메뉴 건너뛰기




Volumn 218, Issue 1, 2003, Pages 1-14

Plant responses to drought, salinity and extreme temperatures: Towards genetic engineering for stress tolerance

Author keywords

Abiotic stress; Antioxidant; Hsp; Ion transport; LEA protein; Osmolyte; Transcription factor

Indexed keywords

BIOTECHNOLOGY; DETOXIFICATION; DROUGHT; GENES; METABOLITES; PLANTS (BOTANY); PROTEINS; SALINITY MEASUREMENT; SIGNALING; STRESSES; TOXICITY;

EID: 0347300280     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00425-003-1105-5     Document Type: Review
Times cited : (2897)

References (171)
  • 1
    • 0037256419 scopus 로고    scopus 로고
    • Arabidopsis AtMYC2 (bHLH) and AtMYB2 (MYB) function as transcriptional activators in abscisic acid signaling
    • Abe H, Urao T, Ito T, Seki M, Shinozaki K, Yamaguchi-Shinozaki K (2003) Arabidopsis AtMYC2 (bHLH) and AtMYB2 (MYB) function as transcriptional activators in abscisic acid signaling. Plant Cell 15:63-78
    • (2003) Plant Cell , vol.15 , pp. 63-78
    • Abe, H.1    Urao, T.2    Ito, T.3    Seki, M.4    Shinozaki, K.5    Yamaguchi-Shinozaki, K.6
  • 2
    • 0029616226 scopus 로고
    • Constitutive expression of small heat shock proteins in vegetative tissues of the resurrection plant Craterostigma plantagineum
    • Alamillo J, Almoguera C, Bartels D, Jordano J (1995) Constitutive expression of small heat shock proteins in vegetative tissues of the resurrection plant Craterostigma plantagineum. Plant Mol Biol 29:1093-1099
    • (1995) Plant Mol Biol , vol.29 , pp. 1093-1099
    • Alamillo, J.1    Almoguera, C.2    Bartels, D.3    Jordano, J.4
  • 3
    • 0032191255 scopus 로고    scopus 로고
    • Enhancement of the tolerance of Arabidopsis to high temperatures by genetic engineering of the synthesis of glycinebetaine
    • Alia, Hayashi H, Sakamoto A, Murata N (1998a) Enhancement of the tolerance of Arabidopsis to high temperatures by genetic engineering of the synthesis of glycinebetaine. Plant J 16:155-161
    • (1998) Plant J , vol.16 , pp. 155-161
    • Alia1    Hayashi, H.2    Sakamoto, A.3    Murata, N.4
  • 4
    • 0031957417 scopus 로고    scopus 로고
    • Transformation with a gene for choline oxidase enhances the cold tolerance of Arabidopsis during germination and early growth
    • Alia, Hayashi H, Chen THH, Murata N (1998b) Transformation with a gene for choline oxidase enhances the cold tolerance of Arabidopsis during germination and early growth. Plant Cell Environ 21:232-239
    • (1998) Plant Cell Environ , vol.21 , pp. 232-239
    • Alia1    Hayashi, H.2    Chen, T.H.H.3    Murata, N.4
  • 5
    • 0027131328 scopus 로고
    • Tissue-specific expression of sunflower heat shock proteins in response to water stress
    • Almoguera C, Coca MA, Jordano J (1993) Tissue-specific expression of sunflower heat shock proteins in response to water stress. Plant J 4:947-958
    • (1993) Plant J , vol.4 , pp. 947-958
    • Almoguera, C.1    Coca, M.A.2    Jordano, J.3
  • 7
    • 0029825615 scopus 로고    scopus 로고
    • Constitutive expression of the cold-regulated Arabidopsis thaliana COR15a gene affects both chloroplast and protoplast freezing tolerance
    • Artus NN, Uemura M, Steponkus PL, Gilmour SJ, Lin C, Thomashow MF (1996) Constitutive expression of the cold-regulated Arabidopsis thaliana COR15a gene affects both chloroplast and protoplast freezing tolerance. Proc Natl Acad Sci USA 93:13404-13409
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13404-13409
    • Artus, N.N.1    Uemura, M.2    Steponkus, P.L.3    Gilmour, S.J.4    Lin, C.5    Thomashow, M.F.6
  • 9
    • 0035209289 scopus 로고    scopus 로고
    • Targeting detoxification pathways: An efficient approach to obtain plants with multiple stress tolerance
    • Bartels D (2001) Targeting detoxification pathways: an efficient approach to obtain plants with multiple stress tolerance. Trends Plant Sci 6:284-286
    • (2001) Trends Plant Sci , vol.6 , pp. 284-286
    • Bartels, D.1
  • 10
    • 0033922517 scopus 로고    scopus 로고
    • Sodium transport and salt tolerance in plants
    • Blumwald E (2000) Sodium transport and salt tolerance in plants. Curr Opin Cell Biol 12:431-434
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 431-434
    • Blumwald, E.1
  • 11
    • 0344527923 scopus 로고    scopus 로고
    • Transformation and compatible solutes
    • Bohnert HJ, Shen B (1999) Transformation and compatible solutes. Sci Hort 78:237-260
    • (1999) Sci Hort , vol.78 , pp. 237-260
    • Bohnert, H.J.1    Shen, B.2
  • 12
    • 0032081990 scopus 로고    scopus 로고
    • Plant stress adaptations - Making metabolism move
    • Bohnert HJ, Sheveleva E (1998) Plant stress adaptations - making metabolism move. Curr Opin Plant Biol 1:267-274
    • (1998) Curr Opin Plant Biol , vol.1 , pp. 267-274
    • Bohnert, H.J.1    Sheveleva, E.2
  • 14
    • 0030895247 scopus 로고    scopus 로고
    • Transfer of the yeast salt tolerance gene HAL1 to Cucumis melo L. cultivars and in vitro evaluation of salt tolerance
    • Bordas M, Montesinos C, Debauza M, Salvador A, Roig LA, Serrano R, Moreno V (1997) Transfer of the yeast salt tolerance gene HAL1 to Cucumis melo L. cultivars and in vitro evaluation of salt tolerance. Transgenic Res 6:41-50
    • (1997) Transgenic Res , vol.6 , pp. 41-50
    • Bordas, M.1    Montesinos, C.2    Debauza, M.3    Salvador, A.4    Roig, L.A.5    Serrano, R.6    Moreno, V.7
  • 15
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • Boston RS, Viitanen PV, Vierling E (1996) Molecular chaperones and protein folding in plants. Plant Mol Biol 32:191-222
    • (1996) Plant Mol Biol , vol.32 , pp. 191-222
    • Boston, R.S.1    Viitanen, P.V.2    Vierling, E.3
  • 17
    • 0020458787 scopus 로고
    • Plant productivity and environment
    • Boyer JS (1982) Plant productivity and environment. Science 218:443-448
    • (1982) Science , vol.218 , pp. 443-448
    • Boyer, J.S.1
  • 18
    • 0002915845 scopus 로고    scopus 로고
    • Responses to abiotic stresses
    • Gruissem W, Buchannan B, Jones R (eds). American Society of Plant Physiologists, Rockville, MD
    • Bray EA, Bailey-Serres J, Weretilnyk E (2000) Responses to abiotic stresses. In: Gruissem W, Buchannan B, Jones R (eds) Biochemistry and molecular biology of plants. American Society of Plant Physiologists, Rockville, MD, pp 1158-1249
    • (2000) Biochemistry and Molecular Biology of Plants , pp. 1158-1249
    • Bray, E.A.1    Bailey-Serres, J.2    Weretilnyk, E.3
  • 20
    • 0031741822 scopus 로고    scopus 로고
    • Phospholipase activity during plant growth and development and in response to environmental stress
    • Chapman D (1998) Phospholipase activity during plant growth and development and in response to environmental stress. Trends Plant Sci. 3:419-426
    • (1998) Trends Plant Sci , vol.3 , pp. 419-426
    • Chapman, D.1
  • 22
    • 0028233236 scopus 로고
    • A 21-kDa chloroplast heat shock protein assembles into high molecular weight complexes in vitro and in organelle
    • Chen Q, Osteryoung K, Vierling E (1994) A 21-kDa chloroplast heat shock protein assembles into high molecular weight complexes in vitro and in organelle. J Biol Chem 269:13216-13233
    • (1994) J Biol Chem , vol.269 , pp. 13216-13233
    • Chen, Q.1    Osteryoung, K.2    Vierling, E.3
  • 23
    • 0036011086 scopus 로고    scopus 로고
    • Enhancement of tolerance of abiotic stress by metabolic engineering of betaines and other compatible solutes
    • Chen THH, Murata N (2002) Enhancement of tolerance of abiotic stress by metabolic engineering of betaines and other compatible solutes. Curr Opin Plant Biol 5:250-257
    • (2002) Curr Opin Plant Biol , vol.5 , pp. 250-257
    • Chen, T.H.H.1    Murata, N.2
  • 25
    • 0034695679 scopus 로고    scopus 로고
    • ABFs, a family of ABA-responsive element binding factors
    • Choi HI, Hong JH, Ha J, Kang JY, Kim SY (2000) ABFs, a family of ABA-responsive element binding factors. J Biol Chem 275:1723-1730
    • (2000) J Biol Chem , vol.275 , pp. 1723-1730
    • Choi, H.I.1    Hong, J.H.2    Ha, J.3    Kang, J.Y.4    Kim, S.Y.5
  • 26
    • 0030498675 scopus 로고    scopus 로고
    • Dehydrins: Emergence of a biochemical role of a family of plant dehydration proteins
    • Close TJ (1996) Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol Plant 97:795-803
    • (1996) Physiol Plant , vol.97 , pp. 795-803
    • Close, T.J.1
  • 27
    • 0024698889 scopus 로고
    • A cDNA-based comparison of dehydration-induced proteins (dehydrins) in barley and corn
    • Close TJ, Kortt AA, Chandler PM (1989) A cDNA-based comparison of dehydration-induced proteins (dehydrins) in barley and corn. Plant Mol Biol 13:95-108
    • (1989) Plant Mol Biol , vol.13 , pp. 95-108
    • Close, T.J.1    Kortt, A.A.2    Chandler, P.M.3
  • 28
    • 3543024452 scopus 로고    scopus 로고
    • Purification and in vitro chaperone activity of a class I small heat-shock protein abundant in recalcitrant chestnut seeds
    • Collada C, Gomez L, Casado R, Aragoncillo C (1997) Purification and in vitro chaperone activity of a class I small heat-shock protein abundant in recalcitrant chestnut seeds. Plant Physiol 115:71-77
    • (1997) Plant Physiol , vol.115 , pp. 71-77
    • Collada, C.1    Gomez, L.2    Casado, R.3    Aragoncillo, C.4
  • 29
    • 0034014059 scopus 로고    scopus 로고
    • Genomic approaches to plant stress tolerance
    • Cushman JC, Bohnert HJ (2000) Genomic approaches to plant stress tolerance. Curr Opin Plant Biol 3:117-124
    • (2000) Curr Opin Plant Biol , vol.3 , pp. 117-124
    • Cushman, J.C.1    Bohnert, H.J.2
  • 30
    • 0037062998 scopus 로고    scopus 로고
    • Overexpression of β-carotene hydroxylase enhances stress tolerance in Arabidopsis
    • Davison PA, Hunter CN, Horton P (2002) Overexpression of β-carotene hydroxylase enhances stress tolerance in Arabidopsis. Nature 418:201-206
    • (2002) Nature , vol.418 , pp. 201-206
    • Davison, P.A.1    Hunter, C.N.2    Horton, P.3
  • 31
    • 0035955743 scopus 로고    scopus 로고
    • Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses
    • Diamant S, Eliahu N, Rosenthal D, Goloubinoff P (2001) Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses. J Biol Chem 276:39586-39591
    • (2001) J Biol Chem , vol.276 , pp. 39586-39591
    • Diamant, S.1    Eliahu, N.2    Rosenthal, D.3    Goloubinoff, P.4
  • 32
    • 0034737774 scopus 로고    scopus 로고
    • HSP25, a small heat shock protein associated with dense bodies and M-lines of body wall muscle in Caenorhabditis elegans
    • Ding L, Candido EPM (2000) HSP25, a small heat shock protein associated with dense bodies and M-lines of body wall muscle in Caenorhabditis elegans. J Biol Chem 275:9510-9517
    • (2000) J Biol Chem , vol.275 , pp. 9510-9517
    • Ding, L.1    Candido, E.P.M.2
  • 33
    • 0033962695 scopus 로고    scopus 로고
    • Transgenic approaches to crop improvement
    • Dunwell JM (2000) Transgenic approaches to crop improvement. J Exp Bot 51:487-496
    • (2000) J Exp Bot , vol.51 , pp. 487-496
    • Dunwell, J.M.1
  • 34
    • 0002663990 scopus 로고
    • Structural motifs in Lea proteins
    • Close TJ, Bray EA (eds). American Society of Plant Physiologists, Rockville, MD
    • Dure III L (1993a) Structural motifs in Lea proteins. In: Close TJ, Bray EA (eds) Plant response to cellular dehydration during environmental stress. American Society of Plant Physiologists, Rockville, MD, pp 91-103
    • (1993) Plant Response to Cellular Dehydration during Environmental Stress , pp. 91-103
    • Dure III, L.1
  • 35
    • 0027564435 scopus 로고
    • A repeating 11-mer amino acid motif and plant desiccation
    • Dure III L (1993b) A repeating 11-mer amino acid motif and plant desiccation. Plant J 3:363-369
    • (1993) Plant J , vol.3 , pp. 363-369
    • Dure III, L.1
  • 36
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M, Gräber S, Gaestel M, Buchner J (1997) Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J 16:221-229
    • (1997) EMBO J , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Gräber, S.2    Gaestel, M.3    Buchner, J.4
  • 37
    • 0034106785 scopus 로고    scopus 로고
    • The Arabidopsis abscisic acid response gene ABI5 encodes a basic leucine zipper transcription factor
    • Finkelstein RR, Lynch TJ (2000) The Arabidopsis abscisic acid response gene ABI5 encodes a basic leucine zipper transcription factor. Plant Cell 12:599-609
    • (2000) Plant Cell , vol.12 , pp. 599-609
    • Finkelstein, R.R.1    Lynch, T.J.2
  • 38
    • 0036671216 scopus 로고    scopus 로고
    • Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway
    • Fowler S, Thomashow MF (2002) Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway. Plant Cell 14:1675-1690
    • (2002) Plant Cell , vol.14 , pp. 1675-1690
    • Fowler, S.1    Thomashow, M.F.2
  • 39
    • 0033980712 scopus 로고    scopus 로고
    • Water deficit triggers phospholipase D activity in the resurrection plant Craterostigma plantagineum
    • Frank W, Munnik T, Kerkmann K, Salamini F, Bartels D (2000) Water deficit triggers phospholipase D activity in the resurrection plant Craterostigma plantagineum. Plant Cell 12:111-124
    • (2000) Plant Cell , vol.12 , pp. 111-124
    • Frank, W.1    Munnik, T.2    Kerkmann, K.3    Salamini, F.4    Bartels, D.5
  • 41
    • 0034007384 scopus 로고    scopus 로고
    • Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit
    • Garay-Arroyo A, Colmenero-Flores JM, Garciarrubio A, Covarrubias AA (2000) Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit. J Biol Chem 275:5668-5674
    • (2000) J Biol Chem , vol.275 , pp. 5668-5674
    • Garay-Arroyo, A.1    Colmenero-Flores, J.M.2    Garciarrubio, A.3    Covarrubias, A.A.4
  • 43
    • 0033573896 scopus 로고    scopus 로고
    • The Arabidopsis thaliana proton transporters, AtNhx1 and Avp1, can function in cation detoxification in yeast
    • Gaxiola RA, Rao R, Sherman A, Grisafi P, Alper SL, Fink GR (1999) The Arabidopsis thaliana proton transporters, AtNhx1 and Avp1, can function in cation detoxification in yeast. Proc Natl Acad Sci USA. 96:1480-1485
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1480-1485
    • Gaxiola, R.A.1    Rao, R.2    Sherman, A.3    Grisafi, P.4    Alper, S.L.5    Fink, G.R.6
  • 45
    • 0032213180 scopus 로고    scopus 로고
    • Low temperature regulation of the Arabidopsis CBF family of AP2 transcriptional activators as an early step in cold-induced COR gene expression
    • Gilmour SJ, Zarka DG, Stockinger EJ, Salazar MP, Houghton JM, Thomashow MF (1998) Low temperature regulation of the Arabidopsis CBF family of AP2 transcriptional activators as an early step in cold-induced COR gene expression. Plant J 16:433-442
    • (1998) Plant J , vol.16 , pp. 433-442
    • Gilmour, S.J.1    Zarka, D.G.2    Stockinger, E.J.3    Salazar, M.P.4    Houghton, J.M.5    Thomashow, M.F.6
  • 46
    • 0034527513 scopus 로고    scopus 로고
    • Overexpression of the arabidopsis CBF3 transcriptional activator mimics multiple biochemical changes associated with cold acclimation
    • Gilmour SJ, Sebolt AM, Salazar MP, Everard JD, Thomashow MF (2000) Overexpression of the arabidopsis CBF3 transcriptional activator mimics multiple biochemical changes associated with cold acclimation. Plant Physiol 124:1854-1865
    • (2000) Plant Physiol , vol.124 , pp. 1854-1865
    • Gilmour, S.J.1    Sebolt, A.M.2    Salazar, M.P.3    Everard, J.D.4    Thomashow, M.F.5
  • 48
    • 0025706143 scopus 로고
    • A plant leucine zipper protein that recognizes an abscisic acid response element
    • Guiltinan MJ, Marcotte WR, Quatrano RS (1990) A plant leucine zipper protein that recognizes an abscisic acid response element. Science 250:267-271
    • (1990) Science , vol.250 , pp. 267-271
    • Guiltinan, M.J.1    Marcotte, W.R.2    Quatrano, R.S.3
  • 49
    • 0027511499 scopus 로고
    • Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dismutase
    • Gupta AS, Heinen JL, Holaday AS, Burke JJ, Allen RD (1993a) Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dismutase. Proc Natl Acad Sci USA 90:1629-1633
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1629-1633
    • Gupta, A.S.1    Heinen, J.L.2    Holaday, A.S.3    Burke, J.J.4    Allen, R.D.5
  • 50
    • 0027141553 scopus 로고
    • Overexpression of superoxide dismutase protects plants from oxidative stress
    • Gupta AS, Webb RP, Holaday AS, Allen RD (1993b) Overexpression of superoxide dismutase protects plants from oxidative stress. Plant Physiol 103:1067-1073
    • (1993) Plant Physiol , vol.103 , pp. 1067-1073
    • Gupta, A.S.1    Webb, R.P.2    Holaday, A.S.3    Allen, R.D.4
  • 53
    • 0034958914 scopus 로고    scopus 로고
    • Mitochondrial adaptations to NaCl. Complex I is protected by anti-oxidants and small heat shock proteins, whereas complex II is protected by proline and betaine
    • Hamilton III EW, Heckathorn SA (2001) Mitochondrial adaptations to NaCl. Complex I is protected by anti-oxidants and small heat shock proteins, whereas complex II is protected by proline and betaine. Plant Physiol 126:1266-1274
    • (2001) Plant Physiol , vol.126 , pp. 1266-1274
    • Hamilton III, E.W.1    Heckathorn, S.A.2
  • 54
    • 0031851152 scopus 로고    scopus 로고
    • Dissecting the roles of osmolyte accumulation during stress
    • Hare PD, Cress WA, Van Staden J (1998) Dissecting the roles of osmolyte accumulation during stress. Plant Cell Environ 21:535-553
    • (1998) Plant Cell Environ , vol.21 , pp. 535-553
    • Hare, P.D.1    Cress, W.A.2    Van Staden, J.3
  • 55
    • 0344172562 scopus 로고    scopus 로고
    • The chloroplast small heat shock protein undergoes oxidation-dependent conformational changes and may protect plants from oxidative stress
    • Härndahl U, Hall RB, Osteryoung KW, Vierling E, Bornman JF, Sundby C (1999) The chloroplast small heat shock protein undergoes oxidation-dependent conformational changes and may protect plants from oxidative stress. Cell Stress Chaperones 4:129-138
    • (1999) Cell Stress Chaperones , vol.4 , pp. 129-138
    • Härndahl, U.1    Hall, R.B.2    Osteryoung, K.W.3    Vierling, E.4    Bornman, J.F.5    Sundby, C.6
  • 56
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381:571-579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 59
    • 0031194854 scopus 로고    scopus 로고
    • Transformation of Arabidopsis thaliana with the codA gene for choline oxidase: Accumulation of glycinebetaine and enhanced tolerance to salt and cold stress
    • Hayashi H, Mustardy L, Deshnium P, Ida M, Murata N (1997) Transformation of Arabidopsis thaliana with the codA gene for choline oxidase: accumulation of glycinebetaine and enhanced tolerance to salt and cold stress. Plant J 12:133-142
    • (1997) Plant J , vol.12 , pp. 133-142
    • Hayashi, H.1    Mustardy, L.2    Deshnium, P.3    Ida, M.4    Murata, N.5
  • 60
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick JP, Hartl FU (1993) Molecular chaperone functions of heat-shock proteins. Annu Rev Biochem 62:349-384
    • (1993) Annu Rev Biochem , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 61
    • 0033592931 scopus 로고    scopus 로고
    • A bZIP factor, TRAB1, interacts with VP1 and mediates abscisic acid-induced transcription
    • Hobo T, Kowyama Y, Hattori T (1999) A bZIP factor, TRAB1, interacts with VP1 and mediates abscisic acid-induced transcription. Proc Natl Acad Sci USA 96:15348-15353
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 15348-15353
    • Hobo, T.1    Kowyama, Y.2    Hattori, T.3
  • 63
    • 0033998921 scopus 로고    scopus 로고
    • 1-pyrroline-5- carboxylate synthetase results in increased proline accumulation and protection of plants from osmotic stress
    • 1-pyrroline-5-carboxylate synthetase results in increased proline accumulation and protection of plants from osmotic stress. Plant Physiol 122: 1129-1136
    • (2000) Plant Physiol , vol.122 , pp. 1129-1136
    • Hong, Z.1    Lakkineni, K.2    Zhang, K.3    Verma, D.P.S.4
  • 64
    • 0032078109 scopus 로고    scopus 로고
    • Protection of enzymes by α-crystallin acting as a molecular chaperone
    • Hook DWA, Harding JJ (1998) Protection of enzymes by α-crystallin acting as a molecular chaperone. Int J Biol Macromol 22:295-306
    • (1998) Int J Biol Macromol , vol.22 , pp. 295-306
    • Hook, D.W.A.1    Harding, J.J.2
  • 65
    • 0026483279 scopus 로고
    • α-Crystallin can function as a molecular chaperone
    • Horwitz J (1992) α-Crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 89:10449-10453
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 66
    • 0029379706 scopus 로고
    • Immunolocalization of freezing-tolerance-associated proteins in the cytoplasm and nucleoplasm of wheat crown tissue
    • Houde M, Daniel C, Lachapelle M, Allard F, Laliberte S, Sarhan F (1995) Immunolocalization of freezing-tolerance-associated proteins in the cytoplasm and nucleoplasm of wheat crown tissue. Plant J 8:583-593
    • (1995) Plant J , vol.8 , pp. 583-593
    • Houde, M.1    Daniel, C.2    Lachapelle, M.3    Allard, F.4    Laliberte, S.5    Sarhan, F.6
  • 67
    • 0035984065 scopus 로고    scopus 로고
    • Heterology expression of the Arabidopsis C-repeat/dehydration response element binding factor 1 gene confers elevated tolerance to chilling and oxidative stresses in transgenic tomato
    • Hsieh TH, Lee JT, Yang PT, Chiu LH, Charng YY, Wang YC, Chan MT (2002) Heterology expression of the Arabidopsis C-repeat/dehydration response element binding factor 1 gene confers elevated tolerance to chilling and oxidative stresses in transgenic tomato. Plant Physiol 129:1086-1094
    • (2002) Plant Physiol , vol.129 , pp. 1086-1094
    • Hsieh, T.H.1    Lee, J.T.2    Yang, P.T.3    Chiu, L.H.4    Charng, Y.Y.5    Wang, Y.C.6    Chan, M.T.7
  • 68
    • 0033764221 scopus 로고    scopus 로고
    • Genetic engineering of glycinebetaine production toward enhancing stress tolerance in plants: Metabolic limitations
    • Huang J, Hirji R, Adam L, Rozwadowski KL, Hammerlindl JK, Keller WA, Selvaraj G (2000) Genetic engineering of glycinebetaine production toward enhancing stress tolerance in plants: metabolic limitations. Plant Physiol 122:747-756
    • (2000) Plant Physiol , vol.122 , pp. 747-756
    • Huang, J.1    Hirji, R.2    Adam, L.3    Rozwadowski, K.L.4    Hammerlindl, J.K.5    Keller, W.A.6    Selvaraj, G.7
  • 69
    • 0001319976 scopus 로고    scopus 로고
    • The molecular basis of dehydration tolerance in plants
    • Ingram J, Bartels D (1996) The molecular basis of dehydration tolerance in plants. Annu Rev Plant Biol 47:377-403
    • (1996) Annu Rev Plant Biol , vol.47 , pp. 377-403
    • Ingram, J.1    Bartels, D.2
  • 70
    • 0026953670 scopus 로고
    • Expression of desiccation-related proteins from the resurrection plant in transgenic tobacco
    • Iturriaga G, Schneider K, Salamini F. Bartels D (1992) Expression of desiccation-related proteins from the resurrection plant in transgenic tobacco. Plant Mol Biol 20:555-558
    • (1992) Plant Mol Biol , vol.20 , pp. 555-558
    • Iturriaga, G.1    Schneider, K.2    Salamini, F.3    Bartels, D.4
  • 71
    • 0035198080 scopus 로고    scopus 로고
    • Components of the Arabidopsis C-repeat/dehydration-responsive element binding factor cold-response pathway are conserved in Brassica napus and other plant species
    • Jaglo KR, Kleff S, Amundsen KL, Zhang X, Haake V, Zhang JZ, Deits T, Thomashow MF (2001) Components of the Arabidopsis C-repeat/dehydration- responsive element binding factor cold-response pathway are conserved in Brassica napus and other plant species. Plant Physiol 127:910-917
    • (2001) Plant Physiol , vol.127 , pp. 910-917
    • Jaglo, K.R.1    Kleff, S.2    Amundsen, K.L.3    Zhang, X.4    Haake, V.5    Zhang, J.Z.6    Deits, T.7    Thomashow, M.F.8
  • 73
    • 0036009783 scopus 로고    scopus 로고
    • Arabidopsis basic leucine zipper proteins that mediate stress-responsive abscisic acid signaling
    • Kang JY, Choi HI, Im MY, Kim SY (2002) Arabidopsis basic leucine zipper proteins that mediate stress-responsive abscisic acid signaling. Plant Cell 14:343-357
    • (2002) Plant Cell , vol.14 , pp. 343-357
    • Kang, J.Y.1    Choi, H.I.2    Im, M.Y.3    Kim, S.Y.4
  • 74
    • 0032993342 scopus 로고    scopus 로고
    • Improving plant drought, salt, and freezing tolerance by gene transfer of a single stress-inducible transcription factor
    • Kasuga M, Liu Q, Miura S, Yamaguchi-Shinozaki K, Shinozaki K (1999) Improving plant drought, salt, and freezing tolerance by gene transfer of a single stress-inducible transcription factor. Nature Biotech 17:287-291
    • (1999) Nature Biotech , vol.17 , pp. 287-291
    • Kasuga, M.1    Liu, Q.2    Miura, S.3    Yamaguchi-Shinozaki, K.4    Shinozaki, K.5
  • 75
    • 0028150137 scopus 로고
    • Purification and characterization of COR85-oligomeric complex from cold-acclimated spinach
    • Kazuoka T, Oeda K (1994) Purification and characterization of COR85-oligomeric complex from cold-acclimated spinach. Plant Cell Physiol 35:601-611
    • (1994) Plant Cell Physiol , vol.35 , pp. 601-611
    • Kazuoka, T.1    Oeda, K.2
  • 76
    • 0028835509 scopus 로고
    • 1-pyrroline-5-carboxylate synthetase increase proline production and confers osmotolerance in transgenic plants
    • 1-pyrroline-5-carboxylate synthetase increase proline production and confers osmotolerance in transgenic plants. Plant Physiol 108:1387-1394
    • (1995) Plant Physiol , vol.108 , pp. 1387-1394
    • Kishor, K.P.B.1    Hong, Z.2    Miao, G.H.3    Hu, C.A.A.4    Verma, D.P.S.5
  • 77
    • 0035206163 scopus 로고    scopus 로고
    • Abiotic stress signalling pathways: Specificity and cross-talk
    • Knight H, Knight MR (2001) Abiotic stress signalling pathways: specificity and cross-talk. Trends Plant Sci 6:262-267
    • (2001) Trends Plant Sci , vol.6 , pp. 262-267
    • Knight, H.1    Knight, M.R.2
  • 78
    • 0036664584 scopus 로고    scopus 로고
    • Freezing tolerant tobacco, transformed to accumulate osmoprotectants
    • Konstantinova T, Parvanova D, Atanassov A, Djilianov D (2002) Freezing tolerant tobacco, transformed to accumulate osmoprotectants. Plant Sci 163:157-164
    • (2002) Plant Sci , vol.163 , pp. 157-164
    • Konstantinova, T.1    Parvanova, D.2    Atanassov, A.3    Djilianov, D.4
  • 79
    • 0036909761 scopus 로고    scopus 로고
    • Transcriptome changes for Arabidopsis in response to salt, osmotic, and cold stress
    • Kreps JA, Wu Y, Chang HS, Zhu T, Wang X, Harper JF (2002) Transcriptome changes for Arabidopsis in response to salt, osmotic, and cold stress. Plant Physiol 130:2129-2141
    • (2002) Plant Physiol , vol.130 , pp. 2129-2141
    • Kreps, J.A.1    Wu, Y.2    Chang, H.S.3    Zhu, T.4    Wang, X.5    Harper, J.F.6
  • 80
    • 0028949832 scopus 로고
    • Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea
    • Lee GJ, Pokala N, Vierling E (1995) Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea. J Biol Chem 270:10432-10438
    • (1995) J Biol Chem , vol.270 , pp. 10432-10438
    • Lee, G.J.1    Pokala, N.2    Vierling, E.3
  • 81
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee GJ, Roseman AM, Saibil HR, Vierling E (1997) A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J 3:659-671
    • (1997) EMBO J , vol.3 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 82
    • 0029379547 scopus 로고
    • Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis
    • Lee JH, Hübel A, Schöffl F (1995) Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis. Plant J 8:603-612
    • (1995) Plant J , vol.8 , pp. 603-612
    • Lee, J.H.1    Hübel, A.2    Schöffl, F.3
  • 83
    • 0031766869 scopus 로고    scopus 로고
    • Abscisic acid signal transduction
    • Leung J, Giraudat J (1998) Abscisic acid signal transduction. Annu Rev Plant Biol 49:199-222
    • (1998) Annu Rev Plant Biol , vol.49 , pp. 199-222
    • Leung, J.1    Giraudat, J.2
  • 84
    • 0030029354 scopus 로고    scopus 로고
    • Enhanced NaCl stress tolerance in transgenic tobacco expressing bacterial choline dehydrogenase
    • Lilius G, Holmberg N, Bülow L (1996) Enhanced NaCl stress tolerance in transgenic tobacco expressing bacterial choline dehydrogenase. Bio-Technology 14:177-180
    • (1996) Bio-Technology , vol.14 , pp. 177-180
    • Lilius, G.1    Holmberg, N.2    Bülow, L.3
  • 85
    • 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, Kasuga M, Sakuma Y, Abe H, Miura S, Yamaguchi-Shinozaki K, Shinozaki K (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    Abe, H.4    Miura, S.5    Yamaguchi-Shinozaki, K.6    Shinozaki, K.7
  • 86
    • 0034121176 scopus 로고    scopus 로고
    • A null mutation in a bZIP factor confers ABA-insensitivity in Arabidopsis thaliana
    • Lopez-Molina L, Chua NH (2000) A null mutation in a bZIP factor confers ABA-insensitivity in Arabidopsis thaliana. Plant Cell Physiol 41:541-547
    • (2000) Plant Cell Physiol , vol.41 , pp. 541-547
    • Lopez-Molina, L.1    Chua, N.H.2
  • 87
    • 0032697142 scopus 로고    scopus 로고
    • Modified expression of a carrot small heat shock protein gene, Hsp17.7, results in increased or decreased thermotolerance
    • Malik MK, Slovin JP, Hwang CH, Zimmerman JL (1999) Modified expression of a carrot small heat shock protein gene, Hsp17.7, results in increased or decreased thermotolerance. Plant J 20:89-99
    • (1999) Plant J , vol.20 , pp. 89-99
    • Malik, M.K.1    Slovin, J.P.2    Hwang, C.H.3    Zimmerman, J.L.4
  • 88
    • 0034693132 scopus 로고    scopus 로고
    • Complete protection by α-crystallin of lens sorbitol dehydrogenase undergoing thermal stress
    • Marini I, Moschini R, Corso AD, Mura U (2000) Complete protection by α-crystallin of lens sorbitol dehydrogenase undergoing thermal stress. J Biol Chem 275:32559-32565
    • (2000) J Biol Chem , vol.275 , pp. 32559-32565
    • Marini, I.1    Moschini, R.2    Corso, A.D.3    Mura, U.4
  • 89
    • 0348199154 scopus 로고    scopus 로고
    • Aquaporins and water permeability of plant membranes
    • Maurel C, (1997) Aquaporins and water permeability of plant membranes. Annu Rev Plant Biol 48:399-429
    • (1997) Annu Rev Plant Biol , vol.48 , pp. 399-429
    • Maurel, C.1
  • 90
    • 0025570130 scopus 로고
    • Drought and salt tolerance: Toward understanding and application
    • McCue KF, Hanson AD (1990) Drought and salt tolerance: toward understanding and application. Trends Biotechnol 8:358-362
    • (1990) Trends Biotechnol , vol.8 , pp. 358-362
    • McCue, K.F.1    Hanson, A.D.2
  • 91
    • 0029824775 scopus 로고    scopus 로고
    • Water-deficit tolerance and field performance of transgenic alfalfa overexpressing superoxide dismutase
    • McKersie BD, Bowley SR, Harjanto E, Leprince O (1996) Water-deficit tolerance and field performance of transgenic alfalfa overexpressing superoxide dismutase. Plant Physiol 111:1177-1181
    • (1996) Plant Physiol , vol.111 , pp. 1177-1181
    • McKersie, B.D.1    Bowley, S.R.2    Harjanto, E.3    Leprince, O.4
  • 92
    • 0032793927 scopus 로고    scopus 로고
    • Winter survival of transgenic alfalfa overexpressing superoxide dismutase
    • McKersie BD, Bowley SR, Jones KS (1999) Winter survival of transgenic alfalfa overexpressing superoxide dismutase. Plant Physiol 119:839-848
    • (1999) Plant Physiol , vol.119 , pp. 839-848
    • McKersie, B.D.1    Bowley, S.R.2    Jones, K.S.3
  • 93
    • 0034001533 scopus 로고    scopus 로고
    • Iron-superoxide dismutase expression in transgenic alfalfa increases winter survival without a detectable increase in photosynthetic oxidative stress tolerance
    • McKersie BD, Murnaghan J, Jones KS, Bowley SR (2000) Iron-superoxide dismutase expression in transgenic alfalfa increases winter survival without a detectable increase in photosynthetic oxidative stress tolerance. Plant Physiol 122:1427-1438
    • (2000) Plant Physiol , vol.122 , pp. 1427-1438
    • McKersie, B.D.1    Murnaghan, J.2    Jones, K.S.3    Bowley, S.R.4
  • 94
    • 0032825731 scopus 로고    scopus 로고
    • Betaines and related osmoprotectants: Targets for metabolic engineering of stress resistance
    • McNeil SD, Nuccio ML, Hanson AD (1999) Betaines and related osmoprotectants: targets for metabolic engineering of stress resistance: Plant Physiol 120:945-949
    • (1999) Plant Physiol , vol.120 , pp. 945-949
    • McNeil, S.D.1    Nuccio, M.L.2    Hanson, A.D.3
  • 95
    • 0037097984 scopus 로고    scopus 로고
    • In the complex family of heat stress transcription factors, HsfA1 has a unique role as master regulator of thermotolerance in tomato
    • Mishra SK, Tripp J, Winkelhaus S, Tschiersch B, Theres K, Nover L, Scharf KD (2002) In the complex family of heat stress transcription factors, HsfA1 has a unique role as master regulator of thermotolerance in tomato. Gene Dev 16:1555-1567
    • (2002) Gene Dev , vol.16 , pp. 1555-1567
    • Mishra, S.K.1    Tripp, J.2    Winkelhaus, S.3    Tschiersch, B.4    Theres, K.5    Nover, L.6    Scharf, K.D.7
  • 96
    • 0036728244 scopus 로고    scopus 로고
    • Oxidative stress, antioxidants and stress tolerance
    • Mittler R (2002) Oxidative stress, antioxidants and stress tolerance. Trends Plant Sci 7:405-410
    • (2002) Trends Plant Sci , vol.7 , pp. 405-410
    • Mittler, R.1
  • 97
    • 0033565453 scopus 로고    scopus 로고
    • Animal cell-death suppressors Bcl-xL and Ced-9 inhibit cell death in tobacco plants
    • Mitsuhara I, Malik KA, Miura M, Ohashi Y (1999) Animal cell-death suppressors Bcl-xL and Ced-9 inhibit cell death in tobacco plants. Curr Biol 9:775-778
    • (1999) Curr Biol , vol.9 , pp. 775-778
    • Mitsuhara, I.1    Malik, K.A.2    Miura, M.3    Ohashi, Y.4
  • 99
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto RI (1998) Regulation of the heat shock transcriptional response: cross talk between family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev 12:3788-3796
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 100
    • 0032477726 scopus 로고    scopus 로고
    • ATP-enhance molecular chaperone functions of the small heat shock protein human αB crystallin
    • Muchowski PJ, Clark JI (1998) ATP-enhance molecular chaperone functions of the small heat shock protein human αB crystallin. Biochemistry 95:1004-1009
    • (1998) Biochemistry , vol.95 , pp. 1004-1009
    • Muchowski, P.J.1    Clark, J.I.2
  • 101
    • 0024066710 scopus 로고
    • Abscisic acid and water stress induce the expression of a novel rice gene
    • Mundy J, Chua NH (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
  • 102
    • 0025098288 scopus 로고
    • Nuclear proteins bind conserved elements in the abscisic acid-responsive promoter of a rice rab gene
    • Mundy J, Yamaguchi-Shinozaki K, Chua, NH (1990) Nuclear proteins bind conserved elements in the abscisic acid-responsive promoter of a rice rab gene. Proc. Natl Acad Sci USA 87:406-410
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 406-410
    • Mundy, J.1    Yamaguchi-Shinozaki, K.2    Chua, N.H.3
  • 103
    • 0033386060 scopus 로고    scopus 로고
    • Distinct osmo-sensing protein kinase pathways are involved in signaling moderate and severe hyper-osmotic stress
    • Munnik T, Ligterink W, Meskiene I, Calderini O, Beyerly J, Musgrave A, Hirt H (1999) Distinct osmo-sensing protein kinase pathways are involved in signaling moderate and severe hyper-osmotic stress. Plant J 20:381-388
    • (1999) Plant J , vol.20 , pp. 381-388
    • Munnik, T.1    Ligterink, W.2    Meskiene, I.3    Calderini, O.4    Beyerly, J.5    Musgrave, A.6    Hirt, H.7
  • 104
    • 0032693585 scopus 로고    scopus 로고
    • Antisense suppression of proline degradation improves tolerance to freezing and salinity in Arabidopsis thaliana
    • Nanjo T, Kobayashia M, Yoshibab Y, Kakubaric Y, Yamaguchi-Shinozaki K, Shinozaki K (1999) Antisense suppression of proline degradation improves tolerance to freezing and salinity in Arabidopsis thaliana. FEBS Lett 461:205-210
    • (1999) FEBS Lett , vol.461 , pp. 205-210
    • Nanjo, T.1    Kobayashia, M.2    Yoshibab, Y.3    Kakubaric, Y.4    Yamaguchi-Shinozaki, K.5    Shinozaki, K.6
  • 105
    • 0035983961 scopus 로고    scopus 로고
    • Cold-regulated cereal chloroplast late embryogenesis abundant-like proteins. Molecular characterization and functional analyses
    • Ndong C, Danyluk J, Wilson KE, Pocock T, Huner NPA, Sarhan F (2002) Cold-regulated cereal chloroplast late embryogenesis abundant-like proteins. Molecular characterization and functional analyses. Plant Physiol 129:1368-1381
    • (2002) Plant Physiol , vol.129 , pp. 1368-1381
    • Ndong, C.1    Danyluk, J.2    Wilson, K.E.3    Pocock, T.4    Huner, N.P.A.5    Sarhan, F.6
  • 106
    • 0031735647 scopus 로고    scopus 로고
    • Ascorbate and glutathione: Keeping active oxygen under control
    • Noctor G, Foyer C (1998) Ascorbate and glutathione: keeping active oxygen under control. Annu Rev Plant Physiol Plant Mol Biol 49:249-279
    • (1998) Annu Rev Plant Physiol Plant Mol Biol , vol.49 , pp. 249-279
    • Noctor, G.1    Foyer, C.2
  • 107
    • 0034804489 scopus 로고    scopus 로고
    • Arabidopsis and the heat stress transcription factor world: How many heat stress transcription factors do we need?
    • Nover L, Bharti K, Döring P, Mishra SK, Ganguli A, Scharf KD (2001) Arabidopsis and the heat stress transcription factor world: How many heat stress transcription factors do we need? Cell Stress Chaperones 6:177-189
    • (2001) Cell Stress Chaperones , vol.6 , pp. 177-189
    • Nover, L.1    Bharti, K.2    Döring, P.3    Mishra, S.K.4    Ganguli, A.5    Scharf, K.D.6
  • 108
    • 0032212062 scopus 로고    scopus 로고
    • The endogenous choline supply limits glycine betaine synthesis in transgenic tobacco expressing choline monooxygenase
    • Nuccio ML, Russell BL, Nolte KD, Rathinasabapathi B, Gage DA, Hanson AD (1998) The endogenous choline supply limits glycine betaine synthesis in transgenic tobacco expressing choline monooxygenase. Plant J 16:487-498
    • (1998) Plant J , vol.16 , pp. 487-498
    • Nuccio, M.L.1    Russell, B.L.2    Nolte, K.D.3    Rathinasabapathi, B.4    Gage, D.A.5    Hanson, A.D.6
  • 109
    • 0034541782 scopus 로고    scopus 로고
    • A novel aldose/aldehyde reductase protects transgenic plants against lipid peroxidation under chemical and drought stresses
    • Oberschall A, Deák M, Török K, Sass L, Vass I, Kovács I, Fehér A, Dudits D, Horváth GV (2000) A novel aldose/aldehyde reductase protects transgenic plants against lipid peroxidation under chemical and drought stresses. Plant J 24:437-446
    • (2000) Plant J , vol.24 , pp. 437-446
    • Oberschall, A.1    Deák, M.2    Török, K.3    Sass, L.4    Vass, I.5    Kovács, I.6    Fehér, A.7    Dudits, D.8    Horváth, G.V.9
  • 110
    • 0034863456 scopus 로고    scopus 로고
    • Constitutive over-expression of AtGSK1 induces NaCl stress responses in the absence of NaCl stress and results in enhanced NaCl tolerance in Arabidopsis
    • Piao HL, Lim JH, Kim SJ, Cheong GW, Hwang I (2001) Constitutive over-expression of AtGSK1 induces NaCl stress responses in the absence of NaCl stress and results in enhanced NaCl tolerance in Arabidopsis. Plant J 27:305-314
    • (2001) Plant J , vol.27 , pp. 305-314
    • Piao, H.L.1    Lim, J.H.2    Kim, S.J.3    Cheong, G.W.4    Hwang, I.5
  • 111
    • 0030019049 scopus 로고    scopus 로고
    • Overexpression of copper/zinc superoxide dismutase in the cytosol of transgenic tobacco confers partial resistance to ozone-induced foliar necrosis
    • Pitcher LH, Zilinskas BA (1996) Overexpression of copper/zinc superoxide dismutase in the cytosol of transgenic tobacco confers partial resistance to ozone-induced foliar necrosis. Plant Physiol 110:583-588
    • (1996) Plant Physiol , vol.110 , pp. 583-588
    • Pitcher, L.H.1    Zilinskas, B.A.2
  • 112
    • 0031842946 scopus 로고    scopus 로고
    • HSF3, a new heat shock factor from Arabidopsis thaliana, derepresses the heat shock response and confers thermotolerance when overexpressed in transgenic plants
    • Prändl R, Hinderhofer K, Eggers-Schumacher G, Schöffl F (1998) HSF3, a new heat shock factor from Arabidopsis thaliana, derepresses the heat shock response and confers thermotolerance when overexpressed in transgenic plants. Mol Gen Genet 258:269-278
    • (1998) Mol Gen Genet , vol.258 , pp. 269-278
    • Prändl, R.1    Hinderhofer, K.2    Eggers-Schumacher, G.3    Schöffl, F.4
  • 114
    • 0036747241 scopus 로고    scopus 로고
    • Enhanced resistance to salt, cold and wound stresses by overproduction of animal cell death suppressors Bcl-xL and Ced-9 in tobacco cells - Their possible contribution through improved function of organella
    • Qiao J, Mitsuhara I, Yazaki Y, Sakano K, Gotoh Y, Miura M, Ohashi Y (2002) Enhanced resistance to salt, cold and wound stresses by overproduction of animal cell death suppressors Bcl-xL and Ced-9 in tobacco cells - their possible contribution through improved function of organella. Plant Cell Physiol 43:992-1005
    • (2002) Plant Cell Physiol , vol.43 , pp. 992-1005
    • Qiao, J.1    Mitsuhara, I.2    Yazaki, Y.3    Sakano, K.4    Gotoh, Y.5    Miura, M.6    Ohashi, Y.7
  • 116
    • 0030771838 scopus 로고    scopus 로고
    • Overexpression of glutathione S-transferase/glutathione peroxidase enhances the growth of transgenic tobacco seedlings during stress
    • Roxas VP, Smith RK Jr, Allen ER, Allen RD (1997) Overexpression of glutathione S-transferase/glutathione peroxidase enhances the growth of transgenic tobacco seedlings during stress. Nature Biotech 15:988-991
    • (1997) Nature Biotech , vol.15 , pp. 988-991
    • Roxas, V.P.1    Smith Jr., R.K.2    Allen, E.R.3    Allen, R.D.4
  • 118
    • 0031989203 scopus 로고    scopus 로고
    • Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth
    • Russell BL, Rathinasabapathi B, Hanson AD (1998) Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth. Plant Physiol 116:859-865
    • (1998) Plant Physiol , vol.116 , pp. 859-865
    • Russell, B.L.1    Rathinasabapathi, B.2    Hanson, A.D.3
  • 119
    • 0032090396 scopus 로고    scopus 로고
    • Expression of small heat-shock proteins at low temperatures
    • Sabehat A, Lurie S, Weiss D (1998) Expression of small heat-shock proteins at low temperatures. Plant Physiol 117:651-658
    • (1998) Plant Physiol , vol.117 , pp. 651-658
    • Sabehat, A.1    Lurie, S.2    Weiss, D.3
  • 120
    • 0033624156 scopus 로고    scopus 로고
    • 2+-dependent protein kinase confers both cold and salt/drought tolerance on rice plants
    • 2+-dependent protein kinase confers both cold and salt/drought tolerance on rice plants. Plant J 23:319-327
    • (2000) Plant J , vol.23 , pp. 319-327
    • Saijo, Y.1    Hata, S.2    Kyozuka, J.3    Shimamoto, K.4    Izui, K.5
  • 121
    • 0035142718 scopus 로고    scopus 로고
    • The use of bacterial choline oxidase, a glycinebetaine-synthesizing enzyme, to create stress-resistant transgenic plants
    • Sakamoto A, Murata N (2001) The use of bacterial choline oxidase, a glycinebetaine-synthesizing enzyme, to create stress-resistant transgenic plants. Plant Physiol 125:180-188
    • (2001) Plant Physiol , vol.125 , pp. 180-188
    • Sakamoto, A.1    Murata, N.2
  • 122
    • 0036183314 scopus 로고    scopus 로고
    • The role of glycine betaine in the protection of plants from stress: Clues from transgenic plants
    • Sakamoto A, Murata N (2002) The role of glycine betaine in the protection of plants from stress: clues from transgenic plants. Plant Cell Environ 25:163-171
    • (2002) Plant Cell Environ , vol.25 , pp. 163-171
    • Sakamoto, A.1    Murata, N.2
  • 123
    • 6544290514 scopus 로고    scopus 로고
    • Metabolic engineering of rice leading to biosynthesis of glycinebetaine and tolerance to salt and cold
    • Sakamoto A, Alia, Murata N (1998) Metabolic engineering of rice leading to biosynthesis of glycinebetaine and tolerance to salt and cold. Plant Mol Biol 38:1011-1019
    • (1998) Plant Mol Biol , vol.38 , pp. 1011-1019
    • Sakamoto, A.1    Alia2    Murata, N.3
  • 124
    • 0034131202 scopus 로고    scopus 로고
    • Transformation of Arabidopsis with the codA gene for choline oxidase enhances freezing tolerance of plants
    • Sakamoto A, Valverde R, Alia, Chen THH, Murata N (2000) Transformation of Arabidopsis with the codA gene for choline oxidase enhances freezing tolerance of plants. Plant J 22:449-453
    • (2000) Plant J , vol.22 , pp. 449-453
    • Sakamoto, A.1    Valverde, R.2    Alia3    Chen, T.H.H.4    Murata, N.5
  • 125
    • 0032133306 scopus 로고    scopus 로고
    • Regulation of the heat-shock response
    • Schöffl F, Prändl R, Reindl A (1998) Regulation of the heat-shock response. Plant Physiol 117:1135-1141
    • (1998) Plant Physiol , vol.117 , pp. 1135-1141
    • Schöffl, F.1    Prändl, R.2    Reindl, A.3
  • 126
  • 129
    • 0031403567 scopus 로고    scopus 로고
    • Increased salt and drought tolerance by D-ononitol production in transgenic Nicotiana tabacum L.
    • Sheveleva E, Chmara W, Bohnert HJ, Jensen RG (1997) Increased salt and drought tolerance by D-ononitol production in transgenic Nicotiana tabacum L. Plant Physiol 115:1211-1219
    • (1997) Plant Physiol , vol.115 , pp. 1211-1219
    • Sheveleva, E.1    Chmara, W.2    Bohnert, H.J.3    Jensen, R.G.4
  • 133
    • 0037228275 scopus 로고    scopus 로고
    • + antiporter gene improves salt tolerance in Arabidopsis thaliana
    • + antiporter gene improves salt tolerance in Arabidopsis thaliana. Nature Biotech 21:81-85
    • (2003) Nature Biotech , vol.21 , pp. 81-85
    • Shi, H.1    Lee, B.H.2    Wu, S.J.3    Zhu, J.K.4
  • 134
    • 0031397805 scopus 로고    scopus 로고
    • Gene expression and signal transduction in water-stress response
    • Shinozaki K, Yamaguchi-Shinozaki K (1997) Gene expression and signal transduction in water-stress response. Plant Physiol 115:327-334
    • (1997) Plant Physiol , vol.115 , pp. 327-334
    • Shinozaki, K.1    Yamaguchi-Shinozaki, K.2
  • 135
    • 0034028259 scopus 로고    scopus 로고
    • Molecular responses to dehydration and low temperature: Differences and cross-talk between two stress signalling pathways
    • Shinozaki K, Yamaguchi-Shinozaki K (2000) Molecular responses to dehydration and low temperature: differences and cross-talk between two stress signalling pathways. Curr Opin Plant Biol 3:217-223
    • (2000) Curr Opin Plant Biol , vol.3 , pp. 217-223
    • Shinozaki, K.1    Yamaguchi-Shinozaki, K.2
  • 136
    • 0034640863 scopus 로고    scopus 로고
    • Improved biomass productivity and water use efficiency under water deficit conditions in transgenic wheat constitutively expressing the barley HVA1 gene
    • Sivamani E, Bahieldin A, Wraithc JM, Al-Niemia T, Dyera WE, Hod THD, Qu R (2000) Improved biomass productivity and water use efficiency under water deficit conditions in transgenic wheat constitutively expressing the barley HVA1 gene. Plant Sci 155:1-9
    • (2000) Plant Sci , vol.155 , pp. 1-9
    • Sivamani, E.1    Bahieldin, A.2    Wraithc, J.M.3    Al-Niemia, T.4    Dyera, W.E.5    Hod, T.H.D.6    Qu, R.7
  • 137
    • 0025443920 scopus 로고
    • Gene expression in response to abscisic acid and osmotic stress
    • Skriver K, Mundy J (1990) Gene expression in response to abscisic acid and osmotic stress. Plant Cell 2:503-512
    • (1990) Plant Cell , vol.2 , pp. 503-512
    • Skriver, K.1    Mundy, J.2
  • 138
    • 0031898169 scopus 로고    scopus 로고
    • Plant resistance to environmental stress
    • Smirnoff N (1998) Plant resistance to environmental stress. Curr Opin Biotech 9:214-219
    • (1998) Curr Opin Biotech , vol.9 , pp. 214-219
    • Smirnoff, N.1
  • 139
    • 0033801457 scopus 로고    scopus 로고
    • Chaperone activity of tobacco HSP18, a small heat-shock protein, is inhibited by ATP
    • Smýkal P, Mašín J, Hrdý I, Konopásek I, Žárský V (2000) Chaperone activity of tobacco HSP18, a small heat-shock protein, is inhibited by ATP. Plant J 23:703-713
    • (2000) Plant J , vol.23 , pp. 703-713
    • Smýkal, P.1    Mašín, J.2    Hrdý, I.3    Konopásek, I.4    Žárský, V.5
  • 141
    • 0031017671 scopus 로고    scopus 로고
    • Arabidopsis thaliana CBF1 encodes an AP2 domain-containing transcriptional activator that binds to the C-repeat/DRE, a cis-acting DNA regulatory element that stimulates transcription in response to low temperature and water deficit
    • Stockinger EJ, Gilmour SJ, Thomashow MF (1997) Arabidopsis thaliana CBF1 encodes an AP2 domain-containing transcriptional activator that binds to the C-repeat/DRE, a cis-acting DNA regulatory element that stimulates transcription in response to low temperature and water deficit. Proc Natl Acad Sci USA 94:1035-40
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1035-1040
    • Stockinger, E.J.1    Gilmour, S.J.2    Thomashow, M.F.3
  • 142
    • 0034711315 scopus 로고    scopus 로고
    • Chaperone activity and homo- and hetero-oligomer formation of bacterial small heat shock proteins
    • Studer S, Narberhaus F (2000) Chaperone activity and homo- and hetero-oligomer formation of bacterial small heat shock proteins. J Biol Chem 275:37212-37218
    • (2000) J Biol Chem , vol.275 , pp. 37212-37218
    • Studer, S.1    Narberhaus, F.2
  • 143
    • 0033618864 scopus 로고    scopus 로고
    • Overexpression of DnaK from a halotolerant cyanobacterium Aphanothece halophytice acquires resistance to salt stress in transgenic tobacco plants
    • Sugino M, Hibino T, Tanaka Y, Nii N, Takabe T (1999) Overexpression of DnaK from a halotolerant cyanobacterium Aphanothece halophytice acquires resistance to salt stress in transgenic tobacco plants. Plant Sci 146:81-88
    • (1999) Plant Sci , vol.146 , pp. 81-88
    • Sugino, M.1    Hibino, T.2    Tanaka, Y.3    Nii, N.4    Takabe, T.5
  • 144
    • 0034789981 scopus 로고    scopus 로고
    • At-HSP17.6A, encoding a small heat-shock protein in Arabidopsis, can enhance osmotolerance upon overexpression
    • Sun W, Bernard C, van de Cotte B, Van Montagu M, Verbruggen, N (2001) At-HSP17.6A, encoding a small heat-shock protein in Arabidopsis, can enhance osmotolerance upon overexpression. Plant J 27:407-415
    • (2001) Plant J , vol.27 , pp. 407-415
    • Sun, W.1    Bernard, C.2    Van De Cotte, B.3    Van Montagu, M.4    Verbruggen, N.5
  • 145
    • 0032013798 scopus 로고    scopus 로고
    • The chloroplast small heat-shock protein oligomer is not phosphorylated and does not dissociate during heat stress in vivo
    • Suzuki TC, Denise C, Krawitz DC, Vierling E (1998) The chloroplast small heat-shock protein oligomer is not phosphorylated and does not dissociate during heat stress in vivo. Plant Physiol 116:1151-1161
    • (1998) Plant Physiol , vol.116 , pp. 1151-1161
    • Suzuki, T.C.1    Denise, C.2    Krawitz, D.C.3    Vierling, E.4
  • 146
    • 0032718566 scopus 로고    scopus 로고
    • Energization of plant cell membranes by H-pumping ATPases: Regulation and biosynthesis
    • Sze H, Lia X, Palmgrenb MG (1999) Energization of plant cell membranes by H-pumping ATPases: regulation and biosynthesis. Plant Cell 11:677-690
    • (1999) Plant Cell , vol.11 , pp. 677-690
    • Sze, H.1    Lia, X.2    Palmgrenb, M.G.3
  • 147
    • 0027464813 scopus 로고
    • Stress protection of transgenic tobacco by production of the osmolyte mannitol
    • Tarczynski MC, Jensen RG, Bohnert HJ (1993) Stress protection of transgenic tobacco by production of the osmolyte mannitol. Science 259:508-510
    • (1993) Science , vol.259 , pp. 508-510
    • Tarczynski, M.C.1    Jensen, R.G.2    Bohnert, H.J.3
  • 148
    • 0032161654 scopus 로고    scopus 로고
    • Role of cold-responsive genes in plant freezing tolerance
    • Thomashow MF (1998) Role of cold-responsive genes in plant freezing tolerance. Plant Physiol 118:1-7
    • (1998) Plant Physiol , vol.118 , pp. 1-7
    • Thomashow, M.F.1
  • 149
    • 0033498862 scopus 로고    scopus 로고
    • Plant cold acclimation: Freezing tolerance genes and regulatory mechanisms
    • Thomashow MF (1999) Plant cold acclimation: freezing tolerance genes and regulatory mechanisms. Annu Rev Plant Biol 50:571-599
    • (1999) Annu Rev Plant Biol , vol.50 , pp. 571-599
    • Thomashow, M.F.1
  • 152
    • 0032971712 scopus 로고    scopus 로고
    • Plant aquaporins: Their molecular biology, biophysics and significance for plant water relations
    • Tyerman SD, Bohnert HJ, Maurel C, Steudle E, Smith JAC (1999) Plant aquaporins: their molecular biology, biophysics and significance for plant water relations. J Exp Bot 50:1055-1071
    • (1999) J Exp Bot , vol.50 , pp. 1055-1071
    • Tyerman, S.D.1    Bohnert, H.J.2    Maurel, C.3    Steudle, E.4    Smith, J.A.C.5
  • 153
    • 0034633775 scopus 로고    scopus 로고
    • Novel Arabidopsis bZIP transcription factors involved in an abscisic-acid-dependent signal transduction pathway under drought and high salinity conditions
    • Uno Y, Furihata T, Abe H, Yoshida R, Shinozaki K, Yamaguchi-Shinozaki K (2000) Novel Arabidopsis bZIP transcription factors involved in an abscisic-acid-dependent signal transduction pathway under drought and high salinity conditions. Proc Natl Acad Sci USA 97:11632-11637
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11632-11637
    • Uno, Y.1    Furihata, T.2    Abe, H.3    Yoshida, R.4    Shinozaki, K.5    Yamaguchi-Shinozaki, K.6
  • 154
    • 0030452648 scopus 로고    scopus 로고
    • Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-superoxide dismutase in chloroplasts
    • Van Camp W, Capiau K, Van Montagu M, Inze D, Slooten L (1996) Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-superoxide dismutase in chloroplasts. Plant Physiol 112:1703-1714
    • (1996) Plant Physiol , vol.112 , pp. 1703-1714
    • Van Camp, W.1    Capiau, K.2    Van Montagu, M.3    Inze, D.4    Slooten, L.5
  • 155
    • 0032079487 scopus 로고    scopus 로고
    • The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
    • Veinger L, Diamant S, Buchner J, Goloubinoff P (1998) The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J Biol Chem 273:11032-11037
    • (1998) J Biol Chem , vol.273 , pp. 11032-11037
    • Veinger, L.1    Diamant, S.2    Buchner, J.3    Goloubinoff, P.4
  • 156
    • 0000321971 scopus 로고
    • The roles of heat-shock proteins in plants
    • Vierling E (1991) The roles of heat-shock proteins in plants. Annu Rev Plant Biol 42:579-620
    • (1991) Annu Rev Plant Biol , vol.42 , pp. 579-620
    • Vierling, E.1
  • 157
    • 0026843754 scopus 로고
    • Plant responses to environmental stress
    • Vierling E, Kimpel JA (1992) Plant responses to environmental stress. Curr Opin Biotech 3:164-170
    • (1992) Curr Opin Biotech , vol.3 , pp. 164-170
    • Vierling, E.1    Kimpel, J.A.2
  • 158
    • 0037888827 scopus 로고    scopus 로고
    • Biotechnology of plant osmotic stress tolerance: Physiological and molecular considerations
    • Wang WX, Vinocur B, Shoseyov O, Altman A (2001a) Biotechnology of plant osmotic stress tolerance: physiological and molecular considerations. Acta Hort 560:285-292
    • (2001) Acta Hort , vol.560 , pp. 285-292
    • Wang, W.X.1    Vinocur, B.2    Shoseyov, O.3    Altman, A.4
  • 159
    • 0346898246 scopus 로고    scopus 로고
    • Denaturate stable and/or protease resistant, chaperone-like oligomeric proteins, polynucleotides encoding same and their uses. Provisional Patent Application No. 60/272,771. USA
    • Wang WX, Pelah D, Alergand T, Shoseyov O, Altman A (2001b) Denaturate stable and/or protease resistant, chaperone-like oligomeric proteins, polynucleotides encoding same and their uses. Provisional Patent Application No. 60/272,771. USA
    • (2001)
    • Wang, W.X.1    Pelah, D.2    Alergand, T.3    Shoseyov, O.4    Altman, A.5
  • 160
    • 0036773161 scopus 로고    scopus 로고
    • Characterization of SP1, a stress-responsive, boiling-soluble, homo-oligomeric protein from aspen (Populus tremula L.)
    • Wang WX, Pelah D, Alergand T, Shoseyov O, Altman A (2002) Characterization of SP1, a stress-responsive, boiling-soluble, homo-oligomeric protein from aspen (Populus tremula L.). Plant Physiol 130:865-875
    • (2002) Plant Physiol , vol.130 , pp. 865-875
    • Wang, W.X.1    Pelah, D.2    Alergand, T.3    Shoseyov, O.4    Altman, A.5
  • 161
    • 0348158667 scopus 로고    scopus 로고
    • Abiotic resistance and chaperones: Possible physiological role of SP1, a stable and stabilizing protein from Populus
    • Vasil IK (ed). Kluwer, Dordrecht
    • Wang WX, Barak T, Vinocur B, Shoseyov O, Altman A (2003) Abiotic resistance and chaperones: possible physiological role of SP1, a stable and stabilizing protein from Populus. In: Vasil IK (ed) Plant biotechnology 2000 and beyond. Kluwer, Dordrecht, pp 439-443
    • (2003) Plant Biotechnology 2000 and Beyond , pp. 439-443
    • Wang, W.X.1    Barak, T.2    Vinocur, B.3    Shoseyov, O.4    Altman, A.5
  • 162
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters ER, Lee GJ, Vierling E (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
  • 163
    • 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, Duan X, Wang B, Hong B, Ho THD, Wu R (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
  • 164
    • 0037188555 scopus 로고    scopus 로고
    • A rice spotted leaf gene, Sp17, encodes a heat stress transcription factor protein
    • Yamanouchi U, Yano M, Lin H, Ashikari M, Yamada K (2002) A rice spotted leaf gene, Sp17, encodes a heat stress transcription factor protein. Proc Natl Acad Sci USA 99:7530-7535
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7530-7535
    • Yamanouchi, U.1    Yano, M.2    Lin, H.3    Ashikari, M.4    Yamada, K.5
  • 165
    • 0034899261 scopus 로고    scopus 로고
    • Transgenic salt-tolerant tomato plants accumulate salt in foliage but not in fruit
    • Zhang HX, Blumwald E (2001) Transgenic salt-tolerant tomato plants accumulate salt in foliage but not in fruit. Nature Biotech 19:765-768
    • (2001) Nature Biotech , vol.19 , pp. 765-768
    • Zhang, H.X.1    Blumwald, E.2
  • 166
    • 0035940423 scopus 로고    scopus 로고
    • Engineering salt-tolerant Brassica plants: Characterization of yield and seed oil quality in transgenic plants with increased vacuolar sodium accumulation
    • Zhang HX, Hodson JN, Williams JP, Blumwald E (2001) Engineering salt-tolerant Brassica plants: characterization of yield and seed oil quality in transgenic plants with increased vacuolar sodium accumulation. Proc Natl Acad Sci USA 98:12832-12836
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12832-12836
    • Zhang, H.X.1    Hodson, J.N.2    Williams, J.P.3    Blumwald, E.4
  • 167
    • 0035213385 scopus 로고    scopus 로고
    • Plant salt tolerance
    • Zhu JK (2001a) Plant salt tolerance. Trends Plant Sci 6:66-71
    • (2001) Trends Plant Sci , vol.6 , pp. 66-71
    • Zhu, J.K.1
  • 168
    • 0034865459 scopus 로고    scopus 로고
    • Cell signaling under salt, water and cold stresses
    • Zhu JK (2001b) Cell signaling under salt, water and cold stresses. Curr Opin Plant Biol 4:401-406
    • (2001) Curr Opin Plant Biol , vol.4 , pp. 401-406
    • Zhu, J.K.1
  • 169
    • 0036999615 scopus 로고    scopus 로고
    • Salt and drought stress signal transduction in plants
    • Zhu JK (2002) Salt and drought stress signal transduction in plants. Annu Rev Plant Biol 53:247-73
    • (2002) Annu Rev Plant Biol , vol.53 , pp. 247-273
    • Zhu, J.K.1
  • 171
    • 0033485271 scopus 로고    scopus 로고
    • Plant ion channels: From molecular structures to physiological functions
    • Zimmermann S, Sentenac H (1999) Plant ion channels: from molecular structures to physiological functions. Curr Opin Plant Biol 2:477-482
    • (1999) Curr Opin Plant Biol , vol.2 , pp. 477-482
    • Zimmermann, S.1    Sentenac, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.