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Volumn 67, Issue , 2013, Pages 7-14

Proteomics reveal cucumber Spd-responses under normal condition and salt stress

Author keywords

Cucumber; Proteomics; Salt stress; Spermidine

Indexed keywords

CUCUMIS SATIVUS;

EID: 84875590827     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2013.02.016     Document Type: Article
Times cited : (62)

References (40)
  • 1
    • 69349099692 scopus 로고    scopus 로고
    • Recent developments in understanding salinity tolerance
    • Türkan I., Demiral T. Recent developments in understanding salinity tolerance. Environ. Exp. Bot. 2009, 67:2-9.
    • (2009) Environ. Exp. Bot. , vol.67 , pp. 2-9
    • Türkan, I.1    Demiral, T.2
  • 2
    • 35248837430 scopus 로고    scopus 로고
    • Modulation of spermidine and spermine levels in maize seedlings subjected to long-term salt stress
    • Jiménez-Bremont J.F., Ruiz O.A., Rodríguez-Kessler M. Modulation of spermidine and spermine levels in maize seedlings subjected to long-term salt stress. Plant Physiol. Biochem. 2007, 45:812-821.
    • (2007) Plant Physiol. Biochem. , vol.45 , pp. 812-821
    • Jiménez-Bremont, J.F.1    Ruiz, O.A.2    Rodríguez-Kessler, M.3
  • 3
    • 3142567130 scopus 로고    scopus 로고
    • Overexpression of spermidine synthase enhances tolerance to multiple environmental stresses and up-regulates the expression of various stress-regulated genes in transgenic Arabidopsis thaliana
    • Kasukabe Y., He L., Nada K., Misawa S., Ihara I., Tachibana S. Overexpression of spermidine synthase enhances tolerance to multiple environmental stresses and up-regulates the expression of various stress-regulated genes in transgenic Arabidopsis thaliana. Plant Cell Physiol. 2004, 45:712-722.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 712-722
    • Kasukabe, Y.1    He, L.2    Nada, K.3    Misawa, S.4    Ihara, I.5    Tachibana, S.6
  • 4
    • 51249093660 scopus 로고    scopus 로고
    • Exogenous spermidine affects polyamine metabolism in salinity-stressed Cucumis sativus roots and enhances short-term salinity tolerance
    • Duan J., Li J., Guo S., Kang Y. Exogenous spermidine affects polyamine metabolism in salinity-stressed Cucumis sativus roots and enhances short-term salinity tolerance. J. Plant Physiol. 2008, 165:1620-1635.
    • (2008) J. Plant Physiol. , vol.165 , pp. 1620-1635
    • Duan, J.1    Li, J.2    Guo, S.3    Kang, Y.4
  • 6
    • 70449382488 scopus 로고    scopus 로고
    • The effect of salinity on lipid peroxidation and some antioxidant enzyme activities in two cucumber cultivars
    • Baysal G., Tipirdamaz R. The effect of salinity on lipid peroxidation and some antioxidant enzyme activities in two cucumber cultivars. Acta Hortic. 2007, 729:199-203.
    • (2007) Acta Hortic. , vol.729 , pp. 199-203
    • Baysal, G.1    Tipirdamaz, R.2
  • 7
    • 77949555883 scopus 로고    scopus 로고
    • Applying spermidine for differential responses of antioxidant enzymes in cucumber subjected to short-term salinity
    • Du C.X., Fan H.F., Guo S.R., Tezuka T. Applying spermidine for differential responses of antioxidant enzymes in cucumber subjected to short-term salinity. J. Am. Soc. Hortic. Sci. 2010, 135:18-24.
    • (2010) J. Am. Soc. Hortic. Sci. , vol.135 , pp. 18-24
    • Du, C.X.1    Fan, H.F.2    Guo, S.R.3    Tezuka, T.4
  • 8
    • 0033601838 scopus 로고    scopus 로고
    • Polyamines and environmental challenges: recent development
    • Bouchereau A., Aziz A., Larher F., Martin-Tanguy J. Polyamines and environmental challenges: recent development. Plant Sci. 1999, 140:103-125.
    • (1999) Plant Sci. , vol.140 , pp. 103-125
    • Bouchereau, A.1    Aziz, A.2    Larher, F.3    Martin-Tanguy, J.4
  • 9
    • 17844397216 scopus 로고    scopus 로고
    • Effects of salt stress on basic processes of photosynthesis
    • Sudhir P., Murthy S. Effects of salt stress on basic processes of photosynthesis. Photosynthetica 2004, 42:481-486.
    • (2004) Photosynthetica , vol.42 , pp. 481-486
    • Sudhir, P.1    Murthy, S.2
  • 10
    • 59849088805 scopus 로고    scopus 로고
    • Photosynthesis under drought and salt stress: regulation mechanisms from whole plant to cell
    • Chaves M., Flexas J., Pinheiro C. Photosynthesis under drought and salt stress: regulation mechanisms from whole plant to cell. Ann. Bot. 2009, 103:551-560.
    • (2009) Ann. Bot. , vol.103 , pp. 551-560
    • Chaves, M.1    Flexas, J.2    Pinheiro, C.3
  • 11
    • 71349087543 scopus 로고    scopus 로고
    • Effects of exogenous putrescine on gas-exchange characteristics and chlorophyll fluorescence of NaCl-stressed cucumber seedlings
    • Zhang R.H., Li J., Guo S.R., Tezuka T. Effects of exogenous putrescine on gas-exchange characteristics and chlorophyll fluorescence of NaCl-stressed cucumber seedlings. Photosynth. Res. 2009, 100:155-162.
    • (2009) Photosynth. Res. , vol.100 , pp. 155-162
    • Zhang, R.H.1    Li, J.2    Guo, S.R.3    Tezuka, T.4
  • 13
    • 0036005921 scopus 로고    scopus 로고
    • Enhanced susceptibility of photosynthesis to low-temperature photoinhibition due to interruption of chill-induced increase of S-adenosylmethionine decarboxylase activity in leaves of spinach (Spinacia oleracea L.)
    • He L., Nada K., Kasukabe Y., Tachibana S. Enhanced susceptibility of photosynthesis to low-temperature photoinhibition due to interruption of chill-induced increase of S-adenosylmethionine decarboxylase activity in leaves of spinach (Spinacia oleracea L.). Plant Cell. Physiol. 2002, 43:196-206.
    • (2002) Plant Cell. Physiol. , vol.43 , pp. 196-206
    • He, L.1    Nada, K.2    Kasukabe, Y.3    Tachibana, S.4
  • 15
    • 0031282485 scopus 로고    scopus 로고
    • Isolation and characterization of an Arabidopsis biotin carboxylase gene and its promoter
    • Bao X., Shorrosh B.S., Ohlrogge J.B. Isolation and characterization of an Arabidopsis biotin carboxylase gene and its promoter. Plant Mol. Biol. 1997, 35:539-550.
    • (1997) Plant Mol. Biol. , vol.35 , pp. 539-550
    • Bao, X.1    Shorrosh, B.S.2    Ohlrogge, J.B.3
  • 16
  • 18
    • 0035148521 scopus 로고    scopus 로고
    • Phylogenetic analyses and comparative genomics of vitamin B6 (pyridoxine) and pyridoxal phosphate biosynthesis pathways
    • Mittenhuber G. Phylogenetic analyses and comparative genomics of vitamin B6 (pyridoxine) and pyridoxal phosphate biosynthesis pathways. J. Mol. Microb. Biotech. 2001, 3:1-20.
    • (2001) J. Mol. Microb. Biotech. , vol.3 , pp. 1-20
    • Mittenhuber, G.1
  • 20
    • 11844266632 scopus 로고    scopus 로고
    • Salt stress enhances xylem development and expression of S-adenosyl-l-methionine synthase in lignifying tissues of tomato plants
    • Sanchez-Aguayo I., Rodriguez-Galan J.M., Garcia R., Torreblanca J., Pardo J.M. Salt stress enhances xylem development and expression of S-adenosyl-l-methionine synthase in lignifying tissues of tomato plants. Planta 2004, 220:278-285.
    • (2004) Planta , vol.220 , pp. 278-285
    • Sanchez-Aguayo, I.1    Rodriguez-Galan, J.M.2    Garcia, R.3    Torreblanca, J.4    Pardo, J.M.5
  • 21
    • 77958513940 scopus 로고    scopus 로고
    • Overexpression of suadea salsa S-adenosylmethionine synthetase gene promotes salt tolerance in transgenic tobacco
    • Qi Y.C., Wang F.F., Zhang H., Liu W.Q. Overexpression of suadea salsa S-adenosylmethionine synthetase gene promotes salt tolerance in transgenic tobacco. Acta Physiol. Plant 2010, 32:263-269.
    • (2010) Acta Physiol. Plant , vol.32 , pp. 263-269
    • Qi, Y.C.1    Wang, F.F.2    Zhang, H.3    Liu, W.Q.4
  • 22
    • 68949161024 scopus 로고    scopus 로고
    • Salt stress-induced alterations in the root proteome of barley genotypes with contrasting response towards salinity
    • Witzel K., Weidner A., Surabhi G.K., Börner A., Mock H.P. Salt stress-induced alterations in the root proteome of barley genotypes with contrasting response towards salinity. J. Exp. Bot. 2009, 60:3545-3557.
    • (2009) J. Exp. Bot. , vol.60 , pp. 3545-3557
    • Witzel, K.1    Weidner, A.2    Surabhi, G.K.3    Börner, A.4    Mock, H.P.5
  • 23
    • 50249184711 scopus 로고    scopus 로고
    • Comparative proteomics analysis reveals an intimate protein network provoked by hydrogen peroxide stress in rice seedling leaves
    • Wan X.Y., Liu J.Y. Comparative proteomics analysis reveals an intimate protein network provoked by hydrogen peroxide stress in rice seedling leaves. Mol. Cell. Proteomics 2008, 7:1469-1488.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1469-1488
    • Wan, X.Y.1    Liu, J.Y.2
  • 24
    • 84856356675 scopus 로고    scopus 로고
    • Comparative proteomic analysis of seedling leaves of different salt tolerant soybean genotypes
    • Ma H., Song L., Shu Y., Wang S., Niu J., Wang Z., Yu T., Gu W., Ma H. Comparative proteomic analysis of seedling leaves of different salt tolerant soybean genotypes. J. Proteomics 2012, 75:1529-1546.
    • (2012) J. Proteomics , vol.75 , pp. 1529-1546
    • Ma, H.1    Song, L.2    Shu, Y.3    Wang, S.4    Niu, J.5    Wang, Z.6    Yu, T.7    Gu, W.8    Ma, H.9
  • 25
    • 1842479300 scopus 로고    scopus 로고
    • Regulation of senescence by eukaryotic translation initiation factor 5A: implications for plant growth and development
    • Thompson J.E., Hopkins M.T., Taylor C., Wang T.W. Regulation of senescence by eukaryotic translation initiation factor 5A: implications for plant growth and development. Trends Plant Sci. 2004, 9:174-179.
    • (2004) Trends Plant Sci. , vol.9 , pp. 174-179
    • Thompson, J.E.1    Hopkins, M.T.2    Taylor, C.3    Wang, T.W.4
  • 26
    • 0017364133 scopus 로고    scopus 로고
    • The role of polyamines in cell-free protein synthesis in the wheat-germ system
    • Hunter A.R., Farrell P.J., Jackson R.J., Hunt T. The role of polyamines in cell-free protein synthesis in the wheat-germ system. Eur. J. Biochem. 2008, 75:149-157.
    • (2008) Eur. J. Biochem. , vol.75 , pp. 149-157
    • Hunter, A.R.1    Farrell, P.J.2    Jackson, R.J.3    Hunt, T.4
  • 28
    • 0025303147 scopus 로고
    • Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly
    • Beckmann R.P., Mizzen L., Welch W.J. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science 1990, 248:850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.2    Welch, W.J.3
  • 29
    • 0026338017 scopus 로고
    • Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg C.S., Birckbichler P.J., Rice R.H. Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. FASEB J. 1991, 5:3071-3077.
    • (1991) FASEB J. , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 30
    • 0033830284 scopus 로고    scopus 로고
    • Involvement of polyamines in the chilling tolerance of cucumber cultivars
    • Shen W., Nada K., Tachibana S. Involvement of polyamines in the chilling tolerance of cucumber cultivars. Plant Physiol. 2000, 124:431-440.
    • (2000) Plant Physiol. , vol.124 , pp. 431-440
    • Shen, W.1    Nada, K.2    Tachibana, S.3
  • 31
    • 0041762551 scopus 로고    scopus 로고
    • Overexpression of a stress-inducible aldehyde dehydrogenase gene from Arabidopsis thaliana in transgenic plants improves stress tolerance
    • Sunkar R., Bartels D., Kirch H.H. Overexpression of a stress-inducible aldehyde dehydrogenase gene from Arabidopsis thaliana in transgenic plants improves stress tolerance. Plant J. 2003, 35:452-464.
    • (2003) Plant J. , vol.35 , pp. 452-464
    • Sunkar, R.1    Bartels, D.2    Kirch, H.H.3
  • 33
    • 0035213385 scopus 로고    scopus 로고
    • Plant salt tolerance
    • Zhu J.K. Plant salt tolerance. Trends Plant Sci. 2001, 6:66-71.
    • (2001) Trends Plant Sci. , vol.6 , pp. 66-71
    • Zhu, J.K.1
  • 34
    • 3042674367 scopus 로고    scopus 로고
    • Cell cycle modulation in the response of the primary root of Arabidopsis to salt stress
    • West G., Inzé D., Beemster G.T.S. Cell cycle modulation in the response of the primary root of Arabidopsis to salt stress. Plant Physiol. 2004, 135:1050-1058.
    • (2004) Plant Physiol. , vol.135 , pp. 1050-1058
    • West, G.1    Inzé, D.2    Beemster, G.T.S.3
  • 36
    • 0001510436 scopus 로고
    • Solubilization of plant membrane proteins for analysis by two-dimensional gel electrophoresis
    • Hurkman W.J., Tanaka C.K. Solubilization of plant membrane proteins for analysis by two-dimensional gel electrophoresis. Plant Physiol. 1986, 81:802-806.
    • (1986) Plant Physiol. , vol.81 , pp. 802-806
    • Hurkman, W.J.1    Tanaka, C.K.2
  • 37
    • 0021418471 scopus 로고
    • Evaluation of isoelectric focusing running conditions during two-dimensional isoelectric focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresis: variation of gel patterns with changing conditions and optimized isoelectric focusing conditions
    • Duncan R., Hershey J.W.B. Evaluation of isoelectric focusing running conditions during two-dimensional isoelectric focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresis: variation of gel patterns with changing conditions and optimized isoelectric focusing conditions. Anal. Biochem. 1984, 138:144-155.
    • (1984) Anal. Biochem. , vol.138 , pp. 144-155
    • Duncan, R.1    Hershey, J.W.B.2
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the 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
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. 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.K.1
  • 40
    • 66049157970 scopus 로고    scopus 로고
    • Proteomic analysis of changes induced by nonylphenol in sprague-dawley rat sertoli cells
    • Wu J., Wang F., Gong Y., Li D., Sha J., Huang X., Han X. Proteomic analysis of changes induced by nonylphenol in sprague-dawley rat sertoli cells. Chem. Res. Toxicol. 2009, 22:668-675.
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 668-675
    • Wu, J.1    Wang, F.2    Gong, Y.3    Li, D.4    Sha, J.5    Huang, X.6    Han, X.7


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