0035226437 scopus 로고    scopus 로고
    • Towards defining the urinary proteome using liquid chromatographytandem mass spectrometry. II. Limitations of complex mixture analyses
    • Davis, M. T., Spahr, C. S., McGinley, M. D., Robinson, J. H., Bures, E. J., Beierle, J., Mort, J., Yu, W., Luethy, R., and Patterson, S. D. 2001. Towards defining the urinary proteome using liquid chromatographytandem mass spectrometry. II. Limitations of complex mixture analyses. Proteomics 1:108-117.
    • (2001) Proteomics , vol.1 , pp. 108-117
    • Davis, M.T.1    Spahr, C.S.2    McGinley, M.D.3    Robinson, J.H.4    Bures, E.J.5    Beierle, J.6    Mort, J.7    Yu, W.8    Luethy, R.9    Patterson, S.D.10
  • 25
    • 0034969736 scopus 로고    scopus 로고
    • The Arabidopsis 14-3-3 family of signaling regulators
    • DeLille, J. M., Sehnke, P. C., and Ferl, R. J. 2001. The Arabidopsis 14-3-3 family of signaling regulators. Plant Physiol. 126:35-38.
    • (2001) Plant Physiol. , vol.126 , pp. 35-38
    • De Lille, J.M.1    Sehnke, P.C.2    Ferl, R.J.3
  • 26
    • 84867466100 scopus 로고    scopus 로고
    • Recent insights into plant-virus interactions through proteomic analysis
    • Di Carli, M., Benvenuto, E., and Donini, M. 2012. Recent insights into plant-virus interactions through proteomic analysis. J. Proteome Res. 11:4765-4780.
    • (2012) J. Proteome Res. , vol.11 , pp. 4765-4780
    • Di Carli, M.1    Benvenuto, E.2    Donini, M.3
  • 27
    • 77954763024 scopus 로고    scopus 로고
    • Plant immunity: Towards an integrated view of plant-pathogen interactions
    • Dodds, P. N., and Rathjen, J. P. 2010. Plant immunity: Towards an integrated view of plant-pathogen interactions. Nat. Rev. Genet. 11:539-548.
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 539-548
    • Dodds, P.N.1    Rathjen, J.P.2
  • 29
    • 41049098779 scopus 로고    scopus 로고
    • Volatiles from potato plants infected with potato leafroll virus attract and arrest the virus vector, Myzus persicae (Homoptera: Aphididae)
    • Eigenbrode, S. D., Ding, H., Shiel, P., and Berger, P. H. 2002. Volatiles from potato plants infected with potato leafroll virus attract and arrest the virus vector, Myzus persicae (Homoptera: Aphididae). Proc. Biol. Sci. 269:455-460.
    • (2002) Proc. Biol. Sci. , vol.269 , pp. 455-460
    • Eigenbrode, S.D.1    Ding, H.2    Shiel, P.3    Berger, P.H.4
  • 30
    • 84876423513 scopus 로고    scopus 로고
    • Towards an integrated molecular model of plant-virus interactions
    • Elena, S. F., and Rodrigo, G. 2012. Towards an integrated molecular model of plant-virus interactions. Curr. Opin. Virol. 2:719-724.
    • (2012) Curr. Opin. Virol. , vol.2 , pp. 719-724
    • Elena, S.F.1    Rodrigo, G.2
  • 31
    • 0015400527 scopus 로고
    • Ultrastructure of sugarbeet leaves infected with Beet western yellows virus
    • Esau, K., and Hoefert, L. L. 1972. Ultrastructure of sugarbeet leaves infected with Beet western yellows virus. J. Ultrastruct. Res. 40:556-571.
    • (1972) J. Ultrastruct. Res. , vol.40 , pp. 556-571
    • Esau, K.1    Hoefert, L.L.2
  • 32
    • 0028135705 scopus 로고
    • In vivo expression and mutational analysis of the Barley yellow dwarf virus readthrough gene
    • Filichkin, S. A., Lister, R. M., McGrath, P. F., and Young, M. J. 1994. In vivo expression and mutational analysis of the Barley yellow dwarf virus readthrough gene. Virology 205:290-299.
    • (1994) Virology , vol.205 , pp. 290-299
    • Filichkin, S.A.1    Lister, R.M.2    McGrath, P.F.3    Young, M.J.4
  • 34
    • 84903723588 scopus 로고    scopus 로고
    • Getting to the edge: Protein dynamical networks as a new frontier in plant-microbe interactions
    • Garbutt, C. C., Bangalore, P. V., Kannar, P., and Mukhtar, M. S. 2014. Getting to the edge: Protein dynamical networks as a new frontier in plant-microbe interactions. Front. Plant Sci. 5:312.
    • (2014) Front. Plant Sci. , vol.5 , pp. 312
    • Garbutt, C.C.1    Bangalore, P.V.2    Kannar, P.3    Mukhtar, M.S.4
  • 35
    • 0000632047 scopus 로고
    • Ultrastructural studies on potato phloem cells infected with Potato leafroll virus-comparison of two potato varieties
    • Golinowski, W., Tomenius, K., and Oxelfelt, P. 1987. Ultrastructural studies on potato phloem cells infected with Potato leafroll virus-comparison of two potato varieties. Acta. Agric. Scand. 37:3-19.
    • (1987) Acta. Agric. Scand. , vol.37 , pp. 3-19
    • Golinowski, W.1    Tomenius, K.2    Oxelfelt, P.3
  • 36
    • 84876425407 scopus 로고    scopus 로고
    • Host endomembrane recruitment for plant RNA virus replication
    • Grangeon, R., Jiang, J., and Laliberté, J. F. 2012. Host endomembrane recruitment for plant RNA virus replication. Curr. Opin. Virol. 2:683-690.
    • (2012) Curr. Opin. Virol. , vol.2 , pp. 683-690
    • Grangeon, R.1    Jiang, J.2    Laliberté, J.F.3
  • 37
  • 38
    • 84898917856 scopus 로고    scopus 로고
    • Circulative, "nonpropagative" virus transmission: An orchestra of virus-, insect-, and plant-derived instruments
    • Gray, S., Cilia, M., and Ghanim, M. 2014. Circulative, "nonpropagative" virus transmission: An orchestra of virus-, insect-, and plant-derived instruments. Adv. Virus Res. 89:141-199.
    • (2014) Adv. Virus Res. , vol.89 , pp. 141-199
    • Gray, S.1    Cilia, M.2    Ghanim, M.3
  • 39
    • 84876431861 scopus 로고    scopus 로고
    • Coat proteins, host factors and plant viral replication
    • Ivanov, K. I., and Mäkinen, K. 2012. Coat proteins, host factors and plant viral replication. Curr. Opin. Virol. 2:712-718.
    • (2012) Curr. Opin. Virol. , vol.2 , pp. 712-718
    • Ivanov, K.I.1    Mäkinen, K.2
  • 41
    • 7644221574 scopus 로고    scopus 로고
    • Volatile cues influence the response of Rhopalosiphum padi (Homoptera: Aphididae) to Barley yellow dwarf virus-infected transgenic and untransformed Wheat
    • Jiménez-Martínez, E. S., Bosque-Pérez, S. A., Berger, P. H., Zemetrad, R. S., Ding, H., and Eigenbrode, S. D. 2004. Volatile cues influence the response of Rhopalosiphum padi (Homoptera: Aphididae) to Barley yellow dwarf virus-infected transgenic and untransformed Wheat. Environ. Entomol. 33:1207-1216.
    • (2004) Environ. Entomol. , vol.33 , pp. 1207-1216
    • Jiménez-Martínez, E.S.1    Bosque-Pérez, S.A.2    Berger, P.H.3    Zemetrad, R.S.4    Ding, H.5    Eigenbrode, S.D.6
  • 42
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • Jones, J. D., and Dangl, J. L. 2006. The plant immune system. Nature 444:323-329.
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.1    Dangl, J.L.2
  • 43
    • 35748972060 scopus 로고    scopus 로고
    • Semi-supervised learning for peptide identification from shotgun proteomics datasets
    • Käll, L., Canterbury, J. D., Weston, J., Noble, W. S., and MacCoss, M. J. 2007. Semi-supervised learning for peptide identification from shotgun proteomics datasets. Nat. Methods 4:923-925.
    • (2007) Nat. Methods , vol.4 , pp. 923-925
    • Käll, L.1    Canterbury, J.D.2    Weston, J.3    Noble, W.S.4    MacCoss, M.J.5
  • 44
    • 0033982936 scopus 로고    scopus 로고
    • KEGG: Kyoto encyclopedia of genes and genomes
    • Kanehisa, M., and Goto, H. 2000. KEGG: Kyoto Encyclopedia of Genes and Genomes. Nucleic Acids Res. 28:27-30.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 27-30
    • Kanehisa, M.1    Goto, H.2
  • 46
    • 34249802894 scopus 로고    scopus 로고
    • Point mutations in the potato leafroll virus major capsid protein alter virion stability and aphid transmission
    • Kaplan, I. B., Lee, L., Ripoll, D. R., Palukaitis, P., Gildow, F., and Gray, S. M. 2007. Point mutations in the potato leafroll virus major capsid protein alter virion stability and aphid transmission. J. Gen. Virol. 88:1821-1830.
    • (2007) J. Gen. Virol. , vol.88 , pp. 1821-1830
    • Kaplan, I.B.1    Lee, L.2    Ripoll, D.R.3    Palukaitis, P.4    Gildow, F.5    Gray, S.M.6
  • 47
    • 54949129419 scopus 로고    scopus 로고
    • ProteoWizard: Open source software for rapid proteomics tools development
    • Kessner, D., Chambers, M., Burke, R., Agus, D., and Mallick, P. 2008. ProteoWizard: Open source software for rapid proteomics tools development. Bioinformatics 24:2534-2536.
    • (2008) Bioinformatics , vol.24 , pp. 2534-2536
    • Kessner, D.1    Chambers, M.2    Burke, R.3    Agus, D.4    Mallick, P.5
  • 49
    • 11144248920 scopus 로고    scopus 로고
    • A surface loop of the Potato leafroll virus coat protein is involved in virion assembly, systemic movement, and aphid transmission
    • Lee, L., Kaplan, I. B., Ripoll, D. R., Liang, D., Palukaitis, P., and Gray, S. M. 2005. A surface loop of the Potato leafroll virus coat protein is involved in virion assembly, systemic movement, and aphid transmission. J. Virol. 79:1207-1214.
    • (2005) J. Virol. , vol.79 , pp. 1207-1214
    • Lee, L.1    Kaplan, I.B.2    Ripoll, D.R.3    Liang, D.4    Palukaitis, P.5    Gray, S.M.6
  • 50
    • 84886750395 scopus 로고    scopus 로고
    • The cell biology of Tobacco mosaic virus replication and movement
    • Liu, C., and Nelson, R. S. 2013. The cell biology of Tobacco mosaic virus replication and movement. Front. Plant Sci. 4:12.
    • (2013) Front. Plant Sci. , vol.4 , pp. 12
    • Liu, C.1    Nelson, R.S.2
  • 51
    • 79961043839 scopus 로고    scopus 로고
    • Comparative morphology and phylogeny of Nicotiana section Suaveolentes (Solanaceae) in Australia and the South Pacific
    • Marks, C. E., Newbigin, E., and Ladiges, P. Y. 2011. Comparative morphology and phylogeny of Nicotiana section Suaveolentes (Solanaceae) in Australia and the South Pacific. Aust. Syst. Bot. 24:61-86.
    • (2011) Aust. Syst. Bot. , vol.24 , pp. 61-86
    • Marks, C.E.1    Newbigin, E.2    Ladiges, P.Y.3
  • 52
    • 84901041535 scopus 로고    scopus 로고
    • RNA-directed DNA methylation: An epigenetic pathway of increasing complexity
    • Matzke, M. A., and Mosher, R. A. 2014. RNA-directed DNA methylation: An epigenetic pathway of increasing complexity. Nat. Rev. Genet. 15:394-408.
    • (2014) Nat. Rev. Genet. , vol.15 , pp. 394-408
    • Matzke, M.A.1    Mosher, R.A.2
  • 53
    • 77649250252 scopus 로고    scopus 로고
    • Deceptive chemical signals induced by a plant virus attract insect vectors to inferior hosts
    • Mauck, K. E., De Moraes, C. M., and Mescher, M. C. 2010. Deceptive chemical signals induced by a plant virus attract insect vectors to inferior hosts. Proc. Natl. Acad. Sci. U. S. A. 107:3600-3605.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 3600-3605
    • Mauck, K.E.1    De Moraes, C.M.2    Mescher, M.C.3
  • 54
    • 0036017852 scopus 로고    scopus 로고
    • The dialogue between viruses and hosts in compatible interactions
    • Maule, A., Leh, V., and Lederer, C. 2002. The dialogue between viruses and hosts in compatible interactions. Curr. Opin. Plant Biol. 5:279-284.
    • (2002) Curr. Opin. Plant Biol. , vol.5 , pp. 279-284
    • Maule, A.1    Leh, V.2    Lederer, C.3
  • 56
    • 84872524590 scopus 로고    scopus 로고
    • Proteomics-based methods for discovery, quantification, and validation of protein-protein interactions
    • Miteva, Y. V., Budayeva, H. G., and Cristea, I. M. 2013. Proteomics-based methods for discovery, quantification, and validation of protein-protein interactions. Anal. Chem. 85:749-768.
    • (2013) Anal. Chem. , vol.85 , pp. 749-768
    • Miteva, Y.V.1    Budayeva, H.G.2    Cristea, I.M.3
  • 57
    • 84926255482 scopus 로고    scopus 로고
    • Interactome analysis of AMP-activated protein kinase (AMPK)-a1 and -b1 in INS-1 pancreatic beta-cells by affinity purification-mass spectrometry
    • Moon, S., Han, D., Kim, Y., Jin, J., Ho, W. K., and Kim, Y. 2014. Interactome analysis of AMP-activated protein kinase (AMPK)-a1 and -b1 in INS-1 pancreatic beta-cells by affinity purification-mass spectrometry. Sci. Rep. 4:4376.
    • (2014) Sci. Rep. , vol.4 , pp. 4376
    • Moon, S.1    Han, D.2    Kim, Y.3    Jin, J.4    Ho, W.K.5    Kim, Y.6
  • 59
    • 51849139963 scopus 로고    scopus 로고
    • Yeast as a model host to explore plant virus-host interactions
    • Nagy, P. D. 2008. Yeast as a model host to explore plant virus-host interactions. Annu. Rev. Phytopathol. 46:217-242.
    • (2008) Annu. Rev. Phytopathol. , vol.46 , pp. 217-242
    • Nagy, P.D.1
  • 60
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A. I., Keller, A., Kolker, E., and Aebersold, R. 2003. A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 75:4646-4658.
    • (2003) Anal. Chem. , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 61
    • 84878702840 scopus 로고    scopus 로고
    • Regulation of protein-protein binding by coupling between phosphorylation and intrinsic disorder: Analysis of human protein complexes
    • Nishi, H., Fong, J. H., Chang, C., Teichmann, S. A., and Panchenko, A. R. 2013. Regulation of protein-protein binding by coupling between phosphorylation and intrinsic disorder: Analysis of human protein complexes. Mol. Biosyst. 9:1620-1626.
    • (2013) Mol. Biosyst. , vol.9 , pp. 1620-1626
    • Nishi, H.1    Fong, J.H.2    Chang, C.3    Teichmann, S.A.4    Panchenko, A.R.5
  • 62
    • 79954600120 scopus 로고    scopus 로고
    • Tomato 14-3-3 protein TFT7 interacts with a MAP kinase kinase to regulate immunity-associated programmed cell death mediated by diverse disease resistance proteins
    • Oh, C. S., and Martin, G. B. 2011. Tomato 14-3-3 protein TFT7 interacts with a MAP kinase kinase to regulate immunity-associated programmed cell death mediated by diverse disease resistance proteins. J. Biol. Chem. 286:14129-14136.
    • (2011) J. Biol. Chem. , vol.286 , pp. 14129-14136
    • Oh, C.S.1    Martin, G.B.2
  • 63
    • 84907958781 scopus 로고    scopus 로고
    • Phosphoproteomics combined with quantitative 14-3-3-affinity capture identifies SIRT1 and RAI as novel regulators of cytosolic doublestranded RNA recognition pathway
    • Ohman, T., Söderholm, S., Hintsanen, P., Välimäki, E., Lietzén, N., MacKintosh, C., Aittokallio, T., Matikainen, S., and Nyman, T. A. 2014. Phosphoproteomics combined with quantitative 14-3-3-affinity capture identifies SIRT1 and RAI as novel regulators of cytosolic doublestranded RNA recognition pathway. Mol. Cell. Proteomics 13:2604-2617.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 2604-2617
    • Ohman, T.1    Söderholm, S.2    Hintsanen, P.3    Välimäki, E.4    Lietzén, N.5    MacKintosh, C.6    Aittokallio, T.7    Matikainen, S.8    Nyman, T.A.9
  • 65
    • 81255143126 scopus 로고    scopus 로고
    • How do plant viruses induce disease? Interactions and interference with host components
    • Pallas, V., and García, J. A. 2011. How do plant viruses induce disease? Interactions and interference with host components. J. Gen. Virol. 92:2691-2705.
    • (2011) J. Gen. Virol. , vol.92 , pp. 2691-2705
    • Pallas, V.1    García, J.A.2
  • 66
    • 84878582473 scopus 로고    scopus 로고
    • Hijack it, change it: How do plant viruses utilize the host secretory pathway for efficient viral replication and spread?
    • Patarroyo, C., Laliberté, J. F., and Zheng, H. 2012. Hijack it, change it: how do plant viruses utilize the host secretory pathway for efficient viral replication and spread? Front. Plant Sci. 3:308.
    • (2012) Front. Plant Sci. , vol.3 , pp. 308
    • Patarroyo, C.1    Laliberté, J.F.2    Zheng, H.3
  • 67
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. 1999. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 69
    • 50549094568 scopus 로고    scopus 로고
    • Small deletions in the potato leafroll virus readthrough protein affect particle morphology, aphid transmission, virus movement and accumulation
    • Peter, K. A., Liang, D., Palukaitis, P., and Gray, S. M. 2008. Small deletions in the potato leafroll virus readthrough protein affect particle morphology, aphid transmission, virus movement and accumulation. J. Gen. Virol. 89:2037-2045.
    • (2008) J. Gen. Virol. , vol.89 , pp. 2037-2045
    • Peter, K.A.1    Liang, D.2    Palukaitis, P.3    Gray, S.M.4
  • 70
    • 66149150254 scopus 로고    scopus 로고
    • The C terminus of the polerovirus p5 readthrough domain limits virus infection to the phloem
    • Peter, K. A., Gildow, F., Palukaitis, P., and Gray, S. M. 2009. The C terminus of the polerovirus p5 readthrough domain limits virus infection to the phloem. J. Virol. 83:5419-5429.
    • (2009) J. Virol. , vol.83 , pp. 5419-5429
    • Peter, K.A.1    Gildow, F.2    Palukaitis, P.3    Gray, S.M.4
  • 73
    • 0042233291 scopus 로고    scopus 로고
    • Virus specificity in disease systems: Are species redundant?
    • P. Kareiva and S. A. Levin, eds. Princeton University Press, Princeton, NJ, U. S. A.
    • Power, A. G., and Flecker, A. S. 2003. Virus specificity in disease systems: Are species redundant? Pages 330-334 in: The Importance of Species: Perspectives on Expendability and Triage. P. Kareiva and S. A. Levin, eds. Princeton University Press, Princeton, NJ, U. S. A.
    • (2003) The Importance of Species: Perspectives on Expendability and Triage , pp. 330-334
    • Power, A.G.1    Flecker, A.S.2
  • 74
    • 84887879790 scopus 로고    scopus 로고
    • RNA silencing suppression by plant pathogens: Defence, counter-defence and counter-counter-defence
    • Pumplin, N., and Voinnet, O. 2013. RNA silencing suppression by plant pathogens: Defence, counter-defence and counter-counter-defence. Nat. Rev. Microbiol. 11:745-760.
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 745-760
    • Pumplin, N.1    Voinnet, O.2
  • 76
    • 78650153662 scopus 로고    scopus 로고
    • Pathogen-mediated posttranslational modifications: A re-emerging field
    • Ribet, D., and Cossart, P. 2010. Pathogen-mediated posttranslational modifications: A re-emerging field. Cell 143:694-702.
    • (2010) Cell , vol.143 , pp. 694-702
    • Ribet, D.1    Cossart, P.2
  • 77
    • 0026573174 scopus 로고
    • Highlights and prospects of potyvirus molecular biology
    • Riechmann, J. L., Laín, S., and García, J. A. 1992. Highlights and prospects of potyvirus molecular biology. J. Gen. Virol. 73:1-16.
    • (1992) J. Gen. Virol. , vol.73 , pp. 1-16
    • Riechmann, J.L.1    Laín, S.2    García, J.A.3
  • 78
    • 27644475955 scopus 로고    scopus 로고
    • The Arabidopsis HOMOLOGY-DEPENDENT GENE SILENCING1 gene codes for an S-adenosyl-L-homocysteine hydrolase required for DNA methylation-dependent gene silencing
    • Rocha, P. S., Sheikh, M., Melchiorre, R., Fagard, M., Boutet, S., Loach, R., Moffatt, B., Wagner, C., Vaucheret, H., and Furner, I. 2005. The Arabidopsis HOMOLOGY-DEPENDENT GENE SILENCING1 gene codes for an S-adenosyl-L-homocysteine hydrolase required for DNA methylation-dependent gene silencing. Plant Cell 17:404-417.
    • (2005) Plant Cell , vol.17 , pp. 404-417
    • Rocha, P.S.1    Sheikh, M.2    Melchiorre, R.3    Fagard, M.4    Boutet, S.5    Loach, R.6    Moffatt, B.7    Wagner, C.8    Vaucheret, H.9    Furner, I.10
  • 79
    • 84863732942 scopus 로고    scopus 로고
    • A meta-analysis reveals the commonalities and differences in Arabidopsis thaliana response to different viral pathogens
    • Rodrigo, G., Carrera, J., Ruiz-Ferrer, V., Del Toro, F. J., Llave, C., Voinnet, O., and Elena, S. F. 2012. A meta-analysis reveals the commonalities and differences in Arabidopsis thaliana response to different viral pathogens. PLoS One 7:e40526.
    • (2012) PLoS One , vol.7 , pp. e40526
    • Rodrigo, G.1    Carrera, J.2    Ruiz-Ferrer, V.3    Del Toro, F.J.4    Llave, C.5    Voinnet, O.6    Elena, S.F.7
  • 80
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C. A., Rasband, W. S., and Eliceiri, K. W. 2012. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods 9:671-675.
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 81
    • 80053463385 scopus 로고    scopus 로고
    • Intracellular transport of plant viruses: Finding the door out of the cell
    • Schoelz, J. E., Harries, P. A., and Nelson, R. S. 2011. Intracellular transport of plant viruses: Finding the door out of the cell. Mol. Plant 4:813-831.
    • (2011) Mol. Plant , vol.4 , pp. 813-831
    • Schoelz, J.E.1    Harries, P.A.2    Nelson, R.S.3
  • 82
    • 0018942564 scopus 로고
    • Ultrastructure of potato leaf phloem infected with potato leafroll virus
    • Shepardson, S., Esau, K., and McCrum, R. 1980. Ultrastructure of potato leaf phloem infected with potato leafroll virus. Virology 105:379-392.
    • (1980) Virology , vol.105 , pp. 379-392
    • Shepardson, S.1    Esau, K.2    McCrum, R.3
  • 83
    • 79953713220 scopus 로고    scopus 로고
    • Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5
    • Skarra, D. V., Goudreault, M., Choi, H., Mullin, M., Nesvizhskii, A. I., Gingras, A. C., and Honkanen, R. E. 2011. Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5. Proteomics 11:1508-1516.
    • (2011) Proteomics , vol.11 , pp. 1508-1516
    • Skarra, D.V.1    Goudreault, M.2    Choi, H.3    Mullin, M.4    Nesvizhskii, A.I.5    Gingras, A.C.6    Honkanen, R.E.7
  • 85
    • 79551587720 scopus 로고    scopus 로고
    • Cytoscape 2.8: New features for data integration and network visualization
    • Smoot, M. E., Ono, K., Ruscheinski, J., Wang, P. L., and Ideker, T. 2011. Cytoscape 2.8: New features for data integration and network visualization. Bioinformatics 27:431-432.
    • (2011) Bioinformatics , vol.27 , pp. 431-432
    • Smoot, M.E.1    Ono, K.2    Ruscheinski, J.3    Wang, P.L.4    Ideker, T.5
  • 87
    • 84886533144 scopus 로고    scopus 로고
    • Viroids and phloem-limited viruses: Unique molecular probes of phloem biology
    • G. A. Thompson and A. J. E. van Bel, eds. Wiley-Blackwell, Hoboken, NJ, U. S. A
    • Stewart, L. R., Ding, B., and Falk, B. W. 2013. Viroids and phloem-limited viruses: Unique molecular probes of phloem biology. In: Phloem: Molecular Cell Biology, Systemic Communication, Biotic Interactions. G. A. Thompson and A. J. E. van Bel, eds. Wiley-Blackwell, Hoboken, NJ, U. S. A.
    • (2013) Phloem: Molecular Cell Biology, Systemic Communication, Biotic Interactions
    • Stewart, L.R.1    Ding, B.2    Falk, B.W.3
  • 89
    • 84876544295 scopus 로고    scopus 로고
    • SUBA3: A database for integrating experimentation and prediction to define the SUBcellular location of proteins in Arabidopsis
    • Tanz, S. K., Castleden, I., Hooper, C. M., Vacher, M., Small, I., and Millar, H. A. 2013. SUBA3: A database for integrating experimentation and prediction to define the SUBcellular location of proteins in Arabidopsis. Nucleic Acids Res. 41:D1185-D1191.
    • (2013) Nucleic Acids Res. , vol.41 , pp. D1185-D1191
    • Tanz, S.K.1    Castleden, I.2    Hooper, C.M.3    Vacher, M.4    Small, I.5    Millar, H.A.6
  • 90
    • 0026794418 scopus 로고
    • Analysis of epitopes on potato leafroll virus capsid protein
    • Torrance, L. 1992. Analysis of epitopes on potato leafroll virus capsid protein. Virology 191:485-489.
    • (1992) Virology , vol.191 , pp. 485-489
    • Torrance, L.1
  • 91
    • 84897711870 scopus 로고    scopus 로고
    • Protein intrinsic disorder and network connectivity. The case of 14-3-3 proteins
    • Uhart, M., and Bustos, D. M. 2014. Protein intrinsic disorder and network connectivity. The case of 14-3-3 proteins. Front. Genet. 5:10.
    • (2014) Front. Genet. , vol.5 , pp. 10
    • Uhart, M.1    Bustos, D.M.2
  • 92
    • 84891783174 scopus 로고    scopus 로고
    • Activities at the Universal Protein Resource (UniProt)
    • UniProt Consortium. 2014. Activities at the Universal Protein Resource (UniProt). Nucleic Acids Res. 42:D191-D198.
    • (2014) Nucleic Acids Res. , vol.42 , pp. D191-D198
    • UniProt Consortium1
  • 93
    • 0028985008 scopus 로고
    • Readthrough protein associated with virions of barley yellow dwarf luteovirus and its potential role in regulating the efficiency of aphid transmission
    • Wang, J. Y., Chay, C., Gildow, F. E., and Gray, S. M. 1995. Readthrough protein associated with virions of barley yellow dwarf luteovirus and its potential role in regulating the efficiency of aphid transmission. Virology 206:954-962.
    • (1995) Virology , vol.206 , pp. 954-962
    • Wang, J.Y.1    Chay, C.2    Gildow, F.E.3    Gray, S.M.4
  • 94
    • 33750209744 scopus 로고    scopus 로고
    • Global impact: Elucidating plant responses to viral infection
    • Whitham, S. A., Yang, C., and Goodin, M. M. 2006. Global impact: Elucidating plant responses to viral infection. Mol. Plant-Microbe Interact. 19:1207-1215.
    • (2006) Mol. Plant-Microbe Interact. , vol.19 , pp. 1207-1215
    • Whitham, S.A.1    Yang, C.2    Goodin, M.M.3
  • 95
    • 0034057586 scopus 로고    scopus 로고
    • Functional analysis of HD2 histone deacetylase homologues in Arabidopsis thaliana
    • Wu, K., Tian, L., Malik, K., Brown, D., and Miki, B. 2000. Functional analysis of HD2 histone deacetylase homologues in Arabidopsis thaliana. Plant J. 22:19-27.
    • (2000) Plant J. , vol.22 , pp. 19-27
    • Wu, K.1    Tian, L.2    Malik, K.3    Brown, D.4    Miki, B.5
  • 96
    • 0028842296 scopus 로고
    • The remarkable variety of plant RNA virus genomes
    • Zaccomer, B., Haenni, A. L., and Macaya, G. 1995. The remarkable variety of plant RNA virus genomes. J. Gen. Virol. 76:231-247.
    • (1995) J. Gen. Virol. , vol.76 , pp. 231-247
    • Zaccomer, B.1    Haenni, A.L.2    Macaya, G.3


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