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Volumn , Issue , 2016, Pages 465-518

Protein synthesis by plants under stressful conditions

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EID: 84895759276     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (7)

References (342)
  • 1
    • 0037212265 scopus 로고    scopus 로고
    • Expression of an ABA responsive 21 kDa protein in finger millet (Eleusine coracana Gaertn.) under stress and its relevance in stress tolerance
    • Aarati, P., B. T. Krishnaprasad, G. M. Savitha, R. Gopalakrishna, G. Ramamohan, and M. Udayakumar. 2003. Expression of an ABA responsive 21 kDa protein in finger millet (Eleusine coracana Gaertn.) under stress and its relevance in stress tolerance. Plant Sci. 164:25-34.
    • (2003) Plant Sci , vol.164 , pp. 25-34
    • Aarati, P.1    Krishnaprasad, B.T.2    Savitha, G.M.3    Gopalakrishna, R.4    Ramamohan, G.5    Udayakumar, M.6
  • 2
    • 0030596559 scopus 로고    scopus 로고
    • Antifungal activity of tobacco osmotin has specificity and involves plasma membrane permeabilization
    • Abad, L. R., M. P. D'Urzo, D. Liu, et al. 1996. Antifungal activity of tobacco osmotin has specificity and involves plasma membrane permeabilization. Plant Sci. 118:11-23.
    • (1996) Plant Sci , vol.118 , pp. 11-23
    • Abad, L.R.1    D'Urzo, M.P.2    Liu, D.3
  • 3
    • 34247193165 scopus 로고    scopus 로고
    • High salt-stress in wheat leaves (Triticum aestivum) causes retardation of chlorophyll accumulation due to a limited rate of protochlorophyllide formation
    • Abdelkader, A. F., H. Aronsson, and C. Sundqvist. 2007. High salt-stress in wheat leaves (Triticum aestivum) causes retardation of chlorophyll accumulation due to a limited rate of protochlorophyllide formation. Physiol. Plant. 130:157-166.
    • (2007) Physiol. Plant , vol.130 , pp. 157-166
    • Abdelkader, A.F.1    Aronsson, H.2    Sundqvist, C.3
  • 4
    • 0036113353 scopus 로고    scopus 로고
    • Rapid induction of defense/stress-related proteins in leaves of rice (Oryza sativa) seedlings exposed to ozone is preceded by newly phosphorylated proteins and changes in a 66 kDa ERK-type MAPK
    • Agrawal, G. K., R. Rakwal, M. Yonekura, A. Kubo, and H. Saji. 2002. Rapid induction of defense/stress-related proteins in leaves of rice (Oryza sativa) seedlings exposed to ozone is preceded by newly phosphorylated proteins and changes in a 66 kDa ERK-type MAPK. J. Plant Physiol. 159:361-369.
    • (2002) J. Plant Physiol , vol.159 , pp. 361-369
    • Agrawal, G.K.1    Rakwal, R.2    Yonekura, M.3    Kubo, A.4    Saji, H.5
  • 5
    • 0034960119 scopus 로고    scopus 로고
    • Protein patterns in germinating seeds of Vicia faba lines in response to interactive effects of salinity and vitamins treatments
    • Ahmed, A. M., A. M. Ismail, and M. M. Azooz. 2001. Protein patterns in germinating seeds of Vicia faba lines in response to interactive effects of salinity and vitamins treatments. Phyton 41:97-110.
    • (2001) Phyton , vol.41 , pp. 97-110
    • Ahmed, A.M.1    Ismail, A.M.2    Azooz, M.M.3
  • 6
    • 33645088178 scopus 로고    scopus 로고
    • Introduction of the carrot HSP 17.7 into potato (Solanum tuberosum L.) enhances cellular membrane stability and tuberization in vitro
    • Ahn, Y. J. and J. L. Zimmerman. 2006. Introduction of the carrot HSP 17.7 into potato (Solanum tuberosum L.) enhances cellular membrane stability and tuberization in vitro. Plant Cell Environ. 29:95-104.
    • (2006) Plant Cell Environ , vol.29 , pp. 95-104
    • Ahn, Y.J.1    Zimmerman, J.L.2
  • 8
    • 33845234986 scopus 로고    scopus 로고
    • Expression of BjMT2, a metallothionein 2 from Brassica juncea, increases copper and cadmium tolerance in Escherichia coli and Arabidopsis thaliana, but inhibits root elongation in Arabidopsis thaliana seedlings
    • An, Z. G., C. J. Li, Y. G. Zu, et al. 2006. Expression of BjMT2, a metallothionein 2 from Brassica juncea, increases copper and cadmium tolerance in Escherichia coli and Arabidopsis thaliana, but inhibits root elongation in Arabidopsis thaliana seedlings. J. Exp. Bot. 57:3575-3582.
    • (2006) J. Exp. Bot , vol.57 , pp. 3575-3582
    • An, Z.G.1    Li, C.J.2    Zu, Y.G.3
  • 9
    • 0030948014 scopus 로고    scopus 로고
    • Antifreeze protein accumulation in freezing-tolerant cereals
    • Antikainen, M. and M. Griffith. 1997. Antifreeze protein accumulation in freezing-tolerant cereals. Physiol. Plant. 99:423-432.
    • (1997) Physiol. Plant , vol.99 , pp. 423-432
    • Antikainen, M.1    Griffith, M.2
  • 10
    • 0018899012 scopus 로고
    • Comparison of three pathogenesisrelated proteins from plants of two cultivars of tobacco infected with TMV
    • Antoniw, J. F., C. E. Ritter, W. S. Pierpoint, and L. C. Van Loon. 1980. Comparison of three pathogenesisrelated proteins from plants of two cultivars of tobacco infected with TMV. J. Gen. Virol. 47:79-87.
    • (1980) J. Gen. Virol , vol.47 , pp. 79-87
    • Antoniw, J.F.1    Ritter, C.E.2    Pierpoint, W.S.3    Van Loon, L.C.4
  • 11
    • 0031397984 scopus 로고    scopus 로고
    • Chill-response dehydrins in blueberry: Are they associated with cold hardiness or dormancy transitions?
    • Arora, R., L. J. Rowland, and A. R. Panta. 1997. Chill-response dehydrins in blueberry: Are they associated with cold hardiness or dormancy transitions?. Physiol. Plant. 101:8-16.
    • (1997) Physiol. Plant , vol.101 , pp. 8-16
    • Arora, R.1    Rowland, L.J.2    Panta, A.R.3
  • 12
    • 0031850955 scopus 로고    scopus 로고
    • Water-stress-induced heat tolerance in geranium leaf tissues: A possible linkage through stress proteins?
    • Arora, R., D. S. Pitchay, and B. C. Bearce. 1998. Water-stress-induced heat tolerance in geranium leaf tissues: A possible linkage through stress proteins?. Physiol. Plant. 103:24-34.
    • (1998) Physiol. Plant , vol.103 , pp. 24-34
    • Arora, R.1    Pitchay, D.S.2    Bearce, B.C.3
  • 13
    • 1842337657 scopus 로고
    • Protein synthetic responses to environmental stresses
    • In Handbook of Plant and Crop Physiology, New York: Marcel Dekker Inc
    • Artlip, T. S. and E. A. Funkhouser. 1995. Protein synthetic responses to environmental stresses. In Handbook of Plant and Crop Physiology, ed. M. Pessarakli, pp. 627-644. New York: Marcel Dekker Inc.
    • (1995) M. Pessarakli , pp. 627-644
    • Artlip, T.S.1    Funkhouser, E.A.2
  • 14
    • 32244439978 scopus 로고    scopus 로고
    • Effect of salt stress on antioxidative enzymes and lipid perosidation in leaves and roots of salt-tolerant and salt-sensitive maize genotypes
    • Azevedo-Neto, A. D., J. T. Prisco, J. Enéas-Filho, C. E. B. Abreu, and E. Gomes-Filho. 2006. Effect of salt stress on antioxidative enzymes and lipid perosidation in leaves and roots of salt-tolerant and salt-sensitive maize genotypes. Environ. Exp. Bot. 56:87-94.
    • (2006) Environ. Exp. Bot , vol.56 , pp. 87-94
    • Azevedo-Neto, A.D.1    Prisco, J.T.2    Enéas-Filho, J.3    Abreu, C.E.B.4    Gomes-Filho, E.5
  • 15
    • 0028191454 scopus 로고
    • Induction of pathogenesis-related proteins in sugar accumulating tobacco leaves
    • Badur, R., K. Herbers, G. Mönke, F. Ludewig, and U. Sonnewald. 1994. Induction of pathogenesis-related proteins in sugar accumulating tobacco leaves. Photosynthetica 30:575-582.
    • (1994) Photosynthetica , vol.30 , pp. 575-582
    • Badur, R.1    Herbers, K.2    Mönke, G.3    Ludewig, F.4    Sonnewald, U.5
  • 16
    • 0344668825 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis nuclear proteome and its response to cold stress
    • Bae, M. S., E. J. Cho, E. Y. Choi, and O. K. Park. 2003. Analysis of the Arabidopsis nuclear proteome and its response to cold stress. Plant J. 36:652-663.
    • (2003) Plant J , vol.36 , pp. 652-663
    • Bae, M.S.1    Cho, E.J.2    Choi, E.Y.3    Park, O.K.4
  • 17
    • 33745154176 scopus 로고    scopus 로고
    • Effect of soil drought stress on leaf water status, membrane permeability and enzymatic antioxidant system of maize
    • Bai, L. P., F. G. Sui, T. D. Ge, Z. H. Sun, Y. Y. Lu, and G. S. Zhou. 2006. Effect of soil drought stress on leaf water status, membrane permeability and enzymatic antioxidant system of maize. Pedosphere 16:326-332.
    • (2006) Pedosphere , vol.16 , pp. 326-332
    • Bai, L.P.1    Sui, F.G.2    Ge, T.D.3    Sun, Z.H.4    Lu, Y.Y.5    Zhou, G.S.6
  • 18
    • 0029178085 scopus 로고
    • A comparison of desiccation-related proteins (dehydrin and QP47) in peas (Pisum satium)
    • Baker, E. H., K. J. Bradford, J. A. Bryant, and T. L. Rost. 1995. A comparison of desiccation-related proteins (dehydrin and QP47) in peas (Pisum satium). Seed Sci. Res. 5:185-193.
    • (1995) Seed Sci. Res , vol.5 , pp. 185-193
    • Baker, E.H.1    Bradford, K.J.2    Bryant, J.A.3    Rost, T.L.4
  • 19
    • 0029189151 scopus 로고
    • NaCl stress enhances proteolytic turnover of the tonoplast H+-ATPase of Citrus sinensis-appearance of a 35 kDa fragment of subunit A still exhibiting ATPhydrolysis activity
    • Banuls, J., R. Ratajczak, and U. Luttge. 1995. NaCl stress enhances proteolytic turnover of the tonoplast H+-ATPase of Citrus sinensis-appearance of a 35 kDa fragment of subunit A still exhibiting ATPhydrolysis activity. Plant Cell Environ. 18:1341-1344.
    • (1995) Plant Cell Environ , vol.18 , pp. 1341-1344
    • Banuls, J.1    Ratajczak, R.2    Luttge, U.3
  • 20
    • 0000040272 scopus 로고
    • Amino acid and protein metabolism in bermuda grass during water stress
    • Barnett, N. M. and A. W. Naylor. 1966. Amino acid and protein metabolism in bermuda grass during water stress. Plant Physiol. 41:1222-1230.
    • (1966) Plant Physiol , vol.41 , pp. 1222-1230
    • Barnett, N.M.1    Naylor, A.W.2
  • 21
    • 0035099460 scopus 로고    scopus 로고
    • Over-expression of osmotin induces proline accumulation and confers tolerance to osmotic stress in transgenic tobacco
    • Barthakur, S., V. Babu, and K. C. Bansal. 2001. Over-expression of osmotin induces proline accumulation and confers tolerance to osmotic stress in transgenic tobacco. J. Plant Biochem. Biotechnol. 10:31-37.
    • (2001) J. Plant Biochem. Biotechnol , vol.10 , pp. 31-37
    • Barthakur, S.1    Babu, V.2    Bansal, K.C.3
  • 22
    • 0001662576 scopus 로고
    • Proteins associated with salt adaptation in citrus and tomato cells: Involvement of 26 kDa polypeptides
    • Ben-Hayyim, G., Y. Vaadia, and B. G. Williams. 1989. Proteins associated with salt adaptation in citrus and tomato cells: Involvement of 26 kDa polypeptides. Physiol. Plant. 77:332-340.
    • (1989) Physiol. Plant , vol.77 , pp. 332-340
    • Ben-Hayyim, G.1    Vaadia, Y.2    Williams, B.G.3
  • 23
    • 0013354410 scopus 로고
    • Differences in the responses to water stress of growing and non-growing regions of maize mesocotyls: Protein synthesis on total, free and membrane bound polyribosome fractions
    • Bewley, J. D. and K. M. Larsen. 1982. Differences in the responses to water stress of growing and non-growing regions of maize mesocotyls: Protein synthesis on total, free and membrane bound polyribosome fractions. J. Exp. Bot. 33:406-415.
    • (1982) J. Exp. Bot , vol.33 , pp. 406-415
    • Bewley, J.D.1    Larsen, K.M.2
  • 24
    • 79960651657 scopus 로고    scopus 로고
    • Water stress induced variations in protein profiles of germinating cotyledons from seedlings of chickpea genotypes
    • Bibi, N., A. Hameed, H. Ali, et al. 2009. Water stress induced variations in protein profiles of germinating cotyledons from seedlings of chickpea genotypes. Pak. J. Bot. 41:731-736.
    • (2009) Pak. J. Bot , vol.41 , pp. 731-736
    • Bibi, N.1    Hameed, A.2    Ali, H.3
  • 25
    • 0034055539 scopus 로고    scopus 로고
    • Expression and activity of isoenzymes of superoxide dismutase in wheat roots in response to hypoxia and anoxia
    • Biemelt, S., U. Keetman, H. P. Mock, and B. Grimm. 2000. Expression and activity of isoenzymes of superoxide dismutase in wheat roots in response to hypoxia and anoxia. Plant Cell Environ. 23:135-144.
    • (2000) Plant Cell Environ , vol.23 , pp. 135-144
    • Biemelt, S.1    Keetman, U.2    Mock, H.P.3    Grimm, B.4
  • 26
    • 0037237973 scopus 로고    scopus 로고
    • Antioxidants, oxidative damage and oxygen deprivation stress: A review
    • Blokhina, O. B., E. Virolainen, and K. V. Fagerstedt. 2003. Antioxidants, oxidative damage and oxygen deprivation stress: A review. Ann. Bot. 91:179-194.
    • (2003) Ann. Bot , vol.91 , pp. 179-194
    • Blokhina, O.B.1    Virolainen, E.2    Fagerstedt, K.V.3
  • 27
    • 0345540683 scopus 로고    scopus 로고
    • Water deficit induced oxidative stress and antioxidative defence in rice plants
    • Boo, Y. C. and J. Jung. 1999. Water deficit induced oxidative stress and antioxidative defence in rice plants. J. Plant Physiol. 51:255-261.
    • (1999) J. Plant Physiol , vol.51 , pp. 255-261
    • Boo, Y.C.1    Jung, J.2
  • 28
    • 34347397980 scopus 로고
    • Regulation of gene expression during abiotic stresses, and the role of the plant hormone abscisic acid
    • In Handbook of Plant and Crop Physiology, New York: Marcel Dekker Inc
    • Bray, E. A. 1995. Regulation of gene expression during abiotic stresses, and the role of the plant hormone abscisic acid. In Handbook of Plant and Crop Physiology, ed. M. Pessarakli, pp. 733-752. New York: Marcel Dekker Inc.
    • (1995) M. Pessarakli , pp. 733-752
    • Bray, A.E.1
  • 29
    • 35248855455 scopus 로고    scopus 로고
    • Overexpression of wheat dehydrin DHN-5 enhances tolerance to salt and osmotic stress in Arabidopsis thaliana
    • Brini, F., M. Hanin, V. Lumbreras, et al. 2007. Overexpression of wheat dehydrin DHN-5 enhances tolerance to salt and osmotic stress in Arabidopsis thaliana. Plant Cell Rep. 26:2017-2026.
    • (2007) Plant Cell Rep , vol.26 , pp. 2017-2026
    • Brini, F.1    Hanin, M.2    Lumbreras, V.3
  • 30
    • 0342972186 scopus 로고
    • Comparison of some molecular, enzymatic and antifungal properties of chitinases from thorn-apple, tobacco and wheat
    • Broekaert, W. F., J. V. Parijs, A. K. Allen, and W. J. Peumans. 1988. Comparison of some molecular, enzymatic and antifungal properties of chitinases from thorn-apple, tobacco and wheat. Physiol. Mol. Plant. Pathol. 33:319-331.
    • (1988) Physiol. Mol. Plant. Pathol , vol.33 , pp. 319-331
    • Broekaert, W.F.1    Parijs, J.V.2    Allen, A.K.3    Peumans, W.J.4
  • 32
    • 0001082038 scopus 로고
    • Accumulation of heat shock proteins in fieldgrown cotton
    • Burke, J. J., J. L. Hatfield, R. R. Klein, and J. E. Mullet. 1985. Accumulation of heat shock proteins in fieldgrown cotton. Plant Physiol. 78:394-398.
    • (1985) Plant Physiol , vol.78 , pp. 394-398
    • Burke, J.J.1    Hatfield, J.L.2    Klein, R.R.3    Mullet, J.E.4
  • 33
    • 0028252689 scopus 로고
    • Chitinase and beta-1,3-glucanase activities in chickpea (Cicer arietinum)-Induction of different isoenzymes in response to wounding and ethephon
    • Cabello, F., J. V. Jorrín, and M. Tena. 1994. Chitinase and beta-1,3-glucanase activities in chickpea (Cicer arietinum)-Induction of different isoenzymes in response to wounding and ethephon. Physiol. Plant. 92:654-660.
    • (1994) Physiol. Plant , vol.92 , pp. 654-660
    • Cabello, F.1    Jorrín, J.V.2    Tena, M.3
  • 34
    • 14644398626 scopus 로고    scopus 로고
    • High temperature effects on photosynthetic activity of two tomato cultivars with different heat susceptibility
    • Camejo, D., P. Rodriguez, M. A. Morales, J. M. Dell'amico, A. Torrecillas, and J. J. Alarcon. 2005. High temperature effects on photosynthetic activity of two tomato cultivars with different heat susceptibility. J. Plant Physiol. 162:281-289.
    • (2005) J. Plant Physiol , vol.162 , pp. 281-289
    • Camejo, D.1    Rodriguez, P.2    Morales, M.A.3    Dell'amico, J.M.4    Torrecillas, A.5    Alarcon, J.J.6
  • 35
    • 0029663798 scopus 로고    scopus 로고
    • Differences in responses to urban air pollutants by Ligustrum lucidum AIT and Ligustrum lucidum AIT F tricolor (REHD)
    • Carreras, H. A., M. S. Canas, and M. L. Pignata. 1996. Differences in responses to urban air pollutants by Ligustrum lucidum AIT and Ligustrum lucidum AIT F tricolor (REHD). Environ. Pollut. 93:211-218.
    • (1996) Environ. Pollut , vol.93 , pp. 211-218
    • Carreras, H.A.1    Canas, M.S.2    Pignata, M.L.3
  • 36
    • 28644445106 scopus 로고    scopus 로고
    • Analysis of leaf proteome after UV-B irradiation in maize lines differing in sensitivity
    • Casati, P., X. Zhang, A. L. Burlingame, and V. Walbot. 2005. Analysis of leaf proteome after UV-B irradiation in maize lines differing in sensitivity. Mol. Cell. Proteomics 4:1673-1685.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1673-1685
    • Casati, P.1    Zhang, X.2    Burlingame, A.L.3    Walbot, V.4
  • 37
    • 0031148691 scopus 로고    scopus 로고
    • The isolation of a novel metallothionein-related cDNA expressed in somatic and zygotic embryos of Douglas-fir: Regulation by ABA, osmoticum and metal ions
    • Chatthai, M., K. H. Kaukinen, T. J. Tranbarger, P. K. Gupta, and S. Misra. 1997. The isolation of a novel metallothionein-related cDNA expressed in somatic and zygotic embryos of Douglas-fir: Regulation by ABA, osmoticum and metal ions. Plant Mol. Biol. 34:243-254.
    • (1997) Plant Mol. Biol , vol.34 , pp. 243-254
    • Chatthai, M.1    Kaukinen, K.H.2    Tranbarger, T.J.3    Gupta, P.K.4    Misra, S.5
  • 38
    • 0031401692 scopus 로고    scopus 로고
    • Characterization of phytochelatin synthase from tomato
    • Chen, J., J. Zhou, and P. B. Goldsbrough. 1997. Characterization of phytochelatin synthase from tomato. Physiol. Plant. 101:165-172.
    • (1997) Physiol. Plant , vol.101 , pp. 165-172
    • Chen, J.1    Zhou, J.2    Goldsbrough, P.B.3
  • 39
    • 13444257653 scopus 로고    scopus 로고
    • Characterization of the wound-inducible protein ipomoelin from sweet potato
    • Chen, Y. C., H. S. Chang, H. M. Lai, and S. T. Jeng. 2005. Characterization of the wound-inducible protein ipomoelin from sweet potato. Plant Cell Environ. 28:251-259.
    • (2005) Plant Cell Environ , vol.28 , pp. 251-259
    • Chen, Y.C.1    Chang, H.S.2    Lai, H.M.3    Jeng, S.T.4
  • 40
    • 61449177749 scopus 로고    scopus 로고
    • A nuclear-localized HSP70 confers thermoprotective activity and droughtstress tolerance on plants
    • Cho, E. K. and Y. J. Choi. 2009. A nuclear-localized HSP70 confers thermoprotective activity and droughtstress tolerance on plants. Biotechnol. Lett. 31:597-606.
    • (2009) Biotechnol. Lett , vol.31 , pp. 597-606
    • Cho, E.K.1    Choi, Y.J.2
  • 41
    • 85050897586 scopus 로고
    • A cDNA differentially expressed by Cadmium stress in Arabidopsis
    • Choi, S. Y., E. M. Baek, and S. Y. Lee. 1995. A cDNA differentially expressed by Cadmium stress in Arabidopsis. Plant Physiol. 101:699-700.
    • (1995) Plant Physiol , vol.101 , pp. 699-700
    • Choi, S.Y.1    Baek, E.M.2    Lee, S.Y.3
  • 42
    • 0029766034 scopus 로고    scopus 로고
    • Characterization of hypoxically inducible lactate dehydrogenase in maize
    • Christopher, M. E. and A. G. Good. 1996. Characterization of hypoxically inducible lactate dehydrogenase in maize. Plant Physiol. 112:1015-1022.
    • (1996) Plant Physiol , vol.112 , pp. 1015-1022
    • Christopher, M.E.1    Good, A.G.2
  • 43
    • 0024982162 scopus 로고
    • Characterization of a rice gene showing organ-specific expression in response to salt stress and drought
    • Claes, B., R. Dekeyser, R. Villarroel, et al. 1990. Characterization of a rice gene showing organ-specific expression in response to salt stress and drought. Plant Cell 2:19-27.
    • (1990) Plant Cell , vol.2 , pp. 19-27
    • Claes, B.1    Dekeyser, R.2    Villarroel, R.3
  • 44
    • 0031007034 scopus 로고    scopus 로고
    • Dehydrins-A commonalty in the response of plants to dehydration and low temperature
    • Close, T. J. 1997. Dehydrins-A commonalty in the response of plants to dehydration and low temperature. Physiol. Plant. 100:291-296.
    • (1997) Physiol. Plant , vol.100 , pp. 291-296
    • Close, J.T.1
  • 45
    • 0037002169 scopus 로고    scopus 로고
    • Phytochelatins and metallothioneins: Roles in heavy metal detoxification and homeostasis
    • Cobbett, C. and P. Goldsbrough. 2002. Phytochelatins and metallothioneins: Roles in heavy metal detoxification and homeostasis. Annu. Rev. Plant Biol. 53:159-182.
    • (2002) Annu. Rev. Plant Biol , vol.53 , pp. 159-182
    • Cobbett, C.1    Goldsbrough, P.2
  • 46
    • 0029360417 scopus 로고
    • Differential accumulation of antioxidant mRNAs in Arabidopsis thaliana exposed to ozone
    • Conklin, P. L. and R. L. Last. 1995. Differential accumulation of antioxidant mRNAs in Arabidopsis thaliana exposed to ozone. Plant Physiol. 109:203-212.
    • (1995) Plant Physiol , vol.109 , pp. 203-212
    • Conklin, P.L.1    Last, R.L.2
  • 47
    • 0030976480 scopus 로고    scopus 로고
    • Protein dephosphorylation mediates salicylic acid-induced expression of PR-1 genes in tobacco
    • Conrath, U., H. Silva, and D. F. Klessig. 1997. Protein dephosphorylation mediates salicylic acid-induced expression of PR-1 genes in tobacco. Plant J. 11:747-757.
    • (1997) Plant J , vol.11 , pp. 747-757
    • Conrath, U.1    Silva, H.2    Klessig, D.F.3
  • 48
    • 0001469584 scopus 로고
    • Heat shock proteins in maize
    • Cooper, P. and T. H. D. Ho. 1983. Heat shock proteins in maize. Plant Physiol. 71:215-222.
    • (1983) Plant Physiol , vol.71 , pp. 215-222
    • Cooper, P.1    Ho, T.H.D.2
  • 49
    • 0028837057 scopus 로고
    • Change in synthesis and localization of members of the 70 kDa class of heat-stress proteins accompany the induction of embryogenesis in Brassica napus L
    • Cordewener, J. H. G., G. Hause, E. Gorgen, et al. 1995. Change in synthesis and localization of members of the 70 kDa class of heat-stress proteins accompany the induction of embryogenesis in Brassica napus L. microspores. Planta 196:747-755.
    • (1995) microspores. Planta , vol.196 , pp. 747-755
    • Cordewener, J.H.G.1    Hause, G.2    Gorgen, E.3
  • 50
    • 0029141436 scopus 로고
    • Cell-wall proteins induced by water deficit in bean (Phaseolus vulgaris L.) seedlings
    • Covarrubias, A. A., J. W. Ayala, J. L. Reyes, M. Hernandez, and A. Garciarrubio. 1995. Cell-wall proteins induced by water deficit in bean (Phaseolus vulgaris L.) seedlings. Plant Physiol. 107:1119-1128.
    • (1995) Plant Physiol , vol.107 , pp. 1119-1128
    • Covarrubias, A.A.1    Ayala, J.W.2    Reyes, J.L.3    Hernandez, M.4    Garciarrubio, A.5
  • 52
    • 33947194870 scopus 로고    scopus 로고
    • Osmotin induces cold protection in olive trees by affecting programmed cell death and cytoskeleton organization
    • D'Angeli, S. and M. M. Altamura. 2007. Osmotin induces cold protection in olive trees by affecting programmed cell death and cytoskeleton organization. Planta 225:1147-1163.
    • (2007) Planta , vol.225 , pp. 1147-1163
    • D'Angeli, S.1    Altamura, M.M.2
  • 54
    • 57949100310 scopus 로고    scopus 로고
    • Abiotic stress and ABA-inducible Group 4 LEA from Brassica napus plays a key role in salt and drought tolerance
    • Dalal, M., D. Tayal, V. Chinnusamy, and K. C. Bansal. 2009. Abiotic stress and ABA-inducible Group 4 LEA from Brassica napus plays a key role in salt and drought tolerance. J. Biotechnol. 139:137-145.
    • (2009) J. Biotechnol , vol.139 , pp. 137-145
    • Dalal, M.1    Tayal, D.2    Chinnusamy, V.3    Bansal, K.C.4
  • 55
    • 0030295021 scopus 로고    scopus 로고
    • The effect of pathogen inoculation or chemical treatment on activities of chitinase and beta-1,3-glucanase and accumulation of salicylic acid in leaves of green bean, Phaseolus vulgaris
    • Dann, E. K., P. Meuwly, J. P. Metraux, and B. J. Deverall. 1996. The effect of pathogen inoculation or chemical treatment on activities of chitinase and beta-1,3-glucanase and accumulation of salicylic acid in leaves of green bean, Phaseolus vulgaris. Physiol. Mol. Plant Pathol. 49:307-319.
    • (1996) Physiol. Mol. Plant Pathol , vol.49 , pp. 307-319
    • Dann, E.K.1    Meuwly, P.2    Metraux, J.P.3    Deverall, B.J.4
  • 56
    • 37349075469 scopus 로고    scopus 로고
    • Germination, initial growth and cotyledon protein content of bean cultivars under salinity stress
    • Dantas, B. F., L. S. Ribeiro, and C. A. Aragao. 2007. Germination, initial growth and cotyledon protein content of bean cultivars under salinity stress. Rev. Bras. Sementes 29:106-110.
    • (2007) Rev. Bras. Sementes , vol.29 , pp. 106-110
    • Dantas, B.F.1    Ribeiro, L.S.2    Aragao, C.A.3
  • 57
    • 0005594918 scopus 로고
    • Variations in protein synthesis in different regions of greening leaves of barley seedlings and effects of imposed water stress
    • Dasgupta, J. and J. D. Bewley. 1984. Variations in protein synthesis in different regions of greening leaves of barley seedlings and effects of imposed water stress. J. Exp. Bot. 35:1450-1459.
    • (1984) J. Exp. Bot , vol.35 , pp. 1450-1459
    • Dasgupta, J.1    Bewley, J.D.2
  • 58
    • 0011909302 scopus 로고
    • Molecular responses to environmental stresses and their relationship to soft rot
    • In Molecular and Cellular Biology of Potato, Wallingford, CT: CAB International
    • Davis, M., W. Butler, and M. E. Vayda. 1990. Molecular responses to environmental stresses and their relationship to soft rot. In Molecular and Cellular Biology of Potato, eds. M. Vayda and W. Park, pp. 71-87. Wallingford, CT: CAB International.
    • (1990) M. Vayda and W. Park , pp. 71-87
    • Davis, M.1    Butler, W.2    Vayda, M.E.3
  • 59
    • 34547754592 scopus 로고    scopus 로고
    • Changes in growth and activity of enzymes involved in nitrate reduction and ammonium assimilation in tomato seedlings in response to NaCl stress
    • Debouba, M., H. Maâroufi-Dghimi, A. Suzuki, M. H. Ghorbel, and H. Gouia. 2007. Changes in growth and activity of enzymes involved in nitrate reduction and ammonium assimilation in tomato seedlings in response to NaCl stress. Ann. Bot. 99:1143-1151.
    • (2007) Ann. Bot , vol.99 , pp. 1143-1151
    • Debouba, M.1    Maâroufi-Dghimi, H.2    Suzuki, A.3    Ghorbel, M.H.4    Gouia, H.5
  • 61
    • 34548225360 scopus 로고    scopus 로고
    • Cadmium induced changes in carbohydrate status and enzymes of carbohydrate metabolism, glycolysis and pentose phosphate pathway in pea
    • Devi, R., N. Munjral, A. K. Gupta, and N. Kaur. 2007. Cadmium induced changes in carbohydrate status and enzymes of carbohydrate metabolism, glycolysis and pentose phosphate pathway in pea. Environ. Exp. Bot. 61:167-174.
    • (2007) Environ. Exp. Bot , vol.61 , pp. 167-174
    • Devi, R.1    Munjral, N.2    Gupta, A.K.3    Kaur, N.4
  • 63
    • 0029689870 scopus 로고    scopus 로고
    • Heavy-metal-responsive genes in maize- Identification and comparison of their expression upon various forms of abiotic stress
    • Didierjean, L., P. Frendo, W. Nasser, G. Genot, J. Marivet, and G. Burkard. 1996. Heavy-metal-responsive genes in maize- Identification and comparison of their expression upon various forms of abiotic stress. Planta 199:1-8.
    • (1996) Planta , vol.199 , pp. 1-8
    • Didierjean, L.1    Frendo, P.2    Nasser, W.3    Genot, G.4    Marivet, J.5    Burkard, G.6
  • 64
    • 0003018764 scopus 로고    scopus 로고
    • Free radicals and reactive oxygen species as mediators of heavy metal toxicity in plants
    • In Heavy Metal Stress in Plant, Heidelberg, Germany: Springer-Verlag
    • Dietz, K. J., M. Baier, and U. Krämer. 1999. Free radicals and reactive oxygen species as mediators of heavy metal toxicity in plants. In Heavy Metal Stress in Plant, eds. M. N. V. Prasad and J. Hagemeyer, pp. 73-97. Heidelberg, Germany: Springer-Verlag.
    • (1999) M. N. V. Prasad and J. Hagemeyer , pp. 73-97
    • Dietz, K.J.1    Baier, M.2    Krämer, U.3
  • 65
    • 0030980186 scopus 로고    scopus 로고
    • Strategies of gene action in Arabidopsis during hypoxia
    • Dolferus, R., M. Ellis, G. Debruxelles, et al. 1997. Strategies of gene action in Arabidopsis during hypoxia. Ann. Bot. 79:21-31.
    • (1997) Ann. Bot , vol.79 , pp. 21-31
    • Dolferus, R.1    Ellis, M.2    Debruxelles, G.3
  • 67
    • 0029135828 scopus 로고
    • Light and stress-dependent enhancement of amylolitic activities in white and green barley leaves-beta-amylases are stress-induced proteins
    • Dreier, W., C. Schnarrenberger, and T. Borner. 1995. Light and stress-dependent enhancement of amylolitic activities in white and green barley leaves-beta-amylases are stress-induced proteins. J. Plant Physiol. 145:342-348.
    • (1995) J. Plant Physiol , vol.145 , pp. 342-348
    • Dreier, W.1    Schnarrenberger, C.2    Borner, T.3
  • 68
    • 0030453335 scopus 로고    scopus 로고
    • Effects of water stress on carbon exchange rate and activities of photosynthetic enzymes in leaves of sugarcane (Saccharum sp)
    • Du, Y. C., Y. Kawamitsu, A. Nose, et al. 1996. Effects of water stress on carbon exchange rate and activities of photosynthetic enzymes in leaves of sugarcane (Saccharum sp). Aust. J. Plant Physiol. 23:719-726.
    • (1996) Aust. J. Plant Physiol , vol.23 , pp. 719-726
    • Du, Y.C.1    Kawamitsu, Y.2    Nose, A.3
  • 69
    • 84864420251 scopus 로고    scopus 로고
    • Effects of salt stress on proline and polyamine metabolisms in the roots of cucumber seedlings
    • Duan, J. J., S. R. Guo, H. F. Fan, S. P. Wang, and Y. Y. Kang. 2006. Effects of salt stress on proline and polyamine metabolisms in the roots of cucumber seedlings. Acta Botanica Boreali-Occidentalia Sinica 26:2486-2492.
    • (2006) Acta Botanica Boreali-Occidentalia Sinica , vol.26 , pp. 2486-2492
    • Duan, J.J.1    Guo, S.R.2    Fan, H.F.3    Wang, S.P.4    Kang, Y.Y.5
  • 70
    • 0344366905 scopus 로고
    • Biochemical changes in germinating rice seeds under saline stress
    • Dubey, R. S. 1983. Biochemical changes in germinating rice seeds under saline stress. Biochem. Physiol. Pflanzen. 177:523-535.
    • (1983) Biochem. Physiol. Pflanzen , vol.177 , pp. 523-535
    • Dubey, S.R.1
  • 71
    • 0012186986 scopus 로고
    • Hydrolytic enzymes of rice seeds differing in salt tolerance
    • Dubey, R. S. 1983. Hydrolytic enzymes of rice seeds differing in salt tolerance. Plant Physiol. Biochem. 10(s):168-175.
    • (1983) Plant Physiol. Biochem , vol.10 , pp. 168-175
    • Dubey, S.R.1
  • 72
    • 1842677846 scopus 로고
    • Effect of salinity on nucleic acid metabolism of germinating rice seeds differing in salt tolerance
    • Dubey, R. S. 1985. Effect of salinity on nucleic acid metabolism of germinating rice seeds differing in salt tolerance. Plant Physiol. Biochem. (India) 12:9-16.
    • (1985) Plant Physiol. Biochem. (India) , vol.12 , pp. 9-16
    • Dubey, S.R.1
  • 73
    • 4243909384 scopus 로고    scopus 로고
    • Nitrogen metabolism in plants under salt stress
    • In Strategies for Improving Salt Tolerance in Higher Plants, New Delhi, India: IBH Publication
    • Dubey, R. S. 1997. Nitrogen metabolism in plants under salt stress. In Strategies for Improving Salt Tolerance in Higher Plants, eds. P. K. Jaiwal, R. P. Singh, and A. Gulati, pp. 129-158. New Delhi, India: IBH Publication.
    • (1997) P. K. Jaiwal, R. P. Singh, and A. Gulati , pp. 129-158
    • Dubey, S.R.1
  • 74
    • 0001748996 scopus 로고
    • Proteases and proteins in germinating rice seeds in relation to salt tolerance
    • Dubey, R. S. and M. Rani. 1987. Proteases and proteins in germinating rice seeds in relation to salt tolerance. Plant Physiol. Biochem. (India) 14:174-182.
    • (1987) Plant Physiol. Biochem. (India) , vol.14 , pp. 174-182
    • Dubey, R.S.1    Rani, M.2
  • 75
    • 0002841022 scopus 로고
    • Influence of NaCl salinity on growth and metabolic status of proteins and amino acids in rice seedlings
    • Dubey, R. S. and M. Rani. 1989. Influence of NaCl salinity on growth and metabolic status of proteins and amino acids in rice seedlings. J. Agron. Crop Sci. 162:97-106.
    • (1989) J. Agron. Crop Sci , vol.162 , pp. 97-106
    • Dubey, R.S.1    Rani, M.2
  • 76
    • 0001344429 scopus 로고
    • Acid and alkaline phosphatases in rice seedlings growing under salinity stress
    • Dubey, R. S. and K. N. Sharma. 1989. Acid and alkaline phosphatases in rice seedlings growing under salinity stress. Indian J. Plant Physiol. 32:217-223.
    • (1989) Indian J. Plant Physiol , vol.32 , pp. 217-223
    • Dubey, R.S.1    Sharma, K.N.2
  • 77
    • 0000276695 scopus 로고
    • Influence of NaCl salinity on behaviours of protease, aminopeptidase and carboxypeptidase in rice seedling in relation to salt tolerance
    • Dubey, R. S. and M. Rani. 1990. Influence of NaCl salinity on behaviours of protease, aminopeptidase and carboxypeptidase in rice seedling in relation to salt tolerance. Aust. J. Plant Physiol. 17:215-221.
    • (1990) Aust. J. Plant Physiol , vol.17 , pp. 215-221
    • Dubey, R.S.1    Rani, M.2
  • 78
    • 0002445515 scopus 로고
    • Behaviours of phosphatases in germinating rice in relation to salt tolerance
    • Dubey, R. S. and K. N. Sharma. 1990. Behaviours of phosphatases in germinating rice in relation to salt tolerance. Plant Physiol. Biochem. (Paris) 28:17-26.
    • (1990) Plant Physiol. Biochem. (Paris) , vol.28 , pp. 17-26
    • Dubey, R.S.1    Sharma, K.N.2
  • 79
    • 0002755018 scopus 로고
    • Physiological mechanisms of nitrogen absorption, and assimilation in plants under stressful conditions
    • In Handbook of Plant and Crop Physiology, New York: Marcel Dekker Inc
    • Dubey, R. S. and M. Pessarakli. 1995. Physiological mechanisms of nitrogen absorption, and assimilation in plants under stressful conditions. In Handbook of Plant and Crop Physiology, ed. M. Pessarakli, pp. 605-625. New York: Marcel Dekker Inc.
    • (1995) M. Pessarakli , pp. 605-625
    • Dubey, R.S.1    Pessarakli, M.2
  • 80
    • 84862574193 scopus 로고
    • Salinity induced adenosine triphosphatase activity in germinating rice seeds
    • Dubey, R. S., K. N. Sharma, and B. Singh. 1987. Salinity induced adenosine triphosphatase activity in germinating rice seeds. Indian J. Plant Physiol. 30: 256-260.
    • (1987) Indian J. Plant Physiol , vol.30 , pp. 256-260
    • Dubey, R.S.1    Sharma, K.N.2    Singh, B.3
  • 81
    • 84989725925 scopus 로고
    • Cold-acclimation induced changes in freezing tolerance and translatable RNA content in Citrus grandis and Poncirus trifoliata
    • Durham, R. E., G. A. Moore, D. Haskell, and C. L. Guy. 1991. Cold-acclimation induced changes in freezing tolerance and translatable RNA content in Citrus grandis and Poncirus trifoliata. Physiol. Plant. 82:519-522.
    • (1991) Physiol. Plant , vol.82 , pp. 519-522
    • Durham, R.E.1    Moore, G.A.2    Haskell, D.3    Guy, C.L.4
  • 82
    • 34247223134 scopus 로고    scopus 로고
    • Varying patterns of protein synthesis in bread wheat during heat shock
    • Efeoglu, B. and S. Terzioglu. 2007. Varying patterns of protein synthesis in bread wheat during heat shock. Acta Biol. Hung. 58:93-104.
    • (2007) Acta Biol. Hung , vol.58 , pp. 93-104
    • Efeoglu, B.1    Terzioglu, S.2
  • 83
    • 0029763573 scopus 로고    scopus 로고
    • Beta-1,3-glucanase and chitinase as pathogenesis-related proteins in the defense reaction of two Capsicum annuum cultivars infected with cucumber mosaic virus
    • Egea, C., M. D. Alcázar, and M. E. Candela. 1996. Beta-1,3-glucanase and chitinase as pathogenesis-related proteins in the defense reaction of two Capsicum annuum cultivars infected with cucumber mosaic virus. Biol. Plant. 38:437-443.
    • (1996) Biol. Plant , vol.38 , pp. 437-443
    • Egea, C.1    Alcázar, M.D.2    Candela, M.E.3
  • 84
    • 0030944537 scopus 로고    scopus 로고
    • Shoot regeneration and protein synthesis in tomato tissue cultures
    • Elenany, A. E. 1997. Shoot regeneration and protein synthesis in tomato tissue cultures. Biol. Plant. 39:303-308.
    • (1997) Biol. Plant , vol.39 , pp. 303-308
    • Elenany, E.A.1
  • 85
    • 0342683826 scopus 로고    scopus 로고
    • Salt tolerance of soybean cultivars
    • Elsamad, H. M. A. and M. A. K. Shaddad. 1997. Salt tolerance of soybean cultivars. Biol. Plant. 39:263-269.
    • (1997) Biol. Plant , vol.39 , pp. 263-269
    • Elsamad, H.M.A.1    Shaddad, M.A.K.2
  • 86
    • 0005558604 scopus 로고
    • Protein produced during salt-stress in tobacco cell cultures
    • Ericson, M. E. and S. H. Alfinito. 1984. Protein produced during salt-stress in tobacco cell cultures. Plant Physiol. 74:506-509.
    • (1984) Plant Physiol , vol.74 , pp. 506-509
    • Ericson, M.E.1    Alfinito, S.H.2
  • 87
    • 0035200884 scopus 로고    scopus 로고
    • Different mechanisms of four aluminum (Al)-resistant transgenes for Al toxicity in Arabidopsis
    • Ezaki, B., M. Katsuhara, M. Kawamura, and H. Matsumoto. 2001. Different mechanisms of four aluminum (Al)-resistant transgenes for Al toxicity in Arabidopsis. Plant Physiol. 127:918-927.
    • (2001) Plant Physiol , vol.127 , pp. 918-927
    • Ezaki, B.1    Katsuhara, M.2    Kawamura, M.3    Matsumoto, H.4
  • 88
    • 0030945883 scopus 로고    scopus 로고
    • Salinity, oxidative stress and antioxidant responses in shoot cultures of rice
    • Fadzilla, N. M., R. P. Finch, and R. H. Burdon. 1997. Salinity, oxidative stress and antioxidant responses in shoot cultures of rice. J. Exp. Bot. 48:325-331.
    • (1997) J. Exp. Bot , vol.48 , pp. 325-331
    • Fadzilla, N.M.1    Finch, R.P.2    Burdon, R.H.3
  • 89
    • 0036923208 scopus 로고    scopus 로고
    • Cloning of an antifreeze protein gene from carrot and its influence on cold tolerance in transgenic tobacco plants
    • Fan, Y., B. Liu, H. Wang, S. Wang, and J. Wang. 2002. Cloning of an antifreeze protein gene from carrot and its influence on cold tolerance in transgenic tobacco plants. Plant Cell Rep. 21:296-301.
    • (2002) Plant Cell Rep , vol.21 , pp. 296-301
    • Fan, Y.1    Liu, B.2    Wang, H.3    Wang, S.4    Wang, J.5
  • 90
    • 78149375658 scopus 로고    scopus 로고
    • Degradation of RUBISCO and other chloroplast proteins under abiotic stress
    • Feller, U., I. Anders, and K. Demirevska. 2008. Degradation of RUBISCO and other chloroplast proteins under abiotic stress. Gen. Appl. Plant Physiol. 34:5-18.
    • (2008) Gen. Appl. Plant Physiol , vol.34 , pp. 5-18
    • Feller, U.1    Anders, I.2    Demirevska, K.3
  • 91
    • 0005444039 scopus 로고    scopus 로고
    • Effects of enhanced UV-B radiation on protein metabolism of bean leaves
    • Feng, G. N., L. Z. An, H. Y. Feng, and X. L. Wang. 1999. Effects of enhanced UV-B radiation on protein metabolism of bean leaves. Acta Bot. Sin. 41:833-836.
    • (1999) Acta Bot. Sin , vol.41 , pp. 833-836
    • Feng, G.N.1    An, L.Z.2    Feng, H.Y.3    Wang, X.L.4
  • 93
    • 0031105993 scopus 로고    scopus 로고
    • Differential accumulation of two glycine-rich proteins during cold-acclimation alfalfa
    • Ferullo, J. M., L. P. Vezina, J. Rail, S. Laberge, P. Nadeau, and Y. Castonguay. 1997. Differential accumulation of two glycine-rich proteins during cold-acclimation alfalfa. Plant Mol. Biol. 33:625-633.
    • (1997) Plant Mol. Biol , vol.33 , pp. 625-633
    • Ferullo, J.M.1    Vezina, L.P.2    Rail, J.3    Laberge, S.4    Nadeau, P.5    Castonguay, Y.6
  • 94
    • 34347224374 scopus 로고    scopus 로고
    • Understanding abiotic stress tolerance mechanisms: Recent studies on stress response in rice
    • Gao, J. P., D. Y. Chao, and H. X. Lin. 2007. Understanding abiotic stress tolerance mechanisms: Recent studies on stress response in rice. J. Integr. Plant Biol. 49:742-750.
    • (2007) J. Integr. Plant Biol , vol.49 , pp. 742-750
    • Gao, J.P.1    Chao, D.Y.2    Lin, H.X.3
  • 95
    • 34249783484 scopus 로고    scopus 로고
    • Transgenic Indian mustard (Brassica juncea) plants expressing an Arabidopsis phytochelatin synthase (AtPCS1) exhibit enhanced As and Cd tolerance
    • Gasic, K. and S. S. Korban. 2007. Transgenic Indian mustard (Brassica juncea) plants expressing an Arabidopsis phytochelatin synthase (AtPCS1) exhibit enhanced As and Cd tolerance. Plant Mol. Biol. 64:361-369.
    • (2007) Plant Mol. Biol , vol.64 , pp. 361-369
    • Gasic, K.1    Korban, S.S.2
  • 96
    • 0030901402 scopus 로고    scopus 로고
    • Regulation of sucrose and starch metabolism in potato tubers in response to short-term water deficit
    • Geigenberger, P., R. Reimholz, M. Geiger, L. Merlo, V. Canale, and M. Stitt. 1997. Regulation of sucrose and starch metabolism in potato tubers in response to short-term water deficit. Planta 201:502-518.
    • (1997) Planta , vol.201 , pp. 502-518
    • Geigenberger, P.1    Reimholz, R.2    Geiger, M.3    Merlo, L.4    Canale, V.5    Stitt, M.6
  • 98
    • 33845265284 scopus 로고    scopus 로고
    • Antifungal properties of haem peroxidase from Acorus calamus
    • Ghosh, M. 2006. Antifungal properties of haem peroxidase from Acorus calamus. Ann. Bot. 98:1145-1153.
    • (2006) Ann. Bot , vol.98 , pp. 1145-1153
    • Ghosh, M.1
  • 99
    • 33745659672 scopus 로고    scopus 로고
    • High light response of the thylakoid proteome in Arabidopsis wild type and the ascorbate-deficient mutant vtc2-2
    • Giacomelli, L., A. Rudella, and K. J. van Wijk. 2006. High light response of the thylakoid proteome in Arabidopsis wild type and the ascorbate-deficient mutant vtc2-2. A comparative proteomics study. Plant Physiol. 141:685-701.
    • (2006) A comparative proteomics study. Plant Physiol , vol.141 , pp. 685-701
    • Giacomelli, L.1    Rudella, A.2    van Wijk, K.J.3
  • 100
    • 0029187862 scopus 로고
    • Ozone-induced ethylene emission accelerates the loss of ribulose-1,5-bisphosphate carboxylase/oxygenase and nuclear-encoded mRNAs in senescing potato leaves
    • Glick, R. E., C. D. Schlagnhaufer, R. N. Arteca, and E. J. Pell. 1995. Ozone-induced ethylene emission accelerates the loss of ribulose-1,5-bisphosphate carboxylase/oxygenase and nuclear-encoded mRNAs in senescing potato leaves. Plant Physiol. 109:891-898.
    • (1995) Plant Physiol , vol.109 , pp. 891-898
    • Glick, R.E.1    Schlagnhaufer, C.D.2    Arteca, R.N.3    Pell, E.J.4
  • 101
    • 0028878440 scopus 로고
    • Antioxidant defenses against activated oxygen in pea nodules subjected to water stress
    • Gogorcena, Y., I. Iturbeormaetxe, P. R. Escuredo, and M. Becana. 1995. Antioxidant defenses against activated oxygen in pea nodules subjected to water stress. Plant Physiol. 108:753-759.
    • (1995) Plant Physiol , vol.108 , pp. 753-759
    • Gogorcena, Y.1    Iturbeormaetxe, I.2    Escuredo, P.R.3    Becana, M.4
  • 102
    • 0030198895 scopus 로고    scopus 로고
    • Transcripts of a gene encoding a putative cell wallplasma membrane linker protein are specifically cold-induced in Brassica napus
    • Goodwin, W., J. A. Pallas, and G. I. Jenkins. 1996. Transcripts of a gene encoding a putative cell wallplasma membrane linker protein are specifically cold-induced in Brassica napus. Plant Mol. Biol. 31:771-781.
    • (1996) Plant Mol. Biol , vol.31 , pp. 771-781
    • Goodwin, W.1    Pallas, J.A.2    Jenkins, G.I.3
  • 103
    • 33747046042 scopus 로고    scopus 로고
    • The chloroplast lumen and stromal proteomes of Arabidopsis thaliana show differential sensitivity to short and long-term exposure to low temperature
    • Goulas, E., M. Schubert, T. Kieselbach, et al. 2006. The chloroplast lumen and stromal proteomes of Arabidopsis thaliana show differential sensitivity to short and long-term exposure to low temperature. Plant J. 47:720-734.
    • (2006) Plant J , vol.47 , pp. 720-734
    • Goulas, E.1    Schubert, M.2    Kieselbach, T.3
  • 104
    • 85050898545 scopus 로고
    • Effect of water stress on some enzymes and free proline contents in the leaves of two genotypes of rice
    • Goyal, A. and V. K. Kochhar. 1988a. Effect of water stress on some enzymes and free proline contents in the leaves of two genotypes of rice. Indian J. Agric. Biochem. 1:23-27.
    • (1988) Indian J. Agric. Biochem , vol.1 , pp. 23-27
    • Goyal, A.1    Kochhar, V.K.2
  • 105
    • 85050903940 scopus 로고
    • Effect of water stress on the activity of peroxidase and IAA oxidase in the etiolated and green seedlings of Amaranthus and winged bean
    • Goyal, A. and V. K. Kochhar. 1988b. Effect of water stress on the activity of peroxidase and IAA oxidase in the etiolated and green seedlings of Amaranthus and winged bean. Indian J. Agric. Biochem. 1:11-16.
    • (1988) Indian J. Agric. Biochem , vol.1 , pp. 11-16
    • Goyal, A.1    Kochhar, V.K.2
  • 106
    • 0001123955 scopus 로고
    • Mechanisms of salt tolerance in nonhalophytes
    • Greenway, H. and R. Munns. 1980. Mechanisms of salt tolerance in nonhalophytes. Ann. Rev. Plant Physiol. 31:149-1190.
    • (1980) Ann. Rev. Plant Physiol , vol.31 , pp. 149-1190
    • Greenway, H.1    Munns, R.2
  • 107
    • 0028675453 scopus 로고
    • A putative O-methyltransferase from barley is induced by fungal pathogens and UV light
    • Gregersen, P. L., A. B. Christensen, J. Sommerknudsen, and D. B. Collinge. 1994. A putative O-methyltransferase from barley is induced by fungal pathogens and UV light. Plant Mol. Biol. 26:1797-1806.
    • (1994) Plant Mol. Biol , vol.26 , pp. 1797-1806
    • Gregersen, P.L.1    Christensen, A.B.2    Sommerknudsen, J.3    Collinge, D.B.4
  • 108
  • 109
    • 0001068301 scopus 로고
    • Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific ?.-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase)
    • Grill, E., S. Löffler, E. L. Winnacker, and M. H. Zenk. 1989. Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific ?.-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase). Proc. Natl. Acad. Sci. USA 86:6838-6842.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6838-6842
    • Grill, E.1    Löffler, S.2    Winnacker, E.L.3    Zenk, M.H.4
  • 110
    • 61549124398 scopus 로고    scopus 로고
    • Differential response of arsenic stress in two varieties of Brassica juncea L
    • Gupta, M., P. Sharma, N. B. Sarin, and A. K. Sinha. 2009. Differential response of arsenic stress in two varieties of Brassica juncea L. Chemosphere 74:1201-1208.
    • (2009) Chemosphere , vol.74 , pp. 1201-1208
    • Gupta, M.1    Sharma, P.2    Sarin, N.B.3    Sinha, A.K.4
  • 111
    • 29544436438 scopus 로고    scopus 로고
    • Plant cold acclimation: The role of abscisic acid
    • Gusta, L. V., R. Trischuk, and C. J. Weiser. 2005. Plant cold acclimation: The role of abscisic acid. J. Plant Growth Regul. 24:308-318.
    • (2005) J. Plant Growth Regul , vol.24 , pp. 308-318
    • Gusta, L.V.1    Trischuk, R.2    Weiser, C.J.3
  • 112
    • 54849406754 scopus 로고    scopus 로고
    • Rice DREB1B promoter shows distinct stress-specific responses and the overexpression of cDNA in tobacco confers improved abiotic and biotic stress tolerance
    • Gutha, L. R. and A. R. Reddy. 2008. Rice DREB1B promoter shows distinct stress-specific responses and the overexpression of cDNA in tobacco confers improved abiotic and biotic stress tolerance. Plant Mol. Biol. 68:533-555.
    • (2008) Plant Mol. Biol , vol.68 , pp. 533-555
    • Gutha, L.R.1    Reddy, A.R.2
  • 113
    • 0006908826 scopus 로고
    • Characterization of partially purified glutathione reductase from cold-hardened and nonhardened spinach leaf tissue
    • Guy, C. L. and J. V. Carter. 1984. Characterization of partially purified glutathione reductase from cold-hardened and nonhardened spinach leaf tissue. Cryobiology 21:454-464.
    • (1984) Cryobiology , vol.21 , pp. 454-464
    • Guy, C.L.1    Carter, J.V.2
  • 114
    • 0001594812 scopus 로고
    • Induction of freezing tolerance in spinach is associated with the synthesis of cold acclimation induced proteins
    • Guy, C. L. and D. Haskell. 1987. Induction of freezing tolerance in spinach is associated with the synthesis of cold acclimation induced proteins. Plant Physiol. 84:872-878.
    • (1987) Plant Physiol , vol.84 , pp. 872-878
    • Guy, C.L.1    Haskell, D.2
  • 115
    • 38249027470 scopus 로고
    • Changes in freezing tolerance and polypeptide content of spinach and citrus at 5°C
    • Guy, C. L., D. Haskell, and G. Yelenosky. 1988. Changes in freezing tolerance and polypeptide content of spinach and citrus at 5°C. Cryobiology 25:264-271.
    • (1988) Cryobiology , vol.25 , pp. 264-271
    • Guy, C.L.1    Haskell, D.2    Yelenosky, G.3
  • 116
    • 0000118153 scopus 로고
    • Effects of cold-treatment on protein-synthesis and mRNA levels in rice leaves
    • Hahn, M. and V. Walbot. 1989. Effects of cold-treatment on protein-synthesis and mRNA levels in rice leaves. Plant Physiol. 91:930-938.
    • (1989) Plant Physiol , vol.91 , pp. 930-938
    • Hahn, M.1    Walbot, V.2
  • 117
    • 0001133969 scopus 로고
    • The effect of salt on protein synthesis in the halophyte Suaeda maritinta
    • Hall, J. L. and T. J. Flowers. 1973. The effect of salt on protein synthesis in the halophyte Suaeda maritinta. Planta 110:361-368.
    • (1973) Planta , vol.110 , pp. 361-368
    • Hall, J.L.1    Flowers, T.J.2
  • 118
    • 0029825817 scopus 로고    scopus 로고
    • Dehydrin-like proteins in castor bean seeds and seedlings are differentially produced in response to ABA and water-deficit-related stresses
    • Han, B. and A. R. Kermode. 1996. Dehydrin-like proteins in castor bean seeds and seedlings are differentially produced in response to ABA and water-deficit-related stresses. J. Exp. Bot. 47:933-939.
    • (1996) J. Exp. Bot , vol.47 , pp. 933-939
    • Han, B.1    Kermode, A.R.2
  • 120
    • 34248228084 scopus 로고    scopus 로고
    • Proteomic analysis of rice seedlings during cold stress
    • Hashimoto, M. and S. Komatsu. 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
  • 121
    • 21544453594 scopus 로고    scopus 로고
    • Protein changes in response to heat stress in acclimated and nonacclimated creeping bentgrass
    • He, Y. L., X. Z. Liu, and B. R. Huang. 2005. Protein changes in response to heat stress in acclimated and nonacclimated creeping bentgrass. J. Am. Soc. Hort. Sci. 130:521-526.
    • (2005) J. Am. Soc. Hort. Sci , vol.130 , pp. 521-526
    • He, Y.L.1    Liu, X.Z.2    Huang, B.R.3
  • 122
    • 29744450489 scopus 로고    scopus 로고
    • Chloroplast small heat-shock proteins protect photosynthesis during heavy metal stress
    • Heckathorn, S. A., J. K. Mueller, S. LaGuidice, et al. 2004. Chloroplast small heat-shock proteins protect photosynthesis during heavy metal stress. Am. J. Bot. 91:1312-1318.
    • (2004) Am. J. Bot , vol.91 , pp. 1312-1318
    • Heckathorn, S.A.1    Mueller, J.K.2    LaGuidice, S.3
  • 123
    • 0001379284 scopus 로고
    • Induction of heat shock protein messenger RNA in maize mesocotyls by water stress, abscisic acid and wounding
    • Heikkila, J. J., J. E. T. Papp, J. D. Schultz, and J. D. Bewley. 1984. Induction of heat shock protein messenger RNA in maize mesocotyls by water stress, abscisic acid and wounding. Plant Physiol. 76:270-274.
    • (1984) Plant Physiol , vol.76 , pp. 270-274
    • Heikkila, J.J.1    Papp, J.E.T.2    Schultz, J.D.3    Bewley, J.D.4
  • 124
    • 0030592841 scopus 로고    scopus 로고
    • Salicylic acid-independent induction of pathogenesis-related protein transcripts by sugars is dependent on leaf developmental stage
    • Herbers, K., P. Meuwly, J. P. Métraux, and U. Sonnewald. 1996. Salicylic acid-independent induction of pathogenesis-related protein transcripts by sugars is dependent on leaf developmental stage. FEBS Lett. 397:239-244.
    • (1996) FEBS Lett , vol.397 , pp. 239-244
    • Herbers, K.1    Meuwly, P.2    Métraux, J.P.3    Sonnewald, U.4
  • 125
    • 0029278660 scopus 로고
    • Cadmium sensitive, cad1 mutants of Arabidopsis thaliana are phytochelatin deficient
    • Howden, R., P. B. Goldsbrough, C. R. Anderson, and C. S. Cobbett. 1995. Cadmium sensitive, cad1 mutants of Arabidopsis thaliana are phytochelatin deficient. Plant Physiol. 107:1059-1066.
    • (1995) Plant Physiol , vol.107 , pp. 1059-1066
    • Howden, R.1    Goldsbrough, P.B.2    Anderson, C.R.3    Cobbett, C.S.4
  • 126
    • 0000694408 scopus 로고
    • Plant responses to water stress
    • Hsiao, T. C. 1973. Plant responses to water stress. Ann. Rev. Plant Physiol. 24:519-570.
    • (1973) Ann. Rev. Plant Physiol , vol.24 , pp. 519-570
    • Hsiao, C.T.1
  • 127
    • 48249114070 scopus 로고    scopus 로고
    • OsLEA3, a late embryogenesis abundant protein gene from rice, confers tolerance to water deficit and salt stress to transgenic rice
    • Hu, T. Z. 2008. OsLEA3, a late embryogenesis abundant protein gene from rice, confers tolerance to water deficit and salt stress to transgenic rice. Russ. J. Plant Physiol. 55:530-537.
    • (2008) Russ. J. Plant Physiol , vol.55 , pp. 530-537
    • Hu, Z.T.1
  • 128
    • 53549117701 scopus 로고    scopus 로고
    • Identification and characterization of proteins associated with plant tolerance to heat stress
    • Huang, B. R. and C. P. Xu. 2008. Identification and characterization of proteins associated with plant tolerance to heat stress. J. Integr. Plant Biol. 50:1230-1237.
    • (2008) J. Integr. Plant Biol , vol.50 , pp. 1230-1237
    • Huang, B.R.1    Xu, C.P.2
  • 129
    • 24744471645 scopus 로고    scopus 로고
    • Protein synthesis by rice coleoptiles during prolonged anoxia: implications for glycolysis, growth and energy utilization
    • Huang, S., H. Greenway, T. D. Colmer, and A. H. Millar. 2005. Protein synthesis by rice coleoptiles during prolonged anoxia: implications for glycolysis, growth and energy utilization. Ann. Bot. 96:703-715.
    • (2005) Ann. Bot , vol.96 , pp. 703-715
    • Huang, S.1    Greenway, H.2    Colmer, T.D.3    Millar, A.H.4
  • 130
    • 0030050597 scopus 로고    scopus 로고
    • The molecular biology of plant acclimation to low temperature
    • Hughes, M. A. and M. A. Dunn. 1996. The molecular biology of plant acclimation to low temperature. J. Exp. Bot. 47:291-305.
    • (1996) J. Exp. Bot , vol.47 , pp. 291-305
    • Hughes, M.A.1    Dunn, M.A.2
  • 131
    • 0000940866 scopus 로고
    • The effects of salt on the pattern of proteins synthesis in barley roots
    • Hurkman, W. J. and C. K. Tanaka. 1987. The effects of salt on the pattern of proteins synthesis in barley roots. Plant Physiol. 83:517-524.
    • (1987) Plant Physiol , vol.83 , pp. 517-524
    • Hurkman, W.J.1    Tanaka, C.K.2
  • 132
    • 77953310949 scopus 로고    scopus 로고
    • Overexpression of tobacco osmotin gene leads to salt stress tolerance in strawberry (Fragaria x ananassa Duch.) plants
    • Husaini, A. M. and M. Z. Abdin. 2008. Overexpression of tobacco osmotin gene leads to salt stress tolerance in strawberry (Fragaria x ananassa Duch.) plants. Indian J. Biotechnol. 7:465-471.
    • (2008) Indian J. Biotechnol , vol.7 , pp. 465-471
    • Husaini, A.M.1    Abdin, M.Z.2
  • 133
    • 0000844640 scopus 로고
    • Abscisic acid induces anaerobiosis tolerance in corn
    • Hwang, S. Y. and T. T. Van Toai. 1991. Abscisic acid induces anaerobiosis tolerance in corn. Plant Physiol. 97:593-597.
    • (1991) Plant Physiol , vol.97 , pp. 593-597
    • Hwang, S.Y.1    Van Toai, T.T.2
  • 134
    • 0037004330 scopus 로고    scopus 로고
    • Acclimative response to temperature stress in higher plants: approaches of gene engineering for temperature tolerance
    • Iba, K. 2002. Acclimative response to temperature stress in higher plants: approaches of gene engineering for temperature tolerance. Annu. Rev. Plant. Biol. 53:225-245.
    • (2002) Annu. Rev. Plant. Biol , vol.53 , pp. 225-245
    • Iba, K.1
  • 135
    • 0030615287 scopus 로고    scopus 로고
    • Characterization of the gene for delta (1)-pyrroline-5-carboxylate synthetase and correlation between the expression of the gene and salt tolerance in Oryza sativa L
    • Igarashi, Y., Y. Yoshiba, Y. Sanada, K. Wada, K. Yamaguchi-Shinozaki, and K. Shinozaki. 1997. Characterization of the gene for delta (1)-pyrroline-5-carboxylate synthetase and correlation between the expression of the gene and salt tolerance in Oryza sativa L. Plant Mol. Biol. 33:857-865.
    • (1997) Plant Mol. Biol , vol.33 , pp. 857-865
    • Igarashi, Y.1    Yoshiba, Y.2    Sanada, Y.3    Wada, K.4    Yamaguchi-Shinozaki, K.5    Shinozaki, K.6
  • 136
    • 0030527368 scopus 로고    scopus 로고
    • Characterization of two cDNA for novel drought-inducible genes in the highly drought-tolerant cowpea
    • Iuchi, S., K. Yamaguchishinozaki, T. Urao, and K. Shinozaki. 1996a. Characterization of two cDNA for novel drought-inducible genes in the highly drought-tolerant cowpea. J. Plant Res. 109:415-424.
    • (1996) J. Plant Res , vol.109 , pp. 415-424
    • Iuchi, S.1    Yamaguchishinozaki, K.2    Urao, T.3    Shinozaki, K.4
  • 137
    • 0030432181 scopus 로고    scopus 로고
    • Novel drought-inducible genes in the highly drought-tolerant cowpea: Cloning of cDNAs and analysis of the expression of the corresponding genes
    • Iuchi, S., K. Yamaguchishinozaki, T. Urao, T. Terao, and K. Shinozaki. 1996b. Novel drought-inducible genes in the highly drought-tolerant cowpea: Cloning of cDNAs and analysis of the expression of the corresponding genes. Plant Cell Physiol. 37:1073-1082.
    • (1996) Plant Cell Physiol , vol.37 , pp. 1073-1082
    • Iuchi, S.1    Yamaguchishinozaki, K.2    Urao, T.3    Terao, T.4    Shinozaki, K.5
  • 138
    • 0001612521 scopus 로고
    • Water stress enhances expression of an a-amylase gene in barley leaves
    • Jacobsen, J. V., A. D. Hanson, and P. C. Chandler. 1986. Water stress enhances expression of an a-amylase gene in barley leaves. Plant Physiol. 80:350-359.
    • (1986) Plant Physiol , vol.80 , pp. 350-359
    • Jacobsen, J.V.1    Hanson, A.D.2    Chandler, P.C.3
  • 139
  • 141
    • 3242661817 scopus 로고    scopus 로고
    • Carbohydrate metabolism in growing rice seedlings under arsenic toxicity
    • Jha, A. B. and R. S. Dubey. 2004a. Carbohydrate metabolism in growing rice seedlings under arsenic toxicity. J. Plant Physiol. 161:867-872.
    • (2004) J. Plant Physiol , vol.161 , pp. 867-872
    • Jha, A.B.1    Dubey, R.S.2
  • 142
    • 18444389784 scopus 로고    scopus 로고
    • Arsenic exposure alters the activities of key nitrogen assimilatory enzymes in growing rice seedlings
    • Jha, A. B. and R. S. Dubey. 2004b. Arsenic exposure alters the activities of key nitrogen assimilatory enzymes in growing rice seedlings. Plant Growth Regul. 43:259-268.
    • (2004) Plant Growth Regul , vol.43 , pp. 259-268
    • Jha, A.B.1    Dubey, R.S.2
  • 143
    • 0036156543 scopus 로고    scopus 로고
    • Protein alterations in tall fescue in response to drought stress and abscisic acid
    • Jiang, Y. and B. Huang. 2002. Protein alterations in tall fescue in response to drought stress and abscisic acid. Crop Sci. 42:202-207.
    • (2002) Crop Sci , vol.42 , pp. 202-207
    • Jiang, Y.1    Huang, B.2
  • 144
    • 38949168852 scopus 로고    scopus 로고
    • The accumulation of a Kunitz trypsin inhibitor from chickpea (TPI-2) located in cell walls is increased in wounded leaves and elongating epicotyls
    • Jimenez, T., I. Martin, J. Hernandez-Nistal, E. Labrador, and B. Dopico. 2008. The accumulation of a Kunitz trypsin inhibitor from chickpea (TPI-2) located in cell walls is increased in wounded leaves and elongating epicotyls. Physiol. Plant. 132:306-317.
    • (2008) Physiol. Plant , vol.132 , pp. 306-317
    • Jimenez, T.1    Martin, I.2    Hernandez-Nistal, J.3    Labrador, E.4    Dopico, B.5
  • 145
    • 61649087488 scopus 로고    scopus 로고
    • Ice recrystallization inhibition proteins (IRIPs) and freeze tolerance in the cryophilic Antarctic hair grass Deschampsia antarctica E
    • John, U. P., R. M. Polotnianka, K. A. Sivakumaran, et al. 2009. Ice recrystallization inhibition proteins (IRIPs) and freeze tolerance in the cryophilic Antarctic hair grass Deschampsia antarctica E. Desv. Plant Cell Environ. 32:336-348.
    • (2009) Desv. Plant Cell Environ , vol.32 , pp. 336-348
    • John, U.P.1    Polotnianka, R.M.2    Sivakumaran, K.A.3
  • 146
    • 0028002199 scopus 로고
    • The effect of ultraviolet-B radiation on gene expression and pigment composition in etiolated and green pea leaf tissue: UV-B induced changes are gene-specific and dependent upon the development stage
    • Jordan, B. R., P. E. James, A. Strid, and R. G. Anthony. 1994. The effect of ultraviolet-B radiation on gene expression and pigment composition in etiolated and green pea leaf tissue: UV-B induced changes are gene-specific and dependent upon the development stage. Plant Cell Environ. 17:45-54.
    • (1994) Plant Cell Environ , vol.17 , pp. 45-54
    • Jordan, B.R.1    James, P.E.2    Strid, A.3    Anthony, R.G.4
  • 147
    • 0342494768 scopus 로고
    • Effect of soil salinity on nitrogen metabolism in Cajanus cajan L
    • Joshi, S. 1987. Effect of soil salinity on nitrogen metabolism in Cajanus cajan L. Indian J. Plant Physiol. 30:223-225.
    • (1987) Indian J. Plant Physiol , vol.30 , pp. 223-225
    • Joshi, S.1
  • 148
    • 0029110434 scopus 로고
    • Different pathogenesis-related proteins are expressed in sunflower (Helianthus annuus L.) in response to physical, chemical and stress factors
    • Jung, J. L., S. Maurel, B. Fritig, and G. Hahne. 1995. Different pathogenesis-related proteins are expressed in sunflower (Helianthus annuus L.) in response to physical, chemical and stress factors. J. Plant Physiol. 145:153-160.
    • (1995) J. Plant Physiol , vol.145 , pp. 153-160
    • Jung, J.L.1    Maurel, S.2    Fritig, B.3    Hahne, G.4
  • 149
    • 84905549538 scopus 로고
    • Effect of waters deficit on photosynthetic capacity
    • Kaiser, W. M. 1987. Effect of waters deficit on photosynthetic capacity. Physiol. Plant. 71:142-149.
    • (1987) Physiol. Plant , vol.71 , pp. 142-149
    • Kaiser, M.W.1
  • 150
    • 0000155640 scopus 로고
    • Heat shock proteins in tobacco cell suspension during growth cycle
    • Kanabus, J., C. S. Pikaard, and J. H. Cherry. 1984. Heat shock proteins in tobacco cell suspension during growth cycle. Plant Physiol. 75:639-644.
    • (1984) Plant Physiol , vol.75 , pp. 639-644
    • Kanabus, J.1    Pikaard, C.S.2    Cherry, J.H.3
  • 151
    • 34248583440 scopus 로고    scopus 로고
    • Soluble proteins induced by low temperature treatment in the leaves of spring and winter wheat cultivars
    • Karimzadeh, G., G. R. Sharifi-Sirchi, M. Jalali-Javaran, H. Dehghani, and D. Francis. 2006. Soluble proteins induced by low temperature treatment in the leaves of spring and winter wheat cultivars. Pak. J. Bot. 38:1015-1026.
    • (2006) Pak. J. Bot , vol.38 , pp. 1015-1026
    • Karimzadeh, G.1    Sharifi-Sirchi, G.R.2    Jalali-Javaran, M.3    Dehghani, H.4    Francis, D.5
  • 152
    • 0032993342 scopus 로고    scopus 로고
    • Improving plant drought, salt and freezing tolerance by gene transfer of a single stress-inducible transcription factor
    • Kasuga, M., Q. Liu, S. Miura, K. Yamaguchi-Shinozaki, and K. Shinozaki. 1999. Improving plant drought, salt and freezing tolerance by gene transfer of a single stress-inducible transcription factor. Nat. Biotechnol. 17:287-291.
    • (1999) Nat. Biotechnol , vol.17 , pp. 287-291
    • Kasuga, M.1    Liu, Q.2    Miura, S.3    Yamaguchi-Shinozaki, K.4    Shinozaki, K.5
  • 153
    • 1842817622 scopus 로고    scopus 로고
    • A combination of the Arabidopsis DREB1A gene and stress-inducible rd29A promoter improved drought- and low-temperature stress tolerance in tobacco by gene transfer
    • Kasuga, M., S. Miura, K. Shinozaki, and K. Yamaguchi-Shinozaki. 2004. A combination of the Arabidopsis DREB1A gene and stress-inducible rd29A promoter improved drought- and low-temperature stress tolerance in tobacco by gene transfer. Plant Cell Physiol. 45:346-350.
    • (2004) Plant Cell Physiol , vol.45 , pp. 346-350
    • Kasuga, M.1    Miura, S.2    Shinozaki, K.3    Yamaguchi-Shinozaki, K.4
  • 154
    • 2842520415 scopus 로고
    • Influence of NaCl salinity on behaviour of nitrate reductase and nitrite reductase in rice seedlings differing in salt tolerance
    • Katiyar, S. and R. S. Dubey. 1992. Influence of NaCl salinity on behaviour of nitrate reductase and nitrite reductase in rice seedlings differing in salt tolerance. J. Agron. Crop Sci. 169:289-297.
    • (1992) J. Agron. Crop Sci , vol.169 , pp. 289-297
    • Katiyar, S.1    Dubey, R.S.2
  • 155
    • 0033819338 scopus 로고    scopus 로고
    • Anaerobically induced proteins in rice seedlings
    • Kato-Noguchi, H. 2000. Anaerobically induced proteins in rice seedlings. Plant Prod. Sci. 3:225-228.
    • (2000) Plant Prod. Sci , vol.3 , pp. 225-228
    • Kato-Noguchi, H.1
  • 156
    • 23744474021 scopus 로고    scopus 로고
    • Signal transduction pathways under abiotic stresses in plants
    • Kaur, N. and A. K. Gupta. 2005. Signal transduction pathways under abiotic stresses in plants. Curr. Sci. 88:1771-1780.
    • (2005) Curr. Sci , vol.88 , pp. 1771-1780
    • Kaur, N.1    Gupta, A.K.2
  • 157
    • 0009204175 scopus 로고
    • Alterations in protein synthesis in vivo in chilling sensitive mung bean hypocotyls caused by chilling stress
    • Kawata, T. and S. Yoshida. 1988. Alterations in protein synthesis in vivo in chilling sensitive mung bean hypocotyls caused by chilling stress. Plant Cell Physiol. 29:1423-1427.
    • (1988) Plant Cell Physiol , vol.29 , pp. 1423-1427
    • Kawata, T.1    Yoshida, S.2
  • 158
    • 58149277123 scopus 로고    scopus 로고
    • Differential regulation of proteins and phosphoproteins in rice under drought stress
    • Ke, Y., G. Han, H. He, and J. Li. 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
  • 159
    • 0001324001 scopus 로고
    • Concomitant changes in high temperature tolerance and heat-shock proteins in desert succulents
    • Kee, S. C. and P. S. Nobel. 1986. Concomitant changes in high temperature tolerance and heat-shock proteins in desert succulents. Plant Physiol. 80:596-598.
    • (1986) Plant Physiol , vol.80 , pp. 596-598
    • Kee, S.C.1    Nobel, P.S.2
  • 160
    • 77950517468 scopus 로고    scopus 로고
    • Antioxidant responses of two barley varieties to saline stress
    • Khosravinejad, F., R. Heydari, and T. Farboodnia. 2008. Antioxidant responses of two barley varieties to saline stress. Res. J. Biol. Sci. 3:486-490.
    • (2008) Res. J. Biol. Sci , vol.3 , pp. 486-490
    • Khosravinejad, F.1    Heydari, R.2    Farboodnia, T.3
  • 161
    • 61449088387 scopus 로고    scopus 로고
    • Genetic approaches towards overcoming water deficit in plants- special emphasis on LEAs
    • Khurana, P., D. Vishnudasan, and A. K. Chhibbar. 2008. Genetic approaches towards overcoming water deficit in plants- special emphasis on LEAs. Physiol. Mol. Biol. Plants 14:277-298.
    • (2008) Physiol. Mol. Biol. Plants , vol.14 , pp. 277-298
    • Khurana, P.1    Vishnudasan, D.2    Chhibbar, A.K.3
  • 162
    • 60549093722 scopus 로고    scopus 로고
    • Class II chitinase accumulated in the bark tissue involves with the cold hardiness of shoot stems in highbush blueberry (Vaccinium corymbosum L.)
    • Kikuchi, T. and K. Masuda. 2009. Class II chitinase accumulated in the bark tissue involves with the cold hardiness of shoot stems in highbush blueberry (Vaccinium corymbosum L.). Sci. Hort. 120:230-236.
    • (2009) Sci. Hort , vol.120 , pp. 230-236
    • Kikuchi, T.1    Masuda, K.2
  • 163
    • 33947408660 scopus 로고    scopus 로고
    • Chloroplast-targeted BrMT1 (Brassica rapa type-1 metallothionein) enhances resistance to cadmium and ROS in transgenic Arabidopsis plants
    • Kim, S. H., H. S. Lee, W. Y. Song, K. S. Choi, and Y. Hur. 2007. Chloroplast-targeted BrMT1 (Brassica rapa type-1 metallothionein) enhances resistance to cadmium and ROS in transgenic Arabidopsis plants. J. Plant Biol. 50:1-7.
    • (2007) J. Plant Biol , vol.50 , pp. 1-7
    • Kim, S.H.1    Lee, H.S.2    Song, W.Y.3    Choi, K.S.4    Hur, Y.5
  • 164
    • 63049130681 scopus 로고    scopus 로고
    • Secretome analysis of differentially induced proteins in rice suspension-cultured cells triggered by rice blast fungus and elicitor
    • Kim, S. T., Y. H. Kang, Y. Wang, et al. 2009. Secretome analysis of differentially induced proteins in rice suspension-cultured cells triggered by rice blast fungus and elicitor. Proteomics 9:1302-1313.
    • (2009) Proteomics , vol.9 , pp. 1302-1313
    • Kim, S.T.1    Kang, Y.H.2    Wang, Y.3
  • 165
    • 0029853913 scopus 로고    scopus 로고
    • Alteration in protein accumulation, gene expression and ascorbateglutathione pathway in tomato (Lycopersicon esculentum) under paraquat and ozone stress
    • Kirtikara, K. and D. Talbot. 1996. Alteration in protein accumulation, gene expression and ascorbateglutathione pathway in tomato (Lycopersicon esculentum) under paraquat and ozone stress. J. Plant Physiol. 148:752-760.
    • (1996) J. Plant Physiol , vol.148 , pp. 752-760
    • Kirtikara, K.1    Talbot, D.2
  • 166
    • 84951657939 scopus 로고
    • Intracellular distribution of heat shock proteins in pigeon pea (Cajanus cajan)
    • Kishore R. and K. C. Upadhyaya. 1994. Intracellular distribution of heat shock proteins in pigeon pea (Cajanus cajan). J. Plant Biochem. Biotechnol. 3:43-46.
    • (1994) J. Plant Biochem. Biotechnol , vol.3 , pp. 43-46
    • Kishore, R.1    Upadhyaya, K.C.2
  • 167
    • 0028835509 scopus 로고
    • Overexpression of 1-pyrroline- 5-carboxylate synthetase increases proline production and confers osmotolerance in transgenic plants
    • Kishor, P. B. K., Z. Hong, G. H. Miao, C. A. Hu, and D. P. S Verma. 1995. Overexpression of 1-pyrroline- 5-carboxylate synthetase increases proline production and confers osmotolerance in transgenic plants. Plant Physiol. 108:1387-1394.
    • (1995) Plant Physiol , vol.108 , pp. 1387-1394
    • Kishor, P.B.K.1    Hong, Z.2    Miao, G.H.3    Hu, C.A.4    Verma, D.P.S.5
  • 168
    • 0029141360 scopus 로고
    • Synthesis of phytochelatins and homo-phytochelatins in Pisum sativum L
    • Klapheck, S., S. Schlunz, and L. Bergmann. 1995. Synthesis of phytochelatins and homo-phytochelatins in Pisum sativum L. Plant Physiol. 107:515-521.
    • (1995) Plant Physiol , vol.107 , pp. 515-521
    • Klapheck, S.1    Schlunz, S.2    Bergmann, L.3
  • 169
    • 80053509906 scopus 로고    scopus 로고
    • Stress proteins and ultrastructural characteristics of leaf cells of plants with different types of ecological strategies
    • Kosakivska, I., D. Klymchuk, V. Negretzky, D. Bluma, and A. Ustinova. 2008. Stress proteins and ultrastructural characteristics of leaf cells of plants with different types of ecological strategies. Gen. Appl. Plant Physiol. 34:405-418.
    • (2008) Gen. Appl. Plant Physiol , vol.34 , pp. 405-418
    • Kosakivska, I.1    Klymchuk, D.2    Negretzky, V.3    Bluma, D.4    Ustinova, A.5
  • 170
    • 0000420760 scopus 로고
    • Induction of phenylalanine ammonia-lyase and 4-coumarate:CoA ligase mRNAs in cultured plant cells by UV light or fungal elicitor
    • Kuhn, D. N., J. Chappell, A. Boudet, and K. Hahlbrock. 1984. Induction of phenylalanine ammonia-lyase and 4-coumarate:CoA ligase mRNAs in cultured plant cells by UV light or fungal elicitor. Proc. Natl. Acad. Sci. USA 81:1102-1106.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1102-1106
    • Kuhn, D.N.1    Chappell, J.2    Boudet, A.3    Hahlbrock, K.4
  • 171
    • 0008078834 scopus 로고
    • Changes in contents of chlorophyll, proteins and lipids in whole chloroplast membrane fractions at different leaf water potentials in drought resistant and sensitive genotype of wheat
    • Kulshrestha, S., D. P. Mishra, and R. K. Gupta. 1987. Changes in contents of chlorophyll, proteins and lipids in whole chloroplast membrane fractions at different leaf water potentials in drought resistant and sensitive genotype of wheat. Photosynthetica 21:65-70.
    • (1987) Photosynthetica , vol.21 , pp. 65-70
    • Kulshrestha, S.1    Mishra, D.P.2    Gupta, R.K.3
  • 172
    • 0345661645 scopus 로고
    • Germination and metabolism in susceptible and tolerant mung bean genotypes under moisture stress
    • Kumar, P. K. and R. A. Singh. 1991. Germination and metabolism in susceptible and tolerant mung bean genotypes under moisture stress. Indian J. Plant Physiol. 34:267-270.
    • (1991) Indian J. Plant Physiol , vol.34 , pp. 267-270
    • Kumar, P.K.1    Singh, R.A.2
  • 173
    • 50949104270 scopus 로고    scopus 로고
    • Differential regulation of rice mitogen activated protein kinase kinase (MKK) by abiotic stress
    • Kumar, K., K. P. Rao, P. Sharma, and A. K. Sinha. 2008. Differential regulation of rice mitogen activated protein kinase kinase (MKK) by abiotic stress. Plant Physiol. Biochem. 46:891-897.
    • (2008) Plant Physiol. Biochem , vol.46 , pp. 891-897
    • Kumar, K.1    Rao, K.P.2    Sharma, P.3    Sinha, A.K.4
  • 174
    • 0030175013 scopus 로고    scopus 로고
    • Differential induction of pathogenesis-related proteins in tomato by Alternaria solani and the association of a basic chitinase isozyme with resistance
    • Lawrence, C. B., M. H. A. J. Joosten, and S. Tuzun. 1996. Differential induction of pathogenesis-related proteins in tomato by Alternaria solani and the association of a basic chitinase isozyme with resistance. Physiol. Mol. Plant Pathol. 48:361-377.
    • (1996) Physiol. Mol. Plant Pathol , vol.48 , pp. 361-377
    • Lawrence, C.B.1    Joosten, M.H.A.J.2    Tuzun, S.3
  • 175
    • 34948843692 scopus 로고    scopus 로고
    • A proteomic approach in analyzing heat-responsive proteins in rice leaves
    • Lee, D. G., N. Ahsan, S. H. Lee, et al. 2007. A proteomic approach in analyzing heat-responsive proteins in rice leaves. Proteomics 7:3369-3383.
    • (2007) Proteomics , vol.7 , pp. 3369-3383
    • Lee, D.G.1    Ahsan, N.2    Lee, S.H.3
  • 176
    • 56949099175 scopus 로고    scopus 로고
    • Chilling stress-induced proteomic changes in rice roots
    • Lee, D. G., N. Ahsan, S. H. Lee, et al. 2009. Chilling stress-induced proteomic changes in rice roots. J. Plant Physiol. 166:1-11.
    • (2009) J. Plant Physiol , vol.166 , pp. 1-11
    • Lee, D.G.1    Ahsan, N.2    Lee, S.H.3
  • 177
    • 0028002821 scopus 로고
    • A low molecular mass heat-shock protein is localized to higher plant mitochondria
    • Lenne, C. and R. Douce. 1994. A low molecular mass heat-shock protein is localized to higher plant mitochondria. Plant Physiol. 105:1255-1261.
    • (1994) Plant Physiol , vol.105 , pp. 1255-1261
    • Lenne, C.1    Douce, R.2
  • 179
    • 0033728462 scopus 로고    scopus 로고
    • Identification of a stress-induced protein in stem exudates of soybean seedlings root-infected with Fusarium solani f
    • Li, S. X., G. L. Hartman, B. S. Lee, and J. W. Widholm. 2000. Identification of a stress-induced protein in stem exudates of soybean seedlings root-infected with Fusarium solani f. sp glycines. Plant Physiol. Biochem. 38:803-809.
    • (2000) sp glycines. Plant Physiol. Biochem , vol.38 , pp. 803-809
    • Li, S.X.1    Hartman, G.L.2    Lee, B.S.3    Widholm, J.W.4
  • 180
    • 0031032289 scopus 로고    scopus 로고
    • Salt sensitivity and the activities of the H+-ATPases in cotton seedlings
    • Lin, H., S. S. Salus, and K. S. Schumaker. 1997. Salt sensitivity and the activities of the H+-ATPases in cotton seedlings. Crop Sci. 37:190-197.
    • (1997) Crop Sci , vol.37 , pp. 190-197
    • Lin, H.1    Salus, S.S.2    Schumaker, K.S.3
  • 182
    • 0032144961 scopus 로고    scopus 로고
    • Two transcription factors, DREB1 and DREB2, with an EREBP/ AP2 DNA binding domain separate two cellular signal transduction pathways in drought- and low temperature- responsive gene expression, respectively, in Arabidopsis
    • Liu, Q., M. Kasuga, Y. Sakuma, et al. 1998. Two transcription factors, DREB1 and DREB2, with an EREBP/ AP2 DNA binding domain separate two cellular signal transduction pathways in drought- and low temperature- responsive gene expression, respectively, in Arabidopsis. Plant Cell 10:1391-1406.
    • (1998) Plant Cell , vol.10 , pp. 1391-1406
    • Liu, Q.1    Kasuga, M.2    Sakuma, Y.3
  • 183
    • 0000843346 scopus 로고    scopus 로고
    • Classification and nomenclature of plant metallothionein-like proteins based on their cysteine arrangement patterns
    • Liu, J. Y., T. Lu, and N. M. Zhao. 2000. Classification and nomenclature of plant metallothionein-like proteins based on their cysteine arrangement patterns. Acta Bot. Sin. 42:649-652.
    • (2000) Acta Bot. Sin , vol.42 , pp. 649-652
    • Liu, J.Y.1    Lu, T.2    Zhao, N.M.3
  • 185
    • 85028966288 scopus 로고
    • Studies on the oxidative enzymes of rice in relation to soil moisture stress
    • Lodh, S. B., D. P. Bhattacharya, G. Ramkrishnaya, and S. P. Deb. 1977. Studies on the oxidative enzymes of rice in relation to soil moisture stress. Indian Agric. 21:181-186.
    • (1977) Indian Agric , vol.21 , pp. 181-186
    • Lodh, S.B.1    Bhattacharya, D.P.2    Ramkrishnaya, G.3    Deb, S.P.4
  • 186
    • 1942533519 scopus 로고    scopus 로고
    • Protein cryoprotective activity of a cytosolic small heat shock protein that accumulates constitutively in chestnut stems and is up-regulated by low and high temperatures
    • Lopez-Matas, M. A., P. Nuñez, A. Soto, et al. 2004. Protein cryoprotective activity of a cytosolic small heat shock protein that accumulates constitutively in chestnut stems and is up-regulated by low and high temperatures. Plant Physiol. 134:1708-1717.
    • (2004) Plant Physiol , vol.134 , pp. 1708-1717
    • Lopez-Matas, M.A.1    Nuñez, P.2    Soto, A.3
  • 187
    • 33847767179 scopus 로고    scopus 로고
    • Nickel toxicity inhibits ribonuclease and protease activities in rice seedlings: Protective effects of proline
    • Maheshwari, R. and R. S. Dubey. 2007. Nickel toxicity inhibits ribonuclease and protease activities in rice seedlings: Protective effects of proline. Plant Growth Regul. 51:231-243.
    • (2007) Plant Growth Regul , vol.51 , pp. 231-243
    • Maheshwari, R.1    Dubey, R.S.2
  • 188
    • 54049128847 scopus 로고    scopus 로고
    • Inhibition of ribonuclease and protease activities in germinating rice seeds exposed to nickel
    • Maheshwari, R. and R. S. Dubey. 2008. Inhibition of ribonuclease and protease activities in germinating rice seeds exposed to nickel. Acta Physiol. Plant. 30:863-872.
    • (2008) Acta Physiol. Plant , vol.30 , pp. 863-872
    • Maheshwari, R.1    Dubey, R.S.2
  • 189
    • 70349988990 scopus 로고    scopus 로고
    • Nickel-induced oxidative stress and the role of antioxidative defense in rice seedlings
    • Maheshwari, R. and R. S. Dubey. 2009. Nickel-induced oxidative stress and the role of antioxidative defense in rice seedlings. Plant Growth Regul. 59:37-49.
    • (2009) Plant Growth Regul , vol.59 , pp. 37-49
    • Maheshwari, R.1    Dubey, R.S.2
  • 190
    • 77954079080 scopus 로고    scopus 로고
    • Protein profiles in response to salt stress in seeds of Brassica napus
    • Mahmoodzadeh, H. 2009. Protein profiles in response to salt stress in seeds of Brassica napus. Res. J. Environ. Sci. 3:225-231.
    • (2009) Res. J. Environ. Sci , vol.3 , pp. 225-231
    • Mahmoodzadeh, H.1
  • 192
    • 75449104118 scopus 로고
    • Changes in the activity of some enzymes and free proline in rice (Oryza sativa L.) during water stress
    • Mali, P. C., B. B. Nanda, D. P. Bhattacharya, and S. B. Lodh. 1980. Changes in the activity of some enzymes and free proline in rice (Oryza sativa L.) during water stress. Plant Biochem. J 7:126-132.
    • (1980) Plant Biochem. J , vol.7 , pp. 126-132
    • Mali, P.C.1    Nanda, B.B.2    Bhattacharya, D.P.3    Lodh, S.B.4
  • 193
    • 0000279337 scopus 로고
    • Cytoplasmic distribution of heat-shock proteins in soybean
    • Mansfield, M. A. and J. L. Key. 1988. Cytoplasmic distribution of heat-shock proteins in soybean. Plant Physiol. 86:1240-1246.
    • (1988) Plant Physiol , vol.86 , pp. 1240-1246
    • Mansfield, M.A.1    Key, J.L.2
  • 194
    • 0029158529 scopus 로고
    • Role of abscisic acid in drought-induced freezing tolerance, cold acclimation and accumulation of LTI78 and RAB18 proteins in Arabidopsis
    • Mantyla, E., V. Lang, and E. T. Palva. 1995. Role of abscisic acid in drought-induced freezing tolerance, cold acclimation and accumulation of LTI78 and RAB18 proteins in Arabidopsis. Plant Physiol. 107:141-148.
    • (1995) Plant Physiol , vol.107 , pp. 141-148
    • Mantyla, E.1    Lang, V.2    Palva, E.T.3
  • 195
    • 0031055944 scopus 로고    scopus 로고
    • Photosynthetic responses to temperature of phosphoenolpyruvate carboxykinase type C-4 species differing in cold sensitivity
    • Matsuba, K., N. Imaizumi, S. Kaneko, M. Samejima, and R. Ohsugi. 1997. Photosynthetic responses to temperature of phosphoenolpyruvate carboxykinase type C-4 species differing in cold sensitivity. Plant Cell Environ. 20:268-274.
    • (1997) Plant Cell Environ , vol.20 , pp. 268-274
    • Matsuba, K.1    Imaizumi, N.2    Kaneko, S.3    Samejima, M.4    Ohsugi, R.5
  • 197
    • 85032069334 scopus 로고
    • Differential protein metabolism and gene expression in tomato fruit during wounding stress
    • Mehta, R. A., B. L. Parsons, A. M. Mehta, H. L. Nakhasi, and A. K. Mattoo. 1991. Differential protein metabolism and gene expression in tomato fruit during wounding stress. Plant Cell Physiol. 32:1057-1065.
    • (1991) Plant Cell Physiol , vol.32 , pp. 1057-1065
    • Mehta, R.A.1    Parsons, B.L.2    Mehta, A.M.3    Nakhasi, H.L.4    Mattoo, A.K.5
  • 198
    • 0001757414 scopus 로고
    • Changes in protein synthesis in rapeseed (Brassica napus) seedlings during a low temperature treatment
    • Meza-Basso, L., M. Alberdi, M. Raynal, M. L. Ferrero-Cadinanos, and M. Delseny. 1986. Changes in protein synthesis in rapeseed (Brassica napus) seedlings during a low temperature treatment. Plant Physiol. 82:733-738.
    • (1986) Plant Physiol , vol.82 , pp. 733-738
    • Meza-Basso, L.1    Alberdi, M.2    Raynal, M.3    Ferrero-Cadinanos, M.L.4    Delseny, M.5
  • 199
    • 33747880087 scopus 로고    scopus 로고
    • Inhibition of ribonuclease and protease activities in arsenic exposed rice seedlings: Role of proline as enzyme protectant
    • Mishra, S. and R. S. Dubey. 2006. Inhibition of ribonuclease and protease activities in arsenic exposed rice seedlings: Role of proline as enzyme protectant. J. Plant Physiol. 163:927-936.
    • (2006) J. Plant Physiol , vol.163 , pp. 927-936
    • Mishra, S.1    Dubey, R.S.2
  • 200
    • 42449155907 scopus 로고    scopus 로고
    • Effect of aluminium on metabolism of starch and sugars in growing rice seedlings
    • Mishra, P. and R. S. Dubey. 2008. Effect of aluminium on metabolism of starch and sugars in growing rice seedlings. Acta Physiol. Plant. 30:265-275.
    • (2008) Acta Physiol. Plant , vol.30 , pp. 265-275
    • Mishra, P.1    Dubey, R.S.2
  • 201
    • 46249091899 scopus 로고    scopus 로고
    • Changes in phosphate content and phosphatase activities in rice seedlings exposed to arsenite
    • Mishra, S. and R. S. Dubey. 2008. Changes in phosphate content and phosphatase activities in rice seedlings exposed to arsenite. Braz. J. Plant Physiol. 20:19-28.
    • (2008) Braz. J. Plant Physiol , vol.20 , pp. 19-28
    • Mishra, S.1    Dubey, R.S.2
  • 202
    • 84987316019 scopus 로고
    • Effect of NaCl salinity on RNA level as well as activity and molecular forms of ribonuclease in germinating rice seeds differing in salt tolerance
    • Mittal, R. and R. S. Dubey. 1990. Effect of NaCl salinity on RNA level as well as activity and molecular forms of ribonuclease in germinating rice seeds differing in salt tolerance. Indian J. Plant Physiol. 33:32-39.
    • (1990) Indian J. Plant Physiol , vol.33 , pp. 32-39
    • Mittal, R.1    Dubey, R.S.2
  • 203
    • 0002790950 scopus 로고
    • Behaviour of peroxidases in rice: Changes in enzyme activity and isoforms in relation to salt tolerance
    • Mittal, R. and R. S. Dubey. 1991. Behaviour of peroxidases in rice: Changes in enzyme activity and isoforms in relation to salt tolerance. Plant Physiol. Biochem. (Paris) 29:31-40.
    • (1991) Plant Physiol. Biochem. (Paris) , vol.29 , pp. 31-40
    • Mittal, R.1    Dubey, R.S.2
  • 204
    • 0028852861 scopus 로고
    • Influence of sodium chloride salinity on polyphenol oxidase, indole 3-acetic acid oxidase and catalase activities in rice seedlings differing in salt tolerance
    • Mittal, R. and R. S. Dubey. 1995. Influence of sodium chloride salinity on polyphenol oxidase, indole 3-acetic acid oxidase and catalase activities in rice seedlings differing in salt tolerance. Trop. Sci. 35:141-149.
    • (1995) Trop. Sci , vol.35 , pp. 141-149
    • Mittal, R.1    Dubey, R.S.2
  • 205
    • 0002715188 scopus 로고    scopus 로고
    • Characteristics of pathogenesis-related proteins induced in Phaseolus vulgaris cv
    • Mohamed, F. and O. P. Sehgal. 1997. Characteristics of pathogenesis-related proteins induced in Phaseolus vulgaris cv. pinto following viral infection. J. Phytopathol. 145:49-58.
    • (1997) pinto following viral infection. J. Phytopathol , vol.145 , pp. 49-58
    • Mohamed, F.1    Sehgal, O.P.2
  • 206
    • 0001017259 scopus 로고
    • Abscisic acid-regulated gene expression in relation to freezing tolerance in alfalfa
    • Mohapatra, S. S., R. J. Poole, and R. S. Dhindsa. 1988. Abscisic acid-regulated gene expression in relation to freezing tolerance in alfalfa. Plant Physiol. 87:468-473.
    • (1988) Plant Physiol , vol.87 , pp. 468-473
    • Mohapatra, S.S.1    Poole, R.J.2    Dhindsa, R.S.3
  • 207
    • 33845906597 scopus 로고    scopus 로고
    • Expression of chloroplast protein synthesis elongation factor, EF-Tu, in two lines of maize with contrasting tolerance to heat stress during early stages of plant development
    • Momcilovic, I. and Z. Ristic. 2007. Expression of chloroplast protein synthesis elongation factor, EF-Tu, in two lines of maize with contrasting tolerance to heat stress during early stages of plant development. J. Plant Physiol. 164:90-99.
    • (2007) J. Plant Physiol , vol.164 , pp. 90-99
    • Momcilovic, I.1    Ristic, Z.2
  • 208
    • 0030927111 scopus 로고    scopus 로고
    • A group 3 lea cDNA of rice, responsive to abscisic acid, but not to jasmonic acid, shows variety-specific differences in salt stress response
    • Moons, A., A. Dekeyser, and M. Vanmontagu. 1997. A group 3 lea cDNA of rice, responsive to abscisic acid, but not to jasmonic acid, shows variety-specific differences in salt stress response. Gene 191:197-204.
    • (1997) Gene , vol.191 , pp. 197-204
    • Moons, A.1    Dekeyser, A.2    Vanmontagu, M.3
  • 209
    • 0024066710 scopus 로고
    • Abscisic acid and water-stress induce the expression of a novel rice gene
    • Mundy, J. and N. H. Chua. 1988. Abscisic acid and water-stress induce the expression of a novel rice gene. EMBO J. 7:2279-2286.
    • (1988) EMBO J , vol.7 , pp. 2279-2286
    • Mundy, J.1    Chua, N.H.2
  • 210
    • 0036179253 scopus 로고    scopus 로고
    • Comparative physiology of salt and water stress
    • Munns, R. 2002. Comparative physiology of salt and water stress. Plant Cell Environ. 25:239-250.
    • (2002) Plant Cell Environ , vol.25 , pp. 239-250
    • Munns, R.1
  • 211
    • 0348162536 scopus 로고
    • Influence of salt stress on Biochemical processes in chickpea, Cicer arietinum L
    • Murumkar, C. V. and P. D. Chavan. 1986. Influence of salt stress on Biochemical processes in chickpea, Cicer arietinum L. Plant Soil 96:439-443.
    • (1986) Plant Soil , vol.96 , pp. 439-443
    • Murumkar, C.V.1    Chavan, P.D.2
  • 212
    • 0028409345 scopus 로고
    • Identification of dehydrin-like proteins responsive to chilling in floral buds of blueberry (Vaccinium, Section Cyanococcus)
    • Muthalif, M. M. and L. J. Rowland. 1994. Identification of dehydrin-like proteins responsive to chilling in floral buds of blueberry (Vaccinium, Section Cyanococcus). Plant Physiol. 104:1439-1447.
    • (1994) Plant Physiol , vol.104 , pp. 1439-1447
    • Muthalif, M.M.1    Rowland, L.J.2
  • 213
    • 0029240297 scopus 로고
    • Drought, heat and salt stress induce the expression of a citrus homologue of an atypical late-embryogenesis lea5 gene
    • Naot, D., G. Ben-Hayyim, Y. Eshdat, and D. Holland. 1995. Drought, heat and salt stress induce the expression of a citrus homologue of an atypical late-embryogenesis lea5 gene. Plant Mol. Biol. 27:619-622.
    • (1995) Plant Mol. Biol , vol.27 , pp. 619-622
    • Naot, D.1    Ben-Hayyim, G.2    Eshdat, Y.3    Holland, D.4
  • 214
    • 0029139497 scopus 로고
    • Salt induced synthesis of new proteins in the roots of rice varieties
    • Naqvi, S. M. S., V. C. Ozalp, H. A. Oktem, and M. Yucel. 1995. Salt induced synthesis of new proteins in the roots of rice varieties. J. Plant Nutr. 18:1121-1137.
    • (1995) J. Plant Nutr , vol.18 , pp. 1121-1137
    • Naqvi, S.M.S.1    Ozalp, V.C.2    Oktem, H.A.3    Yucel, M.4
  • 216
    • 0028042928 scopus 로고
    • Heat-shock proteins induce heavy-metal tolerance in higher plants
    • Neumann, D., O. Lichtenberger, D. Günther, K. Tschiersch, and L. Nover. 1994. Heat-shock proteins induce heavy-metal tolerance in higher plants. Planta 194:360-367.
    • (1994) Planta , vol.194 , pp. 360-367
    • Neumann, D.1    Lichtenberger, O.2    Günther, D.3    Tschiersch, K.4    Nover, L.5
  • 217
    • 33745645618 scopus 로고    scopus 로고
    • Effect of NaCl on biomass, protein and proline contents and antioxidant enzymes in seedlings and calli of two Trigonella species
    • Niknam, V., N. Razavi, H. Ebrahimzadeh, and B. Sharifizadeh. 2006. Effect of NaCl on biomass, protein and proline contents and antioxidant enzymes in seedlings and calli of two Trigonella species. Biol. Plant. 50:591-596.
    • (2006) Biol. Plant , vol.50 , pp. 591-596
    • Niknam, V.1    Razavi, N.2    Ebrahimzadeh, H.3    Sharifizadeh, B.4
  • 218
    • 36148933350 scopus 로고    scopus 로고
    • Proteomics reveals new salt responsive proteins associated with rice plasma membrane
    • Nohzadeh, M. S., R. M. Habibi, M. Heidari, and G. H. Salekdeh. 2007. Proteomics reveals new salt responsive proteins associated with rice plasma membrane. Biosci. Biotechnol. Biochem. 71:2144-2154.
    • (2007) Biosci. Biotechnol. Biochem , vol.71 , pp. 2144-2154
    • Nohzadeh, M.S.1    Habibi, R.M.2    Heidari, M.3    Salekdeh, G.H.4
  • 219
    • 34547584433 scopus 로고    scopus 로고
    • Expression of barley HvCBF4 enhances tolerance to abiotic stress in transgenic rice
    • Oh, S. J., C. W. Kwon, D. W. Choi, S. I. Song, and J. K. Kim. 2007. Expression of barley HvCBF4 enhances tolerance to abiotic stress in transgenic rice. Plant Biotechnol. J. 5:646-656.
    • (2007) Plant Biotechnol. J , vol.5 , pp. 646-656
    • Oh, S.J.1    Kwon, C.W.2    Choi, D.W.3    Song, S.I.4    Kim, J.K.5
  • 220
    • 0000924706 scopus 로고
    • Synthesis of stress proteins in tobacco leaves
    • Ohashi, Y. and M. Matsuoka. 1985. Synthesis of stress proteins in tobacco leaves. Plant Cell Physiol. 26:473-480.
    • (1985) Plant Cell Physiol , vol.26 , pp. 473-480
    • Ohashi, Y.1    Matsuoka, M.2
  • 222
    • 0028831818 scopus 로고
    • Seasonal changes in photosystem II organization and pigment composition in Pinus sylvestris
    • Ottander, C., D. Campbell, and G. Oquist. 1995. Seasonal changes in photosystem II organization and pigment composition in Pinus sylvestris. Planta 197:176-183.
    • (1995) Planta , vol.197 , pp. 176-183
    • Ottander, C.1    Campbell, D.2    Oquist, G.3
  • 223
    • 53549126960 scopus 로고    scopus 로고
    • Changes in carbohydrates, ABA and bark proteins during seasonal cold acclimation and deacclimation in Hydrangea species differing in cold hardiness
    • Pagter, M., C. R. Jensen, K. K. Petersen, F. L. Liu, and R. Arora. 2008. Changes in carbohydrates, ABA and bark proteins during seasonal cold acclimation and deacclimation in Hydrangea species differing in cold hardiness. Physiol. Plant. 134:473-485.
    • (2008) Physiol. Plant , vol.134 , pp. 473-485
    • Pagter, M.1    Jensen, C.R.2    Petersen, K.K.3    Liu, F.L.4    Arora, R.5
  • 224
    • 64749101905 scopus 로고    scopus 로고
    • Enhanced fungal resistance in Arabidopsis expressing wild rice PR-3 (OgChitIVa) encoding chitinase class IV
    • Pak, J. H., E. S. Chung, S. H. Shin, et al. 2009. Enhanced fungal resistance in Arabidopsis expressing wild rice PR-3 (OgChitIVa) encoding chitinase class IV. Plant. Biotechnol. Rep. 3:147-155.
    • (2009) Plant. Biotechnol. Rep , vol.3 , pp. 147-155
    • Pak, J.H.1    Chung, E.S.2    Shin, S.H.3
  • 225
    • 58749110117 scopus 로고    scopus 로고
    • Amounts and subcellular localization of stilbene synthase in response of grape berries to UV irradiation
    • Pan, Q. H., L. Wang, and J. M. Li. 2009. Amounts and subcellular localization of stilbene synthase in response of grape berries to UV irradiation. Plant Sci. 176:360-366.
    • (2009) Plant Sci , vol.176 , pp. 360-366
    • Pan, Q.H.1    Wang, L.2    Li, J.M.3
  • 226
    • 0031591585 scopus 로고    scopus 로고
    • Distribution patterns of HSP 90 protein in rice
    • Pareek, A., S. L. Singla, A. K. Kush, and A. Grover. 1997. Distribution patterns of HSP 90 protein in rice. Plant Sci. 125:221-230.
    • (1997) Plant Sci , vol.125 , pp. 221-230
    • Pareek, A.1    Singla, S.L.2    Kush, A.K.3    Grover, A.4
  • 227
    • 50249126058 scopus 로고    scopus 로고
    • Differential responses of the enzymes involved in proline biosynthesis and degradation in drought tolerant and sensitive cotton genotypes during drought stress and recovery
    • Parida, A. K., V. S. Dagaonkar, M. S. Phalak, and L. P. Aurangabadkar. 2008. Differential responses of the enzymes involved in proline biosynthesis and degradation in drought tolerant and sensitive cotton genotypes during drought stress and recovery. Acta Physiol. Plant. 30:619-627.
    • (2008) Acta Physiol. Plant , vol.30 , pp. 619-627
    • Parida, A.K.1    Dagaonkar, V.S.2    Phalak, M.S.3    Aurangabadkar, L.P.4
  • 228
    • 63949084782 scopus 로고    scopus 로고
    • Expression of apoplastically secreted tobacco osmotin in cotton confers drought tolerance
    • Parkhi, V., V. Kumar, G. S. Kumar, L. M. Campbell, N. K. Singh, and K. S. Rathore. 2009. Expression of apoplastically secreted tobacco osmotin in cotton confers drought tolerance. Mol. Breed. 23:625-639.
    • (2009) Mol. Breed , vol.23 , pp. 625-639
    • Parkhi, V.1    Kumar, V.2    Kumar, G.S.3    Campbell, L.M.4    Singh, N.K.5    Rathore, K.S.6
  • 229
    • 0030939473 scopus 로고    scopus 로고
    • Differential accumulation of water stressrelated proteins, sucrose synthase and soluble sugars in Populus species that differ in their water stress response
    • Pelah, D., W. Wang, A. Altman, O. Shoseyov, and D. Bartels. 1997. Differential accumulation of water stressrelated proteins, sucrose synthase and soluble sugars in Populus species that differ in their water stress response. Physiol. Plant. 99:153-159.
    • (1997) Physiol. Plant , vol.99 , pp. 153-159
    • Pelah, D.1    Wang, W.2    Altman, A.3    Shoseyov, O.4    Bartels, D.5
  • 230
    • 55649121213 scopus 로고    scopus 로고
    • RcDhn5, a cold acclimation-responsive dehydrin from Rhododendron catawbiense rescues enzyme activity from dehydration effects in vitro and enhances freezing tolerance in RcDhn5-overexpressing Arabidopsis plants
    • Peng, Y. H., J. L. Reyes, H. Wei, et al. 2008. RcDhn5, a cold acclimation-responsive dehydrin from Rhododendron catawbiense rescues enzyme activity from dehydration effects in vitro and enhances freezing tolerance in RcDhn5-overexpressing Arabidopsis plants. Physiol. Plant. 134:583-597.
    • (2008) Physiol. Plant , vol.134 , pp. 583-597
    • Peng, Y.H.1    Reyes, J.L.2    Wei, H.3
  • 231
    • 0030068633 scopus 로고    scopus 로고
    • Effects of water stress on plant growth and root proteins in three cultivars of rice (Oryza sativa) with different levels of drought tolerance
    • Perezmolphebalch, E., M. Gidekel, M. Seguranieto, L. Herreraestrella, and N. Ochoaalejo. 1996. Effects of water stress on plant growth and root proteins in three cultivars of rice (Oryza sativa) with different levels of drought tolerance. Physiol. Plant. 96:284-290.
    • (1996) Physiol. Plant , vol.96 , pp. 284-290
    • Perezmolphebalch, E.1    Gidekel, M.2    Seguranieto, M.3    Herreraestrella, L.4    Ochoaalejo, N.5
  • 232
    • 0029793025 scopus 로고    scopus 로고
    • Changes in antioxidant enzymes and organic solutes associated with adaptation of citrus cells to salt stress
    • Piqueras, A., J. L. Hernandez, E. Olmos, F. Sevilla, and E. Hellin. 1996. Changes in antioxidant enzymes and organic solutes associated with adaptation of citrus cells to salt stress. Plant Cell Tissue Organ Cult. 45:53-60.
    • (1996) Plant Cell Tissue Organ Cult , vol.45 , pp. 53-60
    • Piqueras, A.1    Hernandez, J.L.2    Olmos, E.3    Sevilla, F.4    Hellin, E.5
  • 233
    • 0001190256 scopus 로고
    • Analysis of heat-shock protein pattern during somatic embryogenesis of carrots
    • Pitto, L., F. Loschiavo, G. Giuliano, and M. Terzi. 1983. Analysis of heat-shock protein pattern during somatic embryogenesis of carrots. Plant Mol. Biol. 2:231-237.
    • (1983) Plant Mol. Biol , vol.2 , pp. 231-237
    • Pitto, L.1    Loschiavo, F.2    Giuliano, G.3    Terzi, M.4
  • 234
    • 29444458426 scopus 로고    scopus 로고
    • Overexpression of Arabidopsis phytochelatin synthase in tobacco plants enhances Cd2+ stop tolerance and accumulation but not translocation to the shoot
    • Pomponi, M., V. Censi, V. Di Girolamo, et al. 2006. Overexpression of Arabidopsis phytochelatin synthase in tobacco plants enhances Cd2+ stop tolerance and accumulation but not translocation to the shoot. Planta 223:180-190.
    • (2006) Planta , vol.223 , pp. 180-190
    • Pomponi, M.1    Censi, V.2    Di Girolamo, V.3
  • 236
    • 0001003626 scopus 로고    scopus 로고
    • Effects of low temperature, high salinity and exogenous ABA on the synthesis of two chloroplastic drought-induced proteins in Solanum tuberosum
    • Pruvot, G., J. Massimino, G. Peltier, and P. Rey. 1996. Effects of low temperature, high salinity and exogenous ABA on the synthesis of two chloroplastic drought-induced proteins in Solanum tuberosum. Physiol. Plant. 97:123-131.
    • (1996) Physiol. Plant , vol.97 , pp. 123-131
    • Pruvot, G.1    Massimino, J.2    Peltier, G.3    Rey, P.4
  • 237
    • 0029186911 scopus 로고
    • The stress-stimulated 16 kDa polypeptide from lupin roots has properties of cytosolic Cu-Zn-superoxide dismutase
    • Przymusinski, R., R. Rucinska, and E. A. Gwozdz. 1995. The stress-stimulated 16 kDa polypeptide from lupin roots has properties of cytosolic Cu-Zn-superoxide dismutase. Environ. Exp. Bot. 35:485-495.
    • (1995) Environ. Exp. Bot , vol.35 , pp. 485-495
    • Przymusinski, R.1    Rucinska, R.2    Gwozdz, E.A.3
  • 238
    • 16544387856 scopus 로고    scopus 로고
    • Overexpression of multiple dehydrin genes enhances tolerance to freezing stress in Arabidopsis
    • Puhakainen, T., M. W. Hess, P. Makela, J. Svensson, P. Heino, and E. T. Palva. 2004. Overexpression of multiple dehydrin genes enhances tolerance to freezing stress in Arabidopsis. Plant Mol. Biol. 54:743-753.
    • (2004) Plant Mol. Biol , vol.54 , pp. 743-753
    • Puhakainen, T.1    Hess, M.W.2    Makela, P.3    Svensson, J.4    Heino, P.5    Palva, E.T.6
  • 239
    • 34548757949 scopus 로고    scopus 로고
    • Proteomics-based dissection of stress-responsive pathways in plants
    • Qureshi, M. I., S. Qadir, and L. Zolla. 2007. Proteomics-based dissection of stress-responsive pathways in plants. J. Plant Physiol. 164:1239-1260.
    • (2007) J. Plant Physiol , vol.164 , pp. 1239-1260
    • Qureshi, M.I.1    Qadir, S.2    Zolla, L.3
  • 240
    • 30744475861 scopus 로고
    • Protein and amino acid relationship during water stress in relation to drought resistance
    • Rai, V. K., G. Singh, P. K. Thakur, and S. Banyal. 1983. Protein and amino acid relationship during water stress in relation to drought resistance. Plant Physiol. Biochem. 10(s):161-167.
    • (1983) Plant Physiol. Biochem , vol.10 , pp. 161-167
    • Rai, V.K.1    Singh, G.2    Thakur, P.K.3    Banyal, S.4
  • 241
    • 0344175953 scopus 로고
    • Protein synthesis in a maize callus exposed to NaCl and mannitol
    • Ramagopal, S. 1986. Protein synthesis in a maize callus exposed to NaCl and mannitol. Plant Cell Rep. 5:430-434.
    • (1986) Plant Cell Rep , vol.5 , pp. 430-434
    • Ramagopal, S.1
  • 242
    • 4344699141 scopus 로고
    • Advances in understanding the molecular biology of drought, and salinity tolerance in plantsthe first decade
    • In Advances in Plant Biotechnology and Biochemistry, Kanpur, India: Ind. Soc. Agril. Biochem
    • Ramagopal, S. 1993. Advances in understanding the molecular biology of drought, and salinity tolerance in plantsthe first decade. In Advances in Plant Biotechnology and Biochemistry, eds. M. L. Lodha, S. L. Mehta, S. Ramagopal, and G. P. Srivastava, pp. 39-48. Kanpur, India: Ind. Soc. Agril. Biochem.
    • (1993) M. L. Lodha, S. L. Mehta, S. Ramagopal, and G. P. Srivastava , pp. 39-48
    • Ramagopal, S.1
  • 244
    • 0030023240 scopus 로고    scopus 로고
    • Ultraviolet-B and ozone-induced biochemical changes in antioxidant enzymes of Arabidopsis thaliana
    • Rao, M. V., G. Paliyath, and D. P. Ormrod. 1996. Ultraviolet-B and ozone-induced biochemical changes in antioxidant enzymes of Arabidopsis thaliana. Plant Physiol. 110:125-136.
    • (1996) Plant Physiol , vol.110 , pp. 125-136
    • Rao, M.V.1    Paliyath, G.2    Ormrod, D.P.3
  • 245
    • 0030238286 scopus 로고    scopus 로고
    • Fructose 2,6-bisphosphate-modulated photosynthesis in sorghum leaves grown under low water regimes
    • Reddy, A. R. 1996. Fructose 2,6-bisphosphate-modulated photosynthesis in sorghum leaves grown under low water regimes. Phytochemistry 43:319-322.
    • (1996) Phytochemistry , vol.43 , pp. 319-322
    • Reddy, R.A.1
  • 246
    • 0000770984 scopus 로고
    • Anaerobic stress induces the transcription and translation of sucrose synthase in rice
    • Ricard, B., J. Rivoal, A. Spiteri, and A. Pradet. 1991. Anaerobic stress induces the transcription and translation of sucrose synthase in rice. Plant Physiol. 95:669-674.
    • (1991) Plant Physiol , vol.95 , pp. 669-674
    • Ricard, B.1    Rivoal, J.2    Spiteri, A.3    Pradet, A.4
  • 247
    • 0000382475 scopus 로고    scopus 로고
    • Protein changes in responses to progressive water deficit in maize
    • Riccardi, F., P. Gazeau, D. V. Vienne, and M. Zivy. 1998. Protein changes in responses to progressive water deficit in maize. Plant Physiol. 117:1253-1263.
    • (1998) Plant Physiol , vol.117 , pp. 1253-1263
    • Riccardi, F.1    Gazeau, P.2    Vienne, D.V.3    Zivy, M.4
  • 248
    • 0028535436 scopus 로고
    • A dehydrin cognate protein from pea (Pisum sativum L.) with an atypical pattern of expression
    • Robertson, M. and P. M. Chandler. 1994. A dehydrin cognate protein from pea (Pisum sativum L.) with an atypical pattern of expression. Plant Mol. Biol. 26:805-816.
    • (1994) Plant Mol. Biol , vol.26 , pp. 805-816
    • Robertson, M.1    Chandler, P.M.2
  • 249
    • 0028191675 scopus 로고
    • Comparison of dehydrin gene expression and freezing tolerance in Bromus inermis and Secale cereale grown in controlled environments, hydroponics and the field
    • Robertson, A. J., A. Weninger, R. W. Wilen, P. Fu, and L. V. Gusta. 1994. Comparison of dehydrin gene expression and freezing tolerance in Bromus inermis and Secale cereale grown in controlled environments, hydroponics and the field. Plant Physiol. 106:1213-1216.
    • (1994) Plant Physiol , vol.106 , pp. 1213-1216
    • Robertson, A.J.1    Weninger, A.2    Wilen, R.W.3    Fu, P.4    Gusta, L.V.5
  • 251
    • 33845653187 scopus 로고    scopus 로고
    • Proteome changes in Arabidopsis thaliana roots upon exposure to Cd2+
    • Roth, U., E. von Roepenack-Lahaye, and S. Clemens. 2006. Proteome changes in Arabidopsis thaliana roots upon exposure to Cd2+. J. Exp. Bot. 57:4003-4013.
    • (2006) J. Exp. Bot , vol.57 , pp. 4003-4013
    • Roth, U.1    von Roepenack-Lahaye, E.2    Clemens, S.3
  • 252
    • 0028816006 scopus 로고
    • The induction of 1,3-ß-glucanases and other enzymes in groundnut leaves infected with Cercospora arachidicola
    • Roulin, S. and A. J. Buchala. 1995. The induction of 1,3-ß-glucanases and other enzymes in groundnut leaves infected with Cercospora arachidicola. Physiol Mol. Plant. Pathol. 46:471-489.
    • (1995) Physiol Mol. Plant. Pathol , vol.46 , pp. 471-489
    • Roulin, S.1    Buchala, A.J.2
  • 254
    • 0001329109 scopus 로고
    • Proteolytic enzymes and their inhibitors in plants
    • Ryan, C. A., 1973. Proteolytic enzymes and their inhibitors in plants. Ann. Rev. Plant Physiol. 24:173-196.
    • (1973) Ann. Rev. Plant Physiol , vol.24 , pp. 173-196
    • Ryan, C.A.1
  • 255
    • 0018869288 scopus 로고
    • The anaerobic proteins of maize
    • Sachs, M. M., M. Freeling, and R. Okimoto. 1980. The anaerobic proteins of maize. Cell 20:761-767.
    • (1980) Cell , vol.20 , pp. 761-767
    • Sachs, M.M.1    Freeling, M.2    Okimoto, R.3
  • 256
    • 0030039181 scopus 로고    scopus 로고
    • Anaerobic gene expression and flooding tolerance in maize
    • Sachs, M. M., C. C. Subbaiah, and I. N. Saab. 1996. Anaerobic gene expression and flooding tolerance in maize. J. Exp. Bot. 47:1-15.
    • (1996) J. Exp. Bot , vol.47 , pp. 1-15
    • Sachs, M.M.1    Subbaiah, C.C.2    Saab, I.N.3
  • 257
    • 0030443246 scopus 로고    scopus 로고
    • Characterization of alfalfa (Medicago sativa L.) following in vitro selection for salt tolerance
    • Safarnejad, A., H. A. Collin, K. D. Bruce, and T. McNeilly. 1996. Characterization of alfalfa (Medicago sativa L.) following in vitro selection for salt tolerance. Euphytica 92:55-61.
    • (1996) Euphytica , vol.92 , pp. 55-61
    • Safarnejad, A.1    Collin, H.A.2    Bruce, K.D.3    McNeilly, T.4
  • 259
    • 0001413068 scopus 로고
    • Developmental and pathogen induced activation of the Arabidopsis acidic chitinase promoter
    • Samac, D. A. and D. M. Shah. 1991. Developmental and pathogen induced activation of the Arabidopsis acidic chitinase promoter. Plant Cell 3:1063-1072.
    • (1991) Plant Cell , vol.3 , pp. 1063-1072
    • Samac, D.A.1    Shah, D.M.2
  • 261
    • 38349137099 scopus 로고    scopus 로고
    • Enhanced tolerance to drought stress in transgenic rice plants overexpressing a small heat-shock protein, sHSP17.7
    • Sato, Y. and S. Yokoya. 2008. Enhanced tolerance to drought stress in transgenic rice plants overexpressing a small heat-shock protein, sHSP17.7. Plant Cell Rep. 27:329-334.
    • (2008) Plant Cell Rep , vol.27 , pp. 329-334
    • Sato, Y.1    Yokoya, S.2
  • 262
    • 0030220455 scopus 로고    scopus 로고
    • Molecular cloning of a tomato leaf cDNA encoding an aspartic protease, a systemic wound response protein
    • Schaller, A. and C. A. Ryan. 1996. Molecular cloning of a tomato leaf cDNA encoding an aspartic protease, a systemic wound response protein. Plant Mol. Biol. 31:1073-1077.
    • (1996) Plant Mol. Biol , vol.31 , pp. 1073-1077
    • Schaller, A.1    Ryan, C.A.2
  • 263
    • 0009631577 scopus 로고    scopus 로고
    • Molecular responses to heat stress
    • In Molecular Responses to Cold, Drought, Heat, and Salt Stress in Higher Plants, Austin, TX: R. G. Landes Co
    • Schoffl, F., R. Prandl, and A. Reindl. 1999. Molecular responses to heat stress. In Molecular Responses to Cold, Drought, Heat, and Salt Stress in Higher Plants, eds. K. Shinozaki and K. Yamaguchi-Shinozaki, pp. 81-98. Austin, TX: R. G. Landes Co.
    • (1999) K. Shinozaki and K. Yamaguchi-Shinozaki , pp. 81-98
    • Schoffl, F.1    Prandl, R.2    Reindl, A.3
  • 264
    • 0035193592 scopus 로고    scopus 로고
    • Cadmium-induced changes in antioxidative systems, hydrogen peroxide content, and differentiation in Scots pine roots
    • Schützendübel, A., P. Schwanz, T. Teichmann, et al. 2001. Cadmium-induced changes in antioxidative systems, hydrogen peroxide content, and differentiation in Scots pine roots. Plant Physiol. 127:887-898.
    • (2001) Plant Physiol , vol.127 , pp. 887-898
    • Schützendübel, A.1    Schwanz, P.2    Teichmann, T.3
  • 265
    • 0013451209 scopus 로고
    • Polyribosome content in young and aged wheat leaves subjected to drought
    • Scott, N. S., R. Munns, and E. W. R. Barlow. 1979. Polyribosome content in young and aged wheat leaves subjected to drought. J. Exp. Bot. 30:905-911.
    • (1979) J. Exp. Bot , vol.30 , pp. 905-911
    • Scott, N.S.1    Munns, R.2    Barlow, E.W.R.3
  • 267
    • 63949083095 scopus 로고    scopus 로고
    • Effect of cadmium and salinity stresses on growth and antioxidant enzyme activities of wheat (Triticum aestivum L.)
    • Shafi, M., J. Bakht, M. J. Hassan, M. Raziuddin, and G. Zhang. 2009. Effect of cadmium and salinity stresses on growth and antioxidant enzyme activities of wheat (Triticum aestivum L.). Bull. Environ. Contam. Toxicol. 82:772-776.
    • (2009) Bull. Environ. Contam. Toxicol , vol.82 , pp. 772-776
    • Shafi, M.1    Bakht, J.2    Hassan, M.J.3    Raziuddin, M.4    Zhang, G.5
  • 268
    • 84982344889 scopus 로고
    • Ribonucleic acid and protein metabolism in sugar beet during drought
    • Shah, C. B. and R. S. Loomis. 1965. Ribonucleic acid and protein metabolism in sugar beet during drought. Physiol. Plant. 18:240-254.
    • (1965) Physiol. Plant , vol.18 , pp. 240-254
    • Shah, C.B.1    Loomis, R.S.2
  • 269
    • 0141511636 scopus 로고
    • Cadmium induced changes on germination, RNA level and ribonuclease activity in rice seeds
    • Shah, K. and R. S. Dubey. 1995. Cadmium induced changes on germination, RNA level and ribonuclease activity in rice seeds. Plant Physiol. Biochem. (New Delhi) 22:101-107.
    • (1995) Plant Physiol. Biochem. (New Delhi) , vol.22 , pp. 101-107
    • Shah, K.1    Dubey, R.S.2
  • 270
    • 0028871031 scopus 로고
    • Effect of cadmium on RNA level as well as activity and molecular forms of ribonuclease in growing rice seedlings
    • Shah, K. and R. S. Dubey. 1995. Effect of cadmium on RNA level as well as activity and molecular forms of ribonuclease in growing rice seedlings. Plant Physiol. Biochem. (Paris) 33:577-584.
    • (1995) Plant Physiol. Biochem. (Paris) , vol.33 , pp. 577-584
    • Shah, K.1    Dubey, R.S.2
  • 271
    • 0031751377 scopus 로고    scopus 로고
    • A 18 kDa Cd inducible protein complex: Its isolation and characterization from rice (Oryza sativa L.) seedlings
    • Shah, K. and R. S. Dubey. 1998. A 18 kDa Cd inducible protein complex: Its isolation and characterization from rice (Oryza sativa L.) seedlings. J. Plant Physiol. 152:448-454.
    • (1998) J. Plant Physiol , vol.152 , pp. 448-454
    • Shah, K.1    Dubey, R.S.2
  • 272
    • 0031823437 scopus 로고    scopus 로고
    • Cadmium elevates level of protein, amino acids and alters the activity of proteolytic enzymes in germinating rice seeds
    • Shah, K. and R. S. Dubey. 1998. Cadmium elevates level of protein, amino acids and alters the activity of proteolytic enzymes in germinating rice seeds. Acta Physiol. Plant. 20:189-196.
    • (1998) Acta Physiol. Plant , vol.20 , pp. 189-196
    • Shah, K.1    Dubey, R.S.2
  • 273
    • 0031874428 scopus 로고    scopus 로고
    • Cadmium suppresses phosphate level and inhibits the activity of phosphatases in growing rice seedlings
    • Shah, K. and R. S. Dubey. 1998. Cadmium suppresses phosphate level and inhibits the activity of phosphatases in growing rice seedlings. J. Agron. Crop Sci. 180:223-231.
    • (1998) J. Agron. Crop Sci , vol.180 , pp. 223-231
    • Shah, K.1    Dubey, R.S.2
  • 274
    • 0035661857 scopus 로고    scopus 로고
    • Effect of cadmium on lipid peroxidation, superoxide anion generation and activities of antioxidant enzymes in growing rice seedlings
    • Shah, K., R. G. Kumar, S. Verma, and R. S. Dubey. 2001. Effect of cadmium on lipid peroxidation, superoxide anion generation and activities of antioxidant enzymes in growing rice seedlings. Plant Sci. 161:1135-1144.
    • (2001) Plant Sci , vol.161 , pp. 1135-1144
    • Shah, K.1    Kumar, R.G.2    Verma, S.3    Dubey, R.S.4
  • 275
    • 0031010548 scopus 로고    scopus 로고
    • The effects of ozone on antioxidant responses in plants
    • Sharma, Y. K. and K. R. Davis. 1997. The effects of ozone on antioxidant responses in plants. Free Rad. Biol. Med. 23:480-488.
    • (1997) Free Rad. Biol. Med , vol.23 , pp. 480-488
    • Sharma, Y.K.1    Davis, K.R.2
  • 276
    • 3142741917 scopus 로고    scopus 로고
    • Ascorbate peroxidase from rice seedlings: Properties of enzyme isoforms, effects of stresses and protective roles of osmolytes
    • Sharma, P. and R. S. Dubey. 2004. Ascorbate peroxidase from rice seedlings: Properties of enzyme isoforms, effects of stresses and protective roles of osmolytes. Plant Sci. 167:541-550.
    • (2004) Plant Sci , vol.167 , pp. 541-550
    • Sharma, P.1    Dubey, R.S.2
  • 277
    • 26444507306 scopus 로고    scopus 로고
    • Drought induces oxidative stress and enhances the activities of antioxidant enzymes in growing rice seedlings
    • Sharma, P. and R. S. Dubey. 2005a. Drought induces oxidative stress and enhances the activities of antioxidant enzymes in growing rice seedlings. Plant Growth Regul. 46:209-221.
    • (2005) Plant Growth Regul , vol.46 , pp. 209-221
    • Sharma, P.1    Dubey, R.S.2
  • 278
    • 23044445844 scopus 로고    scopus 로고
    • Modulation of nitrate reductase activity in rice seedlings under aluminium toxicity and water stress: Role of osmolytes as enzyme protectant
    • Sharma, P. and R. S. Dubey. 2005b. Modulation of nitrate reductase activity in rice seedlings under aluminium toxicity and water stress: Role of osmolytes as enzyme protectant. J. Plant Physiol. 162:854-864.
    • (2005) J. Plant Physiol , vol.162 , pp. 854-864
    • Sharma, P.1    Dubey, R.S.2
  • 279
    • 35248894326 scopus 로고    scopus 로고
    • Involvement of oxidative stress and role of antioxidative defense system in growing rice seedlings exposed to toxic concentrations of aluminum
    • Sharma, P. and R. S. Dubey. 2007. Involvement of oxidative stress and role of antioxidative defense system in growing rice seedlings exposed to toxic concentrations of aluminum. Plant Cell Rep. 26:2027-2038.
    • (2007) Plant Cell Rep , vol.26 , pp. 2027-2038
    • Sharma, P.1    Dubey, R.S.2
  • 280
    • 0037388680 scopus 로고    scopus 로고
    • Proteomics approach to identify wound-response related proteins from rice leaf sheath
    • Shen, S., Y. Jing, and T. Kuang. 2003. Proteomics approach to identify wound-response related proteins from rice leaf sheath. Proteomics 3:527-535.
    • (2003) Proteomics , vol.3 , pp. 527-535
    • Shen, S.1    Jing, Y.2    Kuang, T.3
  • 281
    • 66949175552 scopus 로고    scopus 로고
    • Gene expression changes in response to drought stress in Citrullus colocynthis
    • Si, Y., C. Zhang, S. Meng, and F. Dane. 2009. Gene expression changes in response to drought stress in Citrullus colocynthis. Plant Cell Rep. 28:997-1009.
    • (2009) Plant Cell Rep , vol.28 , pp. 997-1009
    • Si, Y.1    Zhang, C.2    Meng, S.3    Dane, F.4
  • 283
    • 0001575537 scopus 로고
    • Proteins associated with adaptation of cultured tobacco cells to NaCl
    • Singh, N. K., A. K. Handa, P. M. Hasegawa, and R. A. Bressan. 1985. Proteins associated with adaptation of cultured tobacco cells to NaCl. Plant Physiol. 79:126-137.
    • (1985) Plant Physiol , vol.79 , pp. 126-137
    • Singh, N.K.1    Handa, A.K.2    Hasegawa, P.M.3    Bressan, R.A.4
  • 284
    • 0001500217 scopus 로고
    • Characterization of osmotin, a thaumatin like protein associated with osmotic adaptation in plant cells
    • Singh, N. K., C. A. Bracker, P. M. Hasegawa, et al. 1987. Characterization of osmotin, a thaumatin like protein associated with osmotic adaptation in plant cells. Plant Physiol. 85:529-536.
    • (1987) Plant Physiol , vol.85 , pp. 529-536
    • Singh, N.K.1    Bracker, C.A.2    Hasegawa, P.M.3
  • 285
    • 84969792040 scopus 로고
    • Molecular cloning of the osmotin and regulation of its expression by ABA and adaptation to low water potential
    • Singh, N. K., D. E. Nelson, D. Kuhn, P. M. Hasegawa, and R. A. Bressan. 1989. Molecular cloning of the osmotin and regulation of its expression by ABA and adaptation to low water potential. Plant Physiol. 90:1096-1101.
    • (1989) Plant Physiol , vol.90 , pp. 1096-1101
    • Singh, N.K.1    Nelson, D.E.2    Kuhn, D.3    Hasegawa, P.M.4    Bressan, R.A.5
  • 286
    • 0028045339 scopus 로고
    • Detection and quantification of a rapidly accumulating and predominant kDa heat stress polypeptide in rice
    • Singla, S. L. and A. Grover. 1994. Detection and quantification of a rapidly accumulating and predominant kDa heat stress polypeptide in rice. Plant Sci. 97:23-30.
    • (1994) Plant Sci , vol.97 , pp. 23-30
    • Singla, S.L.1    Grover, A.2
  • 287
    • 9444288166 scopus 로고    scopus 로고
    • Lathyrus dehydrin-A drought inducible cDNA clone: Isolation and characterization
    • Sinha, K. M., A. Sachdev, R. P. Johari, and S. L. Mehta. 1996. Lathyrus dehydrin-A drought inducible cDNA clone: Isolation and characterization. J. Plant Biochem. Biotechnol. 5:97-101.
    • (1996) J. Plant Biochem. Biotechnol , vol.5 , pp. 97-101
    • Sinha, K.M.1    Sachdev, A.2    Johari, R.P.3    Mehta, S.L.4
  • 288
    • 0002427619 scopus 로고
    • In The physiology and Biochemistry of Drought Resistance in Plants, eds. L. G. Paleg and D. Aspinall, pp. 145-168, Sydney, Australia: Academic Press
    • Sinha, S. K. and D. J. Nicholas. 1981. Nitrate reductase. In The physiology and Biochemistry of Drought Resistance in Plants, eds. L. G. Paleg and D. Aspinall, pp. 145-168, Sydney, Australia: Academic Press.
    • (1981) Nitrate reductase
    • Sinha, S.K.1    Nicholas, D.J.2
  • 289
    • 33749431711 scopus 로고    scopus 로고
    • Proteins induced by cadmium in soybean cells
    • Sobkowiak, R. and J. Deckert. 2006. Proteins induced by cadmium in soybean cells. J. Plant Physiol. 163:1203-1206.
    • (2006) J. Plant Physiol , vol.163 , pp. 1203-1206
    • Sobkowiak, R.1    Deckert, J.2
  • 290
    • 0030210460 scopus 로고    scopus 로고
    • The Arabidopsis homeobox gene ATHB-7 is induced by water deficit and by abscisic acid
    • Soderman, E., J. Mattsson, and P. Engstrom. 1996. The Arabidopsis homeobox gene ATHB-7 is induced by water deficit and by abscisic acid. Plant J. 10:375-381.
    • (1996) Plant J , vol.10 , pp. 375-381
    • Soderman, E.1    Mattsson, J.2    Engstrom, P.3
  • 291
    • 61349171868 scopus 로고    scopus 로고
    • Overexpression of AtHsp90.2, AtHsp90.5 and AtHsp90.7 in Arabidopsis thaliana enhances plant sensitivity to salt and drought stresses
    • Song, H. M., R. M. Zhao, P. X. Fan, X. C. Wang, X. Y. Chen, and Y. X. Li. 2009. Overexpression of AtHsp90.2, AtHsp90.5 and AtHsp90.7 in Arabidopsis thaliana enhances plant sensitivity to salt and drought stresses. Planta 229:955-964.
    • (2009) Planta , vol.229 , pp. 955-964
    • Song, H.M.1    Zhao, R.M.2    Fan, P.X.3    Wang, X.C.4    Chen, X.Y.5    Li, Y.X.6
  • 292
    • 0000278403 scopus 로고
    • Identification of a basic pathogenesis-regulated thaumatin-like protein of virus-infected tobacco as OSM
    • Stintzi, A., T. Heitz, S. Kauffmann, M. Legrand, and B. Fritig. 1991. Identification of a basic pathogenesis-regulated thaumatin-like protein of virus-infected tobacco as OSM. Physiol. Mol. Plant. Pathol. 38:137-146.
    • (1991) Physiol. Mol. Plant. Pathol , vol.38 , pp. 137-146
    • Stintzi, A.1    Heitz, T.2    Kauffmann, S.3    Legrand, M.4    Fritig, B.5
  • 293
    • 0001130048 scopus 로고
    • UV-B damage and protection at the molecular level in plants
    • Strid, A., W. S. Chow, and J. M. Anderson. 1994. UV-B damage and protection at the molecular level in plants. Photosynth. Res. 39:475-489.
    • (1994) Photosynth. Res , vol.39 , pp. 475-489
    • Strid, A.1    Chow, W.S.2    Anderson, J.M.3
  • 294
    • 2642645107 scopus 로고
    • Freezing injury in spinach leaf tissue: Effects on water-soluble proteins, protein-sulfhydryl and water-soluble non-protein-sulfhydryl groups
    • Stuiver, C. E. E., L. J. de Kok, and P. J. C. Kuiper. 1988. Freezing injury in spinach leaf tissue: Effects on water-soluble proteins, protein-sulfhydryl and water-soluble non-protein-sulfhydryl groups. Physiol. Plant. 74:72-76.
    • (1988) Physiol. Plant , vol.74 , pp. 72-76
    • Stuiver, C.E.E.1    de Kok, L.J.2    Kuiper, P.J.C.3
  • 295
    • 3543014424 scopus 로고    scopus 로고
    • Calcium-mediated responses of maize to oxygen deprivation
    • Subbaiah, C. C. and M. M. Sachs. 2003. Calcium-mediated responses of maize to oxygen deprivation. Russ. J. Plant Physiol. 50:752-761.
    • (2003) Russ. J. Plant Physiol , vol.50 , pp. 752-761
    • Subbaiah, C.C.1    Sachs, M.M.2
  • 297
    • 0028895937 scopus 로고
    • Identification and immunolocalization of a 65 kDa drought induced protein in cultivated tomato Lycopersicon esculentum
    • Tabaeizadeh, Z., H. Chamberland, R. D. Chen, L. X. Yu, G. Bellemare, and J. G. Lafontaine. 1995. Identification and immunolocalization of a 65 kDa drought induced protein in cultivated tomato Lycopersicon esculentum. Protoplasma 186:208-219.
    • (1995) Protoplasma , vol.186 , pp. 208-219
    • Tabaeizadeh, Z.1    Chamberland, H.2    Chen, R.D.3    Yu, L.X.4    Bellemare, G.5    Lafontaine, J.G.6
  • 298
    • 63049138121 scopus 로고    scopus 로고
    • Proteomic analysis of salt-responsive proteins in the mangrove plant, Bruguiera gymnorhiza
    • Tada, Y. and T. Kashimura. 2009. Proteomic analysis of salt-responsive proteins in the mangrove plant, Bruguiera gymnorhiza. Plant Cell Physiol. 50:439-446.
    • (2009) Plant Cell Physiol , vol.50 , pp. 439-446
    • Tada, Y.1    Kashimura, T.2
  • 299
    • 3042970469 scopus 로고    scopus 로고
    • Accumulation of pathogenesis-related proteins in barley induced by phosphate and salicylic acid
    • Tamas, L. and Huttova J. 1996. Accumulation of pathogenesis-related proteins in barley induced by phosphate and salicylic acid. Biologia 51:479-484.
    • (1996) Biologia , vol.51 , pp. 479-484
    • Tamas, L.1    Huttova, J.2
  • 300
    • 63549119436 scopus 로고    scopus 로고
    • Abiotic environmental stress induced changes in the Arabidopsis thaliana chloroplast, mitochondria and peroxisome proteomes
    • Taylor, N. L., Y. F. Tan, R. P. Jacoby, and A. H. Millar. 2009. Abiotic environmental stress induced changes in the Arabidopsis thaliana chloroplast, mitochondria and peroxisome proteomes. J. Proteomics 72:367-378.
    • (2009) J. Proteomics , vol.72 , pp. 367-378
    • Taylor, N.L.1    Tan, Y.F.2    Jacoby, R.P.3    Millar, A.H.4
  • 301
    • 0002801680 scopus 로고
    • Protease activity in response to water stress in two differentially sensitive Zea mays L
    • Thakur, P. S. and A. Thakur. 1987. Protease activity in response to water stress in two differentially sensitive Zea mays L. cultivars. Plant Physiol. Biochem. (India) 14:136-139.
    • (1987) cultivars. Plant Physiol. Biochem. (India) , vol.14 , pp. 136-139
    • Thakur, P.S.1    Thakur, A.2
  • 302
    • 33846822133 scopus 로고    scopus 로고
    • Changes in phytochelatins and their biosynthetic intermediates in red spruce (Picea rubens Sarg.) cell suspension cultures under cadmium and zinc stress
    • Thangavel, P., S. Long, and R. Minocha. 2007. Changes in phytochelatins and their biosynthetic intermediates in red spruce (Picea rubens Sarg.) cell suspension cultures under cadmium and zinc stress. Plant Cell Tissue Organ Cult. 88:201-216.
    • (2007) Plant Cell Tissue Organ Cult , vol.88 , pp. 201-216
    • Thangavel, P.1    Long, S.2    Minocha, R.3
  • 303
    • 51649117559 scopus 로고    scopus 로고
    • Proteomics applied on plant abiotic stresses: Role of heat shock proteins (HSP)
    • Timperio, A. M., M. G. Egidi, and L. Zolla. 2008. Proteomics applied on plant abiotic stresses: Role of heat shock proteins (HSP). J. Proteomics 71:391-411.
    • (2008) J. Proteomics , vol.71 , pp. 391-411
    • Timperio, A.M.1    Egidi, M.G.2    Zolla, L.3
  • 304
    • 0031195130 scopus 로고    scopus 로고
    • Two PR-1 genes from tomato are differentially regulated and reveal a novel mode of expression for a pathogenesis-related gene during the hypersensitive response and development
    • Tornero, P., J. Gadea, V. Conejero, and P. Vera. 1997. Two PR-1 genes from tomato are differentially regulated and reveal a novel mode of expression for a pathogenesis-related gene during the hypersensitive response and development. Mol. Plant Microbe Interact. 10:624-634.
    • (1997) Mol. Plant Microbe Interact , vol.10 , pp. 624-634
    • Tornero, P.1    Gadea, J.2    Conejero, V.3    Vera, P.4
  • 305
    • 37149034888 scopus 로고    scopus 로고
    • Gel-based proteomics reveals potential novel protein markers of ozone stress in leaves of cultivated bean and maize species of Panama
    • Torres, N. L., K. Cho, J. Shibato, et al. 2007. Gel-based proteomics reveals potential novel protein markers of ozone stress in leaves of cultivated bean and maize species of Panama. Electrophoresis 28:4369-4381.
    • (2007) Electrophoresis , vol.28 , pp. 4369-4381
    • Torres, N.L.1    Cho, K.2    Shibato, J.3
  • 306
    • 0342459424 scopus 로고
    • Changes in protein synthesis and translatable messenger RNA populations associated with ABA-induced cold hardiness in potato (Solatium commersonii)
    • Tseng, M. J. and P. H. Li. 1991. Changes in protein synthesis and translatable messenger RNA populations associated with ABA-induced cold hardiness in potato (Solatium commersonii). Physiol. Plant. 81:349-358.
    • (1991) Physiol. Plant , vol.81 , pp. 349-358
    • Tseng, M.J.1    Li, P.H.2
  • 307
    • 63549092248 scopus 로고    scopus 로고
    • Genotype-dependent expression of specific members of potato protease inhibitor gene families in different tissues and in response to wounding and nematode infection
    • Turrà, D., D. Bellin, M. Lorito, and C. Gebhardt. 2009. Genotype-dependent expression of specific members of potato protease inhibitor gene families in different tissues and in response to wounding and nematode infection. J. Plant Physiol. 166:762-774.
    • (2009) J. Plant Physiol , vol.166 , pp. 762-774
    • Turrà, D.1    Bellin, D.2    Lorito, M.3    Gebhardt, C.4
  • 308
    • 0000610981 scopus 로고
    • Involvement of plasma membrane alterations in cold acclimation of winter rye seedlings (Secale cereale L
    • Uemura, M. and S. Yoshida. 1984. Involvement of plasma membrane alterations in cold acclimation of winter rye seedlings (Secale cereale L. cv. Puma). Plant Physiol. 75:818-826.
    • (1984) cv. Puma). Plant Physiol , vol.75 , pp. 818-826
    • Uemura, M.1    Yoshida, S.2
  • 309
    • 0028891190 scopus 로고
    • Genetic variability in recovery growth and synthesis of stress proteins in response to polyethylene glycol and salt stress in finger millet
    • Uma, S., T. G. Prasad, and M. U. Kumar. 1995. Genetic variability in recovery growth and synthesis of stress proteins in response to polyethylene glycol and salt stress in finger millet. Ann. Bot. 76:43-49.
    • (1995) Ann. Bot , vol.76 , pp. 43-49
    • Uma, S.1    Prasad, T.G.2    Kumar, M.U.3
  • 311
    • 0842270131 scopus 로고    scopus 로고
    • Transgenic tobacco plants constitutively overexpressing a rice thaumatin-like protein (PR-5) show enhanced resistance to Alternaria alternata
    • Velazhahan, R. and S. Muthukrishnan. 2003. Transgenic tobacco plants constitutively overexpressing a rice thaumatin-like protein (PR-5) show enhanced resistance to Alternaria alternata. Biol. Plant. 47:347-354.
    • (2003) Biol. Plant , vol.47 , pp. 347-354
    • Velazhahan, R.1    Muthukrishnan, S.2
  • 312
    • 0035043536 scopus 로고    scopus 로고
    • Effect of cadmium on soluble sugars and enzymes of their metabolism in rice
    • Verma, S. and R. S. Dubey. 2001. Effect of cadmium on soluble sugars and enzymes of their metabolism in rice. Biol. Plant. 44:117-123.
    • (2001) Biol. Plant , vol.44 , pp. 117-123
    • Verma, S.1    Dubey, R.S.2
  • 313
    • 0037393291 scopus 로고    scopus 로고
    • Lead toxicity induces lipid peroxidation and alters the activities of antioxidant enzymes in growing rice plants
    • Verma, S. and R. S. Dubey. 2003. Lead toxicity induces lipid peroxidation and alters the activities of antioxidant enzymes in growing rice plants. Plant Sci. 164:645-655.
    • (2003) Plant Sci , vol.164 , pp. 645-655
    • Verma, S.1    Dubey, R.S.2
  • 316
    • 85050899732 scopus 로고
    • International Conference of Plant Physiologists of SAARC Countries, Gorakhpur, India (Abstr):119
    • Vyas, A. V. and N. U. Rao. 1987. Protein mechanism in salt stressed cowpea seedlings. International Conference of Plant Physiologists of SAARC Countries, Gorakhpur, India (Abstr):119.
    • (1987) Protein mechanism in salt stressed cowpea seedlings
    • Vyas, A.V.1    Rao, N.U.2
  • 318
    • 2442445139 scopus 로고    scopus 로고
    • Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response
    • Wang, W., B. Vinocur, O. Shoseyov, and A. Altman. 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
  • 319
    • 16244419047 scopus 로고    scopus 로고
    • Enhanced drought tolerance of transgenic rice plants expressing a pea manganese superoxide dismutase
    • Wang, F. Z., Q. B. Wang, S. Y. Kwon, S. S. Kwak, and W. A. Su. 2005. Enhanced drought tolerance of transgenic rice plants expressing a pea manganese superoxide dismutase. J. Plant Physiol. 162:465-472.
    • (2005) J. Plant Physiol , vol.162 , pp. 465-472
    • Wang, F.Z.1    Wang, Q.B.2    Kwon, S.Y.3    Kwak, S.S.4    Su, W.A.5
  • 320
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters, E. R., G. J. Lee, and E. Vierling. 1996. Evolution, structure and function of the small heat shock proteins in plants. J. Exp. Bot. 47:325-338.
    • (1996) J. Exp. Bot , vol.47 , pp. 325-338
    • Waters, E.R.1    Lee, G.J.2    Vierling, E.3
  • 321
    • 1142293854 scopus 로고    scopus 로고
    • Photoperiod and temperature differentially regulate the expression of two dehydrin genes during overwintering of birch (Betula pubescens Ehrh.)
    • Welling, A., P. Rinne, A. Vihera-Aarnio, S. Kontunen-Soppela, P. Heino, and E. T. Palva. 2004. Photoperiod and temperature differentially regulate the expression of two dehydrin genes during overwintering of birch (Betula pubescens Ehrh.). J. Exp. Bot. 55:507-516.
    • (2004) J. Exp. Bot , vol.55 , pp. 507-516
    • Welling, A.1    Rinne, P.2    Vihera-Aarnio, A.3    Kontunen-Soppela, S.4    Heino, P.5    Palva, E.T.6
  • 322
    • 33646487152 scopus 로고    scopus 로고
    • Differential regulation of two dehydrin genes from peach (Prunus persica) by photoperiod, low temperature and water deficit
    • Wisniewski, M. E., C. L. Bassett, J. Renaut, R. Farrell, T. Tworkoski, and T. S. Artlip. 2006. Differential regulation of two dehydrin genes from peach (Prunus persica) by photoperiod, low temperature and water deficit. Tree Physiol. 26:575-584.
    • (2006) Tree Physiol , vol.26 , pp. 575-584
    • Wisniewski, M.E.1    Bassett, C.L.2    Renaut, J.3    Farrell, R.4    Tworkoski, T.5    Artlip, T.S.6
  • 324
    • 0032475833 scopus 로고    scopus 로고
    • A carrot leucine-rich-repeat protein that inhibits ice recrystallization
    • Worrall, D., L. Elias, D. Ashford, et al. 1998. A carrot leucine-rich-repeat protein that inhibits ice recrystallization. Science 282:115-117.
    • (1998) Science , vol.282 , pp. 115-117
    • Worrall, D.1    Elias, L.2    Ashford, D.3
  • 325
    • 17844406175 scopus 로고    scopus 로고
    • Effects of water stress on photosynthesis and nitrogen metabolism in vegetative and reproductive shoots of Leymus chinensis
    • Xu, Z. Z. and G. S. Zhou. 2005. Effects of water stress on photosynthesis and nitrogen metabolism in vegetative and reproductive shoots of Leymus chinensis. Photosynthetica 43:29-35.
    • (2005) Photosynthetica , vol.43 , pp. 29-35
    • Xu, Z.Z.1    Zhou, G.S.2
  • 326
    • 0030021536 scopus 로고    scopus 로고
    • Expression of a late embryogenesis abundant protein gene, HVA1, from barley confers tolerance to water deficit and salt stress in transgenic rice
    • Xu, D., X. Duan, B. Wang, B. Hong, T. H. D. Ho, and R. Wu. 1996. Expression of a late embryogenesis abundant protein gene, HVA1, from barley confers tolerance to water deficit and salt stress in transgenic rice. Plant Physiol. 110:249-257.
    • (1996) Plant Physiol , vol.110 , pp. 249-257
    • Xu, D.1    Duan, X.2    Wang, B.3    Hong, B.4    Ho, T.H.D.5    Wu, R.6
  • 327
    • 37149054654 scopus 로고    scopus 로고
    • Impact of solar Ultraviolet-B on the proteome in soybean lines differing in flavonoid contents
    • Xu, C. P., J. H. Sullivan, W. M. Garrett, T. J. Caperna, and S. Natarajan. 2008. Impact of solar Ultraviolet-B on the proteome in soybean lines differing in flavonoid contents. Phytochemistry 69:38-48.
    • (2008) Phytochemistry , vol.69 , pp. 38-48
    • Xu, C.P.1    Sullivan, J.H.2    Garrett, W.M.3    Caperna, T.J.4    Natarajan, S.5
  • 328
    • 21344474557 scopus 로고    scopus 로고
    • Effects of free proline accumulation in petunias under drought stress
    • Yamada, M., H. Morishita, K. Urano, et al. 2005. Effects of free proline accumulation in petunias under drought stress. J. Exp. Bot. 56:1975-1981.
    • (2005) J. Exp. Bot , vol.56 , pp. 1975-1981
    • Yamada, M.1    Morishita, H.2    Urano, K.3
  • 329
    • 33847692807 scopus 로고    scopus 로고
    • Proline accumulation in transgenic tobacco as a result of expression of Arabidopsis Delta(1)-pyrroline-5-carboxylate synthetase (P5CS) during osmotic stress
    • Yamchi, A., F. R. Jazii, A. Mousavi, and A. A. Karkhane. 2007. Proline accumulation in transgenic tobacco as a result of expression of Arabidopsis Delta(1)-pyrroline-5-carboxylate synthetase (P5CS) during osmotic stress. J. Plant Biochem. Biotechnol. 16:9-15.
    • (2007) J. Plant Biochem. Biotechnol , vol.16 , pp. 9-15
    • Yamchi, A.1    Jazii, F.R.2    Mousavi, A.3    Karkhane, A.A.4
  • 330
    • 33645472456 scopus 로고    scopus 로고
    • Comparative proteomic analysis provides new insights into chilling stress responses in rice
    • Yan, S. P., Q. Y. Zhang, Z. C. Tang, W. A. Su, and W. N. Sun. 2006. Comparative proteomic analysis provides new insights into chilling stress responses in rice. Mol. Cell Proteomics 5:484-496.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 484-496
    • Yan, S.P.1    Zhang, Q.Y.2    Tang, Z.C.3    Su, W.A.4    Sun, W.N.5
  • 331
    • 33749011396 scopus 로고    scopus 로고
    • The involvement of chloroplast HSP100/ClpB in the acquired thermotolerance in tomato
    • Yang, J., Y. Sun, A. Sun, S. Yi, J. Qin, M. Li, and J. Liu. 2006. The involvement of chloroplast HSP100/ClpB in the acquired thermotolerance in tomato. Plant Mol. Biol. 62:385-395.
    • (2006) Plant Mol. Biol , vol.62 , pp. 385-395
    • Yang, J.1    Sun, Y.2    Sun, A.3    Yi, S.4    Qin, J.5    Li, M.6    Liu, J.7
  • 332
    • 61849166670 scopus 로고    scopus 로고
    • Salt stress responses in Populus cathayana Rehder
    • Yang, F., X. W. Xiao, S. Zhang, H. Korpelainen, and C. Y. Li. 2009. Salt stress responses in Populus cathayana Rehder. Plant Sci. 176:669-677.
    • (2009) Plant Sci , vol.176 , pp. 669-677
    • Yang, F.1    Xiao, X.W.2    Zhang, S.3    Korpelainen, H.4    Li, C.Y.5
  • 333
    • 0031105110 scopus 로고    scopus 로고
    • A novel glycine-rich/hydrophobic 16 kDa polypeptide gene from tobacco: Similarity to proline-rich protein genes and its wound-inducible and developmentally regulated expression
    • Yasuda, E., H. Ebinuma, and H. Wabiko. 1996. A novel glycine-rich/hydrophobic 16 kDa polypeptide gene from tobacco: Similarity to proline-rich protein genes and its wound-inducible and developmentally regulated expression. Plant Mol. Biol. 33:667-678.
    • (1996) Plant Mol. Biol , vol.33 , pp. 667-678
    • Yasuda, E.1    Ebinuma, H.2    Wabiko, H.3
  • 334
    • 34347370229 scopus 로고    scopus 로고
    • Two-dimensional electrophoretic analysis of soluble leaf proteins of a salt-sensitive (Triticum aestivum) and a salt-tolerant (T
    • Yildiz, M. 2007. Two-dimensional electrophoretic analysis of soluble leaf proteins of a salt-sensitive (Triticum aestivum) and a salt-tolerant (T. durum) cultivar in response to NaCl stress. J. Integr. Plant Biol. 49:975-981.
    • (2007) durum) cultivar in response to NaCl stress. J. Integr. Plant Biol , vol.49 , pp. 975-981
    • Yildiz, M.1
  • 335
    • 45749104094 scopus 로고    scopus 로고
    • Small heat shock protein responses in leaf tissues of wheat cultivars with different heat susceptibility
    • Yildiz, M. and H. Terzi. 2008. Small heat shock protein responses in leaf tissues of wheat cultivars with different heat susceptibility. Biologia 63:521-525.
    • (2008) Biologia , vol.63 , pp. 521-525
    • Yildiz, M.1    Terzi, H.2
  • 336
    • 33748255935 scopus 로고    scopus 로고
    • Expression of a Solanum sogarandinum SK3-type dehydrin enhances cold tolerance in transgenic cucumber seedlings
    • Yin, Z., T. Rorat, B. M. Szabala, A. Ziolkowska, and S. Malepszy. 2006. Expression of a Solanum sogarandinum SK3-type dehydrin enhances cold tolerance in transgenic cucumber seedlings. Plant Sci. 170:1164-1172.
    • (2006) Plant Sci , vol.170 , pp. 1164-1172
    • Yin, Z.1    Rorat, T.2    Szabala, B.M.3    Ziolkowska, A.4    Malepszy, S.5
  • 337
    • 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., A. Masuda, M. Kuwano, A. Yokota, and K. Akashi. 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
  • 338
    • 0030393492 scopus 로고    scopus 로고
    • Negative regulation of gene expression of a novel proline-, threonine- and glycine-rich protein by water stress in Lycopersicon chilense
    • Yu, L. X., H. Chamberland, J. G. Lafontain, and Z. Tabaeizadeh. 1996. Negative regulation of gene expression of a novel proline-, threonine- and glycine-rich protein by water stress in Lycopersicon chilense. Genome 39:1185-1193.
    • (1996) Genome , vol.39 , pp. 1185-1193
    • Yu, L.X.1    Chamberland, H.2    Lafontain, J.G.3    Tabaeizadeh, Z.4
  • 340
    • 10344238540 scopus 로고    scopus 로고
    • Analysis of an ABA- and osmotic stress-inducible dehydrin from Stellaria longipes
    • Zhang, X. H., M. M. Moloney, and C. C. Chinnappa. 1996. Analysis of an ABA- and osmotic stress-inducible dehydrin from Stellaria longipes. J. Plant Physiol. 149:617-622.
    • (1996) J. Plant Physiol , vol.149 , pp. 617-622
    • Zhang, X.H.1    Moloney, M.M.2    Chinnappa, C.C.3
  • 341
    • 64949108782 scopus 로고    scopus 로고
    • Proteomic identification of small, copper-responsive proteins in germinating embryos of Oryza sativa
    • Zhang, H. X., C. L. Lian, and Z. G. Shen. 2009. Proteomic identification of small, copper-responsive proteins in germinating embryos of Oryza sativa. Ann. Bot. 103:923-930.
    • (2009) Ann. Bot , vol.103 , pp. 923-930
    • Zhang, H.X.1    Lian, C.L.2    Shen, Z.G.3
  • 342
    • 34548525483 scopus 로고    scopus 로고
    • Effects of enhanced UV-B radiation on the activity and expression of alternative oxidase in red kidney bean leaves
    • Zhao, M. G., Y. G. Liu, L. X. Zhang, L. Zheng, and Y. R. Bi. 2007. Effects of enhanced UV-B radiation on the activity and expression of alternative oxidase in red kidney bean leaves. J. Integr. Plant Biol. 49:1320-1326.
    • (2007) J. Integr. Plant Biol , vol.49 , pp. 1320-1326
    • Zhao, M.G.1    Liu, Y.G.2    Zhang, L.X.3    Zheng, L.4    Bi, Y.R.5


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