메뉴 건너뛰기




Volumn 2, Issue 3, 2009, Pages 430-441

The level of expression of thioredoxin is linked to fundamental properties and applications of wheat seeds

Author keywords

Metabolic regulation; Molecular physiology; Preharvest sprouting; Seed biology; Seed germination; Thioredoxin h; Wheat allergenicity

Indexed keywords

ARABIDOPSIS; HORDEUM; MEDICAGO TRUNCATULA; TRITICUM AESTIVUM;

EID: 70350441419     PISSN: 16742052     EISSN: 17529867     Source Type: Journal    
DOI: 10.1093/mp/ssp025     Document Type: Article
Times cited : (51)

References (62)
  • 2
    • 0028369233 scopus 로고
    • Fertile transgenic wheat from microprojectile bombardment of scutellar tissue
    • Becker, D., Brettschneider, R., and Lorz, H. (1994). Fertile transgenic wheat from microprojectile bombardment of scutellar tissue. Plant J. 5, 299-307.
    • (1994) Plant J. , vol.5 , pp. 299-307
    • Becker, D.1    Brettschneider, R.2    Lorz, H.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0000765807 scopus 로고
    • Role of light in the regulation of chloroplast enzymes
    • Buchanan, B. B. (1980). Role of light in the regulation of chloroplast enzymes. Rev. Plant Physiol. 31, 341-374.
    • (1980) Rev. Plant Physiol. , vol.31 , pp. 341-374
    • Buchanan, B.B.1
  • 5
    • 20044367629 scopus 로고    scopus 로고
    • Redox regulation: A broadening horizon
    • Buchanan, B. B., and Balmer, Y. (2005). Redox regulation: a broadening horizon. Annu. Rev. Plant Biol. 56, 187-220.
    • (2005) Annu. Rev. Plant Biol. , vol.56 , pp. 187-220
    • Buchanan, B.B.1    Balmer, Y.2
  • 6
    • 0036260518 scopus 로고    scopus 로고
    • The dog as a model for food allergy
    • Ann. N. Y. Acad. Sci. New York Academy of Sciences, New York, NY
    • Buchanan, B. B., and Frick, O. L. (2002). The dog as a model for food allergy. In Genetically Engineered Food: Assessing Potential Allergenicity, Ann. N. Y. Acad. Sci. New York Academy of Sciences, New York, NY, 964, 173-183.
    • (2002) Genetically Engineered Food: Assessing Potential Allergenicity , vol.964 , pp. 173-183
    • Buchanan, B.B.1    Frick, O.L.2
  • 10
    • 0014200334 scopus 로고
    • Ferredoxin-activated fructose diphosphatase in isolated chloroplasts
    • Buchanan, B. B., Kalberer, P. P., and Arnon, D. I. (1967). Ferredoxin-activated fructose diphosphatase in isolated chloroplasts. Biochem. Biophys. Res. Commun. 29, 74-79.
    • (1967) Biochem. Biophys. Res. Commun. , vol.29 , pp. 74-79
    • Buchanan, B.B.1    Kalberer, P.P.2    Arnon, D.I.3
  • 11
    • 0028171569 scopus 로고
    • Thioredoxin: A multifunctional regulatory protein with a bright future in technology and medicine
    • Buchanan, B. B., Schürmann, P., Decottignies, P., and Lozano, R. M. (1994). Thioredoxin: a multifunctional regulatory protein with a bright future in technology and medicine. Arch. Biochem. Biophys. 314, 257-260.
    • (1994) Arch. Biochem. Biophys. , vol.314 , pp. 257-260
    • Buchanan, B.B.1    Schürmann, P.2    Decottignies, P.3    Lozano, R.M.4
  • 12
    • 0036413565 scopus 로고    scopus 로고
    • The ferredoxin/thioredoxin system: From discovery to molecular structures and beyond
    • Buchanan, B. B., Schürmann, P., Wolosiuk, R. A., and Jacquot, J. P. (2002). The ferredoxin/thioredoxin system: from discovery to molecular structures and beyond. Photosynth. Res. 73, 215-222.
    • (2002) Photosynth. Res. , vol.73 , pp. 215-222
    • Buchanan, B.B.1    Schürmann, P.2    Wolosiuk, R.A.3    Jacquot, J.P.4
  • 13
    • 0032561699 scopus 로고    scopus 로고
    • Transformation of recalcitrant barley cultivars through improvement of regenerability and decreased albinism
    • Cho, M.-J., Jiang, W., and Lemaux, P. G. (1998). Transformation of recalcitrant barley cultivars through improvement of regenerability and decreased albinism. Plant Sci. 138, 229-244.
    • (1998) Plant Sci. , vol.138 , pp. 229-244
    • Cho, M.-J.1    Jiang, W.2    Lemaux, P.G.3
  • 14
    • 0033428817 scopus 로고    scopus 로고
    • Overexpression of thioredoxin h leads to enhanced activity of starch debranching enzyme (pullulanase) in barley grain
    • Cho, M.-J., Wong, J. H., Marx, C., Jiang, W., Lemaux, P. G., and Buchanan, B. B. (1999). Overexpression of thioredoxin h leads to enhanced activity of starch debranching enzyme (pullulanase) in barley grain. Proc. Natl Acad. Sci. U S A. 96, 14641-14646.
    • (1999) Proc. Natl Acad. Sci. U S A. , vol.96 , pp. 14641-14646
    • Cho, M.-J.1    Wong, J.H.2    Marx, C.3    Jiang, W.4    Lemaux, P.G.5    Buchanan, B.B.6
  • 15
    • 0000941910 scopus 로고
    • Gibberellic acidenhanced synthesis and release of alphα-amylase and ribonuclease by isolated barley and aleurone layers
    • Chrispeels, M. J., and Varner, J. E. (1967). Gibberellic acidenhanced synthesis and release of alphα-amylase and ribonuclease by isolated barley and aleurone layers. Plant Physiol. 42, 398-406.
    • (1967) Plant Physiol. , vol.42 , pp. 398-406
    • Chrispeels, M.J.1    Varner, J.E.2
  • 16
    • 0037300659 scopus 로고    scopus 로고
    • Redox regulation and storage processes during maturation in kernels of Triticum durum
    • De Gara, L., de Pinto, M. C., Moliterni, V. M. C., and D'Egidio, M. G. (2003). Redox regulation and storage processes during maturation in kernels of Triticum durum. J. Exp. Bot. 54, 249-258.
    • (2003) J. Exp. Bot. , vol.54 , pp. 249-258
    • De Gara, L.1    De Pinto, M.C.2    Moliterni, V.M.C.3    D'Egidio, M.G.4
  • 18
    • 0000026219 scopus 로고
    • Plant DNA miniprep and microprep
    • M. and Walbot, V., eds (New York: Springer-Verlag)
    • Dellaporta, S. (1994). Plant DNA miniprep and microprep. In Maize Handbook, Freeling, M. and Walbot, V., eds (New York: Springer-Verlag), pp. 522-525.
    • (1994) Maize Handbook, Freeling , pp. 522-525
    • Dellaporta, S.1
  • 20
    • 51649118669 scopus 로고    scopus 로고
    • Improving digestibility of soy flour by reducing disulfide bonds with thioredoxin
    • Faris, R. J., Wang, H., andWang, T. (2008). Improving digestibility of soy flour by reducing disulfide bonds with thioredoxin. J. Agric. Food Chem. 56, 7146-7150.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 7146-7150
    • Faris, R.J.1    Wang, H.2    Wang, T.3
  • 21
    • 0000860075 scopus 로고
    • Molecular and cellular biology associated with endosperm mobilization in germinating cereals
    • Fincher, G. B. (1989). Molecular and cellular biology associated with endosperm mobilization in germinating cereals. Annu. Rev. Plant Physiol. 40, 305-346.
    • (1989) Annu. Rev. Plant Physiol. , vol.40 , pp. 305-346
    • Fincher, G.B.1
  • 22
    • 0030433647 scopus 로고    scopus 로고
    • Food allergy in atopic dogs
    • Frick, O. (1996). Food allergy in atopic dogs. Adv. Exp. Med. Biol. 409, 1-7.
    • (1996) Adv. Exp. Med. Biol. , vol.409 , pp. 1-7
    • Frick, O.1
  • 23
    • 0020726771 scopus 로고
    • Immunoglobulin e antibodies to pollens augmented in dogs by virus vaccines
    • Frick, O., and Brooks, D. (1983). Immunoglobulin E antibodies to pollens augmented in dogs by virus vaccines. Am. J. Vet. Res. 44, 440-445.
    • (1983) Am. J. Vet. Res. , vol.44 , pp. 440-445
    • Frick, O.1    Brooks, D.2
  • 24
    • 13244249705 scopus 로고    scopus 로고
    • Allergen immunotherapy with heat-killed Listeria monocytogenes alleviates peanut and food-induced anaphylaxis in dogs
    • Frick, O. L., Teuber, S. S., Buchanan, B. B., Morigasaki, S., and Umetsu, D. T. (2005). Allergen immunotherapy with heat-killed Listeria monocytogenes alleviates peanut and food-induced anaphylaxis in dogs. Allergy. 60, 243-250.
    • (2005) Allergy. , vol.60 , pp. 243-250
    • Frick, O.L.1    Teuber, S.S.2    Buchanan, B.B.3    Morigasaki, S.4    Umetsu, D.T.5
  • 25
    • 0032032912 scopus 로고    scopus 로고
    • Characterization of wheat thioredoxin h cDNA and production of an active Triticum aestivum protein in Escherichia coli
    • Gautier, M. F., Lullien-Pellerin, V., de Lamotte-Guéry, F., Guirao, A., and Joudrier, P. (1998). Characterization of wheat thioredoxin h cDNA and production of an active Triticum aestivum protein in Escherichia coli. Eur. J. Biochem. 252, 314-324.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 314-324
    • Gautier, M.F.1    Lullien-Pellerin, V.2    De Lamotte-Guéry, F.3    Guirao, A.4    Joudrier, P.5
  • 26
    • 0029914175 scopus 로고    scopus 로고
    • Change in sulfhydryl-disulfide status of wheat proteins during conditioning and milling
    • Gobin, P., Duviau, M.-P., Wong, J. H., Buchanan, B. B., and Kobrehel, K. (1996). Change in sulfhydryl-disulfide status of wheat proteins during conditioning and milling. Cereal. Chem. 73, 495-498.
    • (1996) Cereal. Chem. , vol.73 , pp. 495-498
    • Gobin, P.1    Duviau, M.-P.2    Wong, J.H.3    Buchanan, B.B.4    Kobrehel, K.5
  • 27
    • 33947206984 scopus 로고    scopus 로고
    • Changes in proteins within germinating seeds of transgenic wheat with an antisense construct directed against the thioredoxin
    • Guo, H. X., Yin, J., Ren, J. P., Wang, Z. Y., and Chen, H. L. (2007). Changes in proteins within germinating seeds of transgenic wheat with an antisense construct directed against the thioredoxin. Zhi Wu Sheng Li Yu Fen Zi Sheng Wu Xue Xue Bao. 33, 18-24.
    • (2007) Zhi Wu Sheng Li Yu Fen Zi Sheng Wu Xue Xue Bao. , vol.33 , pp. 18-24
    • Guo, H.X.1    Yin, J.2    Ren, J.P.3    Wang, Z.Y.4    Chen, H.L.5
  • 28
    • 0000739332 scopus 로고
    • Evaluation of methods used in testing winter wheat susceptibility to preharvest sprouting
    • Hagemann, M. G., and Ciha, A. J. (1984). Evaluation of methods used in testing winter wheat susceptibility to preharvest sprouting. Crop Sci. 24, 249-254.
    • (1984) Crop Sci. , vol.24 , pp. 249-254
    • Hagemann, M.G.1    Ciha, A.J.2
  • 29
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren, A. (1979). Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J. Biol. Chem. 254, 9627-9632.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 30
    • 43549116704 scopus 로고    scopus 로고
    • Characterization of quantitative trait loci controlling genetic variation for preharvest sprouting in synthetic backcross-derived wheat lines
    • Imtiaz, M., Ogbonnaya, F. C., Oman, J., and van Ginkel, M. (2008). Characterization of quantitative trait loci controlling genetic variation for preharvest sprouting in synthetic backcross-derived wheat lines. Genetics. 178, 1725-1736.
    • (2008) Genetics. , vol.178 , pp. 1725-1736
    • Imtiaz, M.1    Ogbonnaya, F.C.2    Oman, J.3    Van Ginkel, M.4
  • 31
    • 0000941909 scopus 로고
    • Gibberellic acid-induced synthesis of protease by isolated aleurone layers of barley
    • Jacobsen, J., and Varner, J. (1967). Gibberellic acid-induced synthesis of protease by isolated aleurone layers of barley. Plant Physiol. 42, 1596-1600.
    • (1967) Plant Physiol. , vol.42 , pp. 1596-1600
    • Jacobsen, J.1    Varner, J.2
  • 32
    • 0000579043 scopus 로고
    • Effect of thioredoxin-linked reduction on the activity and stability of the Kunitz and Bowman-Birk soybean trypsin inhibitor proteins
    • Jiao, J., Yee, B. C., Kobrehel, K., and Buchanan, B. B. (1992). Effect of thioredoxin-linked reduction on the activity and stability of the Kunitz and Bowman-Birk soybean trypsin inhibitor proteins. J. Agric. Food Chem. 40, 2333-2336.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 2333-2336
    • Jiao, J.1    Yee, B.C.2    Kobrehel, K.3    Buchanan, B.B.4
  • 33
    • 0027143431 scopus 로고
    • Thioredoxin-linked changes in regulatory properties of barley α-amylase/subtilisin inhibitor protein
    • Jiao, J., Yee, B. C., Wong, J. H., Kobrehel, K., and Buchanan, B. B. (1993). Thioredoxin-linked changes in regulatory properties of barley α-amylase/subtilisin inhibitor protein. Plant Physiol. Biochem. 31, 799-804.
    • (1993) Plant Physiol. Biochem. , vol.31 , pp. 799-804
    • Jiao, J.1    Yee, B.C.2    Wong, J.H.3    Kobrehel, K.4    Buchanan, B.B.5
  • 34
    • 0034529823 scopus 로고    scopus 로고
    • Cloning and expression of a distinct subclass of plant thioredoxins
    • Juttner, J., Olde, D., Langridge, P., and Baumann, U. (2000). Cloning and expression of a distinct subclass of plant thioredoxins. Eur. J. Biochem. 267, 7109-7117.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 7109-7117
    • Juttner, J.1    Olde, D.2    Langridge, P.3    Baumann, U.4
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227 (5259 680-685.
    • (1970) Nature. , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.1
  • 38
    • 33845944404 scopus 로고    scopus 로고
    • Cross-reactivity and 1. 4-A crystal structure of Malassezia sympodialis thioredoxin (Mala s 13), a member of a new pan-allergen family
    • Limacher, A., Glaser, A. G., Meier, C., Schmid-Grendelmeier, P., Zeller, S., Scapozza, L., and Crameri, R. (2007). Cross-reactivity and 1. 4-A crystal structure of Malassezia sympodialis thioredoxin (Mala s 13), a member of a new pan-allergen family. J. Immunol. 178, 389-396.
    • (2007) J. Immunol. , vol.178 , pp. 389-396
    • Limacher, A.1    Glaser, A.G.2    Meier, C.3    Schmid-Grendelmeier, P.4    Zeller, S.5    Scapozza, L.6    Crameri, R.7
  • 39
    • 0029839611 scopus 로고    scopus 로고
    • New evidence for a role for thioredoxin h in germination and seedling development
    • Lozano, R. M., Wong, J. H., Yee, B. C., Peters, A., Kobrehel, K., and Buchanan, B. B. (1996). New evidence for a role for thioredoxin h in germination and seedling development. Planta. 200, 100-106.
    • (1996) Planta. , vol.200 , pp. 100-106
    • Lozano, R.M.1    Wong, J.H.2    Yee, B.C.3    Peters, A.4    Kobrehel, K.5    Buchanan, B.B.6
  • 40
    • 1642409412 scopus 로고    scopus 로고
    • Cy5 maleimide labelling for sensitive detection of free thiols in native protein extracts: Identification of seed proteins targeted by barley thioredoxin h isoforms
    • Maeda, K., Finnie, C., and Svensson, B. (2004). Cy5 maleimide labelling for sensitive detection of free thiols in native protein extracts: identification of seed proteins targeted by barley thioredoxin h isoforms. Biochem. J. 378, 497-507.
    • (2004) Biochem. J. , vol.378 , pp. 497-507
    • Maeda, K.1    Finnie, C.2    Svensson, B.3
  • 41
    • 17844411493 scopus 로고    scopus 로고
    • Identification of thioredoxin h-reducible disulphides in proteomes by differential labelling of cysteines: Insight into recognition and regulation of proteins in barley seeds by thioredoxin h
    • Maeda, K., Finnie, C., and Svensson, B. (2005). Identification of thioredoxin h-reducible disulphides in proteomes by differential labelling of cysteines: insight into recognition and regulation of proteins in barley seeds by thioredoxin h. Proteomics. 5, 1634-1644.
    • (2005) Proteomics. , vol.5 , pp. 1634-1644
    • Maeda, K.1    Finnie, C.2    Svensson, B.3
  • 42
    • 0037636244 scopus 로고    scopus 로고
    • Identification, cloning and characterization of two thioredoxin h isoforms, HvTrxh1 and HvTrxh2, from the barley seed proteome
    • Maeda, K., Finnie, C., Østergaard, O., and Svensson, B. (2003). Identification, cloning and characterization of two thioredoxin h isoforms, HvTrxh1 and HvTrxh2, from the barley seed proteome. Eur J. Biochem. 270, 2633-2643.
    • (2003) Eur J. Biochem. , vol.270 , pp. 2633-2643
    • Maeda, K.1    Finnie, C.2    Østergaard, O.3    Svensson, B.4
  • 43
    • 0038662709 scopus 로고    scopus 로고
    • Thioredoxin and germinating barley: Targets and protein redox changes
    • Marx, C., Wong, J. H., and Buchanan, B. B. (2003). Thioredoxin and germinating barley: targets and protein redox changes. Planta. 216, 454-460.
    • (2003) Planta. , vol.216 , pp. 454-460
    • Marx, C.1    Wong, J.H.2    Buchanan, B.B.3
  • 44
    • 34250658872 scopus 로고    scopus 로고
    • Mitigated binding of IgE to thioredoxin-treated salt-soluble wheat allergens in a child with Baker's asthma
    • Matsumoto, T., Shimada, Y., and Hirai, S. (2007). Mitigated binding of IgE to thioredoxin-treated salt-soluble wheat allergens in a child with Baker's asthma. Ann. Allergy Asthma Immunol. 98, 599-600.
    • (2007) Ann. Allergy Asthma Immunol. , vol.98 , pp. 599-600
    • Matsumoto, T.1    Shimada, Y.2    Hirai, S.3
  • 45
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic aid reagent for determination of reducing sugar
    • Miller, G. L. (1959). Use of dinitrosalicylic aid reagent for determination of reducing sugar. Anal. Chem. 31, 426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 46
    • 34548605506 scopus 로고    scopus 로고
    • Effects of antisense-thioredoxin s gene on expression of endogenous thioredoxin h gene in transgenic wheat seed
    • Ren, J. P., Yin, J., Niu, H. B., Wang, X. G., and Li, Y. C. (2007). Effects of antisense-thioredoxin s gene on expression of endogenous thioredoxin h gene in transgenic wheat seed. ZhiWu Sheng Li Yu Fen Zi Sheng Wu Xue Xue Bao. 33, 325-332.
    • (2007) ZhiWu Sheng Li Yu Fen Zi Sheng Wu Xue Xue Bao. , vol.33 , pp. 325-332
    • Ren, J.P.1    Yin, J.2    Niu, H.B.3    Wang, X.G.4    Li, Y.C.5
  • 47
    • 0038538239 scopus 로고    scopus 로고
    • Sulfhydryl-disulfide changes in storage proteins of developing wheat grain: Influence on the SDS-unextractable glutenin polymer formation
    • Rhazi, L., Cazalis, R., and Aussenac, T. (2003). Sulfhydryl-disulfide changes in storage proteins of developing wheat grain: influence on the SDS-unextractable glutenin polymer formation. J. Cereal Sci. 38, 3-13.
    • (2003) J. Cereal Sci. , vol.38 , pp. 3-13
    • Rhazi, L.1    Cazalis, R.2    Aussenac, T.3
  • 48
    • 0021695885 scopus 로고
    • Ribosomal DNA spacer-length polymorphisms in barley:mendelian inheritance, chromosomal location, and population dynamics
    • Saghai-Maroof, M. A., Soliman, K. M., Jorgensen, R. A., and Allard, R. W. (1984). Ribosomal DNA spacer-length polymorphisms in barley:mendelian inheritance, chromosomal location, and population dynamics. Proc. Natl Acad. Sci. U S A. 81, 8014-8018.
    • (1984) Proc. Natl Acad. Sci. U S A. , vol.81 , pp. 8014-8018
    • Saghai-Maroof, M.A.1    Soliman, K.M.2    Jorgensen, R.A.3    Allard, R.W.4
  • 49
    • 0037108728 scopus 로고    scopus 로고
    • Cloning of thioredoxinhreductaseandcharacterizationof thethioredoxinreductasethioredoxin h system from wheat
    • Serrato, A. J., Pérez-Ruiz, J. M., andCejudo, F. J. (2002). Cloning of thioredoxinhreductaseandcharacterizationof thethioredoxinreductasethioredoxin h system from wheat. Biochem. J. 367, 491-497.
    • (2002) Biochem. J. , vol.367 , pp. 491-497
    • Serrato, A.J.1    Pérez-Ruiz, J.M.2    Cejudo, F.J.3
  • 50
    • 38949203862 scopus 로고    scopus 로고
    • The NADPH-dependent thioredoxin reductase/thioredoxin system in germinating barley seeds: Gene expression, protein profiles, and interactions between isoforms of thioredoxin h and thioredoxin reductase
    • Shahpiri, A., Svensson, B., and Finnie, C. (2008). The NADPH-dependent thioredoxin reductase/thioredoxin system in germinating barley seeds: gene expression, protein profiles, and interactions between isoforms of thioredoxin h and thioredoxin reductase. Plant Physiol. 146, 789-799.
    • (2008) Plant Physiol. , vol.146 , pp. 789-799
    • Shahpiri, A.1    Svensson, B.2    Finnie, C.3
  • 52
    • 48349124720 scopus 로고    scopus 로고
    • Gliadin immunoreactivity and dough rheological properties of winter wheat genotypes modified by thioredoxin
    • Waga, J., Zientarski, J., Obtulowicz, K., Bilo, B., and Stachowicz, M. (2008). Gliadin immunoreactivity and dough rheological properties of winter wheat genotypes modified by thioredoxin. Cereal Chem. 85, 488-494.
    • (2008) Cereal Chem. , vol.85 , pp. 488-494
    • Waga, J.1    Zientarski, J.2    Obtulowicz, K.3    Bilo, B.4    Stachowicz, M.5
  • 53
    • 0037628370 scopus 로고    scopus 로고
    • Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics
    • Wong, J. H., Balmer, Y., Cai, N., Tanaka, C. K., Vensel, W. H., Hurkman, W. J., and Buchanan, B. B. (2003). Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics. FEBS Lett. 547, 151-156.
    • (2003) FEBS Lett. , vol.547 , pp. 151-156
    • Wong, J.H.1    Balmer, Y.2    Cai, N.3    Tanaka, C.K.4    Vensel, W.H.5    Hurkman, W.J.6    Buchanan, B.B.7
  • 54
    • 3242791842 scopus 로고    scopus 로고
    • Thioredoxin targets of developing wheat seeds identified by complementary proteomic approaches
    • Wong, J. H., Cai, N., Balmer, Y., Tanaka, C. K., Vensel, W. H., Hurkman, W. J., and Buchanan, B. B. (2004a). Thioredoxin targets of developing wheat seeds identified by complementary proteomic approaches. Phytochemistry. 65, 1629-1640.
    • (2004) Phytochemistry. , vol.65 , pp. 1629-1640
    • Wong, J.H.1    Cai, N.2    Balmer, Y.3    Tanaka, C.K.4    Vensel, W.H.5    Hurkman, W.J.6    Buchanan, B.B.7
  • 55
    • 2342597074 scopus 로고    scopus 로고
    • Thioredoxin reduction alters the solubility of proteins of wheat starchy endosperm: An early event in germination
    • Wong, J. H., Cai, N., Tanaka, C. K., Vensel, W. H., Hurkman, W. J., and Buchanan, B. B. (2004b). Thioredoxin reduction alters the solubility of proteins of wheat starchy endosperm: an early event in germination. Plant Cell Physiol. 45, 407-415.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 407-415
    • Wong, J.H.1    Cai, N.2    Tanaka, C.K.3    Vensel, W.H.4    Hurkman, W.J.5    Buchanan, B.B.6
  • 56
    • 0037058928 scopus 로고    scopus 로고
    • Transgenic barley grain overexpressing thioredoxin shows evidence that the starchy endosperm communicates with the embryo and the aleurone
    • Wong, J. H., Kim, Y. B., Ren, P. H., Cai, N., Cho, M.-J., Hedden, P., Lemaux, P. G., and Buchanan, B. B. (2002). Transgenic barley grain overexpressing thioredoxin shows evidence that the starchy endosperm communicates with the embryo and the aleurone. Proc. Natl Acad. Sci. U S A. 99, 16325-16330.
    • (2002) Proc. Natl Acad. Sci. U S A. , vol.99 , pp. 16325-16330
    • Wong, J.H.1    Kim, Y.B.2    Ren, P.H.3    Cai, N.4    Cho, M.-J.5    Hedden, P.6    Lemaux, P.G.7    Buchanan, B.B.8
  • 58
    • 0036038573 scopus 로고    scopus 로고
    • Germplasm improvement for preharvest sprouting resistance in Chinese white-grained wheat: An overview of the current strategy
    • Xiao, S.-H., Zhang, X.-Y., Yan, C.-S., and Lin, H. (2002). Germplasm improvement for preharvest sprouting resistance in Chinese white-grained wheat: an overview of the current strategy. Euphytica. 126, 35-38.
    • (2002) Euphytica. , vol.126 , pp. 35-38
    • Xiao, S.-H.1    Zhang, X.-Y.2    Yan, C.-S.3    Lin, H.4
  • 59
    • 0043126075 scopus 로고
    • Debranching enzyme of rice seeds at milky stage, its purification and substrate specificities
    • Yamada, J., and Izawa, M. (1979). Debranching enzyme of rice seeds at milky stage, its purification and substrate specificities. Agri. Biol. Chem. 43, 37-44.
    • (1979) Agri. Biol. Chem. , vol.43 , pp. 37-44
    • Yamada, J.1    Izawa, M.2
  • 61
    • 57449092976 scopus 로고    scopus 로고
    • Thioredoxin h system and wheat seed quality
    • Zahid, A., Afoulous, S., and Cazalia, R. (2008). Thioredoxin h system and wheat seed quality. Cereal Chem. 85, 799-807.
    • (2008) Cereal Chem. , vol.85 , pp. 799-807
    • Zahid, A.1    Afoulous, S.2    Cazalia, R.3
  • 62
    • 33947286986 scopus 로고    scopus 로고
    • Study on molecular identification and pre-harvest sprouting characteristic of the transgenic anti-trxs-gene wheat line 00T89
    • Zhou, S. M., Yin, J., Ren, J. P., and Zhang, R. (2006). Study on molecular identification and pre-harvest sprouting characteristic of the transgenic anti-trxs-gene wheat line 00T89. Sheng Wu Gong Cheng Xue Bao. 22, 438-444.
    • (2006) Sheng Wu Gong Cheng Xue Bao. , vol.22 , pp. 438-444
    • Zhou, S.M.1    Yin, J.2    Ren, J.P.3    Zhang, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.