메뉴 건너뛰기




Volumn 146, Issue 2, 2008, Pages 789-799

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

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; ESCHERICHIA COLI; HORDEUM; HORDEUM VULGARE;

EID: 38949203862     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.107.113639     Document Type: Article
Times cited : (75)

References (58)
  • 1
    • 34247270164 scopus 로고    scopus 로고
    • Unique properties of NADP-thioredoxin reductase C in legumes
    • Alkhalfioui F, Renard M, Montrichard F (2007a) Unique properties of NADP-thioredoxin reductase C in legumes. J Exp Bot 58: 969-978
    • (2007) J Exp Bot , vol.58 , pp. 969-978
    • Alkhalfioui, F.1    Renard, M.2    Montrichard, F.3
  • 3
    • 0029928068 scopus 로고    scopus 로고
    • Thiocalsin: A thioredoxin-linked, substrate-specific protease dependent on calcium
    • Besse I, Wong JH, Kobrehel K, Buchanan BB (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
  • 5
    • 38049070264 scopus 로고    scopus 로고
    • Germination and radicle elongation in barley tracked using proteome analysis of dissected embryo, aleurone layer and endosperm tissues
    • Bønsager BC, Finnie C, Roepstorff P, Svensson B (2007) Germination and radicle elongation in barley tracked using proteome analysis of dissected embryo, aleurone layer and endosperm tissues. Proteomics 7: 4538-4540
    • (2007) Proteomics , vol.7 , pp. 4538-4540
    • Bønsager, B.C.1    Finnie, C.2    Roepstorff, P.3    Svensson, B.4
  • 6
    • 20044367629 scopus 로고    scopus 로고
    • Redox regulation: A broadening horizon
    • Buchanan BB, 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
  • 7
    • 0035826255 scopus 로고    scopus 로고
    • The S-locus receptor kinase is inhibited by thioredoxins and activated by pollen coat proteins
    • Cabrillac D, Cock JM, Dumas C, 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
  • 9
    • 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 JM, Cejudo FJ (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
  • 10
    • 0033428817 scopus 로고    scopus 로고
    • Overexpression of thioredoxin h leads to enhanced activity of starch debranching enzyme (pullulanase) in barley grain
    • Cho MJ, Wong JH, Marx C, Jiang W, Lemaux PG, Buchanan BB (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
  • 11
    • 0030596062 scopus 로고    scopus 로고
    • Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5 Å resolution
    • Dai S, Saarinen M, Ramaswamy S, Meyer Y, Jacquot JP, Eklund H (1996) Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5 Å resolution. J Mol Biol 264: 1044-1057
    • (1996) J Mol Biol , vol.264 , pp. 1044-1057
    • Dai, S.1    Saarinen, M.2    Ramaswamy, S.3    Meyer, Y.4    Jacquot, J.P.5    Eklund, H.6
  • 12
    • 0031803072 scopus 로고    scopus 로고
    • Post-transcriptional gene regulatory mechanisms in eukaryotes: An overview
    • Day DA, Tuite MF (1998) Post-transcriptional gene regulatory mechanisms in eukaryotes: an overview. J Endocrinol 157: 361-371
    • (1998) J Endocrinol , vol.157 , pp. 361-371
    • Day, D.A.1    Tuite, M.F.2
  • 13
    • 0344563591 scopus 로고    scopus 로고
    • Patterns of starchy endospermacidification and protease gene expression in wheat grains following germination
    • Dominguez F, Cejudo FJ (1999) Patterns of starchy endospermacidification and protease gene expression in wheat grains following germination. Plant Physiol 119: 81-88
    • (1999) Plant Physiol , vol.119 , pp. 81-88
    • Dominguez, F.1    Cejudo, F.J.2
  • 14
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman GL (1959) Tissue sulfhydryl groups. Arch Biochem Biophys 82: 70-77
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 15
    • 0034965537 scopus 로고    scopus 로고
    • Enzymes that scavenge reactive oxygen species are down-regulated prior to gibberellic acid-induced programmed cell death in barley aleurone
    • Fath A, Bethke PC, Jones RL (2001) Enzymes that scavenge reactive oxygen species are down-regulated prior to gibberellic acid-induced programmed cell death in barley aleurone. Plant Physiol 126: 156-166
    • (2001) Plant Physiol , vol.126 , pp. 156-166
    • Fath, A.1    Bethke, P.C.2    Jones, R.L.3
  • 16
    • 0035983965 scopus 로고    scopus 로고
    • Proteome analysis of grain filling and seed maturation in barley
    • Finnie C, Melchior S, Roepstorff P, Svensson B (2002) Proteome analysis of grain filling and seed maturation in barley. Plant Physiol 129: 1308-1319
    • (2002) Plant Physiol , vol.129 , pp. 1308-1319
    • Finnie, C.1    Melchior, S.2    Roepstorff, P.3    Svensson, B.4
  • 17
    • 0037953141 scopus 로고    scopus 로고
    • Feasibility study of a tissue-specific approach to barley proteome analysis: Aleurone layer, endosperm, embryo and single seeds
    • Finnie C, Svensson B (2003) Feasibility study of a tissue-specific approach to barley proteome analysis: aleurone layer, endosperm, embryo and single seeds. J Cereal Sci 38: 217-227
    • (2003) J Cereal Sci , vol.38 , pp. 217-227
    • Finnie, C.1    Svensson, B.2
  • 18
    • 0032032912 scopus 로고    scopus 로고
    • Characterization of wheat thioredoxin h cDNA and production of an active Triticum aestivum protein in Escherichia coli
    • Gautier MF, Lullien-Pellerin V, de Lamotte-Guéry F, Guirao A, 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
  • 20
    • 0346366724 scopus 로고    scopus 로고
    • Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction
    • Gelhaye E, Rouhier N, Jacquot JP (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
  • 22
    • 0033057707 scopus 로고    scopus 로고
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry
    • Gobom J, Nordhoff E, Mirgorodskaya E, Ekman R, Roepstorff P (1999) Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J Mass Spectrom 34: 105-116
    • (1999) J Mass Spectrom , vol.34 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5
  • 23
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi SP, Rochon Y, Franza BR, Aebersold R (1999) Correlation between protein and mRNA abundance in yeast. Mol Cell Biol 19: 1720-1730
    • (1999) Mol Cell Biol , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 24
    • 0023825124 scopus 로고
    • Improved silver staining procedure for fast staining in PhastSystem Development Unit. I. Staining of sodium dodecyl sulfate gels
    • Heukeshoven J, Dernick R (1985) Improved silver staining procedure for fast staining in PhastSystem Development Unit. I. Staining of sodium dodecyl sulfate gels. Electrophoresis 9: 28-32
    • (1985) Electrophoresis , vol.9 , pp. 28-32
    • Heukeshoven, J.1    Dernick, R.2
  • 25
    • 0040799938 scopus 로고    scopus 로고
    • Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase, and thioredoxin f-regulated enzymes
    • Hirasawa M, Schürmann P, Jacquot JP, Manieri W, Jacquot P, Keryer E, Hartman FC, Knaff DB (1999) Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase, and thioredoxin f-regulated enzymes. Biochemistry 38: 5200-5205
    • (1999) Biochemistry , vol.38 , pp. 5200-5205
    • Hirasawa, M.1    Schürmann, P.2    Jacquot, J.P.3    Manieri, W.4    Jacquot, P.5    Keryer, E.6    Hartman, F.C.7    Knaff, D.B.8
  • 26
    • 33750973618 scopus 로고    scopus 로고
    • Enrichment and identification of integral membrane proteins from barley aleurone layers by reversed-phase chromatography, SDS-PAGE, and LC-MS/MS
    • Hynek R, Svensson B, Jensen ON, Barkholt V, Finnie C (2006) Enrichment and identification of integral membrane proteins from barley aleurone layers by reversed-phase chromatography, SDS-PAGE, and LC-MS/MS. J Proteome Res 5: 3105-3113
    • (2006) J Proteome Res , vol.5 , pp. 3105-3113
    • Hynek, R.1    Svensson, B.2    Jensen, O.N.3    Barkholt, V.4    Finnie, C.5
  • 28
    • 0031444519 scopus 로고    scopus 로고
    • Thioredoxins: Structure and function in plant cells
    • Jacquot JP, Lancelin JM, Meyer Y (1997) Thioredoxins: structure and function in plant cells. New Phytol 136: 543-570
    • (1997) New Phytol , vol.136 , pp. 543-570
    • Jacquot, J.P.1    Lancelin, J.M.2    Meyer, Y.3
  • 29
    • 0028354036 scopus 로고
    • Arabidopsis thaliana NAPHP thioredoxin reductase. cDNA characterization and expression of the recombinant protein in Escherichia coli
    • Jacquot JP, Rivera-Madrid R, Marinho P, Kollarova M, Le Maréchal P, Miginiac-Maslow M, Meyer Y (1994) Arabidopsis thaliana NAPHP 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
  • 30
    • 0019163962 scopus 로고
    • Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli
    • Kallis GB, Holmgren A (1980) Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli. J Biol Chem 255: 10261-10265
    • (1980) J Biol Chem , vol.255 , pp. 10261-10265
    • Kallis, G.B.1    Holmgren, A.2
  • 32
    • 0025944354 scopus 로고
    • Role of the NADP/thioredoxin system in the reduction of alpha-amylase and trypsin inhibitor proteins
    • Kobrehel K, Yee BC, Buchanan BB (1991) Role of the NADP/thioredoxin system in the reduction of alpha-amylase and trypsin inhibitor proteins. J Biol Chem 266: 16135-16140
    • (1991) J Biol Chem , vol.266 , pp. 16135-16140
    • Kobrehel, K.1    Yee, B.C.2    Buchanan, B.B.3
  • 33
    • 0035109514 scopus 로고    scopus 로고
    • The malaria parasite Plasmodium falciparum possesses a functional thioredoxin system
    • Krnajski Z, Gilberger TW, Walter RD, Müller S (2001) The malaria parasite Plasmodium falciparum possesses a functional thioredoxin system. Mol Biochem Parasitol 112: 219-228
    • (2001) Mol Biochem Parasitol , vol.112 , pp. 219-228
    • Krnajski, Z.1    Gilberger, T.W.2    Walter, R.D.3    Müller, S.4
  • 34
    • 33745194343 scopus 로고    scopus 로고
    • Characterization of mitochondrial thioredoxin reductase from C. elegans
    • Lacey BM, Hondal RJ (2006) Characterization of mitochondrial thioredoxin reductase from C. elegans. Biochem Biophys Res Commun 346: 629-636
    • (2006) Biochem Biophys Res Commun , vol.346 , pp. 629-636
    • Lacey, B.M.1    Hondal, R.J.2
  • 36
    • 0029839611 scopus 로고    scopus 로고
    • New evidence for a role for thioredoxin h in germination and seedling development
    • Lozano RM, Wong JH, Yee BC, Peters A, Kobrehel K, Buchanan BB (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
  • 37
    • 0037636244 scopus 로고    scopus 로고
    • Maeda K, Finnie C, Østergaard O, 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
    • Maeda K, Finnie C, Østergaard O, 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
  • 38
    • 33846393586 scopus 로고    scopus 로고
    • Structural basis for target protein recognition by the protein disulphide reductase thioredoxin
    • Maeda K, Hägglund P, Finnie C, Svensson B, Henriksen A (2006) Structural basis for target protein recognition by the protein disulphide 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
  • 39
    • 0038662709 scopus 로고    scopus 로고
    • Thioredoxin and germinating barley: Targets and protein redox changes
    • Marx C, Wong JH, Buchanan BB (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
  • 40
    • 29944441650 scopus 로고    scopus 로고
    • Thioredoxins in Arabidopsis and other plants
    • Meyer Y, Reichheld JP, 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
  • 41
    • 0036119804 scopus 로고    scopus 로고
    • Classification of plant thioredoxins by sequence similarity and intron position
    • Meyer Y, Vignols F, Reichheld JP (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
  • 42
    • 0030722209 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a novel Escherichia coli thioredoxin
    • Miranda-Vizuete A, Damdimopoulos AE, Gustafsson J, Spyrou G (1997) Cloning, expression, and characterization of a novel Escherichia coli thioredoxin. J Biol Chem 272: 30841-30847
    • (1997) J Biol Chem , vol.272 , pp. 30841-30847
    • Miranda-Vizuete, A.1    Damdimopoulos, A.E.2    Gustafsson, J.3    Spyrou, G.4
  • 43
    • 0038038334 scopus 로고    scopus 로고
    • Identification and differential expression of two thioredoxin h isoforms in germinating seeds from pea
    • Montrichard F, Renard M, Alkhalfioui F, Duval FD, Macherel D (2003) Identification and differential expression of two thioredoxin h isoforms in germinating seeds from pea. Plant Physiol 132: 1707-1715
    • (2003) Plant Physiol , vol.132 , pp. 1707-1715
    • Montrichard, F.1    Renard, M.2    Alkhalfioui, F.3    Duval, F.D.4    Macherel, D.5
  • 44
    • 0034652113 scopus 로고    scopus 로고
    • Thioredoxin reductase
    • Mustacich D, Powis G (2000) Thioredoxin reductase. Biochem J 346: 1-8
    • (2000) Biochem J , vol.346 , pp. 1-8
    • Mustacich, D.1    Powis, G.2
  • 45
    • 0016616415 scopus 로고
    • Eine störungsfreie Mikromethode zur Bestimmung des Proteinghaltes in Gewbehomogenaten.
    • Popov N, Schmitt M, Schulzeck S, Matthies H (1975) Eine störungsfreie Mikromethode zur Bestimmung des Proteinghaltes in Gewbehomogenaten. Acta Biol Med Ger 34: 1441-1446
    • (1975) Acta Biol Med Ger , vol.34 , pp. 1441-1446
    • Popov, N.1    Schmitt, M.2    Schulzeck, S.3    Matthies, H.4
  • 46
    • 11844285694 scopus 로고    scopus 로고
    • AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana
    • Reichheld JP, Meyer E, Khafif M, Bonnard G, 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
  • 47
    • 0042209787 scopus 로고    scopus 로고
    • Type-h thioredoxins accumulate in the nucleus of developing wheat seed tissues suffering oxidative stress
    • Serrato AJ, Cejudo FJ (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
  • 48
    • 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 AJ, Crespo JL, Florencio FJ, Cejudo FJ (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
  • 49
    • 0037108728 scopus 로고    scopus 로고
    • Cloning of thioredoxin h reductase and characterization of the thioredoxin reductase-thioredoxin h system from wheat
    • Serrato AJ, Pérez-Ruiz JM, Cejudo FJ (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
  • 50
    • 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 AJ, Pérez-Ruiz JM, Spínola MC, Cejudo FJ (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
  • 52
    • 0030020576 scopus 로고    scopus 로고
    • A new selenoprotein from human lung adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity
    • Tamura T, Stadtman TC (1996) A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity. Proc Natl Acad Sci USA 93: 1006-1011
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1006-1011
    • Tamura, T.1    Stadtman, T.C.2
  • 53
    • 0022958816 scopus 로고
    • Enhanced chemiluminescent reactions catalyzed by horseradish peroxidase
    • Thorpe GH, Kricka LJ (1986) Enhanced chemiluminescent reactions catalyzed by horseradish peroxidase. Methods Enzymol 133: 331-353
    • (1986) Methods Enzymol , vol.133 , pp. 331-353
    • Thorpe, G.H.1    Kricka, L.J.2
  • 55
    • 2342597074 scopus 로고    scopus 로고
    • Thioredoxin reduction alters the solubility of proteins of wheat starchy endosperm: An early event in cereal germination
    • Wong JH, Cai N, Tanaka CK, Vensel WH, Hurkman WJ, Buchanan BB (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
  • 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 JH, Kim YB, Ren PH, Cai N, Cho MJ, Hedden P, Lemaux PG, Buchanan BB (2002) Transgenic barley grain overexpressing thioredoxin shows evidence that the starchy endosperm communicates with the embryo and the 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.H.3    Cai, N.4    Cho, M.J.5    Hedden, P.6    Lemaux, P.G.7    Buchanan, B.B.8
  • 58
    • 0033662157 scopus 로고    scopus 로고
    • Patterns of regulation from mRNA and protein time series
    • You L, Yin J (2000) Patterns of regulation from mRNA and protein time series. Metab Eng 2: 210-217
    • (2000) Metab Eng , vol.2 , pp. 210-217
    • You, L.1    Yin, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.