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Volumn 85, Issue 6, 2008, Pages 799-807

Thioredoxin h system and wheat seed quality

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; QUALITY CONTROL; SEED;

EID: 57449092976     PISSN: 00090352     EISSN: None     Source Type: Journal    
DOI: 10.1094/CCHEM-85-6-0799     Document Type: Review
Times cited : (5)

References (119)
  • 3
    • 1642371610 scopus 로고    scopus 로고
    • Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts
    • Balmer, Y., Koller, A., del Val, G., Schürmann, P., and Buchanan, B. B. 2004. Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynth. Res. 79:275-280,
    • (2004) Photosynth. Res , vol.79 , pp. 275-280
    • Balmer, Y.1    Koller, A.2    del Val, G.3    Schürmann, P.4    Buchanan, B.B.5
  • 5
    • 33646261644 scopus 로고    scopus 로고
    • 20066. Proteome of amyloplasts isolated from developing wheat endosperm presents evidence of broad metabolic capability
    • Balmer, Y., Vensel, W. H., Dupont, F. M., Buchanan, B. B., and Hurkman, W. J. 20066. Proteome of amyloplasts isolated from developing wheat endosperm presents evidence of broad metabolic capability. J. Exp. Bot. 57:1591-1602.
    • J. Exp. Bot , vol.57 , pp. 1591-1602
    • Balmer, Y.1    Vensel, W.H.2    Dupont, F.M.3    Buchanan, B.B.4    Hurkman, W.J.5
  • 6
    • 36248936703 scopus 로고    scopus 로고
    • Localization in roots and flowers of pea chloroplastic thioredoxin f and thioredoxin m proteins reveals new roles in nonphotosynthetic organs
    • Barajas-López, J. D., Serrato, A. J. Olmedilla, A., Chueca, A., and Sahrawy. M. 2007. Localization in roots and flowers of pea chloroplastic thioredoxin f and thioredoxin m proteins reveals new roles in nonphotosynthetic organs. Plant Physiol. 145:946-960.
    • (2007) Plant Physiol , vol.145 , pp. 946-960
    • Barajas-López, J.D.1    Serrato, A.J.2    Olmedilla, A.3    Chueca, A.4    Sahrawy, M.5
  • 8
    • 0029928068 scopus 로고    scopus 로고
    • Thiocalsin: A thioredoxin-linked, substrate-specific protease dependent on calcium
    • Besse, I., Wong, J. H., Kobrehel, K., and Buchanan, B. B. 1996. Thiocalsin: A thioredoxin-linked, substrate-specific protease dependent on calcium. Proc. Natl. Acad. Sci. USA 93:3169-3175.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3169-3175
    • Besse, I.1    Wong, J.H.2    Kobrehel, K.3    Buchanan, B.B.4
  • 9
    • 85153980925 scopus 로고    scopus 로고
    • Bewley, J. D., and Black, M. 1994. Seeds. Physiology and Germination. Plenum Press: New York.
    • Bewley, J. D., and Black, M. 1994. Seeds. Physiology and Germination. Plenum Press: New York.
  • 10
    • 0038038526 scopus 로고    scopus 로고
    • Potato plants lacking the cdsp32 plastidic thioredoxin exhibit overoxidation of the bas1 2-cysteine peroxiredoxin and increased lipid peroxidation in thylakoids under photooxidative stress
    • Broin, M., and Rey, P. 2003. Potato plants lacking the cdsp32 plastidic thioredoxin exhibit overoxidation of the bas1 2-cysteine peroxiredoxin and increased lipid peroxidation in thylakoids under photooxidative stress. Plant Physiol. 132:1335-1343.
    • (2003) Plant Physiol , vol.132 , pp. 1335-1343
    • Broin, M.1    Rey, P.2
  • 11
    • 0030249317 scopus 로고    scopus 로고
    • Two members of the thioredoxin-h family interact with the kinase domain of a Brassica S locus receptor kinase
    • Bower, M. S., Matias, D. D., Fernandes-Carvalho, E., Mazzurco, M., Gu, T., Gu, T., Rothstein, S., and Goring, D. R. 1996. Two members of the thioredoxin-h family interact with the kinase domain of a Brassica S locus receptor kinase. Pant Cell 8:1641-1650.
    • (1996) Pant Cell , vol.8 , pp. 1641-1650
    • Bower, M.S.1    Matias, D.D.2    Fernandes-Carvalho, E.3    Mazzurco, M.4    Gu, T.5    Gu, T.6    Rothstein, S.7    Goring, D.R.8
  • 12
    • 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
  • 15
    • 34548181018 scopus 로고    scopus 로고
    • Use of thiol redox proteins for reducing protein intramolecular disulfide bonds, for improving the quality of cereal products, dough and baked goods and for inactivating snake, bee and scorpion toxins
    • US patent 6113951
    • Buchanan, B. B., Kobrehel, K., Yee, B. C., Wong, J. H., Lozano, R., Jiao, J., and Shin, S. 2000. Use of thiol redox proteins for reducing protein intramolecular disulfide bonds, for improving the quality of cereal products, dough and baked goods and for inactivating snake, bee and scorpion toxins. US patent 6113951.
    • (2000)
    • Buchanan, B.B.1    Kobrehel, K.2    Yee, B.C.3    Wong, J.H.4    Lozano, R.5    Jiao, J.6    Shin, S.7
  • 16
    • 0035826255 scopus 로고    scopus 로고
    • The S-locus receptor kinase is inhibited by thioredoxins and activated by pollen coat proteins
    • Cabrillac, D., Cock, J. M., Dumas, C., and Gaude, T. 2001. The S-locus receptor kinase is inhibited by thioredoxins and activated by pollen coat proteins. Nature 410:220-223.
    • (2001) Nature , vol.410 , pp. 220-223
    • Cabrillac, D.1    Cock, J.M.2    Dumas, C.3    Gaude, T.4
  • 18
    • 33747884128 scopus 로고    scopus 로고
    • Cloning and characterization of three thioredoxin h isoforms from wheat showing differential expression in seeds
    • Cazalis, R., Pulido, P., Aussenac, T., Pérez-Ruiz, J. M., and Cejudo, F. J. 2006. Cloning and characterization of three thioredoxin h isoforms from wheat showing differential expression in seeds. J. Exp. Bot. 57:2165-2172.
    • (2006) J. Exp. Bot , vol.57 , pp. 2165-2172
    • Cazalis, R.1    Pulido, P.2    Aussenac, T.3    Pérez-Ruiz, J.M.4    Cejudo, F.J.5
  • 19
    • 0030934272 scopus 로고    scopus 로고
    • The CXXC motif: A rheostat in the active site
    • Chivers, P. T., Prehoda, K. E., and Raines, R. T. 1997. The CXXC motif: a rheostat in the active site. Biochemistry 36:4061-4066.
    • (1997) Biochemistry , vol.36 , pp. 4061-4066
    • Chivers, P.T.1    Prehoda, K.E.2    Raines, R.T.3
  • 20
    • 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. USA 96:14641-14646.
    • (1999) Proc. Natl. Acad. Sci. USA , 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
  • 22
    • 2442610947 scopus 로고    scopus 로고
    • The architecture of the binding site in redox protein complexes: Implications for fast dissociation
    • Crowley, P. B., and Carrondo, M. A. 2004. The architecture of the binding site in redox protein complexes: Implications for fast dissociation. Proteins 55:603-612.
    • (2004) Proteins , vol.55 , pp. 603-612
    • Crowley, P.B.1    Carrondo, M.A.2
  • 25
    • 85153985465 scopus 로고
    • Turnover of soluble proteins in the wheat tube sieve
    • Fisher, D. B., Wu, Y., and Ku, M. S. 1992. Turnover of soluble proteins in the wheat tube sieve. Plant Physiol. 100:349-356.
    • (1992) Plant Physiol , vol.100 , pp. 349-356
    • Fisher, D.B.1    Wu, Y.2    Ku, M.S.3
  • 26
    • 0024110181 scopus 로고
    • An NADP/thioredoxin system in leaves: Purification and characterization of NADP-thioredoxin reductase and thioredoxin h from spinach
    • Florencio, F. J., Yee, B. C., Johnson, T. C., and Buchanan, B. B. 1988. An NADP/thioredoxin system in leaves: Purification and characterization of NADP-thioredoxin reductase and thioredoxin h from spinach. Arch. Biochem. Biophys. 266:496-507.
    • (1988) Arch. Biochem. Biophys , vol.266 , pp. 496-507
    • Florencio, F.J.1    Yee, B.C.2    Johnson, T.C.3    Buchanan, B.B.4
  • 27
    • 0141679346 scopus 로고    scopus 로고
    • Identity and functions of CxxC-derived motifs
    • Fomenko, D. E., and Gladyshev, V. N. 2003. Identity and functions of CxxC-derived motifs. Biochemistry 42:11214-11225.
    • (2003) Biochemistry , vol.42 , pp. 11214-11225
    • Fomenko, D.E.1    Gladyshev, V.N.2
  • 28
    • 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
  • 29
    • 0346366724 scopus 로고    scopus 로고
    • Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction
    • Gelhaye, E., Rouhier N., and Jacquot, J.-P. 2003. Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction. FEBS Lett. 555:443-448.
    • (2003) FEBS Lett , vol.555 , pp. 443-448
    • Gelhaye, E.1    Rouhier, N.2    Jacquot, J.-P.3
  • 33
    • 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. J. Plant Physiol. Mol. Biol. 33:18-24.
    • (2007) J. Plant Physiol. Mol. Biol , vol.33 , pp. 18-24
    • Guo, H.X.1    Yin, J.2    Ren, J.P.3    Wang, Z.Y.4    Chen, H.L.5
  • 34
    • 0028821270 scopus 로고
    • Differentiation of six distinct thioredoxins in seeds of soybean
    • Häberlein, I., Wolf, M., Mohr, L., and Follmann, H. 1995. Differentiation of six distinct thioredoxins in seeds of soybean. J. Plant Physiol. 146:385-392.
    • (1995) J. Plant Physiol , vol.146 , pp. 385-392
    • Häberlein, I.1    Wolf, M.2    Mohr, L.3    Follmann, H.4
  • 35
    • 0025341185 scopus 로고
    • Contrasting evolutionary histories of chloroplast thioredoxins f and m
    • Hartman, H., Syvanen, M., and Buchanan, B. B. 1990. Contrasting evolutionary histories of chloroplast thioredoxins f and m. Mol. Biol. Evol. 7:247-254.
    • (1990) Mol. Biol. Evol , vol.7 , pp. 247-254
    • Hartman, H.1    Syvanen, M.2    Buchanan, B.B.3
  • 36
    • 0018728098 scopus 로고
    • Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action
    • Holmgren, A. 1979. Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action. J. Biol. Chem. 254:9113-9119.
    • (1979) J. Biol. Chem , vol.254 , pp. 9113-9119
    • Holmgren, A.1
  • 37
    • 0000962563 scopus 로고
    • Three dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 Angström resolution
    • Holmgren, A., Söderberg, B. O., Eklund, H., and Bränden, C. I. 1975. Three dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 Angström resolution. Proc. Natl. Acad. Sci. USA 72:2305-2309.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 2305-2309
    • Holmgren, A.1    Söderberg, B.O.2    Eklund, H.3    Bränden, C.I.4
  • 38
    • 0017904146 scopus 로고
    • Thioredoxin from Escherichia coli. Radioimmunological and enzymatic determinations in wild type cells and mutants defective in phage T7 DNA replication
    • Holmgren, A., Ohlsson, I., and Grankvist, M. L. 1978. Thioredoxin from Escherichia coli. Radioimmunological and enzymatic determinations in wild type cells and mutants defective in phage T7 DNA replication. J. Biol. Chem. 253:430-436.
    • (1978) J. Biol. Chem , vol.253 , pp. 430-436
    • Holmgren, A.1    Ohlsson, I.2    Grankvist, M.L.3
  • 40
    • 0032080260 scopus 로고    scopus 로고
    • Rice phloem thioredoxin h has the capacity to mediate its own cell-to-cell transport through plasmodesmata
    • Ishiwatari, Y., Fijiwara, T., McFarland, K. C., Nemoto, K., Hayashi, H,. Chino, M., and Lucas, W. J. 1998. Rice phloem thioredoxin h has the capacity to mediate its own cell-to-cell transport through plasmodesmata. Planta 205:12-22.
    • (1998) Planta , vol.205 , pp. 12-22
    • Ishiwatari, Y.1    Fijiwara, T.2    McFarland, K.C.3    Nemoto, K.4    Hayashi, H.5    Chino, M.6    Lucas, W.J.7
  • 41
    • 0018072333 scopus 로고
    • Evidence for the existence of several enzyme-specific thioredoxins in plants
    • Jacquot, J. P., Vidal, J., Gadal, P, and Schürmann, P.1978. Evidence for the existence of several enzyme-specific thioredoxins in plants. FEBS Lett. 94:243-246.
    • (1978) FEBS Lett , vol.94 , pp. 243-246
    • Jacquot, J.P.1    Vidal, J.2    Gadal, P.3    Schürmann, P.4
  • 42
    • 0028354036 scopus 로고
    • Arabidopsis thaliana NADPH thioredoxin reductase. cDNA characterization and expression of the recombinant protein in Escherichia coli
    • Jacquot, J. P., Rivera-Madrid, R., Marinho, P., Kollarova, M., Le Maréchal, P., Miginiac-Maslow, M., and Meyer, Y. 1994. Arabidopsis thaliana NADPH thioredoxin reductase. cDNA characterization and expression of the recombinant protein in Escherichia coli. J. Mol. Biol. 235:1357-1363.
    • (1994) J. Mol. Biol , vol.235 , pp. 1357-1363
    • Jacquot, J.P.1    Rivera-Madrid, R.2    Marinho, P.3    Kollarova, M.4    Le Maréchal, P.5    Miginiac-Maslow, M.6    Meyer, Y.7
  • 43
    • 0028774178 scopus 로고
    • High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin
    • Jeng, M. F., Campbell, A. P., Begley, T., Holmgren, A., Case, D. A., Wright, P. E., and Dyson, H. J. 1994. High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. Structure 2:853-868.
    • (1994) Structure , vol.2 , pp. 853-868
    • Jeng, M.F.1    Campbell, A.P.2    Begley, T.3    Holmgren, A.4    Case, D.A.5    Wright, P.E.6    Dyson, H.J.7
  • 46
    • 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
  • 49
    • 0038393110 scopus 로고    scopus 로고
    • Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii
    • Lemaire, S. D., Collin, V., Keryer, E., Quesada, A. L., and Miginiac-Maslow, M. 2003 Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii. FEBS Lett. 543:87-92.
    • (2003) FEBS Lett , vol.543 , pp. 87-92
    • Lemaire, S.D.1    Collin, V.2    Keryer, E.3    Quesada, A.L.4    Miginiac-Maslow, M.5
  • 52
    • 33947262279 scopus 로고    scopus 로고
    • Effects of antisense trxs on germination of transgenic wheat seeds
    • Liu, L., Yin, J., Ren, J. P., and Han, J. F., 2004. Effects of antisense trxs on germination of transgenic wheat seeds. Acta Agron. Sin. 30:801-805.
    • (2004) Acta Agron. Sin , vol.30 , pp. 801-805
    • Liu, L.1    Yin, J.2    Ren, J.P.3    Han, J.F.4
  • 53
    • 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
  • 54
    • 0037636244 scopus 로고    scopus 로고
    • Identification, cloning and characterization of two thioredoxin h isoforms. HvTrx h1 and HvTrx h2, from barley seed proteome
    • Maeda, K., Finnie, C., Ostergaard, O., and Svensson, B. 2003. Identification, cloning and characterization of two thioredoxin h isoforms. HvTrx h1 and HvTrx h2, from barley seed proteome. Eur. J. Biochem. 270:2633-2643.
    • (2003) Eur. J. Biochem , vol.270 , pp. 2633-2643
    • Maeda, K.1    Finnie, C.2    Ostergaard, O.3    Svensson, B.4
  • 55
    • 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
  • 56
    • 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
  • 57
    • 33846393586 scopus 로고    scopus 로고
    • Structural basis for target protein recognition by the protein disulfide reductase thioredoxin
    • Maeda, K., Hägglund, P., Finnie, C., Svensson, B., and Henriksen, A. 2006. Structural basis for target protein recognition by the protein disulfide reductase thioredoxin. Structure 14:1701-1710.
    • (2006) Structure , vol.14 , pp. 1701-1710
    • Maeda, K.1    Hägglund, P.2    Finnie, C.3    Svensson, B.4    Henriksen, A.5
  • 58
    • 44349183189 scopus 로고    scopus 로고
    • Crystal structures of barley thioredoxin h isoforms HvTrxh1 andHvTrxh2 reveal features involved in protein recognition and possibly in discriminating the isoform specificity
    • Maeda, K., Hägglund, P., Finnie, C., Svensson, B., and Henriksen, A. 2008. Crystal structures of barley thioredoxin h isoforms HvTrxh1 andHvTrxh2 reveal features involved in protein recognition and possibly in discriminating the isoform specificity. Protein Sci. 17:1015-1024.
    • (2008) Protein Sci , vol.17 , pp. 1015-1024
    • Maeda, K.1    Hägglund, P.2    Finnie, C.3    Svensson, B.4    Henriksen, A.5
  • 59
    • 0029165589 scopus 로고
    • Thioredoxin: A fold for all reasons
    • Martin, J. L. 1995. Thioredoxin: A fold for all reasons. Structure 3:245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 60
    • 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
  • 62
    • 0035078188 scopus 로고    scopus 로고
    • Identification of a cysteine required for the interaction of two thioredoxin h proteins with the kinase domain of the S locus receptor kinase
    • Mazzurco, M., Sulaman, W., Elina, H., Cock, J. M., and Goring, D. R. 2001. Identification of a cysteine required for the interaction of two thioredoxin h proteins with the kinase domain of the S locus receptor kinase. Plant Mol. Biol. 45:365-376.
    • (2001) Plant Mol. Biol , vol.45 , pp. 365-376
    • Mazzurco, M.1    Sulaman, W.2    Elina, H.3    Cock, J.M.4    Goring, D.R.5
  • 63
    • 85153976102 scopus 로고    scopus 로고
    • The Arabidopsis thaliana genome encodes at least four thioredoxins m and a new prokaryotic-like thioredoxin
    • Mestre-Ortega, D., and Meyer, Y. 1999. The Arabidopsis thaliana genome encodes at least four thioredoxins m and a new prokaryotic-like thioredoxin. Gene 240:7109-7117.
    • (1999) Gene , vol.240 , pp. 7109-7117
    • Mestre-Ortega, D.1    Meyer, Y.2
  • 64
    • 0036119804 scopus 로고    scopus 로고
    • Classification of plant thioredoxins by sequence similarity and intron position
    • Meyer, Y., Vignols, F., and Reichheld, J. P. 2002. Classification of plant thioredoxins by sequence similarity and intron position. Methods Enzymol. 347:394-402.
    • (2002) Methods Enzymol , vol.347 , pp. 394-402
    • Meyer, Y.1    Vignols, F.2    Reichheld, J.P.3
  • 65
    • 29944441650 scopus 로고    scopus 로고
    • Thioredoxins in Arabidopsis and other plants
    • Meyer, Y., Reichheld, J.-P., and Vignols, F. 2005. Thioredoxins in Arabidopsis and other plants. Photosynth. Res. 86:419-433.
    • (2005) Photosynth. Res , vol.86 , pp. 419-433
    • Meyer, Y.1    Reichheld, J.-P.2    Vignols, F.3
  • 68
    • 34247604468 scopus 로고    scopus 로고
    • Reduction of 1-cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin c
    • Monteiro, G., Horta, B. B., Pimenta, D. C., Augusto, O., and Netto, L. E. S. 2007. Reduction of 1-cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin c, Proc. Natl. Acad. Sci. USA 104:4886-4891.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 4886-4891
    • Monteiro, G.1    Horta, B.B.2    Pimenta, D.C.3    Augusto, O.4    Netto, L.E.S.5
  • 69
    • 0035949574 scopus 로고    scopus 로고
    • Comprehensive survey of proteins targeted by chloroplast thioredoxin
    • Motohashi, K., Kondoh, A., Stumpp, M. T., and Hisabori, T. 2001. Comprehensive survey of proteins targeted by chloroplast thioredoxin. Proc. Natl. Acad. Sci. USA 98:11224-11229.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11224-11229
    • Motohashi, K.1    Kondoh, A.2    Stumpp, M.T.3    Hisabori, T.4
  • 70
    • 0034652113 scopus 로고    scopus 로고
    • Thioredoxin reductase
    • Mustacich, D., and Powis, G. 2000. Thioredoxin reductase. Biochem. J. 346:1-8.
    • (2000) Biochem. J , vol.346 , pp. 1-8
    • Mustacich, D.1    Powis, G.2
  • 71
    • 33845631208 scopus 로고    scopus 로고
    • Plant glutathione peroxidase are functional peroxiredoxins distributed in several subcellular compartments and regulated during hiotic and ahiotic stresses
    • Navrot, N., Collin, V., Gualberto, J., Gelhaye, E., Hirasawa, M., Rey, P., Knaff, D. B., Issakidis, E., Jacquot, J.-P., and Rouhier, N. 2006. Plant glutathione peroxidase are functional peroxiredoxins distributed in several subcellular compartments and regulated during hiotic and ahiotic stresses. Plant Physiol. 142:1364-1379.
    • (2006) Plant Physiol , vol.142 , pp. 1364-1379
    • Navrot, N.1    Collin, V.2    Gualberto, J.3    Gelhaye, E.4    Hirasawa, M.5    Rey, P.6    Knaff, D.B.7    Issakidis, E.8    Jacquot, J.-P.9    Rouhier, N.10
  • 74
    • 0033914955 scopus 로고    scopus 로고
    • Expression of thioredoxins f and m, and of their targets fructose-1,6-bisphosphatase and NADP-malate dehydrogenase, in pea plants grown under normal and light/temperature stress conditions
    • Pagano, E. A., Chueca, A., and Lopez-Gorge, J. 2000. Expression of thioredoxins f and m, and of their targets fructose-1,6-bisphosphatase and NADP-malate dehydrogenase, in pea plants grown under normal and light/temperature stress conditions. J. Exp. Bot. 51:1299-1307.
    • (2000) J. Exp. Bot , vol.51 , pp. 1299-1307
    • Pagano, E.A.1    Chueca, A.2    Lopez-Gorge, J.3
  • 75
    • 0028773644 scopus 로고
    • The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin
    • Qin, J., Clore, G. M., and Gronenbom, A. M. 1994. The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure 2:503-522.
    • (1994) Structure , vol.2 , pp. 503-522
    • Qin, J.1    Clore, G.M.2    Gronenbom, A.M.3
  • 77
    • 0038699131 scopus 로고    scopus 로고
    • The small GTPase ran: Interpreting the signs
    • Quimby, B. B., and Dasso, M. 2003. The small GTPase ran: Interpreting the signs. Curr. Opin. Cell. Biol. 15:338-344.
    • (2003) Curr. Opin. Cell. Biol , vol.15 , pp. 338-344
    • Quimby, B.B.1    Dasso, M.2
  • 79
    • 11844285694 scopus 로고    scopus 로고
    • AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana
    • Reichheld, J. P., Meyer, E., Khafif, M., Bonnard, G., and Meyer, Y. 2005. AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana. FEBS Lett. 579:337-342.
    • (2005) FEBS Lett , vol.579 , pp. 337-342
    • Reichheld, J.P.1    Meyer, E.2    Khafif, M.3    Bonnard, G.4    Meyer, Y.5
  • 80
    • 34547698762 scopus 로고    scopus 로고
    • Inactivation of thioredoxin reductases reveals a complex interplay between thioredoxin and glutathione pathways in Arabidopsis development
    • Reichheld, J.-P., Khafif, M., Riondet, C., Droux, M., Bonnard, G., and Meyer, Y. 2007. Inactivation of thioredoxin reductases reveals a complex interplay between thioredoxin and glutathione pathways in Arabidopsis development. Plant Cell 19:1851-1865.
    • (2007) Plant Cell , vol.19 , pp. 1851-1865
    • Reichheld, J.-P.1    Khafif, M.2    Riondet, C.3    Droux, M.4    Bonnard, G.5    Meyer, Y.6
  • 81
    • 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, Y. 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, Y.3
  • 82
    • 0035202123 scopus 로고    scopus 로고
    • Isolation and characterization of a new peroxiredoxin from poplar sieve a tube that uses either glutaredoxin or thioredoxin as a proton donor
    • Rouhier, N., Gelhaye, E., Sautiere, P. E., Brun, A., Laurent, P., Tagu, D., Gerard, J., de Fäy, E., Meyer, Y., and Jacquot, J. P. 2001. Isolation and characterization of a new peroxiredoxin from poplar sieve a tube that uses either glutaredoxin or thioredoxin as a proton donor. Plant Physiol. 127:1299-1309.
    • (2001) Plant Physiol , vol.127 , pp. 1299-1309
    • Rouhier, N.1    Gelhaye, E.2    Sautiere, P.E.3    Brun, A.4    Laurent, P.5    Tagu, D.6    Gerard, J.7    de Fäy, E.8    Meyer, Y.9    Jacquot, J.P.10
  • 84
    • 33749856059 scopus 로고    scopus 로고
    • Plant methionine sulfoxide reductase a and b multigenic families
    • Rouhier, N., Vieira Dos Santos, C., Tarrago, L., and Rey, P. 2006. Plant methionine sulfoxide reductase a and b multigenic families, Photosynth. Res. 89:247-262.
    • (2006) Photosynth. Res , vol.89 , pp. 247-262
    • Rouhier, N.1    Vieira Dos Santos, C.2    Tarrago, L.3    Rey, P.4
  • 86
  • 88
    • 0000234911 scopus 로고
    • Specific proteins in the sieve tube exudates of Ricinus communis L. seedlings: Separation, characterization and in vivo labeling
    • Sakuth, T., Schobert, C., Pecsvaradi, A., Eichholz, A., Komor, E., and Orlich, G. 1993. Specific proteins in the sieve tube exudates of Ricinus communis L. seedlings: Separation, characterization and in vivo labeling. Planta 91:207-213.
    • (1993) Planta , vol.91 , pp. 207-213
    • Sakuth, T.1    Schobert, C.2    Pecsvaradi, A.3    Eichholz, A.4    Komor, E.5    Orlich, G.6
  • 89
    • 0033607660 scopus 로고    scopus 로고
    • The male determinant of self-incompatibility in Brassica
    • Schopfer, C. R., Nasrallah, M. E., and Nasrallah, J. B. 1999. The male determinant of self-incompatibility in Brassica. Science 286:1697-1700.
    • (1999) Science , vol.286 , pp. 1697-1700
    • Schopfer, C.R.1    Nasrallah, M.E.2    Nasrallah, J.B.3
  • 92
    • 0042209787 scopus 로고    scopus 로고
    • Type-h thioredoxins accumulate in the nucleus of developing wheat seed tissues suffering oxidative stress
    • Serrato, A. J., and Cejudo, F. J. 2003. Type-h thioredoxins accumulate in the nucleus of developing wheat seed tissues suffering oxidative stress. Planta 217:392-399.
    • (2003) Planta , vol.217 , pp. 392-399
    • Serrato, A.J.1    Cejudo, F.J.2
  • 93
    • 0034928212 scopus 로고    scopus 로고
    • Characterization of two thioredoxins h with predominant localization in the nucleus of aleurone and scutellum cells of germinating wheat seeds
    • Serrato, A. J. Crespo, J. L., Florencio, F. J., and Cejudo, F. J. 2001. Characterization of two thioredoxins h with predominant localization in the nucleus of aleurone and scutellum cells of germinating wheat seeds. Plant Mol. Biol. 46:361-371.
    • (2001) Plant Mol. Biol , vol.46 , pp. 361-371
    • Serrato, A.J.1    Crespo, J.L.2    Florencio, F.J.3    Cejudo, F.J.4
  • 94
    • 0037108728 scopus 로고    scopus 로고
    • Cloning of thioredoxin h reductase and characterization of the thioredoxin reductase-thioredoxin h system from wheat
    • Serrato, A. J., Pérez-Ruiz, J. M., and Cejudo, F. J. 2002. Cloning of thioredoxin h reductase and characterization of the thioredoxin reductase-thioredoxin 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
  • 95
    • 6344235622 scopus 로고    scopus 로고
    • A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana
    • Serrato, A. J., Pérez-Ruiz, J. M., Spínola, M. C., and Cejudo, F. J. 2004. A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana. J. Biol. Chem. 279:43821-43827.
    • (2004) J. Biol. Chem , vol.279 , pp. 43821-43827
    • Serrato, A.J.1    Pérez-Ruiz, J.M.2    Spínola, M.C.3    Cejudo, F.J.4
  • 96
    • 45249107767 scopus 로고    scopus 로고
    • AtCXXS: Atypical members of the Arabidopsis thaliana thioredoxin h family with a remarkably high disulfide isomerase activity
    • Serrato, A. J., Guilleminot, J., Meyer, Y., and Florence Vignols, F. 2008. AtCXXS: Atypical members of the Arabidopsis thaliana thioredoxin h family with a remarkably high disulfide isomerase activity. Physiol. Plant. 133:611-622.
    • (2008) Physiol. Plant , vol.133 , pp. 611-622
    • Serrato, A.J.1    Guilleminot, J.2    Meyer, Y.3    Florence Vignols, F.4
  • 97
    • 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
  • 98
    • 0012342479 scopus 로고    scopus 로고
    • Disulphide bonds in wheat gluten proteins
    • Shewry, P. R., and Tatham, A. S. 1997. Disulphide bonds in wheat gluten proteins. J. Cereal Sci. 25:207-227.
    • (1997) J. Cereal Sci , vol.25 , pp. 207-227
    • Shewry, P.R.1    Tatham, A.S.2
  • 99
    • 0030293733 scopus 로고    scopus 로고
    • A novel plasma membrane-bound thioredoxin from soybean
    • Shi, J., and. Bhattacharyya, M. K. 1996. A novel plasma membrane-bound thioredoxin from soybean. Plant Mol. Biol. 32:653-662.
    • (1996) Plant Mol. Biol , vol.32 , pp. 653-662
    • Shi, J.1    Bhattacharyya, M.K.2
  • 102
    • 33749840484 scopus 로고    scopus 로고
    • Thioredoxin-dependent regulation of photosynthetic glyceraldehyde-3-phosphate dehydrogenase: Autonomous vs. CP12-dependent mechanisms
    • Trost, P., Fermani, S., Marri, L., Zaffagnini, M., Falini, G., Scagliarini, S., Pupillo, P., and Sparla, F. 2006. Thioredoxin-dependent regulation of photosynthetic glyceraldehyde-3-phosphate dehydrogenase: autonomous vs. CP12-dependent mechanisms. Photosynth. Res. 89:263-275.
    • (2006) Photosynth. Res , vol.89 , pp. 263-275
    • Trost, P.1    Fermani, S.2    Marri, L.3    Zaffagnini, M.4    Falini, G.5    Scagliarini, S.6    Pupillo, P.7    Sparla, F.8
  • 103
    • 0033538442 scopus 로고    scopus 로고
    • In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family
    • Verdoucq, L., Vignols, F., Jacquot, J. P., Hartier, Y., and Meyer, Y. 1999. In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. J. Biol. Chem. 274:19714-19722.
    • (1999) J. Biol. Chem , vol.274 , pp. 19714-19722
    • Verdoucq, L.1    Vignols, F.2    Jacquot, J.P.3    Hartier, Y.4    Meyer, Y.5
  • 104
    • 34548503203 scopus 로고    scopus 로고
    • Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases b
    • Vieira Dos Santos, C., Laugier, E., Tarrago, L., Massot, V., Issakidis-Bourguet, E., Rouhier, N., and Rey, P. 2007. Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases b. FEBS Lett. 581:4371-4376.
    • (2007) FEBS Lett , vol.581 , pp. 4371-4376
    • Vieira Dos Santos, C.1    Laugier, E.2    Tarrago, L.3    Massot, V.4    Issakidis-Bourguet, E.5    Rouhier, N.6    Rey, P.7
  • 105
    • 28044457914 scopus 로고    scopus 로고
    • A yeast two-hybrid knockout strain to explore thioredoxin-interacting proteins in vivo
    • Vignols, F., Bréhélin, C., Surdin-Kerjan, Y., Thomas, D., and Meyer, Y. 2005. A yeast two-hybrid knockout strain to explore thioredoxin-interacting proteins in vivo. Proc. Natl. Acad. Sci. USA 102:16729-16734.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16729-16734
    • Vignols, F.1    Bréhélin, C.2    Surdin-Kerjan, Y.3    Thomas, D.4    Meyer, Y.5
  • 106
    • 0030924125 scopus 로고    scopus 로고
    • CP12 provides a new mode of light regulation of Calvin cycle activity in higher plants
    • Wedel, N., Soll, J., and Paap, B. K. 1997. CP12 provides a new mode of light regulation of Calvin cycle activity in higher plants. Proc. Natl. Acad. Sci. USA 94:10479-10484.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10479-10484
    • Wedel, N.1    Soll, J.2    Paap, B.K.3
  • 108
    • 0030585429 scopus 로고    scopus 로고
    • Crystal structures of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer
    • Weichsel, A., Gasdaska, J. R., Powis, G., and Montfort, W. R. 1996. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure 4:735-751.
    • (1996) Structure , vol.4 , pp. 735-751
    • Weichsel, A.1    Gasdaska, J.R.2    Powis, G.3    Montfort, W.R.4
  • 111
    • 0008581550 scopus 로고
    • Thioredoxin-dependent deinhibition of pullulanase of barley malt by inactivation of a specific inhibitor protein
    • Wong, J. H., Jiao, J.-A., Kobrehel, K., and Buchanan, B. B. 1995. Thioredoxin-dependent deinhibition of pullulanase of barley malt by inactivation of a specific inhibitor protein. Plant Physiol. 108:67.
    • (1995) Plant Physiol , vol.108 , pp. 67
    • Wong, J.H.1    Jiao, J.-A.2    Kobrehel, K.3    Buchanan, B.B.4
  • 112
    • 0037058928 scopus 로고    scopus 로고
    • Transgenic barley grain overexpressing thioredoxin shows evidence of communication between the endosperm and the embryo and aleurone
    • Wong, J. H., Kim, Y. B., Ren, P-S., Cai, N., Cho, M.-J., Heden, P., Lemaux, P. G., and Buchanan, B. B. 2002. Transgenic barley grain overexpressing thioredoxin shows evidence of communication between the endosperm and the embryo and aleurone. Proc. Natl. Acad. Sci. USA 99:16325-16330.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16325-16330
    • Wong, J.H.1    Kim, Y.B.2    Ren, P.-S.3    Cai, N.4    Cho, M.-J.5    Heden, P.6    Lemaux, P.G.7    Buchanan, B.B.8
  • 113
    • 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
  • 114
    • 2342597074 scopus 로고    scopus 로고
    • Thioredoxin reduction alters the solubility of proteins of wheat starchy endosperm: An early event in cereal germination
    • Wong, J. H., Cai, N., Tanaka, C. K., Vensel, W. H., Hurkman, W. J., and Buchanan, B. B. 2004. Thioredoxin reduction alters the solubility of proteins of wheat starchy endosperm: An early event in cereal 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
  • 117
    • 0034838039 scopus 로고    scopus 로고
    • Redox changes accompanying the degradation of seed storage proteins in germinating rice
    • Yano, H., Wong, J. H., Cho, M.-J., and Buchanan, B. B. 2001a. Redox changes accompanying the degradation of seed storage proteins in germinating rice. Plant Cell Physiol. 42:879-883.
    • (2001) Plant Cell Physiol , vol.42 , pp. 879-883
    • Yano, H.1    Wong, J.H.2    Cho, M.-J.3    Buchanan, B.B.4
  • 119
    • 85153978187 scopus 로고    scopus 로고
    • Zahid, A., Gabarrou, J.-F., and Cazalis, R. 2008. Reducing and cross-linking wheat seed storage proteins with thioredoxin h. In: Consumer Driven Cereal Innovation: Where Science Meets Industry. ICC: Vienna.
    • Zahid, A., Gabarrou, J.-F., and Cazalis, R. 2008. Reducing and cross-linking wheat seed storage proteins with thioredoxin h. In: Consumer Driven Cereal Innovation: Where Science Meets Industry. ICC: Vienna.


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