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Volumn 36, Issue 3, 2014, Pages 795-807

Changes in the proteome of pea (Pisum sativum L.) seeds germinating under optimal and osmotic stress conditions and subjected to post-stress recovery

Author keywords

Germination; Osmotic stress; Pea seeds; Pisum sativum L.; Proteome; Recovery

Indexed keywords

PISUM SATIVUM;

EID: 84894276085     PISSN: 01375881     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11738-013-1458-8     Document Type: Article
Times cited : (13)

References (100)
  • 4
    • 0036113740 scopus 로고    scopus 로고
    • Identification and characterization of mRNA transcripts differentially expressed in response to high salinity by means of differential display in the mangrove, Bruguiera gymnorrhiza
    • doi:10.1016/S0168-9452(01)00601-X
    • Banzai T, Hershkovits G, Katcoff DJ, Hanagata N, Dubinsky Z, Karube I (2002) Identification and characterization of mRNA transcripts differentially expressed in response to high salinity by means of differential display in the mangrove, Bruguiera gymnorrhiza. Plant Sci 162: 499-505. doi: 10. 1016/S0168-9452(01)00601-X.
    • (2002) Plant Sci , vol.162 , pp. 499-505
    • Banzai, T.1    Hershkovits, G.2    Katcoff, D.J.3    Hanagata, N.4    Dubinsky, Z.5    Karube, I.6
  • 5
    • 0035826718 scopus 로고    scopus 로고
    • Plant biology in the future
    • doi:10.1073/pnas.101093298
    • Bazzaz FA (2001) Plant biology in the future. Proc Natl Acad Sci 98: 5441-5445. doi: 10. 1073/pnas. 101093298.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 5441-5445
    • Bazzaz, F.A.1
  • 6
    • 0000512669 scopus 로고
    • Water deficit-induced changes in abscisic acid, growth, polysomes, and translatable RNA in soybean hypocotyls
    • doi:10.1104/pp.88.2.289
    • Bensen RJ, Boyer JS, Mullet JE (1988) Water deficit-induced changes in abscisic acid, growth, polysomes, and translatable RNA in soybean hypocotyls. Plant Physiol 88: 289-294. doi: 10. 1104/pp. 88. 2. 289.
    • (1988) Plant Physiol , vol.88 , pp. 289-294
    • Bensen, R.J.1    Boyer, J.S.2    Mullet, J.E.3
  • 7
    • 0022291796 scopus 로고
    • Porin from bacterial and mitochondrial outer membranes
    • doi:10.3109/10409238509082542
    • Benz R (1985) Porin from bacterial and mitochondrial outer membranes. Crit Rev Biochem 19: 145-190. doi: 10. 3109/10409238509082542.
    • (1985) Crit Rev Biochem , vol.19 , pp. 145-190
    • Benz, R.1
  • 8
    • 0006922663 scopus 로고    scopus 로고
    • Analysis of 1, 9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana
    • Bevan M, Bansroft I, Bent E, Love K, Goodman H, Dean C, et al (1998) Analysis of 1, 9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana. Nature 391: 485-488.
    • (1998) Nature , vol.391 , pp. 485-488
    • Bevan, M.1    Bansroft, I.2    Bent, E.3    Love, K.4    Goodman, H.5    Dean, C.6
  • 10
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • doi:10.1002/elps.1150080203
    • Blum H, Beier H, Gross HJ (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8: 93-99. doi: 10. 1002/elps. 1150080203.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 12
    • 0020458787 scopus 로고
    • Plant productivity and environment potential for increasing crop plant productivity, genotypic selection
    • Boyer JS (1982) Plant productivity and environment potential for increasing crop plant productivity, genotypic selection. Science 218: 443-448.
    • (1982) Science , vol.218 , pp. 443-448
    • Boyer, J.S.1
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • doi:10.1016/0003-2697(76)90527-3
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254. doi: 10. 1016/0003-2697(76)90527-3.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0000015823 scopus 로고
    • Activities of hydrogen peroxide-scavenging enzymes in germinating wheat seeds
    • doi:10.1093/jxb/44.1.127
    • Cakmak I, Strbac D, Marschner H (1993) Activities of hydrogen peroxide-scavenging enzymes in germinating wheat seeds. J Exp Bot 44: 127-132. doi: 10. 1093/jxb/44. 1. 127.
    • (1993) J Exp Bot , vol.44 , pp. 127-132
    • Cakmak, I.1    Strbac, D.2    Marschner, H.3
  • 15
    • 0032479463 scopus 로고    scopus 로고
    • 14-3-3 proteins activate a plant calcium-dependent protein kinase (CDPK)
    • doi:10.1016/S0014-5793(98)00696-6
    • Camoni L, Harper JF, Palmgren MG (1998) 14-3-3 proteins activate a plant calcium-dependent protein kinase (CDPK). FEBS Lett 430: 381-384. doi: 10. 1016/S0014-5793(98)00696-6.
    • (1998) FEBS Lett , vol.430 , pp. 381-384
    • Camoni, L.1    Harper, J.F.2    Palmgren, M.G.3
  • 16
    • 0034640543 scopus 로고    scopus 로고
    • The phosphorylation state and expression of soybean BiP isoforms are differentially regulated following abiotic stresses
    • doi:10.1074/jbc.275.19.14494
    • Cascardo JCM, Almeida RS, Buzeli RAA, Carolino SMB, Otoni WC, Fontes EPB (2000) The phosphorylation state and expression of soybean BiP isoforms are differentially regulated following abiotic stresses. J Biol Chem 275: 14494-14500. doi: 10. 1074/jbc. 275. 19. 14494.
    • (2000) J Biol Chem , vol.275 , pp. 14494-14500
    • Cascardo, J.C.M.1    Almeida, R.S.2    Buzeli, R.A.A.3    Carolino, S.M.B.4    Otoni, W.C.5    Fontes, E.P.B.6
  • 17
    • 0032133248 scopus 로고    scopus 로고
    • Characterization of a maize tonoplast aquaporin expressed in zones of cell division and elongation
    • doi:10.1104/pp.117.4.1143
    • Chaumont F, Barrieu F, Herman EM, Chrispeels MJ (1998) Characterization of a maize tonoplast aquaporin expressed in zones of cell division and elongation. Plant Physiol 117: 1143-1152. doi: 10. 1104/pp. 117. 4. 1143.
    • (1998) Plant Physiol , vol.117 , pp. 1143-1152
    • Chaumont, F.1    Barrieu, F.2    Herman, E.M.3    Chrispeels, M.J.4
  • 18
    • 0242500364 scopus 로고    scopus 로고
    • Understanding plant responses to drought-from genes to the whole plant
    • doi:10.1071/FP02076
    • Chaves MM, Maroco J, Pereira J (2003) Understanding plant responses to drought-from genes to the whole plant. Funct Plant Biol 30: 2639-2647. doi: 10. 1071/FP02076.
    • (2003) Funct Plant Biol , vol.30 , pp. 2639-2647
    • Chaves, M.M.1    Maroco, J.2    Pereira, J.3
  • 19
    • 0037244871 scopus 로고    scopus 로고
    • Function and specifity of 14-3-3 proteins in the regulation of carbohydrate and nitrogen metabolism
    • doi:10.1093/jxb/erg057
    • Comparot S, Lingiah G, Martin T (2003) Function and specifity of 14-3-3 proteins in the regulation of carbohydrate and nitrogen metabolism. J Exp Bot 54: 595-604. doi: 10. 1093/jxb/erg057.
    • (2003) J Exp Bot , vol.54 , pp. 595-604
    • Comparot, S.1    Lingiah, G.2    Martin, T.3
  • 20
    • 0033080474 scopus 로고    scopus 로고
    • Mutations affecting induction of glycolytic and fermentative genes during germination and environmental stresses in Arabidopsis
    • doi:10.1104/pp.119.2.599
    • Conley TR, Peng HP, Shih MC (1999) Mutations affecting induction of glycolytic and fermentative genes during germination and environmental stresses in Arabidopsis. Plant Physiol 119: 599-607. doi: 10. 1104/pp. 119. 2. 599.
    • (1999) Plant Physiol , vol.119 , pp. 599-607
    • Conley, T.R.1    Peng, H.P.2    Shih, M.C.3
  • 21
    • 0000414374 scopus 로고
    • Surface tension of polyethylene glycol solutuion
    • Couper A, Eley D (1984) Surface tension of polyethylene glycol solutuion. J Polym Sci 3: 345-349.
    • (1984) J Polym Sci , vol.3 , pp. 345-349
    • Couper, A.1    Eley, D.2
  • 22
    • 0030161470 scopus 로고    scopus 로고
    • Abscisic acid induces the alcohol dehydrogenase gene in Arabidopsis
    • doi:10.1104/pp.111.2.381
    • De Bruxelles GL, Peacock WJ, Dennis ES, Dolferus R (1996) Abscisic acid induces the alcohol dehydrogenase gene in Arabidopsis. Plant Physiol 111: 381-391. doi: 10. 1104/pp. 111. 2. 381.
    • (1996) Plant Physiol , vol.111 , pp. 381-391
    • De Bruxelles, G.L.1    Peacock, W.J.2    Dennis, E.S.3    Dolferus, R.4
  • 23
    • 0035112491 scopus 로고    scopus 로고
    • Overexpression of 3-ketoacyl-acyl-carrier protein synthase IIIs in plants reduces the rate of lipid synthesis
    • doi:10.1104/pp.125.2.1103
    • Dehesh K, Tai H, Edwards P, Byrne J, Jaworski JG (2001) Overexpression of 3-ketoacyl-acyl-carrier protein synthase IIIs in plants reduces the rate of lipid synthesis. Plant Physiol 125: 1103-1114. doi: 10. 1104/pp. 125. 2. 1103.
    • (2001) Plant Physiol , vol.125 , pp. 1103-1114
    • Dehesh, K.1    Tai, H.2    Edwards, P.3    Byrne, J.4    Jaworski, J.G.5
  • 24
    • 27644495532 scopus 로고    scopus 로고
    • Proteomic analysis of cellular response to osmotic stress in thick ascending limb of henle's loop (TALH) cells
    • doi:10.1074/mcp.M400184-MCP200
    • Dihazi H, Asif AR, Agarwal NK, Doncheva Y, Müller G (2005) Proteomic analysis of cellular response to osmotic stress in thick ascending limb of henle's loop (TALH) cells. Mol Cell Proteomics 4: 1445-1458. doi: 10. 1074/mcp. M400184-MCP200.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1445-1458
    • Dihazi, H.1    Asif, A.R.2    Agarwal, N.K.3    Doncheva, Y.4    Müller, G.5
  • 25
    • 0028426943 scopus 로고
    • Differential accumulation of S-adenosylmethionine synthetase transcripts in response to salt stress
    • doi:10.1007/BF00023239
    • Espartero J, Pintor-Toro JA, Pardo JM (1994) Differential accumulation of S-adenosylmethionine synthetase transcripts in response to salt stress. Plant Mol Biol 25: 217-227. doi: 10. 1007/BF00023239.
    • (1994) Plant Mol Biol , vol.25 , pp. 217-227
    • Espartero, J.1    Pintor-Toro, J.A.2    Pardo, J.M.3
  • 26
    • 0036240336 scopus 로고    scopus 로고
    • A seedling specific vegetative lectin gene is related to development in Cicer arietinum
    • doi:10.1034/j.1399-3054.2002.1140416.x
    • Esteban R, Dopico B, Muñoz FJ, Romo S, Labrador E (2002) A seedling specific vegetative lectin gene is related to development in Cicer arietinum. Physiol Plant 114: 619-626. doi: 10. 1034/j. 1399-3054. 2002. 1140416. x.
    • (2002) Physiol Plant , vol.114 , pp. 619-626
    • Esteban, R.1    Dopico, B.2    Muñoz, F.J.3    Romo, S.4    Labrador, E.5
  • 27
    • 0003064116 scopus 로고    scopus 로고
    • 14-3-3 proteins and signal transduction
    • doi:10.1146/annurev.arplant.47.1.49
    • Ferl RJ (1996) 14-3-3 proteins and signal transduction. Annu Rev Plant Physiol Plant Mol Biol 47: 49-73. doi: 10. 1146/annurev. arplant. 47. 1. 49.
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 49-73
    • Ferl, R.J.1
  • 29
    • 0036789354 scopus 로고    scopus 로고
    • Importance of methionine biosynthesis for Arabidopsis seed germination and seedling growth
    • doi:10.1034/j.1399-3054.2002.1160214.x
    • Gallardo K, Job C, Groot SPC, Puype M, Demol H, Vandekerckhove J, Job D (2002a) Importance of methionine biosynthesis for Arabidopsis seed germination and seedling growth. Physiol Plant 116: 238-247. doi: 10. 1034/j. 1399-3054. 2002. 1160214. x.
    • (2002) Physiol Plant , vol.116 , pp. 238-247
    • Gallardo, K.1    Job, C.2    Groot, S.P.C.3    Puype, M.4    Demol, H.5    Vandekerckhove, J.6    Job, D.7
  • 30
    • 0035983666 scopus 로고    scopus 로고
    • Proteomics of Arabidopsis seed germination: a comparative study of wild-type and gibberellin-deficient seeds
    • doi:10.1104/pp.002816
    • Gallardo K, Job C, Groot SPC, Puype M, Demol H, Vandekerckhove J, Job D (2002b) Proteomics of Arabidopsis seed germination: a comparative study of wild-type and gibberellin-deficient seeds. Plant Physiol 129: 823-837. doi: 10. 1104/pp. 002816.
    • (2002) Plant Physiol , vol.129 , pp. 823-837
    • Gallardo, K.1    Job, C.2    Groot, S.P.C.3    Puype, M.4    Demol, H.5    Vandekerckhove, J.6    Job, D.7
  • 31
    • 20444450912 scopus 로고    scopus 로고
    • Legumes as a model plant family. Genomics for food and feed report of the cross-legume advances through genomics conference
    • doi:10.1104/pp.105.060871
    • Gepts P, Beavis WD, Brummer C, Shoemaker RC, Stalker HT, Weeden NF, Young ND (2005) Legumes as a model plant family. Genomics for food and feed report of the cross-legume advances through genomics conference. Plant Physiol 137: 1228-1235. doi: 10. 1104/pp. 105. 060871.
    • (2005) Plant Physiol , vol.137 , pp. 1228-1235
    • Gepts, P.1    Beavis, W.D.2    Brummer, C.3    Shoemaker, R.C.4    Stalker, H.T.5    Weeden, N.F.6    Young, N.D.7
  • 32
    • 0031842514 scopus 로고    scopus 로고
    • A peptide concentration and purification method for protein characterization in the subpicomole range using matrix assisted laser desorption/ionization-postsource decay (MALDI-MS) sequencing
    • doi:10.1002/elps.1150190606
    • Gevaert K, Demol H, Sklyarova T, Vandekerckhove J, Houthaeve T (1998) A peptide concentration and purification method for protein characterization in the subpicomole range using matrix assisted laser desorption/ionization-postsource decay (MALDI-MS) sequencing. Electrophoresis 19: 909-917. doi: 10. 1002/elps. 1150190606.
    • (1998) Electrophoresis , vol.19 , pp. 909-917
    • Gevaert, K.1    Demol, H.2    Sklyarova, T.3    Vandekerckhove, J.4    Houthaeve, T.5
  • 33
    • 33745670492 scopus 로고    scopus 로고
    • Osmotic stress-induced changes in germination, growth and soluble sugar content of Sorghum bicolor (L.) moench seeds
    • Gill PK, Sharma AD, Singh P, Bhullar SS (2002) Osmotic stress-induced changes in germination, growth and soluble sugar content of Sorghum bicolor (L.) moench seeds. Bulg J Plant Physiol 28: 12-25.
    • (2002) Bulg J Plant Physiol , vol.28 , pp. 12-25
    • Gill, P.K.1    Sharma, A.D.2    Singh, P.3    Bhullar, S.S.4
  • 34
    • 0034961628 scopus 로고    scopus 로고
    • Evaluation and refinement of a continuous seed germination and early seedling growth test for the use in the ecotoxicological assessment of soils
    • doi:10.1016/S0045-6535(00)00280-0
    • Gong P, Wilke BM, Strozzi E, Fleischmann S (2001) Evaluation and refinement of a continuous seed germination and early seedling growth test for the use in the ecotoxicological assessment of soils. Chemosphere 44: 491-500. doi: 10. 1016/S0045-6535(00)00280-0.
    • (2001) Chemosphere , vol.44 , pp. 491-500
    • Gong, P.1    Wilke, B.M.2    Strozzi, E.3    Fleischmann, S.4
  • 35
    • 84988122211 scopus 로고
    • Elimination of point streaking on silver-stained two-dimensional gels by addition of iodoacetamide to the equilibration buffer
    • doi:10.1002/elps.1150080207
    • Görg A, Postel W, Weser J, Günther S, Strahler JR, Hanash SM, Somerlot L (1987) Elimination of point streaking on silver-stained two-dimensional gels by addition of iodoacetamide to the equilibration buffer. Electrophoresis 8: 122-124. doi: 10. 1002/elps. 1150080207.
    • (1987) Electrophoresis , vol.8 , pp. 122-124
    • Görg, A.1    Postel, W.2    Weser, J.3    Günther, S.4    Strahler, J.R.5    Hanash, S.M.6    Somerlot, L.7
  • 36
    • 0037353554 scopus 로고    scopus 로고
    • Legumes. Importance and constraints to greater use
    • doi:10.1104/pp.017004
    • Graham PH, Vance CP (2003) Legumes. Importance and constraints to greater use. Plant Physiol 131: 872-877. doi: 10. 1104/pp. 017004.
    • (2003) Plant Physiol , vol.131 , pp. 872-877
    • Graham, P.H.1    Vance, C.P.2
  • 37
    • 0036200945 scopus 로고    scopus 로고
    • Molecular biologist's guide to proteomics
    • doi:10.1128/MMBR.66.1.39-63.2002
    • Graves PR, Haystead TAJ (2002) Molecular biologist's guide to proteomics. Microbiol Mol Biol R 66: 39-63. doi: 10. 1128/MMBR. 66. 1. 39-63. 2002.
    • (2002) Microbiol Mol Biol R , vol.66 , pp. 39-63
    • Graves, P.R.1    Haystead, T.A.J.2
  • 38
    • 0032052674 scopus 로고    scopus 로고
    • A moderate decrease of plastid aldolase activity inhibits photosynthesis, alters the levels of sugars and starch, and inhibits growth of potato plants
    • doi:10.1046/j.1365-313X.1998.00089.x
    • Haake V, Zrenner R, Sonnewald U, Stitt M (1998) A moderate decrease of plastid aldolase activity inhibits photosynthesis, alters the levels of sugars and starch, and inhibits growth of potato plants. Plant J 14: 147-157. doi: 10. 1046/j. 1365-313X. 1998. 00089. x.
    • (1998) Plant J , vol.14 , pp. 147-157
    • Haake, V.1    Zrenner, R.2    Sonnewald, U.3    Stitt, M.4
  • 39
    • 0032935808 scopus 로고    scopus 로고
    • Comparison of yeast cell protein solubilization procedures for two-dimensional electrophoresis
    • doi:10.1002/(SICI)1522-2683(19990101)20:4/5<826::AID-ELPS826>3.0.CO;2-A
    • Harder A, Wildgruber R, Nawrocki A, Fey SJ, Larsen PM, Görg A (1999) Comparison of yeast cell protein solubilization procedures for two-dimensional electrophoresis. Electrophoresis 20: 826-829. doi: 10. 1002/(SICI)1522-2683(19990101)20: 4/5<826: AID-ELPS826>3. 0. CO;2-A.
    • (1999) Electrophoresis , vol.20 , pp. 826-829
    • Harder, A.1    Wildgruber, R.2    Nawrocki, A.3    Fey, S.J.4    Larsen, P.M.5    Görg, A.6
  • 40
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: molecular properties, iron storage function and cellular regulation
    • doi:10.1016/0005-2728(96)00022-9
    • Harrison PM, Arosio P (1996) The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1275: 161-203. doi: 10. 1016/0005-2728(96)00022-9.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 41
    • 0034489614 scopus 로고    scopus 로고
    • Plant cellular and molecular responses to high salinity
    • doi:10.1146/annurev.arplant.51.1.463
    • Hasegawa PM, Bressan RA, Zhu JK, Bohnert HJ (2000) Plant cellular and molecular responses to high salinity. Annu Rev Plant Mol Plant Physiol 51: 463-499. doi: 10. 1146/annurev. arplant. 51. 1. 463.
    • (2000) Annu Rev Plant Mol Plant Physiol , vol.51 , pp. 463-499
    • Hasegawa, P.M.1    Bressan, R.A.2    Zhu, J.K.3    Bohnert, H.J.4
  • 42
    • 34249067364 scopus 로고    scopus 로고
    • The 6-phosphogluconate dehydrogenase genes are responsive to abiotic stresses in rice
    • doi:10.1111/j.1744-7909.2007.00460.x
    • Hou FY, Huang J, Yu SL, Zhang HS (2007) The 6-phosphogluconate dehydrogenase genes are responsive to abiotic stresses in rice. J Integr Plant Biol 49: 655-663. doi: 10. 1111/j. 1744-7909. 2007. 00460. x.
    • (2007) J Integr Plant Biol , vol.49 , pp. 655-663
    • Hou, F.Y.1    Huang, J.2    Yu, S.L.3    Zhang, H.S.4
  • 43
    • 85032132015 scopus 로고
    • Gene expression under temperature stress
    • Howarth CJ, Ougham HJ (1993) Gene expression under temperature stress. N Phytol 125: 1-26.
    • (1993) N Phytol , vol.125 , pp. 1-26
    • Howarth, C.J.1    Ougham, H.J.2
  • 44
    • 0345307147 scopus 로고    scopus 로고
    • Molecular cloning and characterization of rice 6-phosphogluconate dehydrogenase gene that is up-regulated by salt stress
    • doi:10.1023/A:1026392422995
    • Huang J, Zhang H, Wang J, Yang J (2003) Molecular cloning and characterization of rice 6-phosphogluconate dehydrogenase gene that is up-regulated by salt stress. Mol Biol Rep 30: 223-227. doi: 10. 1023/A: 1026392422995.
    • (2003) Mol Biol Rep , vol.30 , pp. 223-227
    • Huang, J.1    Zhang, H.2    Wang, J.3    Yang, J.4
  • 45
    • 28544447639 scopus 로고    scopus 로고
    • Increased sensitivity to salt stress in an ascorbate-deficient Arabidopsis mutant
    • doi:10.1111/j.1469-8137.1993.tb03862.x
    • Huang C, He W, Guo J, Chang X, Su P, Zhang L (2005) Increased sensitivity to salt stress in an ascorbate-deficient Arabidopsis mutant. J Exp Bot 56: 3041-3049. doi: 10. 1111/j. 1469-8137. 1993. tb03862. x.
    • (2005) J Exp Bot , vol.56 , pp. 3041-3049
    • Huang, C.1    He, W.2    Guo, J.3    Chang, X.4    Su, P.5    Zhang, L.6
  • 46
    • 2942557132 scopus 로고    scopus 로고
    • Dihydrolipoamide dehydrogenase from porcine heart catalyzes NADH-dependent scavenging of nitric oxide
    • doi:10.1016/j.febslet.2004.05.024
    • Igamberdiev AU, Bykowa NV, Ens W, Hill RD (2004) Dihydrolipoamide dehydrogenase from porcine heart catalyzes NADH-dependent scavenging of nitric oxide. FEBS Lett 568: 146-150. doi: 10. 1016/j. febslet. 2004. 05. 024.
    • (2004) FEBS Lett , vol.568 , pp. 146-150
    • Igamberdiev, A.U.1    Bykowa, N.V.2    Ens, W.3    Hill, R.D.4
  • 47
    • 0001319976 scopus 로고    scopus 로고
    • The molecular basis of dehydration tolerance in plants
    • doi:10.1146/annurev.arplant.47.1.377
    • Ingram J, Bartels D (1996) The molecular basis of dehydration tolerance in plants. Ann Rev Plant Physiol Plant Mol Biol 47: 377-403. doi: 10. 1146/annurev. arplant. 47. 1. 377.
    • (1996) Ann Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 377-403
    • Ingram, J.1    Bartels, D.2
  • 49
    • 0000290462 scopus 로고
    • Low temperature induces the accumulation of alcohol dehydrogenase mRNA in Arabidopsis thaliana, a chilling-tolerant plant
    • doi:10.1104/pp.101.3.833
    • Jarillo JA, Leyva A, Salinas J, Martinez-Zapater JM (1993) Low temperature induces the accumulation of alcohol dehydrogenase mRNA in Arabidopsis thaliana, a chilling-tolerant plant. Plant Physiol 101: 833-837. doi: 10. 1104/pp. 101. 3. 833.
    • (1993) Plant Physiol , vol.101 , pp. 833-837
    • Jarillo, J.A.1    Leyva, A.2    Salinas, J.3    Martinez-Zapater, J.M.4
  • 50
    • 0029105589 scopus 로고
    • Binding-protein expression is subject to temporal, developmental and stress-induced regulation in terminally differentiated soybean organs
    • doi:10.1007/BF00195722
    • Kalinski A, Rowley DL, Loer DS, Foley C, Buta G, Herman EM (1995) Binding-protein expression is subject to temporal, developmental and stress-induced regulation in terminally differentiated soybean organs. Planta 195: 611-621. doi: 10. 1007/BF00195722.
    • (1995) Planta , vol.195 , pp. 611-621
    • Kalinski, A.1    Rowley, D.L.2    Loer, D.S.3    Foley, C.4    Buta, G.5    Herman, E.M.6
  • 51
    • 0033952084 scopus 로고    scopus 로고
    • Induction of alcohol dehydrogenase by plant hormones in alfalfa seedlings
    • doi:10.1023/A:1006253615894
    • Kato-Noguchi H (2000a) Induction of alcohol dehydrogenase by plant hormones in alfalfa seedlings. Plant Growth Regul 30: 1-3. doi: 10. 1023/A: 1006253615894.
    • (2000) Plant Growth Regul , vol.30 , pp. 1-3
    • Kato-Noguchi, H.1
  • 52
    • 0033793029 scopus 로고    scopus 로고
    • Osmotic stress increase alcohol dehydrogenase activity in maize seedlings
    • doi:10.1023/A:1002864318871
    • Kato-Noguchi H (2000b) Osmotic stress increase alcohol dehydrogenase activity in maize seedlings. Biol Plant 43: 621-624. doi: 10. 1023/A: 1002864318871.
    • (2000) Biol Plant , vol.43 , pp. 621-624
    • Kato-Noguchi, H.1
  • 53
    • 2542642407 scopus 로고    scopus 로고
    • Differential mRNA translation contributes to gene regulation under non-stress and dehydration stress conditions in Arabidopsis thaliana
    • doi:10.1111/j.1365-313X.2004.02090.x
    • Kawaguchi R, Girke T, Bray EA, Bailey-Serres J (2004) Differential mRNA translation contributes to gene regulation under non-stress and dehydration stress conditions in Arabidopsis thaliana. Plant J 38: 823-839. doi: 10. 1111/j. 1365-313X. 2004. 02090. x.
    • (2004) Plant J , vol.38 , pp. 823-839
    • Kawaguchi, R.1    Girke, T.2    Bray, E.A.3    Bailey-Serres, J.4
  • 54
    • 0036735712 scopus 로고    scopus 로고
    • +-ATPase and increased 14-3-3 protein content in plasma membrane of tomato cells upon osmotic shock
    • doi:10.1034/j.1399-3054.2002.1160105.x
    • +-ATPase and increased 14-3-3 protein content in plasma membrane of tomato cells upon osmotic shock. Physiol Plant 116: 37-41. doi: 10. 1034/j. 1399-3054. 2002. 1160105. x.
    • (2002) Physiol Plant , vol.116 , pp. 37-41
    • Kerkeb, L.1    Venema, K.2    Donaire, J.P.3    Rodriguez-Rosales, M.P.4
  • 56
    • 84875522334 scopus 로고    scopus 로고
    • Molekularne podstawy odpowiedzi roślin na niska{ogonek} temperature{ogonek}
    • Kmieć B, Drynda R, Wołoszyńska M (2005) Molekularne podstawy odpowiedzi roślin na niska{ogonek} temperature{ogonek}. Biotechnologia 3: 184-200.
    • (2005) Biotechnologia , vol.3 , pp. 184-200
    • Kmieć, B.1    Drynda, R.2    Wołoszyńska, M.3
  • 57
    • 84894255551 scopus 로고    scopus 로고
    • Phytoalexin protects plants
    • Kuniga T (2004) Phytoalexin protects plants. Foods Food Ingred J Jpn 209: 1117-1127.
    • (2004) Foods Food Ingred J Jpn , vol.209 , pp. 1117-1127
    • Kuniga, T.1
  • 58
    • 0013500751 scopus 로고    scopus 로고
    • Plant protein kinase genes induced by drought, high salinity and cold stress
    • Liu Q, Zhang Y, Chen SY (2000) Plant protein kinase genes induced by drought, high salinity and cold stress. Chin Sci Bull 45: 1153-1157.
    • (2000) Chin Sci Bull , vol.45 , pp. 1153-1157
    • Liu, Q.1    Zhang, Y.2    Chen, S.Y.3
  • 59
    • 33947534869 scopus 로고    scopus 로고
    • Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses
    • doi:10.1105/tpc.106.041376
    • Liu CHJ, Deavours BE, Richard SB, Ferrer JL, Blount JW, Huhman D, Dixon RA, Noel JP (2006) Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses. Plant Cell 18: 3656-3669. doi: 10. 1105/tpc. 106. 041376.
    • (2006) Plant Cell , vol.18 , pp. 3656-3669
    • Liu, C.H.J.1    Deavours, B.E.2    Richard, S.B.3    Ferrer, J.L.4    Blount, J.W.5    Huhman, D.6    Dixon, R.A.7    Noel, J.P.8
  • 60
    • 0000436359 scopus 로고
    • The expression pattern of the tonoplast intrinsic protein γ-TIP in Arabidopsis thaliana is correlated with cell enlargement
    • doi:10.1104/pp.100.4.1633
    • Ludevid D, Höfte H, Himelblau E, Chrispeels MJ (1992) The expression pattern of the tonoplast intrinsic protein γ-TIP in Arabidopsis thaliana is correlated with cell enlargement. Plant Physiol 100: 1633-1639. doi: 10. 1104/pp. 100. 4. 1633.
    • (1992) Plant Physiol , vol.100 , pp. 1633-1639
    • Ludevid, D.1    Höfte, H.2    Himelblau, E.3    Chrispeels, M.J.4
  • 61
    • 0347298563 scopus 로고    scopus 로고
    • Plasma membrane aquaporins play a significant role during recovery from water deficit
    • doi:10.1104/pp.009019
    • Martre P, Morillon R, Barrieu F, North GB, Nobel PN, Chrispeels MJ (2002) Plasma membrane aquaporins play a significant role during recovery from water deficit. Plant Physiol 130: 2101-2110. doi: 10. 1104/pp. 009019.
    • (2002) Plant Physiol , vol.130 , pp. 2101-2110
    • Martre, P.1    Morillon, R.2    Barrieu, F.3    North, G.B.4    Nobel, P.N.5    Chrispeels, M.J.6
  • 62
    • 0035525061 scopus 로고    scopus 로고
    • Establishment of a root proteome reference map for the model legume Medicago truncatula using the expressed sequence tag database for peptide mass fingerprinting
    • doi:10.1002/1615-9861(200111)1:11<1424
    • Mathesius U, Keijzers G, Natera SH, Weinman JJ, Djordjevic MA, Rolfe BG (2001) Establishment of a root proteome reference map for the model legume Medicago truncatula using the expressed sequence tag database for peptide mass fingerprinting. Proteomics 1: 1424-1440. doi: 10. 1002/1615-9861(200111)1: 11<1424.
    • (2001) Proteomics , vol.1 , pp. 1424-1440
    • Mathesius, U.1    Keijzers, G.2    Natera, S.H.3    Weinman, J.J.4    Djordjevic, M.A.5    Rolfe, B.G.6
  • 63
    • 0022385984 scopus 로고
    • Differential expression of the three yeast glyceraldehydes-3-phosphate dehydrogenase genes
    • McAlister L, Holland MJ (1985) Differential expression of the three yeast glyceraldehydes-3-phosphate dehydrogenase genes. J Biol Chem 260: 15019-15027.
    • (1985) J Biol Chem , vol.260 , pp. 15019-15027
    • McAlister, L.1    Holland, M.J.2
  • 64
    • 0030188522 scopus 로고    scopus 로고
    • The Arabidopsis ACT7 actin gene is expressed in rapidly developing tissue and responds to several external stimuli
    • doi:10.1104/pp.111.3.699
    • McDowell JM, An YQ, Huang S, McKinney EC, Meagher RB (1996) The Arabidopsis ACT7 actin gene is expressed in rapidly developing tissue and responds to several external stimuli. Plant Physiol 111: 699-711. doi: 10. 1104/pp. 111. 3. 699.
    • (1996) Plant Physiol , vol.111 , pp. 699-711
    • McDowell, J.M.1    An, Y.Q.2    Huang, S.3    McKinney, E.C.4    Meagher, R.B.5
  • 65
    • 34047135374 scopus 로고    scopus 로고
    • Phytoalexins: defence or just a response to stress?
    • Mert-Türk F (2002) Phytoalexins: defence or just a response to stress? J Cell Mol Biol 1: 1-6.
    • (2002) J Cell Mol Biol , vol.1 , pp. 1-6
    • Mert-Türk, F.1
  • 66
    • 0000191196 scopus 로고
    • Auxin-stimulated NADH oxidase (semidehydroascorbate reductase) of soybean plasma membrane: role in acidification of cytoplasm
    • doi:10.1007/BF01304635
    • Morre DJ, Navas P, Penel C, Castillo FJ (1986) Auxin-stimulated NADH oxidase (semidehydroascorbate reductase) of soybean plasma membrane: role in acidification of cytoplasm. Protoplasma 133: 195-197. doi: 10. 1007/BF01304635.
    • (1986) Protoplasma , vol.133 , pp. 195-197
    • Morre, D.J.1    Navas, P.2    Penel, C.3    Castillo, F.J.4
  • 67
    • 0036679089 scopus 로고    scopus 로고
    • Comparative effects of NaCl and polyethylene glycol on germination, emergence and seedling growth of cowpea
    • doi:10.1046/j.1439-037X.2002.00563.x
    • Murillo-Amador B, López-Aguilar R, Kaya C, Larrinaga-Mayoral J, Flores-Hernández A (2002) Comparative effects of NaCl and polyethylene glycol on germination, emergence and seedling growth of cowpea. J Agron Crop Sci 188: 235-247. doi: 10. 1046/j. 1439-037X. 2002. 00563. x.
    • (2002) J Agron Crop Sci , vol.188 , pp. 235-247
    • Murillo-Amador, B.1    López-Aguilar, R.2    Kaya, C.3    Larrinaga-Mayoral, J.4    Flores-Hernández, A.5
  • 68
    • 84986967777 scopus 로고
    • A storage role for albumins in pea cotyledons
    • doi:10.1111/j.1365-3040.1979.tb00073.x
    • Murray DR (1979) A storage role for albumins in pea cotyledons. Plant Cell Environ 2: 221-226. doi: 10. 1111/j. 1365-3040. 1979. tb00073. x.
    • (1979) Plant Cell Environ , vol.2 , pp. 221-226
    • Murray, D.R.1
  • 69
    • 0030942257 scopus 로고    scopus 로고
    • Differences in the regulation of iron regulatory protein-1 (IRP-1) by extra-and intracellular oxidative stress
    • doi:10.1074/jbc.272.15.9802
    • Pantopoulos K, Mueller S, Atzberger A, Ansorge W, Stremmel W, Hentze MW (1997) Differences in the regulation of iron regulatory protein-1 (IRP-1) by extra-and intracellular oxidative stress. J Biol Chem 272: 9802-9808. doi: 10. 1074/jbc. 272. 15. 9802.
    • (1997) J Biol Chem , vol.272 , pp. 9802-9808
    • Pantopoulos, K.1    Mueller, S.2    Atzberger, A.3    Ansorge, W.4    Stremmel, W.5    Hentze, M.W.6
  • 70
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • doi:10.1016/0960-9822(93)90195-T
    • Pappin DJC, Hojrup P, Bleasby AJ (1993) Rapid identification of proteins by peptide-mass fingerprinting. Curr Biol 3: 327-332. doi: 10. 1016/0960-9822(93)90195-T.
    • (1993) Curr Biol , vol.3 , pp. 327-332
    • Pappin, D.J.C.1    Hojrup, P.2    Bleasby, A.J.3
  • 71
    • 0035504261 scopus 로고    scopus 로고
    • Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family
    • doi:10.1042/0264-6021:3590575
    • Petit JM, Briat JF, Lobreáux S (2001) Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family. Biochem J 359: 575-582. doi: 10. 1042/0264-6021: 3590575.
    • (2001) Biochem J , vol.359 , pp. 575-582
    • Petit, J.M.1    Briat, J.F.2    Lobreáux, S.3
  • 72
    • 0034858417 scopus 로고    scopus 로고
    • Some features of NADP-dependent isocitrate dehydrogenase functioning in pea leaves upon exposure to salt stress
    • doi:10.1023/A:1009406830497
    • Popova OV, Popova TN, Izmailov SF (2001) Some features of NADP-dependent isocitrate dehydrogenase functioning in pea leaves upon exposure to salt stress. Biol Bull 28: 134-138. doi: 10. 1023/A: 1009406830497.
    • (2001) Biol Bull , vol.28 , pp. 134-138
    • Popova, O.V.1    Popova, T.N.2    Izmailov, S.F.3
  • 73
    • 0034476937 scopus 로고    scopus 로고
    • Entering an era of water scarcity
    • doi: 10. 1890/1051-0761(2000)010[0941: EAEOWS]2. 0. CO;2
    • Postel SL (2000) Entering an era of water scarcity. Ecol Appl 10: 941-948. doi: 10. 1890/1051-0761(2000)010[0941: EAEOWS]2. 0. CO;2.
    • (2000) Ecol Appl , vol.10 , pp. 941-948
    • Postel, S.L.1
  • 74
    • 0001292265 scopus 로고
    • Purification and characterization of S-adenosyl-l-methionine:6a-hydroxymaackiain 3-O-methyltransferase from Pisum sativum
    • Preisig CL, Matthews DE, VanEtten HD (1989) Purification and characterization of S-adenosyl-l-methionine: 6a-hydroxymaackiain 3-O-methyltransferase from Pisum sativum. Plant Physiol 91: 559-566.
    • (1989) Plant Physiol , vol.91 , pp. 559-566
    • Preisig, C.L.1    Matthews, D.E.2    VanEtten, H.D.3
  • 75
    • 0000753841 scopus 로고
    • Rice cytosolic glyceraldehyde 3-phosphate dehydrogenase contains two subunits differentially regulated by anaerobiosis
    • doi:10.1007/BF00020498
    • Ricard B, Rivoal J, Pradet A (1989) Rice cytosolic glyceraldehyde 3-phosphate dehydrogenase contains two subunits differentially regulated by anaerobiosis. Plant Mol Biol 12: 131-139. doi: 10. 1007/BF00020498.
    • (1989) Plant Mol Biol , vol.12 , pp. 131-139
    • Ricard, B.1    Rivoal, J.2    Pradet, A.3
  • 76
    • 4444271855 scopus 로고    scopus 로고
    • Proteome reference maps of vegetative tissues in pea. An investigation of nitrogen mobilization from leaves during seed filling
    • doi:10.1104/pp.104.041947
    • Schiltz S, Gallardo K, Huart M, Negroni L, Sommerer N, Burstin J (2004) Proteome reference maps of vegetative tissues in pea. An investigation of nitrogen mobilization from leaves during seed filling. Plant Physiol 135: 2241-2260. doi: 10. 1104/pp. 104. 041947.
    • (2004) Plant Physiol , vol.135 , pp. 2241-2260
    • Schiltz, S.1    Gallardo, K.2    Huart, M.3    Negroni, L.4    Sommerer, N.5    Burstin, J.6
  • 77
    • 0030977750 scopus 로고    scopus 로고
    • Three differentially expressed S-adenosylmethionine synthetase from Catharanthus roseus: molecular and functional characterization
    • doi:10.1023/A:1005711720930
    • Schröder G, Eichel J, Breinig S, Schröder J (1997) Three differentially expressed S-adenosylmethionine synthetase from Catharanthus roseus: molecular and functional characterization. Plant Mol Biol 33: 211-222. doi: 10. 1023/A: 1005711720930.
    • (1997) Plant Mol Biol , vol.33 , pp. 211-222
    • Schröder, G.1    Eichel, J.2    Breinig, S.3    Schröder, J.4
  • 78
    • 0038323167 scopus 로고    scopus 로고
    • Control mechanisms of lectin accumulation in wheat seedlings under salinity
    • doi:10.1016/S0168-9452(02)00415-6
    • Shakirova FM, Bezrukova MV, Aval'baev AM, Fatkhutdinova RA (2003) Control mechanisms of lectin accumulation in wheat seedlings under salinity. Russ J. Plant Physiol 50: 301-304. doi: 10. 1016/S0168-9452(02)00415-6.
    • (2003) Russ J. Plant Physiol , vol.50 , pp. 301-304
    • Shakirova, F.M.1    Bezrukova, M.V.2    Aval'baev, A.M.3    Fatkhutdinova, R.A.4
  • 79
    • 1542743168 scopus 로고    scopus 로고
    • Proton pumping in growing part of maize root: its correlation with 14-3-3 protein content and changes in response to osmotic stress
    • doi:10.1023/B:BIRY.0000011653.46422.c3
    • Shanko AV, Mesenko MM, Klychnikov OI, Nosov AV, Ivanov VB (2003) Proton pumping in growing part of maize root: its correlation with 14-3-3 protein content and changes in response to osmotic stress. Biochemistry 68: 1320-1326. doi: 10. 1023/B: BIRY. 0000011653. 46422. c3.
    • (2003) Biochemistry , vol.68 , pp. 1320-1326
    • Shanko, A.V.1    Mesenko, M.M.2    Klychnikov, O.I.3    Nosov, A.V.4    Ivanov, V.B.5
  • 80
    • 21344432430 scopus 로고    scopus 로고
    • Molecular mechanisms of higher plant adaptation to environment
    • Shao HB, Liang ZS, Shao MA (2005) Molecular mechanisms of higher plant adaptation to environment. Acta Ecol Sin 257: 1772-1781.
    • (2005) Acta Ecol Sin , vol.257 , pp. 1772-1781
    • Shao, H.B.1    Liang, Z.S.2    Shao, M.A.3
  • 81
    • 33646520905 scopus 로고    scopus 로고
    • Effect of temperature on secondary metabolites production and antioxidant enzyme activities in Eleutherococcus senticosus somatic embryos
    • doi:10.1007/s11240-005-9075-x
    • Shohael AM, Ali MB, Yu KW, Hahn EJ, Paek KJ (2006) Effect of temperature on secondary metabolites production and antioxidant enzyme activities in Eleutherococcus senticosus somatic embryos. Plant Cell Tissue Organ Cult 85: 219-228. doi: 10. 1007/s11240-005-9075-x.
    • (2006) Plant Cell Tissue Organ Cult , vol.85 , pp. 219-228
    • Shohael, A.M.1    Ali, M.B.2    Yu, K.W.3    Hahn, E.J.4    Paek, K.J.5
  • 83
    • 0034921854 scopus 로고    scopus 로고
    • MIP genes are down-regulated under drought stress in Nicotiana glauca
    • doi:10.1093/pcp/pce085
    • Smart LB, Moskal WA, Cameron KD, Bennett AB (2001) MIP genes are down-regulated under drought stress in Nicotiana glauca. Plant Cell Physiol 42: 686-693. doi: 10. 1093/pcp/pce085.
    • (2001) Plant Cell Physiol , vol.42 , pp. 686-693
    • Smart, L.B.1    Moskal, W.A.2    Cameron, K.D.3    Bennett, A.B.4
  • 84
    • 0036984330 scopus 로고    scopus 로고
    • Induction of phytoalexin accumulation in broad bean (Vicia faba L.) cotyledons following treatments with biotic and abiotic elicitors
    • Soylu S, Bennett MH, Mansfield JW (2002) Induction of phytoalexin accumulation in broad bean (Vicia faba L.) cotyledons following treatments with biotic and abiotic elicitors. Turk J Agric For 26: 343-348.
    • (2002) Turk J Agric For , vol.26 , pp. 343-348
    • Soylu, S.1    Bennett, M.H.2    Mansfield, J.W.3
  • 85
    • 84894251868 scopus 로고    scopus 로고
    • Wpływm stresów abiotycznych na plonowanie roślin
    • R. J. Górecki and S. Grzsiuk (Eds.), Olsztyn: UWM
    • Starck Z (2002) Wpływm stresów abiotycznych na plonowanie roślin. In: Górecki RJ, Grzsiuk S (eds) Fizjologia plonowania roślin. UWM, Olsztyn, pp 447-486.
    • (2002) Fizjologia Plonowania roślin , pp. 447-486
    • Starck, Z.1
  • 86
    • 0008988045 scopus 로고
    • Synthesis of the phytoalexin pisatin by a methyltransferase from pea
    • doi:10.1104/pp.80.1.277
    • Sweigard JA, Matthews DE, VanEtten HD (1986) Synthesis of the phytoalexin pisatin by a methyltransferase from pea. Plant Physiol 80: 277-279. doi: 10. 1104/pp. 80. 1. 277.
    • (1986) Plant Physiol , vol.80 , pp. 277-279
    • Sweigard, J.A.1    Matthews, D.E.2    VanEtten, H.D.3
  • 87
    • 0025941117 scopus 로고
    • Characteristics of the interaction of the ferritin repressor protein with the iron-responsive element
    • doi:10.1007/BF01135557
    • Swenson GR, Patino MM, Beck MM, Gaffield L, Walden WE (1991) Characteristics of the interaction of the ferritin repressor protein with the iron-responsive element. Biol Met 4: 48-55. doi: 10. 1007/BF01135557.
    • (1991) Biol Met , vol.4 , pp. 48-55
    • Swenson, G.R.1    Patino, M.M.2    Beck, M.M.3    Gaffield, L.4    Walden, W.E.5
  • 88
    • 0033806845 scopus 로고    scopus 로고
    • Control of abscisic acid synthesis
    • doi:10.1093/jexbot/51.350.1563
    • Taylor IB, Burbidge A, Thompson AJ (2000) Control of abscisic acid synthesis. J Exp Bot 51: 1563-1575. doi: 10. 1093/jexbot/51. 350. 1563.
    • (2000) J Exp Bot , vol.51 , pp. 1563-1575
    • Taylor, I.B.1    Burbidge, A.2    Thompson, A.J.3
  • 89
    • 13844253987 scopus 로고    scopus 로고
    • Nutritional assessment of raw and germinated pea (Pisum sativum L.) protein and carbohydrate by in vitro and in vivo techniques
    • doi:10.1016/j.nut.2004.04.025
    • Urbano G, Lopez-Jurado M, Frejnagel S, Gomez-Villalva E, Porres JM, Frias J, Vidal-Valverde C, Aranda P (2005) Nutritional assessment of raw and germinated pea (Pisum sativum L.) protein and carbohydrate by in vitro and in vivo techniques. Nutrition 21: 230-239. doi: 10. 1016/j. nut. 2004. 04. 025.
    • (2005) Nutrition , vol.21 , pp. 230-239
    • Urbano, G.1    Lopez-Jurado, M.2    Frejnagel, S.3    Gomez-Villalva, E.4    Porres, J.M.5    Frias, J.6    Vidal-Valverde, C.7    Aranda, P.8
  • 90
    • 0032445817 scopus 로고    scopus 로고
    • Cu/Zn superoxide dismutase, glutathione reductase and ascorbate peroxidase levels during drought stress in potato
    • van Der Mescht A, De Ronde JA, Rossouw FT (1998) Cu/Zn superoxide dismutase, glutathione reductase and ascorbate peroxidase levels during drought stress in potato. S Afr J Sci 94: 496-499.
    • (1998) S Afr J Sci , vol.94 , pp. 496-499
    • van Der Mescht, A.1    De Ronde, J.A.2    Rossouw, F.T.3
  • 91
    • 4444221804 scopus 로고    scopus 로고
    • Novel regulation of aquaporins during osmotic stress
    • doi:10.1104/pp.104.044891
    • Vera-Estrella R, Barkla BJ, Bohnert HJ, Pantoja O (2004) Novel regulation of aquaporins during osmotic stress. Plant Physiol 135: 2318-2329. doi: 10. 1104/pp. 104. 044891.
    • (2004) Plant Physiol , vol.135 , pp. 2318-2329
    • Vera-Estrella, R.1    Barkla, B.J.2    Bohnert, H.J.3    Pantoja, O.4
  • 93
    • 0037356823 scopus 로고    scopus 로고
    • Can we improve the nutritional quality of legume seeds?
    • doi:10.1104/pp.102.017665
    • Wang TL, Domoney C, Hedley CL, Casey R, Grusak MA (2003) Can we improve the nutritional quality of legume seeds? Plant Physiol 131: 886-891. doi: 10. 1104/pp. 102. 017665.
    • (2003) Plant Physiol , vol.131 , pp. 886-891
    • Wang, T.L.1    Domoney, C.2    Hedley, C.L.3    Casey, R.4    Grusak, M.A.5
  • 94
    • 0031282612 scopus 로고    scopus 로고
    • Isolation of the cDNAs encoding (+)6a-hydroxymaackiain 3-O-methyltransferase, the terminal strep for the synthesis of the phytoalexin pisatin in Pisum sativum
    • doi:10.1023/A:1005836508844
    • Wu Q, Preisig CL, VanEtten HD (1997) Isolation of the cDNAs encoding (+)6a-hydroxymaackiain 3-O-methyltransferase, the terminal strep for the synthesis of the phytoalexin pisatin in Pisum sativum. Plant Mol Biol 35: 551-560. doi: 10. 1023/A: 1005836508844.
    • (1997) Plant Mol Biol , vol.35 , pp. 551-560
    • Wu, Q.1    Preisig, C.L.2    VanEtten, H.D.3
  • 95
    • 0036273511 scopus 로고    scopus 로고
    • Cell signaling during cold, drought, and salt stress
    • doi:10.1105/tpc.000596
    • Xiong L, Schumaker KS, Zhu JK (2002) Cell signaling during cold, drought, and salt stress. Plant Cell supplement: S165-S183. doi: 10. 1105/tpc. 000596.
    • (2002) Plant Cell , Issue.SUPPL. , pp. 165-183
    • Xiong, L.1    Schumaker, K.S.2    Zhu, J.K.3
  • 96
    • 0001181290 scopus 로고
    • Sensitivity to abscisic acid and osmoticum changes during embryogenesis of alfalfa (Medicago sativa)
    • doi:10.1093/jxb/42.6.821
    • Xu N, Bewley JD (1991) Sensitivity to abscisic acid and osmoticum changes during embryogenesis of alfalfa (Medicago sativa). J Exp Bot 42: 821-826. doi: 10. 1093/jxb/42. 6. 821.
    • (1991) J Exp Bot , vol.42 , pp. 821-826
    • Xu, N.1    Bewley, J.D.2
  • 97
    • 0034658010 scopus 로고    scopus 로고
    • Differential expression of plastidic aldolase genes in Nicotiana plants under salt stress
    • doi:10.1016/S0168-9452(00)00188-6
    • Yamada S, Komori T, Hashimoto A, Kuwata S, Imaseki H, Kubo T (2000) Differential expression of plastidic aldolase genes in Nicotiana plants under salt stress. Plant Sci 154: 61-69. doi: 10. 1016/S0168-9452(00)00188-6.
    • (2000) Plant Sci , vol.154 , pp. 61-69
    • Yamada, S.1    Komori, T.2    Hashimoto, A.3    Kuwata, S.4    Imaseki, H.5    Kubo, T.6
  • 98
    • 4644285404 scopus 로고    scopus 로고
    • Overexpression of the Arabidopsis 14-3-3 protein GF14λ in cotton leads to "stay-green" phenotype and improves stress tolerance under moderate drought conditions
    • Yan J, He C, Wang J, Mao Z, Holaday SA, Allen RD, Zhang H (2004) Overexpression of the Arabidopsis 14-3-3 protein GF14λ in cotton leads to "stay-green" phenotype and improves stress tolerance under moderate drought conditions. Plant Cell Physiol 5: 1007-1014.
    • (2004) Plant Cell Physiol , vol.5 , pp. 1007-1014
    • Yan, J.1    He, C.2    Wang, J.3    Mao, Z.4    Holaday, S.A.5    Allen, R.D.6    Zhang, H.7
  • 99
    • 21344435270 scopus 로고    scopus 로고
    • The accumulation of phytoalexin in cucumber plant after stress
    • doi:10.1016/j.colsurfb.2005.03.018
    • Zhao HC, Li GJ, Wang JB (2005) The accumulation of phytoalexin in cucumber plant after stress. Colloids Surf B Biointerfaces 43: 187-193. doi: 10. 1016/j. colsurfb. 2005. 03. 018.
    • (2005) Colloids Surf B Biointerfaces , vol.43 , pp. 187-193
    • Zhao, H.C.1    Li, G.J.2    Wang, J.B.3
  • 100
    • 0037227958 scopus 로고    scopus 로고
    • ADP ribosylation factor regulates metabolism and antioxidant capacity of transgenic potato tubers
    • doi:10.1021/jf020779r
    • Żuk M, Prescha A, Ke{ogonek}pczyński J, Szopa J (2003) ADP ribosylation factor regulates metabolism and antioxidant capacity of transgenic potato tubers. J Agric Food Chem 51: 288-294. doi: 10. 1021/jf020779r.
    • (2003) J Agric Food Chem , vol.51 , pp. 288-294
    • Zuk, M.1    Prescha, A.2    Kepczyński, J.3    Szopa, J.4


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