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Volumn 41, Issue 1, 2005, Pages 31-42

Analysis of the proteins targeted by CDSP32, a plastidic thioredoxin participating in oxidative stress responses

Author keywords

CDSP32; Chloroplast; Co immunoprecipitation; Oxidative stress; Peroxiredoxin; Thioredoxin

Indexed keywords

AFFINITY CHROMATOGRAPHY; CHLOROPHYLL; DROUGHT; ENVIRONMENTAL IMPACT; ENZYMES; IMMUNOLOGY; OXIDATION; PHOTOSYNTHESIS; PLANTS (BOTANY); PRECIPITATION (CHEMICAL);

EID: 12744274638     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2004.02271.x     Document Type: Article
Times cited : (135)

References (60)
  • 2
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arnér, E.S.J. and Holmgren, A. (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267, 6102-6109.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6102-6109
    • Arnér, E.S.J.1    Holmgren, A.2
  • 3
    • 0033117456 scopus 로고    scopus 로고
    • Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis. Evidence from transgenic Arabidopsis
    • Baier, M. and Dietz, K.J. (1999) Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis. Evidence from transgenic Arabidopsis. Plant Physiol. 119, 1407-1414.
    • (1999) Plant Physiol. , vol.119 , pp. 1407-1414
    • Baier, M.1    Dietz, K.J.2
  • 4
    • 0035831133 scopus 로고    scopus 로고
    • Heterodimer formation between thioredoxin f and fructose 1,6-biphosphatase from spinach chloroplasts
    • Balmer, Y. and Schürmann, P. (2001) Heterodimer formation between thioredoxin f and fructose 1,6-biphosphatase from spinach chloroplasts. FEBS Lett. 492, 58-61.
    • (2001) FEBS Lett. , vol.492 , pp. 58-61
    • Balmer, Y.1    Schürmann, P.2
  • 6
    • 10744230621 scopus 로고    scopus 로고
    • Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria
    • Balmer, Y., Vensel, W.H., Tanaka, C.K. et al. (2004) Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria. Proc. Natl Acad. Sci. USA, 101, 2642-2647.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2642-2647
    • Balmer, Y.1    Vensel, W.H.2    Tanaka, C.K.3
  • 7
    • 1842712573 scopus 로고    scopus 로고
    • Arabidopsis peptide methionine sulfoxide reductase prevents cellular oxidative damage in long nights
    • Bechtold, U., Murphy, D.J. and Mullineaux, P.M. (2004) Arabidopsis peptide methionine sulfoxide reductase prevents cellular oxidative damage in long nights. Plant Cell, 16, 908-919.
    • (2004) Plant Cell , vol.16 , pp. 908-919
    • Bechtold, U.1    Murphy, D.J.2    Mullineaux, P.M.3
  • 8
    • 0043011656 scopus 로고    scopus 로고
    • Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: Similar sequences for divergent gene expression, protein localization and activity
    • Bréhelin, C., Meyer, E.H., de Souris, J.P., Bonnard, G. and Meyer, Y. (2003) Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization and activity. Plant Physiol. 132, 2045-2057.
    • (2003) Plant Physiol. , vol.132 , pp. 2045-2057
    • Bréhelin, C.1    Meyer, E.H.2    De Souris, J.P.3    Bonnard, G.4    Meyer, Y.5
  • 9
    • 0038038526 scopus 로고    scopus 로고
    • Potato plants lacking the CDSP32 plastidic thioredoxin exhibit over-oxidation of the BAS1 2-cys peroxiredoxin and increased lipid peroxidation in thylakoids under photooxidative stress
    • Broin, M. and Rey, P. (2003) Potato plants lacking the CDSP32 plastidic thioredoxin exhibit over-oxidation of the BAS1 2-cys 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
  • 10
    • 0033962438 scopus 로고    scopus 로고
    • Involvement of CDSP32, a drought-induced thioredoxin, in the response to oxidative stress in potato plants
    • Broin, M., Cuiné, S., Peltier, G. and Rey, P. (2000) Involvement of CDSP32, a drought-induced thioredoxin, in the response to oxidative stress in potato plants. FEBS Lett. 467, 245-248.
    • (2000) FEBS Lett. , vol.467 , pp. 245-248
    • Broin, M.1    Cuiné, S.2    Peltier, G.3    Rey, P.4
  • 11
    • 0035983856 scopus 로고    scopus 로고
    • The plastidic 2-cysteine peroxiredoxin is a target for a thioredoxin involved in the protection of the photosynthetic apparatus against oxidative damage
    • Broin, M., Cuiné, S., Eymery, F. and Rey, P. (2002) The plastidic 2-cysteine peroxiredoxin is a target for a thioredoxin involved in the protection of the photosynthetic apparatus against oxidative damage. Plant Cell, 14, 1417-1432.
    • (2002) Plant Cell , vol.14 , pp. 1417-1432
    • Broin, M.1    Cuiné, S.2    Eymery, F.3    Rey, P.4
  • 12
    • 0038522835 scopus 로고    scopus 로고
    • Evidence for post-translational control in the expression of a gene encoding a plastidic thioredoxin during leaf development in Solanum tuberosum plants
    • Broin, M., Besse, I. and Rey, P. (2003) Evidence for post-translational control in the expression of a gene encoding a plastidic thioredoxin during leaf development in Solanum tuberosum plants. Plant Physiol. Biochem. 41, 303-308.
    • (2003) Plant Physiol. Biochem. , vol.41 , pp. 303-308
    • Broin, M.1    Besse, I.2    Rey, P.3
  • 13
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae, H.Z., Chung, S.J. and Rhee, S.G. (1994) Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269, 27670-27678.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.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. 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
  • 15
    • 0003144630 scopus 로고
    • Gene assembly by 'splicing by overlap extension'
    • (McPherson, M.J., Quirke, P. and Taylor, G.R., eds). New York: Oxford University Press
    • Clackson, T., Güssow, D. and Jones, P.T. (1991) Gene assembly by 'splicing by overlap extension'. In PCR, A Practical Approach (McPherson, M.J., Quirke, P. and Taylor, G.R., eds). New York: Oxford University Press, pp. 187-214.
    • (1991) PCR, A Practical Approach , pp. 187-214
    • Clackson, T.1    Güssow, D.2    Jones, P.T.3
  • 17
    • 0142057021 scopus 로고    scopus 로고
    • Plant peroxiredoxins
    • Dietz, K.J. (2003) Plant peroxiredoxins. Ann. Rev. Plant Biol. 54, 93-107.
    • (2003) Ann. Rev. Plant Biol. , vol.54 , pp. 93-107
    • Dietz, K.J.1
  • 18
    • 0025883245 scopus 로고
    • Structural and functional relations among thioredoxins of different species
    • Eklund, H., Gleason, F.K. and Holmgren, A. (1991) Structural and functional relations among thioredoxins of different species. Proteins Struct. Funct. Genet. 11, 13-28.
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 13-28
    • Eklund, H.1    Gleason, F.K.2    Holmgren, A.3
  • 20
    • 0346366724 scopus 로고    scopus 로고
    • Evidence for a subgroup of thioredoxin rithat requires GSH/Grx for its reduction
    • Gelhaye, E., Rouhier, N. and Jacquot, J.P. (2003) Evidence for a subgroup of thioredoxin rithat 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
  • 23
    • 0032052674 scopus 로고    scopus 로고
    • A moderate decrease of plastid aldolase activity inhibits photosynthesis, alters the level of sugars and starch, and inhibits growth of potato plants
    • Haake, V., Zrenner, R., Sonnewald, U. and Stitt, M. (1998) A moderate decrease of plastid aldolase activity inhibits photosynthesis, alters the level of sugars and starch, and inhibits growth of potato plants. Plant J. 14, 147-157.
    • (1998) Plant J. , vol.14 , pp. 147-157
    • Haake, V.1    Zrenner, R.2    Sonnewald, U.3    Stitt, M.4
  • 24
    • 0033514307 scopus 로고    scopus 로고
    • The minimal gene set member msrA, encoding peptide methionine sulfoxide reductase, is a virulence determinant of the plant pathogen Erwinia chrysanthemi
    • Hassouni, M.E., Chambost, J.P., Expert, D., Van Gijsegen, F. and Barras, F. (1999) The minimal gene set member msrA, encoding peptide methionine sulfoxide reductase, is a virulence determinant of the plant pathogen Erwinia chrysanthemi. Proc. Natl Acad. Sci. USA, 96, 887-892.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 887-892
    • Hassouni, M.E.1    Chambost, J.P.2    Expert, D.3    Van Gijsegen, F.4    Barras, F.5
  • 25
    • 0034607966 scopus 로고    scopus 로고
    • Mechanism of activation of the chloroplast ATP synthase. A kinetic study of the thiol modulation of isolated ATPase and membrane-bound ATP synthase from spinach by Escherichia coli thioredoxin
    • He, X., Miginiac-Maslow, M., Sigala, C., Keryer, E. and Haraux, F. (2000) Mechanism of activation of the chloroplast ATP synthase. A kinetic study of the thiol modulation of isolated ATPase and membrane-bound ATP synthase from spinach by Escherichia coli thioredoxin. J. Biol. Chem. 275, 13250-13258.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13250-13258
    • He, X.1    Miginiac-Maslow, M.2    Sigala, C.3    Keryer, E.4    Haraux, F.5
  • 26
    • 0034306117 scopus 로고    scopus 로고
    • A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp)
    • Kong, W., Shiota, S., Shi, Y., Nakayama, H. and Nakayama, K. (2000) A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp). Biochem. J. 351, 107-114.
    • (2000) Biochem. J. , vol.351 , pp. 107-114
    • Kong, W.1    Shiota, S.2    Shi, Y.3    Nakayama, H.4    Nakayama, K.5
  • 27
    • 0037117488 scopus 로고    scopus 로고
    • The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux
    • König, J., Baier, M., Horling, F., Kahmann, U., Harris, G., Schürmann, P. and Dietz, K.J. (2002) The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux. Proc. Natl Acad. Sci. USA, 99, 5738-5743.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5738-5743
    • König, J.1    Baier, M.2    Horling, F.3    Kahmann, U.4    Harris, G.5    Schürmann, P.6    Dietz, K.J.7
  • 28
    • 0037020249 scopus 로고    scopus 로고
    • Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase
    • Kumar, R.A., Koc, A., Cerny, R.L. and Gladishev, V.N. (2002) Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase. J. Biol. Chem. 277, 37527-37535.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37527-37535
    • Kumar, R.A.1    Koc, A.2    Cerny, R.L.3    Gladishev, V.N.4
  • 29
    • 1642363933 scopus 로고    scopus 로고
    • Proteomic analysis of thioredoxin-targetd proteins in Escherichia coli
    • Kumar, J.K., Tabor, S. and Richardson, C.C. (2004) Proteomic analysis of thioredoxin-targetd proteins in Escherichia coli. Proc. Natl Acad. Sci. USA, 101, 3759-3764.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 3759-3764
    • Kumar, J.K.1    Tabor, S.2    Richardson, C.C.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 1642547085 scopus 로고    scopus 로고
    • The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative stress and its W-box-mediated response to pathogen elicitor
    • Laloi, C., Mestres-Ortega, D., Marco, Y., Meyer, Y. and Reichheld, J.P. (2004) The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative stress and its W-box-mediated response to pathogen elicitor. Plant Physiol. 134, 1006-1016.
    • (2004) Plant Physiol. , vol.134 , pp. 1006-1016
    • Laloi, C.1    Mestres-Ortega, D.2    Marco, Y.3    Meyer, Y.4    Reichheld, J.P.5
  • 33
    • 0032197184 scopus 로고    scopus 로고
    • A novel nuclear member of the thioredoxin superfamily
    • Laughner, B.J., Shenke, P.C. and Ferl, R.J. (1998) A novel nuclear member of the thioredoxin superfamily. Plant Physiol. 118, 987-996.
    • (1998) Plant Physiol. , vol.118 , pp. 987-996
    • Laughner, B.J.1    Shenke, P.C.2    Ferl, R.J.3
  • 34
    • 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, M. 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, M.4    Miginiac-Maslow, M.5
  • 36
    • 0000444532 scopus 로고
    • Determination of total carotenoids and chlorophylls a and b of leaf extracts in different solvents
    • Lichtenthaler, H.K. and Wellburn, A.R. (1983) Determination of total carotenoids and chlorophylls a and b of leaf extracts in different solvents. Biochem. Soc. Trans. 603, 591-592.
    • (1983) Biochem. Soc. Trans. , vol.603 , pp. 591-592
    • Lichtenthaler, H.K.1    Wellburn, A.R.2
  • 37
    • 0038662709 scopus 로고    scopus 로고
    • Thioredoxin and germinating barley: Targets and protein redox changes
    • Marx, C., Wong, J.H. and Buchanan, 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.3
  • 38
    • 0034063592 scopus 로고    scopus 로고
    • Chlorophyll fluorescence - A practical guide
    • Maxwell, K. and Johnson, G.N. (2000) Chlorophyll fluorescence - a practical guide. J. Exp. Bot. 51, 659-668.
    • (2000) J. Exp. Bot. , vol.51 , pp. 659-668
    • Maxwell, K.1    Johnson, G.N.2
  • 39
    • 0033214489 scopus 로고    scopus 로고
    • Plant thioredoxins and glutaredoxins: Identity and putative roles
    • Meyer, Y., Verdoucq, L. and Vignols, F. (1999) Plant thioredoxins and glutaredoxins: identity and putative roles. Trends Plant Sci. 4, 388-394.
    • (1999) Trends Plant Sci. , vol.4 , pp. 388-394
    • Meyer, Y.1    Verdoucq, L.2    Vignols, F.3
  • 40
    • 0030955353 scopus 로고    scopus 로고
    • The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo
    • Moskovitz, J., Berlett, B.S., Poston, J.M. and Stadtman, E.R. (1997) The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc. Natl Acad. Sci. USA, 94, 9585-9589.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9585-9589
    • Moskovitz, J.1    Berlett, B.S.2    Poston, J.M.3    Stadtman, E.R.4
  • 41
    • 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
  • 42
    • 0032539799 scopus 로고    scopus 로고
    • In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae
    • Mouaheb, N., Thomas, D., Verdoucq, L., Montfort, P. and Meyer, Y. (1998) In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA, 95, 3312-3317.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3312-3317
    • Mouaheb, N.1    Thomas, D.2    Verdoucq, L.3    Montfort, P.4    Meyer, Y.5
  • 43
    • 0021919918 scopus 로고
    • Identification of DNA sequences required for activity of the cauliflower mosaic virus 35S promoter
    • Odell, J.T., Nagy, F. and Chua, N.H. (1985) Identification of DNA sequences required for activity of the cauliflower mosaic virus 35S promoter. Nature, 313, 810-812.
    • (1985) Nature , vol.313 , pp. 810-812
    • Odell, J.T.1    Nagy, F.2    Chua, N.H.3
  • 44
    • 0034612366 scopus 로고    scopus 로고
    • AhpF can be dissected into two functional units: Tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C-terminus to AhpC
    • Poole, L.B., Godzik, A., Nayeem, A. and Schmitt, J.D. (2000) AhpF can be dissected into two functional units: tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C-terminus to AhpC. Biochemistry, 39, 6602-6615.
    • (2000) Biochemistry , vol.39 , pp. 6602-6615
    • Poole, L.B.1    Godzik, A.2    Nayeem, A.3    Schmitt, J.D.4
  • 45
    • 0030062411 scopus 로고    scopus 로고
    • Characterization of a novel drought-induced 34-kDa protein located in the thylakoids of Solanum tuberosum L. plants
    • Pruvot, G., Cuiné, S., Peltier, G. and Rey, P. (1996) Characterization of a novel drought-induced 34-kDa protein located in the thylakoids of Solanum tuberosum L. plants. Planta, 198, 471-479.
    • (1996) Planta , vol.198 , pp. 471-479
    • Pruvot, G.1    Cuiné, S.2    Peltier, G.3    Rey, P.4
  • 46
    • 0031885601 scopus 로고    scopus 로고
    • A novel thioredoxin-like protein located in the chloroplast is induced by water deficit in Solanum tuberosum L. plants
    • Rey, P., Pruvot, G., Becuwe, N., Eymery, F., Rumeau, D. and Peltier, G. (1998) A novel thioredoxin-like protein located in the chloroplast is induced by water deficit in Solanum tuberosum L. plants. Plant J. 13, 97-107.
    • (1998) Plant J. , vol.13 , pp. 97-107
    • Rey, P.1    Pruvot, G.2    Becuwe, N.3    Eymery, F.4    Rumeau, D.5    Peltier, G.6
  • 47
    • 0035202123 scopus 로고    scopus 로고
    • Isolation and characterization of a new peroxiredoxin from poplar sieve tubes 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 Fa, E., Meyer, Y. and Jacquot, J.P. (2001) Isolation and characterization of a new peroxiredoxin from poplar sieve tubes 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 Fa, E.8    Meyer, Y.9    Jacquot, J.P.10
  • 48
    • 12144287638 scopus 로고    scopus 로고
    • Poplar peroxiredoxin Q. A thioredoxin-linked antioxidant functional in pathogen defense
    • Rouhier, N., Gelhaye, E., Gualberto, J.M. et al. (2004) Poplar peroxiredoxin Q. A thioredoxin-linked antioxidant functional in pathogen defense. Plant Physiol. 134, 1027-1038.
    • (2004) Plant Physiol. , vol.134 , pp. 1027-1038
    • Rouhier, N.1    Gelhaye, E.2    Gualberto, J.M.3
  • 49
    • 0032922625 scopus 로고    scopus 로고
    • Regulation of chloroplast enzyme activities by thioredoxins: Activation or relief from inhibition?
    • Ruelland, E. and Miginiac-Maslow, M. (1999) Regulation of chloroplast enzyme activities by thioredoxins: activation or relief from inhibition? Trends Plant. Sci. 4, 136-141.
    • (1999) Trends Plant. Sci. , vol.4 , pp. 136-141
    • Ruelland, E.1    Miginiac-Maslow, M.2
  • 50
    • 0034070583 scopus 로고    scopus 로고
    • Differential regulation of plastidial and cytosolic isoforms of peptide methionine sulfoxide reductase in Arabidopsis
    • Sadanandom, A., Poghosyan, Z., Fairbairn, D.J. and Murphy, D.J. (2000) Differential regulation of plastidial and cytosolic isoforms of peptide methionine sulfoxide reductase in Arabidopsis. Plant Physiol. 123, 255-263.
    • (2000) Plant Physiol. , vol.123 , pp. 255-263
    • Sadanandom, A.1    Poghosyan, Z.2    Fairbairn, D.J.3    Murphy, D.J.4
  • 51
    • 0023575311 scopus 로고
    • Design and construction of a versatile system for the expression of foreign genes in plants
    • Schardl, C.L., Byrd, A.D., Benzion, G., Altschuler, M.A., Hildebrand, D.F. and Hunt, A.G. (1987) Design and construction of a versatile system for the expression of foreign genes in plants. Gene, 61, 1-11.
    • (1987) Gene , vol.61 , pp. 1-11
    • Schardl, C.L.1    Byrd, A.D.2    Benzion, G.3    Altschuler, M.A.4    Hildebrand, D.F.5    Hunt, A.G.6
  • 53
    • 4244218956 scopus 로고    scopus 로고
    • Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism
    • Stadtman, E.R., Moskowitz, J., Berlett, B.S. and Levine, R.L. (2002) Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism. Mol. Cell Biochem. 234/235, 3-9.
    • (2002) Mol. Cell Biochem. , vol.234-235 , pp. 3-9
    • Stadtman, E.R.1    Moskowitz, J.2    Berlett, B.S.3    Levine, R.L.4
  • 54
    • 0033166052 scopus 로고    scopus 로고
    • Chloroplast thioredoxin mutants without active-site cysteine facilitate the reduction of the regulatory disulphide bridge on the γ-subunit of chloroplast ATP synthase
    • Stumpp, M.T., Motohashi, K. and Hisabori, T. (1999) Chloroplast thioredoxin mutants without active-site cysteine facilitate the reduction of the regulatory disulphide bridge on the γ-subunit of chloroplast ATP synthase. Biochem. J. 341, 157-163.
    • (1999) Biochem. J. , vol.341 , pp. 157-163
    • Stumpp, M.T.1    Motohashi, K.2    Hisabori, T.3
  • 55
    • 0033538442 scopus 로고    scopus 로고
    • In vivo characterisation of a thioredoxin h target protein defines a new peroxiredoxin family
    • Verdoucq, L., Vignols, F., Jacquot, J.P., Chartier, Y. and Meyer, Y. (1999) In vivo characterisation 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    Chartier, Y.4    Meyer, Y.5
  • 56
    • 0000686366 scopus 로고
    • Transformation of homozygous diploid potato with an Agrobacterium tumefaciens binary vector system by adventitious shoot regeneration on leaf and stem segments
    • Visser, R.G.F., Jacoben, E., Hesseleng-Meinders, A., Schans, M.J., Witholt, B. and Feenstra, W.J. (1989) Transformation of homozygous diploid potato with an Agrobacterium tumefaciens binary vector system by adventitious shoot regeneration on leaf and stem segments. Plant Mol. Biol. 12, 329-337.
    • (1989) Plant Mol. Biol. , vol.12 , pp. 329-337
    • Visser, R.G.F.1    Jacoben, E.2    Hesseleng-Meinders, A.3    Schans, M.J.4    Witholt, B.5    Feenstra, W.J.6
  • 57
    • 0029867678 scopus 로고    scopus 로고
    • A stable mixed disulphide between thioredoxin reductase and its substrate, thioredoxin: Preparation and characterisation
    • Wang, P.P., Veine, D.M., Ahn, S.H. and Williams, C.H. (1996) A stable mixed disulphide between thioredoxin reductase and its substrate, thioredoxin: preparation and characterisation. Biochemistry, 35, 4812-4819.
    • (1996) Biochemistry , vol.35 , pp. 4812-4819
    • Wang, P.P.1    Veine, D.M.2    Ahn, S.H.3    Williams, C.H.4
  • 58
    • 0028306066 scopus 로고
    • Ferrous ion oxidation in the presence of ferric ion indicator xylenol orange for measurement of hydroperoxides
    • Wolff, S.P. (1994) Ferrous ion oxidation in the presence of ferric ion indicator xylenol orange for measurement of hydroperoxides. Methods Enzymol. 233, 182-189.
    • (1994) Methods Enzymol. , vol.233 , pp. 182-189
    • Wolff, S.P.1


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