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Volumn 4, Issue APR, 2013, Pages

Organ-specific proteome analysis for identification of abiotic stress response mechanism in crop

Author keywords

Abiotic stress; Crop; Drought; Flooding; Organ specific; Proteomics; Salinity

Indexed keywords


EID: 84897957706     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2013.00071     Document Type: Review
Times cited : (68)

References (88)
  • 1
    • 3042852627 scopus 로고    scopus 로고
    • A proteomic approach to analyze salt responsive proteins in rice leaf sheath
    • Abbasi, F. M., and Komatsu, S. (2004). A proteomic approach to analyze salt responsive proteins in rice leaf sheath. Proteomics 4, 2072-2081.
    • (2004) Proteomics , vol.4 , pp. 2072-2081
    • Abbasi, F.M.1    Komatsu, S.2
  • 2
    • 58149383884 scopus 로고    scopus 로고
    • Proteome analysis of potato under salt stress
    • Aghaei, K., Ehsanpour, A. A., and Komatsu, S. (2008). Proteome analysis of potato under salt stress. J. Proteome Res. 7, 4858-4868.
    • (2008) J. Proteome Res. , vol.7 , pp. 4858-4868
    • Aghaei, K.1    Ehsanpour, A.A.2    Komatsu, S.3
  • 3
    • 70350448007 scopus 로고    scopus 로고
    • Comparative analyses of the proteomes of leaves and flowers at various stages of development reveal organ-specific functional differentiation of proteins in soybean
    • Ahsan, N., and Komatsu, S. (2009). Comparative analyses of the proteomes of leaves and flowers at various stages of development reveal organ-specific functional differentiation of proteins in soybean. Proteomics 9, 4889-4907.
    • (2009) Proteomics , vol.9 , pp. 4889-4907
    • Ahsan, N.1    Komatsu, S.2
  • 4
    • 35948944351 scopus 로고    scopus 로고
    • A comparative proteomic analysis of tomato leaves in response to waterlogging stress
    • Ahsan, N., Lee, D. G., Lee, S. H., Kang, K. Y., Bahk, J. D., Choi, M. S., et al. (2007a). A comparative proteomic analysis of tomato leaves in response to waterlogging stress. Physiol. Plant. 131, 555-570.
    • (2007) Physiol. Plant. , vol.131 , pp. 555-570
    • Ahsan, N.1    Lee, D.G.2    Lee, S.H.3    Kang, K.Y.4    Bahk, J.D.5    Choi, M.S.6
  • 5
    • 34250630549 scopus 로고    scopus 로고
    • A proteomic screen and identification Waterlogging-regulated proteins in tomato roots
    • Ahsan, N., Lee, D. G., Lee, S. H., Lee, K. W., Bahk, J., and Lee, B. H. (2007b). A proteomic screen and identification Waterlogging-regulated proteins in tomato roots. Plant Soil 295, 37-51.
    • (2007) Plant Soil , vol.295 , pp. 37-51
    • Ahsan, N.1    Lee, D.G.2    Lee, S.H.3    Lee, K.W.4    Bahk, J.5    Lee, B.H.6
  • 6
    • 0029967990 scopus 로고    scopus 로고
    • Root system regulation of whole plant growth
    • Aiken, R. M., and Smucker, A. J. M. (1996). Root system regulation of whole plant growth. Annu. Rev. Phytopathol. 34, 325-346.
    • (1996) Annu. Rev. Phytopathol. , vol.34 , pp. 325-346
    • Aiken, R.M.1    Smucker, A.J.M.2
  • 7
    • 77951711549 scopus 로고    scopus 로고
    • Proteome analysis of soybean roots under waterlogging stress at an early vegetative stage
    • Alam, I., Lee, D. G., Kim, K. H., Park, C. H., Sharmin, S. A., Lee, H., et al. (2010). Proteome analysis of soybean roots under waterlogging stress at an early vegetative stage. J. Biosci. 35, 49-62.
    • (2010) J. Biosci. , vol.35 , pp. 49-62
    • Alam, I.1    Lee, D.G.2    Kim, K.H.3    Park, C.H.4    Sharmin, S.A.5    Lee, H.6
  • 8
    • 32344442922 scopus 로고    scopus 로고
    • Proteomic analysis of rice leaf sheath during drought stress
    • Ali, G. M., and Komatsu, S. (2006). Proteomic analysis of rice leaf sheath during drought stress. J. Proteome Res. 5, 396-403.
    • (2006) J. Proteome Res. , vol.5 , pp. 396-403
    • Ali, G.M.1    Komatsu, S.2
  • 9
    • 33646255908 scopus 로고    scopus 로고
    • Effects of salinity levels on proteome of Suaeda aegyptiaca leaves
    • Askari, H., Edqvist, J., Hajheidari, M., Kafi, M., and Salekdeh, G. H. (2006). Effects of salinity levels on proteome of Suaeda aegyptiaca leaves. Proteomics 6, 2542-2554.
    • (2006) Proteomics , vol.6 , pp. 2542-2554
    • Askari, H.1    Edqvist, J.2    Hajheidari, M.3    Kafi, M.4    Salekdeh, G.H.5
  • 10
    • 0026744722 scopus 로고
    • Identification, characterization, and DNA sequence of a functional "double" groES-like chaperonin from chloroplasts of higher plants
    • Bertsch, U., Soll, J., Seetharam, R., and Viitanen, P. V. (1992). Identification, characterization, and DNA sequence of a functional "double" groES-like chaperonin from chloroplasts of higher plants. Proc. Natl. Acad. Sci. U.S.A. 89, 8696-8700.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 8696-8700
    • Bertsch, U.1    Soll, J.2    Seetharam, R.3    Viitanen, P.V.4
  • 11
    • 0028784952 scopus 로고
    • From xenobiotic to antibiotic, formation of protoanemonin from 4-Chlorocatechol by enzymes of the 3-Oxoadipate pathway
    • Blasco, R., Wittich, R. M., Mallavarapu, M., Timmis, K. N., and Pieper, D. H. (1995). From xenobiotic to antibiotic, formation of protoanemonin from 4-Chlorocatechol by enzymes of the 3-Oxoadipate pathway. J. Biol. Chem. 270, 9229-9235.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9229-9235
    • Blasco, R.1    Wittich, R.M.2    Mallavarapu, M.3    Timmis, K.N.4    Pieper, D.H.5
  • 12
    • 67650128347 scopus 로고    scopus 로고
    • Genetic variation and drought response in two Populus euramericana genotypes through 2-DE proteomic analysis of leaves from field and glasshouse cultivated plants
    • Bonhomme, L., Monclus, R., Vincent, D., Carpin, S., Claverol, S., Lomenech, A. M., et al. (2009). Genetic variation and drought response in two Populus euramericana genotypes through 2-DE proteomic analysis of leaves from field and glasshouse cultivated plants. Phytochemistry 70, 988-1002.
    • (2009) Phytochemistry , vol.70 , pp. 988-1002
    • Bonhomme, L.1    Monclus, R.2    Vincent, D.3    Carpin, S.4    Claverol, S.5    Lomenech, A.M.6
  • 13
    • 2542632763 scopus 로고    scopus 로고
    • Is photosynthesis limited by decreased Rubisco activity and RuBP content under progressive water stress?
    • Bota, J., Flexas, J., and Medrano, H. (2004). Is photosynthesis limited by decreased Rubisco activity and RuBP content under progressive water stress? New Phytol. 162, 671-681.
    • (2004) New Phytol. , vol.162 , pp. 671-681
    • Bota, J.1    Flexas, J.2    Medrano, H.3
  • 15
    • 70349764296 scopus 로고    scopus 로고
    • Analysis of drought responsive proteins in wheat (Triticum durum) by 2D-PAGE and MALDI-TOF mass spectrometry
    • Caruso, G., Cavaliere, C., Foglia, P., Gubbiotti, R., Samperi, R., and Laganà, A. (2009). Analysis of drought responsive proteins in wheat (Triticum durum) by 2D-PAGE and MALDI-TOF mass spectrometry. Plant Sci. 177, 570-576.
    • (2009) Plant Sci. , vol.177 , pp. 570-576
    • Caruso, G.1    Cavaliere, C.2    Foglia, P.3    Gubbiotti, R.4    Samperi, R.5    Laganà, A.6
  • 16
    • 77952128989 scopus 로고    scopus 로고
    • Proteomic analysis of responses to drought stress in sunflower (Helianthus annuus) leaves by 2DE gel electrophoresis and mass spectrometry
    • Castillejo, M. A., Maldonado, A. M., Ogueta, S., and Jorrín, J. V. (2008). Proteomic analysis of responses to drought stress in sunflower (Helianthus annuus) leaves by 2DE gel electrophoresis and mass spectrometry. Open Proteomics J. 1, 59-71.
    • (2008) Open Proteomics J. , vol.1 , pp. 59-71
    • Castillejo, M.A.1    Maldonado, A.M.2    Ogueta, S.3    Jorrín, J.V.4
  • 18
    • 0030197596 scopus 로고    scopus 로고
    • Plant cell enlargement and the action of expansins
    • Cosgrove, D. J. (1996). Plant cell enlargement and the action of expansins. Bioessays 18, 533-540.
    • (1996) Bioessays , vol.18 , pp. 533-540
    • Cosgrove, D.J.1
  • 19
    • 0343463214 scopus 로고
    • Differential two-dimensional protein patterns as related to tissue specificity and water conditions in Brassica napus var oleifera root system
    • Damerval, C., Vartanian, N., and de Vienne, D. (1988). Differential two-dimensional protein patterns as related to tissue specificity and water conditions in Brassica napus var oleifera root system. Plant Physiol. 86, 1304-1309.
    • (1988) Plant Physiol. , vol.86 , pp. 1304-1309
    • Damerval, C.1    Vartanian, N.2    de Vienne, D.3
  • 20
    • 0036188286 scopus 로고    scopus 로고
    • Stomatal control by chemical signalling and the exploitation of this mechanism to increase water use efficiency in agriculture
    • Davies, W. J., Wilkinson, S., and Loveys, B. (2002). Stomatal control by chemical signalling and the exploitation of this mechanism to increase water use efficiency in agriculture. New Phytol. 153, 449-460.
    • (2002) New Phytol. , vol.153 , pp. 449-460
    • Davies, W.J.1    Wilkinson, S.2    Loveys, B.3
  • 21
    • 36248951584 scopus 로고    scopus 로고
    • Transcriptomic and proteomic analyses of pericycle cells of the maize primary root
    • Dembinsky, D., Woll, K., Saleem, M., Liu, Y., Fu, Y., Borsuk, L. A., et al. (2007). Transcriptomic and proteomic analyses of pericycle cells of the maize primary root. Plant Physiol. 145, 575-588.
    • (2007) Plant Physiol. , vol.145 , pp. 575-588
    • Dembinsky, D.1    Woll, K.2    Saleem, M.3    Liu, Y.4    Fu, Y.5    Borsuk, L.A.6
  • 24
    • 58349112093 scopus 로고    scopus 로고
    • Changes in the protein profile of Quercus ilex leaves in response to drought stress and recovery
    • Echevarría-Zomeno, S., Ariza, D., Jorge, I., Lenz, C., Del Campo, A., Jorrín, J. V., et al. (2009). Changes in the protein profile of Quercus ilex leaves in response to drought stress and recovery. J. Plant Physiol. 166, 233-245.
    • (2009) J. Plant Physiol. , vol.166 , pp. 233-245
    • Echevarría-Zomeno, S.1    Ariza, D.2    Jorge, I.3    Lenz, C.4    Del Campo, A.5    Jorrín, J.V.6
  • 25
    • 35649013698 scopus 로고    scopus 로고
    • Alternative and effective proteomic analysis in Arabidopsis
    • Espagne, C., Martinez, A., Valot, B., Meinnel, T., and Giglione, C. (2007). Alternative and effective proteomic analysis in Arabidopsis. Proteomics 7, 3788-3799.
    • (2007) Proteomics , vol.7 , pp. 3788-3799
    • Espagne, C.1    Martinez, A.2    Valot, B.3    Meinnel, T.4    Giglione, C.5
  • 26
    • 0021516033 scopus 로고
    • The development and dynamics of the root apical meristem
    • Feldman, L. J. (1984). The development and dynamics of the root apical meristem. Am. J. Bot. 71, 1308-1314.
    • (1984) Am. J. Bot. , vol.71 , pp. 1308-1314
    • Feldman, L.J.1
  • 28
    • 33846810065 scopus 로고    scopus 로고
    • Proteome response of Elymus elongatum to severe water stress and recovery
    • Gazanchian, A., Hajheidari, M., Sima, N. K., and Salekdeh, G. H. (2007). Proteome response of Elymus elongatum to severe water stress and recovery. J. Exp. Bot. 58, 291-300.
    • (2007) J. Exp. Bot. , vol.58 , pp. 291-300
    • Gazanchian, A.1    Hajheidari, M.2    Sima, N.K.3    Salekdeh, G.H.4
  • 29
    • 79954584833 scopus 로고    scopus 로고
    • Root targeted biotechnology to mediate hormonal signaling and improve crop stress tolerance
    • Ghanem, M. E., Hichri, I., Smigocki, A. C., Albacete, A., Fauconnier, M. L., Diatloff, E., et al. (2011). Root targeted biotechnology to mediate hormonal signaling and improve crop stress tolerance. Plant Cell Rep. 30, 807-823.
    • (2011) Plant Cell Rep. , vol.30 , pp. 807-823
    • Ghanem, M.E.1    Hichri, I.2    Smigocki, A.C.3    Albacete, A.4    Fauconnier, M.L.5    Diatloff, E.6
  • 30
    • 33646241061 scopus 로고    scopus 로고
    • Apoptosis-like programmed cell death occurs in procambium and ground meristem of pea (Pisum sativum) root tips exposed to sudden flooding
    • Gladish, D. K., Xu, J., and Niki, T. (2006). Apoptosis-like programmed cell death occurs in procambium and ground meristem of pea (Pisum sativum) root tips exposed to sudden flooding. Ann. Bot. 97, 895-902.
    • (2006) Ann. Bot. , vol.97 , pp. 895-902
    • Gladish, D.K.1    Xu, J.2    Niki, T.3
  • 31
    • 0002003852 scopus 로고
    • Growth responses and adaptations of Fraxinus pennsylvanica seedlings to flooding
    • Gomes, A. R., and Kozlowski, T. T. (1980). Growth responses and adaptations of Fraxinus pennsylvanica seedlings to flooding. Plant Physiol. 66, 267-271.
    • (1980) Plant Physiol. , vol.66 , pp. 267-271
    • Gomes, A.R.1    Kozlowski, T.T.2
  • 32
    • 84862799415 scopus 로고    scopus 로고
    • Comparative proteomic analysis of salt response proteins in seedling roots of two wheat varieties
    • Guo, G., Ge, P., Ma, C., Li, X., Lv, D., Wang, S., et al. (2012). Comparative proteomic analysis of salt response proteins in seedling roots of two wheat varieties. J. Proteomics 75, 1867-1885.
    • (2012) J. Proteomics , vol.75 , pp. 1867-1885
    • Guo, G.1    Ge, P.2    Ma, C.3    Li, X.4    Lv, D.5    Wang, S.6
  • 34
    • 79959426399 scopus 로고    scopus 로고
    • Analysis of proteins in aerenchymatous seminal roots of wheat grown in hypoxic soils under waterlogged conditions
    • Haque, M. E., Kawaguchi, K., and Komatsu, S. (2011). Analysis of proteins in aerenchymatous seminal roots of wheat grown in hypoxic soils under waterlogged conditions. Protein Pept. Lett. 18, 912-924.
    • (2011) Protein Pept. Lett. , vol.18 , pp. 912-924
    • Haque, M.E.1    Kawaguchi, K.2    Komatsu, S.3
  • 35
    • 65249095341 scopus 로고    scopus 로고
    • Proteome analysis of early-stage soybean seedlings under flooding stress
    • Hashiguchi, A., Sakata, K., and Komatsu, S. (2009). Proteome analysis of early-stage soybean seedlings under flooding stress. J. Proteome Res. 8, 2058-2069.
    • (2009) J. Proteome Res. , vol.8 , pp. 2058-2069
    • Hashiguchi, A.1    Sakata, K.2    Komatsu, S.3
  • 36
    • 34248228084 scopus 로고    scopus 로고
    • Proteomic analysis of rice seedlings during cold stress
    • Hashimoto, M., and Komatsu, S. (2007). Proteomic analysis of rice seedlings during cold stress. Proteomics 7, 1293-1302.
    • (2007) Proteomics , vol.7 , pp. 1293-1302
    • Hashimoto, M.1    Komatsu, S.2
  • 37
    • 46149125267 scopus 로고    scopus 로고
    • Membrane-associated stress proteins: More than simply chaperones
    • Horvath, I., Multhoff, G., Sonnleitner, A., and Vigh, L. (2008). Membrane-associated stress proteins: more than simply chaperones. Biochim. Biophys. Acta 1778, 1653-1664.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1653-1664
    • Horvath, I.1    Multhoff, G.2    Sonnleitner, A.3    Vigh, L.4
  • 38
    • 29944437052 scopus 로고    scopus 로고
    • Isolation of a NaCl-tolerant mutant of Chrysanthemum morifolium by gamma radiation: In vitro mutagenesis and selection by salt stress
    • Hossain, Z., Mandal, A. K. A., Datta, S. K., and Biswas, A. K. (2006). Isolation of a NaCl-tolerant mutant of Chrysanthemum morifolium by gamma radiation: in vitro mutagenesis and selection by salt stress. Funct. Plant Biol. 33, 91-101.
    • (2006) Funct. Plant Biol. , vol.33 , pp. 91-101
    • Hossain, Z.1    Mandal, A.K.A.2    Datta, S.K.3    Biswas, A.K.4
  • 39
    • 84855523412 scopus 로고    scopus 로고
    • Plant cell organelle proteomics in response to abiotic stress
    • Hossain, Z., Nouri, M. Z., and Komatsu, S. (2012). Plant cell organelle proteomics in response to abiotic stress. J. Proteome Res. 11, 37-48.
    • (2012) J. Proteome Res. , vol.11 , pp. 37-48
    • Hossain, Z.1    Nouri, M.Z.2    Komatsu, S.3
  • 41
    • 0021016118 scopus 로고
    • Inhibition of ribulose bisphosphate carboxylase by substrate ribulose 1, 5-bisphosphate
    • Jordan, D. B., and Chollet, R. (1983). Inhibition of ribulose bisphosphate carboxylase by substrate ribulose 1, 5-bisphosphate. J. Biol. Chem. 258, 13752-13758.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13752-13758
    • Jordan, D.B.1    Chollet, R.2
  • 42
    • 58549116129 scopus 로고    scopus 로고
    • A PIP-family protein is required for biosynthesis of tobacco alkaloids
    • Kajikawa, M., Hirai, N., and Hashimoto, T. (2009). A PIP-family protein is required for biosynthesis of tobacco alkaloids. Plant Mol. Biol. 69, 287-298.
    • (2009) Plant Mol. Biol. , vol.69 , pp. 287-298
    • Kajikawa, M.1    Hirai, N.2    Hashimoto, T.3
  • 43
    • 58149277123 scopus 로고    scopus 로고
    • Differential regulation of proteins and phosphoproteins in rice under drought stress
    • Ke, Y., Han, G., He, H., and Li, J. (2009). Differential regulation of proteins and phosphoproteins in rice under drought stress. Biochem. Biophys. Res. Commun. 379, 133-138.
    • (2009) Biochem. Biophys. Res. Commun. , vol.379 , pp. 133-138
    • Ke, Y.1    Han, G.2    He, H.3    Li, J.4
  • 44
    • 84866179240 scopus 로고    scopus 로고
    • Organ-specific proteomics analysis for response mechanism in soybean seedlings under flooding stress
    • Khatoon, A., Rehman, S., Hiraga, S., Makino, T., and Komatsu, S. (2012). Organ-specific proteomics analysis for response mechanism in soybean seedlings under flooding stress. J. Proteomics 75, 5706-5723.
    • (2012) J. Proteomics , vol.75 , pp. 5706-5723
    • Khatoon, A.1    Rehman, S.2    Hiraga, S.3    Makino, T.4    Komatsu, S.5
  • 45
    • 63349106787 scopus 로고    scopus 로고
    • Soybean proteomics and its application to functional analysis
    • Komatsu, S., and Ahsan, N. (2009). Soybean proteomics and its application to functional analysis. J. Proteomics 72, 325-336.
    • (2009) J. Proteomics , vol.72 , pp. 325-336
    • Komatsu, S.1    Ahsan, N.2
  • 46
    • 70349970273 scopus 로고    scopus 로고
    • A comprehensive analysis of the soybean genes and proteins expressed under flooding stress using transcriptome and proteome techniques
    • Komatsu, S., Yamamoto, R., Nanjo, Y., Mikami, Y., Yunokawa, H., and Sakata, K. (2009). A comprehensive analysis of the soybean genes and proteins expressed under flooding stress using transcriptome and proteome techniques. J. Proteome Res. 8, 4766-4778.
    • (2009) J. Proteome Res. , vol.8 , pp. 4766-4778
    • Komatsu, S.1    Yamamoto, R.2    Nanjo, Y.3    Mikami, Y.4    Yunokawa, H.5    Sakata, K.6
  • 47
    • 71649088751 scopus 로고    scopus 로고
    • Cell wall proteome of wheat roots under flooding stress using gel-based and LC MS/MS-based proteomics approaches
    • Kong, F. J., Oyanagi, A., and Komatsu, S. (2010). Cell wall proteome of wheat roots under flooding stress using gel-based and LC MS/MS-based proteomics approaches. Biochim. Biophys. Acta 1804, 124-136.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 124-136
    • Kong, F.J.1    Oyanagi, A.2    Komatsu, S.3
  • 48
    • 0017018253 scopus 로고
    • Catalysis of the peptide bond formation by 50S subunits of E. Coli ribosomes with N-(formil) methionine ester of adenylic acid as peptide donor
    • Kotusov, V. V., Kukhanova, M. K., Krayevsky, A. A., and Gottikh, B. P. (1976). Catalysis of the peptide bond formation by 50S subunits of E. Coli ribosomes with N-(formil) methionine ester of adenylic acid as peptide donor. Mol. Biol. Rep. 3, 151-156.
    • (1976) Mol. Biol. Rep. , vol.3 , pp. 151-156
    • Kotusov, V.V.1    Kukhanova, M.K.2    Krayevsky, A.A.3    Gottikh, B.P.4
  • 49
    • 84862744802 scopus 로고    scopus 로고
    • Proteomic analysis of salt-responsive ubiquitin-related proteins in rice roots
    • Liu, C. W., Hsu, Y. K., Cheng, Y. H., Yen, H. C., Wu, Y. P., Wang, C. S., et al. (2012). Proteomic analysis of salt-responsive ubiquitin-related proteins in rice roots. Rapid Commun. Mass Spectrom. 26, 1649-1660.
    • (2012) Rapid Commun. Mass Spectrom. , vol.26 , pp. 1649-1660
    • Liu, C.W.1    Hsu, Y.K.2    Cheng, Y.H.3    Yen, H.C.4    Wu, Y.P.5    Wang, C.S.6
  • 50
    • 0029200349 scopus 로고
    • On the relationship between electron transport rate and photosynthesis in leaves of the C4 plant Sorghum bicolor exposed to water stress, temperature changes and carbon metabolism inhibition
    • Loreto, F., Tricoli, D., and di Marco, G. (1995). On the relationship between electron transport rate and photosynthesis in leaves of the C4 plant Sorghum bicolor exposed to water stress, temperature changes and carbon metabolism inhibition. Aust. J. Plant Physiol. 22, 885-892.
    • (1995) Aust. J. Plant Physiol. , vol.22 , pp. 885-892
    • Loreto, F.1    Tricoli, D.2    di Marco, G.3
  • 51
    • 34547950547 scopus 로고    scopus 로고
    • Roots of the second green revolution
    • Lynch, J. P. (2007). Roots of the second green revolution. Aust. J. Bot. 55, 493-512.
    • (2007) Aust. J. Bot. , vol.55 , pp. 493-512
    • Lynch, J.P.1
  • 52
    • 53549102732 scopus 로고    scopus 로고
    • Photosynthetic activity during olive (Olea europaea) leaf development correlates with plastid biogenesis and RuBisCO levels
    • Maayan, I., Shaya, F., Ratner, K., Mani, Y., Lavee, S., Avidan, B., et al. (2008). Photosynthetic activity during olive (Olea europaea) leaf development correlates with plastid biogenesis and RuBisCO levels. Physiol. Plant. 134, 547-558.
    • (2008) Physiol. Plant. , vol.134 , pp. 547-558
    • Maayan, I.1    Shaya, F.2    Ratner, K.3    Mani, Y.4    Lavee, S.5    Avidan, B.6
  • 53
    • 79955037355 scopus 로고    scopus 로고
    • Comparative proteomic profiles of the soybean (Glycine max) root apex and differentiated root zone
    • Mathesius, U., Djordjevic, M. A., Oakes, M., Goffard, N., Haerizadeh, F., Weiller, G. F., et al. (2011). Comparative proteomic profiles of the soybean (Glycine max) root apex and differentiated root zone. Proteomics 11, 1707-1719.
    • (2011) Proteomics , vol.11 , pp. 1707-1719
    • Mathesius, U.1    Djordjevic, M.A.2    Oakes, M.3    Goffard, N.4    Haerizadeh, F.5    Weiller, G.F.6
  • 55
    • 0344100071 scopus 로고    scopus 로고
    • Leaf gas exchange, chlorophyll fluorescence and growth responses of Genipa americana seedlings to soil flooding
    • Mielke, M. S., de Almeida, A. A. F., Gomes, F. P., Aguilar, A. G., and Mangabeira, P. A. O. (2003). Leaf gas exchange, chlorophyll fluorescence and growth responses of Genipa americana seedlings to soil flooding. Environ. Exp. Bot. 50, 221-231.
    • (2003) Environ. Exp. Bot. , vol.50 , pp. 221-231
    • Mielke, M.S.1    de Almeida, A.A.F.2    Gomes, F.P.3    Aguilar, A.G.4    Mangabeira, P.A.O.5
  • 57
    • 84857651754 scopus 로고    scopus 로고
    • Organ-specific proteomic analysis of drought-stressed soybean seedlings
    • Mohammadi, P. P., Moieni, A., Hiraga, S., and Komatsu, S. (2012a). Organ-specific proteomic analysis of drought-stressed soybean seedlings. J. Proteomics 75, 1906-1923.
    • (2012) J. Proteomics , vol.75 , pp. 1906-1923
    • Mohammadi, P.P.1    Moieni, A.2    Hiraga, S.3    Komatsu, S.4
  • 58
    • 84868105446 scopus 로고    scopus 로고
    • Comparative proteome analysis of drought-sensitive and drought-tolerant rapeseed roots and their hybrid F1 line under drought stress
    • Mohammadi, P. P., Moieni, A., and Komatsu, S. (2012b). Comparative proteome analysis of drought-sensitive and drought-tolerant rapeseed roots and their hybrid F1 line under drought stress. Amino Acids 43, 2137-2152.
    • (2012) Amino Acids , vol.43 , pp. 2137-2152
    • Mohammadi, P.P.1    Moieni, A.2    Komatsu, S.3
  • 59
    • 3242774747 scopus 로고    scopus 로고
    • High throughput peptide mass fingerprinting of soybean seed proteins: Automated workflow and utility of UniGene expressed sequence tag databases for protein identification
    • Mooney, B. P., Krishnan, H. B., and Thelen, J. J. (2004). High throughput peptide mass fingerprinting of soybean seed proteins: automated workflow and utility of UniGene expressed sequence tag databases for protein identification. Phytochemistry 65, 1733-1744.
    • (2004) Phytochemistry , vol.65 , pp. 1733-1744
    • Mooney, B.P.1    Krishnan, H.B.2    Thelen, J.J.3
  • 60
    • 77955459998 scopus 로고    scopus 로고
    • Comparative proteomic analysis of early-stage soybean seedlings responses to flooding by using gel and gel-free techniques
    • Nanjo, Y., Skultety, L., Ashraf, Y., and Komatsu, S. (2010). Comparative proteomic analysis of early-stage soybean seedlings responses to flooding by using gel and gel-free techniques. J. Proteome Res. 9, 3989-4002.
    • (2010) J. Proteome Res. , vol.9 , pp. 3989-4002
    • Nanjo, Y.1    Skultety, L.2    Ashraf, Y.3    Komatsu, S.4
  • 61
    • 84855560266 scopus 로고    scopus 로고
    • Mass spectrometry-based analysis of proteomic changes in the root tips of flooded soybean seedlings
    • Nanjo, Y., Skultety, L., Uvackova, L., Klubicová, K., Hajduch, M., and Komatsu, S. (2012). Mass spectrometry-based analysis of proteomic changes in the root tips of flooded soybean seedlings. J. Proteome Res. 11, 372-385.
    • (2012) J. Proteome Res. , vol.11 , pp. 372-385
    • Nanjo, Y.1    Skultety, L.2    Uvackova, L.3    Klubicová, K.4    Hajduch, M.5    Komatsu, S.6
  • 62
    • 33645029435 scopus 로고    scopus 로고
    • An accurate and eproducible method for proteome profiling of the effects of salt stress in the rice leaf lamina
    • Parker, R., Flowers, T. J., Moore, A. L., and Harpham, N. V. J. (2006). An accurate and eproducible method for proteome profiling of the effects of salt stress in the rice leaf lamina. J. Exp. Bot. 57, 1109-1118.
    • (2006) J. Exp. Bot. , vol.57 , pp. 1109-1118
    • Parker, R.1    Flowers, T.J.2    Moore, A.L.3    Harpham, N.V.J.4
  • 63
    • 84861990380 scopus 로고    scopus 로고
    • Selected reaction monitoring-based proteomics: Workflows, potential, pitfalls and future directions
    • Picotti, P., and Aebersold, R. (2012). Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions. Nat. Methods 9, 555-566.
    • (2012) Nat. Methods , vol.9 , pp. 555-566
    • Picotti, P.1    Aebersold, R.2
  • 64
    • 68749094119 scopus 로고    scopus 로고
    • Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics
    • Picotti, P., Bodenmiller, B., Mueller, L. N., Domon, B., and Aebersold, R. (2009). Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics. Cell 138, 795-806.
    • (2009) Cell , vol.138 , pp. 795-806
    • Picotti, P.1    Bodenmiller, B.2    Mueller, L.N.3    Domon, B.4    Aebersold, R.5
  • 65
    • 84873724658 scopus 로고    scopus 로고
    • A complete mass-spectrometric map of the yeast proteome applied to quantitative trait analysis
    • Picotti, P., Clément-Ziza, M., Lam, H., Campbell, D. S., Schmidt, A., Deutsch, E. W., et al. (2013). A complete mass-spectrometric map of the yeast proteome applied to quantitative trait analysis. Nature 494, 266-270.
    • (2013) Nature , vol.494 , pp. 266-270
    • Picotti, P.1    Clément-Ziza, M.2    Lam, H.3    Campbell, D.S.4    Schmidt, A.5    Deutsch, E.W.6
  • 66
    • 84864356128 scopus 로고    scopus 로고
    • Acyl chains of phospholipase D transphosphatidylation products in Arabidopsis cells: A study using multiple reaction monitoring mass spectrometry
    • doi: 10.1371/journal.pone.0041985
    • Rainteau, D., Humbert, L., Delage, E., Vergnolle, C., Cantrel, C., Maubert, M. A., et al. (2012). Acyl chains of phospholipase D transphosphatidylation products in Arabidopsis cells: a study using multiple reaction monitoring mass spectrometry. PLoS ONE 7:e41985. doi: 10.1371/journal.pone.0041985
    • (2012) PLoS ONE , vol.7
    • Rainteau, D.1    Humbert, L.2    Delage, E.3    Vergnolle, C.4    Cantrel, C.5    Maubert, M.A.6
  • 67
    • 0035081121 scopus 로고    scopus 로고
    • RuBisCO activase: An enzyme with a temperature dependent dual function?
    • Rokka, A., Zhang, L., and Aro, E. M. (2001). RuBisCO activase: an enzyme with a temperature dependent dual function? Plant J. 25, 463-471.
    • (2001) Plant J. , vol.25 , pp. 463-471
    • Rokka, A.1    Zhang, L.2    Aro, E.M.3
  • 68
    • 4544265213 scopus 로고    scopus 로고
    • Tackling the plant proteome: Practical approaches, hurdles and experimental tools
    • Rose, J. K., Bashir, S., Giovannoni, J. J., Jahn, M. M., and Saravanan, R. S. (2004). Tackling the plant proteome: practical approaches, hurdles and experimental tools. Plant J. 39, 715-733.
    • (2004) Plant J. , vol.39 , pp. 715-733
    • Rose, J.K.1    Bashir, S.2    Giovannoni, J.J.3    Jahn, M.M.4    Saravanan, R.S.5
  • 69
    • 0036746417 scopus 로고    scopus 로고
    • Proteomics analysis of rice leaves during drought stress and recovery
    • Salekdeh, G. H., Siopongco, J., Wade, L. J., Ghareyazie, B., and Bennett, J. (2002a). Proteomics analysis of rice leaves during drought stress and recovery. Proteomics 2, 1131-1145.
    • (2002) Proteomics , vol.2 , pp. 1131-1145
    • Salekdeh, G.H.1    Siopongco, J.2    Wade, L.J.3    Ghareyazie, B.4    Bennett, J.5
  • 70
  • 71
    • 0025006443 scopus 로고
    • Different types of dienelactone hydrolase in 4-fluorobenzoate utilizing bacteria
    • Schlomann, M., Schmidt, E., and Knackmuss, H. J. (1990). Different types of dienelactone hydrolase in 4-fluorobenzoate utilizing bacteria. J. Bacteriol. 179, 5112-5118.
    • (1990) J. Bacteriol. , vol.179 , pp. 5112-5118
    • Schlomann, M.1    Schmidt, E.2    Knackmuss, H.J.3
  • 72
    • 84870625577 scopus 로고    scopus 로고
    • Proteomics-based identification of low-abundance signaling and regulatory protein complexes in native plant tissues
    • Smaczniak, C., Li, N., Boeren, S., America, T., van Dongen, W., Goerdayal, S. S., et al. (2012). Proteomics-based identification of low-abundance signaling and regulatory protein complexes in native plant tissues. Nat. Protoc. 7, 2144-2158.
    • (2012) Nat. Protoc. , vol.7 , pp. 2144-2158
    • Smaczniak, C.1    Li, N.2    Boeren, S.3    America, T.4    van Dongen, W.5    Goerdayal, S.S.6
  • 73
    • 77952250066 scopus 로고    scopus 로고
    • Proteome analysis of soybean leaves, hypocotyls and roots under salt stress
    • doi: 10.1186/1477-5956-8-19
    • Sobhanian, H., Razavizadeh, R., Nanjo, Y., Ehsanpour, A. A., Jazii, F. R., Motamed, N., et al. (2010). Proteome analysis of soybean leaves, hypocotyls and roots under salt stress. Proteome Sci. 8:19. doi: 10.1186/1477-5956-8-19
    • (2010) Proteome Sci. , vol.8 , pp. 19
    • Sobhanian, H.1    Razavizadeh, R.2    Nanjo, Y.3    Ehsanpour, A.A.4    Jazii, F.R.5    Motamed, N.6
  • 74
    • 0037238767 scopus 로고    scopus 로고
    • Molecular and cellular adaptations of maize to flooding stress
    • Subbaiah, C. C., and Sachs, M. M. (2003). Molecular and cellular adaptations of maize to flooding stress. Ann. Bot. 90, 119-127.
    • (2003) Ann. Bot. , vol.90 , pp. 119-127
    • Subbaiah, C.C.1    Sachs, M.M.2
  • 75
    • 74349083387 scopus 로고    scopus 로고
    • Proteomic analysis of specific proteins in the root of salt-tolerant barley
    • Sugimoto, M., and Takeda, K. (2009). Proteomic analysis of specific proteins in the root of salt-tolerant barley. Biosci. Biotechnol. Biochem. 73, 2762-2765.
    • (2009) Biosci. Biotechnol. Biochem. , vol.73 , pp. 2762-2765
    • Sugimoto, M.1    Takeda, K.2
  • 76
    • 71949124535 scopus 로고    scopus 로고
    • Proteomics reveals the overlapping roles of hydrogen peroxide and nitric oxide in the acclimation of citrus plants to salinity
    • Tanou, G., Job, C., Rajjou, L., Arc, E., Belghazi, M., Diamantidis, G., et al. (2009). Proteomics reveals the overlapping roles of hydrogen peroxide and nitric oxide in the acclimation of citrus plants to salinity. Plant J. 60, 795-804.
    • (2009) Plant J. , vol.60 , pp. 795-804
    • Tanou, G.1    Job, C.2    Rajjou, L.3    Arc, E.4    Belghazi, M.5    Diamantidis, G.6
  • 77
    • 70449622771 scopus 로고    scopus 로고
    • Proteomics approach for identifying osmotic-stress-related proteins in soybean roots
    • Toorchi, M., Yukawa, K., Nouri, M. Z., and Komatsu, S. (2009). Proteomics approach for identifying osmotic-stress-related proteins in soybean roots. Peptides 30, 2108-2117.
    • (2009) Peptides , vol.30 , pp. 2108-2117
    • Toorchi, M.1    Yukawa, K.2    Nouri, M.Z.3    Komatsu, S.4
  • 78
    • 51149107839 scopus 로고    scopus 로고
    • Comparison of photosynthetic induction and transient limitations during the induction phase in young and mature leaves from three poplar clones
    • Urban, O., Sprtova, M., Kosvancova, M., Tomaskova, I., Lichtenthaler, H. K., and Marek, M. V. (2008). Comparison of photosynthetic induction and transient limitations during the induction phase in young and mature leaves from three poplar clones. Tree Physiol. 28, 1189-1197.
    • (2008) Tree Physiol. , vol.28 , pp. 1189-1197
    • Urban, O.1    Sprtova, M.2    Kosvancova, M.3    Tomaskova, I.4    Lichtenthaler, H.K.5    Marek, M.V.6
  • 79
    • 20444472040 scopus 로고    scopus 로고
    • Water deficits affect caffeate O-methyltransferase, lignification, and related enzymes in maize leaves. A proteomic investigation
    • Vincent, D., Lapierre, C., Pollet, B., Cornic, G., Negroni, L., and Zivy, M. (2005). Water deficits affect caffeate O-methyltransferase, lignification, and related enzymes in maize leaves. A proteomic investigation. Plant Physiol. 137, 949-960.
    • (2005) Plant Physiol. , vol.137 , pp. 949-960
    • Vincent, D.1    Lapierre, C.2    Pollet, B.3    Cornic, G.4    Negroni, L.5    Zivy, M.6
  • 80
    • 2442445139 scopus 로고    scopus 로고
    • Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response
    • Wang, W., Vinocur, B., Shoseyov, O., and Altman, A. (2004). Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response. Trends Plant Sci. 9, 244-252.
    • (2004) Trends Plant Sci. , vol.9 , pp. 244-252
    • Wang, W.1    Vinocur, B.2    Shoseyov, O.3    Altman, A.4
  • 81
    • 67650388759 scopus 로고    scopus 로고
    • Comparative proteomic analysis of differentially expressed proteins in shoots of Salicornia europaea under different salinity
    • Wang, X., Fan, P., Song, H., Chen, X., Li, X., and Li, Y. (2009). Comparative proteomic analysis of differentially expressed proteins in shoots of Salicornia europaea under different salinity. J. Proteome Res. 8, 3331-3345.
    • (2009) J. Proteome Res. , vol.8 , pp. 3331-3345
    • Wang, X.1    Fan, P.2    Song, H.3    Chen, X.4    Li, X.5    Li, Y.6
  • 82
    • 0037353383 scopus 로고    scopus 로고
    • Mapping the proteome of barrel medic (Medicago truncatula)
    • Watson, B. S., Asirvatham, V. S., Wang, L., and Sumner, L. W. (2003). Mapping the proteome of barrel medic (Medicago truncatula). Plant Physiol. 131, 1104-1123.
    • (2003) Plant Physiol. , vol.131 , pp. 1104-1123
    • Watson, B.S.1    Asirvatham, V.S.2    Wang, L.3    Sumner, L.W.4
  • 83
    • 0036181615 scopus 로고    scopus 로고
    • ABA-based chemical signalling: The coordination of responses to stress in plants
    • Wilkinson, S., and Davies, W. J. (2002). ABA-based chemical signalling: the coordination of responses to stress in plants. Plant Cell Environ. 25, 195-210.
    • (2002) Plant Cell Environ. , vol.25 , pp. 195-210
    • Wilkinson, S.1    Davies, W.J.2
  • 84
    • 13244258357 scopus 로고    scopus 로고
    • Proteomic analysis of salt stress-responsive proteins in rice roots
    • Yan, S., Tang, Z., Su, W., and Sun, W. (2005). Proteomic analysis of salt stress-responsive proteins in rice roots. Proteomics 5, 235-244.
    • (2005) Proteomics , vol.5 , pp. 235-244
    • Yan, S.1    Tang, Z.2    Su, W.3    Sun, W.4
  • 85
    • 84856654636 scopus 로고    scopus 로고
    • Ubiquitin/proteasome-mediated proteolysis is involved in the response to flooding stress in soybean roots, independent of oxygen limitation
    • Yanagawa, Y., and Komatsu, S. (2012). Ubiquitin/proteasome-mediated proteolysis is involved in the response to flooding stress in soybean roots, independent of oxygen limitation. Plant Sci. 185-186, 250-258.
    • (2012) Plant Sci. , vol.185-186 , pp. 250-258
    • Yanagawa, Y.1    Komatsu, S.2
  • 86
    • 38949158775 scopus 로고    scopus 로고
    • Programmed proteome response for drought avoidance/tolerance in the root of a c3 xerophyte (wild watermelon) under water deficits
    • Yoshimura, K., Masuda, A., Kuwano, M., Yokota, A., and Akashi, K. (2008). Programmed proteome response for drought avoidance/tolerance in the root of a c3 xerophyte (wild watermelon) under water deficits. Plant Cell Physiol. 49, 226-241.
    • (2008) Plant Cell Physiol. , vol.49 , pp. 226-241
    • Yoshimura, K.1    Masuda, A.2    Kuwano, M.3    Yokota, A.4    Akashi, K.5
  • 87
    • 33846570438 scopus 로고    scopus 로고
    • A proteomics approach for identifying osmotic stress-related proteins in rice
    • Zang, X., and Komatsu, S. (2007). A proteomics approach for identifying osmotic stress-related proteins in rice. Phytochemistry 68, 426-437.
    • (2007) Phytochemistry , vol.68 , pp. 426-437
    • Zang, X.1    Komatsu, S.2
  • 88
    • 78650038012 scopus 로고    scopus 로고
    • Proteomic changes in maize roots after short-term adjustment to saline growth conditions
    • Zörb, C., Schmitt, S., and Mühling, K. H. (2010). Proteomic changes in maize roots after short-term adjustment to saline growth conditions. Proteomics 10, 4441-4449.
    • (2010) Proteomics , vol.10 , pp. 4441-4449
    • Zörb, C.1    Schmitt, S.2    Mühling, K.H.3


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