메뉴 건너뛰기




Volumn 7, Issue 4, 2010, Pages 275-297

Plant biotic stress and proteomics

Author keywords

2DE gel electrophoresis; Biotic stress; Proteomics; Technical developments

Indexed keywords


EID: 79952791695     PISSN: 15701646     EISSN: None     Source Type: Journal    
DOI: 10.2174/157016410793611765     Document Type: Review
Times cited : (20)

References (239)
  • 1
    • 0027943082 scopus 로고
    • Four hundred-million-year-old vesicular arbuscular mycorrhizae
    • Remy, W.; Taylor, T.N.; Hass, H. and Kerp, H. Four hundred-million-year-old vesicular arbuscular mycorrhizae. Proc. Natl. Acad. Sci. USA, 1994, 91(25), 11841-11843.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.25 , pp. 11841-11843
    • Remy, W.1    Taylor, T.N.2    Hass, H.3    Kerp, H.4
  • 2
    • 0031851166 scopus 로고    scopus 로고
    • The stress concept in plants: An introduction
    • Lichtenthaler, H.K. The stress concept in plants: an introduction. Ann. N. Y. Acad. Sci., 1998, 851, 187-198.
    • (1998) Ann. N. Y. Acad. Sci , vol.851 , pp. 187-198
    • Lichtenthaler, H.K.1
  • 3
    • 84879891163 scopus 로고    scopus 로고
    • Social vulnerability and ecological fragility: Building bridges between social and natural sciences using the Irish Potato Famine as a case study
    • Fraser, E.D.G. Social vulnerability and ecological fragility: building bridges between social and natural sciences using the Irish Potato Famine as a case study. Conserv. Ecol., 2003, 7(2), 9.
    • (2003) Conserv. Ecol , vol.7 , Issue.2 , pp. 9
    • Fraser, E.D.G.1
  • 4
    • 0032478185 scopus 로고    scopus 로고
    • Multiple evolutionary origins of the fungus causing Panama disease of banana: Concordant evidence from nuclear and mitochondrial gene genealogies
    • O'Donnell, K.; Kistler, H.C.; Cigelnik, E. and Ploetz, R.C. Multiple evolutionary origins of the fungus causing Panama disease of banana: concordant evidence from nuclear and mitochondrial gene genealogies. Proc. Natl. Acad. Sci. USA, 1998, 95(5), 2044-2049.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.5 , pp. 2044-2049
    • O'Donnell, K.1    Kistler, H.C.2    Cigelnik, E.3    Ploetz, R.C.4
  • 5
    • 0002583077 scopus 로고    scopus 로고
    • High level of chestnut blight control on grafted American chestnut trees inoculated with hypovirulent strains
    • Dierauf, T.F.; Artman, J.; Elkins, J.R.; Griffin, S.L. and Griffin, G.J. High level of chestnut blight control on grafted American chestnut trees inoculated with hypovirulent strains. J. Arboric, 1997, 23(3), 87-88.
    • (1997) J. Arboric , vol.23 , Issue.3 , pp. 87-88
    • Dierauf, T.F.1    Artman, J.2    Elkins, J.R.3    Griffin, S.L.4    Griffin, G.J.5
  • 6
    • 0002685286 scopus 로고
    • China and the origins of Dutch elm disease: An appraisal
    • Brasier, C.M. China and the origins of Dutch elm disease: an appraisal. Plant Pathol., 1990, 39(1), 5-16.
    • (1990) Plant Pathol , vol.39 , Issue.1 , pp. 5-16
    • Brasier, C.M.1
  • 7
    • 51849148001 scopus 로고    scopus 로고
    • Breaking the barriers: Microbial effec tor molecules subvert plant immunity
    • Gohre, V. and Robatzek, S. Breaking the barriers: microbial effec tor molecules subvert plant immunity. Annu. Rev. Phytopathol., 2008, 46, 189-215.
    • (2008) Annu. Rev. Phytopathol , vol.46 , pp. 189-215
    • Gohre, V.1    Robatzek, S.2
  • 8
    • 38549125550 scopus 로고    scopus 로고
    • How plants recognize pathogens and defend themselves
    • de Wit, P.J. How plants recognize pathogens and defend themselves. Cell Mol. Life Sci., 2007, 64(21), 2726-2732.
    • (2007) Cell Mol. Life Sci , vol.64 , Issue.21 , pp. 2726-2732
    • Wit, P.J.D.1
  • 9
    • 0035859020 scopus 로고    scopus 로고
    • Plant pathogens and integrated responses to infection
    • Dangl, J.L. and Jones, J.D. Plant pathogens and integrated responses to infection. Nature, 2001, 411(6839), 826-833.
    • (2001) Nature , vol.411 , Issue.6839 , pp. 826-833
    • Dangl, J.L.1    Jones, J.D.2
  • 10
    • 0002887787 scopus 로고    scopus 로고
    • Responses to plant pathogens
    • Buchanan B, Gruissen W, Jones R, Eds. Rockville. MD: ASPP
    • Jones, J. and Hammond-Kosack, K. Responses to plant pathogens. In Biochemistry and molecular biology of plants, Buchanan B, Gruissen W, Jones R, Eds. Rockville. MD: ASPP, 2000, pp. 1102-1157.
    • (2000) Biochemistry and Molecular Biology of Plants , pp. 1102-1157
    • Jones, J.1    Hammond-Kosack, K.2
  • 11
    • 0032422882 scopus 로고    scopus 로고
    • Plant disease-resistance proteins and the gene-for-gene concept
    • Van der Biezen, E.A. and Jones, J.D. Plant disease-resistance proteins and the gene-for-gene concept. Trends Biochem Sci., 1998, 23(12), 454-456.
    • (1998) Trends Biochem Sci , vol.23 , Issue.12 , pp. 454-456
    • Biezen, E.A.V.D.1    Jones, J.D.2
  • 12
    • 42249104880 scopus 로고    scopus 로고
    • Self/nonself perception and recognition mechanisms in plants: A comparison of self-incompatibility and innate immunity
    • Sanabria, N.; Goring, D.; Nurnberger, T. and Dubery, I. Self/nonself perception and recognition mechanisms in plants: a comparison of self-incompatibility and innate immunity. New Phy-tol., 2008, 178(3), 503-514.
    • (2008) New Phy-tol , vol.178 , Issue.3 , pp. 503-514
    • Sanabria, N.1    Goring, D.2    Nurnberger, T.3    Dubery, I.4
  • 13
    • 70449509972 scopus 로고    scopus 로고
    • Plant systems for recognition of pathogen-associated molecular patterns
    • Postel, S. and Kemmerling, B. Plant systems for recognition of pathogen-associated molecular patterns. Semin. Cell Dev. Biol., 2009, s20(9), 1025-1031.
    • (2009) Semin. Cell Dev. Biol , vol.20 , Issue.9 , pp. 1025-1031
    • Postel, S.1    Kemmerling, B.2
  • 14
    • 64849103801 scopus 로고    scopus 로고
    • The multilevel and dynamic interplay between plant and pathogen
    • Hou, S.; Yang, Y. and Zhou, J.M. The multilevel and dynamic interplay between plant and pathogen. Plant Signal Behav., 2009, 4(4), 283-293.
    • (2009) Plant Signal Behav , vol.4 , Issue.4 , pp. 283-293
    • Hou, S.1    Yang, Y.2    Zhou, J.M.3
  • 15
    • 64749114678 scopus 로고    scopus 로고
    • Population genetics of fungal and oomycete effectors involved in gene-for-gene interactions
    • Stukenbrock, E.H. and McDonald, B.A. Population genetics of fungal and oomycete effectors involved in gene-for-gene interactions. Mol. Plant Microbe Interact., 2009, 22(4), 371-380.
    • (2009) Mol. Plant Microbe Interact , vol.22 , Issue.4 , pp. 371-380
    • Stukenbrock, E.H.1    McDonald, B.A.2
  • 16
    • 70349493149 scopus 로고    scopus 로고
    • Quantitative fitness effects of infection in a gene-for-gene system
    • Gao, L.; Roux, F. and Bergelson, J. Quantitative fitness effects of infection in a gene-for-gene system. New Phytol., 2009, 184(2), 485-494.
    • (2009) New Phytol , vol.184 , Issue.2 , pp. 485-494
    • Gao, L.1    Roux, F.2    Bergelson, J.3
  • 17
    • 34250897234 scopus 로고    scopus 로고
    • Ubiquitin, hormones and biotic stress in plants
    • Dreher, K. and Callis, J. Ubiquitin, hormones and biotic stress in plants. Ann. Bot., 2007, 99(5), 787-822.
    • (2007) Ann. Bot , vol.99 , Issue.5 , pp. 787-822
    • Dreher, K.1    Callis, J.2
  • 18
    • 0034484977 scopus 로고    scopus 로고
    • Hypersensitive response-related death
    • Heath, M.C. Hypersensitive response-related death. Plant Mol. Biol., 2000, 44(3), 321-334.
    • (2000) Plant Mol. Biol , vol.44 , Issue.3 , pp. 321-334
    • Heath, M.C.1
  • 20
    • 8444241218 scopus 로고    scopus 로고
    • Systemic acquired resistance and induced systemic resistance in conventional agriculture
    • Vallad, G.E. and Goodman, R.M. Systemic acquired resistance and induced systemic resistance in conventional agriculture. Crop Sci., 2004, 44(4), 1920-1934.
    • (2004) Crop Sci , vol.44 , Issue.4 , pp. 1920-1934
    • Vallad, G.E.1    Goodman, R.M.2
  • 21
    • 50549158514 scopus 로고
    • Localized acquired resistance to plant virus infection in hypersensitive hosts
    • Ross A.F. Localized acquired resistance to plant virus infection in hypersensitive hosts. Virology, 1961, 14, 329-339.
    • (1961) Virology , vol.14 , pp. 329-339
    • Ross, A.F.1
  • 22
    • 51649140828 scopus 로고
    • Recommendations for naming plant pathogenesis-related proteins
    • van Loon, L.C.; Pierpoint, W.S.; Boller T. and Conejero, V. Recommendations for naming plant pathogenesis-related proteins. Plant Mol. Biol. Rep., 1994, 12(3), 245-264.
    • (1994) Plant Mol. Biol. Rep , vol.12 , Issue.3 , pp. 245-264
    • van Loon, L.C.1    Pierpoint, W.S.2    Boller, T.3    Conejero, V.4
  • 23
    • 33845250983 scopus 로고    scopus 로고
    • Pathogenesis-related proteins: Research progress in the last 15 years
    • Edreva, A. Pathogenesis-related proteins: research progress in the last 15 years. Gen. Appl. Plant Physiology, 2005, 31(1-2), 105-124.
    • (2005) Gen. Appl. Plant Physiology , vol.31 , Issue.1-2 , pp. 105-124
    • Edreva, A.1
  • 24
    • 0033179482 scopus 로고    scopus 로고
    • The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins
    • van Loon, L.C. and van Strien, E.A. The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins. Phys. Mol. Plant Pathol., 1999, 55(1), 85-97.
    • (1999) Phys. Mol. Plant Pathol , vol.55 , Issue.1 , pp. 85-97
    • van Loon, L.C.1    van Strien, E.A.2
  • 25
    • 0029411516 scopus 로고
    • Antifreeze proteins in winter rye are similar to pathogenesis-related proteins
    • Hon, W.C.; Griffith, M.; Mlynarz, A.; Kwok, Y.C. and Yang, D.S. Antifreeze proteins in winter rye are similar to pathogenesis-related proteins. Plant Physiol., 1995, 109(3), 879-889.
    • (1995) Plant Physiol , vol.109 , Issue.3 , pp. 879-889
    • Hon, W.C.1    Griffith, M.2    Mlynarz, A.3    Kwok, Y.C.4    Yang, D.S.5
  • 26
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R. and Mann, M. Mass spectrometry-based proteomics. Nature, 2003, 422(6928), 198-207.
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 27
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.H. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem., 1975, 250(10), 4007-4021.
    • (1975) J. Biol. Chem , vol.250 , Issue.10 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 30
    • 33644896212 scopus 로고    scopus 로고
    • The role of mass spectrometry in plant systems biology
    • Glinski, M. and Weckwerth, W. The role of mass spectrometry in plant systems biology. Mass Spectrom Rev., 2006, 25(2), 173-214.
    • (2006) Mass Spectrom Rev , vol.25 , Issue.2 , pp. 173-214
    • Glinski, M.1    Weckwerth, W.2
  • 31
    • 0032200910 scopus 로고    scopus 로고
    • Functional genomics in plants
    • Bouchez, D. and Hofte, H. Functional genomics in plants. Plant Physiol., 1998, 118(3), 725-732.
    • (1998) Plant Physiol , vol.118 , Issue.3 , pp. 725-732
    • Bouchez, D.1    Hofte, H.2
  • 32
    • 75949116834 scopus 로고    scopus 로고
    • Gene expression analysis, proteomics, and network discovery
    • Baginsky, S.; Hennig, L.; Zimmermann, P. and Gruissem, W. Gene expression analysis, proteomics, and network discovery. Plant Physiol., 2010, 152(2), 402-410.
    • (2010) Plant Physiol , vol.152 , Issue.2 , pp. 402-410
    • Baginsky, S.1    Hennig, L.2    Zimmermann, P.3    Gruissem, W.4
  • 33
    • 0028806048 scopus 로고
    • Quantitative monitoring of gene expression patterns with a complementary DNA microarray
    • Schena, M.; Shalon, D.; Davis, R.W. and Brown, P.O. Quantitative monitoring of gene expression patterns with a complementary DNA microarray. Science, 1995, 270(5235), 467-470.
    • (1995) Science , vol.270 , Issue.5235 , pp. 467-470
    • Schena, M.1    Shalon, D.2    Davis, R.W.3    Brown, P.O.4
  • 34
    • 53649088131 scopus 로고    scopus 로고
    • Applications of next-generation sequencing technologies in functional genomics
    • Morozova, O. and Marra, M.A. Applications of next-generation sequencing technologies in functional genomics. Genomics, 2008, 92(5), 255-264.
    • (2008) Genomics , vol.92 , Issue.5 , pp. 255-264
    • Morozova, O.1    Marra, M.A.2
  • 35
    • 68949186256 scopus 로고    scopus 로고
    • Next-generation sequencing technologies and their implications for crop genetics and breeding
    • Varshney, R.K.; Nayak, S.N.; May, G.D. and Jackson S.A. Next-generation sequencing technologies and their implications for crop genetics and breeding. Trends Biotechnol., 2009, 27(9), 522-530.
    • (2009) Trends Biotechnol , vol.27 , Issue.9 , pp. 522-530
    • Varshney, R.K.1    Nayak, S.N.2    May, G.D.3    Jackson, S.A.4
  • 36
    • 52949096084 scopus 로고    scopus 로고
    • Next-generation DNA sequencing methods
    • Mardis, E.R. Next-generation DNA sequencing methods. Annu. Rev. Genomics Hum. Genet., 2008, 9, 387-402.
    • (2008) Annu. Rev. Genomics Hum. Genet , vol.9 , pp. 387-402
    • Mardis, E.R.1
  • 37
    • 72849144434 scopus 로고    scopus 로고
    • Sequencing technologies-the next generation
    • Metzker, M.L. Sequencing technologies-the next generation. Nat. Rev. Genet., 2010, 11(1), 31-46.
    • (2010) Nat. Rev. Genet , vol.11 , Issue.1 , pp. 31-46
    • Metzker, M.L.1
  • 40
    • 77952479671 scopus 로고    scopus 로고
    • Uncovering the evolutionary origin of plant molecular processes: Comparison of Coleochaete (Coleochaetales) and Spirogyra (Zygnematales) transcriptomes
    • Timme, R.E. and Delwiche, C.F. Uncovering the evolutionary origin of plant molecular processes: comparison of Coleochaete (Coleochaetales) and Spirogyra (Zygnematales) transcriptomes. BMC Plant Biol., 2010, 10, 96.
    • (2010) BMC Plant Biol , vol.10 , pp. 96
    • Timme, R.E.1    Delwiche, C.F.2
  • 41
    • 58249088751 scopus 로고    scopus 로고
    • MicroRNAs: Target recognition and regulatory functions
    • Bartel, D.P. MicroRNAs: target recognition and regulatory functions. Cell, 2009, 136(2), 215-233.
    • (2009) Cell , vol.136 , Issue.2 , pp. 215-233
    • Bartel, D.P.1
  • 42
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi, S.P.; Rochon, Y.; Franza, B.R. and Aebersold, R. Correlation between protein and mRNA abundance in yeast. Mol. Cell Biol., 1999, 19(3), 1720-1730.
    • (1999) Mol. Cell Biol , vol.19 , Issue.3 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 43
    • 0037353383 scopus 로고    scopus 로고
    • Mapping the proteome of barrel medic (Medicago truncatula)
    • Watson, B.S.; Asirvatham, V.S.; Wang, L. and Sumner, L.W. Mapping the proteome of barrel medic (Medicago truncatula). Plant Physiol., 2003, 131(3), 1104-1123.
    • (2003) Plant Physiol , vol.131 , Issue.3 , pp. 1104-1123
    • Watson, B.S.1    Asirvatham, V.S.2    Wang, L.3    Sumner, L.W.4
  • 44
    • 63349097597 scopus 로고    scopus 로고
    • Plant proteomics update (2007-2008): Second-generation proteomic techniques, an appropriate experimental design, and data analysis to fulfill MIAPE standards, increase plant proteome coverage and expand biological knowledge
    • Jorrin-Novo, J.V.; Maldonado, A.M.; Echevarria-Zomeno, S.; Valledor, L.; Castillejo, M.A.; Curto, M.; Valero, J.; Sghaier, B.; Donoso, G. and Redondo, I. Plant proteomics update (2007-2008): Second-generation proteomic techniques, an appropriate experimental design, and data analysis to fulfill MIAPE standards, increase plant proteome coverage and expand biological knowledge. J. Proteomics, 2009, 72(3), 285-314.
    • (2009) J. Proteomics , vol.72 , Issue.3 , pp. 285-314
    • Jorrin-Novo, J.V.1    Maldonado, A.M.2    Echevarria-Zomeno, S.3    Valledor, L.4    Castillejo, M.A.5    Curto, M.6    Valero, J.7    Sghaier, B.8    Donoso, G.9    Redondo, I.10
  • 47
    • 16844368869 scopus 로고    scopus 로고
    • A new method for C-terminal sequence analysis in the proteomic era
    • Samyn, B.; Sergeant, K.; Castanheira, P.; Faro, C. and Van Beeumen, J. A new method for C-terminal sequence analysis in the proteomic era. Nat. Methods, 2005, 2(3), 193-200.
    • (2005) Nat. Methods , vol.2 , Issue.3 , pp. 193-200
    • Samyn, B.1    Sergeant, K.2    Castanheira, P.3    Faro, C.4    van Beeumen, J.5
  • 48
    • 33646248895 scopus 로고    scopus 로고
    • Pro-teomics studies of post-translational modifications in plants
    • Kwon, S.J.; Choi, E.Y.; Choi, Y.J.; Ahn, J.H. and Park, O.K. Pro-teomics studies of post-translational modifications in plants. J. Exp Bot., 2006, 57(7), 1547-1551.
    • (2006) J. Exp Bot , vol.57 , Issue.7 , pp. 1547-1551
    • Kwon, S.J.1    Choi, E.Y.2    Choi, Y.J.3    Ahn, J.H.4    Park, O.K.5
  • 49
    • 19444366791 scopus 로고    scopus 로고
    • Techniques for studying protein heterogeneity and post-translational modifications
    • Baumann, M. and Meri, S. Techniques for studying protein heterogeneity and post-translational modifications. Expert Rev. Pro-teomics, 2004, 1(2), 207-217.
    • (2004) Expert Rev. Pro-teomics , vol.1 , Issue.2 , pp. 207-217
    • Baumann, M.1    Meri, S.2
  • 50
    • 4544265213 scopus 로고    scopus 로고
    • Tackling the plant proteome: Practical approaches, hurdles and experimental tools
    • Rose, J.K.; Bashir, S.; Giovannoni, J.J.; Jahn, M.M. and Saravanan, R.S. Tackling the plant proteome: practical approaches, hurdles and experimental tools. Plant J., 2004, 39(5), 715-733.
    • (2004) Plant J , vol.39 , Issue.5 , pp. 715-733
    • Rose, J.K.1    Bashir, S.2    Giovannoni, J.J.3    Jahn, M.M.4    Saravanan, R.S.5
  • 51
    • 4444237731 scopus 로고    scopus 로고
    • A critical evaluation of sample extraction techniques for enhanced proteomic analysis of recalcitrant plant tissues
    • Saravanan, R.S. and Rose, J.K. A critical evaluation of sample extraction techniques for enhanced proteomic analysis of recalcitrant plant tissues. Proteomics, 2004, 4(9), 2522-2532.
    • (2004) Proteomics , vol.4 , Issue.9 , pp. 2522-2532
    • Saravanan, R.S.1    Rose, J.K.2
  • 52
    • 22044456721 scopus 로고    scopus 로고
    • Preparation of protein extracts from recalcitrant plant tissues: An evaluation of different methods for two-dimensional gel electrophoresis analysis
    • Carpentier, S.C.; Witters, E.; Laukens, K.; Deckers, P.; Swennen, R. and Panis, B. Preparation of protein extracts from recalcitrant plant tissues: an evaluation of different methods for two-dimensional gel electrophoresis analysis. Proteomics, 2005, 5(10), 2497-2507.
    • (2005) Proteomics , vol.5 , Issue.10 , pp. 2497-2507
    • Carpentier, S.C.1    Witters, E.2    Laukens, K.3    Deckers, P.4    Swennen, R.5    Panis, B.6
  • 53
    • 3242755176 scopus 로고    scopus 로고
    • Plant proteome analysis by mass spectrometry: Principles, problems, pitfalls and recent developments
    • Newton, R.P.; Brenton, A.G.; Smith, C.J. and Dudley, E. Plant proteome analysis by mass spectrometry: principles, problems, pitfalls and recent developments. Phytochemistry, 2004, 65(11), 1449-1485.
    • (2004) Phytochemistry , vol.65 , Issue.11 , pp. 1449-1485
    • Newton, R.P.1    Brenton, A.G.2    Smith, C.J.3    Dudley, E.4
  • 54
    • 59449111124 scopus 로고    scopus 로고
    • Combining subproteome enrichment and Rubisco depletion enables identification of low abundance proteins differentially regulated during plant defense
    • Widjaja, I.; Naumann, K.; Roth, U.; Wolf, N.; Mackey, D.; Dangl, J.L.; Scheel, D. and Lee, J. Combining subproteome enrichment and Rubisco depletion enables identification of low abundance proteins differentially regulated during plant defense. Proteomics, 2009, 9(1), 138-147.
    • (2009) Proteomics , vol.9 , Issue.1 , pp. 138-147
    • Widjaja, I.1    Naumann, K.2    Roth, U.3    Wolf, N.4    Mackey, D.5    Dangl, J.L.6    Scheel, D.7    Lee, J.8
  • 55
    • 34250846498 scopus 로고    scopus 로고
    • Method development of efficient protein extraction in bone tissue for proteome analysis
    • Jiang, X.; Ye, M.; Jiang, X.; Liu, G.; Feng, S.; Cui, L. and Zou, H. Method development of efficient protein extraction in bone tissue for proteome analysis. J. Proteome. Res., 2007, 6(6), 2287-2294.
    • (2007) J. Proteome. Res , vol.6 , Issue.6 , pp. 2287-2294
    • Jiang, X.1    Ye, M.2    Jiang, X.3    Liu, G.4    Feng, S.5    Cui, L.6    Zou, H.7
  • 56
    • 67049155252 scopus 로고    scopus 로고
    • Taking advantage of non-specific trypsin cleavages for the identification of seed storage proteins in cereals
    • Sergeant, K.; Pinheiro, C.; Ricardo, C.P.; Hausman, J.F. and Ren-aut, J. Taking advantage of non-specific trypsin cleavages for the identification of seed storage proteins in cereals. J. Proteome. Res., 2009, 8(6), 3182-3190.
    • (2009) J. Proteome. Res , vol.8 , Issue.6 , pp. 3182-3190
    • Sergeant, K.1    Pinheiro, C.2    Ricardo, C.P.3    Hausman, J.F.4    Ren-Aut, J.5
  • 57
    • 13444267478 scopus 로고    scopus 로고
    • Plastid proteomics
    • van Wijk, K.J. Plastid proteomics. Plant Physiol. Biochem., 2004, 42(12), 963-977.
    • (2004) Plant Physiol. Biochem , vol.42 , Issue.12 , pp. 963-977
    • van Wijk, K.J.1
  • 58
    • 2942530586 scopus 로고    scopus 로고
    • Chloroplast proteomics: Potentials and challenges
    • Baginsky, S. and Gruissem, W. Chloroplast proteomics: potentials and challenges. J. Exp. Bot., 2004, 55(400), 1213-1220.
    • (2004) J. Exp. Bot , vol.55 , Issue.400 , pp. 1213-1220
    • Baginsky, S.1    Gruissem, W.2
  • 59
    • 3242810631 scopus 로고    scopus 로고
    • Sub-cellular pro-teomic analysis of a Medicago truncatula root microsomal fraction
    • Valot, B.; Gianinazzi, S. and Dumas-Gaudot, E. Sub-cellular pro-teomic analysis of a Medicago truncatula root microsomal fraction. Phytochemistry, 2004, 65(12), 1721-1732.
    • (2004) Phytochemistry , vol.65 , Issue.12 , pp. 1721-1732
    • Valot, B.1    Gianinazzi, S.2    Dumas-Gaudot, E.3
  • 60
    • 60249086737 scopus 로고    scopus 로고
    • Experimental analysis of the rice mitochondrial pro-teome, its biogenesis, and heterogeneity
    • Huang, S.; Taylor, N.L.; Narsai, R.; Eubel, H.; Whelan, J. and Millar, A.H. Experimental analysis of the rice mitochondrial pro-teome, its biogenesis, and heterogeneity. Plant Physiol., 2009, 149(2), 719-734.
    • (2009) Plant Physiol , vol.149 , Issue.2 , pp. 719-734
    • Huang, S.1    Taylor, N.L.2    Narsai, R.3    Eubel, H.4    Whelan, J.5    Millar, A.H.6
  • 62
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Gorg, A.; Weiss, W. and Dunn, M.J. Current two-dimensional electrophoresis technology for proteomics. Proteomics, 2004, 4(12), 3665-3685.
    • (2004) Proteomics , vol.4 , Issue.12 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 63
    • 0036468595 scopus 로고    scopus 로고
    • Two-dimensional gel elec-trophoresis: Recent advances in sample preparation, detection and quantitation
    • Lilley, K.S.; Razzaq, A. and Dupree, P. Two-dimensional gel elec-trophoresis: recent advances in sample preparation, detection and quantitation. Curr. Opin. Chem. Biol., 2002, 6(1), 46-50.
    • (2002) Curr. Opin. Chem. Biol , vol.6 , Issue.1 , pp. 46-50
    • Lilley, K.S.1    Razzaq, A.2    Dupree, P.3
  • 64
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electro-phoresis: A single gel method for detecting changes in protein extracts
    • Unlu, M.; Morgan, M.E. and Minden, J.S. Difference gel electro-phoresis: a single gel method for detecting changes in protein extracts. Electrophoresis, 1997, 18(11), 2071-2077.
    • (1997) Electrophoresis , vol.18 , Issue.11 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 65
    • 27744583045 scopus 로고    scopus 로고
    • All about DIGE: Quantification technology for differential-display 2D-gel proteomics
    • Lilley, K.S. and Friedman, D.B. All about DIGE: quantification technology for differential-display 2D-gel proteomics. Expert. Rev. Proteomics, 2004, 1(4), 401-409.
    • (2004) Expert. Rev. Proteomics , vol.1 , Issue.4 , pp. 401-409
    • Lilley, K.S.1    Friedman, D.B.2
  • 66
    • 77950478286 scopus 로고    scopus 로고
    • A multi-laboratory study assessing reproducibility of a 2D-DIGE differential proteomic experiment
    • Bech-Serra, J.J.; Borthwick, A.; Colome, N.; Albar, J.P.; Wells, M.; Sanchez del, P.M. and Canals, F. A multi-laboratory study assessing reproducibility of a 2D-DIGE differential proteomic experiment. J. Biomol. Tech., 2009, 20(5), 293-296.
    • (2009) J. Biomol. Tech , vol.20 , Issue.5 , pp. 293-296
    • Bech-Serra, J.J.1    Borthwick, A.2    Colome, N.3    Albar, J.P.4    Wells, M.5    Sanchez, D.P.M.6    Canals, F.7
  • 67
    • 71849100712 scopus 로고    scopus 로고
    • Isoelectric focusing and two-dimensional gel electrophoresis
    • Friedman, D.B.; Hoving, S. and Westermeier, R. Isoelectric focusing and two-dimensional gel electrophoresis. Methods Enzymol., 2009, 463, 515-540.
    • (2009) Methods Enzymol , vol.463 , pp. 515-540
    • Friedman, D.B.1    Hoving, S.2    Westermeier, R.3
  • 69
    • 77249098683 scopus 로고    scopus 로고
    • Proteomics of extreme freezing tolerance in Siberian spruce (Picea obovata)
    • Kjellsen, T.D.; Shiryaeva, L.; Schroder, W.P. and Strimbeck, G.R. Proteomics of extreme freezing tolerance in Siberian spruce (Picea obovata). J. Proteomics, 2010, 73(5), 965-975.
    • (2010) J. Proteomics , vol.73 , Issue.5 , pp. 965-975
    • Kjellsen, T.D.1    Shiryaeva, L.2    Schroder, W.P.3    Strimbeck, G.R.4
  • 70
    • 70449523440 scopus 로고    scopus 로고
    • Wheat quality related differential expressions of albumins and globulins revealed by two-dimensional difference gel electrophoresis (2-D DIGE)
    • Gao, L.; Wang, A.; Li, X.; Dong, K.; Wang, K.; Appels, R.; Ma, W. and Yan, Y. Wheat quality related differential expressions of albumins and globulins revealed by two-dimensional difference gel electrophoresis (2-D DIGE). J. Proteomics, 2009, 73(2), 279-296.
    • (2009) J. Proteomics , vol.73 , Issue.2 , pp. 279-296
    • Gao, L.1    Wang, A.2    Li, X.3    Dong, K.4    Wang, K.5    Appels, R.6    Ma, W.7    Yan, Y.8
  • 72
    • 69449094077 scopus 로고    scopus 로고
    • Proteomic characterization of Phrag-mites communis in ecotypes of swamp and desert dune
    • Cui, S.; Hu, J.; Yang, B.; Shi, L.; Huang, F.; Tsai, S.N.; Ngai, S.M.; He, Y. and Zhang, J. Proteomic characterization of Phrag-mites communis in ecotypes of swamp and desert dune. Pro-teomics, 2009, 9(16), 3950-3967.
    • (2009) Pro-teomics , vol.9 , Issue.16 , pp. 3950-3967
    • Cui, S.1    Hu, J.2    Yang, B.3    Shi, L.4    Huang, F.5    Tsai, S.N.6    Ngai, S.M.7    He, Y.8    Zhang, J.9
  • 73
    • 70349119507 scopus 로고    scopus 로고
    • Proteomic analysis from haploid and diploid embryos of Quercus suber L. identifies qualitative and quantitative differential expression patterns
    • Gomez, A.; Lopez, J.A.; Pintos, B.; Camafeita, E. and Bueno, M.A. Proteomic analysis from haploid and diploid embryos of Quercus suber L. identifies qualitative and quantitative differential expression patterns. Proteomics, 2009, 9(18), 4355-4367.
    • (2009) Proteomics , vol.9 , Issue.18 , pp. 4355-4367
    • Gomez, A.1    Lopez, J.A.2    Pintos, B.3    Camafeita, E.4    Bueno, M.A.5
  • 75
    • 0031888036 scopus 로고    scopus 로고
    • High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrome-try
    • Ducret, A.; Van Oostveen, I.; Eng, J.K.; Yates, J.R. III. and Aeber-sold, R. High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrome-try. Protein Sci., 1998, 7(3), 706-719.
    • (1998) Protein Sci , vol.7 , Issue.3 , pp. 706-719
    • Ducret, A.1    van Oostveen, I.2    Eng, J.K.3    Yates, J.R.4    Aeber-Sold, R.5
  • 77
    • 0031568420 scopus 로고    scopus 로고
    • Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level
    • McCormack, A.L.; Schieltz, D.M.; Goode, B.; Yang, S.; Barnes, G.; Drubin, D. and Yates, J.R. III. Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level. Anal. Chem., 1997, 69(4), 767-776.
    • (1997) Anal. Chem , vol.69 , Issue.4 , pp. 767-776
    • McCormack, A.L.1    Schieltz, D.M.2    Goode, B.3    Yang, S.4    Barnes, G.5    Drubin, D.6    Yates, J.R.7
  • 78
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun pro-teomics
    • Wolters, D.A.; Washburn, M.P. and Yates, J.R. III. An automated multidimensional protein identification technology for shotgun pro-teomics. Anal. Chem., 2001, 73(23), 5683-5690.
    • (2001) Anal. Chem , vol.73 , Issue.23 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates, J.R.3
  • 79
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S.P.; Rist, B.; Gerber, S.A.; Turecek, F.; Gelb, M.H. and Aebersold, R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol., 1999, 17(10), 994-999.
    • (1999) Nat. Biotechnol , vol.17 , Issue.10 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 80
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S.E.; Blagoev, B.; Kratchmarova, I.; Kristensen, D.B.; Steen, H.; Pandey, A. and Mann, M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell Proteomics, 2002, 1(5), 376-386.
    • (2002) Mol. Cell Proteomics , vol.1 , Issue.5 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 81
    • 45649083365 scopus 로고    scopus 로고
    • Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study
    • Bindschedler, L.V.; Palmblad, M. and Cramer, R. Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study. Phytochemistry, 2008, 69(10), 1962-1972.
    • (2008) Phytochemistry , vol.69 , Issue.10 , pp. 1962-1972
    • Bindschedler, L.V.1    Palmblad, M.2    Cramer, R.3
  • 82
    • 63349084973 scopus 로고    scopus 로고
    • Advancements in plant proteomics using quantitative mass spectrometry
    • Oeljeklaus, S.; Meyer, H.E. and Warscheid, B. Advancements in plant proteomics using quantitative mass spectrometry. J. Pro-teomics, 2009, 72(3), 545-554.
    • (2009) J. Pro-teomics , vol.72 , Issue.3 , pp. 545-554
    • Oeljeklaus, S.1    Meyer, H.E.2    Warscheid, B.3
  • 84
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S.E. and Mann, M. Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol., 2005, 1(5), 252-262.
    • (2005) Nat. Chem. Biol , vol.1 , Issue.5 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 85
    • 40549107755 scopus 로고    scopus 로고
    • Comparative LC-MS: A landscape of peaks and valleys
    • America, A.H. and Cordewener, J.H. Comparative LC-MS: a landscape of peaks and valleys. Proteomics, 2008, 8(4), 731-749.
    • (2008) Proteomics , vol.8 , Issue.4 , pp. 731-749
    • America, A.H.1    Cordewener, J.H.2
  • 87
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon, B. and Aebersold, R. Mass spectrometry and protein analysis. Science, 2006, 312(5771), 212-217.
    • (2006) Science , vol.312 , Issue.5771 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 88
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates, J.R. III; Eng, J.K.; McCormack, A.L. and Schieltz, D. Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal. Chem., 1995, 67(8), 1426-1436.
    • (1995) Anal. Chem , vol.67 , Issue.8 , pp. 1426-1436
    • Yates, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 89
    • 59149087245 scopus 로고    scopus 로고
    • Plant proteomics: Concepts, applications, and novel strategies for data interpretation
    • Baginsky, S. Plant proteomics: concepts, applications, and novel strategies for data interpretation. Mass Spectrom Rev., 2009, 28(1), 93-120.
    • (2009) Mass Spectrom Rev , vol.28 , Issue.1 , pp. 93-120
    • Baginsky, S.1
  • 90
    • 0035241690 scopus 로고    scopus 로고
    • Mass spectrometry in proteomics
    • Aebersold, R. and Goodlett, D.R. Mass spectrometry in proteomics. Chem. Rev., 2001, 101(2), 269-295.
    • (2001) Chem. Rev , vol.101 , Issue.2 , pp. 269-295
    • Aebersold, R.1    Goodlett, D.R.2
  • 91
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (+/-10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • Clauser, K.R.; Baker, P. and Burlingame, A.L. Role of accurate mass measurement (+/-10 ppm) in protein identification strategies employing MS or MS/MS and database searching. Anal. Chem., 1999, 71(14), 2871-2882.
    • (1999) Anal. Chem , vol.71 , Issue.14 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3
  • 92
    • 0031298696 scopus 로고    scopus 로고
    • Identification of the components of simple protein mixtures by high-accuracy pep-tide mass mapping and database searching
    • Jensen, O.N.; Podtelejnikov, A.V. and Mann, M. Identification of the components of simple protein mixtures by high-accuracy pep-tide mass mapping and database searching. Anal. Chem., 1997, 69(23), 4741-4750.
    • (1997) Anal. Chem , vol.69 , Issue.23 , pp. 4741-4750
    • Jensen, O.N.1    Podtelejnikov, A.V.2    Mann, M.3
  • 93
    • 0042386237 scopus 로고    scopus 로고
    • Iterative data analysis is the key for exhaustive analysis of peptide mass fingerprints from proteins separated by two-dimensional electrophoresis
    • Schmidt, F.; Schmid, M.; Jungblut, P.R.; Mattow, J.; Facius, A. and Pleissner, K.P. Iterative data analysis is the key for exhaustive analysis of peptide mass fingerprints from proteins separated by two-dimensional electrophoresis. J. Am. Soc. Mass Spectrom., 2003, 14(9), 943-956.
    • (2003) J. Am. Soc. Mass Spectrom , vol.14 , Issue.9 , pp. 943-956
    • Schmidt, F.1    Schmid, M.2    Jungblut, P.R.3    Mattow, J.4    Facius, A.5    Pleissner, K.P.6
  • 95
    • 0031557882 scopus 로고    scopus 로고
    • Cross-species protein identification using amino acid composition, peptide mass fingerprinting, isoelectric point and molecular mass: A theoretical evaluation
    • Wilkins, M.R. and Williams, K.L. Cross-species protein identification using amino acid composition, peptide mass fingerprinting, isoelectric point and molecular mass: a theoretical evaluation. J. Theor. Biol., 1997, 186(1), 7-15.
    • (1997) J. Theor. Biol , vol.186 , Issue.1 , pp. 7-15
    • Wilkins, M.R.1    Williams, K.L.2
  • 97
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching
    • Shevchenko, A.; Sunyaev, S.; Loboda, A.; Shevchenko, A.; Bork, P.; Ens, W. and Standing, K.G. Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching. Anal. Chem., 2001, 73(9), 1917-1926.
    • (2001) Anal. Chem , vol.73 , Issue.9 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Shevchenko, A.4    Bork, P.5    Ens, W.6    Standing, K.G.7
  • 98
    • 0036463587 scopus 로고    scopus 로고
    • Getting more from less: Algorithms for rapid protein identification with multiple short peptide sequences
    • Mackey, A.J.; Haystead, T.A. and Pearson, W.R. Getting more from less: algorithms for rapid protein identification with multiple short peptide sequences. Mol. Cell Proteomics, 2002, 1(2), 139-147.
    • (2002) Mol. Cell Proteomics , vol.1 , Issue.2 , pp. 139-147
    • Mackey, A.J.1    Haystead, T.A.2    Pearson, W.R.3
  • 99
    • 21644450554 scopus 로고    scopus 로고
    • Defining parameters for homology-tolerant database searching
    • Kayser, J.P.; Vallet, J.L. and Cerny, R.L. Defining parameters for homology-tolerant database searching. J. Biomol. Tech., 2004, 15(4), 285-295.
    • (2004) J. Biomol. Tech , vol.15 , Issue.4 , pp. 285-295
    • Kayser, J.P.1    Vallet, J.L.2    Cerny, R.L.3
  • 101
    • 34547153650 scopus 로고    scopus 로고
    • Sequence similarity-driven pro-teomics in organisms with unknown genomes by LC-MS/MS and automated de novo sequencing
    • Waridel, P.; Frank, A.; Thomas, H.; Surendranath, V.; Sunyaev, S.; Pevzner, P. and Shevchenko, A. Sequence similarity-driven pro-teomics in organisms with unknown genomes by LC-MS/MS and automated de novo sequencing. Proteomics, 2007, 7(14), 2318-2329.
    • (2007) Proteomics , vol.7 , Issue.14 , pp. 2318-2329
    • Waridel, P.1    Frank, A.2    Thomas, H.3    Surendranath, V.4    Sunyaev, S.5    Pevzner, P.6    Shevchenko, A.7
  • 102
    • 1442324456 scopus 로고    scopus 로고
    • Influence of basic residue content on fragment ion peak intensities in low-energy collision-induced dissociation spectra of peptides
    • Tabb, D.L.; Huang, Y.; Wysocki, V.H. and Yates, J.R. III. Influence of basic residue content on fragment ion peak intensities in low-energy collision-induced dissociation spectra of peptides. Anal. Chem., 2004, 76(5), 1243-1248.
    • (2004) Anal. Chem , vol.76 , Issue.5 , pp. 1243-1248
    • Tabb, D.L.1    Huang, Y.2    Wysocki, V.H.3    Yates, J.R.4
  • 103
    • 21844457685 scopus 로고    scopus 로고
    • Fragmentation pathways of protonated peptides
    • Paizs, B. and Suhai, S. Fragmentation pathways of protonated peptides. Mass Spectrom. Rev., 2005, 24(4), 508-548.
    • (2005) Mass Spectrom. Rev , vol.24 , Issue.4 , pp. 508-548
    • Paizs, B.1    Suhai, S.2
  • 104
    • 0034501099 scopus 로고    scopus 로고
    • Mobile and localized protons: A framework for understanding peptide dissociation
    • Wysocki, V.H.; Tsaprailis, G.; Smith, L.L. and Breci, L.A. Mobile and localized protons: a framework for understanding peptide dissociation. J. Mass Spectrom., 2000, 35(12), 1399-1406.
    • (2000) J. Mass Spectrom , vol.35 , Issue.12 , pp. 1399-1406
    • Wysocki, V.H.1    Tsaprailis, G.2    Smith, L.L.3    Breci, L.A.4
  • 105
    • 0035356977 scopus 로고    scopus 로고
    • Implementation and uses of automated de novo peptide sequencing by tandem mass spectrometry
    • Taylor, J.A. and Johnson, R.S. Implementation and uses of automated de novo peptide sequencing by tandem mass spectrometry. Anal. Chem., 2001, 73(11), 2594-2604.
    • (2001) Anal. Chem , vol.73 , Issue.11 , pp. 2594-2604
    • Taylor, J.A.1    Johnson, R.S.2
  • 106
    • 13844319908 scopus 로고    scopus 로고
    • PepNovo: De novo peptide sequencing via probabilistic network modeling
    • Frank, A. and Pevzner, P. PepNovo: de novo peptide sequencing via probabilistic network modeling. Anal. Chem., 2005, 77(4), 964-973.
    • (2005) Anal. Chem , vol.77 , Issue.4 , pp. 964-973
    • Frank, A.1    Pevzner, P.2
  • 109
    • 5144222072 scopus 로고    scopus 로고
    • Sequence optimization as an alternative to de novo analysis of tandem mass spectrometry data
    • Heredia-Langner, A.; Cannon, W.R.; Jarman, K.D. and Jarman, K.H. Sequence optimization as an alternative to de novo analysis of tandem mass spectrometry data. Bioinformatics, 2004, 20(14), 2296-2304.
    • (2004) Bioinformatics , vol.20 , Issue.14 , pp. 2296-2304
    • Heredia-Langner, A.1    Cannon, W.R.2    Jarman, K.D.3    Jarman, K.H.4
  • 110
    • 72449165051 scopus 로고    scopus 로고
    • Silencing OsHI-LOX makes rice more susceptible to chewing herbivores, but enhances resistance to a phloem feeder
    • Zhou, G.; Qi, J.; Ren, N.; Cheng, J.; Erb, M.; Mao, B. and Lou, Y. Silencing OsHI-LOX makes rice more susceptible to chewing herbivores, but enhances resistance to a phloem feeder. Plant J., 2009, 60(4), 638-648.
    • (2009) Plant J , vol.60 , Issue.4 , pp. 638-648
    • Zhou, G.1    Qi, J.2    Ren, N.3    Cheng, J.4    Erb, M.5    Mao, B.6    Lou, Y.7
  • 111
    • 46749089201 scopus 로고    scopus 로고
    • Lys Tag: An easy and robust chemical modification for improved de novo sequencing with a matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometer
    • Conrotto, P. and Hellman, U. Lys Tag: an easy and robust chemical modification for improved de novo sequencing with a matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometer. Rapid Commun. Mass Spectrom., 2008, 22(12), 1823-1833.
    • (2008) Rapid Commun. Mass Spectrom , vol.22 , Issue.12 , pp. 1823-1833
    • Conrotto, P.1    Hellman, U.2
  • 112
    • 0034534884 scopus 로고    scopus 로고
    • Derivatization procedures to facilitate de novo sequencing of lysine-terminated tryptic peptides using postsource decay matrix-assisted laser desorption/ionization mass spectrometry
    • Keough, T.; Lacey, M.P. and Youngquist, R.S. Derivatization procedures to facilitate de novo sequencing of lysine-terminated tryptic peptides using postsource decay matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom., 2000, 14(24), 2348-2356.
    • (2000) Rapid Commun. Mass Spectrom , vol.14 , Issue.24 , pp. 2348-2356
    • Keough, T.1    Lacey, M.P.2    Youngquist, R.S.3
  • 113
    • 20644441789 scopus 로고    scopus 로고
    • De novo sequence analysis of N-terminal sulfonated peptides after in-gel guanidination
    • Sergeant, K.; Samyn, B.; Debyser, G. and Van Beeumen, J. De novo sequence analysis of N-terminal sulfonated peptides after in-gel guanidination. Proteomics, 2005, 5(9), 2369-2380.
    • (2005) Proteomics , vol.5 , Issue.9 , pp. 2369-2380
    • Sergeant, K.1    Samyn, B.2    Debyser, G.3    van Beeumen, J.4
  • 114
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann, M. and Jensen, O.N. Proteomic analysis of post-translational modifications. Nat. Biotechnol., 2003, 21(3), 255-261.
    • (2003) Nat. Biotechnol , vol.21 , Issue.3 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 115
    • 64749087403 scopus 로고    scopus 로고
    • Recent developments in mass spectrometry analysis of phosphoproteomes
    • Dass, C. Recent developments in mass spectrometry analysis of phosphoproteomes. Curr. Proteomics, 2009, 6(1), 32-42.
    • (2009) Curr. Proteomics , vol.6 , Issue.1 , pp. 32-42
    • Dass, C.1
  • 116
    • 70350247861 scopus 로고    scopus 로고
    • Modification-specific proteomics: Strategies for characterization of post-translational modifications using enrichment techniques
    • Zhao, Y. and Jensen, O.N. Modification-specific proteomics: strategies for characterization of post-translational modifications using enrichment techniques. Proteomics, 2009, 9(20), 4632-4641.
    • (2009) Proteomics , vol.9 , Issue.20 , pp. 4632-4641
    • Zhao, Y.1    Jensen, O.N.2
  • 117
    • 0042572083 scopus 로고    scopus 로고
    • Early phosphorylation events in biotic stress
    • Peck, S.C. Early phosphorylation events in biotic stress. Curr. Opin. Plant. Biol., 2003, 6(4), 334-338.
    • (2003) Curr. Opin. Plant. Biol , vol.6 , Issue.4 , pp. 334-338
    • Peck, S.C.1
  • 119
    • 33750579665 scopus 로고    scopus 로고
    • Plant phosphoproteomics: A long road ahead
    • Kersten, B.; Agrawal, G.K.; Iwahashi, H. and Rakwal, R. Plant phosphoproteomics: a long road ahead. Proteomics, 2006, 6(20), 5517-5528.
    • (2006) Proteomics , vol.6 , Issue.20 , pp. 5517-5528
    • Kersten, B.1    Agrawal, G.K.2    Iwahashi, H.3    Rakwal, R.4
  • 121
    • 77956028057 scopus 로고    scopus 로고
    • Quantitative analysis of protein phosphorylation on a system-wide scale by mass spectrometry-based proteomics
    • Bodenmiller, B. and Aebershold, R. Quantitative analysis of protein phosphorylation on a system-wide scale by mass spectrometry-based proteomics. Methods Enzym., 2010, 470, 317-334.
    • (2010) Methods Enzym , vol.470 , pp. 317-334
    • Bodenmiller, B.1    Aebershold, R.2
  • 122
    • 70149092747 scopus 로고    scopus 로고
    • Coupling oxidative signals to protein phosphorylation via methionine oxidation in Arabidopsis
    • Hardin S.C., Larue C.T., Oh M.H., Jain V., and Huber S.C. Coupling oxidative signals to protein phosphorylation via methionine oxidation in Arabidopsis. Biochem. J., 2009, 422(2), 305-312.
    • (2009) Biochem. J , vol.422 , Issue.2 , pp. 305-312
    • Hardin, S.C.1    Larue, C.T.2    Oh, M.H.3    Jain, V.4    Huber, S.C.5
  • 123
    • 0036001076 scopus 로고    scopus 로고
    • Hydrogen peroxide and nitric oxide as signalling molecules in plants
    • Neill, S.J.; Desikan, R.; Clarke, A.; Hurst, R.D. and Hancock, J.T. Hydrogen peroxide and nitric oxide as signalling molecules in plants. J. Exp. Bot., 2002, 53(372), 1237-1247.
    • (2002) J. Exp. Bot , vol.53 , Issue.372 , pp. 1237-1247
    • Neill, S.J.1    Desikan, R.2    Clarke, A.3    Hurst, R.D.4    Hancock, J.T.5
  • 124
    • 41849130604 scopus 로고    scopus 로고
    • Nitric oxide synthesis and signalling in plants
    • Wilson, I.D.; Neill, S.J. and Hancock, J.T. Nitric oxide synthesis and signalling in plants. Plant Cell Environ., 2008, 31(5), 622-631.
    • (2008) Plant Cell Environ , vol.31 , Issue.5 , pp. 622-631
    • Wilson, I.D.1    Neill, S.J.2    Hancock, J.T.3
  • 125
    • 20444475362 scopus 로고    scopus 로고
    • NO news is good news for plants
    • Delledonne, M. NO news is good news for plants. Curr. Opin. Plant Biol., 2005, 8(4), 390-396.
    • (2005) Curr. Opin. Plant Biol , vol.8 , Issue.4 , pp. 390-396
    • Delledonne, M.1
  • 128
    • 38049091477 scopus 로고    scopus 로고
    • Proteomic identification of tyrosine nitration targets in kidney of spontaneously hypertensive rats
    • Tyther, R.; Ahmeda, A.; Johns, E. and Sheehan, D. Proteomic identification of tyrosine nitration targets in kidney of spontaneously hypertensive rats. Proteomics, 2007, 7(24), 4555-4564.
    • (2007) Proteomics , vol.7 , Issue.24 , pp. 4555-4564
    • Tyther, R.1    Ahmeda, A.2    Johns, E.3    Sheehan, D.4
  • 131
    • 77952075913 scopus 로고    scopus 로고
    • NO synthesis and signaling in plants-where do we stand?
    • Moreau, M.; Lindermayr, C.; Durner, J. and Klessig, D.F. NO synthesis and signaling in plants-where do we stand? Physiol. Plant., 2010, 138(4), 372-383.
    • (2010) Physiol. Plant , vol.138 , Issue.4 , pp. 372-383
    • Moreau, M.1    Lindermayr, C.2    Durner, J.3    Klessig, D.F.4
  • 132
    • 33745210764 scopus 로고    scopus 로고
    • Crosstalk between abiotic and biotic stress responses: A current view from the points of convergence in the stress signaling networks
    • Fujita, M.; Fujita, Y.; Noutoshi, Y.; Takahashi, F.; Narusaka, Y.; Yamaguchi-Shinozaki, K. and Shinozaki, K. Crosstalk between abiotic and biotic stress responses: a current view from the points of convergence in the stress signaling networks. Curr. Opin. Plant Biol., 2006, 9(4), 436-442.
    • (2006) Curr. Opin. Plant Biol , vol.9 , Issue.4 , pp. 436-442
    • Fujita, M.1    Fujita, Y.2    Noutoshi, Y.3    Takahashi, F.4    Narusaka, Y.5    Yamaguchi-Shinozaki, K.6    Shinozaki, K.7
  • 133
    • 0034545719 scopus 로고    scopus 로고
    • Quantification and significance of protein oxidation in biological samples
    • Shacter, E. Quantification and significance of protein oxidation in biological samples. Drug Metab. Rev., 2000, 32(3-4), 307-326.
    • (2000) Drug Metab. Rev , vol.32 , Issue.3-4 , pp. 307-326
    • Shacter, E.1
  • 134
    • 34250849635 scopus 로고    scopus 로고
    • Oxidative modifications to cellular components in plants
    • Moller, I.M.; Jensen, P.E. and Hansson, A. Oxidative modifications to cellular components in plants. Annu. Rev. Plant Biol., 2007, 58, 459-481.
    • (2007) Annu. Rev. Plant Biol , vol.58 , pp. 459-481
    • Moller, I.M.1    Jensen, P.E.2    Hansson, A.3
  • 135
    • 55249125700 scopus 로고    scopus 로고
    • Redox proteomics: Basic principles and future perspectives for the detection of protein oxidation in plants
    • Rinalducci, S.; Murgiano, L. and Zolla, L. Redox proteomics: basic principles and future perspectives for the detection of protein oxidation in plants. J. Exp. Bot., 2008, 59(14), 3781-3801.
    • (2008) J. Exp. Bot , vol.59 , Issue.14 , pp. 3781-3801
    • Rinalducci, S.1    Murgiano, L.2    Zolla, L.3
  • 137
    • 77957751135 scopus 로고    scopus 로고
    • Shotgun redox proteomics in sub-proteomes trapped on functionalised beads: Identification of proteins targeted by oxidative stress
    • doi:10.1016/j.marenvres.2009.11.005
    • Hu, W.; Tedesco, S.; McDonagh, B. and Sheehan, D. Shotgun redox proteomics in sub-proteomes trapped on functionalised beads: Identification of proteins targeted by oxidative stress. Mar. Environ. Res., 2009, doi:10.1016/j.marenvres.2009.11.005
    • (2009) Mar. Environ. Res
    • Hu, W.1    Tedesco, S.2    McDonagh, B.3    Sheehan, D.4
  • 138
    • 44749089879 scopus 로고    scopus 로고
    • Effects of oxidative stress on protein thiols and disulphides in Mytilus edulis revealed by pro-teomics: Actin and protein disulphide isomerase are redox targets
    • McDonagh, B. and Sheehan, D. Effects of oxidative stress on protein thiols and disulphides in Mytilus edulis revealed by pro-teomics: actin and protein disulphide isomerase are redox targets. Mar. Environ. Res., 2008, 66(1), 193-195.
    • (2008) Mar. Environ. Res , vol.66 , Issue.1 , pp. 193-195
    • McDonagh, B.1    Sheehan, D.2
  • 139
    • 31344457662 scopus 로고    scopus 로고
    • Protein oxidation in plant mito chondria detected as oxidized tryptophan
    • Moller, I.M. and Kristensen, B.K. Protein oxidation in plant mito chondria detected as oxidized tryptophan. Free Radic. Biol. Med., 2006, 40(3), 430-435.
    • (2006) Free Radic. Biol. Med , vol.40 , Issue.3 , pp. 430-435
    • Moller, I.M.1    Kristensen, B.K.2
  • 140
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • Pickart, C.M. and Eddins, M.J. Ubiquitin: structures, functions, mechanisms. Biochim. Biophys. Acta, 2004, 1695(1-3), 55-72.
    • (2004) Biochim. Biophys. Acta , vol.1695 , Issue.1-3 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 142
    • 0037470238 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and-2 conjugates is increased by stress
    • Kurepa, J.; Walker, J.M.; Smalle, J.; Gosink, M.M.; Davis, S.J.; Durham, T.L. Sung, D.Y. and Vierstra, R.D. The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and-2 conjugates is increased by stress. J. Biol. Chem., 2003, 278(9), 6862-6872.
    • (2003) J. Biol. Chem , vol.278 , Issue.9 , pp. 6862-6872
    • Kurepa, J.1    Walker, J.M.2    Smalle, J.3    Gosink, M.M.4    Davis, S.J.5    Durham, T.L.6    Sung, D.Y.7    Vierstra, R.D.8
  • 143
    • 70949102199 scopus 로고    scopus 로고
    • Sumoylation and abscisic acid signaling
    • Miura, K. and Hasegawa, P.M. Sumoylation and abscisic acid signaling. Plant Signal. Behav., 2009, 4(12).
    • (2009) Plant Signal. Behav , vol.4 , Issue.12
    • Miura, K.1    Hasegawa, P.M.2
  • 144
    • 34848870906 scopus 로고    scopus 로고
    • Sumoylation, a post-translational regulatory process in plants
    • Miura, K.; Jin, J.B. and Hasegawa, P.M. Sumoylation, a post-translational regulatory process in plants. Curr. Opin. Plant Biol., 2007, 10(5), 495-502.
    • (2007) Curr. Opin. Plant Biol , vol.10 , Issue.5 , pp. 495-502
    • Miura, K.1    Jin, J.B.2    Hasegawa, P.M.3
  • 147
    • 33745384253 scopus 로고    scopus 로고
    • Protecting crops from non-persistently aphid-transmitted viruses: A review on the use of barrier plants as a management tool
    • Hooks, C.R. and Fereres, A. Protecting crops from non-persistently aphid-transmitted viruses: a review on the use of barrier plants as a management tool. Virus Res., 2006, 120(1-2), 1-16.
    • (2006) Virus Res , vol.120 , Issue.1-2 , pp. 1-16
    • Hooks, C.R.1    Fereres, A.2
  • 148
  • 149
    • 68249108680 scopus 로고    scopus 로고
    • Herbivory-induced signalling in plants: Perception and action
    • Wu, J. and Baldwin, I.T. Herbivory-induced signalling in plants: perception and action. Plant Cell Environ., 2009, 32(9), 1161-1174.
    • (2009) Plant Cell Environ , vol.32 , Issue.9 , pp. 1161-1174
    • Wu, J.1    Baldwin, I.T.2
  • 150
    • 34247868984 scopus 로고    scopus 로고
    • Proteomic profiling of aphid Macrosiphum euphorbiae responses to host-plant-mediated stress induced by defoliation and water deficit
    • An Nguyen, T.T.; Michaud, D. and Cloutier, C. Proteomic profiling of aphid Macrosiphum euphorbiae responses to host-plant-mediated stress induced by defoliation and water deficit. J. Insect. Physiol., 2007, 53(6), 601-611.
    • (2007) J. Insect. Physiol , vol.53 , Issue.6 , pp. 601-611
    • Nguyen, T.T.A.1    Michaud, D.2    Cloutier, C.3
  • 153
    • 33845653619 scopus 로고    scopus 로고
    • Molecular interactions between the specialist herbivore Manduca sexta (Lepidoptera, Sphingidae) and its natural host Nicotiana attenuata. VII. Changes in the plant's proteome
    • Giri, A.P.; Wunsche, H.; Mitra, S.; Zavala, J.A.; Muck, A.; Svatos, A. and Baldwin, I.T. Molecular interactions between the specialist herbivore Manduca sexta (Lepidoptera, Sphingidae) and its natural host Nicotiana attenuata. VII. Changes in the plant's proteome. Plant Physiol., 2006, 142(4), 1621-1641.
    • (2006) Plant Physiol , vol.142 , Issue.4 , pp. 1621-1641
    • Giri, A.P.1    Wunsche, H.2    Mitra, S.3    Zavala, J.A.4    Muck, A.5    Svatos, A.6    Baldwin, I.T.7
  • 154
    • 33846626473 scopus 로고    scopus 로고
    • Conifer defense against insects: Proteome analysis of Sitka spruce (Picea sitchensis) bark induced by mechanical wounding or feeding by white pine weevils (Pissodes strobi)
    • Lippert, D.; Chowrira, S.; Ralph, S.G.; Zhuang, J.; Aeschliman, D.; Ritland, C.; Ritland, K. and Bohlmann, J. Conifer defense against insects: proteome analysis of Sitka spruce (Picea sitchensis) bark induced by mechanical wounding or feeding by white pine weevils (Pissodes strobi). Proteomics, 2007, 7(2), 248-270.
    • (2007) Proteomics , vol.7 , Issue.2 , pp. 248-270
    • Lippert, D.1    Chowrira, S.2    Ralph, S.G.3    Zhuang, J.4    Aeschliman, D.5    Ritland, C.6    Ritland, K.7    Bohlmann, J.8
  • 155
    • 77952880385 scopus 로고    scopus 로고
    • Proteomic analysis of interactions between the generalist herbivore Spodoptera exigua (Lepidoptera: Noctuidae) and Arabidopsis thaliana
    • Zhang, J.H.; Sun, L.W.; Liu, L.L.; An, S.L.; Wang, X.; Zhang, J.; Jin, J.L.; Li, S.Y. and Xi, J.H. Proteomic analysis of interactions between the generalist herbivore Spodoptera exigua (Lepidoptera: Noctuidae) and Arabidopsis thaliana. Plant Mol. Biol. Rep., 2010, 28, 324-333.
    • (2010) Plant Mol. Biol. Rep , vol.28 , pp. 324-333
    • Zhang, J.H.1    Sun, L.W.2    Liu, L.L.3    An, S.L.4    Wang, X.5    Zhang, J.6    Jin, J.L.7    Li, S.Y.8    Xi, J.H.9
  • 156
    • 66449134802 scopus 로고    scopus 로고
    • Understanding rice plant resistance to the Brown Planthopper (Nilaparvata lugens): A proteomic approach
    • Wei, Z.; Hu, W.; Lin, Q.; Cheng, X.; Tong, M.; Zhu, L.; Chen, R. and He, G. Understanding rice plant resistance to the Brown Planthopper (Nilaparvata lugens): a proteomic approach. Pro-teomics, 2009, 9(10), 2798-2808.
    • (2009) Pro-teomics , vol.9 , Issue.10 , pp. 2798-2808
    • Wei, Z.1    Hu, W.2    Lin, Q.3    Cheng, X.4    Tong, M.5    Zhu, L.6    Chen, R.7    He, G.8
  • 157
    • 30044443050 scopus 로고    scopus 로고
    • Jasmonate-inducible plant enzymes degrade essential amino acids in the herbivore midgut
    • Chen, H.; Wilkerson, C.G.; Kuchar, J.A.; Phinney, B.S. and Howe, G.A. Jasmonate-inducible plant enzymes degrade essential amino acids in the herbivore midgut. Proc. Natl. Acad. Sci. USA, 2005, 102(52), 19237-19242.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.52 , pp. 19237-19242
    • Chen, H.1    Wilkerson, C.G.2    Kuchar, J.A.3    Phinney, B.S.4    Howe, G.A.5
  • 158
    • 36749013655 scopus 로고    scopus 로고
    • Plant virus transmission from the insect point of view
    • Hohn, T. Plant virus transmission from the insect point of view. Proc. Natl. Acad. Sci. USA, 2007, 104(46), 17905-17906.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.46 , pp. 17905-17906
    • Hohn, T.1
  • 159
    • 60549106098 scopus 로고    scopus 로고
    • Cellular and molecular aspects of rhabdovirus interactions with insect and plant hosts
    • Ammar, E.; Tsai, C.W.; Whitfield, A.E.; Redinbaugh, M.G. and Hogenhout, S.A. Cellular and molecular aspects of rhabdovirus interactions with insect and plant hosts. Annu. Rev. Entomol., 2009, 54, 447-468.
    • (2009) Annu. Rev. Entomol , vol.54 , pp. 447-468
    • Ammar, E.1    Tsai, C.W.2    Whitfield, A.E.3    Redinbaugh, M.G.4    Hogenhout, S.A.5
  • 160
    • 64149112410 scopus 로고    scopus 로고
    • Behavioural aspects influencing plant virus transmission by homopteran insects
    • Fereres, A. and Moreno, A. Behavioural aspects influencing plant virus transmission by homopteran insects. Virus Res., 2009, 141(2), 158-168.
    • (2009) Virus Res , vol.141 , Issue.2 , pp. 158-168
    • Fereres, A.1    Moreno, A.2
  • 161
    • 76849110999 scopus 로고    scopus 로고
    • Transcriptomic analysis of intestinal genes following acquisition of pea enation mosaic virus by the pea aphid Acyrthosiphon pisum
    • Brault, V.; Tanguy, S.; Reinbold, C.; Le Trionnaire, G.; Arneodo, J.; Jaubert-Possamai, S.; Guernec, G. and Tagu, D. Transcriptomic analysis of intestinal genes following acquisition of pea enation mosaic virus by the pea aphid Acyrthosiphon pisum. J. Gen. Virol., 2010, 91(3), 802-808.
    • (2010) J. Gen. Virol , vol.91 , Issue.3 , pp. 802-808
    • Brault, V.1    Tanguy, S.2    Reinbold, C.3    Trionnaire, G.L.4    Arneodo, J.5    Jaubert-Possamai, S.6    Guernec, G.7    Tagu, D.8
  • 162
    • 34248154353 scopus 로고    scopus 로고
    • In vitro association between the helper component-proteinase of zucchini yellow mosaic virus and cuticle proteins of Myzus persicae
    • Dombrovsky, A.; Gollop, N.; Chen, S.; Chejanovsky, N. and Raccah, B. In vitro association between the helper component-proteinase of zucchini yellow mosaic virus and cuticle proteins of Myzus persicae. J. Gen. Virol., 2007, 88(5), 1602-1610.
    • (2007) J. Gen. Virol , vol.88 , Issue.5 , pp. 1602-1610
    • Dombrovsky, A.1    Gollop, N.2    Chen, S.3    Chejanovsky, N.4    Raccah, B.5
  • 163
    • 37349062718 scopus 로고    scopus 로고
    • Coupling genetics and proteomics to identify aphid proteins associated with vector-specific transmission of polerovirus (luteoviridae)
    • Yang, X.; Thannhauser, T.W.; Burrows, M.; Cox-Foster, D.; Gil-dow, F.E. and Gray, S.M. Coupling genetics and proteomics to identify aphid proteins associated with vector-specific transmission of polerovirus (luteoviridae). J. Virol., 2008, 82(1), 291-299.
    • (2008) J. Virol , vol.82 , Issue.1 , pp. 291-299
    • Yang, X.1    Thannhauser, T.W.2    Burrows, M.3    Cox-Foster, D.4    Gil-Dow, F.E.5    Gray, S.M.6
  • 164
    • 0036402642 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of proteins discriminates aphid clones of Sitobion avenae differing in BYDV-PAV transmission
    • Papura, D.; Jacquot, E.; Dedryver, C.A.; Luche, S.; Riault, G.; Bossis, M. and Rabilloud, T. Two-dimensional electrophoresis of proteins discriminates aphid clones of Sitobion avenae differing in BYDV-PAV transmission. Arch Virol., 2002, 147(10), 1881-1898.
    • (2002) Arch Virol , vol.147 , Issue.10 , pp. 1881-1898
    • Papura, D.1    Jacquot, E.2    Dedryver, C.A.3    Luche, S.4    Riault, G.5    Bossis, M.6    Rabilloud, T.7
  • 165
    • 3142530530 scopus 로고    scopus 로고
    • Rack-1, GAPDH3, and actin: Proteins of Myzus persicae potentially involved in the transcytosis of beet western yellows virus particles in the aphid
    • Seddas, P.; Boissinot, S.; Strub, J.M.; Van Dorsselaer, A.; Van Regenmortel, M.H. and Pattus, F. Rack-1, GAPDH3, and actin: proteins of Myzus persicae potentially involved in the transcytosis of beet western yellows virus particles in the aphid. Virology, 2004, 325(2), 399-412.
    • (2004) Virology , vol.325 , Issue.2 , pp. 399-412
    • Seddas, P.1    Boissinot, S.2    Strub, J.M.3    van Dorsselaer, A.4    van Regenmortel, M.H.5    Pattus, F.6
  • 166
    • 70449465091 scopus 로고    scopus 로고
    • Begomovirus coat protein interacts with a small heat-shock protein of its transmission vector (Be-misia tabaci)
    • Ohnesorge, S. and Bejarano, E.R. Begomovirus coat protein interacts with a small heat-shock protein of its transmission vector (Be-misia tabaci). Insect. Mol. Biol., 2009, 18(6), 693-703.
    • (2009) Insect. Mol. Biol , vol.18 , Issue.6 , pp. 693-703
    • Ohnesorge, S.1    Bejarano, E.R.2
  • 167
    • 48949120134 scopus 로고    scopus 로고
    • Avoiding effective defenses: Strategies employed by phloem-feeding insects
    • Walling, L.L. Avoiding effective defenses: strategies employed by phloem-feeding insects. Plant Physiol., 2008, 146(3), 859-866.
    • (2008) Plant Physiol , vol.146 , Issue.3 , pp. 859-866
    • Walling, L.L.1
  • 168
    • 40349098946 scopus 로고    scopus 로고
    • Plant-mediated interactions between whiteflies, herbivores, and natural enemies
    • Inbar, M. and Gerling, D. Plant-mediated interactions between whiteflies, herbivores, and natural enemies. Annu. Rev. Entomol., 2008, 53, 431-448.
    • (2008) Annu. Rev. Entomol , vol.53 , pp. 431-448
    • Inbar, M.1    Gerling, D.2
  • 169
    • 46449090254 scopus 로고    scopus 로고
    • Early progress in aphid genomics and consequences for plant-aphid interactions studies
    • Tagu, D.; Klingler, J.P.; Moya, A. and Simon, J.C. Early progress in aphid genomics and consequences for plant-aphid interactions studies. Mol. Plant Microbe Interact., 2008, 21(6), 701-708.
    • (2008) Mol. Plant Microbe Interact , vol.21 , Issue.6 , pp. 701-708
    • Tagu, D.1    Klingler, J.P.2    Moya, A.3    Simon, J.C.4
  • 170
    • 33644926728 scopus 로고    scopus 로고
    • Phloem sap proteins: Their identities and potential roles in the interaction between plants and phloem-feeding insects
    • Kehr, J. Phloem sap proteins: their identities and potential roles in the interaction between plants and phloem-feeding insects. J. Exp. Bot., 2006, 57(4), 767-774.
    • (2006) J. Exp. Bot , vol.57 , Issue.4 , pp. 767-774
    • Kehr, J.1
  • 171
    • 48949120136 scopus 로고    scopus 로고
    • Arthropod-inducible proteins: Broad spectrum defenses against multiple herbivores
    • Zhu-Salzman, K.; Luthe, D.S. and Felton, G.W. Arthropod-inducible proteins: broad spectrum defenses against multiple herbivores. Plant Physiol., 2008, 146(3), 852-858.
    • (2008) Plant Physiol , vol.146 , Issue.3 , pp. 852-858
    • Zhu-Salzman, K.1    Luthe, D.S.2    Felton, G.W.3
  • 172
    • 48949120135 scopus 로고    scopus 로고
    • Why does herbivore attack reconfigure primary metabolism?
    • Schwachtje, J. and Baldwin, I.T. Why does herbivore attack reconfigure primary metabolism? Plant Physiol., 2008, 146(3), 845-851.
    • (2008) Plant Physiol , vol.146 , Issue.3 , pp. 845-851
    • Schwachtje, J.1    Baldwin, I.T.2
  • 173
    • 70449363862 scopus 로고    scopus 로고
    • Poplar defense against insects: Genome analysis, full-length cDNA cloning, and transcriptome and protein analysis of the poplar Kunitz-type protease inhibitor family
    • Philippe, R.N.; Ralph, S.G.; Kulheim, C.; Jancsik, S.I. and Bohl-mann, J. Poplar defense against insects: genome analysis, full-length cDNA cloning, and transcriptome and protein analysis of the poplar Kunitz-type protease inhibitor family. New Phytol., 2009, 184(4), 865-884.
    • (2009) New Phytol , vol.184 , Issue.4 , pp. 865-884
    • Philippe, R.N.1    Ralph, S.G.2    Kulheim, C.3    Jancsik, S.I.4    Bohl-Mann, J.5
  • 175
    • 77649194646 scopus 로고    scopus 로고
    • Genetically engineered virus-resistant plants in developing countries: Current status and future prospects
    • Reddy, D.V.; Sudarshana, M.R.; Fuchs, M.; Rao, N.C. and Thot-tappilly, G. Genetically engineered virus-resistant plants in developing countries: current status and future prospects. Adv. Virus Res., 2009, 75, 185-220.
    • (2009) Adv. Virus Res , vol.75 , pp. 185-220
    • Reddy, D.V.1    Sudarshana, M.R.2    Fuchs, M.3    Rao, N.C.4    Thot-Tappilly, G.5
  • 176
    • 64149117554 scopus 로고    scopus 로고
    • Seed, soil and vegetative transmission contribute to the spread of pecluviruses in Western Africa and the Indian subcontinent
    • Dieryck, B.; Otto, G.; Doucet, D.; Legreve, A.; Delfosse, P. and Bragard, C. Seed, soil and vegetative transmission contribute to the spread of pecluviruses in Western Africa and the Indian subcontinent. Virus Res., 2009, 141(2), 184-189.
    • (2009) Virus Res , vol.141 , Issue.2 , pp. 184-189
    • Dieryck, B.1    Otto, G.2    Doucet, D.3    Legreve, A.4    Delfosse, P.5    Bragard, C.6
  • 177
    • 4744365812 scopus 로고    scopus 로고
    • Molecular aspects of plant virus transmission by olpidium and plasmodio-phorid vectors
    • Rochon, D.; Kakani, K.; Robbins, M. and Reade, R. Molecular aspects of plant virus transmission by olpidium and plasmodio-phorid vectors. Annu. Rev. Phytopathol., 2004, 42, 211-241.
    • (2004) Annu. Rev. Phytopathol , vol.42 , pp. 211-241
    • Rochon, D.1    Kakani, K.2    Robbins, M.3    Reade, R.4
  • 178
    • 33847066702 scopus 로고    scopus 로고
    • Plasmodesmata and intercellular transport of viral RNA
    • Hofmann, C.; Sambade, A. and 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.1 , pp. 142-145
    • Hofmann, C.1    Sambade, A.2    Heinlein, M.3
  • 179
    • 56149089390 scopus 로고    scopus 로고
    • Transport of TMV movement protein particles associated with the targeting of RNA to plasmodesmata
    • Sambade, A.; Brandner, K.; Hofmann, C.; Seemanpillai, M.; Mut-terer, J. and Heinlein, M. Transport of TMV movement protein particles associated with the targeting of RNA to plasmodesmata. Traffic, 2008, 9(12), 2073-2088.
    • (2008) Traffic , vol.9 , Issue.12 , pp. 2073-2088
    • Sambade, A.1    Brandner, K.2    Hofmann, C.3    Seemanpillai, M.4    Mut-Terer, J.5    Heinlein, M.6
  • 183
    • 4644242349 scopus 로고    scopus 로고
    • RNA silencing in plants
    • Baulcombe, D. RNA silencing in plants. Nature, 2004, 431(7006), 356-363.
    • (2004) Nature , vol.431 , Issue.7006 , pp. 356-363
    • Baulcombe, D.1
  • 184
  • 185
    • 77649212984 scopus 로고    scopus 로고
    • Toward a quarter century of pathogen-derived resistance and practical approaches to plant virus disease control
    • Gottula, J. and Fuchs, M. Toward a quarter century of pathogen-derived resistance and practical approaches to plant virus disease control. Adv. Virus Res., 2009, 75, 161-183.
    • (2009) Adv. Virus Res , vol.75 , pp. 161-183
    • Gottula, J.1    Fuchs, M.2
  • 187
    • 1242294383 scopus 로고    scopus 로고
    • Proteomic analysis of the oxygen-evolving complex of photosystem II under biotec stress: Studies on Nicotiana benthami-ana infected with tobamoviruses
    • Perez-Bueno, M.L.; Rahoutei, J.; Sajnani, C.; Garcia-Luque, I. and Baron, M. Proteomic analysis of the oxygen-evolving complex of photosystem II under biotec stress: Studies on Nicotiana benthami-ana infected with tobamoviruses. Proteomics, 2004, 4(2), 418-425.
    • (2004) Proteomics , vol.4 , Issue.2 , pp. 418-425
    • Perez-Bueno, M.L.1    Rahoutei, J.2    Sajnani, C.3    Garcia-Luque, I.4    Baron, M.5
  • 188
    • 0942297973 scopus 로고    scopus 로고
    • Proteome analysis of cultivar-specific deregulations of Oryza sativa indica and O. sativa japon-ica cellular suspensions undergoing rice yellow mottle virus infection
    • Ventelon-Debout, M.; Delalande, F.; Brizard, J.P.; Diemer, H.; Van Dorsselaer, A. and Brugidou, C. Proteome analysis of cultivar-specific deregulations of Oryza sativa indica and O. sativa japon-ica cellular suspensions undergoing rice yellow mottle virus infection. Proteomics, 2004, 4(1), 216-225.
    • (2004) Proteomics , vol.4 , Issue.1 , pp. 216-225
    • Ventelon-Debout, M.1    Delalande, F.2    Brizard, J.P.3    Diemer, H.4    van Dorsselaer, A.5    Brugidou, C.6
  • 189
    • 76149127653 scopus 로고    scopus 로고
    • Changes induced by the Pepper mild mottle tobamovirus on the chloroplast proteome of Nicotiana benthamiana
    • Pineda, M.; Sajnani, C. and Baron, M. Changes induced by the Pepper mild mottle tobamovirus on the chloroplast proteome of Nicotiana benthamiana. Photosynth. Res., 2010, 103(1), 31-45.
    • (2010) Photosynth. Res , vol.103 , Issue.1 , pp. 31-45
    • Pineda, M.1    Sajnani, C.2    Baron, M.3
  • 191
    • 37149031663 scopus 로고    scopus 로고
    • Viral proteomics: Global evaluation of viruses and their interaction with the host
    • Viswanathan, K. and Fruh, K. Viral proteomics: global evaluation of viruses and their interaction with the host. Expert Rev. Pro-teomics, 2007, 4(6), 815-829.
    • (2007) Expert Rev. Pro-teomics , vol.4 , Issue.6 , pp. 815-829
    • Viswanathan, K.1    Fruh, K.2
  • 192
    • 49449105359 scopus 로고    scopus 로고
    • Nico-tiana benthamiana: Its history and future as a model for plant-pathogen interactions
    • Goodin, M.M.; Zaitlin, D.; Naidu, R.A. and Lommel, S.A. Nico-tiana benthamiana: its history and future as a model for plant-pathogen interactions. Mol. Plant Microbe Interact., 2008, 21(8), 1015-1026.
    • (2008) Mol. Plant Microbe Interact , vol.21 , Issue.8 , pp. 1015-1026
    • Goodin, M.M.1    Zaitlin, D.2    Naidu, R.A.3    Lommel, S.A.4
  • 193
    • 67849097553 scopus 로고    scopus 로고
    • A model system for plant-virus interaction-infectivity and seed transmission of Cherry leaf roll virus (CLRV) in Arabidopsis thaliana
    • Rumbou, A.; von Bargen, S. and Büttner, C. A model system for plant-virus interaction-infectivity and seed transmission of Cherry leaf roll virus (CLRV) in Arabidopsis thaliana. Eur. J. Plant Path., 2009, 124(3), 527-532.
    • (2009) Eur. J. Plant Path , vol.124 , Issue.3 , pp. 527-532
    • Rumbou, A.1    von Bargen, S.2    Büttner, C.3
  • 194
    • 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
  • 195
    • 77649219275 scopus 로고    scopus 로고
    • Inhibition of sterol biosyn thesis reduces tombusvirus replication in yeast and plants
    • Sharma, M.; Sasvari, Z. and Nagy, P.D. Inhibition of sterol biosyn thesis reduces tombusvirus replication in yeast and plants. J. Virol., 2010, 84(5), 2270-2281.
    • (2010) J. Virol , vol.84 , Issue.5 , pp. 2270-2281
    • Sharma, M.1    Sasvari, Z.2    Nagy, P.D.3
  • 196
    • 67649886956 scopus 로고    scopus 로고
    • Replication of Tomato bushy stunt virus RNA in a plant in vitro system
    • Gursinsky, T.; Schulz, B. and Behrens, S.E. Replication of Tomato bushy stunt virus RNA in a plant in vitro system. Virology, 2009, 390(2), 250-260.
    • (2009) Virology , vol.390 , Issue.2 , pp. 250-260
    • Gursinsky, T.1    Schulz, B.2    Behrens, S.E.3
  • 197
    • 34548461256 scopus 로고    scopus 로고
    • Subcellular shotgun proteomics in plants: Looking beyond the usual suspects
    • Haynes, P.A. and Roberts, T.H. Subcellular shotgun proteomics in plants: looking beyond the usual suspects. Proteomics, 2007, 7(16), 2963-2975.
    • (2007) Proteomics , vol.7 , Issue.16 , pp. 2963-2975
    • Haynes, P.A.1    Roberts, T.H.2
  • 199
    • 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. Proteome analysis of plant-virus interactome: comprehensive data for virus multiplication inside their hosts. Mol. Cell Proteomics, 2006, 5(12), 2279-2297.
    • (2006) Mol. Cell Proteomics , vol.5 , Issue.12 , pp. 2279-2297
    • Brizard, J.P.1    Carapito, C.2    Delalande, F.3    van Dorsselaer, A.4    Brugidou, C.5
  • 200
    • 43249130010 scopus 로고    scopus 로고
    • A novel methyl-transferase methylates Cucumber mosaic virus 1a protein and promotes systemic spread
    • Kim, M.J.; Huh, S.U.; Ham, B.K. and Paek K.H. A novel methyl-transferase methylates Cucumber mosaic virus 1a protein and promotes systemic spread. J. Virol., 2008, 82(10), 4823-4833.
    • (2008) J. Virol , vol.82 , Issue.10 , pp. 4823-4833
    • Kim, M.J.1    Huh, S.U.2    Ham, B.K.3    Paek, K.H.4
  • 201
    • 77950944677 scopus 로고    scopus 로고
    • A plastid-targeted heat shock cognate 70kDa protein interacts with the Abutilon mosaic virus movement protein
    • Krenz, B.; Windeisen, V.; Wege, C.; Jeske, H. and Kleinow, T. A plastid-targeted heat shock cognate 70kDa protein interacts with the Abutilon mosaic virus movement protein. Virology, 2010, 401(1), 6-17.
    • (2010) Virology , vol.401 , Issue.1 , pp. 6-17
    • Krenz, B.1    Windeisen, V.2    Wege, C.3    Jeske, H.4    Kleinow, T.5
  • 202
    • 60349095840 scopus 로고    scopus 로고
    • Translation elongation factor 1A is a component of the tombusvirus replicase complex and affects the stability of the p33 replication co-factor
    • Li, Z.; Pogany, J.; Panavas, T.; Xu, K.; Esposito, A.M.; Kinzy, T.G. and Nagy, P.D. Translation elongation factor 1A is a component of the tombusvirus replicase complex and affects the stability of the p33 replication co-factor. Virology, 2009, 385(1), 245-260.
    • (2009) Virology , vol.385 , Issue.1 , pp. 245-260
    • Li, Z.1    Pogany, J.2    Panavas, T.3    Xu, K.4    Esposito, A.M.5    Kinzy, T.G.6    Nagy, P.D.7
  • 203
    • 35148832545 scopus 로고    scopus 로고
    • Microarrays for rapid identification of plant viruses
    • Boonham, N.; Tomlinson, J. and Mumford, R. Microarrays for rapid identification of plant viruses. Annu. Rev. Phytopathol., 2007, 45, 307-328.
    • (2007) Annu. Rev. Phytopathol , vol.45 , pp. 307-328
    • Boonham, N.1    Tomlinson, J.2    Mumford, R.3
  • 204
    • 0036606429 scopus 로고    scopus 로고
    • Mass spectrometry-based proteolytic mapping for rapid virus identification
    • Yao, Z.P.; Demirev, P.A. and Fenselau, C. Mass spectrometry-based proteolytic mapping for rapid virus identification. Anal. Chem., 2002, 74(11), 2529-2534.
    • (2002) Anal. Chem , vol.74 , Issue.11 , pp. 2529-2534
    • Yao, Z.P.1    Demirev, P.A.2    Fenselau, C.3
  • 205
    • 33846240849 scopus 로고    scopus 로고
    • Analysis of a model virus using residue-specific chemical cleavage and MALDI-TOF mass spectrometry
    • Swatkoski, S.; Russell, S.; Edwards, N. and Fenselau, C. Analysis of a model virus using residue-specific chemical cleavage and MALDI-TOF mass spectrometry. Anal. Chem., 2007, 79(2), 654-658.
    • (2007) Anal. Chem , vol.79 , Issue.2 , pp. 654-658
    • Swatkoski, S.1    Russell, S.2    Edwards, N.3    Fenselau, C.4
  • 206
    • 0038488181 scopus 로고    scopus 로고
    • Investigative proteomics: Identification of an unknown plant virus from infected plants using mass spectrometry
    • Cooper, B.; Eckert, D.; Andon, N.L.; Yates, J.R. and Haynes, P.A. Investigative proteomics: identification of an unknown plant virus from infected plants using mass spectrometry. J. Am. Soc. Mass Spectrom., 2003, 14(7), 736-741.
    • (2003) J. Am. Soc. Mass Spectrom , vol.14 , Issue.7 , pp. 736-741
    • Cooper, B.1    Eckert, D.2    Andon, N.L.3    Yates, J.R.4    Haynes, P.A.5
  • 207
    • 70849135639 scopus 로고    scopus 로고
    • A generic method to identify plant viruses by high-resolution tandem mass spec-trometry of their coat proteins
    • Blouin, A.G.; Greenwood, D.R.; Chavan, R.R.; Pearson, M.N.; Clover, G.R.; MacDiarmid, R.M. and Cohen, D. A generic method to identify plant viruses by high-resolution tandem mass spec-trometry of their coat proteins. J. Virol. Methods, 2010, 163(1), 49-56.
    • (2010) J. Virol. Methods , vol.163 , Issue.1 , pp. 49-56
    • Blouin, A.G.1    Greenwood, D.R.2    Chavan, R.R.3    Pearson, M.N.4    Clover, G.R.5    Macdiarmid, R.M.6    Cohen, D.7
  • 208
    • 77951025400 scopus 로고    scopus 로고
    • Identification of plant viruses using one-dimensional gel electrophoresis and peptide mass fingerprinting
    • Luo, H.; Wylie, S.J. and Jones, M.G.K. Identification of plant viruses using one-dimensional gel electrophoresis and peptide mass fingerprinting. J. Virol. Methods, 2010, 165(2), 397-401.
    • (2010) J. Virol. Methods , vol.165 , Issue.2 , pp. 397-401
    • Luo, H.1    Wylie, S.J.2    Jones, M.G.K.3
  • 209
    • 1042289393 scopus 로고    scopus 로고
    • Polyga-lacturonases, polygalacturonase-inhibiting proteins and pectic oli-gomers in plant-pathogen interactions
    • D'Ovidio, R.; Mattei, B.; Roberti, S. and Bellincampi, D. Polyga-lacturonases, polygalacturonase-inhibiting proteins and pectic oli-gomers in plant-pathogen interactions. Biochim. Biophys. Acta, 2004, 1696(2), 237-244.
    • (2004) Biochim. Biophys. Acta , vol.1696 , Issue.2 , pp. 237-244
    • D'ovidio, R.1    Mattei, B.2    Roberti, S.3    Bellincampi, D.4
  • 210
    • 74849135697 scopus 로고    scopus 로고
    • Proteomics of the response of Arabidopsis thaliana to infection with Alternaria brassicicola
    • Mukherjee, A.K.; Carp, M.J.; Zuchman, R.; Ziv, T.; Horwitz, B.A. and Gepstein, S. Proteomics of the response of Arabidopsis thaliana to infection with Alternaria brassicicola. J. Proteomics, 2010, 73(4), 709-720.
    • (2010) J. Proteomics , vol.73 , Issue.4 , pp. 709-720
    • Mukherjee, A.K.1    Carp, M.J.2    Zuchman, R.3    Ziv, T.4    Horwitz, B.A.5    Gepstein, S.6
  • 211
    • 33748337522 scopus 로고    scopus 로고
    • Proteomic and genetic approaches to identifying defence-related proteins in rice challenged with the fungal pathogen Rhizoctonia solani
    • Lee, J.; Bricker, T.M.; Lefevre, M.; Pinson, S.R. and Oard J.H. Proteomic and genetic approaches to identifying defence-related proteins in rice challenged with the fungal pathogen Rhizoctonia solani. Mol. Plant Pathol., 2006, 7(5), 405-416.
    • (2006) Mol. Plant Pathol , vol.7 , Issue.5 , pp. 405-416
    • Lee, J.1    Bricker, T.M.2    Lefevre, M.3    Pinson, S.R.4    Oard, J.H.5
  • 212
    • 41849098566 scopus 로고    scopus 로고
    • Proteome changes in leaves of Brassica napus L. as a result of Sclerotinia sclerotiorum challenge
    • Liang, Y.; Srivastava, S.; Rahman, M.H.; Strelkov, S.E. and Kav, N.N. Proteome changes in leaves of Brassica napus L. as a result of Sclerotinia sclerotiorum challenge. J. Agric. Food Chem., 2008, 56(6), 1963-1976.
    • (2008) J. Agric. Food Chem , vol.56 , Issue.6 , pp. 1963-1976
    • Liang, Y.1    Srivastava, S.2    Rahman, M.H.3    Strelkov, S.E.4    Kav, N.N.5
  • 213
    • 68549089150 scopus 로고    scopus 로고
    • Comparative proteomic analysis of responses to pathogen infection and wounding in Fagus sylvatica
    • Valcu, C.M.; Junqueira, M.; Shevchenko, A. and Schlink, K. Comparative proteomic analysis of responses to pathogen infection and wounding in Fagus sylvatica. J. Proteome Res., 2009, 8(8), 4077-4091.
    • (2009) J. Proteome Res , vol.8 , Issue.8 , pp. 4077-4091
    • Valcu, C.M.1    Junqueira, M.2    Shevchenko, A.3    Schlink, K.4
  • 214
    • 33646113170 scopus 로고    scopus 로고
    • Black Point is associated with reduced levels of stress, disease-and defence-related proteins in wheat grain
    • Mak, Y.; Willows, R.D.; Roberts, T.H.; Wrigley, C.W.; Sharp, P.J. and Copeland, L. Black Point is associated with reduced levels of stress, disease-and defence-related proteins in wheat grain. Mol. Plant Pathol., 2006, 7(3), 177-189.
    • (2006) Mol. Plant Pathol , vol.7 , Issue.3 , pp. 177-189
    • Mak, Y.1    Willows, R.D.2    Roberts, T.H.3    Wrigley, C.W.4    Sharp, P.J.5    Copeland, L.6
  • 215
    • 12744281106 scopus 로고    scopus 로고
    • Proteomic approach: Identification of Medicago truncatula proteins induced in roots after infection with the pathogenic oomycete Aphanomyces euteiches
    • Colditz, F.; Nyamsuren, O.; Niehaus, K.; Eubel, H.; Braun, H.P. and Krajinski, F. Proteomic approach: identification of Medicago truncatula proteins induced in roots after infection with the pathogenic oomycete Aphanomyces euteiches. Plant Mol. Biol., 2004, 55(1), 109-120.
    • (2004) Plant Mol. Biol , vol.55 , Issue.1 , pp. 109-120
    • Colditz, F.1    Nyamsuren, O.2    Niehaus, K.3    Eubel, H.4    Braun, H.P.5    Krajinski, F.6
  • 216
    • 1242294378 scopus 로고    scopus 로고
    • The defense response of germinating maize embryos against fungal infection: A proteomics approach
    • Campo, S.; Carrascal, M.; Coca, M.; Abian, J. and San, S.B. The defense response of germinating maize embryos against fungal infection: a proteomics approach. Proteomics, 2004, 4(2), 383-396.
    • (2004) Proteomics , vol.4 , Issue.2 , pp. 383-396
    • Campo, S.1    Carrascal, M.2    Coca, M.3    Abian, J.4    San, S.B.5
  • 217
    • 33645470420 scopus 로고    scopus 로고
    • Analysis of the wheat and Puccinia triticina (leaf rust) proteo-mes during a susceptible host-pathogen interaction
    • Rampitsch, C.; Bykova, N.V.; McCallum, B.; Beimcik, E. and Ens, W. Analysis of the wheat and Puccinia triticina (leaf rust) proteo-mes during a susceptible host-pathogen interaction. Proteomics, 2006, 6(6), 1897-1907.
    • (2006) Proteomics , vol.6 , Issue.6 , pp. 1897-1907
    • Rampitsch, C.1    Bykova, N.V.2    McCallum, B.3    Beimcik, E.4    Ens, W.5
  • 218
    • 52649130307 scopus 로고    scopus 로고
    • Towards identifying Brassica proteins involved in mediating resistance to Leptosphaeria maculans: A pro-teomics-based approach
    • Sharma, N.; Hotte, N.; Rahman, M.H.; Mohammadi, M.; Deyholos, M.K. and Kav, N.N. Towards identifying Brassica proteins involved in mediating resistance to Leptosphaeria maculans: a pro-teomics-based approach. Proteomics, 2008, 8(17), 3516-3535.
    • (2008) Proteomics , vol.8 , Issue.17 , pp. 3516-3535
    • Sharma, N.1    Hotte, N.2    Rahman, M.H.3    Mohammadi, M.4    Deyholos, M.K.5    Kav, N.N.6
  • 219
    • 0346256836 scopus 로고    scopus 로고
    • Proteomic analysis of differentially expressed proteins induced by rice blast fungus and elicitor in suspension-cultured rice cells
    • Kim, S.T.; Cho, K.S.; Yu, S.; Kim, S.G.; Hong, J.C.; Han, C.D.; Bae, D.W.; Nam, M.H. and Kang, K.Y. Proteomic analysis of differentially expressed proteins induced by rice blast fungus and elicitor in suspension-cultured rice cells. Proteomics, 2003, 3(12), 2368-2378.
    • (2003) Proteomics , vol.3 , Issue.12 , pp. 2368-2378
    • Kim, S.T.1    Cho, K.S.2    Yu, S.3    Kim, S.G.4    Hong, J.C.5    Han, C.D.6    Bae, D.W.7    Nam, M.H.8    Kang, K.Y.9
  • 220
    • 36049044826 scopus 로고    scopus 로고
    • Proteome, salicylic acid, and jasmonic acid changes in cucumber plants inoculated with Trichoderma asperellum strain T34
    • Segarra, G.; Casanova, E.; Bellido, D.; Odena, M.A.; Oliveira, E. and Trillas, I. Proteome, salicylic acid, and jasmonic acid changes in cucumber plants inoculated with Trichoderma asperellum strain T34. Proteomics, 2007, 7(21), 3943-3952.
    • (2007) Proteomics , vol.7 , Issue.21 , pp. 3943-3952
    • Segarra, G.1    Casanova, E.2    Bellido, D.3    Odena, M.A.4    Oliveira, E.5    Trillas, I.6
  • 221
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • Hueck, C.J. Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol. Mol. Biol. Rev., 1998, 62(2), 379-433.
    • (1998) Microbiol. Mol. Biol. Rev , vol.62 , Issue.2 , pp. 379-433
    • Hueck, C.J.1
  • 222
    • 1842456892 scopus 로고    scopus 로고
    • The versatile bacterial type IV secretion systems
    • Cascales, E. and Christie, P.J. The versatile bacterial type IV secretion systems. Nat. Rev. Microbiol., 2003, 1(2), 137-149.
    • (2003) Nat. Rev. Microbiol , vol.1 , Issue.2 , pp. 137-149
    • Cascales, E.1    Christie, P.J.2
  • 223
    • 1942520270 scopus 로고    scopus 로고
    • Bacterial disease resistance in Arabidopsis through flagellin perception
    • Zipfel, C.; Robatzek, S.; Navarro, L.; Oakeley, E.J.; Jones, J.D.; Felix, G. and Boller, T. Bacterial disease resistance in Arabidopsis through flagellin perception. Nature, 2004, 428(6984), 764-767.
    • (2004) Nature , vol.428 , Issue.6984 , pp. 764-767
    • Zipfel, C.1    Robatzek, S.2    Navarro, L.3    Oakeley, E.J.4    Jones, J.D.5    Felix, G.6    Boller, T.7
  • 225
    • 27944495990 scopus 로고    scopus 로고
    • Membrane release and destabiliza-tion of Arabidopsis RIN4 following cleavage by Pseudomonas sy-ringae AvrRpt2
    • Takemoto, D. and Jones, D.A. Membrane release and destabiliza-tion of Arabidopsis RIN4 following cleavage by Pseudomonas sy-ringae AvrRpt2. Mol. Plant Microbe Interact., 2005, 18(12), 1258-1268.
    • (2005) Mol. Plant Microbe Interact , vol.18 , Issue.12 , pp. 1258-1268
    • Takemoto, D.1    Jones, D.A.2
  • 226
    • 0037155687 scopus 로고    scopus 로고
    • RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis
    • Mackey, D.; Holt, B.F. III; Wiig, A. and Dangl, J.L. RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis. Cell, 2002, 108(6), 743-754.
    • (2002) Cell , vol.108 , Issue.6 , pp. 743-754
    • Mackey, D.1    Holt, B.F.2    Wiig, A.3    Dangl, J.L.4
  • 227
    • 70350731306 scopus 로고    scopus 로고
    • Identification of bacterial protein markers and enolase as a plant response protein in the infection of Olea europaea subsp. europaea by Pseu-domonas savastanoi pv. savastanoi
    • Campos, A.; da Costa, G.; Coelho, A.V. and Fevereiro, P. Identification of bacterial protein markers and enolase as a plant response protein in the infection of Olea europaea subsp. europaea by Pseu-domonas savastanoi pv. savastanoi. Eur. J. Plant Pathol., 2009, 125(4), 603-616.
    • (2009) Eur. J. Plant Pathol , vol.125 , Issue.4 , pp. 603-616
    • Campos, A.1    da Costa, G.2    Coelho, A.V.3    Fevereiro, P.4
  • 228
    • 67649199017 scopus 로고    scopus 로고
    • Priming, signaling, and protein production associated with induced resistance by Bacillus amyloliquefaciens KPS46
    • Buensanteai, N.; Yuen, G.Y. and Prathuangwong, S. Priming, signaling, and protein production associated with induced resistance by Bacillus amyloliquefaciens KPS46. World J. Microbiol. Biotech., 2009, 25(7), 1275-1286.
    • (2009) World J. Microbiol. Biotech , vol.25 , Issue.7 , pp. 1275-1286
    • Buensanteai, N.1    Yuen, G.Y.2    Prathuangwong, S.3
  • 229
    • 3242743833 scopus 로고    scopus 로고
    • Specific changes in the Arabidopsis proteome in response to bacterial challenge: Differentiating basal and R-gene mediated resistance
    • Jones, A.M.; Thomas, V.; Truman, B.; Lilley, K.; Mansfield, J. and Grant, M. Specific changes in the Arabidopsis proteome in response to bacterial challenge: differentiating basal and R-gene mediated resistance. Phytochemistry, 2004, 65(12), 1805-1816.
    • (2004) Phytochemistry , vol.65 , Issue.12 , pp. 1805-1816
    • Jones, A.M.1    Thomas, V.2    Truman, B.3    Lilley, K.4    Mansfield, J.5    Grant, M.6
  • 230
    • 67649484363 scopus 로고    scopus 로고
    • Pathogenesis and stress related, as well as metabolic proteins are regulated in tomato stems infected with Ralstonia solanacearum
    • Dahal, D.; Heintz, D.; Van Dorsselaer, A.; Braun, H.P. and Wydra, K. Pathogenesis and stress related, as well as metabolic proteins are regulated in tomato stems infected with Ralstonia solanacearum. Plant Physiol. Biochem., 2009, 47(9), 838-846.
    • (2009) Plant Physiol. Biochem , vol.47 , Issue.9 , pp. 838-846
    • Dahal, D.1    Heintz, D.2    van Dorsselaer, A.3    Braun, H.P.4    Wydra, K.5
  • 231
    • 85047683656 scopus 로고    scopus 로고
    • Differentially expressed proteins in the interaction of Xanthomonas axonopodis pv. citri with leaf extract of the host plant
    • Mehta, A. and Rosato, Y.B. Differentially expressed proteins in the interaction of Xanthomonas axonopodis pv. citri with leaf extract of the host plant. Proteomics, 2001, 1(9), 1111-1118.
    • (2001) Proteomics , vol.1 , Issue.9 , pp. 1111-1118
    • Mehta, A.1    Rosato, Y.B.2
  • 232
    • 0037251699 scopus 로고    scopus 로고
    • Proteins induced by Xanthomonas axonopodis pv. passiflorae with leaf extract of the host plant (Passiflorae edulis)
    • Tahara, S.T.; Mehta, A. and Rosato, Y.B. Proteins induced by Xanthomonas axonopodis pv. passiflorae with leaf extract of the host plant (Passiflorae edulis). Proteomics, 2003, 3(1), 95-102.
    • (2003) Proteomics , vol.3 , Issue.1 , pp. 95-102
    • Tahara, S.T.1    Mehta, A.2    Rosato, Y.B.3
  • 237
    • 59149088519 scopus 로고    scopus 로고
    • Effector proteins of the bacterial pathogen Pseudomonas syringae alter the extracellular proteome of the host plant, Arabidopsis thaliana
    • Kaffarnik, F.A.; Jones, A.M.; Rathjen, J.P. and Peck, S.C. Effector proteins of the bacterial pathogen Pseudomonas syringae alter the extracellular proteome of the host plant, Arabidopsis thaliana. Mol. Cell Proteomics, 2009, 8(1), 145-156.
    • (2009) Mol. Cell Proteomics , vol.8 , Issue.1 , pp. 145-156
    • Kaffarnik, F.A.1    Jones, A.M.2    Rathjen, J.P.3    Peck, S.C.4
  • 238
    • 3242757613 scopus 로고    scopus 로고
    • A proteomic approach to studying plant response to crenate broomrape (Orobanche crenata) in pea (Pisum sativum)
    • Castillejo, M.A.; Amiour, N.; Dumas-Gaudot, E.; Rubiales, D. and Jorrin-Novo, J.V. A proteomic approach to studying plant response to crenate broomrape (Orobanche crenata) in pea (Pisum sativum). Phytochem., 2004, 65(12), 1817-1828.
    • (2004) Phytochem , vol.65 , Issue.12 , pp. 1817-1828
    • Castillejo, M.A.1    Amiour, N.2    Dumas-Gaudot, E.3    Rubiales, D.4    Jorrin-Novo, J.V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.