메뉴 건너뛰기




Volumn 75, Issue 13, 2012, Pages 4074-4090

Proteomic analysis of strawberry leaves infected with Colletotrichum fragariae

Author keywords

2D gel; Colletotrichum fragariae; Comparative proteomics; Metabolic pathways; Strawberry leaves

Indexed keywords

1,3 BETA GLUCANASE; SMALL HEAT SHOCK PROTEIN;

EID: 84862666790     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.05.022     Document Type: Article
Times cited : (57)

References (76)
  • 1
    • 27644510518 scopus 로고    scopus 로고
    • Genotypic and phenotypic diversity in Colletotrichum acutatum, a cosmopolitan pathogen causing anthracnose on a wide range of hosts
    • Sreenivasaprasad S., Talhinhas P. Genotypic and phenotypic diversity in Colletotrichum acutatum, a cosmopolitan pathogen causing anthracnose on a wide range of hosts. Mol Plant Pathol 2005, 6:361-378.
    • (2005) Mol Plant Pathol , vol.6 , pp. 361-378
    • Sreenivasaprasad, S.1    Talhinhas, P.2
  • 2
    • 0000682021 scopus 로고
    • Taxonomy and morphology of Colletotrichum species pathogenic to strawberry
    • Gunnell P.S., Gubler W.D. Taxonomy and morphology of Colletotrichum species pathogenic to strawberry. Mycologia 1992, 84:157-165.
    • (1992) Mycologia , vol.84 , pp. 157-165
    • Gunnell, P.S.1    Gubler, W.D.2
  • 3
    • 0037302315 scopus 로고    scopus 로고
    • Genetic diversity and pathogenic variability among isolates of Colletotrichum species from strawberry
    • Denoyes-Rothan B., Guérin G., Délye C., Smith B., Minz D., Maymon M. Genetic diversity and pathogenic variability among isolates of Colletotrichum species from strawberry. Phytopathology 2003, 93:219-228.
    • (2003) Phytopathology , vol.93 , pp. 219-228
    • Denoyes-Rothan, B.1    Guérin, G.2    Délye, C.3    Smith, B.4    Minz, D.5    Maymon, M.6
  • 4
    • 0345049161 scopus 로고
    • Production of small fruit in France: importance, main diseases and production of healthy plants
    • Nourrisseau J.G. Production of small fruit in France: importance, main diseases and production of healthy plants. Acta Hortic 1986, 186:97-99.
    • (1986) Acta Hortic , vol.186 , pp. 97-99
    • Nourrisseau, J.G.1
  • 5
    • 0000452049 scopus 로고
    • Disease-free plants for management of strawberry anthracnose crown rot
    • McInnes T.B., Black L.L., Gatti J.M. Disease-free plants for management of strawberry anthracnose crown rot. Plant Dis 1992, 76:260-264.
    • (1992) Plant Dis , vol.76 , pp. 260-264
    • McInnes, T.B.1    Black, L.L.2    Gatti, J.M.3
  • 6
    • 79959996123 scopus 로고    scopus 로고
    • Colletotrichum acutatum interactions with unripe and ripe strawberry fruits and differential responses at histological and transcriptional levels
    • Guidarelli M., Carbone F., Mourgues F., Perrotta G., Rosati C., Bertolini P., et al. Colletotrichum acutatum interactions with unripe and ripe strawberry fruits and differential responses at histological and transcriptional levels. Plant Pathol 2011, 60:685-697.
    • (2011) Plant Pathol , vol.60 , pp. 685-697
    • Guidarelli, M.1    Carbone, F.2    Mourgues, F.3    Perrotta, G.4    Rosati, C.5    Bertolini, P.6
  • 8
    • 33747876243 scopus 로고    scopus 로고
    • Cloning and expression analysis of two β-1,3-glucanase genes from strawberry
    • Yanlin S., Yuhua Z., Ding S. Cloning and expression analysis of two β-1,3-glucanase genes from strawberry. J Plant Physiol 2006, 163:956-967.
    • (2006) J Plant Physiol , vol.163 , pp. 956-967
    • Yanlin, S.1    Yuhua, Z.2    Ding, S.3
  • 9
    • 12344295620 scopus 로고    scopus 로고
    • System, trends and perspectives of proteomics in dicot plants. Part III: unraveling the proteomes influenced by the environment, and at the levels of function and genetic relationships
    • Agrawal G.K., Yonekur M., Iwahash Y., Iwahash H., Rakwal R. System, trends and perspectives of proteomics in dicot plants. Part III: unraveling the proteomes influenced by the environment, and at the levels of function and genetic relationships. J Chromatogr B 2005, 815:137-145.
    • (2005) J Chromatogr B , vol.815 , pp. 137-145
    • Agrawal, G.K.1    Yonekur, M.2    Iwahash, Y.3    Iwahash, H.4    Rakwal, R.5
  • 10
    • 37549053294 scopus 로고    scopus 로고
    • Proteomics studies on plant-pathogen interaction in compatible and incompatible systems
    • Butt Y.K., Lo S.C.L. Proteomics studies on plant-pathogen interaction in compatible and incompatible systems. Curr Proteomics 2007, 4:141-156.
    • (2007) Curr Proteomics , vol.4 , pp. 141-156
    • Butt, Y.K.1    Lo, S.C.L.2
  • 11
    • 0037251699 scopus 로고    scopus 로고
    • Proteins induced by Xanthomonas axonopodis pv. passiflorae with leaf extract of the host plant (Passiflorae edulis)
    • Sandra T., Mehta T.A., Rosato Y.B. Proteins induced by Xanthomonas axonopodis pv. passiflorae with leaf extract of the host plant (Passiflorae edulis). Proteomics 2003, 3:95-102.
    • (2003) Proteomics , vol.3 , pp. 95-102
    • Sandra, T.1    Mehta, T.A.2    Rosato, Y.B.3
  • 12
    • 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., Rosato Y.B. Differentially expressed proteins in the interaction of Xanthomonas axonopodis pv. citri with leaf extract of the host plant. Proteomics 2001, 1:1111-1118.
    • (2001) Proteomics , vol.1 , pp. 1111-1118
    • Mehta, A.1    Rosato, Y.B.2
  • 13
    • 63349086688 scopus 로고    scopus 로고
    • Comparative proteomic studies of root-microbe interactions
    • Mathesius U. Comparative proteomic studies of root-microbe interactions. J Proteomics 2009, 72:353-366.
    • (2009) J Proteomics , vol.72 , pp. 353-366
    • Mathesius, U.1
  • 14
    • 79955827899 scopus 로고    scopus 로고
    • Comparative proteomics analysis of proteins expressed in the I-1 and I-2 internodes of strawberry stolons
    • Xianping F., Huasheng M., Dezhao L., Hong Y., Wenguo L., Ruan Songlin Comparative proteomics analysis of proteins expressed in the I-1 and I-2 internodes of strawberry stolons. Proteome Sci 2011, 9:26.
    • (2011) Proteome Sci , vol.9 , pp. 26
    • Xianping, F.1    Huasheng, M.2    Dezhao, L.3    Hong, Y.4    Wenguo, L.5    Ruan, S.6
  • 15
    • 63649099695 scopus 로고    scopus 로고
    • Strawberry proteome characterization and its regulation during fruit ripening and in different genotypes
    • Bianco L., Lopez L., Scalone A.G., Carli M.D., Desiderio A., Benvenuto E., et al. Strawberry proteome characterization and its regulation during fruit ripening and in different genotypes. J Proteomics 2009, 72:586-607.
    • (2009) J Proteomics , vol.72 , pp. 586-607
    • Bianco, L.1    Lopez, L.2    Scalone, A.G.3    Carli, M.D.4    Desiderio, A.5    Benvenuto, E.6
  • 16
    • 75949115008 scopus 로고    scopus 로고
    • Identification of Colletotrichum spp. isolated from strawberry in Zhejiang Province and Shanghai City, China
    • Liu X., Jingze Z., Yao W., Dongwei H. Identification of Colletotrichum spp. isolated from strawberry in Zhejiang Province and Shanghai City, China. J Zhejiang Univ Sci B 2010, 11:61-70.
    • (2010) J Zhejiang Univ Sci B , vol.11 , pp. 61-70
    • Liu, X.1    Jingze, Z.2    Yao, W.3    Dongwei, H.4
  • 17
    • 84862655487 scopus 로고    scopus 로고
    • Studies on the cold resistance of Cassava
    • Xinglu L., Qiufeng H. Studies on the cold resistance of Cassava. J Agric Sci 2012, 4:104-106.
    • (2012) J Agric Sci , vol.4 , pp. 104-106
    • Xinglu, L.1    Qiufeng, H.2
  • 18
    • 49049133318 scopus 로고
    • Association of enhanced peroxidase activity with induced systemic resistance of cucumber to Colletotrichum lagenarium
    • Hammerschmid T.R., Nuckles E.M., Kuc J. Association of enhanced peroxidase activity with induced systemic resistance of cucumber to Colletotrichum lagenarium. Physiol Plant Pathol 1982, 20:73-82.
    • (1982) Physiol Plant Pathol , vol.20 , pp. 73-82
    • Hammerschmid, T.R.1    Nuckles, E.M.2    Kuc, J.3
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0033662168 scopus 로고    scopus 로고
    • A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry
    • Yan J.X., Wait R., Berkelman T., Harry R.A., Westbrook J.A., Wheeler C.H., et al. A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry. Electrophoresis 2000, 21:3666-3672.
    • (2000) Electrophoresis , vol.21 , pp. 3666-3672
    • Yan, J.X.1    Wait, R.2    Berkelman, T.3    Harry, R.A.4    Westbrook, J.A.5    Wheeler, C.H.6
  • 24
    • 0036728244 scopus 로고    scopus 로고
    • Oxidative stress, antioxidants and stress tolerance
    • Mittler R. Oxidative stress, antioxidants and stress tolerance. Trends Plant Sci 2002, 7:512-546.
    • (2002) Trends Plant Sci , vol.7 , pp. 512-546
    • Mittler, R.1
  • 25
    • 9644278424 scopus 로고    scopus 로고
    • Significance of subnuclear localization of key players of inositol lipid cycle
    • Cocco L., Manzoli L., Barnabei O., Martelli A.M. Significance of subnuclear localization of key players of inositol lipid cycle. Adv Enzyme Regul 2004, 44:51-60.
    • (2004) Adv Enzyme Regul , vol.44 , pp. 51-60
    • Cocco, L.1    Manzoli, L.2    Barnabei, O.3    Martelli, A.M.4
  • 26
    • 33846990139 scopus 로고    scopus 로고
    • Nuclear localization is required for dishevelled function in wnt/beta-catenin signaling
    • Itoh K., Brott B.K., Bae G.U., Ratcliffe M.J., Sokol S.Y. Nuclear localization is required for dishevelled function in wnt/beta-catenin signaling. J Biol 2005, 4:3.
    • (2005) J Biol , vol.4 , pp. 3
    • Itoh, K.1    Brott, B.K.2    Bae, G.U.3    Ratcliffe, M.J.4    Sokol, S.Y.5
  • 27
    • 3142779931 scopus 로고    scopus 로고
    • Prediction of protein subcellular locations by GO-FunD-PseAA predictor
    • Chou K., Cai Y. Prediction of protein subcellular locations by GO-FunD-PseAA predictor. Biochem Biophys Res Commun 2004, 320:1236-1239.
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 1236-1239
    • Chou, K.1    Cai, Y.2
  • 28
    • 33751393465 scopus 로고    scopus 로고
    • Assessing protein similarity with gene ontology and its use in subnuclear localization prediction
    • Lei Z., Dai Y. Assessing protein similarity with gene ontology and its use in subnuclear localization prediction. BMC Bioinf 2006, 7:491.
    • (2006) BMC Bioinf , vol.7 , pp. 491
    • Lei, Z.1    Dai, Y.2
  • 29
    • 70349728612 scopus 로고    scopus 로고
    • MultiLoc2: integrating phylogeny and gene ontology terms improves subcellular protein localization prediction
    • Blum T., Briesemeister S., Kohlbacher O. MultiLoc2: integrating phylogeny and gene ontology terms improves subcellular protein localization prediction. BMC Bioinf 2009, 10:274.
    • (2009) BMC Bioinf , vol.10 , pp. 274
    • Blum, T.1    Briesemeister, S.2    Kohlbacher, O.3
  • 30
    • 70449428562 scopus 로고    scopus 로고
    • SherLoc2: a high-accuracy hybrid method for predicting subcellular localization of proteins
    • Briesemeister S., Blum T., Brady S. SherLoc2: a high-accuracy hybrid method for predicting subcellular localization of proteins. J Proteome Res 2009, 8:5363-5366.
    • (2009) J Proteome Res , vol.8 , pp. 5363-5366
    • Briesemeister, S.1    Blum, T.2    Brady, S.3
  • 31
    • 40249110012 scopus 로고    scopus 로고
    • ProLoc-GO: utilizing informative gene ontology terms for sequence-based prediction of protein subcellular localization
    • Huang W.L., Tung C.W., Ho S.W. ProLoc-GO: utilizing informative gene ontology terms for sequence-based prediction of protein subcellular localization. BMC Bioinf 2008, 9:80.
    • (2008) BMC Bioinf , vol.9 , pp. 80
    • Huang, W.L.1    Tung, C.W.2    Ho, S.W.3
  • 32
    • 0034987772 scopus 로고    scopus 로고
    • Challenges and prospects of plant proteomics
    • Van-Wijk K.J. Challenges and prospects of plant proteomics. Plant Physiol 2001, 126:501-508.
    • (2001) Plant Physiol , vol.126 , pp. 501-508
    • Van-Wijk, K.J.1
  • 33
    • 58949085660 scopus 로고    scopus 로고
    • Chapter 3 genome evolution in plant pathogenic and symbiotic fungi
    • Aguileta G., Hood M.E., Refrégier G., Giraud T. Chapter 3 genome evolution in plant pathogenic and symbiotic fungi. Adv Bot Res 2009, 49:151-193.
    • (2009) Adv Bot Res , vol.49 , pp. 151-193
    • Aguileta, G.1    Hood, M.E.2    Refrégier, G.3    Giraud, T.4
  • 34
    • 0034904236 scopus 로고    scopus 로고
    • Cytology of fungal pathogens and plant-host interactions
    • Howard R.J. Cytology of fungal pathogens and plant-host interactions. Curr Opin Microbiol 2001, 4:365-373.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 365-373
    • Howard, R.J.1
  • 35
    • 33745209410 scopus 로고    scopus 로고
    • Show and tell: cell biology of pathogen invasion
    • Koh S., Somerville S. Show and tell: cell biology of pathogen invasion. Curr Opin Plant Biol 2006, 9:406-413.
    • (2006) Curr Opin Plant Biol , vol.9 , pp. 406-413
    • Koh, S.1    Somerville, S.2
  • 36
    • 2442568469 scopus 로고    scopus 로고
    • Cell wall analysis
    • Pérez P., Ribas J.C. Cell wall analysis. Methods 2004, 33:245-251.
    • (2004) Methods , vol.33 , pp. 245-251
    • Pérez, P.1    Ribas, J.C.2
  • 38
    • 33746388765 scopus 로고    scopus 로고
    • Fundamentals of fungal molecular population genetic analyses
    • Xu J. Fundamentals of fungal molecular population genetic analyses. Curr Issues Mol Biol 2006, 8:75-89.
    • (2006) Curr Issues Mol Biol , vol.8 , pp. 75-89
    • Xu, J.1
  • 39
    • 84855552180 scopus 로고    scopus 로고
    • Contribution of proteomics to the study of plant pathogenic fungi
    • Raquel G.F., Jesus J.N. Contribution of proteomics to the study of plant pathogenic fungi. J Proteome Res 2012, 11:3-16.
    • (2012) J Proteome Res , vol.11 , pp. 3-16
    • Raquel, G.F.1    Jesus, J.N.2
  • 40
    • 84855877000 scopus 로고    scopus 로고
    • Proteomic analysis of the compatible interaction between Vitis vinifera and Plasmopara viticola
    • Milli A., Cecconi D., Bortesi L., Persi A., Rinalducci S., Zamboni A., et al. Proteomic analysis of the compatible interaction between Vitis vinifera and Plasmopara viticola. J Proteomics 2012, 75:1284-1302.
    • (2012) J Proteomics , vol.75 , pp. 1284-1302
    • Milli, A.1    Cecconi, D.2    Bortesi, L.3    Persi, A.4    Rinalducci, S.5    Zamboni, A.6
  • 42
    • 0034823959 scopus 로고    scopus 로고
    • Inhibition of photosynthesis by Colletotrichum lindemuthianum in bean leaves determined by chlorophyll fluorescence imaging
    • Meyer S., Saccardy-Adji K., Rizza F., Genty B. Inhibition of photosynthesis by Colletotrichum lindemuthianum in bean leaves determined by chlorophyll fluorescence imaging. Plant Cell Environ 2001, 24:947-956.
    • (2001) Plant Cell Environ , vol.24 , pp. 947-956
    • Meyer, S.1    Saccardy-Adji, K.2    Rizza, F.3    Genty, B.4
  • 43
    • 0242540444 scopus 로고    scopus 로고
    • Relative tolerance of wild and cultivated barley to infection by Blumeria graminis f.sp. hordei (syn. Erysiphe graminis f.sp. hordei). II - The effects of infection on photosynthesis and respiration
    • Akhkha A., Clarke D.D., Dominy P.J. Relative tolerance of wild and cultivated barley to infection by Blumeria graminis f.sp. hordei (syn. Erysiphe graminis f.sp. hordei). II - The effects of infection on photosynthesis and respiration. Physiol Mol Plant Pathol 2003, 62:347-354.
    • (2003) Physiol Mol Plant Pathol , vol.62 , pp. 347-354
    • Akhkha, A.1    Clarke, D.D.2    Dominy, P.J.3
  • 44
    • 0001066127 scopus 로고
    • 2 fixation and light utilization by sugar beet leaves
    • 2 fixation and light utilization by sugar beet leaves. Plant Physiol 1982, 69:139-142.
    • (1982) Plant Physiol , vol.69 , pp. 139-142
    • Gordon, T.R.1    Duniway, J.M.2
  • 45
    • 0001234216 scopus 로고
    • 2 assimilation in barley infected by powdery mildew Erysiphe graminis hordei
    • 2 assimilation in barley infected by powdery mildew Erysiphe graminis hordei. J Phytopathol 1984, 109:208-218.
    • (1984) J Phytopathol , vol.109 , pp. 208-218
    • Waters, D.R.1    Ayres, P.G.2
  • 46
    • 33646562521 scopus 로고    scopus 로고
    • Metabolic consequences of susceptibility and resistance (race-specific and broad-spectrum) in barley leaves challenged with powdery mildew
    • Swarbrick P.J., Schulze-Lefert P., Scholes J.D. Metabolic consequences of susceptibility and resistance (race-specific and broad-spectrum) in barley leaves challenged with powdery mildew. Plant Cell Environ 2006, 29:1061-1076.
    • (2006) Plant Cell Environ , vol.29 , pp. 1061-1076
    • Swarbrick, P.J.1    Schulze-Lefert, P.2    Scholes, J.D.3
  • 47
    • 0038120061 scopus 로고    scopus 로고
    • The monosaccharide transporter gene, AtSTP4, and the cell-wall invertase, Atbfruct1, are induced in Arabidopsis during infection with the fungal biotroph Erysiphe cichoracearum
    • Fotopoulos V., Gilbert M.J., Pittman J.K., Marvier A.C., Buchanan A.J., Sauer N. The monosaccharide transporter gene, AtSTP4, and the cell-wall invertase, Atbfruct1, are induced in Arabidopsis during infection with the fungal biotroph Erysiphe cichoracearum. Plant Physiol 2003, 132:821-829.
    • (2003) Plant Physiol , vol.132 , pp. 821-829
    • Fotopoulos, V.1    Gilbert, M.J.2    Pittman, J.K.3    Marvier, A.C.4    Buchanan, A.J.5    Sauer, N.6
  • 48
    • 0010472748 scopus 로고
    • The physiology of host-parasite relations. III. The pattern of respiration in rusted & mildewed cereal leaves
    • Shaw M., Samborskid D.J. The physiology of host-parasite relations. III. The pattern of respiration in rusted & mildewed cereal leaves. Can J Bot 1957, 35:389-407.
    • (1957) Can J Bot , vol.35 , pp. 389-407
    • Shaw, M.1    Samborskid, D.J.2
  • 49
    • 79960284373 scopus 로고    scopus 로고
    • Alcohol dehydrogenase 1 of barley modulates susceptibility to the parasitic fungus Blumeria graminis f.sp. hordei
    • Indira P.P., Ines E.R., Ralph H., Reinhard K.P. Alcohol dehydrogenase 1 of barley modulates susceptibility to the parasitic fungus Blumeria graminis f.sp. hordei. J Exp Bot 2011, 62:3449-3457.
    • (2011) J Exp Bot , vol.62 , pp. 3449-3457
    • Indira, P.P.1    Ines, E.R.2    Ralph, H.3    Reinhard, K.P.4
  • 50
    • 0037004330 scopus 로고    scopus 로고
    • Acclimative response to temperature stress in higher plants: approaches of genetic engineering for temperature tolerance
    • Iba K. Acclimative response to temperature stress in higher plants: approaches of genetic engineering for temperature tolerance. Annu Rev Plant Biol 2002, 53:225-245.
    • (2002) Annu Rev Plant Biol , vol.53 , pp. 225-245
    • Iba, K.1
  • 51
    • 0024418447 scopus 로고    scopus 로고
    • Stress proteins, infection and immune surveillance
    • Young R.A., Elliott T.J. Stress proteins, infection and immune surveillance. Cell 2002, 59:5-8.
    • (2002) Cell , vol.59 , pp. 5-8
    • Young, R.A.1    Elliott, T.J.2
  • 52
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters E.R., Lee G.J., Vierling E. Evolution, structure and function of the small heat shock proteins in plants. J Exp Bot 1996, 47:325-338.
    • (1996) J Exp Bot , vol.47 , pp. 325-338
    • Waters, E.R.1    Lee, G.J.2    Vierling, E.3
  • 53
    • 33749259787 scopus 로고    scopus 로고
    • An Arabidopsis chloroplast targeted Hsp101 homologue, APG6, has an essential role in chloroplast development as well as heat stress response
    • Myouga F., Motohashi R., Kuromori T., Nagata N., Shinozaki K. An Arabidopsis chloroplast targeted Hsp101 homologue, APG6, has an essential role in chloroplast development as well as heat stress response. Plant J 2006, 48:249-260.
    • (2006) Plant J , vol.48 , pp. 249-260
    • Myouga, F.1    Motohashi, R.2    Kuromori, T.3    Nagata, N.4    Shinozaki, K.5
  • 54
    • 2442445139 scopus 로고    scopus 로고
    • Role of plant heat shock proteins and molecular chaperons in the abiotic stress response
    • Wang W., Vinocur B., Shoseyov O., Altman A. Role of plant heat shock proteins and molecular chaperons in the abiotic stress response. Trends Plant Sci 2004, 9:1360-1385.
    • (2004) Trends Plant Sci , vol.9 , pp. 1360-1385
    • Wang, W.1    Vinocur, B.2    Shoseyov, O.3    Altman, A.4
  • 55
    • 0034994714 scopus 로고    scopus 로고
    • Heat shock and stress response of Taenia solium and T. crassiceps
    • Vargas-Parada L., Solis C. Heat shock and stress response of Taenia solium and T. crassiceps. Parasitology 2001, 211:583-588.
    • (2001) Parasitology , vol.211 , pp. 583-588
    • Vargas-Parada, L.1    Solis, C.2
  • 56
    • 33745451171 scopus 로고    scopus 로고
    • Identification and characterization of a stress-inducible and a constitutive small heat-shock protein targeted to the matrix of plant peroxisomes
    • Ma C., Haslbeck M., Babujee L., Jahn O., Reumann S. Identification and characterization of a stress-inducible and a constitutive small heat-shock protein targeted to the matrix of plant peroxisomes. Plant Physiol 2006, 141:47-60.
    • (2006) Plant Physiol , vol.141 , pp. 47-60
    • Ma, C.1    Haslbeck, M.2    Babujee, L.3    Jahn, O.4    Reumann, S.5
  • 57
    • 37249054259 scopus 로고    scopus 로고
    • Induction of a small heat shock protein and its functional roles in Nicotiana plants in the defense response against Ralstonia solanacearum
    • Milimo M., Kouhei O., Yasufumi H., Hirofumi Y., Akinori K. Induction of a small heat shock protein and its functional roles in Nicotiana plants in the defense response against Ralstonia solanacearum. Plant Physiol 2007, 145:1588-1599.
    • (2007) Plant Physiol , vol.145 , pp. 1588-1599
    • Milimo, M.1    Kouhei, O.2    Yasufumi, H.3    Hirofumi, Y.4    Akinori, K.5
  • 58
    • 33845640047 scopus 로고    scopus 로고
    • Modifications to the Arabidopsis defense proteome occur prior to significant transcriptional change in response to inoculation with Pseudomonas syringae
    • Jones A.M., Thomas V., Bennett M.H., Mansfield J., Grant M. Modifications to the Arabidopsis defense proteome occur prior to significant transcriptional change in response to inoculation with Pseudomonas syringae. Plant Physiol 2006, 142:1603-1620.
    • (2006) Plant Physiol , vol.142 , pp. 1603-1620
    • Jones, A.M.1    Thomas, V.2    Bennett, M.H.3    Mansfield, J.4    Grant, M.5
  • 59
    • 33646250437 scopus 로고    scopus 로고
    • Proteomic analysis of differentially expressed proteins in fungal elicitor-treated Arabidopsis cell cultures
    • Stephen C., John M.H., Richard S.P., Bongani K.N., William J.S., Keith L., et al. Proteomic analysis of differentially expressed proteins in fungal elicitor-treated Arabidopsis cell cultures. J Exp Bot 2006, 57:1553-1562.
    • (2006) J Exp Bot , vol.57 , pp. 1553-1562
    • Stephen, C.1    John, M.H.2    Richard, S.P.3    Bongani, K.N.4    William, J.S.5    Keith, L.6
  • 60
    • 59149088519 scopus 로고    scopus 로고
    • Effector proteins of the bacterial pathogen Pseudomonas syringae alter the extracellular proteome of the host plant, Arabidopsis thaliana
    • Florian A.R., Kaffarnik A.M., Jones E., John P.R., Scott C.P. Effector proteins of the bacterial pathogen Pseudomonas syringae alter the extracellular proteome of the host plant, Arabidopsis thaliana. Mol Cell Proteomics 2009, 8:145-156.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 145-156
    • Florian, A.R.1    Kaffarnik, A.M.2    Jones, E.3    John, P.R.4    Scott, C.P.5
  • 61
    • 4143099179 scopus 로고    scopus 로고
    • Proteomic analysis of resistance mediated by Rcm 2.0 and Rcm 5.1, two loci controlling resistance to bacterial canker of tomato
    • Gitta L.C., Belinda W., Michael K., Eric J., Stockinger M., David M.F. Proteomic analysis of resistance mediated by Rcm 2.0 and Rcm 5.1, two loci controlling resistance to bacterial canker of tomato. Mol Plant Microbe Interact 2004, 17:1019-1028.
    • (2004) Mol Plant Microbe Interact , vol.17 , pp. 1019-1028
    • Gitta, L.C.1    Belinda, W.2    Michael, K.3    Eric, J.4    Stockinger, M.5    David, M.F.6
  • 62
    • 77952395219 scopus 로고    scopus 로고
    • Changes in protein abundance during powdery mildew infection of leaf tissues of Cabernet Sauvignon grapevine (Vitis vinifera L.)
    • Ellen M., Sophie A., Leslie M.H., Barbazuk W.B., Wenping Q., Laszlo K., et al. Changes in protein abundance during powdery mildew infection of leaf tissues of Cabernet Sauvignon grapevine (Vitis vinifera L.). Proteomics 2010, 10:2057-2064.
    • (2010) Proteomics , vol.10 , pp. 2057-2064
    • Ellen, M.1    Sophie, A.2    Leslie, M.H.3    Barbazuk, W.B.4    Wenping, Q.5    Laszlo, K.6
  • 63
    • 8744262736 scopus 로고    scopus 로고
    • Proteomic analysis of pathogen-responsive proteins from rice leaves induced by rice blast fungus, Magnaporthe grisea
    • Sun T.K., Sang G.K., Du H.H., Sun Y.K., Han J.K., Byung H.L., et al. Proteomic analysis of pathogen-responsive proteins from rice leaves induced by rice blast fungus, Magnaporthe grisea. Proteomics 2004, 4:3569-3578.
    • (2004) Proteomics , vol.4 , pp. 3569-3578
    • Sun, T.K.1    Sang, G.K.2    Du, H.H.3    Sun, Y.K.4    Han, J.K.5    Byung, H.L.6
  • 64
    • 34248668486 scopus 로고    scopus 로고
    • Proteomic analysis of rice plasma membrane reveals proteins involved in early defense response to bacterial blight
    • Fang C., Yuexing Y., Qun L., Zuhua H. Proteomic analysis of rice plasma membrane reveals proteins involved in early defense response to bacterial blight. Proteomics 2007, 7:1529-1539.
    • (2007) Proteomics , vol.7 , pp. 1529-1539
    • Fang, C.1    Yuexing, Y.2    Qun, L.3    Zuhua, H.4
  • 65
    • 33748337522 scopus 로고    scopus 로고
    • Proteomic and genetic approaches to identifying defense-related proteins in rice challenged with the fungal pathogen Rhizoctoniasolani
    • Joohyun T.M., Bricker M.L., Shannon R., Pinson M., James H.D. Proteomic and genetic approaches to identifying defense-related proteins in rice challenged with the fungal pathogen Rhizoctoniasolani. Mol Plant Pathol 2006, 7:405-416.
    • (2006) Mol Plant Pathol , vol.7 , pp. 405-416
    • Joohyun, T.M.1    Bricker, M.L.2    Shannon, R.3    Pinson, M.4    James, H.D.5
  • 66
    • 0942297973 scopus 로고    scopus 로고
    • Proteome analysis of cultivar-specific deregulations of Oryza sativa indica and O. sativa japonica cellular suspensions undergoing rice yellow mottle virus infection
    • Marjolaine V.D., Delalande F., Brizard J.P., Diemer H., Alain V.D., Brugidou C. Proteome analysis of cultivar-specific deregulations of Oryza sativa indica and O. sativa japonica cellular suspensions undergoing rice yellow mottle virus infection. Proteomics 2004, 4:216-225.
    • (2004) Proteomics , vol.4 , pp. 216-225
    • Marjolaine, V.D.1    Delalande, F.2    Brizard, J.P.3    Diemer, H.4    Alain, V.D.5    Brugidou, C.6
  • 67
    • 28444478425 scopus 로고    scopus 로고
    • Differential proteomic analysis of proteins in wheat spikes induced by Fusarium graminearum
    • Yun W., Liming Y., Haibin X., Qifu L., Zhengqiang M., Chenggen C. Differential proteomic analysis of proteins in wheat spikes induced by Fusarium graminearum. Proteomics 2005, 5:4496-4503.
    • (2005) Proteomics , vol.5 , pp. 4496-4503
    • Yun, W.1    Liming, Y.2    Haibin, X.3    Qifu, L.4    Zhengqiang, M.5    Chenggen, C.6
  • 68
    • 33748344060 scopus 로고    scopus 로고
    • Identification of differentially regulated proteins in response to a compatible interaction between the pathogen Fusarium graminearum and its host, Triticum aestivum
    • Wenchun Z., François E., André L. Identification of differentially regulated proteins in response to a compatible interaction between the pathogen Fusarium graminearum and its host, Triticum aestivum. Proteomics 2006, 8:4599-4609.
    • (2006) Proteomics , vol.8 , pp. 4599-4609
    • Wenchun, Z.1    François, E.2    André, L.3
  • 69
    • 39149083788 scopus 로고    scopus 로고
    • Differential expression of proteins in response to the interaction between the pathogen Fusarium graminearum and its host, Hordeum vulgare
    • Jennifer G., François E., André L., Selinger L.B. Differential expression of proteins in response to the interaction between the pathogen Fusarium graminearum and its host, Hordeum vulgare. Proteomics 2008, 8:545-554.
    • (2008) Proteomics , vol.8 , pp. 545-554
    • Jennifer, G.1    François, E.2    André, L.3    Selinger, L.B.4
  • 70
    • 0001324867 scopus 로고
    • Antifungal hydrolases in pea tissue: II. inhibition of fungal growth by combinations of chitinase and beta-1,3-glucanase
    • Mauch F., Mauch-Mani B., Boller T. Antifungal hydrolases in pea tissue: II. inhibition of fungal growth by combinations of chitinase and beta-1,3-glucanase. Plant Physiol 1988, 88:936-942.
    • (1988) Plant Physiol , vol.88 , pp. 936-942
    • Mauch, F.1    Mauch-Mani, B.2    Boller, T.3
  • 71
    • 0027130622 scopus 로고
    • Elicitors: their significance and primary modes of action in the induction of plant defense reactions
    • Yoshikawa M., Yamaoka N., Takeuchi Y. Elicitors: their significance and primary modes of action in the induction of plant defense reactions. Plant Cell Physiol 1993, 34:1163-1173.
    • (1993) Plant Cell Physiol , vol.34 , pp. 1163-1173
    • Yoshikawa, M.1    Yamaoka, N.2    Takeuchi, Y.3
  • 72
    • 0035963414 scopus 로고    scopus 로고
    • Protein dispensability and rate of evolution
    • Hirsh A.E., Fraser H.B. Protein dispensability and rate of evolution. Nature 2001, 411:1046-1049.
    • (2001) Nature , vol.411 , pp. 1046-1049
    • Hirsh, A.E.1    Fraser, H.B.2
  • 73
    • 0036078078 scopus 로고    scopus 로고
    • Essential genes are more evolutionarily conserved than are nonessential genes in bacteria
    • Jordan I.K., Rogozin I.B., Wolf Y.I., Koonin E.V. Essential genes are more evolutionarily conserved than are nonessential genes in bacteria. Genome Res 2002, 12:962-968.
    • (2002) Genome Res , vol.12 , pp. 962-968
    • Jordan, I.K.1    Rogozin, I.B.2    Wolf, Y.I.3    Koonin, E.V.4
  • 74
    • 0034537082 scopus 로고    scopus 로고
    • Accumulation of hydroxycoumarins during post-harvest deterioration of tuberous roots of cassava (Manihot esculenta Crantz)
    • Buschmann H., Rodriguez M.X., Tohme J., Beeching J.R. Accumulation of hydroxycoumarins during post-harvest deterioration of tuberous roots of cassava (Manihot esculenta Crantz). Ann Bot 2000, 86:1153-1160.
    • (2000) Ann Bot , vol.86 , pp. 1153-1160
    • Buschmann, H.1    Rodriguez, M.X.2    Tohme, J.3    Beeching, J.R.4
  • 75
    • 0030574273 scopus 로고    scopus 로고
    • The oxidative burst protects plants against pathogen attack: mechanism and role as an emergency signal for plant bio-defense. A review
    • Doke N., Miura Y., Sanchez L.M., Park H.J., Noritake T., Yoshioka H., et al. The oxidative burst protects plants against pathogen attack: mechanism and role as an emergency signal for plant bio-defense. A review. Gene 1996, 179:45-51.
    • (1996) Gene , vol.179 , pp. 45-51
    • Doke, N.1    Miura, Y.2    Sanchez, L.M.3    Park, H.J.4    Noritake, T.5    Yoshioka, H.6
  • 76
    • 77953687782 scopus 로고    scopus 로고
    • ROS resistance in Pisum sativum cv. Alaska: the involvement of nucleoside diphosphate kinase in oxidative stress responses via the regulation of antioxidants
    • Haque M.E., Yoshida Y., Hasunuma K. ROS resistance in Pisum sativum cv. Alaska: the involvement of nucleoside diphosphate kinase in oxidative stress responses via the regulation of antioxidants. Planta 2010, 232:367-382.
    • (2010) Planta , vol.232 , pp. 367-382
    • Haque, M.E.1    Yoshida, Y.2    Hasunuma, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.