메뉴 건너뛰기




Volumn 36, Issue 6, 1998, Pages 885-895

Molecular cloning of a novel heat induced/chilling tolerance related cDNA in tomato fruit by use of mRNA differential display

Author keywords

Chilling injury; Heat shock protein; Tomato

Indexed keywords

CLONING; COLD TOLERANCE; DNA ANALYSIS; GENETIC ANALYSIS; HEAT SHOCK PROTEIN; HEAT TOLERANCE; MESSENGER RNA; SOUTHERN BLOTTING;

EID: 0032055785     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005954909011     Document Type: Article
Times cited : (41)

References (73)
  • 1
    • 1842413446 scopus 로고
    • Amplification of the human glutathione s-transferase-pi cDNA from a Agt 11 cDNA library with the Expand™ Long Template PCR system
    • Ali-Osman F, Akande O: Amplification of the human glutathione s-transferase-pi cDNA from a Agt 11 cDNA library with the Expand™ Long Template PCR system. Biochemica 4: 28 (1995).
    • (1995) Biochemica , vol.4 , pp. 28
    • Ali-Osman, F.1    Akande, O.2
  • 2
    • 0027131328 scopus 로고
    • Tissue-specific expression of sunflower heat shock proteins in response to water stress
    • Almoguera C, Coca MA, Jordano J: Tissue-specific expression of sunflower heat shock proteins in response to water stress. Plant J 4: 947-958 (1993).
    • (1993) Plant J , vol.4 , pp. 947-958
    • Almoguera, C.1    Coca, M.A.2    Jordano, J.3
  • 4
    • 0027213851 scopus 로고
    • Identification ofdifferential expressed mRNA species by an improved display technique (DDRT-PCR)
    • Bauer D, Muller H, Reich J, Riedel H, Ahrenkiel V, Warthoe P, Strauss M: Identification ofdifferential expressed mRNA species by an improved display technique (DDRT-PCR). Nucl Acids Res 21: 4272-4280 (1993).
    • (1993) Nucl Acids Res , vol.21 , pp. 4272-4280
    • Bauer, D.1    Muller, H.2    Reich, J.3    Riedel, H.4    Ahrenkiel, V.5    Warthoe, P.6    Strauss, M.7
  • 5
    • 0027357772 scopus 로고
    • Characterization of chilling-acclimation-related proteins in soybean and identification of one as a member of the heat shock protein (HSP 70) family
    • Cabane M, Calvet P, Vincens P, Boudet AM: Characterization of chilling-acclimation-related proteins in soybean and identification of one as a member of the heat shock protein (HSP 70) family. Planta 190: 346-353 (1993).
    • (1993) Planta , vol.190 , pp. 346-353
    • Cabane, M.1    Calvet, P.2    Vincens, P.3    Boudet, A.M.4
  • 6
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen GB, Ren R, Baltimore D: Modular binding domains in signal transduction proteins. Cell 80: 237-248 (1995).
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 7
    • 0028854975 scopus 로고
    • Heat shock proteins and chilling sensitivity of mung bean hypocotyls
    • Collins GG, Nie X, Saltviet ME: Heat shock proteins and chilling sensitivity of mung bean hypocotyls. J Exp Bot 46: 795-802 (1995).
    • (1995) J Exp Bot , vol.46 , pp. 795-802
    • Collins, G.G.1    Nie, X.2    Saltviet, M.E.3
  • 8
    • 0029839609 scopus 로고    scopus 로고
    • Characterization of three heat-shock-protein genes and their developmental regulation during somatic empryogenesis in white spruce
    • Dong J-Z, Dunstan DI: Characterization of three heat-shock-protein genes and their developmental regulation during somatic empryogenesis in white spruce. Planta 200: 85-91 (1996).
    • (1996) Planta , vol.200 , pp. 85-91
    • Dong, J.-Z.1    Dunstan, D.I.2
  • 9
    • 0002594984 scopus 로고
    • A rapid DNA isolation procedure for small quantitites of fresh leaf tissues
    • Doyle JJ, Doyle JL: A rapid DNA isolation procedure for small quantitites of fresh leaf tissues. Phytochem Bull 19: 11-15 (1987).
    • (1987) Phytochem Bull , vol.19 , pp. 11-15
    • Doyle, J.J.1    Doyle, J.L.2
  • 11
    • 0027638752 scopus 로고
    • Identification and genetic analysis of normal and mutant phytoene synthase genes of tomato by sequencing, complementation and co-suppression
    • Fray RG, Grierson D: Identification and genetic analysis of normal and mutant phytoene synthase genes of tomato by sequencing, complementation and co-suppression. Plant Mol Biol 22: 589-602 (1993).
    • (1993) Plant Mol Biol , vol.22 , pp. 589-602
    • Fray, R.G.1    Grierson, D.2
  • 14
    • 6844223943 scopus 로고
    • The properties and function of rapidly-labeled nuclear RNA
    • Grierson D, Covey S: The properties and function of rapidly-labeled nuclear RNA. Planta 130: 317-321 (1976).
    • (1976) Planta , vol.130 , pp. 317-321
    • Grierson, D.1    Covey, S.2
  • 15
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU: Molecular chaperones in cellular protein folding. Nature 381: 571-580 (1996).
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 16
    • 0027434618 scopus 로고
    • Localization of small heat-shock proteins to the higher plant endomembrane system
    • Helm KW, Lafayette PR, Nagao RT, Key JL, Vierling E: Localization of small heat-shock proteins to the higher plant endomembrane system. Mol Cell Biol 13: 238-247 (1993).
    • (1993) Mol Cell Biol , vol.13 , pp. 238-247
    • Helm, K.W.1    Lafayette, P.R.2    Nagao, R.T.3    Key, J.L.4    Vierling, E.5
  • 17
    • 0008155279 scopus 로고
    • Effect of pre- and interposed warming on chilling injury, respiratory rate and membrane permeability of cucumber fruits during cold storage
    • Hirose T: Effect of pre- and interposed warming on chilling injury, respiratory rate and membrane permeability of cucumber fruits during cold storage. J Jpn Soc Hort Sci 53: 459-466 (1985).
    • (1985) J Jpn Soc Hort Sci , vol.53 , pp. 459-466
    • Hirose, T.1
  • 18
    • 0001786418 scopus 로고
    • Low-temperature injury and the storage of ripening tomatoes
    • Hobson GE: Low-temperature injury and the storage of ripening tomatoes. J Hort Sci 62: 55-62 (1987).
    • (1987) J Hort Sci , vol.62 , pp. 55-62
    • Hobson, G.E.1
  • 19
    • 0028859629 scopus 로고
    • Characterization and physiological function of class I low-molecular-mass, heat shock protein complex in soybean
    • Jinn TL, Chen YM, Lin CY: Characterization and physiological function of class I low-molecular-mass, heat shock protein complex in soybean. Plant Physiol 108: 693-701 (1995).
    • (1995) Plant Physiol , vol.108 , pp. 693-701
    • Jinn, T.L.1    Chen, Y.M.2    Lin, C.Y.3
  • 20
    • 0029278049 scopus 로고
    • Characterization of cDNA clones for differentially expressed genes in embryos of dormant and nondormant Avena fatua L. caryopses
    • Johnson RR, Cranston HJ, Chaverra ME, Dyer WE: Characterization of cDNA clones for differentially expressed genes in embryos of dormant and nondormant Avena fatua L. caryopses. Plant Mol Biol 28: 113-122 (1995).
    • (1995) Plant Mol Biol , vol.28 , pp. 113-122
    • Johnson, R.R.1    Cranston, H.J.2    Chaverra, M.E.3    Dyer, W.E.4
  • 21
    • 0023650367 scopus 로고
    • Putative polyadenylation signals in nuclear genes of higher plants: A compilation and analysis
    • Joshi CP: Putative polyadenylation signals in nuclear genes of higher plants: a compilation and analysis. Nucl Acid Res 15: 9627-9640 (1987).
    • (1987) Nucl Acid Res , vol.15 , pp. 9627-9640
    • Joshi, C.P.1
  • 24
    • 0001316146 scopus 로고
    • Structure and light-induced expression of a small heat-shock protein gene of Pharbitis nil
    • Krishna P, Felsheim RF, Larkin JC, Das A: Structure and light-induced expression of a small heat-shock protein gene of Pharbitis nil. Plant Physiol 100: 1772-1779 (1992).
    • (1992) Plant Physiol , vol.100 , pp. 1772-1779
    • Krishna, P.1    Felsheim, R.F.2    Larkin, J.C.3    Das, A.4
  • 25
    • 0029106880 scopus 로고
    • Cold-induced accumulation of HSP90 transcripts in Brassica napus
    • KrishnaP, Sacco M, Cherutti JF, Hill S: Cold-induced accumulation of HSP90 transcripts in Brassica napus. Plant Physiol 107: 915-923 (1995).
    • (1995) Plant Physiol , vol.107 , pp. 915-923
    • KrishnaP1    Sacco, M.2    Cherutti, J.F.3    Hill, S.4
  • 26
    • 0030039706 scopus 로고    scopus 로고
    • Molecular characterization of cDNAs encoding lowmolecular-weight heat shock proteins of soybean
    • LaFayette PR, Nagao RT, O'Grady K, Vierling E, Key JL: Molecular characterization of cDNAs encoding lowmolecular-weight heat shock proteins of soybean. Plant Mol Biol 30: 159-169 (1996).
    • (1996) Plant Mol Biol , vol.30 , pp. 159-169
    • LaFayette, P.R.1    Nagao, R.T.2    O'Grady, K.3    Vierling, E.4    Key, J.L.5
  • 27
    • 0000130711 scopus 로고
    • Effect of temperature conditioning on chilling injury of cucumber cotyledons
    • Lafuente MT, Belver A, Guye MG, Saltveit ME: Effect of temperature conditioning on chilling injury of cucumber cotyledons. Plant Physiol 95: 443-449 (1991).
    • (1991) Plant Physiol , vol.95 , pp. 443-449
    • Lafuente, M.T.1    Belver, A.2    Guye, M.G.3    Saltveit, M.E.4
  • 28
    • 0025294956 scopus 로고
    • A cDNA clone from Pisum sativum encoding a low molecular weight heat shock protein
    • Lauzon LM, Helm KW, Vierling E: A cDNA clone from Pisum sativum encoding a low molecular weight heat shock protein. Nucl Acids Res 18: 4274 (1990).
    • (1990) Nucl Acids Res , vol.18 , pp. 4274
    • Lauzon, L.M.1    Helm, K.W.2    Vierling, E.3
  • 29
    • 0028949832 scopus 로고
    • Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea
    • Lee GJ, Pokala N, Vierling E: Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea. J Biol Chem 270: 10432-10438 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 10432-10438
    • Lee, G.J.1    Pokala, N.2    Vierling, E.3
  • 30
    • 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, Hubel A, Schoffl F: 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).
    • (1995) Plant J , vol.8 , pp. 603-612
    • Lee, J.H.1    Hubel, A.2    Schoffl, F.3
  • 31
    • 0028675574 scopus 로고
    • A soybean 101-kD heat shock protein complements a yeast HSP104 deletion mutant in acquiring thermoterance
    • Lee, Y-RL, Nagao RT, Key JL: A soybean 101-kD heat shock protein complements a yeast HSP104 deletion mutant in acquiring thermoterance. Plant Cell 6: 1889-1897 (1994).
    • (1994) Plant Cell , vol.6 , pp. 1889-1897
    • Lee, Y.-R.L.1    Nagao, R.T.2    Key, J.L.3
  • 32
    • 0028002821 scopus 로고
    • A low molecular mass heat-shock proteins is localized to higher plant mitochondria
    • Lenne C, Douce R: A low molecular mass heat-shock proteins is localized to higher plant mitochondria. Plant Physiol 105: 1255-1261 (1994).
    • (1994) Plant Physiol , vol.105 , pp. 1255-1261
    • Lenne, C.1    Douce, R.2
  • 33
    • 0028364096 scopus 로고
    • Rapid method for screening and cloning cDNAs generated in differential mRNA display: Application of Northern blot for affinity capturing of cDNAs
    • Li F, Barrnathan ES, Kariko K: Rapid method for screening and cloning cDNAs generated in differential mRNA display: application of Northern blot for affinity capturing of cDNAs. Nucl Acids Res 22: 1764-1765 (1994).
    • (1994) Nucl Acids Res , vol.22 , pp. 1764-1765
    • Li, F.1    Barrnathan, E.S.2    Kariko, K.3
  • 34
    • 0027328488 scopus 로고
    • Distribution and cloning of eukaryotic mRNA by means of differential display: Refinements and optimization
    • Liang P, Averboukh L, Pardee AB: Distribution and cloning of eukaryotic mRNA by means of differential display: refinements and optimization. Nucleic Acids Res 21: 3269-3275 (1993).
    • (1993) Nucleic Acids Res , vol.21 , pp. 3269-3275
    • Liang, P.1    Averboukh, L.2    Pardee, A.B.3
  • 35
    • 0026674886 scopus 로고
    • Differential display of eukaryotic mRNA by means of the polymerase chain reaction
    • Liang P, Pardee AB: Differential display of eukaryotic mRNA by means of the polymerase chain reaction. Science 257: 967-971 (1992).
    • (1992) Science , vol.257 , pp. 967-971
    • Liang, P.1    Pardee, A.B.2
  • 36
    • 0000340653 scopus 로고
    • Acquisition of low-temperature tolerance in tomatoes by exposure to high-temperature stress
    • Lurie S and Klein JD: Acquisition of low-temperature tolerance in tomatoes by exposure to high-temperature stress. J Amer Soc Hort Sci 116: 1007-1012 (1991).
    • (1991) J Amer Soc Hort Sci , vol.116 , pp. 1007-1012
    • Lurie, S.1    Klein, J.D.2
  • 37
    • 0001169117 scopus 로고
    • Chilling injury in plants
    • Lyons JM: Chilling injury in plants. Ann Rev Plant Physiol 24: 445-466 (1973).
    • (1973) Ann Rev Plant Physiol , vol.24 , pp. 445-466
    • Lyons, J.M.1
  • 38
  • 44
    • 0021396093 scopus 로고
    • Synthesis, modifications and structural binding of heat shock granules in tomato cell cultures
    • Nover L, Scharf K: Synthesis, modifications and structural binding of heat shock granules in tomato cell cultures. Eur J Biochem 139: 303-313 (1984).
    • (1984) Eur J Biochem , vol.139 , pp. 303-313
    • Nover, L.1    Scharf, K.2
  • 45
    • 0024639409 scopus 로고
    • Cytoplasmic heat shock granules are formed from precursor particles and are associated with a special set of mRNA
    • Nover L, Scharf KD, Neumann D: Cytoplasmic heat shock granules are formed from precursor particles and are associated with a special set of mRNA. Mol Cell Biol 9: 1298-1308 (1989).
    • (1989) Mol Cell Biol , vol.9 , pp. 1298-1308
    • Nover, L.1    Scharf, K.D.2    Neumann, D.3
  • 46
    • 51249168932 scopus 로고
    • A modified procedure for PCR-based differential display and demonstration of use in plants for isolation of genes related to fruit ripening
    • Oh BJ, Balint DE, Giovannoni JJ: A modified procedure for PCR-based differential display and demonstration of use in plants for isolation of genes related to fruit ripening. Plant Mol Biol Rep 13: 70-81 (1995).
    • (1995) Plant Mol Biol Rep , vol.13 , pp. 70-81
    • Oh, B.J.1    Balint, D.E.2    Giovannoni, J.J.3
  • 47
    • 0028113521 scopus 로고
    • Dynamics of small heat shock protein distribution within the chloroplasts of higher plants
    • Osteryoung KW, Vierling E: Dynamics of small heat shock protein distribution within the chloroplasts of higher plants. J Biol Chem 269: 28676-28682 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 28676-28682
    • Osteryoung, K.W.1    Vierling, E.2
  • 48
    • 0028859279 scopus 로고
    • Protein module and signaling networks
    • Pawson T: Protein module and signaling networks. Nature 373: 573-560 (1995).
    • (1995) Nature , vol.373 , pp. 573-1560
    • Pawson, T.1
  • 49
    • 0001306372 scopus 로고
    • Nuclear targeting in plants
    • Raikhel N: Nuclear targeting in plants. Plant Physiol 100: 1627-1632 (1992).
    • (1992) Plant Physiol , vol.100 , pp. 1627-1632
    • Raikhel, N.1
  • 50
    • 0024292258 scopus 로고
    • Nucleotide sequence analysis of soybean small heat shock protein genes belonging to two different multigene families
    • Raschke E, Baumann G, Schoffl F: Nucleotide sequence analysis of soybean small heat shock protein genes belonging to two different multigene families. J Mol Biol 199: 549-557 (1988).
    • (1988) J Mol Biol , vol.199 , pp. 549-557
    • Raschke, E.1    Baumann, G.2    Schoffl, F.3
  • 51
    • 0027408247 scopus 로고
    • Identification of a ten-amino acid proline-rich SH3 binding site
    • Ren R, Mayer BJ, Cicchett P, Baltimore D: Identification of a ten-amino acid proline-rich SH3 binding site. Science 259: 1157-1161 (1993).
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Mayer, B.J.2    Cicchett, P.3    Baltimore, D.4
  • 53
    • 0026078249 scopus 로고
    • Two independent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of biparticle nuclear targeting sequence
    • Robbins J, Dilworth SM, Laskey RA, Dingwall C: Two independent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of biparticle nuclear targeting sequence. Cell 64: 615-623 (1991).
    • (1991) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 54
    • 0030088062 scopus 로고    scopus 로고
    • The correlation between heat-shock protein accumulation and persistence and chilling in tomato fruit
    • Sabehat A, Weiss D, Lurie S: The correlation between heat-shock protein accumulation and persistence and chilling in tomato fruit. Plant Physiol 110: 531-537 (1996).
    • (1996) Plant Physiol , vol.110 , pp. 531-537
    • Sabehat, A.1    Weiss, D.2    Lurie, S.3
  • 56
    • 0028084194 scopus 로고
    • Heat-treating 'Sharwil' avocado for cold tolerance in quarantine cold treatments
    • Sanxter SS, Nishijima KA, Chan HT: Heat-treating 'Sharwil' avocado for cold tolerance in quarantine cold treatments. HortScience 29: 1166-1168 (1994).
    • (1994) HortScience , vol.29 , pp. 1166-1168
    • Sanxter, S.S.1    Nishijima, K.A.2    Chan, H.T.3
  • 57
    • 6844234075 scopus 로고
    • Identification of a multigene family for small heat shock proteins in soybean and physical characterization of one individual gene coding region
    • Schoffl F, Key JL: Identification of a multigene family for small heat shock proteins in soybean and physical characterization of one individual gene coding region. Plant Mol Biol 2: 269-278 (1983).
    • (1983) Plant Mol Biol , vol.2 , pp. 269-278
    • Schoffl, F.1    Key, J.L.2
  • 58
    • 0029379648 scopus 로고
    • Isolation of a novel Arabidopsis ozone-induced cDNA by differential display
    • Sharma YK, Davis KR: Isolation of a novel Arabidopsis ozone-induced cDNA by differential display. Plant Mol Biol 29: 91-98 (1995).
    • (1995) Plant Mol Biol , vol.29 , pp. 91-98
    • Sharma, Y.K.1    Davis, K.R.2
  • 59
    • 0026022910 scopus 로고
    • How proteins enter the nucleus
    • Silver PA: How proteins enter the nucleus. Cell 64: 489-497 (1991).
    • (1991) Cell , vol.64 , pp. 489-497
    • Silver, P.A.1
  • 60
    • 6844221575 scopus 로고    scopus 로고
    • A chloroplast small heat shock protein forms a large homo-oligomer and is not phosphorylated
    • Cold Spring Harbor Lab, Cold Spring Harbor, NY
    • Susuki T, Krawitz D, Vierling E: A chloroplast small heat shock protein forms a large homo-oligomer and is not phosphorylated. In Molecular Chaperones and the Heat Shock Response Metting 5/1-5/5, 1996, pp. 288. Cold Spring Harbor Lab, Cold Spring Harbor, NY (1996).
    • (1996) Molecular Chaperones and the Heat Shock Response Metting 5/1-5/5, 1996 , pp. 288
    • Susuki, T.1    Krawitz, D.2    Vierling, E.3
  • 61
    • 0030024983 scopus 로고    scopus 로고
    • Molecular cloning and characterization of genes expressed during early tomato (Lycopersicon esculentum Mill) fruit development by mRNA differential display
    • Tieman DM, Handa AK: Molecular cloning and characterization of genes expressed during early tomato (Lycopersicon esculentum Mill) fruit development by mRNA differential display. J Amer Soc Hort Sci 121: 52-56 (1996).
    • (1996) J Amer Soc Hort Sci , vol.121 , pp. 52-56
    • Tieman, D.M.1    Handa, A.K.2
  • 62
    • 0028372239 scopus 로고
    • Transcripts accumulating during cold storage of potato (Solanum tuberosum L.) tubers are sequence related to stress-responsive genes
    • Van Berkel J, Salamini F, Gebhardt C: Transcripts accumulating during cold storage of potato (Solanum tuberosum L.) tubers are sequence related to stress-responsive genes. Plant Physiol 104: 445-452 (1994).
    • (1994) Plant Physiol , vol.104 , pp. 445-452
    • Van Berkel, J.1    Salamini, F.2    Gebhardt, C.3
  • 63
    • 0029310495 scopus 로고
    • Identification of a gibberellin-induced gene in deep-water rice using differential display of mRNA
    • Van der Knaap E, Kende H: Identification of a gibberellin-induced gene in deep-water rice using differential display of mRNA. Plant Mol Biol 28: 589-592 (1995).
    • (1995) Plant Mol Biol , vol.28 , pp. 589-592
    • Van Der Knaap, E.1    Kende, H.2
  • 64
    • 0026194271 scopus 로고
    • The basic domain of plant B-ZIP proteins facilitates import of a reporter protein into plant nuclei
    • Van der Krol AR, Chua NH: The basic domain of plant B-ZIP proteins facilitates import of a reporter protein into plant nuclei. Plant Cell 3: 667-675 (1991).
    • (1991) Plant Cell , vol.3 , pp. 667-675
    • Van Der Krol, A.R.1    Chua, N.H.2
  • 65
    • 0000321971 scopus 로고
    • The role of heat shock proteins in plants
    • Vierling E: The role of heat shock proteins in plants. Ann Rev Plant Physiol Mol Biol 42: 579-620 (1991).
    • (1991) Ann Rev Plant Physiol Mol Biol , vol.42 , pp. 579-620
    • Vierling, E.1
  • 67
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters EL, Lee GJ, Vierling E: Evolution, structure and function of the small heat shock proteins in plants. J Exp Bot 296: 325-338 (1996).
    • (1996) J Exp Bot , vol.296 , pp. 325-338
    • Waters, E.L.1    Lee, G.J.2    Vierling, E.3
  • 68
    • 0029257371 scopus 로고
    • Identification of mRNAs with enhanced expression in ripening strawberry fruit using polymerase chain reaction differential display
    • Wilkinson JQ, Lanahan MB, Conner TW, Klee HJ: Identification of mRNAs with enhanced expression in ripening strawberry fruit using polymerase chain reaction differential display. Plant Mol Biol 27: 1097-1108 (1995).
    • (1995) Plant Mol Biol , vol.27 , pp. 1097-1108
    • Wilkinson, J.Q.1    Lanahan, M.B.2    Conner, T.W.3    Klee, H.J.4
  • 69
    • 0028192892 scopus 로고
    • Intracellular distribution of small heat stress proteins in culture cells of Lycopersicon peruvianum
    • Wollgiehn R, Neumann D, Nieden UZ, Musch A, Scharf KD, Nover L: Intracellular distribution of small heat stress proteins in culture cells of Lycopersicon peruvianum. J Plant Physiol 144: 491-499 (1994).
    • (1994) J Plant Physiol , vol.144 , pp. 491-499
    • Wollgiehn, R.1    Neumann, D.2    Nieden, U.Z.3    Musch, A.4    Scharf, K.D.5    Nover, L.6
  • 70
    • 0011337433 scopus 로고
    • Protein kinase C and its role in cell growth
    • Elson EL, Frazier WA, Graser L (eds). Plenum, New York
    • Woodgett JR, Hunter T, Gould KL: Protein kinase C and its role in cell growth. In Elson EL, Frazier WA, Graser L (eds). Cell Membranes: Methods and Reviews, 3, p. 215. Plenum, New York (1986).
    • (1986) Cell Membranes: Methods and Reviews , vol.3 , pp. 215
    • Woodgett, J.R.1    Hunter, T.2    Gould, K.L.3
  • 71
    • 0029392520 scopus 로고
    • A recombinant rice 16.9 kDa heat shock protein can provide thermoprotection in vitro
    • Yeh CH, Yeh KW, Wu SH, Chang PFL, Chen YM, Lin CY: A recombinant rice 16.9 kDa heat shock protein can provide thermoprotection in vitro. Plant Cell Physiol 36: 1341-1348 (1995).
    • (1995) Plant Cell Physiol , vol.36 , pp. 1341-1348
    • Yeh, C.H.1    Yeh, K.W.2    Wu, S.H.3    Chang, P.F.L.4    Chen, Y.M.5    Lin, C.Y.6
  • 73
    • 0028283991 scopus 로고
    • Analysis of gene expression in the preimplantation mouse embryo use of mRNA differential display
    • Zimmerman JW, Schultz RM: Analysis of gene expression in the preimplantation mouse embryo use of mRNA differential display. Proc Natl Acad Sci USA 91: 5456-5460 (1994).
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5456-5460
    • Zimmerman, J.W.1    Schultz, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.