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Volumn 175, Issue 5, 2008, Pages 663-673

Identification of differentially expressed genes in soybean seeds differing in oil content

Author keywords

Differentially expressed gene; Oil synthesis; Seed development; Suppression subtractive hybridization

Indexed keywords

GLYCINE MAX;

EID: 51649083954     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2008.06.018     Document Type: Article
Times cited : (22)

References (50)
  • 1
    • 51649096769 scopus 로고    scopus 로고
    • Primary study on protein and lipid accumulation in high oil content soybean varieties
    • Zhou S., Zhang D., Luan H., Yu F., Xin X., and Hu G. Primary study on protein and lipid accumulation in high oil content soybean varieties. Chin. J. Oil Crop Sci. 28 (2006) 214-216
    • (2006) Chin. J. Oil Crop Sci. , vol.28 , pp. 214-216
    • Zhou, S.1    Zhang, D.2    Luan, H.3    Yu, F.4    Xin, X.5    Hu, G.6
  • 2
    • 0026669362 scopus 로고
    • Purification and characterization of 3-ketoacyl-acyl carrier protein synthase III from spinach. A condensing enzyme utilizing acetyl-coenzyme A to initiate fatty acid synthesis
    • Clough R.C., Matthis A.L., Barnum S.R., and Jaworski J.G. Purification and characterization of 3-ketoacyl-acyl carrier protein synthase III from spinach. A condensing enzyme utilizing acetyl-coenzyme A to initiate fatty acid synthesis. J. Biol. Chem. 267 (1992) 20992-20998
    • (1992) J. Biol. Chem. , vol.267 , pp. 20992-20998
    • Clough, R.C.1    Matthis, A.L.2    Barnum, S.R.3    Jaworski, J.G.4
  • 3
    • 0027208207 scopus 로고
    • Acetyl-acyl carrier protein is not a major intermediate in fatty acid biosynthesis in spinach
    • Jaworski J.G., Post-Beittenmiller D., and Ohlrogge J.B. Acetyl-acyl carrier protein is not a major intermediate in fatty acid biosynthesis in spinach. Eur. J. Biochem. 213 (1993) 981-987
    • (1993) Eur. J. Biochem. , vol.213 , pp. 981-987
    • Jaworski, J.G.1    Post-Beittenmiller, D.2    Ohlrogge, J.B.3
  • 4
    • 0001786891 scopus 로고
    • A cerulenin insensitive short chain 3-ketoacyl-acyl carrier protein synthase in Spinacia oleracea leaves
    • Jaworski J.G., Clough R.C., and Barnum S.R. A cerulenin insensitive short chain 3-ketoacyl-acyl carrier protein synthase in Spinacia oleracea leaves. Plant Physiol. 90 (1989) 41-44
    • (1989) Plant Physiol. , vol.90 , pp. 41-44
    • Jaworski, J.G.1    Clough, R.C.2    Barnum, S.R.3
  • 5
    • 0035112491 scopus 로고    scopus 로고
    • Overexpression of 3-ketoacyl-acyl-carrier protein synthase IIIs in plants reduced the rate of lipid synthesis
    • Dehesh K., Tai H., and Edwards P. Overexpression of 3-ketoacyl-acyl-carrier protein synthase IIIs in plants reduced the rate of lipid synthesis. Plant Physiol. 125 (2001) 1103-1114
    • (2001) Plant Physiol. , vol.125 , pp. 1103-1114
    • Dehesh, K.1    Tai, H.2    Edwards, P.3
  • 6
    • 0031051393 scopus 로고    scopus 로고
    • Targeting of the Arabidopsis hormomeric acetyl-coenzyme A carboxylase to plastids of rapeseeds
    • Roesler K., Shintani D., Savage L., Boddupalli S., and Ohlrogge J. Targeting of the Arabidopsis hormomeric acetyl-coenzyme A carboxylase to plastids of rapeseeds. Plant Physiol. 113 (1997) 75-81
    • (1997) Plant Physiol. , vol.113 , pp. 75-81
    • Roesler, K.1    Shintani, D.2    Savage, L.3    Boddupalli, S.4    Ohlrogge, J.5
  • 7
    • 0028893170 scopus 로고
    • Expressed sequence tags from developing caster seeds
    • 1441-1150
    • Van de Loo F.J., Turner S., and Somerville C. Expressed sequence tags from developing caster seeds. Plant Physiol. 108 (1995) 1441-1150
    • (1995) Plant Physiol. , vol.108
    • Van de Loo, F.J.1    Turner, S.2    Somerville, C.3
  • 8
    • 0026085586 scopus 로고
    • Stearoyl-ACP desaturase from higher plants is structurally unrelated to the animal homolog
    • Shanklin J., and Somerville C.R. Stearoyl-ACP desaturase from higher plants is structurally unrelated to the animal homolog. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 2510-2514
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 2510-2514
    • Shanklin, J.1    Somerville, C.R.2
  • 9
    • 0033607294 scopus 로고    scopus 로고
    • Biosynthetic origin of conjugated double bonds: production of fatty acid components of high-value drying oils in transgenic soybean embryos
    • Cahoon E.B., Carlson T.J., Ripp K.G., Schweiger B.J., Cook G.A., Hall S.E., and Kinney A.J. Biosynthetic origin of conjugated double bonds: production of fatty acid components of high-value drying oils in transgenic soybean embryos. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 12935-12940
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 12935-12940
    • Cahoon, E.B.1    Carlson, T.J.2    Ripp, K.G.3    Schweiger, B.J.4    Cook, G.A.5    Hall, S.E.6    Kinney, A.J.7
  • 10
    • 35848936305 scopus 로고    scopus 로고
    • The soybean Dof-type transcription factor genes, GmDof4 and GmDof11, enhance lipid content in the seeds of transgenic Arabidopsis plants
    • Wang H.W., Zhang B., Hao Y.J., Huang J., Tian A.G., Liao Y., Zhang J.S., and Chen S.Y. The soybean Dof-type transcription factor genes, GmDof4 and GmDof11, enhance lipid content in the seeds of transgenic Arabidopsis plants. Plant J. 52 (2007) 716-729
    • (2007) Plant J. , vol.52 , pp. 716-729
    • Wang, H.W.1    Zhang, B.2    Hao, Y.J.3    Huang, J.4    Tian, A.G.5    Liao, Y.6    Zhang, J.S.7    Chen, S.Y.8
  • 11
    • 0029784968 scopus 로고    scopus 로고
    • Metabolism of glucose 6-phosphate and utilization of multiple metabolites for oil synthesis by plastids from developing oils seed rape embryos
    • Kang F., and Rawsthorne S. Metabolism of glucose 6-phosphate and utilization of multiple metabolites for oil synthesis by plastids from developing oils seed rape embryos. Planta 199 (1996) 321-327
    • (1996) Planta , vol.199 , pp. 321-327
    • Kang, F.1    Rawsthorne, S.2
  • 12
    • 0036740911 scopus 로고    scopus 로고
    • Probing in vivo metabolism by stable isotope labeling of storage lipids and proteins in developing Brassica napus embryos
    • Schwender J., and Ohlrogge J. Probing in vivo metabolism by stable isotope labeling of storage lipids and proteins in developing Brassica napus embryos. Plant Physiol. 130 (2002) 347-361
    • (2002) Plant Physiol. , vol.130 , pp. 347-361
    • Schwender, J.1    Ohlrogge, J.2
  • 13
    • 23044511847 scopus 로고    scopus 로고
    • The biogenesis and functions of lipid bodies in animals, plants and microorganisms
    • Murphy D.J. The biogenesis and functions of lipid bodies in animals, plants and microorganisms. Plant J. 13 (2001) 1-16
    • (2001) Plant J. , vol.13 , pp. 1-16
    • Murphy, D.J.1
  • 14
    • 16544370489 scopus 로고    scopus 로고
    • Endoplasmic reticulum, oleosins, and oils in seeds and tapetum cells
    • Hsieh K., and Huang A.H.C. Endoplasmic reticulum, oleosins, and oils in seeds and tapetum cells. Plant Physiol. 136 (2004) 3427-3434
    • (2004) Plant Physiol. , vol.136 , pp. 3427-3434
    • Hsieh, K.1    Huang, A.H.C.2
  • 15
    • 33747864414 scopus 로고    scopus 로고
    • Identification of differentially expressed genes in seeds of two near-isogenic Brassica napus lines with different oil content
    • Li R.J., Wang H.Z., Mao H., Lu Y.T., and Hua W. Identification of differentially expressed genes in seeds of two near-isogenic Brassica napus lines with different oil content. Planta 224 (2006) 952-962
    • (2006) Planta , vol.224 , pp. 952-962
    • Li, R.J.1    Wang, H.Z.2    Mao, H.3    Lu, Y.T.4    Hua, W.5
  • 16
    • 0030061237 scopus 로고    scopus 로고
    • Genetic engineering of a quantitative trait-metabolic and genetic parameters influencing the accumulation of laurate in rapeseed
    • Voelker T.A., Hayes T.R., Cranmer A.M., Turner J.C., and Davies H.M. Genetic engineering of a quantitative trait-metabolic and genetic parameters influencing the accumulation of laurate in rapeseed. Plant J. 9 (1996) 229-241
    • (1996) Plant J. , vol.9 , pp. 229-241
    • Voelker, T.A.1    Hayes, T.R.2    Cranmer, A.M.3    Turner, J.C.4    Davies, H.M.5
  • 17
    • 0031742715 scopus 로고    scopus 로고
    • Expression of lauroyl-acyl carrier protein thioesterase in Brassica napus seeds induces pathways for both fatty acid oxidation and biosynthesis and implies a set point for triacylglycerol accumulation
    • Eccleston V.S., and Ohlrogge J.B. Expression of lauroyl-acyl carrier protein thioesterase in Brassica napus seeds induces pathways for both fatty acid oxidation and biosynthesis and implies a set point for triacylglycerol accumulation. Plant Cell 10 (1998) 613-622
    • (1998) Plant Cell , vol.10 , pp. 613-622
    • Eccleston, V.S.1    Ohlrogge, J.B.2
  • 18
    • 0029007122 scopus 로고
    • A new family of lipolytic enzymes
    • Upton C., and Buckley J.T. A new family of lipolytic enzymes. Trends Biochem. Sci. 20 (1995) 178-179
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 178-179
    • Upton, C.1    Buckley, J.T.2
  • 19
    • 7444229762 scopus 로고    scopus 로고
    • GDSL family of serine esterases/lipases
    • Akoh C.C., Lee G.C., and Liaw Y.C. GDSL family of serine esterases/lipases. Prog. Lipid Res. 43 (2004) 534-552
    • (2004) Prog. Lipid Res. , vol.43 , pp. 534-552
    • Akoh, C.C.1    Lee, G.C.2    Liaw, Y.C.3
  • 21
    • 0027759974 scopus 로고
    • Characterization of an Arabidopsis thaliana lipoxygenase gene responsive to methyl jasmonate and wounding
    • Bell E., and Mulle J.E. Characterization of an Arabidopsis thaliana lipoxygenase gene responsive to methyl jasmonate and wounding. Plant Physiol. 103 (1993) 1133-1137
    • (1993) Plant Physiol. , vol.103 , pp. 1133-1137
    • Bell, E.1    Mulle, J.E.2
  • 22
    • 0002262342 scopus 로고
    • Volatile products of the lipoxygenase pathway evolved from Phaseolus vulgaris (L.) leaves inoculated with Pseudomonas syringae pv. phaseolicola
    • Croft K.P.C., Jutter F., and Slusarenko A.J. Volatile products of the lipoxygenase pathway evolved from Phaseolus vulgaris (L.) leaves inoculated with Pseudomonas syringae pv. phaseolicola. Plant Physiol. 101 (1993) 13-24
    • (1993) Plant Physiol. , vol.101 , pp. 13-24
    • Croft, K.P.C.1    Jutter, F.2    Slusarenko, A.J.3
  • 23
    • 0028055816 scopus 로고
    • Complex spatial and temporal expression of lipoxygenase genes during Phaseolus vulgaris (L) development
    • Eiben H.G., and Slusarenko A.J. Complex spatial and temporal expression of lipoxygenase genes during Phaseolus vulgaris (L) development. Plant J. 5 (1994) 123-135
    • (1994) Plant J. , vol.5 , pp. 123-135
    • Eiben, H.G.1    Slusarenko, A.J.2
  • 24
    • 0001354771 scopus 로고
    • Involvement of a lipoxygenase-like enzyme in abscisic acid biosynthesis
    • Creelman R.A., Bell E., and Mullet J. Involvement of a lipoxygenase-like enzyme in abscisic acid biosynthesis. Plant Physiol. 99 (1992) 1258-1265
    • (1992) Plant Physiol. , vol.99 , pp. 1258-1265
    • Creelman, R.A.1    Bell, E.2    Mullet, J.3
  • 25
    • 0026215401 scopus 로고
    • The Soybean 94-kilodalton vegetative storage protein is a lipoxygenase that is localized in paraveinal mesophyll cell vacuoles
    • Tranbarger T.J., Franceschi V.R., and Hildebrand D.F. The Soybean 94-kilodalton vegetative storage protein is a lipoxygenase that is localized in paraveinal mesophyll cell vacuoles. Plant Cell 3 (1991) 973-987
    • (1991) Plant Cell , vol.3 , pp. 973-987
    • Tranbarger, T.J.1    Franceschi, V.R.2    Hildebrand, D.F.3
  • 26
    • 0027260861 scopus 로고
    • Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase
    • Minor W., Steczko J., and Bolin J.T. Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase. Biochemistry 32 (1993) 6320-6323
    • (1993) Biochemistry , vol.32 , pp. 6320-6323
    • Minor, W.1    Steczko, J.2    Bolin, J.T.3
  • 27
    • 0031105634 scopus 로고    scopus 로고
    • Molecular characterization of L2 lipoxygenase from maize embryos
    • Jensen A.B., Pocal E., and Rigaud M. Molecular characterization of L2 lipoxygenase from maize embryos. Plant Mol. Biol. 33 (1997) 605-614
    • (1997) Plant Mol. Biol. , vol.33 , pp. 605-614
    • Jensen, A.B.1    Pocal, E.2    Rigaud, M.3
  • 28
    • 0022636466 scopus 로고
    • Singlet oxygen production by soybean lipoxygenase isozymes
    • Kanofsky J.R., and Axelrodll B. Singlet oxygen production by soybean lipoxygenase isozymes. J. Biol. Chem. 261 (1986) 1099-1104
    • (1986) J. Biol. Chem. , vol.261 , pp. 1099-1104
    • Kanofsky, J.R.1    Axelrodll, B.2
  • 29
    • 0035206699 scopus 로고    scopus 로고
    • Production and chemiluminescent free radical reactions of glyoxal in lipid peroxidation of linoleic acid by the ligninolytic enzyme, manganese peroxidase
    • Watanabel T., Shirai N., and Okadal H. Production and chemiluminescent free radical reactions of glyoxal in lipid peroxidation of linoleic acid by the ligninolytic enzyme, manganese peroxidase. Eur. J. Biochem. 268 (2001) 6114-6122
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6114-6122
    • Watanabel, T.1    Shirai, N.2    Okadal, H.3
  • 30
    • 0033579474 scopus 로고    scopus 로고
    • Identification of catalytic residues in glyoxal oxidase by targeted mutagenesis
    • Whittaker M.M., Kersten P.J., and Cullen D. Identification of catalytic residues in glyoxal oxidase by targeted mutagenesis. J. Biol. Chem. 274 (1999) 36226-36232
    • (1999) J. Biol. Chem. , vol.274 , pp. 36226-36232
    • Whittaker, M.M.1    Kersten, P.J.2    Cullen, D.3
  • 31
    • 0001360382 scopus 로고
    • Sugar metabolism in developing kernels of starch-deficient endosperm mutants of maize
    • Doehlert D.C., and Kuo T.M. Sugar metabolism in developing kernels of starch-deficient endosperm mutants of maize. Plant Physiol. 92 (1992) 990-994
    • (1992) Plant Physiol. , vol.92 , pp. 990-994
    • Doehlert, D.C.1    Kuo, T.M.2
  • 32
    • 0000839493 scopus 로고
    • Evidence for circadian regulation of starch and sucrose synthesis in sugar beet leaves
    • Li B., Geiger D.R., and Shieh W.J. Evidence for circadian regulation of starch and sucrose synthesis in sugar beet leaves. Plant Physiol. 99 (1992) 1393-1399
    • (1992) Plant Physiol. , vol.99 , pp. 1393-1399
    • Li, B.1    Geiger, D.R.2    Shieh, W.J.3
  • 33
    • 0037189862 scopus 로고    scopus 로고
    • Xylanase, beta-glucanase, and other side enzymatic activities have greater effects on the viscosity of several feedstuffs than xylanase and beta-glucanase used alone or in combination
    • Mathlouthi N., Saulnier L., and Quemener B. Xylanase, beta-glucanase, and other side enzymatic activities have greater effects on the viscosity of several feedstuffs than xylanase and beta-glucanase used alone or in combination. J. Agric. Food Chem. 50 (2002) 5121-5127
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 5121-5127
    • Mathlouthi, N.1    Saulnier, L.2    Quemener, B.3
  • 34
    • 0029346981 scopus 로고
    • Expression of a zeatin-O-glucoside-degrading β-glucosidase in Brassica napus
    • Falk A., and Rask L. Expression of a zeatin-O-glucoside-degrading β-glucosidase in Brassica napus. Plant Physiol. 108 (1995) 1369-1377
    • (1995) Plant Physiol. , vol.108 , pp. 1369-1377
    • Falk, A.1    Rask, L.2
  • 35
    • 0032527978 scopus 로고    scopus 로고
    • Insight into naphthoquinone metabolism: β-glucosidase-catalysed hydrolysis of hydrojuglone β-d-glucopyranoside
    • Duroux L., Delmotte F.M., and Lancelin J.M. Insight into naphthoquinone metabolism: β-glucosidase-catalysed hydrolysis of hydrojuglone β-d-glucopyranoside. Biochem. J. 333 (1998) 275-283
    • (1998) Biochem. J. , vol.333 , pp. 275-283
    • Duroux, L.1    Delmotte, F.M.2    Lancelin, J.M.3
  • 36
    • 20844435464 scopus 로고    scopus 로고
    • Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 1
    • Xu Z., Escamilla-Treviño L.L., and Zeng L. Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 1. Plant Mol. Biol. 55 (2004) 343-367
    • (2004) Plant Mol. Biol. , vol.55 , pp. 343-367
    • Xu, Z.1    Escamilla-Treviño, L.L.2    Zeng, L.3
  • 37
    • 0033134279 scopus 로고    scopus 로고
    • Tissue-specific expression of the β-subunit of tryptophan synthase in Camptotheca acuminata, an indole alkaloid-producing plant
    • Lu H., and McKnight T.D. Tissue-specific expression of the β-subunit of tryptophan synthase in Camptotheca acuminata, an indole alkaloid-producing plant. Plant Physiol. 120 (1999) 43-51
    • (1999) Plant Physiol. , vol.120 , pp. 43-51
    • Lu, H.1    McKnight, T.D.2
  • 38
    • 0027622430 scopus 로고
    • Expression patterns of duplicate tryptophan synthase-6 genes in Arabidopsis thaliana
    • Pruitt K.D., and Last R.L. Expression patterns of duplicate tryptophan synthase-6 genes in Arabidopsis thaliana. Plant Physiol. 102 (1993) 1019-1026
    • (1993) Plant Physiol. , vol.102 , pp. 1019-1026
    • Pruitt, K.D.1    Last, R.L.2
  • 39
    • 0000309081 scopus 로고
    • Protein disulfide-isomerase is located in the endoplasmic reticulum of developing wheat endosperm
    • Roden L.T., Miflin B.J., and Freedman R.B. Protein disulfide-isomerase is located in the endoplasmic reticulum of developing wheat endosperm. FEBS Lett. 138 (1982) 121-124
    • (1982) FEBS Lett. , vol.138 , pp. 121-124
    • Roden, L.T.1    Miflin, B.J.2    Freedman, R.B.3
  • 40
    • 0742287185 scopus 로고    scopus 로고
    • Cupins: the most functionally diverse protein superfamily
    • Dunwell J.M., Purvis A., and Khuri S. Cupins: the most functionally diverse protein superfamily. Phytochemistry 65 (2004) 7-17
    • (2004) Phytochemistry , vol.65 , pp. 7-17
    • Dunwell, J.M.1    Purvis, A.2    Khuri, S.3
  • 41
    • 0027022498 scopus 로고
    • A 62-kDa sucrose binding protein is expressed and localized in tissues actively engaged in sucrose transport
    • Grimes H.D., Overvoorde P.J., and Ripp K. A 62-kDa sucrose binding protein is expressed and localized in tissues actively engaged in sucrose transport. Plant Cell 4 (1992) 1561-1574
    • (1992) Plant Cell , vol.4 , pp. 1561-1574
    • Grimes, H.D.1    Overvoorde, P.J.2    Ripp, K.3
  • 42
    • 33846935280 scopus 로고    scopus 로고
    • A suite of sucrose transporters expressed in coats of developing legume seeds includes novel pH-independent facilitators
    • Zhou Y.C., Qu H.X., and Dibley K.E. A suite of sucrose transporters expressed in coats of developing legume seeds includes novel pH-independent facilitators. Plant J. 49 (2007) 750-764
    • (2007) Plant J. , vol.49 , pp. 750-764
    • Zhou, Y.C.1    Qu, H.X.2    Dibley, K.E.3
  • 43
    • 33645745003 scopus 로고    scopus 로고
    • +-ATPase is involved in the adaptation to phosphorus starvation in soybean seedlings
    • +-ATPase is involved in the adaptation to phosphorus starvation in soybean seedlings. J. Exp. Bot. 57 (2006) 1353-1362
    • (2006) J. Exp. Bot. , vol.57 , pp. 1353-1362
    • Shen, H.1    Chen, J.2    Wang, Z.3    Yamamoto, Y.4    Matsumoto, H.5
  • 44
    • 17944379523 scopus 로고    scopus 로고
    • Recruitment to Golgi membranes of ADP-ribosylation factor1 is mediated by the cytoplasmic domain of p23
    • Gommel D.U., Memon A.R., and Lottspeich A.H.F. Recruitment to Golgi membranes of ADP-ribosylation factor1 is mediated by the cytoplasmic domain of p23. EMBO J. 20 (2001) 6751-6760
    • (2001) EMBO J. , vol.20 , pp. 6751-6760
    • Gommel, D.U.1    Memon, A.R.2    Lottspeich, A.H.F.3
  • 45
    • 3042689728 scopus 로고    scopus 로고
    • The role of ADP-ribosylation factor and SAR1 in vesicular trafficking in plants
    • Memon A.R. The role of ADP-ribosylation factor and SAR1 in vesicular trafficking in plants. Biochim. Biophys. Acta 1664 (2004) 9-30
    • (2004) Biochim. Biophys. Acta , vol.1664 , pp. 9-30
    • Memon, A.R.1
  • 46
    • 0032699429 scopus 로고    scopus 로고
    • A role of for ADP ribosylation factor in the control of cargo uptake during COPI-coated vesicle biogenesis
    • Malsam J., Gommel D., and Wieland F.T. A role of for ADP ribosylation factor in the control of cargo uptake during COPI-coated vesicle biogenesis. FEBS Lett. 462 (1999) 267-272
    • (1999) FEBS Lett. , vol.462 , pp. 267-272
    • Malsam, J.1    Gommel, D.2    Wieland, F.T.3
  • 47
    • 23044443637 scopus 로고    scopus 로고
    • Reticulon 3 is involved in membrane trafficking between the endoplasmic reticulum and Golgi
    • Wakana Y., Koyama S., and Nakajima K. Reticulon 3 is involved in membrane trafficking between the endoplasmic reticulum and Golgi. Biochem. Biophys. Res. 334 (2005) 1198-1205
    • (2005) Biochem. Biophys. Res. , vol.334 , pp. 1198-1205
    • Wakana, Y.1    Koyama, S.2    Nakajima, K.3
  • 48
    • 0026261958 scopus 로고
    • Isoforms of soybean seed oils body membrane protein 24 kDa oleosin are encoded by closely related cDNAs
    • Kalinski A., Loer D.S., and Weisemann J.M. Isoforms of soybean seed oils body membrane protein 24 kDa oleosin are encoded by closely related cDNAs. Plant Mol. Biol. 17 (1991) 1095-1098
    • (1991) Plant Mol. Biol. , vol.17 , pp. 1095-1098
    • Kalinski, A.1    Loer, D.S.2    Weisemann, J.M.3
  • 49
    • 0026878251 scopus 로고
    • Cloning and characterization of an oleosin gene from Brassica napus L
    • Keddie J., Hubner G., and Slocombe S.P. Cloning and characterization of an oleosin gene from Brassica napus L. Plant Mol. Biol. 19 (1992) 443-453
    • (1992) Plant Mol. Biol. , vol.19 , pp. 443-453
    • Keddie, J.1    Hubner, G.2    Slocombe, S.P.3
  • 50
    • 0031224915 scopus 로고    scopus 로고
    • Molecular cloning and further characterization of a probable plant vacuolar sorting receptor
    • Paris N., Rogers S.W., and Jiang L.W. Molecular cloning and further characterization of a probable plant vacuolar sorting receptor. Plant Physiol. 115 (1997) 29-39
    • (1997) Plant Physiol. , vol.115 , pp. 29-39
    • Paris, N.1    Rogers, S.W.2    Jiang, L.W.3


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