메뉴 건너뛰기




Volumn 60, Issue , 2012, Pages 59-66

Hydrophobic proteins secreted into the apoplast may contribute to resistance against Phytophthora infestans in potato

Author keywords

Apoplast; Hydrophobic proteins; P. infestans; Plant pathogen interaction; Protease inhibitors; Solanum tuberosum; Unconventional secretion

Indexed keywords

LEUKOCYTE ELASTASE INHIBITOR; VEGETABLE PROTEIN;

EID: 84867056286     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2012.07.017     Document Type: Article
Times cited : (24)

References (78)
  • 1
    • 0000260623 scopus 로고    scopus 로고
    • Functions and responses of the leaf apoplast under stress
    • Dietz
    • Dietz Functions and responses of the leaf apoplast under stress. Prog. Bot. 1997, 58:221-254.
    • (1997) Prog. Bot. , vol.58 , pp. 221-254
  • 2
    • 60249102042 scopus 로고    scopus 로고
    • Identification of an apoplastic protein involved in the initial phase of salt stress response in rice root by two-dimensional electrophoresis
    • Zhang L., Tian L.H., Zhao J.F., Song Y., Zhang C.J., Guo Y. Identification of an apoplastic protein involved in the initial phase of salt stress response in rice root by two-dimensional electrophoresis. Plant Physiol. 2009, 149:916-928.
    • (2009) Plant Physiol. , vol.149 , pp. 916-928
    • Zhang, L.1    Tian, L.H.2    Zhao, J.F.3    Song, Y.4    Zhang, C.J.5    Guo, Y.6
  • 4
    • 33748941620 scopus 로고    scopus 로고
    • Significance of inducible defense-related proteins in infected plants
    • van Loon L., Rep M., Pieterse C. Significance of inducible defense-related proteins in infected plants. Annu. Rev. Phytopathol. 2006, 44:135-162.
    • (2006) Annu. Rev. Phytopathol. , vol.44 , pp. 135-162
    • van Loon, L.1    Rep, M.2    Pieterse, C.3
  • 7
    • 0034001189 scopus 로고    scopus 로고
    • Purification, characterization, and molecular cloning of the gene of a seed-specific antimicrobial protein from pokeweed
    • Liu Y., Luo J., Xu C., Ren F., Peng C., Wu G., Zhao J. Purification, characterization, and molecular cloning of the gene of a seed-specific antimicrobial protein from pokeweed. Plant Physiol. 2000, 122:1015-1024.
    • (2000) Plant Physiol. , vol.122 , pp. 1015-1024
    • Liu, Y.1    Luo, J.2    Xu, C.3    Ren, F.4    Peng, C.5    Wu, G.6    Zhao, J.7
  • 8
    • 0036840580 scopus 로고    scopus 로고
    • Cationic hydrophobic peptides with antimicrobial activity
    • Stark M., Liu L., Deber C. Cationic hydrophobic peptides with antimicrobial activity. Antimicrob. Agents Chemother. 2002, 46:3585-3590.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 3585-3590
    • Stark, M.1    Liu, L.2    Deber, C.3
  • 9
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman M., NY Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 2003, 55:27-55.
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.1    Ny, Y.2
  • 10
    • 0036938848 scopus 로고    scopus 로고
    • Molecular characterisation of a xyloglucan oligosaccharide-acting alpha-d-xylosidase from nasturtium (Tropaeolum majus L.) cotyledons that resembles plant 'apoplastic' alpha-d-glucosidases
    • Crombie H., Chengappa S., Jarman C., Sidebottom C., Reid J. Molecular characterisation of a xyloglucan oligosaccharide-acting alpha-d-xylosidase from nasturtium (Tropaeolum majus L.) cotyledons that resembles plant 'apoplastic' alpha-d-glucosidases. Planta 2001, 214:406-413.
    • (2001) Planta , vol.214 , pp. 406-413
    • Crombie, H.1    Chengappa, S.2    Jarman, C.3    Sidebottom, C.4    Reid, J.5
  • 11
    • 0037987953 scopus 로고    scopus 로고
    • Molecular genetics of pathogenic oomycetes
    • Kamoun S. Molecular genetics of pathogenic oomycetes. Eukaryot. Cell. 2003, 2:191-199.
    • (2003) Eukaryot. Cell. , vol.2 , pp. 191-199
    • Kamoun, S.1
  • 12
    • 0035563781 scopus 로고    scopus 로고
    • Invasion by the late blight pathogen. Renewed sex and enhanced fitness
    • Smart C., Fry W. Invasion by the late blight pathogen. Renewed sex and enhanced fitness. Biol. Invasions 2001, 3:235-243.
    • (2001) Biol. Invasions , vol.3 , pp. 235-243
    • Smart, C.1    Fry, W.2
  • 13
    • 0036848765 scopus 로고    scopus 로고
    • Tracking historic migrations of the Irish potato famine pathogen, Phytophthora infestans
    • Ristaino J. Tracking historic migrations of the Irish potato famine pathogen, Phytophthora infestans. Microbes Infect. 2002, 4:1369-1377.
    • (2002) Microbes Infect. , vol.4 , pp. 1369-1377
    • Ristaino, J.1
  • 14
    • 0036727072 scopus 로고    scopus 로고
    • Phytophthora infestans: populations, pathogenicity and phenylamides
    • Shattock R. Phytophthora infestans: populations, pathogenicity and phenylamides. Pest Manag. Sci. 2002, 58:944-950.
    • (2002) Pest Manag. Sci. , vol.58 , pp. 944-950
    • Shattock, R.1
  • 15
    • 71149109729 scopus 로고    scopus 로고
    • Proteomic studies of phytopathogenic fungi, oomycetes and their interactions with hosts
    • Bhadauria V., Banniza S., Wang L., Wei Y., Peng Y. Proteomic studies of phytopathogenic fungi, oomycetes and their interactions with hosts. Eur. J. Plant Pathol. 2010, 126:81-95.
    • (2010) Eur. J. Plant Pathol. , vol.126 , pp. 81-95
    • Bhadauria, V.1    Banniza, S.2    Wang, L.3    Wei, Y.4    Peng, Y.5
  • 17
    • 0000163299 scopus 로고
    • The nature and inheritance of weld resistance to late blight (Phytophthora infestans) in potatoes
    • Black W. The nature and inheritance of weld resistance to late blight (Phytophthora infestans) in potatoes. Am. Potato J. 1970, 47:279-288.
    • (1970) Am. Potato J. , vol.47 , pp. 279-288
    • Black, W.1
  • 18
    • 84867059224 scopus 로고
    • Interactions of R genes in breeding for resistance of potatoes against Phytophthora infestans, Planning Conference on Fungal Diseases of the Potato, CIP
    • L. Turkensteen, Interactions of R genes in breeding for resistance of potatoes against Phytophthora infestans, Planning Conference on Fungal Diseases of the Potato, CIP, 1987, pp. 57-73.
    • (1987) , pp. 57-73
    • Turkensteen, L.1
  • 19
    • 0002545083 scopus 로고
    • Differential resistance to tuber late blight in potato cultivars without R-genes
    • Bjor T., Muledid K. Differential resistance to tuber late blight in potato cultivars without R-genes. Potato Res. 1991, 34:3-8.
    • (1991) Potato Res. , vol.34 , pp. 3-8
    • Bjor, T.1    Muledid, K.2
  • 21
    • 0002877483 scopus 로고
    • Molecular aspects of the potato-Phytophthora infestans interactions
    • Pieterse C., De Wit P., Govers F. Molecular aspects of the potato-Phytophthora infestans interactions. Neth. J. Plant Pathol. 1992, 2:85-92.
    • (1992) Neth. J. Plant Pathol. , vol.2 , pp. 85-92
    • Pieterse, C.1    De Wit, P.2    Govers, F.3
  • 22
    • 0000225904 scopus 로고
    • Durable resistance of potatoes against Phytophthora infestans
    • T.H. Jacobs, J.E. Parlevliet (Eds.)
    • Turkensteen L. Durable resistance of potatoes against Phytophthora infestans. Durability of Disease Resistance 1993, 115-124. T.H. Jacobs, J.E. Parlevliet (Eds.).
    • (1993) Durability of Disease Resistance , pp. 115-124
    • Turkensteen, L.1
  • 23
    • 84867092331 scopus 로고    scopus 로고
    • Experiencias, dificultades y logros obtenidos en la busqueda de resistencia durable a enfermedades, Primer taller de preduza en resistencia duradera en cultivos altos en la zona andina, Quito, Ecuador
    • M. Huarte, I. Butzonitch, M. Van Damme, M. Colavita, S. Capezio, S. Micheletto, E. Cacace, A. Clausen, Experiencias, dificultades y logros obtenidos en la busqueda de resistencia durable a enfermedades, Primer taller de preduza en resistencia duradera en cultivos altos en la zona andina, Quito, Ecuador, 1997, pp. 154-163.
    • (1997) , pp. 154-163
    • Huarte, M.1    Butzonitch, I.2    Van Damme, M.3    Colavita, M.4    Capezio, S.5    Micheletto, S.6    Cacace, E.7    Clausen, A.8
  • 24
    • 0031735853 scopus 로고    scopus 로고
    • Analysis of intercellular washing fluids of potato tubers and detection of increased proteolytic activity upon fungal infection
    • Olivieri F., Godoy A., Escande A., Casalongué C. Analysis of intercellular washing fluids of potato tubers and detection of increased proteolytic activity upon fungal infection. Physiol. Plant 1998, 104:232-238.
    • (1998) Physiol. Plant , vol.104 , pp. 232-238
    • Olivieri, F.1    Godoy, A.2    Escande, A.3    Casalongué, C.4
  • 25
    • 0036246831 scopus 로고    scopus 로고
    • An aspartic protease with antimicrobial activity is induced after infection and wounding in intercellular fluids of potato tubers
    • Guevara M., Oliva C., Huarte M., Daleo G. An aspartic protease with antimicrobial activity is induced after infection and wounding in intercellular fluids of potato tubers. Eur. J. Plant Pathol. 2002, 108:131-137.
    • (2002) Eur. J. Plant Pathol. , vol.108 , pp. 131-137
    • Guevara, M.1    Oliva, C.2    Huarte, M.3    Daleo, G.4
  • 26
    • 0001719907 scopus 로고
    • Hydrolytic enzymes in the central vacuole of plant cells
    • Boller T., Kende H. Hydrolytic enzymes in the central vacuole of plant cells. Plant Physiol. 1979, 63:1123-1132.
    • (1979) Plant Physiol. , vol.63 , pp. 1123-1132
    • Boller, T.1    Kende, H.2
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 29
    • 0000544299 scopus 로고
    • A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels
    • Oakley B., Kirsch D., Morris N. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 1980, 105:361-363.
    • (1980) Anal. Biochem. , vol.105 , pp. 361-363
    • Oakley, B.1    Kirsch, D.2    Morris, N.3
  • 30
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff V., Arold N., Taube D., Ehrhardt W. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 1988, 9:255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 32
    • 60849086516 scopus 로고    scopus 로고
    • Absolute protein quantification by LC/MSE for global analysis of salicylic acid-induced plant protein secretion responses
    • Cheng F., Blackburn K., Lin Y., Goshe M., Williamson J. Absolute protein quantification by LC/MSE for global analysis of salicylic acid-induced plant protein secretion responses. J. Proteome Res. 2009, 8:82-93.
    • (2009) J. Proteome Res. , vol.8 , pp. 82-93
    • Cheng, F.1    Blackburn, K.2    Lin, Y.3    Goshe, M.4    Williamson, J.5
  • 34
    • 0000106348 scopus 로고
    • The epidemiology of Phytophthora infestans: IV. Spraying trials 1959 to 1963 and infection of tubers
    • Hirst J., Stedman O.J., Lacey J., Hide G. The epidemiology of Phytophthora infestans: IV. Spraying trials 1959 to 1963 and infection of tubers. Ann. Appl. Biol. 1965, 55:373-395.
    • (1965) Ann. Appl. Biol. , vol.55 , pp. 373-395
    • Hirst, J.1    Stedman, O.J.2    Lacey, J.3    Hide, G.4
  • 35
    • 38249036124 scopus 로고
    • Studies on the resistance of the outer cortical tissues of the tubers of some potato cultivars to Phytophthora infestans
    • Phatak N., Clarke D. Studies on the resistance of the outer cortical tissues of the tubers of some potato cultivars to Phytophthora infestans. Mol. Plant Pathol. 1987, 31:123-132.
    • (1987) Mol. Plant Pathol. , vol.31 , pp. 123-132
    • Phatak, N.1    Clarke, D.2
  • 36
    • 0033066032 scopus 로고    scopus 로고
    • Variation in aggressiveness of Canadian isolates of Phytophthora infestans as indicated by their relative abilities to cause potato tuber rot
    • Peters R., Platt H. Variation in aggressiveness of Canadian isolates of Phytophthora infestans as indicated by their relative abilities to cause potato tuber rot. Plant Dis. 1999, 83:652-661.
    • (1999) Plant Dis. , vol.83 , pp. 652-661
    • Peters, R.1    Platt, H.2
  • 37
    • 84982383867 scopus 로고
    • Factors affecting the field infection of potato tubers of different cultivars by blight (Phvtophthora infestans)
    • Lapwood D. Factors affecting the field infection of potato tubers of different cultivars by blight (Phvtophthora infestans). Ann. Appl. Biol. 1977, 85:23-42.
    • (1977) Ann. Appl. Biol. , vol.85 , pp. 23-42
    • Lapwood, D.1
  • 38
    • 0001640771 scopus 로고
    • Activity of Phytophthora infestans in soil in relation to tuber infection
    • Zan K. Activity of Phytophthora infestans in soil in relation to tuber infection. Trans. Br. Mycol. Soc. 1962, 45:205.
    • (1962) Trans. Br. Mycol. Soc. , vol.45 , pp. 205
    • Zan, K.1
  • 39
    • 0033739620 scopus 로고    scopus 로고
    • Does basal PR gene expression in Solanum species contribute to non-specific resistance to Phytophthora infestans?
    • Vleeshouwers V., Van Dooijeweerta W., Govers F., Kamoun S., Colon L. Does basal PR gene expression in Solanum species contribute to non-specific resistance to Phytophthora infestans?. Physiol. Mol. Plant Pathol. 2000, 57:35-42.
    • (2000) Physiol. Mol. Plant Pathol. , vol.57 , pp. 35-42
    • Vleeshouwers, V.1    Van Dooijeweerta, W.2    Govers, F.3    Kamoun, S.4    Colon, L.5
  • 41
    • 0030609539 scopus 로고    scopus 로고
    • Regulation of protease inhibitors and plant defense
    • Koiwa H., Bressan R., Hasegawa P. Regulation of protease inhibitors and plant defense. Trends Plant Sci. 1997, 2:379-384.
    • (1997) Trends Plant Sci. , vol.2 , pp. 379-384
    • Koiwa, H.1    Bressan, R.2    Hasegawa, P.3
  • 42
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: genes for improving defenses against insects and pathogens
    • Ryan C. Protease inhibitors in plants: genes for improving defenses against insects and pathogens. Annu. Rev. Phytopathol. 1990, 28:425-449.
    • (1990) Annu. Rev. Phytopathol. , vol.28 , pp. 425-449
    • Ryan, C.1
  • 43
    • 0023482897 scopus 로고
    • Induced resistance and interspecific competition between mites and a vascular wilt fungus
    • Karban R., Adamchak R., Schnatorst W. Induced resistance and interspecific competition between mites and a vascular wilt fungus. Science 1987, 235:678-680.
    • (1987) Science , vol.235 , pp. 678-680
    • Karban, R.1    Adamchak, R.2    Schnatorst, W.3
  • 44
    • 0029620233 scopus 로고
    • The plant response in pathogenesis, symbiosis, and wounding: variation on a common theme?
    • Baron C., Zambrynski P. The plant response in pathogenesis, symbiosis, and wounding: variation on a common theme?. Annu. Rev. Genet. 1995, 29:107-129.
    • (1995) Annu. Rev. Genet. , vol.29 , pp. 107-129
    • Baron, C.1    Zambrynski, P.2
  • 45
    • 0032502952 scopus 로고    scopus 로고
    • Kunitz-type proteinase inhibitors from intact and Phytophthora-infected potato tubers
    • Valueva T., Revina T., Kladnitskaya G., Molosov V. Kunitz-type proteinase inhibitors from intact and Phytophthora-infected potato tubers. FEBS Lett. 1998, 426:131-134.
    • (1998) FEBS Lett. , vol.426 , pp. 131-134
    • Valueva, T.1    Revina, T.2    Kladnitskaya, G.3    Molosov, V.4
  • 46
    • 0024972959 scopus 로고
    • Primary structure of cathepsinD inhibitor from potatoes and its structure relationship to soybean trypsin inhibitor family
    • Mares M., Meloun B., Pavlík M., Kostka V., Baudys M. Primary structure of cathepsinD inhibitor from potatoes and its structure relationship to soybean trypsin inhibitor family. FEBS Lett. 1989, 251:94-98.
    • (1989) FEBS Lett. , vol.251 , pp. 94-98
    • Mares, M.1    Meloun, B.2    Pavlík, M.3    Kostka, V.4    Baudys, M.5
  • 47
    • 0000817989 scopus 로고
    • Proteinase-inhibitor activity and wound-inducible gene expression of the 22-kDa potato-tuber proteins
    • Suh S., Snekema W., Hannapel D. Proteinase-inhibitor activity and wound-inducible gene expression of the 22-kDa potato-tuber proteins. Planta 1991, 184:423-430.
    • (1991) Planta , vol.184 , pp. 423-430
    • Suh, S.1    Snekema, W.2    Hannapel, D.3
  • 48
    • 84989737712 scopus 로고
    • Characterization of the early events potato tuber development
    • Hannapel D. Characterization of the early events potato tuber development. Physiol. Plant 1991, 83:568-573.
    • (1991) Physiol. Plant , vol.83 , pp. 568-573
    • Hannapel, D.1
  • 49
    • 0000568941 scopus 로고
    • A wound-inducible potato proteinase inhibitor gene expressed in non-tuber-bearing species is not sucrose inducible
    • Hansen J., Hannapel D. A wound-inducible potato proteinase inhibitor gene expressed in non-tuber-bearing species is not sucrose inducible. Plant Physiol. 1992, 100:164-169.
    • (1992) Plant Physiol. , vol.100 , pp. 164-169
    • Hansen, J.1    Hannapel, D.2
  • 50
    • 0033624577 scopus 로고    scopus 로고
    • Soluble phospholipase A2 activity is induced before oxylipin accumulation in tobacco mosaic virus-infected tobacco leaves and is contributed by patatin-like enzymes
    • Dhondt S., Geoffroy P., Stelmach B., Legrand M., Heitz T. Soluble phospholipase A2 activity is induced before oxylipin accumulation in tobacco mosaic virus-infected tobacco leaves and is contributed by patatin-like enzymes. Plant J. 2000, 23:431-440.
    • (2000) Plant J. , vol.23 , pp. 431-440
    • Dhondt, S.1    Geoffroy, P.2    Stelmach, B.3    Legrand, M.4    Heitz, T.5
  • 51
    • 0000677114 scopus 로고
    • Esterase specificity of patatin from two potato cultivars
    • Racusen D. Esterase specificity of patatin from two potato cultivars. Can. J. Bot. 1986, 64:2104-2106.
    • (1986) Can. J. Bot. , vol.64 , pp. 2104-2106
    • Racusen, D.1
  • 52
    • 0034775005 scopus 로고    scopus 로고
    • An acidic β-1,3 glucanase from potato tubers appears to be patatin
    • Tonón C., Daleo G., Oliva C. An acidic β-1,3 glucanase from potato tubers appears to be patatin. Plant Physiol. Biochem. 2001, 39:849-854.
    • (2001) Plant Physiol. Biochem. , vol.39 , pp. 849-854
    • Tonón, C.1    Daleo, G.2    Oliva, C.3
  • 53
    • 0036278125 scopus 로고    scopus 로고
    • Isolation of a potato acidic 39 kDa β-1,3-glucanase with antifungal activity against Phytophthora infestans and analysis of its expression in potato cultivars differing in their degrees of field resistance
    • Tonón C., Guevara G., Oliva C., Daleo G. Isolation of a potato acidic 39 kDa β-1,3-glucanase with antifungal activity against Phytophthora infestans and analysis of its expression in potato cultivars differing in their degrees of field resistance. J. Phytopathol. 2002, 150:189-195.
    • (2002) J. Phytopathol. , vol.150 , pp. 189-195
    • Tonón, C.1    Guevara, G.2    Oliva, C.3    Daleo, G.4
  • 54
    • 4444256020 scopus 로고    scopus 로고
    • Purification of an isoforms of patatin with antimicrobial activity against Phytophthora infestans
    • Sharma N., Gruszewski H., Park S., Holm D., Vivanco J. Purification of an isoforms of patatin with antimicrobial activity against Phytophthora infestans. Plant Physiol. Biochem. 2004, 42:647-655.
    • (2004) Plant Physiol. Biochem. , vol.42 , pp. 647-655
    • Sharma, N.1    Gruszewski, H.2    Park, S.3    Holm, D.4    Vivanco, J.5
  • 55
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: from structure to function
    • Gerke V., Moss S. Annexins: from structure to function. Physiol. Rev. 2002, 82:331-371.
    • (2002) Physiol. Rev. , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.2
  • 56
    • 0038301526 scopus 로고    scopus 로고
    • Annexin A4 reduces water and proton permeability of model membranes but does not alter aquaporin 2-mediated water transport in isolated endosomes
    • Hill W., Knetzel M., Kishore B., Dedman J., Zeidel M. Annexin A4 reduces water and proton permeability of model membranes but does not alter aquaporin 2-mediated water transport in isolated endosomes. J. Gen. Physiol. 2003, 121:413-425.
    • (2003) J. Gen. Physiol. , vol.121 , pp. 413-425
    • Hill, W.1    Knetzel, M.2    Kishore, B.3    Dedman, J.4    Zeidel, M.5
  • 58
    • 0028676125 scopus 로고
    • A 42-kilodalton annexin-like protein is associated with plant vacuoles
    • Seals D., Parrish M., Randall S. A 42-kilodalton annexin-like protein is associated with plant vacuoles. Plant Physiol. 1994, 106:1403-1412.
    • (1994) Plant Physiol. , vol.106 , pp. 1403-1412
    • Seals, D.1    Parrish, M.2    Randall, S.3
  • 59
    • 0031397571 scopus 로고    scopus 로고
    • A vacuole-associated annexin protein, VCaB42, correlates with the expansion of tobacco cells
    • Seals D., Randall S. A vacuole-associated annexin protein, VCaB42, correlates with the expansion of tobacco cells. Plant Physiol. 1997, 115:753-761.
    • (1997) Plant Physiol. , vol.115 , pp. 753-761
    • Seals, D.1    Randall, S.2
  • 60
    • 15744385479 scopus 로고    scopus 로고
    • The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins
    • Carter C., Pan S., Zouhar J., Avila E., Girke T., Raikhel N. The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins. Plant Cell. 2004, 16:3285-3303.
    • (2004) Plant Cell. , vol.16 , pp. 3285-3303
    • Carter, C.1    Pan, S.2    Zouhar, J.3    Avila, E.4    Girke, T.5    Raikhel, N.6
  • 61
    • 0027106118 scopus 로고
    • Purification and immunolocalization of annexin-like protein in pea seedlings
    • Clark G., Dauwalder M., Roux S. Purification and immunolocalization of annexin-like protein in pea seedlings. Planta 1992, 187:1-9.
    • (1992) Planta , vol.187 , pp. 1-9
    • Clark, G.1    Dauwalder, M.2    Roux, S.3
  • 62
    • 24644494802 scopus 로고    scopus 로고
    • A proteomic approach to apoplastic proteins involved in cell wall regeneration in protoplasts of Arabidopsis suspension-cultured cells
    • Kwon H., Yokoyama R., Nishitani K. A proteomic approach to apoplastic proteins involved in cell wall regeneration in protoplasts of Arabidopsis suspension-cultured cells. Plant Cell. Physiol. 2005, 46:843-857.
    • (2005) Plant Cell. Physiol. , vol.46 , pp. 843-857
    • Kwon, H.1    Yokoyama, R.2    Nishitani, K.3
  • 65
    • 0034888732 scopus 로고    scopus 로고
    • Expression of 35S::Pto globally activates defense-related genes in tomato plants
    • Xiao F., Tang X., Zhou J. Expression of 35S::Pto globally activates defense-related genes in tomato plants. Plant Physiol. 2001, 126:1637-1645.
    • (2001) Plant Physiol. , vol.126 , pp. 1637-1645
    • Xiao, F.1    Tang, X.2    Zhou, J.3
  • 66
    • 33846501703 scopus 로고    scopus 로고
    • Arabidopsis systemic immunity uses conserved defense signalling pathways and is mediated by jasmonates
    • Truman W., Bennett M., Kubigsteltig I., Turnbull C., Grant M. Arabidopsis systemic immunity uses conserved defense signalling pathways and is mediated by jasmonates. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:1075-1080.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 1075-1080
    • Truman, W.1    Bennett, M.2    Kubigsteltig, I.3    Turnbull, C.4    Grant, M.5
  • 68
    • 0000980362 scopus 로고
    • Conservation and duplication of isozymes in plants
    • Gottlieb L. Conservation and duplication of isozymes in plants. Science 1982, 216:373-380.
    • (1982) Science , vol.216 , pp. 373-380
    • Gottlieb, L.1
  • 69
    • 0023046216 scopus 로고
    • Evidence in favor of the symbiotic origin of chloroplasts: primary structure and evolution of tobacco glyceraldehyde-3-phosphate dehydrogenase
    • Shih M., Lazar G., Goodman H. Evidence in favor of the symbiotic origin of chloroplasts: primary structure and evolution of tobacco glyceraldehyde-3-phosphate dehydrogenase. Cell 1986, 47:73-80.
    • (1986) Cell , vol.47 , pp. 73-80
    • Shih, M.1    Lazar, G.2    Goodman, H.3
  • 70
    • 0028445313 scopus 로고
    • Expressed sequence tags from cultured cells of rice (Oryza sativa L.) under stressed conditions: analysis of transcripts of genes engaged in ATP generating pathways
    • Umeda M., Hara C., Matsubayashi Y., Li H., Liu Q., Tadokoro F., Aotsuka S., Uchimiya H. Expressed sequence tags from cultured cells of rice (Oryza sativa L.) under stressed conditions: analysis of transcripts of genes engaged in ATP generating pathways. Plant Mol. Biol. 1994, 25:469-478.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 469-478
    • Umeda, M.1    Hara, C.2    Matsubayashi, Y.3    Li, H.4    Liu, Q.5    Tadokoro, F.6    Aotsuka, S.7    Uchimiya, H.8
  • 71
    • 0028518845 scopus 로고
    • Dehydration and ABA increase mRNA levels and enzyme activity of cytosolic GAPDH in the resurrection plant
    • Velasco R., Salamini F., Bartels D. Dehydration and ABA increase mRNA levels and enzyme activity of cytosolic GAPDH in the resurrection plant. Plant Mol. Biol. 1994, 26:541-546.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 541-546
    • Velasco, R.1    Salamini, F.2    Bartels, D.3
  • 72
    • 0000928706 scopus 로고
    • Salinity stress induced tissue-specific proteins in barley seedlings
    • Ramagopal S. Salinity stress induced tissue-specific proteins in barley seedlings. Plant Physiol. 1987, 84:324-331.
    • (1987) Plant Physiol. , vol.84 , pp. 324-331
    • Ramagopal, S.1
  • 73
    • 0001281332 scopus 로고
    • A comparison of the effect of salt on polypeptides and translatable mRNAs in roots of a salt-tolerant and a salt-sensitive cultivar of barley
    • Hurkman W., Fornari C., Tanaka C. A comparison of the effect of salt on polypeptides and translatable mRNAs in roots of a salt-tolerant and a salt-sensitive cultivar of barley. Plant Physiol. 1989, 90:1444-1456.
    • (1989) Plant Physiol. , vol.90 , pp. 1444-1456
    • Hurkman, W.1    Fornari, C.2    Tanaka, C.3
  • 74
    • 0029152393 scopus 로고
    • Molecular and physiological responses to abscisic acid and salts in roots of salt-sensitive and salt-tolerant indica rice varieties
    • Moons A., Bauw G., Prinsen E., Van Montagu M., Van Der Straeten D. Molecular and physiological responses to abscisic acid and salts in roots of salt-sensitive and salt-tolerant indica rice varieties. Plant Physiol. 1995, 107:177-186.
    • (1995) Plant Physiol. , vol.107 , pp. 177-186
    • Moons, A.1    Bauw, G.2    Prinsen, E.3    Van Montagu, M.4    Van Der Straeten, D.5
  • 75
    • 0000382475 scopus 로고    scopus 로고
    • Protein changes in response to progressive water deficit in maize: quantitative variations and identification
    • Riccardi F., Gazeau P., de Vienne D., Zivy M. Protein changes in response to progressive water deficit in maize: quantitative variations and identification. Plant Physiol. 1998, 117:1253-1263.
    • (1998) Plant Physiol. , vol.117 , pp. 1253-1263
    • Riccardi, F.1    Gazeau, P.2    de Vienne, D.3    Zivy, M.4
  • 76
    • 51149101236 scopus 로고    scopus 로고
    • Cyclophilin and the regulation of symbiosis in Aiptasia pallid
    • Perez S., Weis V. Cyclophilin and the regulation of symbiosis in Aiptasia pallid. Biol. Bull. 2008, 215:63-72.
    • (2008) Biol. Bull. , vol.215 , pp. 63-72
    • Perez, S.1    Weis, V.2
  • 77
    • 0036619384 scopus 로고    scopus 로고
    • Ascorbate and glutathione: guardians of the cell cycle, partners in crime?
    • Potters G., De Gara L., Asard H., Horemans N. Ascorbate and glutathione: guardians of the cell cycle, partners in crime?. Plant Physiol. Biochem. 2002, 40:537-548.
    • (2002) Plant Physiol. Biochem. , vol.40 , pp. 537-548
    • Potters, G.1    De Gara, L.2    Asard, H.3    Horemans, N.4
  • 78
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • Nickel W., Rabouille C. Mechanisms of regulated unconventional protein secretion. Nature 2009, 10:148-155.
    • (2009) Nature , vol.10 , pp. 148-155
    • Nickel, W.1    Rabouille, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.