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Volumn 132, Issue 3, 2003, Pages 1335-1343

Potato plants lacking the CDSP32 plastidic thioredoxin exhibit overoxidation of the BAS1 2-cysteine peroxiredoxin and increased lipid peroxidation in thylakoids under photooxidative stress

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROPHYLL; ENZYMES; FLUORESCENCE; GENETIC ENGINEERING; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; LIPIDS; PHOTOOXIDATION; STRESSES;

EID: 0038038526     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.103.021626     Document Type: Article
Times cited : (100)

References (52)
  • 1
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arnér ESJ, 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
  • 2
    • 0001438616 scopus 로고    scopus 로고
    • Radical production and scavenging in the chloroplast
    • NR Baker, ed. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Asada K (1996) Radical production and scavenging in the chloroplast. In NR Baker, ed, Advances in Photosynthesis, Vol 5, Photosynthesis and the Environment. Kluwer Academic Publishers, Dordrecht, The Netherlands, pp 123-150
    • (1996) Advances in Photosynthesis, Vol 5, Photosynthesis and the Environment , vol.5 , pp. 123-150
    • Asada, K.1
  • 3
    • 0001558790 scopus 로고
    • Lethal hydroxyl radical production in paraquat-treated plants
    • Babbs CF, Pham JA, Coolbaugh RC (1989) Lethal hydroxyl radical production in paraquat-treated plants. Plant Physiol 90: 1267-1270
    • (1989) Plant Physiol , vol.90 , pp. 1267-1270
    • Babbs, C.F.1    Pham, J.A.2    Coolbaugh, R.C.3
  • 4
    • 0031194690 scopus 로고    scopus 로고
    • The plant 2-Cys peroxiredoxin BAS1 is a nuclear-encoded chloroplast protein: Its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants
    • Baier M, Dietz KJ (1997) The plant 2-Cys peroxiredoxin BAS1 is a nuclear-encoded chloroplast protein: its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants. Plant J 12: 179-190
    • (1997) Plant J , vol.12 , pp. 179-190
    • Baier, M.1    Dietz, K.J.2
  • 5
    • 0033117456 scopus 로고    scopus 로고
    • Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis: Evidence from transgenic Arabidopsis
    • Baier M, Dietz KJ (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
  • 6
    • 0033788736 scopus 로고    scopus 로고
    • Antisense suppression of 2-cysteine peroxiredoxin in Arabidopsis specifically enhances the activities and expression of enzymes associated with ascorbate metabolism but not glutathione metabolism
    • Baier M, Noctor G, Foyer C, Dietz KJ (2000) Antisense suppression of 2-cysteine peroxiredoxin in Arabidopsis specifically enhances the activities and expression of enzymes associated with ascorbate metabolism but not glutathione metabolism. Plant Physiol 124: 823-832
    • (2000) Plant Physiol , vol.124 , pp. 823-832
    • Baier, M.1    Noctor, G.2    Foyer, C.3    Dietz, K.J.4
  • 8
    • 0038522835 scopus 로고    scopus 로고
    • Evidence for post-translational control in the expression of a gene encoding a plastidic thioredoxin during leaf development in Solarium tuberosum plants
    • Broin M, Besse I, Rey P (2003) Evidence for post-translational control in the expression of a gene encoding a plastidic thioredoxin during leaf development in Solarium 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
  • 9
    • 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, 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
  • 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, 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
    • 0008157015 scopus 로고
    • Arabidopsis mutants and genetic approaches to the control of lipid composition
    • AR Cossins, ed. Portland Press, London
    • Browse J, Miquel M, McConn M, Wu J (1994) Arabidopsis mutants and genetic approaches to the control of lipid composition. In AR Cossins, ed, Temperature Adaptation of Biological Membranes. Portland Press, London, pp 141-154
    • (1994) Temperature Adaptation of Biological Membranes , pp. 141-154
    • Browse, J.1    Miquel, M.2    McConn, M.3    Wu, J.4
  • 12
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae HZ, Chung SJ, Rhee SG (1994a) 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
  • 13
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large farruly of antioxidant enzymes
    • Chae HZ, Robinson K, Poole LB, Church G, Storz G, Rhee SG (1994b) Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large farruly of antioxidant enzymes. Proc Natl Acad Sci USA 91: 7017-7021
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robinson, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 14
    • 0000650850 scopus 로고    scopus 로고
    • The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux
    • Cheong NE, Choi YO, Lee KO, Kim WY, Jung BG, Chi YH, Jeong JS, Kim K, Cho MJ, Lee SY (1999) The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux. Plant Mol Biol 40: 825-834
    • (1999) Plant Mol Biol , vol.40 , pp. 825-834
    • Cheong, N.E.1    Choi, Y.O.2    Lee, K.O.3    Kim, W.Y.4    Jung, B.G.5    Chi, Y.H.6    Jeong, J.S.7    Kim, K.8    Cho, M.J.9    Lee, S.Y.10
  • 15
    • 0027975129 scopus 로고
    • Involvement of oxidative processes in the signaling mechanisms leading to the activation of glyceollin synthesis in soybean (Glycine max)
    • Degousée N, Triantaphylidès C, Montillet JL (1994) Involvement of oxidative processes in the signaling mechanisms leading to the activation of glyceollin synthesis in soybean (Glycine max). Plant Physiol: 104: 945-952
    • (1994) Plant Physiol , vol.104 , pp. 945-952
    • Degousée, N.1    Triantaphylidès, C.2    Montillet, J.L.3
  • 17
    • 0036001082 scopus 로고    scopus 로고
    • The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation
    • Dietz KJ, Horling F, König J, Baier M (2002) The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation. J Exp Bot 53: 1321-1329
    • (2002) J Exp Bot , vol.53 , pp. 1321-1329
    • Dietz, K.J.1    Horling, F.2    König, J.3    Baier, M.4
  • 19
    • 0025883245 scopus 로고
    • Structural and functional relations among thioredoxins of different species
    • Eklund H, Gleason FK, Holmgren A (1991) Structural and functional relations among thioredoxins of different species. Prot Struct Funct Genet 11: 13-28
    • (1991) Prot Struct Funct Genet , vol.11 , pp. 13-28
    • Eklund, H.1    Gleason, F.K.2    Holmgren, A.3
  • 21
    • 0033587751 scopus 로고    scopus 로고
    • The violaxanthin cycle protects plants from photooxidative damage by more than one mechanism
    • Havaux M, Niyogi KK (1999) The violaxanthin cycle protects plants from photooxidative damage by more than one mechanism. Proc Natl Acad Sci USA 96: 8762-8767
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8762-8767
    • Havaux, M.1    Niyogi, K.K.2
  • 22
    • 0035142197 scopus 로고    scopus 로고
    • Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin
    • Issakidis-Bourguet E, Mouaheb N, Meyer Y, Miginiac-Maslow M (2001) Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin. Plant J 25: 127-135
    • (2001) Plant J , vol.25 , pp. 127-135
    • Issakidis-Bourguet, E.1    Mouaheb, N.2    Meyer, Y.3    Miginiac-Maslow, M.4
  • 23
    • 0036329030 scopus 로고    scopus 로고
    • Leaf discs floated on water are different from intact leaves in photosynthesis and photoinhibition
    • Kato MC, Hikosaka K, Hirose T (2002) Leaf discs floated on water are different from intact leaves in photosynthesis and photoinhibition. Photosynth Res 72: 65-70
    • (2002) Photosynth Res , vol.72 , pp. 65-70
    • Kato, M.C.1    Hikosaka, K.2    Hirose, T.3
  • 24
    • 0032450522 scopus 로고    scopus 로고
    • Inactivation by gene disruption of 2-cysteine peroxiredoxin in Synechocystis sp. PCC 6803 leads to increased stress sensitivity
    • Klughammer B, Baier M, Dietz KJ (1998) Inactivation by gene disruption of 2-cysteine peroxiredoxin in Synechocystis sp. PCC 6803 leads to increased stress sensitivity. Physiol Plant 104: 699-706
    • (1998) Physiol Plant , vol.104 , pp. 699-706
    • Klughammer, B.1    Baier, M.2    Dietz, K.J.3
  • 25
    • 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, Dietz KJ (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
  • 26
    • 0028057226 scopus 로고
    • YAP1 dependent activation of TRX2 is essential for the response of Saccharomyces cerevisiae to oxidative stress by hydroperoxides
    • Kuge S, Jones N (1994) YAP1 dependent activation of TRX2 is essential for the response of Saccharomyces cerevisiae to oxidative stress by hydroperoxides. EMBO J 13: 655-664
    • (1994) EMBO J , vol.13 , pp. 655-664
    • Kuge, S.1    Jones, N.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli UK (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
  • 28
    • 0033582416 scopus 로고    scopus 로고
    • A new antioxidant with alkyl hydroperoxide defense properties in yeast
    • Lee J, Spector D, Godon C, Labarre J, Toledano MB (1999) A new antioxidant with alkyl hydroperoxide defense properties in yeast. J Biol Chem 27: 4537-4544
    • (1999) J Biol Chem , vol.27 , pp. 4537-4544
    • Lee, J.1    Spector, D.2    Godon, C.3    Labarre, J.4    Toledano, M.B.5
  • 29
    • 0028171293 scopus 로고
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell 79: 583-593
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.3    Lamb, C.4
  • 30
    • 0033529335 scopus 로고    scopus 로고
    • The alternative oxidase lowers mitochondrial reactive oxygen production in plant cells
    • Maxwell DP, Wang Y, McIntosh L (1999) The alternative oxidase lowers mitochondrial reactive oxygen production in plant cells. Proc Natl Acad Sci USA 96: 8271-8276
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8271-8276
    • Maxwell, D.P.1    Wang, Y.2    McIntosh, L.3
  • 31
    • 0033214489 scopus 로고    scopus 로고
    • Plant thioredoxins and glutaredoxins: Identity and putative roles
    • Meyer Y, Verdoucq L, 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
  • 32
    • 0003096040 scopus 로고
    • A rapid method for isolation of purified physiologically active chloroplasts used to study the intracellular distribution of amino acids in pea leaves
    • Mills WR, Joy KW (1980) A rapid method for isolation of purified physiologically active chloroplasts used to study the intracellular distribution of amino acids in pea leaves. Planta 148: 75-83
    • (1980) Planta , vol.148 , pp. 75-83
    • Mills, W.R.1    Joy, K.W.2
  • 34
    • 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, 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
  • 35
    • 0025740886 scopus 로고
    • Thioredoxin deficiency in yeast prolongs S phase and shortens G1 interval of the cell cycle
    • Muller EGD (1991) Thioredoxin deficiency in yeast prolongs S phase and shortens G1 interval of the cell cycle. J Biol Chem 266: 9194-9202
    • (1991) J Biol Chem , vol.266 , pp. 9194-9202
    • Muller, E.G.D.1
  • 37
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue culture
    • Murashige T, Skoog F (1962) A revised medium for rapid growth and bioassays with tobacco tissue culture. Physiol Plant 15: 473-497
    • (1962) Physiol Plant , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 38
    • 0032190375 scopus 로고    scopus 로고
    • R, an RNA polymerase sigma factor that modulates expression of the thioredoxin system in response to oxidative stress in Streptomyces coelicolor A3(2)
    • R, an RNA polymerase sigma factor that modulates expression of the thioredoxin system in response to oxidative stress in Streptomyces coelicolor A3(2). EMBO J 17: 5776-5782
    • (1998) EMBO J , vol.17 , pp. 5776-5782
    • Paget, M.S.B.1    Kang, J.G.2    Roe, J.H.3    Buttner, M.J.4
  • 39
    • 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 LB, Godzik A, Nayeem A, Schmitt JD (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
  • 41
    • 0001003626 scopus 로고    scopus 로고
    • Effects of low temperature, high salinity and exogenous ABA on the synthesis of two chloroplastic drought-induced proteins in Solarium tuberosum
    • Pruvot G, Massimino J, Peltier G, Rey P (1996) Effects of low temperature, high salinity and exogenous ABA on the synthesis of two chloroplastic drought-induced proteins in Solarium tuberosum. Physiol Plant 97: 123-131
    • (1996) Physiol Plant , vol.97 , pp. 123-131
    • Pruvot, G.1    Massimino, J.2    Peltier, G.3    Rey, P.4
  • 42
    • 0037205455 scopus 로고    scopus 로고
    • Proteomics analysis of cellular response to oxidative stress: Evidence for in vivo overoxidation of peroxiredoxins at their active site
    • Rabilloud T, Heller M, Gasnier F, Luche S, Rey C, Aebersold R, Benahmed M, Louisot P, Lunardi J (2002) Proteomics analysis of cellular response to oxidative stress: evidence for in vivo overoxidation of peroxiredoxins at their active site. J Biol Chem 277: 19396-19401
    • (2002) J Biol Chem , vol.277 , pp. 19396-19401
    • Rabilloud, T.1    Heller, M.2    Gasnier, F.3    Luche, S.4    Rey, C.5    Aebersold, R.6    Benahmed, M.7    Louisot, P.8    Lunardi, J.9
  • 43
    • 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, 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
  • 44
    • 0034723199 scopus 로고    scopus 로고
    • Thioredoxin 2 is involved in the oxidative stress response in Escherichia coli
    • Ritz D, Patel H, Doan B, Zheng M, Aslund F, Storz G, Beckwith J (2000) Thioredoxin 2 is involved in the oxidative stress response in Escherichia coli. J Biol Chem 275: 2505-2512
    • (2000) J Biol Chem , vol.275 , pp. 2505-2512
    • Ritz, D.1    Patel, H.2    Doan, B.3    Zheng, M.4    Aslund, F.5    Storz, G.6    Beckwith, J.7
  • 45
    • 0029809331 scopus 로고    scopus 로고
    • Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns
    • Royo J, Vancanneyt G, Perez AG, Sanz C, Stormann K, Rosahl S, Sanchez-Serrano JJ (1996) Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns. J Biol Chem 271: 21012-21019
    • (1996) J Biol Chem , vol.271 , pp. 21012-21019
    • Royo, J.1    Vancanneyt, G.2    Perez, A.G.3    Sanz, C.4    Stormann, K.5    Rosahl, S.6    Sanchez-Serrano, J.J.7
  • 46
    • 0039132786 scopus 로고    scopus 로고
    • Involvement of lipoxygenase-dependent production of fatty acid hydroperoxides in the development of the hypersensitive cell death induced by cryptogein on tobacco leaves
    • Rustérucci C, Montillet JL, Agnel JP, Battesti C, Alonso B, Knoll A, Bessoule JJ, Etienne P, Suty L, Blein JP et al. (1999) Involvement of lipoxygenase-dependent production of fatty acid hydroperoxides in the development of the hypersensitive cell death induced by cryptogein on tobacco leaves. J Biol Chem 274: 36446-36455
    • (1999) J Biol Chem , vol.274 , pp. 36446-36455
    • Rustérucci, C.1    Montillet, J.L.2    Agnel, J.P.3    Battesti, C.4    Alonso, B.5    Knoll, A.6    Bessoule, J.J.7    Etienne, P.8    Suty, L.9    Blein, J.P.10
  • 48
    • 0028945214 scopus 로고
    • Lipid peroxidation in tobacco leaves treated with the elicitor cryptogein: Evaluation by high temperature thermoluminescence emission and chlorophyll fluorescence
    • Stallaert VM, Ducruet JM, Tavernier E, Blein JP (1995) Lipid peroxidation in tobacco leaves treated with the elicitor cryptogein: evaluation by high temperature thermoluminescence emission and chlorophyll fluorescence. Biochim Biophys Acta 1229: 290-295
    • (1995) Biochim Biophys Acta , vol.1229 , pp. 290-295
    • Stallaert, V.M.1    Ducruet, J.M.2    Tavernier, E.3    Blein, J.P.4
  • 49
    • 0032031942 scopus 로고    scopus 로고
    • Different mechanisms of thioredoxin in its reduced and oxidized forms in defense against hydrogen peroxide in Escherichia coli
    • Takemoto T, Zhang QM, Yonei S (1998) Different mechanisms of thioredoxin in its reduced and oxidized forms in defense against hydrogen peroxide in Escherichia coli. Free Rad Biol Med 24: 556-562
    • (1998) Free Rad Biol Med , vol.24 , pp. 556-562
    • Takemoto, T.1    Zhang, Q.M.2    Yonei, S.3
  • 50
    • 0001438214 scopus 로고    scopus 로고
    • The origin of 115-130°C thermoluminescence bands in chlorophyll containing material
    • Vavilin D, Ducruet JM (1999) The origin of 115-130°C thermoluminescence bands in chlorophyll containing material. Photochem Photobiol 68: 191-198
    • (1999) Photochem Photobiol , vol.68 , pp. 191-198
    • Vavilin, D.1    Ducruet, J.M.2
  • 51
    • 0033538442 scopus 로고    scopus 로고
    • In vivo characterisation of a thioredoxin h target protein defines a new peroxiredoxin family
    • Verdoucq L, Vignols F, Jacquot JP, Chartier Y, 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
  • 52
    • 0028108976 scopus 로고
    • Oxidation pathways for the intracellular probe 2′,7′-dichlorofluorescein
    • Zhu H, Bannenberg GH, Moldeus P, Shertzer HG (1994) Oxidation pathways for the intracellular probe 2′,7′-dichlorofluorescein. Arch Toxicol 68: 582-587
    • (1994) Arch Toxicol , vol.68 , pp. 582-587
    • Zhu, H.1    Bannenberg, G.H.2    Moldeus, P.3    Shertzer, H.G.4


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