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Volumn 17, Issue 8, 2012, Pages 1124-1160

Thioredoxin and glutaredoxin systems in plants: Molecular mechanisms, crosstalks, and functional significance

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DISULFIDE; GLUTAREDOXIN; GLUTATHIONE; GLUTATHIONE DISULFIDE; IRON SULFUR PROTEIN; PEPTIDYL CARRIER PROTEIN; PHYTOHORMONE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SULFENIC ACID DERIVATIVE; THIOREDOXIN; THIOREDOXIN REDUCTASE;

EID: 84865411350     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2011.4327     Document Type: Review
Times cited : (302)

References (258)
  • 1
    • 77954395496 scopus 로고    scopus 로고
    • Plastidial thioredoxin z interacts with two fructokinase-like proteins in a thiol-dependent manner: Evidence for an essential role in chloroplast development in Arabidopsis and Nicotiana benthamiana
    • Arsova B, Hoja U, Wimmelbacher M, Greiner E, Ustun S, Melzer M, Petersen K, Lein W, and Börnke F. Plastidial thioredoxin z interacts with two fructokinase-like proteins in a thiol-dependent manner: evidence for an essential role in chloroplast development in Arabidopsis and Nicotiana benthamiana. Plant Cell 22: 1498-1515, 2010.
    • (2010) Plant Cell , vol.22 , pp. 1498-1515
    • Arsova, B.1    Hoja, U.2    Wimmelbacher, M.3    Greiner, E.4    Ustun, S.5    Melzer, M.6    Petersen, K.7    Lein, W.8    Börnke, F.9
  • 6
    • 33750900357 scopus 로고    scopus 로고
    • Thioredoxin target proteins in chloroplast thylakoid membranes
    • DOI 10.1089/ars.2006.8.1829
    • Balmer Y, Vensel WH, Hurkman WJ, and Buchanan BB. Thioredoxin target proteins in chloroplast thylakoid membranes. Antioxid Redox Signal 8: 1829-1834, 2006. (Pubitemid 44726355)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.9-10 , pp. 1829-1834
    • Balmer, Y.1    Vensel, W.H.2    Hurkman, W.J.3    Buchanan, B.B.4
  • 7
    • 77956462973 scopus 로고    scopus 로고
    • Redox extends its regulatory reach to chloroplast protein import
    • Balsera M, Soll J, and Buchanan BB. Redox extends its regulatory reach to chloroplast protein import. Trends Plant Sci 9: 515-521, 2010.
    • (2010) Trends Plant Sci , vol.9 , pp. 515-521
    • Balsera, M.1    Soll, J.2    Buchanan, B.B.3
  • 10
    • 67349107873 scopus 로고    scopus 로고
    • Structural and kinetic analysis of Saccharomyces cerevisiae thioredoxin Trx1: Implications for the catalytic mechanism of GSSG reduced by the thioredoxin system
    • Bao R, Zhang X, Lou Y, Zhou CZ, and Chen Y. Structural and kinetic analysis of Saccharomyces cerevisiae thioredoxin Trx1: implications for the catalytic mechanism of GSSG reduced by the thioredoxin system. Biochim Biophys Acta 1794: 1218-1223, 2009.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 1218-1223
    • Bao, R.1    Zhang, X.2    Lou, Y.3    Zhou, C.Z.4    Chen, Y.5
  • 11
    • 51749120178 scopus 로고    scopus 로고
    • Hexameric oligomerization of mitochondrial peroxiredoxin PrxIIF and formation of an ultrahigh affinity complex with its electron donor thioredoxin Trx-o
    • Barranco-Medina S, Krell T, Bernier-Villamor L, Sevilla F, Lázaro JJ, and Dietz KJ. Hexameric oligomerization of mitochondrial peroxiredoxin PrxIIF and formation of an ultrahigh affinity complex with its electron donor thioredoxin Trx-o. J Exp Bot 59: 3259-3269, 2008.
    • (2008) J Exp Bot , vol.59 , pp. 3259-3269
    • Barranco-Medina, S.1    Krell, T.2    Bernier-Villamor, L.3    Sevilla, F.4    Lázaro, J.J.5    Dietz, K.J.6
  • 13
    • 65249158581 scopus 로고    scopus 로고
    • Accumulation of flavonoids in an ntra ntrb mutant leads to tolerance to UV-C
    • Bashandy T, Taconnat L, Renou J-P, Meyer Y, and Reichheld J-P. Accumulation of flavonoids in an ntra ntrb mutant leads to tolerance to UV-C. Mol Plant 2: 249-258, 2009.
    • (2009) Mol Plant , vol.2 , pp. 249-258
    • Bashandy, T.1    Taconnat, L.2    Renou, J.-P.3    Meyer, Y.4    Reichheld, J.-P.5
  • 15
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • DOI 10.1126/science.1158265
    • Benhar M, Forrester MT, Hess DT, and Stamler JS. Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320: 1050-1054, 2008. (Pubitemid 351929542)
    • (2008) Science , vol.320 , Issue.5879 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 16
    • 70349466515 scopus 로고    scopus 로고
    • Protein denitrosylation: Enzymatic mechanisms and cellular functions
    • Benhar M, Forrester MT, and Stamler JS. Protein denitrosylation: enzymatic mechanisms and cellular functions. Nat Rev Mol Cell Biol 10: 721-732, 2009.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 721-732
    • Benhar, M.1    Forrester, M.T.2    Stamler, J.S.3
  • 17
    • 77955576782 scopus 로고    scopus 로고
    • Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach
    • Benhar M, Thompson JW, Moseley MA, and Stamler JS. Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach. Biochemistry 49: 6963-6969, 2010.
    • (2010) Biochemistry , vol.49 , pp. 6963-6969
    • Benhar, M.1    Thompson, J.W.2    Moseley, M.A.3    Stamler, J.S.4
  • 19
    • 67650886282 scopus 로고    scopus 로고
    • Redox homeostasis regulates plasmodesmal communication in Arabidopsis meristems
    • Benitez-Alfonso Y and Jackson D. Redox homeostasis regulates plasmodesmal communication in Arabidopsis meristems. Plant Signal Behav 7: 655-659, 2009.
    • (2009) Plant Signal Behav , vol.7 , pp. 655-659
    • Benitez-Alfonso, Y.1    Jackson, D.2
  • 21
    • 0032493355 scopus 로고    scopus 로고
    • Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5¢-adenylylsulfate reductase
    • Bick JA, Aslund F, Chen Y, and Leustek T. Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5¢-adenylylsulfate reductase. Proc Natl Acad Sci USA 95: 8404-8409, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8404-8409
    • Bick, J.A.1    Aslund, F.2    Chen, Y.3    Leustek, T.4
  • 22
    • 33846903876 scopus 로고    scopus 로고
    • Function of phytochelatin synthase in catabolism of glutathione- conjugates
    • DOI 10.1111/j.1365-313X.2006.02993.x
    • Blum R, Beck A, Korte A, Stengel A, Letzel T, Lendzian K, and Grill E. Function of phytochelatin synthase in catabolism of glutathione-conjugates. Plant J 49: 740-749, 2007. (Pubitemid 46233090)
    • (2007) Plant Journal , vol.49 , Issue.4 , pp. 740-749
    • Blum, R.1    Beck, A.2    Korte, A.3    Stengel, A.4    Letzel, T.5    Lendzian, K.6    Grill, E.7
  • 24
    • 0142071753 scopus 로고    scopus 로고
    • Functional characterization and expression analysis of a glutathione transporter, BjGT1, from Brassica juncea: Evidence for regulation by heavy metal exposure
    • DOI 10.1046/j.1365-3040.2003.01088.x
    • Bogs J, Bourbouloux A, Cagnac O, Wachter A, Rausch D, and Delrot S. Functional chacterization and expression analysis of a glutathione transporter, BjGT1, from Brassica juncea: evidence for regulation by heavy metal exposure. Plant Cell Environ 26: 1703-1711, 2003. (Pubitemid 37292585)
    • (2003) Plant, Cell and Environment , vol.26 , Issue.10 , pp. 1703-1711
    • Bogs, J.1    Bourbouloux, A.2    Cagnac, O.3    Wachter, A.4    Rausch, T.5    Delrot, S.6
  • 27
    • 0043011656 scopus 로고    scopus 로고
    • Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: Similar sequences for divergent gene expression, protein localization, and activity
    • DOI 10.1104/pp.103.022533
    • Bréhélin C, Meyer EH, de Souris J-P, Bonnard G, and Meyer Y. Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization, and activity. Plant Physiol 132: 2045-2057, 2003. (Pubitemid 37024165)
    • (2003) Plant Physiology , vol.132 , Issue.4 , pp. 2045-2057
    • Brehelin, C.1    Meyer, E.H.2    De Souris, J.-P.3    Bonnard, G.4    Meyer, Y.5
  • 28
    • 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
    • DOI 10.1105/tpc.001644
    • Broin M, Cuiné S, Eymery F, and Rey P. 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. (Pubitemid 34780440)
    • (2002) Plant Cell , vol.14 , Issue.6 , pp. 1417-1432
    • Broin, M.1    Cuine, S.2    Eymery, F.3    Rey, P.4
  • 29
    • 0034607697 scopus 로고    scopus 로고
    • Hgt1p, a high affinity glutathione transporter from the yeast Saccharomyces cerevisiae
    • DOI 10.1074/jbc.275.18.13259
    • Bourbouloux A, Shahi P, Chakladar A, Delrot S, and Bachhawat AK. Hgt1p, a high affinity glutathione transporter from the yeast Saccharomyces cerevisiae. J Biol Chem 275: 13259-13265, 2000. (Pubitemid 30257381)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.18 , pp. 13259-13265
    • Bourbouloux, A.1    Shahi, P.2    Chakladar, A.3    Delrot, S.4    Bachhawat, A.K.5
  • 32
    • 33745647317 scopus 로고    scopus 로고
    • Maturation of Arabidopsis seeds is dependent on glutathione biosynthesis within the embryo
    • DOI 10.1104/pp.106.077982
    • Cairns NG, Pasternak M, Wachter A, Cobbett CS, and Meyer AJ. Maturation of arabidopsis seeds is dependent on glutathione biosynthesis within the embryo. Plant Physiol 141: 446-455, 2006. (Pubitemid 43974539)
    • (2006) Plant Physiology , vol.141 , Issue.2 , pp. 446-455
    • Cairns, N.G.1    Pasternak, M.2    Wachter, A.3    Cobbett, C.S.4    Meyer, A.J.5
  • 33
    • 33847637126 scopus 로고    scopus 로고
    • Visualization of ribonucleotide reductase catalytic oxidation establishes thioredoxins as its major reductants in yeast
    • DOI 10.1016/j.freeradbiomed.2006.12.027, PII S0891584907000032
    • Camier S, Ma E, Leroy C, Pruvost A, Toledano M, and Marsolier-Kergoat MC. Visualization of ribonucleotide reductase catalytic oxidation establishes thioredoxins as its major reductants in yeast. Free Radic Biol Med 42: 1008-1016, 2007. (Pubitemid 46356891)
    • (2007) Free Radical Biology and Medicine , vol.42 , Issue.7 , pp. 1008-1016
    • Camier, S.1    Ma, E.2    Leroy, C.3    Pruvost, A.4    Toledano, M.5    Marsolier-Kergoat, M.-C.6
  • 35
    • 78049356626 scopus 로고    scopus 로고
    • The dithiol glutaredoxins of African trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism
    • Ceylan S, Seidel V, Ziebart N, Berndt C, Dirdjaja N, and Krauth-Siegel RL. The dithiol glutaredoxins of African trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism. J Biol Chem 285: 35224-35237, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 35224-35237
    • Ceylan, S.1    Seidel, V.2    Ziebart, N.3    Berndt, C.4    Dirdjaja, N.5    Krauth-Siegel, R.L.6
  • 36
    • 0037458588 scopus 로고    scopus 로고
    • Cloning and characterization of CXIP1, a novel picot domain-containing Arabidopsis protein that associates with CAX1
    • DOI 10.1074/jbc.M210883200
    • Cheng N-H and Hirschi KD. Cloning and characterization of CXIP1, a novel PICOT domain-containing Arabidopsis protein that associates with CAX1. J Biol Chem 278: 6503-6509, 2003. (Pubitemid 36800911)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.8 , pp. 6503-6509
    • Ning-Hui, C.1    Hirschi, K.D.2
  • 37
    • 33748747966 scopus 로고    scopus 로고
    • AtGRXcp, an Arabidopsis chloroplastic glutaredoxin, is critical for protection against protein oxidative damage
    • DOI 10.1074/jbc.M601354200
    • Cheng N-H, Liu J-Z, Brock A, Nelson RS, and Hirschi KD. AtGRXcp, an Arabidopsis chloroplastic glutaredoxin, is critical for protection against protein oxidative damage. J Biol Chem 281: 26280-26288, 2006. (Pubitemid 44401836)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.36 , pp. 26280-26288
    • Cheng, N.-H.1    Liu, J.-Z.2    Brock, A.3    Nelson, R.S.4    Hirschi, K.D.5
  • 38
    • 40349113000 scopus 로고    scopus 로고
    • AtGRX4, an Arabidopsis chloroplastic monothiol glutaredoxin, is able to suppress yeast grx5 mutant phenotypes and respond to oxidative stress
    • Cheng N-H. AtGRX4, an Arabidopsis chloroplastic monothiol glutaredoxin, is able to suppress yeast grx5 mutant phenotypes and respond to oxidative stress. FEBS Lett 582: 848-854, 2008.
    • (2008) FEBS Lett , vol.582 , pp. 848-854
    • Cheng, N.-H.1
  • 39
    • 79958013653 scopus 로고    scopus 로고
    • Arabidopsis monothiol glutaredoxin AtGRXS17 is critical for temperature-dependent postembryonic growth and development via modulating auxin response
    • Cheng NH, Liu JZ, Liu X, Wu Q, Thompson SM, Lin J, Chang J, Whitham SA, Park S, Cohen JD, and Hirschi KD. Arabidopsis monothiol glutaredoxin, AtGRXS17, is critical for temperature-dependent postembryonic growth and development via modulating auxin response. J Biol Chem 286: 20398-20406, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 20398-20406
    • Cheng, N.H.1    Liu, J.Z.2    Liu, X.3    Wu, Q.4    Thompson, S.M.5    Lin, J.6    Chang, J.7    Whitham, S.A.8    Park, S.9    Cohen, J.D.10    Hirschi, K.D.11
  • 40
    • 34347333533 scopus 로고    scopus 로고
    • The relationship of the redox potentials of thioredoxin and thioredoxin reductase from Drosophila melanogaster to the enzymatic mechanism: Reduced thioredoxin is the reductant of glutathione in Drosophila
    • DOI 10.1021/bi700442r
    • Cheng Z, Arscott LD, Ballou DP, and Williams CH, Jr. The relationship of the redox potentials of thioredoxin and thioredoxin reductase from Drosophila melanogaster to the enzymatic mechanism: reduced thioredoxin is the reductant of glutathione in Drosophila. Biochemistry 46: 7875-7885, 2007. (Pubitemid 47016069)
    • (2007) Biochemistry , vol.46 , Issue.26 , pp. 7875-7885
    • Cheng, Z.1    Arscott, L.D.2    Ballou, D.P.3    Williams Jr., C.H.4
  • 41
    • 0344875538 scopus 로고    scopus 로고
    • Molecular definition of the ascorbate-glutathione cycle in arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants
    • DOI 10.1074/jbc.M307525200
    • Chew O, Whelan J, and Millar AH. Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants. J Biol Chem 278: 46869-46877, 2003. (Pubitemid 37452268)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 46869-46877
    • Chew, O.1    Whelan, J.2    Millar, A.H.3
  • 42
    • 65249109913 scopus 로고    scopus 로고
    • Comparative genomic study of the thioredoxin family in photosynthetic organisms with emphasis on Populus trichocarpa
    • Chibani K, Wingsle G, Jacquot J-P, Gelhaye E, and Rouhier N. Comparative genomic study of the thioredoxin family in photosynthetic organisms with emphasis on Populus trichocarpa. Mol Plant 2: 308-322, 2009.
    • (2009) Mol Plant , vol.2 , pp. 308-322
    • Chibani, K.1    Wingsle, G.2    Jacquot, J.-P.3    Gelhaye, E.4    Rouhier, N.5
  • 43
    • 77952237237 scopus 로고    scopus 로고
    • The chloroplastic thiol reducing systems: Dual functions in the regulation of carbohydrate metabolism and regeneration of antioxidant enzymes, emphasis on the poplar redoxin equipment
    • Chibani K, Couturier J, Selles B, Jacquot J-P, and Rouhier N. The chloroplastic thiol reducing systems: dual functions in the regulation of carbohydrate metabolism and regeneration of antioxidant enzymes, emphasis on the poplar redoxin equipment. Photosyn Res 104: 75-99, 2010.
    • (2010) Photosyn Res , vol.104 , pp. 75-99
    • Chibani, K.1    Couturier, J.2    Selles, B.3    Jacquot, J.-P.4    Rouhier, N.5
  • 45
    • 0029063980 scopus 로고
    • Amino acid sequence of spinach ferredoxin: Thioredoxin reductase catalytic subunit and identification of thiol groups constituting a redox-active disulfide and a [4Fe-4S] cluster
    • Chow LP, Iwadate H, Yano K, Kamo M, Tsugita A, Gardet-Salvi L, Stritt-Etter AL, and Schürmann P. Amino acid sequence of spinach ferredoxin: thioredoxin reductase catalytic subunit and identification of thiol groups constituting a redox-active disulfide and a [4Fe-4S] cluster. Eur J Biochem 231: 149-156, 1995.
    • (1995) Eur J Biochem , vol.231 , pp. 149-156
    • Chow, L.P.1    Iwadate, H.2    Yano, K.3    Kamo, M.4    Tsugita, A.5    Gardet-Salvi, L.6    Stritt-Etter, A.L.7    Schürmann, P.8
  • 46
    • 0032190503 scopus 로고    scopus 로고
    • The glutathione-deficient, cadmium-sensitive mutant, cad2-1, of Arabidopsis thaliana is deficient in gamma-glutamylcysteine synthetase
    • Cobbett CS, May MJ, Howden R, and Rolls B. The glutathione-deficient, cadmium-sensitive mutant, cad2-1, of Arabidopsis thaliana is deficient in gamma-glutamylcysteine synthetase. Plant J 16: 73-78, 1998.
    • (1998) Plant J , vol.16 , pp. 73-78
    • Cobbett, C.S.1    May, M.J.2    Howden, R.3    Rolls, B.4
  • 50
    • 67650999518 scopus 로고    scopus 로고
    • Evolution and diversity of glutaredoxins in photosynthetic organisms
    • Couturier J, Jacquot J-P, and Rouhier N. Evolution and diversity of glutaredoxins in photosynthetic organisms. Cell Mol Life Sci 66: 2539-2557, 2009.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2539-2557
    • Couturier, J.1    Jacquot, J.-P.2    Rouhier, N.3
  • 52
    • 78650171927 scopus 로고    scopus 로고
    • Engineered mutated glutaredoxins mimicking peculiar plant class III glutaredoxins bind iron-sulfur centers and possess reductase activity
    • Couturier J, Didierjean C, Jacquot J-P, and Rouhier N. Engineered mutated glutaredoxins mimicking peculiar plant class III glutaredoxins bind iron-sulfur centers and possess reductase activity. Biochem Biophys Res Commun 403: 435-441, 2010.
    • (2010) Biochem Biophys Res Commun , vol.403 , pp. 435-441
    • Couturier, J.1    Didierjean, C.2    Jacquot, J.-P.3    Rouhier, N.4
  • 55
    • 0030596062 scopus 로고    scopus 로고
    • Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5 A resolution
    • DOI 10.1006/jmbi.1996.0695
    • Dai S, Saarinen M, Ramaswamy S, Meyer Y, Jacquot JP, and Eklund H. Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5 A resolution. J Mol Biol 264: 1044-1057, 1996. (Pubitemid 27019491)
    • (1996) Journal of Molecular Biology , vol.264 , Issue.5 , pp. 1044-1057
    • Shaodong, D.1    Saarinen, M.2    Ramaswamy, S.3    Meyer, Y.4    Jacquot, J.-P.5    Eklund, H.6
  • 56
    • 0034723368 scopus 로고    scopus 로고
    • Redox signaling in chloroplasts: Cleavage of disulfides by an iron- sulfur cluster
    • DOI 10.1126/science.287.5453.655
    • Dai S, Schwendtmayer C, Schürmann P, Ramaswamy S, and Eklund H. Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster. Science 287: 655-658, 2000. (Pubitemid 30070913)
    • (2000) Science , vol.287 , Issue.5453 , pp. 655-658
    • Dai, S.1    Schwendtmayer, C.2    Schurmann, P.3    Ramaswamy, S.4    Eklund, H.5
  • 58
    • 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
    • DOI 10.1104/pp.107.105593
    • de Dios Barajas-López J, Serrato AJ, Olmedilla A, Chueca A, and Sahrawy M. 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. (Pubitemid 350127631)
    • (2007) Plant Physiology , vol.145 , Issue.3 , pp. 946-960
    • Barajas-Lopez, J.D.D.1    Serrato, A.J.2    Olmedilla, A.3    Chueca, A.4    Sahrawy, M.5
  • 60
    • 78650992200 scopus 로고    scopus 로고
    • Peroxiredoxins in plants and cyanobacteria
    • Dietz KJ. Peroxiredoxins in plants and cyanobacteria. Antioxid Redox Signal 15: 1129-1159, 2011.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 1129-1159
    • Dietz, K.J.1
  • 61
    • 79953709713 scopus 로고    scopus 로고
    • Novel regulators in photosynthetic redox control of plant metabolism and gene expression
    • Dietz KJ and Pfannschmidt T. Novel regulators in photosynthetic redox control of plant metabolism and gene expression. Plant Physiol 155: 1477-1485, 2011.
    • (2011) Plant Physiol , vol.155 , pp. 1477-1485
    • Dietz, K.J.1    Pfannschmidt, T.2
  • 62
    • 78449231466 scopus 로고    scopus 로고
    • Roles for stress-inducible lambda glutathione transferases in flavonoid metabolism in plants as identified by ligand fishing
    • Dixon DP and Edwards R. Roles for stress-inducible lambda glutathione transferases in flavonoid metabolism in plants as identified by ligand fishing. J Biol Chem 285: 36322-36329, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 36322-36329
    • Dixon, D.P.1    Edwards, R.2
  • 63
    • 78650978418 scopus 로고    scopus 로고
    • Glutathione s-transferases
    • Rockville MD: American Society of Plant Biologists, DOI: 10.1199: tab.0131
    • Dixon DP and Edwards R. Glutathione S-transferases. The Arabidopsis Book. Rockville, MD: American Society of Plant Biologists, 2010, DOI: 10.1199: tab.0131.
    • (2010) The Arabidopsis Book
    • Dixon, D.P.1    Edwards, R.2
  • 64
    • 0034076851 scopus 로고    scopus 로고
    • A single glutaredoxin or thioredoxin gene is essential for viability in the yeast Saccharomyces cerevisiae
    • DOI 10.1046/j.1365-2958.2000.01948.x
    • Draculic T, Dawes IW, and Grant CM. A single glutaredoxin or thioredoxin gene is essential for viability in the yeast Saccharomyces cerevisiae. Mol Microb 36: 1167-1174, 2000. (Pubitemid 30330687)
    • (2000) Molecular Microbiology , vol.36 , Issue.5 , pp. 1167-1174
    • Draculic, T.1    Dawes, I.W.2    Grant, C.M.3
  • 65
    • 0033215309 scopus 로고    scopus 로고
    • Nitric oxide as a signal in plants
    • DOI 10.1016/S1369-5266(99)00007-2
    • Durner J and Klessig DF. Nitric oxide as a signal in plants. Curr Opin Plant Biol 2: 369-374, 1999. (Pubitemid 29464062)
    • (1999) Current Opinion in Plant Biology , vol.2 , Issue.5 , pp. 369-374
    • Durner, J.1    Klessig, D.F.2
  • 66
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System
    • Fernandes AP and Holmgren A. Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid Redox Signal 6: 63-74, 2004. (Pubitemid 38063976)
    • (2004) Antioxidants and Redox Signaling , vol.6 , Issue.1 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 68
    • 81055130050 scopus 로고    scopus 로고
    • Nitric oxide causes root apical meristem defects and growth inhibition while reducing PIN-FORMED 1 (PIN1)-dependent acropetal auxin transport
    • Fernández-Marcos M, Sanz L, Lewis DR, Muday GK, and Lorenzo O. Nitric oxide causes root apical meristem defects and growth inhibition while reducing PIN-FORMED 1 (PIN1)-dependent acropetal auxin transport. Proc Natl Acad Sci USA 108: 18506-18511, 2011.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 18506-18511
    • Fernández-Marcos, M.1    Sanz, L.2    Lewis, D.R.3    Muday, G.K.4    Lorenzo, O.5
  • 69
    • 0035205673 scopus 로고    scopus 로고
    • The functions of inter- and intracellular glutathione transport systems in plants
    • DOI 10.1016/S1360-1385(01)02086-6, PII S1360138501020866
    • Foyer CH, Theodoulou FL, and Delrot S. The functions of inter-and intracellular glutathione transport systems in plants. Trends Plant Sci 6: 486-492, 2001. (Pubitemid 33145957)
    • (2001) Trends in Plant Science , vol.6 , Issue.10 , pp. 486-492
    • Foyer, C.H.1    Theodoulou, F.L.2    Delrot, S.3
  • 70
    • 78650988662 scopus 로고    scopus 로고
    • Ascorbate and glutathione: The heart of the redox hub
    • Foyer CH and Noctor G. Ascorbate and glutathione: the heart of the redox hub. Plant Physiol 155: 2-18, 2011.
    • (2011) Plant Physiol , vol.155 , pp. 2-18
    • Foyer, C.H.1    Noctor, G.2
  • 71
    • 33646858497 scopus 로고    scopus 로고
    • The thioredoxin-related redox-regulating protein nucleoredoxin inhibits Wnt-beta-catenin signalling through dishevelled
    • Funato Y, Michiue T, Asashima M, and Miki H. The thioredoxin-related redox-regulating protein nucleoredoxin inhibits Wnt-beta-catenin signalling through dishevelled. Nat Cell Biol. 8: 501-508, 2006.
    • (2006) Nat Cell Biol , vol.8 , pp. 501-508
    • Funato, Y.1    Michiue, T.2    Asashima, M.3    Miki, H.4
  • 73
    • 0032545346 scopus 로고    scopus 로고
    • Regulation of polar auxin transport by AtPIN1 in Arabidopsis vascular tissue
    • DOI 10.1126/science.282.5397.2226
    • Gälweiler L, Guan C, Müller A, Wisman E, Mendgen K, Yephremov A, and Palme K. Regulation of polar auxin transport by AtPIN1 in Arabidopsis vascular tissue. Science 282: 2226-2230, 1998. (Pubitemid 29004064)
    • (1998) Science , vol.282 , Issue.5397 , pp. 2226-2230
    • Galweiler, L.1    Guan, C.2    Muller, A.3    Wisman, E.4    Mendgen, K.5    Yephremov, A.6    Palme, K.7
  • 74
    • 77952955260 scopus 로고    scopus 로고
    • Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii: Kinetics and specificity in deglutathionylation reactions
    • Gao XH, Zaffagnini M, Bedhomme M, Michelet L, Cassier-Chauvat C, Decottignies P, and Lemaire SD. Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii: kinetics and specificity in deglutathionylation reactions. FEBS Lett 584: 2242-2248, 2010.
    • (2010) FEBS Lett , vol.584 , pp. 2242-2248
    • Gao, X.H.1    Zaffagnini, M.2    Bedhomme, M.3    Michelet, L.4    Cassier-Chauvat, C.5    Decottignies, P.6    Lemaire, S.D.7
  • 75
    • 0036227450 scopus 로고    scopus 로고
    • Role of thioredoxins in the response of Saccharomyces cerevisiae to oxidative stress induced by hydroperoxides
    • DOI 10.1046/j.1365-2958.2002.02795.x
    • Garrido EO and Grant CM. Role of thioredoxins in the response of Saccharomyces cerevisiae to oxidative stress induced by hydroperoxides. Mol Microbiol 43: 993-1003, 2002. (Pubitemid 34415722)
    • (2002) Molecular Microbiology , vol.43 , Issue.4 , pp. 993-1003
    • Garrido, E.O.1    Grant, C.M.2
  • 76
    • 0034623256 scopus 로고    scopus 로고
    • A dicistronic construct for the expression of functional spinach chloroplast ferredoxin: Thioredoxin reductase in Escherichia coli
    • Gaymard E, Franchini L, Manieri W, Stutz E, and Schürmann P. A dicistronic construct for the expression of functional spinach chloroplast ferredoxin: thioredoxin reductase in Escherichia coli. Plant Sci 158: 107-113, 2000.
    • (2000) Plant Sci , vol.158 , pp. 107-113
    • Gaymard, E.1    Franchini, L.2    Manieri, W.3    Stutz, E.4    Schürmann, P.5
  • 77
    • 0346366724 scopus 로고    scopus 로고
    • Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction
    • DOI 10.1016/S0014-5793(03)01301-2
    • Gelhaye E, Rouhier N, and Jacquot JP. Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction. FEBS Lett 555: 443-448, 2003. (Pubitemid 37532590)
    • (2003) FEBS Letters , vol.555 , Issue.3 , pp. 443-448
    • Gelhaye, E.1    Rouhier, N.2    Jacquot, J.-P.3
  • 80
    • 0037292964 scopus 로고    scopus 로고
    • The clot gene of Drosophila melanogaster encodes a conserved member of the Thioredoxin-like protein superfamily
    • Giordano E, Peluso I, Rendina R, Digilio A, and Furia M. The clot gene of Drosophila melanogaster encodes a conserved member of the thioredoxin-like protein superfamily. Mol Genet Genomics 268: 692-697, 2003. (Pubitemid 36286513)
    • (2003) Molecular Genetics and Genomics , vol.268 , Issue.5 , pp. 692-697
    • Giordano, E.1    Peluso, I.2    Rendina, R.3    Digilio, A.4    Furia, M.5
  • 81
    • 0030004354 scopus 로고    scopus 로고
    • Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae
    • DOI 10.1007/s002940050079
    • Grant CM, MacIver FH, and Dawes IW. Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae. Curr Genet 29: 511-515, 1996. (Pubitemid 26166751)
    • (1996) Current Genetics , vol.29 , Issue.6 , pp. 511-515
    • Grant, C.M.1    MacIver, F.H.2    Dawes, I.W.3
  • 82
    • 66349105304 scopus 로고    scopus 로고
    • Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo
    • Greetham D and Grant CM. Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo. Mol Cell Biol 29: 3229-3240, 2009.
    • (2009) Mol Cell Biol , vol.29 , pp. 3229-3240
    • Greetham, D.1    Grant, C.M.2
  • 84
    • 0029830772 scopus 로고    scopus 로고
    • Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and ''APS reductase'' activity
    • Gutierrez-Marcos JF, Roberts MA, Campbell EI, and Wray JL. Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and ''APS reductase'' activity. Proc Natl Acad Sci USA 93: 13377-13382, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13377-13382
    • Gutierrez-Marcos, J.F.1    Roberts, M.A.2    Campbell, E.I.3    Wray, J.L.4
  • 85
    • 0036798856 scopus 로고    scopus 로고
    • Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69
    • DOI 10.1038/ncb851
    • Haendeler J, Hoffmann J, Tischler V, Berk BC, Zeiher AM, and Dimmeler S. Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69. Nat Cell Biol. 4: 743-749, 2002. (Pubitemid 35214767)
    • (2002) Nature Cell Biology , vol.4 , Issue.10 , pp. 743-749
    • Haendeler, J.1    Hoffmann, J.2    Tischler, V.3    Berk, B.C.4    Zeiher, A.M.5    Dimmeler, S.6
  • 86
    • 0842264043 scopus 로고    scopus 로고
    • A post genomic characterization of arabidopsis ferredoxins
    • DOI 10.1104/pp.103.032755
    • Hanke GT, Kimata-Ariga Y, Taniguchi I, and Hase T. A post genomic characterization of Arabidopsis ferredoxins. Plant Physiol 134: 255-264, 2004. (Pubitemid 38178698)
    • (2004) Plant Physiology , vol.134 , Issue.1 , pp. 255-264
    • Hanke, G.T.1    Kimata-Ariga, Y.2    Taniguchi, I.3    Hase, T.4
  • 88
    • 0038384461 scopus 로고    scopus 로고
    • Cell-specific measurement of cytosolic glutathione in poplar leaves
    • DOI 10.1046/j.1365-3040.2003.01031.x
    • Hartmann TN, Fricker MD, Rennenberg H, and Meyer AJ. Cell-specific measurement of cytosolic glutathione in poplar leaves. Plant Cell Environ 26: 965-975, 2003. (Pubitemid 36738002)
    • (2003) Plant, Cell and Environment , vol.26 , Issue.6 , pp. 965-975
    • Hartmann, T.N.1    Fricker, M.D.2    Rennenberg, H.3    Meyer, A.J.4
  • 89
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Höhfeld J, Minami Y, and Hartl FU. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83: 589-598, 1995.
    • (1995) Cell , vol.83 , pp. 589-598
    • Höhfeld, J.1    Minami, Y.2    Hartl, F.U.3
  • 90
    • 0018786716 scopus 로고
    • Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin
    • Holmgren A. Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin. J Biol Chem 254: 3672-3678, 1979.
    • (1979) J Biol Chem , vol.254 , pp. 3672-3678
    • Holmgren, A.1
  • 91
    • 0029278723 scopus 로고
    • A cadmium-sensitive, glutathione-deficient mutant of Arabidopsis thaliana
    • Howden R, Andersen CR, Goldsbrough PB, and Cobbett CS. A cadmium-sensitive, glutathione-deficient mutant of Arabidopsis thaliana. Plant Physiol 107: 1067-1073, 1995.
    • (1995) Plant Physiol , vol.107 , pp. 1067-1073
    • Howden, R.1    Andersen, C.R.2    Goldsbrough, P.B.3    Cobbett, C.S.4
  • 92
    • 0034612325 scopus 로고    scopus 로고
    • Differential effects of chilling-induced photooxidation on the redox regulation of photosynthetic enzymes
    • DOI 10.1021/bi0001978
    • Hutchison RS, Groom Q, and Ort DR. Differential effects of chilling-induced photooxidation on the redox regulation of photosynthetic enzymes. Biochemistry 39: 6679-6688, 2000. (Pubitemid 30354000)
    • (2000) Biochemistry , vol.39 , Issue.22 , pp. 6679-6688
    • Hutchison, R.S.1    Groom, Q.2    Ort, D.R.3
  • 93
    • 0035142197 scopus 로고    scopus 로고
    • Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin
    • DOI 10.1046/j.0960-7412.2000.00943.x
    • Issakidis-Bourguet E, Mouaheb N, Meyer Y, and Miginiac-Maslow M. Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin. Plant J 25: 127-135, 2001. (Pubitemid 32122747)
    • (2001) Plant Journal , vol.25 , Issue.2 , pp. 127-135
    • Issakidis-Bourguet, E.1    Mouaheb, N.2    Meyer, Y.3    Miginiac-Maslow, M.4
  • 94
    • 0017058765 scopus 로고
    • Identification of a protein factor involved in dithiothreitol activation of NADP malate dehydrogenase from French bean leaves
    • DOI 10.1016/0014-5793(76)80937-4
    • Jacquot J-P, Vidal J, and Gadal P. Identification of a protein factor involved in dithiothreitol activation of NADP-malate dehydrogenase. FEBS Lett 71: 223-227, 1976. (Pubitemid 8004530)
    • (1976) FEBS Letters , vol.71 , Issue.2 , pp. 223-227
    • Jacquot, J.P.1    Vidal, J.2    Gadal, P.3
  • 95
    • 0018072333 scopus 로고
    • Evidence for the existence of several enzyme-specific thioredoxins in plants
    • DOI 10.1016/0014-5793(78)80410-4
    • Jacquot J-P, Vidal J, Gadal P, and Schürmann P. Evidence for the existence of several enzyme specific thioredoxins in plants. FEBS Lett 96: 243-246, 1978. (Pubitemid 9077714)
    • (1978) FEBS Letters , vol.96 , Issue.2 , pp. 243-246
    • Jacquot, J.P.1    Vidal, J.2    Gadal, P.3    Schuermann, P.4
  • 96
    • 0028354036 scopus 로고
    • Arabidopsis thaliana NADPH 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, and Meyer Y. Arabidopsis thaliana NADPH thioredoxin reductase. cDNA characterization and expression of the recombinant protein in Escherichia coli. J Mol Biol 235: 1357-1363, 1994.
    • (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
  • 97
    • 66649085738 scopus 로고    scopus 로고
    • Structural and evolutionary aspects of thioredoxin reductases in photosynthetic organisms
    • Jacquot J-P, Eklund H, Rouhier N, and Schürmann P. Structural and evolutionary aspects of thioredoxin reductases in photosynthetic organisms. Trends Plant Sci 214: 336-343, 2009.
    • (2009) Trends Plant Sci , vol.214 , pp. 336-343
    • Jacquot, J.-P.1    Eklund, H.2    Rouhier, N.3    Schürmann, P.4
  • 98
    • 0040557481 scopus 로고    scopus 로고
    • Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves
    • Jiménez A, Hernández JA, del Río LA, and Sevilla F. Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves. Plant Physiol 114: 275-284, 1997. (Pubitemid 28110917)
    • (1997) Plant Physiology , vol.114 , Issue.1 , pp. 275-284
    • Jimenez, A.1    Hernandez, J.A.2    Del Rio, L.A.3    Sevilla, F.4
  • 99
    • 1542320094 scopus 로고    scopus 로고
    • Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase
    • DOI 10.1074/jbc.M312719200
    • Johansson C, Lillig CH, and Holmgren A. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons fromeither glutathione or thioredoxin reductase. J Biol Chem 279: 7537-7543, 2004. (Pubitemid 38294632)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7537-7543
    • Johansson, C.1    Lillig, C.H.2    Holmgren, A.3
  • 100
    • 0017623044 scopus 로고
    • 4 photosynthesis: characterization of a protein factor mediating the activation and inactivation of nadp-malate dehydrogenase
    • Kagawa T and Hatch MD. Regulation of C4 photosynthesis: characterization of a protein factor mediating the activation and inactivation of NADP-malate dehydrogenase. Arch Biochem Biophys 184: 290-297, 1977. (Pubitemid 8220819)
    • (1977) Archives of Biochemistry and Biophysics , vol.184 , Issue.1 , pp. 290-297
    • Kagawa, T.1    Hatch, M.D.2
  • 101
    • 0034704081 scopus 로고    scopus 로고
    • The thioredoxin system of the malaria parasite Plasmodium falciparum
    • DOI 10.1074/jbc.M007633200
    • Kanzok SM, Schirmer RH, Turbachova I, Iozef R, and Becker K. The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited. J Biol Chem 275: 40180-40186, 2000. (Pubitemid 32064647)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.51 , pp. 40180-40186
    • Kanzok, S.M.1    Schirmer, R.H.2    Turbachova, I.3    Iozef, R.4    Becker, K.5
  • 103
    • 77956622614 scopus 로고    scopus 로고
    • Arabidopsis glutathione reductase 1 is dually targeted to peroxisomes and the cytosol
    • Kataya AMR and Reumann S. Arabidopsis glutathione reductase 1 is dually targeted to peroxisomes and the cytosol. Plant Signal Behav 5: 171-175, 2010.
    • (2010) Plant Signal Behav , vol.5 , pp. 171-175
    • Amr, K.1    Reumann, S.2
  • 104
    • 1642356888 scopus 로고    scopus 로고
    • Characterization of Arabidopsis mutants for the variable subunit of ferredoxin:thioredoxin reductase
    • DOI 10.1023/B:PRES.0000017173.46185.3e, Plant Thioredoxins and Releated Proteins
    • Keryer E, Collin V, Lavergne D, Lemaire S, and Issakidis-Bourguet E. Characterization of Arabidopsis mutants for the variable subunit of ferredoxin: thioredoxin reductase. Photosynth Res 79: 265-274, 2004. (Pubitemid 38370829)
    • (2004) Photosynthesis Research , vol.79 , Issue.3 , pp. 265-274
    • Keryer, E.1    Collin, V.2    Lavergne, D.3    Lemaire, S.4    Issakidis-Bourguet, E.5
  • 105
    • 33744960023 scopus 로고    scopus 로고
    • Thioredoxin is required for deoxyribonucleotide pool maintenance during S phase
    • DOI 10.1074/jbc.M601968200
    • Koc A, Mathews CK, Wheeler LJ, Gross MK, and Merrill GF. Thioredoxin is required for deoxyribonucleotide pool maintenance during S phase. J Biol Chem 281: 15058-15063, 2006. (Pubitemid 43855094)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.22 , pp. 15058-15063
    • Koc, A.1    Mathews, C.K.2    Wheeler, L.J.3    Gross, M.K.4    Merrill, G.F.5
  • 107
    • 77956704183 scopus 로고    scopus 로고
    • Arabidopsis root growth dependence on glutathione is linked to auxin transport
    • Koprivova A, Mugford ST, and Kopriva S. Arabidopsis root growth dependence on glutathione is linked to auxin transport. Plant Cell Rep 29: 1157-1167, 2010.
    • (2010) Plant Cell Rep , vol.29 , pp. 1157-1167
    • Koprivova, A.1    Mugford, S.T.2    Kopriva, S.3
  • 108
    • 77953022036 scopus 로고
    • Protein import into chloroplasts: The Tic complex and its regulation
    • Kovács-Bogdán E, Soll J, and Bölter B. Protein import into chloroplasts: the Tic complex and its regulation. Biochim Biophys Acta 1803: 740-747, 2010.
    • (1803) Biochim Biophys Acta , vol.740-747 , pp. 2010
    • Kovács-Bogdán, E.1    Soll, J.2    Bölter, B.3
  • 109
    • 57749084487 scopus 로고    scopus 로고
    • Transport and sorting of the Solanum tuberosum sucrose transporter SUT1 is affected by posttranslational modification
    • DOI 10.1105/tpc.108.058271
    • Krügel U, Veenhoff LM, Langbein J, Wiederhold E, Liesche J, Friedrich T, Grimm B, Martinoia E, Poolman B, and Kühn C. Transport and sorting of the solanum tuberosum sucrose transporter SUT1 is affected by posttranslational modification. Plant Cell 20: 2497-2513, 2008. (Pubitemid 352844614)
    • (2008) Plant Cell , vol.20 , Issue.9 , pp. 2497-2513
    • Krugel, U.1    Veenhoff, L.M.2    Langbein, J.3    Wiederhold, E.4    Liesche, J.5    Friedrich, T.6    Grimm, B.7    Martinoia, E.8    Poolman, B.9    Kuhn, C.10
  • 111
    • 79953768430 scopus 로고    scopus 로고
    • Identification and conformer analysis of a novel redoxactive motif pro-ala -ser-cys-cys-ser, in Drosophila thioredoxin reductase by semiempirical molecular orbital calculation
    • Kuwahara M, Tamura T, Kawamura K, and Inagaki K. Identification and conformer analysis of a novel redoxactive motif, pro-ala-ser-cys-cys-ser, in Drosophila thioredoxin reductase by semiempirical molecular orbital calculation. Biosci Biotechnol Biochem 75: 516-521, 2011.
    • (2011) Biosci Biotechnol Biochem , vol.75 , pp. 516-521
    • Kuwahara, M.1    Tamura, T.2    Kawamura, K.3    Inagaki, K.4
  • 114
    • 1642547085 scopus 로고    scopus 로고
    • The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative stress and its W-box-mediated response to pathogen elicitor
    • DOI 10.1104/pp.103.035782
    • Laloi C, Mestres-Ortega D, Marco Y, Meyer Y, and Reichheld J-P. 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. (Pubitemid 38398249)
    • (2004) Plant Physiology , vol.134 , Issue.3 , pp. 1006-1016
    • Laloi, C.1    Mestres-Ortega, D.2    Marco, Y.3    Meyer, Y.4    Reichheld, J.-P.5
  • 115
    • 84555209313 scopus 로고    scopus 로고
    • Glutaredoxin GRXS13 plays a key role in protection against photooxidative stress in Arabidopsis
    • Laporte D, Olate E, Salinas P, Salazar M, Jordana X, and Holuigue L. Glutaredoxin GRXS13 plays a key role in protection against photooxidative stress in Arabidopsis. J Exp Bot 63: 503-515, 2011.
    • (2011) J Exp Bot , vol.63 , pp. 503-515
    • Laporte, D.1    Olate, E.2    Salinas, P.3    Salazar, M.4    Jordana, X.5    Holuigue, L.6
  • 116
    • 0032197184 scopus 로고    scopus 로고
    • A novel nuclear member of the thioredoxin superfamily
    • Laughner BJ, Sehnke PC, and Ferl RJ. A novel nuclear member of the thioredoxin superfamily. Plant Physiol 118: 987-996, 1998. (Pubitemid 128653024)
    • (1998) Plant Physiology , vol.118 , Issue.3 , pp. 987-996
    • Laughner, B.J.1    Sehnke, P.C.2    Ferl, R.J.3
  • 117
    • 78651146370 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B
    • Laurent TC, Moore EC, and Reichard P. Enzymatic synthesis of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B. J Biol Chem 239: 3436-3444, 1964.
    • (1964) J Biol Chem , vol.239 , pp. 3436-3444
    • Laurent, T.C.1    Moore, E.C.2    Reichard, P.3
  • 120
    • 0038393110 scopus 로고    scopus 로고
    • Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii
    • DOI 10.1016/S0014-5793(03)00416-2
    • Lemaire SD, Collin V, Keryer E, Quesada A, and Miginiac-Maslow M. Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii. FEBS Lett 543: 87-92, 2003. (Pubitemid 36577233)
    • (2003) FEBS Letters , vol.543 , Issue.1-3 , pp. 87-92
    • Lemaire, S.D.1    Collin, V.2    Keryer, E.3    Quesada, A.4    Miginiac-Maslow, M.5
  • 123
    • 33744543755 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae proteome of oxidized protein thiols: Contrasted functions for the thioredoxin and glutathione pathways
    • DOI 10.1074/jbc.M513346200
    • Le Moan N, Clement G, Le Maout S, Tacnet F, and Toledano MB. The Saccharomyces cerevisiae proteome of oxidized protein thiols: contrasted functions for the thioredoxin and glutathione pathways. J Biol Chem 281: 10420-10430, 2006. (Pubitemid 43864581)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.15 , pp. 10420-10430
    • Le Moan, N.1    Clement, G.2    Le Maout, S.3    Tacnet, F.4    Toledano, M.B.5
  • 124
    • 0035209897 scopus 로고    scopus 로고
    • 6f complex in Arabidopsis
    • DOI 10.1105/tpc.13.11.2539
    • Lennartz K, Plücken H, Seidler A, Westhoff P, Bechtold N, and Meierhoff K. HCF164 encodes a thioredoxin-like protein involved in the biogenesis of the cytochrome b(6)f complex in Arabidopsis. Plant Cell 2001: 2539-2551, 2001. (Pubitemid 33146115)
    • (2001) Plant Cell , vol.13 , Issue.11 , pp. 2539-2551
    • Lennartz, K.1    Plucken, H.2    Seidler, A.3    Westhoff, P.4    Bechtold, N.5    Meierhoff, K.6
  • 125
    • 77953165883 scopus 로고    scopus 로고
    • Structure of arabidopsis chloroplastic monothiol glutaredoxin AtGRXcp
    • Li L, Cheng N, Hirschi KD, and Wang X. Structure of Arabidopsis chloroplastic monothiol glutaredoxin AtGRXcp. Acta Crystallogr D Biol Crystallogr 66(Pt 6): 725-732, 2010.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 6 , pp. 725-732
    • Li, L.1    Cheng, N.2    Hirschi, K.D.3    Wang, X.4
  • 126
    • 64749114849 scopus 로고    scopus 로고
    • Nuclear activity of ROXY1, a glutaredoxin interacting with TGA factors, is required for petal development in Arabidopsis thaliana
    • Li S, Lauri A, Ziemann M, Busch A, Bhave M, and Zachgo S. Nuclear activity of ROXY1, a glutaredoxin interacting with TGA factors, is required for petal development in Arabidopsis thaliana. Plant Cell 21: 429-441, 2009.
    • (2009) Plant Cell , vol.21 , pp. 429-441
    • Li, S.1    Lauri, A.2    Ziemann, M.3    Busch, A.4    Bhave, M.5    Zachgo, S.6
  • 128
    • 82755176105 scopus 로고    scopus 로고
    • The ROXY1 C-terminal L**LL motif is essential for the interaction with TGA transcription factors
    • Li S, Gutsche N, and Zachgo S. The ROXY1 C-terminal L**LL motif is essential for the interaction with TGA transcription factors. Plant Physiol 157: 2056-2068, 2011.
    • (2011) Plant Physiol , vol.157 , pp. 2056-2068
    • Li, S.1    Gutsche, N.2    Zachgo, S.3
  • 130
    • 79958839612 scopus 로고    scopus 로고
    • Development of glutathione-deficient embryos in Arabidopsis is influenced by the maternal level of glutathione
    • Lim B, Meyer AJ, and Cobbett CS. Development of glutathione-deficient embryos in Arabidopsis is influenced by the maternal level of glutathione. Plant Biol (Stuttg) 13: 693-697, 2010.
    • (2010) Plant Biol (Stuttg) , vol.13 , pp. 693-697
    • Lim, B.1    Meyer, A.J.2    Cobbett, C.S.3
  • 131
    • 77956266556 scopus 로고    scopus 로고
    • Silencing of SlFTR-c, the catalytic subunit of ferredoxin: Thioredoxin reductase, induces pathogenesisrelated genes and pathogen resistance in tomato plants
    • Lim CJ, Kim WB, Lee BS, Lee HY, Kwon TH, Park JM, and Kwon SY. Silencing of SlFTR-c, the catalytic subunit of ferredoxin: thioredoxin reductase, induces pathogenesisrelated genes and pathogen resistance in tomato plants. Biochem Biophys Res Commun 399: 750-754, 2010.
    • (2010) Biochem Biophys Res Commun , vol.399 , pp. 750-754
    • Lim, C.J.1    Kim, W.B.2    Lee, B.S.3    Lee, H.Y.4    Kwon, T.H.5    Park, J.M.6    Kwon, S.Y.7
  • 132
    • 79957441981 scopus 로고    scopus 로고
    • The disulfide proteome and other reactive cysteine proteomes: Analysis and functional significance
    • Lindahl M, Mata-Cabana A, and Kieselbach T. The disulfide proteome and other reactive cysteine proteomes: analysis and functional significance. Antioxid Redox Signal 14: 2581-2642, 2011.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 2581-2642
    • Lindahl, M.1    Mata-Cabana, A.2    Kieselbach, T.3
  • 133
    • 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
    • DOI 10.1042/BJ20031634
    • Maeda K, Finnie C, and Svensson B. 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(Pt 2): 497-507, 2004. (Pubitemid 38367239)
    • (2004) Biochemical Journal , vol.378 , Issue.2 , pp. 497-507
    • Maeda, K.1    Finnie, C.2    Svensson, B.3
  • 135
    • 33845968455 scopus 로고    scopus 로고
    • Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin
    • DOI 10.1002/pmic.200600443
    • Marchand C, Le Maréchal P, Meyer Y, and Decottignies P. Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin. Proteomics 6: 6528-6537, 2006. (Pubitemid 46048391)
    • (2006) Proteomics , vol.6 , Issue.24 , pp. 6528-6537
    • Marchand, C.1    Le Marechal, P.2    Meyer, Y.3    Decottignies, P.4
  • 136
    • 65249135989 scopus 로고    scopus 로고
    • Prompt and easy activation by specific thioredoxins of Calvin cycle enzymes of Arabidopsis thaliana associated in the GAPDH/CP12/PRK supramolecular complex
    • Marri L, Zaffagnini M, Collin V, Issakidis-Bourguet E, Lemaire SD, Pupillo P, Sparla F, Miginiac-Maslow M, and Trost P. Prompt and easy activation by specific thioredoxins of Calvin cycle enzymes of Arabidopsis thaliana associated in the GAPDH/CP12/PRK supramolecular complex. Mol Plant 2: 259-269, 2009.
    • (2009) Mol Plant , vol.2 , pp. 259-269
    • Marri, L.1    Zaffagnini, M.2    Collin, V.3    Issakidis-Bourguet, E.4    Lemaire, S.D.5    Pupillo, P.6    Sparla, F.7    Miginiac-Maslow, M.8    Trost, P.9
  • 137
    • 29944444177 scopus 로고    scopus 로고
    • The role of 5′-adenylylsulfate reductase in controlling sulfate reduction in plants
    • DOI 10.1007/s11120-005-9006-z
    • Martin MN, Tarczynski MC, Shen B, and Leustek T. The role of 5¢-adenylylsulfate reductase in controlling sulfate reduction in plants. Photosynth Res 86: 309-323, 2005. (Pubitemid 43042758)
    • (2005) Photosynthesis Research , vol.86 , Issue.3 , pp. 309-323
    • Martin, M.N.1    Tarczynski, M.C.2    Shen, B.3    Leustek, T.4
  • 138
    • 0027210070 scopus 로고
    • ATP-dependent glutathione S-conjugate 'export' pump in the vacuolar membrane of plants
    • DOI 10.1038/364247a0
    • Martinoia E, Grill E, Tommasini R, Kreuz K, and Amrhein N. ATP-dependent glutathione S-conjugate ''export'' pump in the vacuolar membrane of plants. Nature 364: 247-249, 1993. (Pubitemid 23257084)
    • (1993) Nature , vol.364 , Issue.6434 , pp. 247-249
    • Martinoia, E.1    Grill, E.2    Tommasini, R.3    Kreuz, K.4    Amrhein, N.5
  • 140
    • 0038662709 scopus 로고    scopus 로고
    • Thioredoxin and germinating barley: Targets and protein redox changes
    • Marx C, Wong JH, and Buchanan BB. Thioredoxin and germinating barley: targets and protein redox changes. Planta 216: 454-460, 2003. (Pubitemid 36761767)
    • (2003) Planta , vol.216 , Issue.3 , pp. 454-460
    • Marx, C.1    Wong, J.H.2    Buchanan, B.B.3
  • 142
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister A. Glutathione metabolism and its selective modification. J Biol Chem 263: 17205-17208, 1988. (Pubitemid 19029311)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.33 , pp. 17205-17208
    • Meister, A.1
  • 143
    • 77649251362 scopus 로고    scopus 로고
    • A membrane-associated thioredoxin required for plant growth moves from cell to cell, suggestive of a role in intercellular communication
    • Meng L, Wong JH, Feldman LJ, Lemaux PG, and Buchanan BB. A membrane-associated thioredoxin required for plant growth moves from cell to cell, suggestive of a role in intercellular communication. Proc Natl Acad Sci USA 107: 3900-3905, 2010.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3900-3905
    • Meng, L.1    Wong, J.H.2    Feldman, L.J.3    Lemaux, P.G.4    Buchanan, B.B.5
  • 144
    • 0032735140 scopus 로고    scopus 로고
    • The arabidopsis thaliana genome encodes at least four thioredoxins m and a new prokaryotic-like thioredoxin
    • Mestres-Ortega D and Meyer Y. The Arabidopsis thaliana genome encodes at least four thioredoxins m and a new prokaryotic-like thioredoxin. Gene 240: 307-316, 1999.
    • (1999) Gene , vol.240 , pp. 307-316
    • Mestres-Ortega, D.1    Meyer, Y.2
  • 145
    • 0034906367 scopus 로고    scopus 로고
    • Quantitative in vivo measurement of glutathione in Arabidopsis cells
    • DOI 10.1046/j.1365-313X.2001.01071.x
    • Meyer AJ, May MJ, and Fricker M. Quantitative in vivo measurement of glutathione in Arabidopsis cells. Plant J 27: 67-78, 2001. (Pubitemid 32704240)
    • (2001) Plant Journal , vol.27 , Issue.1 , pp. 67-78
    • Meyer, A.J.1    May, M.J.2    Fricker, M.3
  • 146
    • 79957626987 scopus 로고    scopus 로고
    • Alternative targeting of Arabidopsis plastidic glucose-6-phosphate dehydrogenase G6PD1 involves cysteine-dependent interaction with G6PD4 in the cytosol
    • Meyer T, Hölscher C, Schwöppe C, and von Schaewen A. Alternative targeting of Arabidopsis plastidic glucose-6-phosphate dehydrogenase G6PD1 involves cysteine-dependent interaction with G6PD4 in the cytosol. Plant J 66: 745-758, 2011.
    • (2011) Plant J , vol.66 , pp. 745-758
    • Meyer, T.1    Hölscher, C.2    Schwöppe, C.3    Von Schaewen, A.4
  • 148
    • 73349133007 scopus 로고    scopus 로고
    • Thioredoxins and glutaredoxins: Unifying elements in redox biology
    • Meyer Y, Buchanan BB, Vignols F, and Reichheld J-P. Thioredoxins and glutaredoxins: unifying elements in redox biology. Annu Rev Genet 43: 335-367, 2009.
    • (2009) Annu Rev Genet , vol.43 , pp. 335-367
    • Meyer, Y.1    Buchanan, B.B.2    Vignols, F.3    Reichheld, J.-P.4
  • 149
    • 77954306359 scopus 로고    scopus 로고
    • Arabidopsis glutathione reductase1 plays a crucial role in leaf responses to intracellular hydrogen peroxide and in ensuring appropriate gene expression through both salicylic acid and jasmonic acid signaling pathways
    • Mhamdi A, Hager J, Chaouch S, Queval G, Han Y, Taconnat L, Saindrenan P, Gouia H, Issakidis-Bourguet E, Renou JP, and Noctor G. Arabidopsis glutathione reductase1 plays a crucial role in leaf responses to intracellular hydrogen peroxide and in ensuring appropriate gene expression through both salicylic acid and jasmonic acid signaling pathways. Plant Physiol 153: 1144-1160, 2010.
    • (2010) Plant Physiol , vol.153 , pp. 1144-1160
    • Mhamdi, A.1    Hager, J.2    Chaouch, S.3    Queval, G.4    Han, Y.5    Taconnat, L.6    Saindrenan, P.7    Gouia, H.8    Issakidis-Bourguet, E.9    Renou, J.P.10    Noctor, G.11
  • 150
    • 67649880593 scopus 로고    scopus 로고
    • NTRC links built-in thioredoxin to light and sucrose in regulating starch synthesis in chloroplasts and amyloplasts
    • Michalska J, Zauber H, Buchanan B, Cejudo FJ, and Geigenberger P. NTRC links built-in thioredoxin to light and sucrose in regulating starch synthesis in chloroplasts and amyloplasts. Proc Natl Acad Sci USA 106: 9908-9913, 2009.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9908-9913
    • Michalska, J.1    Zauber, H.2    Buchanan, B.3    Cejudo, F.J.4    Geigenberger, P.5
  • 155
    • 0001432326 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. V. Purification and properties of thioredoxin reductase from Escherichia coli b
    • Moore EC, Reichard P, and Thelander L. Enzymatic synthesis of deoxyribonucleotides. V. Purification and properties of thioredoxin reductase from Escherichia coli b. J Biol Chem 239: 3445-3452, 1964.
    • (1964) J Biol Chem , vol.239 , pp. 3445-3452
    • Moore, E.C.1    Reichard, P.2    Thelander, L.3
  • 157
    • 33845939598 scopus 로고    scopus 로고
    • HCF164 receives reducing equivalents from stromal thioredoxin across the thylakoid membrane and mediates reduction of target proteins in the thylakoid lumen
    • DOI 10.1074/jbc.M605938200
    • Motohashi K and Hisabori T. HCF164 receives reducing equivalents from stromal thioredoxin across the thylakoid membrane and mediates reduction of target proteins in the thylakoid lumen. J Biol Chem 281: 35039-35047, 2006. (Pubitemid 46036543)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.46 , pp. 35039-35047
    • Motohashi, K.1    Hisabori, T.2
  • 158
    • 77956319563 scopus 로고    scopus 로고
    • CcdA is a thylakoid membrane protein required for the transfer of reducing equivalents from stroma to thylakoid lumen in the higher plant chloroplast
    • Motohashi K and Hisabori T. CcdA is a thylakoid membrane protein required for the transfer of reducing equivalents from stroma to thylakoid lumen in the higher plant chloroplast. Antioxid Redox Signal 13: 1169-1176, 2010.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1169-1176
    • Motohashi, K.1    Hisabori, T.2
  • 159
    • 0038826955 scopus 로고    scopus 로고
    • Inducers of plant systemic acquired resistance Regulate NPR1 function through redox changes
    • DOI 10.1016/S0092-8674(03)00429-X
    • Mou Z, Fan W, and Dong X. Inducers of plant systemic acquired resistance regulate NPR1 function through redox changes. Cell 113: 935-944, 2003. (Pubitemid 36792035)
    • (2003) Cell , vol.113 , Issue.7 , pp. 935-944
    • Mou, Z.1    Fan, W.2    Dong, X.3
  • 160
    • 0026513919 scopus 로고
    • Thioredoxin genes in Saccharomyces cerevisiae: Map positions of TRX1 and TRX2
    • Muller EG. Thioredoxin genes in Saccharomyces cerevisiae: map positions of TRX1 and TRX2. Yeast 8: 117-120, 1992.
    • (1992) Yeast , vol.8 , pp. 117-120
    • Muller, E.G.1
  • 161
    • 0028987974 scopus 로고
    • A redox-dependent function of thioredoxin is necessary to sustain a rapid rate of DNA synthesis in yeast
    • Muller EG. A redox-dependent function of thioredoxin is necessary to sustain a rapid rate of DNA synthesis in yeast. Arch Biochem Biophys 318: 356-361, 1995.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 356-361
    • Muller, E.G.1
  • 162
    • 0029948308 scopus 로고    scopus 로고
    • A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth
    • Muller EG. A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth. Mol Biol Cell 7: 1805-1813, 1996. (Pubitemid 26386731)
    • (1996) Molecular Biology of the Cell , vol.7 , Issue.11 , pp. 1805-1813
    • Muller, E.G.D.1
  • 163
    • 0026533580 scopus 로고
    • Inhibition of the ADP-glucose pyrophosphorylase in transgenic potatoes leads to sugar-storing tubers and influences tuber formation and expression of tuber storage protein genes
    • Müller-Röber B, Sonnewald U, and Willmitzer L. Inhibition of the ADP-glucose pyrophosphorylase in transgenic potatoes leads to sugar-storing tubers and influences tuber formation and expression of tuber storage protein genes. EMBO J 11: 1229-1238, 1992.
    • (1992) EMBO J , vol.11 , pp. 1229-1238
    • Müller-Röber, B.1    Sonnewald, U.2    Willmitzer, L.3
  • 164
    • 78249288758 scopus 로고    scopus 로고
    • Arabidopsis basic leucine-zipper transcription factors TGA9 and TGA10 interact with floral glutaredoxins ROXY1 and ROXY2 and are redundantly required for anther development
    • Murmu J, Bush MJ, DeLong C, Li S, Xu M, Khan M, Malcolmson C, Fobert PR, Zachgo S, and Hepworth SR. Arabidopsis basic leucine-zipper transcription factors TGA9 and TGA10 interact with floral glutaredoxins ROXY1 and ROXY2 and are redundantly required for anther development. Plant Physiol 154: 1492-1504, 2010.
    • (2010) Plant Physiol , vol.154 , pp. 1492-1504
    • Murmu, J.1    Bush, M.J.2    Delong, C.3    Li, S.4    Xu, M.5    Khan, M.6    Malcolmson, C.7    Fobert, P.R.8    Zachgo, S.9    Hepworth, S.R.10
  • 165
    • 33748966838 scopus 로고    scopus 로고
    • Identification of a new family of plant proteins loosely related to glutaredoxins with four CxxC motives
    • DOI 10.1007/s11120-006-9083-7
    • Navrot N, Gelhaye E, Jacquot J-P, and Rouhier N. Identification of a new family of plant proteins loosely related to glutaredoxins with four CxxC motives. Photosynth Res 89: 71-79, 2006. (Pubitemid 44440485)
    • (2006) Photosynthesis Research , vol.89 , Issue.2 , pp. 71-79
    • Navrot, N.1    Gelhaye, E.2    Jacquot, J.-P.3    Rouhier, N.4
  • 166
    • 33947651152 scopus 로고    scopus 로고
    • SA-inducible Arabidopsis glutaredoxin interacts with TGA factors and suppresses JA-responsive PDF1.2 transcription
    • DOI 10.1111/j.1365-313X.2007.03039.x
    • Ndamukong I, Abdallat AA, Thurow C, Fode B, Zander M, Weigel R, and Gatz C. SA-inducible Arabidopsis glutaredoxin interacts with TGA factors and suppresses JA-responsive PDF1.2 transcription. Plant J 50: 128-139, 2007. (Pubitemid 46493401)
    • (2007) Plant Journal , vol.50 , Issue.1 , pp. 128-139
    • Ndamukong, I.1    Abdallat, A.A.2    Thurow, C.3    Fode, B.4    Zander, M.5    Weigel, R.6    Gatz, C.7
  • 167
    • 69249205644 scopus 로고    scopus 로고
    • Redox regulation of chloroplastic glucose-6-phosphate dehydrogenase: A new role for f-type thioredoxin
    • Née G, Zaffagnini M, Trost P, and Issakidis-Bourguet E. Redox regulation of chloroplastic glucose-6-phosphate dehydrogenase: a new role for f-type thioredoxin. FEBS Lett 583: 2827-2832, 2009.
    • (2009) FEBS Lett , vol.583 , pp. 2827-2832
    • Née, G.1    Zaffagnini, M.2    Trost, P.3    Issakidis-Bourguet, E.4
  • 168
    • 33745816673 scopus 로고    scopus 로고
    • CITRX thioredoxin is a putative adaptor protein connecting Cf-9 and the ACIK1 protein kinase during the Cf-9/Avr9- induced defence response
    • DOI 10.1016/j.febslet.2006.06.077, PII S0014579306007940
    • Nekrasov V, Ludwig AA, and Jones JDG. CITRX thioredoxin is a putative adaptor protein connecting Cf-9 and the ACIK1 protein kinase during the Cf-9/Avr9-induced defence response. FEBS Lett 580: 4236-4241, 2006. (Pubitemid 44037594)
    • (2006) FEBS Letters , vol.580 , Issue.17 , pp. 4236-4241
    • Nekrasov, V.1    Ludwig, A.A.2    Jones, J.D.G.3
  • 170
    • 33847148080 scopus 로고    scopus 로고
    • Characterization of the extracellular γ-glutamyl transpeptidases, GGT1 and GGT2, in Arabidopsis
    • DOI 10.1111/j.1365-313X.2006.03004.x
    • Ohkamu-Ohtsu N, Radwan S, Peterson A, Zhao P, Badr AF, Xiang C, and Oliver DJ. Characterization of the extracellular c-glutamyl transpeptidases, GGT1 and GGT2, in Arabidopsis. Plant J 49: 865-877, 2007. (Pubitemid 46279269)
    • (2007) Plant Journal , vol.49 , Issue.5 , pp. 865-877
    • Ohkama-Ohtsu, N.1    Radwan, S.2    Peterson, A.3    Zhao, P.4    Badr, A.F.5    Xiang, C.6    Oliver, D.J.7
  • 172
    • 33845620655 scopus 로고    scopus 로고
    • Identification of PAD2 as a γ-glutamylcysteine synthetase highlights the importance of glutathione in disease resistance of Arabidopsis
    • DOI 10.1111/j.1365-313X.2006.02938.x
    • Parisy V, Poinssot B, Owsianowski L, Buchala A, Glazebrook J, and Mauch F. Identification of PAD2 as a gammaglutamylcysteine synthetase highlights the importance of glutathione in disease resistance of Arabidopsis. Plant J 49: 159-172, 2007. (Pubitemid 44952706)
    • (2007) Plant Journal , vol.49 , Issue.1 , pp. 159-172
    • Parisy, V.1    Poinssot, B.2    Owsianowski, L.3    Buchala, A.4    Glazebrook, J.5    Mauch, F.6
  • 174
    • 40549143429 scopus 로고    scopus 로고
    • Restricting glutathione biosynthesis to the cytosol is sufficient for normal plant development
    • DOI 10.1111/j.1365-313X.2007.03389.x
    • Pasternak M, Lim B, Wirtz M, Hell R, Cobbett CS, and Meyer AJ. Restricting glutathione biosynthesis to the cytosol is sufficient for normal plant development. Plant J 53: 999-1012, 2008. (Pubitemid 351357818)
    • (2008) Plant Journal , vol.53 , Issue.6 , pp. 999-1012
    • Pasternak, M.1    Lim, B.2    Wirtz, M.3    Hell, R.4    Cobbett, C.S.5    Meyer, A.J.6
  • 175
    • 33749233825 scopus 로고    scopus 로고
    • Rice NTRC is a high-efficiency redox system for chloroplast protection against oxidative damage
    • DOI 10.1105/tpc.106.041541
    • Pérez-Ruiz JM, Spínola MC, Kirchsteiger K, Moreno J, Sahrawy M, and Cejudo FJ. Rice NTRC is a high-efficiency redox system for chloroplast protection against oxidative damage. Plant Cell 9: 2356-2368, 2006. (Pubitemid 44484731)
    • (2006) Plant Cell , vol.18 , Issue.9 , pp. 2356-2368
    • Perez-Ruiz, J.M.1    Spinola, M.C.2    Kirchsteiger, K.3    Moreno, J.4    Sahrawy, M.5    Cejudo, F.J.6
  • 176
    • 33645739638 scopus 로고    scopus 로고
    • PTAC2, -6, and -12 are components of the transcriptionally active plastid chromosome that are required for plastid gene expression
    • DOI 10.1105/tpc.105.036392
    • Pfalz J, Liere K, Kandlbinder A, Dietz K-J, and Oelmüller R. pTAC2, -6, and -12 are components of the transcriptionally active plastid chromosome that are required for plastid gene expression. Plant Cell 18: 176-197, 2006. (Pubitemid 43951323)
    • (2006) Plant Cell , vol.18 , Issue.1 , pp. 176-197
    • Pfalz, J.1    Liere, K.2    Kandlbinder, A.3    Dietz, K.-J.4    Oelmuller, R.5
  • 177
    • 70450235178 scopus 로고    scopus 로고
    • Arabidopsis OPT6 is an oligopeptide transporter with exceptionally broad substrate specificity
    • Pike S, Patel A, Stacey G, and Gassmann W. Arabidopsis OPT6 is an oligopeptide transporter with exceptionally broad substrate specificity. Plant Cell Physiol 50: 1923-1932, 2009.
    • (2009) Plant Cell Physiol , vol.50 , pp. 1923-1932
    • Pike, S.1    Patel, A.2    Stacey, G.3    Gassmann, W.4
  • 178
    • 70149108590 scopus 로고    scopus 로고
    • Penetration of the stigma and style elicits a novel transcriptome in pollen tubes, pointing to genes critical for growth in a pistil
    • Qin Y, Leydon AR, Manziello A, Pandey R, Mount D, Denic S, Vasic B, Johnson MA, and Palanivelu R. Penetration of the stigma and style elicits a novel transcriptome in pollen tubes, pointing to genes critical for growth in a pistil. PLoS Genet 8: e1000621, 2009.
    • (2009) PLoS Genet , vol.8
    • Qin, Y.1    Leydon, A.R.2    Manziello, A.3    Pandey, R.4    Mount, D.5    Denic, S.6    Vasic, B.7    Johnson, M.A.8    Palanivelu, R.9
  • 179
  • 180
    • 0033047445 scopus 로고    scopus 로고
    • MRP subfamily transporters from plants and yeast
    • Rea PA. MRP subfamily transporters from plants and yeast. J Exp Bot 50: 895-913, 1999.
    • (1999) J Exp Bot , vol.50 , pp. 895-913
    • Rea, P.A.1
  • 181
    • 0033672274 scopus 로고    scopus 로고
    • Activation properties of the redox-modulated chloroplast enzymes glyceraldehyde 3-phosphate dehydrogenase and fructose-1,6-bisphosphatase
    • Reichert A, Baalmann E, Vetter S, Backhausen JE, and Scheibe R. Activation properties of the redox-modulated chloroplast enzymes glyceraldehyde 3-phosphate dehydrogenase and fructose-1,6-bisphosphatase. Physiol Plant 110: 330-341, 2000.
    • (2000) Physiol Plant , vol.110 , pp. 330-341
    • Reichert, A.1    Baalmann, E.2    Vetter, S.3    Backhausen, J.E.4    Scheibe, R.5
  • 182
    • 11844285694 scopus 로고    scopus 로고
    • AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana
    • DOI 10.1016/j.febslet.2004.11.094, PII S0014579304015030
    • Reichheld J-P, Meyer E, Khafif M, Bonnard G, and Meyer Y. AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana. FEBS Lett 579: 337-342, 2005. (Pubitemid 40092409)
    • (2005) FEBS Letters , vol.579 , Issue.2 , pp. 337-342
    • Reichheld, J.-P.1    Meyer, E.2    Khafif, M.3    Bonnard, G.4    Meyer, Y.5
  • 183
    • 34547698762 scopus 로고    scopus 로고
    • Inactivation of thioredoxin reductases reveals a complex interplay between thioredoxin and glutathione pathways in arabidopsis development
    • DOI 10.1105/tpc.107.050849
    • Reichheld J-P, Khafif M, Riondet C, Droux M, Bonnard G, and Meyer Y. Inactivation of thioredoxin reductases reveals a complex interplay between thioredoxin and glutathione pathways in Arabidopsis development. Plant Cell 19: 1851-1865, 2007. (Pubitemid 47218845)
    • (2007) Plant Cell , vol.19 , Issue.6 , pp. 1851-1865
    • Reichheld, J.-P.1    Khafif, M.2    Riondet, C.3    Droux, M.4    Bonnard, G.5    Meyer, Y.6
  • 184
    • 0031885601 scopus 로고    scopus 로고
    • A novel thioredoxin-like protein located in the chloroplast is induced by water deficit in Solanum tuberosum L. plants
    • DOI 10.1046/j.1365-313X.1998.00015.x
    • Rey P, Pruvot G, Becuwe N, Eymery F, Rumeau D, and Peltier G. 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. (Pubitemid 28065693)
    • (1998) Plant Journal , vol.13 , Issue.1 , pp. 97-107
    • Rey, P.1    Pruvot, G.2    Becuwe, N.3    Eymery, F.4    Rumeau, D.5    Peltier, G.6
  • 185
    • 12744274638 scopus 로고    scopus 로고
    • Analysis of the proteins targeted by CDSP32, a plastidic thioredoxin participating in oxidative stress responses
    • Rey P, Cuiné S, Eymery F, Garin J, Court M, Jacquot JP, Rouhier N, and Broin M. Analysis of the proteins targeted by CDSP32, a plastidic thioredoxin participating in oxidative stress responses. Plant J 41: 31-42, 2005.
    • (2005) Plant J , vol.41 , pp. 31-42
    • Rey, P.1    Cuiné, S.2    Eymery, F.3    Garin, J.4    Court, M.5    Jacquot, J.P.6    Rouhier, N.7    Broin, M.8
  • 186
    • 0033212993 scopus 로고    scopus 로고
    • A defect in beta-oxidation causes abnormal inflorescence development in Arabidopsis
    • Richmond TA and Bleecker AB. A defect in beta-oxidation causes abnormal inflorescence development in Arabidopsis. Plant Cell 11: 1911-1924, 1999.
    • (1999) Plant Cell , vol.11 , pp. 1911-1924
    • Richmond, T.A.1    Bleecker, A.B.2
  • 188
    • 2942535848 scopus 로고    scopus 로고
    • CITRX thioredoxin interacts with the tomato Cf-9 resistance protein and negatively regulates defence
    • DOI 10.1038/sj.emboj.7600224
    • Rivas S, Rougon-Cardoso A, Smoker M, Schauser L, Yoshioka H, and Jones JDG. CITRX thioredoxin interacts with the tomato Cf-9 resistance protein and negatively regulates defence. EMBO J 19;23: 2156-2165, 2004. (Pubitemid 38737742)
    • (2004) EMBO Journal , vol.23 , Issue.10 , pp. 2156-2165
    • Rivas, S.1    Rougon-Cardoso, A.2    Smoker, M.3    Schauser, L.4    Yoshioka, H.5    Jones, J.D.G.6
  • 190
    • 33947501073 scopus 로고    scopus 로고
    • The coactivator function of Arabidopsis NPR1 requires the core of its BTB/POZ domain and the oxidation of C-terminal cysteines
    • DOI 10.1105/tpc.106.046953
    • Rochon A, Boyle P, Wignes T, Fobert PR, and Després C. The coactivator function of Arabidopsis NPR1 requires the core of its BTB/POZ domain and the oxidation of C-terminal cysteines. Plant Cell 18: 3670-3685, 2006. (Pubitemid 46464920)
    • (2006) Plant Cell , vol.18 , Issue.12 , pp. 3670-3685
    • Rochon, A.1    Boyle, P.2    Wignes, T.3    Fobert, P.R.4    Despres, C.5
  • 191
    • 0037196446 scopus 로고    scopus 로고
    • Exploring the active site of plant glutaredoxin by site-directed mutagenesis
    • DOI 10.1016/S0014-5793(01)03302-6, PII S0014579301033026
    • Rouhier N, Gelhaye E, and Jacquot J-P. Exploring the active site of plant glutaredoxin by site-directed mutagenesis. FEBS Lett 511: 145-149, 2002. (Pubitemid 34127839)
    • (2002) FEBS Letters , vol.511 , Issue.1-3 , pp. 145-149
    • Rouhier, N.1    Gelhaye, E.2    Jacquot, J.-P.3
  • 194
    • 42949085825 scopus 로고    scopus 로고
    • The role of glutathione in photosynthetic organisms: Emerging functions for glutaredoxins and glutathionylation
    • DOI 10.1146/annurev.arplant.59.032607.092811
    • Rouhier N, Lemaire SD, and Jacquot J-P. The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation. Annu Rev Plant Biol 59: 143-166, 2008. (Pubitemid 351813027)
    • (2008) Annual Review of Plant Biology , vol.59 , pp. 143-166
    • Rouhier, N.1    Lemaire, S.D.2    Jacquot, J.-P.3
  • 196
    • 77954722636 scopus 로고    scopus 로고
    • Plant glutaredoxins: Pivotal players in redox biology and iron-sulphur centre assembly
    • Rouhier N. Plant glutaredoxins: pivotal players in redox biology and iron-sulphur centre assembly. New Phytol 186: 365-372, 2010.
    • (2010) New Phytol , vol.186 , pp. 365-372
    • Rouhier, N.1
  • 197
    • 0032922625 scopus 로고    scopus 로고
    • Regulation of chloroplast enzyme activities by thioredoxins: Activation or relief from inhibition?
    • DOI 10.1016/S1360-1385(99)01391-6, PII S1360138599013916
    • Ruelland E and Miginiac-Maslow M. Regulation of chloroplast enzyme activities by thioredoxins: activation or relief from inhibition? Trends Plant Sci 4: 136-141, 1999. (Pubitemid 29178028)
    • (1999) Trends in Plant Science , vol.4 , Issue.4 , pp. 136-141
    • Ruelland, E.1    Miginiac-Maslow, M.2
  • 199
    • 13844306891 scopus 로고    scopus 로고
    • Functional specialization of Chlamydomonas reinhardtii cytosolic thioredoxin h1 in the response to alkylation-induced DNA damage
    • DOI 10.1128/EC.4.2.262-273.2005
    • Sarkar N, Lemaire S, Wu-Scharf D, Issakidis-Bourguet E, and Cerutti H. Functional specialization of Chlamydomonas reinhardtii cytosolic thioredoxin h1 in the response to alkylationinduced DNA damage. Eukaryot Cell 4: 262-273, 2005. (Pubitemid 40257126)
    • (2005) Eukaryotic Cell , vol.4 , Issue.2 , pp. 262-273
    • Sarkar, N.1    Lemaire, S.2    Wu-Scharf, D.3    Issakidis-Bourguet, E.4    Cerutti, H.5
  • 200
    • 0019878627 scopus 로고
    • Dark modulation of NADPdependent malate dehydrogenase and glucose-6-phosphate dehydrogenase in the chloroplast
    • Scheibe R and Anderson LE. Dark modulation of NADPdependent malate dehydrogenase and glucose-6-phosphate dehydrogenase in the chloroplast. Biochim Biophys Acta 636: 58-64, 1981.
    • (1981) Biochim Biophys Acta , vol.636 , pp. 58-64
    • Scheibe, R.1    Anderson, L.E.2
  • 201
    • 77952999879 scopus 로고    scopus 로고
    • Analysis of oligomeric protein complexes in the chloroplast sub-proteome of nucleic acid-binding proteins from mustard reveals potential redox regulators of plastid gene expression
    • Schröter Y, Steiner S, Matthäi K, and Pfannschmidt T. Analysis of oligomeric protein complexes in the chloroplast sub-proteome of nucleic acid-binding proteins from mustard reveals potential redox regulators of plastid gene expression. Proteomics 10: 2191-2204, 2010.
    • (2010) Proteomics , vol.10 , pp. 2191-2204
    • Schröter, Y.1    Steiner, S.2    Matthäi, K.3    Pfannschmidt, T.4
  • 202
    • 42949151399 scopus 로고    scopus 로고
    • The ferredoxin/thioredoxin system of oxygenic photosynthesis
    • Schürmann P and Buchanan BB. The ferredoxin/thioredoxin system of oxygenic photosynthesis. Antioxid Redox Signal 10: 1235-1274, 2008.
    • (2008) Antioxid Redox Signal , vol.10 , pp. 1235-1274
    • Schürmann, P.1    Buchanan, B.B.2
  • 203
    • 84860497776 scopus 로고    scopus 로고
    • The role of thioredoxin in the regulation of cellular processes by S-nitrosylation
    • Sengupta R and Holmgren A. The role of thioredoxin in the regulation of cellular processes by S-nitrosylation. Biochim Biophys Acta 1820: 689-700, 2012.
    • (2012) Biochim Biophys Acta , vol.1820 , pp. 689-700
    • Sengupta, R.1    Holmgren, A.2
  • 204
    • 6344235622 scopus 로고    scopus 로고
    • A novel NADPH thioredoxin reductase, localised in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana
    • DOI 10.1074/jbc.M404696200
    • Serrato AJ, Pérez-Ruiz JM, Spínola MC, and Cejudo FJ. 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. (Pubitemid 39390688)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.42 , pp. 43821-43827
    • Serrato, A.J.1    Perez-Ruiz, J.M.2    Spinola, M.C.3    Cejudo, F.J.4
  • 205
    • 45249107767 scopus 로고    scopus 로고
    • AtCXXS: Atypical members of the Arabidopsis thaliana thioredoxin h family with a remarkably high disulfide isomerase activity
    • DOI 10.1111/j.1399-3054.2008.01093.x
    • Serrato AJ, Guilleminot J, Meyer Y, and Vignols F. AtCXXS: atypical members of the Arabidopsis thaliana thioredoxin a family with a remarkably high disulfide isomerase activity. Physiol Plant 133: 611-622, 2008. (Pubitemid 351841676)
    • (2008) Physiologia Plantarum , vol.133 , Issue.3 , pp. 611-622
    • Serrato, A.J.1    Guilleminot, J.2    Meyer, Y.3    Vignols, F.4
  • 206
    • 0029841432 scopus 로고    scopus 로고
    • Sulfate reduction in higher plants: Molecular evidence for a novel 5¢-adenylylsulfate reductase
    • Setya A, Murillo M, and Leustek T. Sulfate reduction in higher plants: molecular evidence for a novel 5¢-adenylylsulfate reductase. Proc Natl Acad Sci U S A 93: 13383-13388, 1996.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 13383-13388
    • Setya, A.1    Murillo, M.2    Leustek, T.3
  • 208
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation: The prototypic redox-based signaling mechanism
    • DOI 10.1016/S0092-8674(01)00495-0
    • Stamler JS, Lamas S, and Fang FC. Nitrosylation: the prototypic redox-based signaling mechanism. Cell 106: 675-683, 2001. (Pubitemid 32900659)
    • (2001) Cell , vol.106 , Issue.6 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 209
    • 0038015010 scopus 로고    scopus 로고
    • Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase): Potential role in redox signal transduction
    • DOI 10.1074/jbc.M210434200
    • Starke DW, Chock PB, and Mieyal JJ. Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction. J Biol Chem 278: 14607-14613, 2003. (Pubitemid 36799782)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.17 , pp. 14607-14613
    • Starke, D.W.1    Chock, P.B.2    Mieyal, J.J.3
  • 210
    • 0002673987 scopus 로고
    • Degradation of glutathione in plant cells: Evidence against the participation of a gglutamyltranspeptidase
    • Steinkamp R and Rennenberg H. Degradation of glutathione in plant cells: evidence against the participation of a gglutamyltranspeptidase. Zeitschrift für Naturforschung Section C 40: 29-33, 1985.
    • (1985) Zeitschrift für Naturforschung Section C , vol.40 , pp. 29-33
    • Steinkamp, R.1    Rennenberg, H.2
  • 211
    • 71249151181 scopus 로고    scopus 로고
    • Preprotein import into chloroplasts via the Toc and Tic complexes is regulated by redox signals in Pisum sativum
    • Stengel A, Benz JP, Buchanan BB, Soll J, and Bölter B. Preprotein import into chloroplasts via the Toc and Tic complexes is regulated by redox signals in Pisum sativum. Mol Plant 2: 1181-1197, 2009.
    • (2009) Mol Plant , vol.2 , pp. 1181-1197
    • Stengel, A.1    Benz, J.P.2    Buchanan, B.B.3    Soll, J.4    Bölter, B.5
  • 212
    • 78449278730 scopus 로고    scopus 로고
    • Why have chloroplasts developed a unique motility system?
    • Suetsugu N, Dolja VV, and Wada M. Why have chloroplasts developed a unique motility system? Plant Signal Behav 5: 1190-1196, 2010.
    • (2010) Plant Signal Behav , vol.5 , pp. 1190-1196
    • Suetsugu, N.1    Dolja, V.V.2    Wada, M.3
  • 213
    • 34250661741 scopus 로고    scopus 로고
    • Thioredoxin h5 is required for victorin sensitivity mediated by a CC-NBS-LRR gene in Arabidopsis
    • DOI 10.1105/tpc.106.047563
    • Sweat TA and Wolpert TJ. Thioredoxin h5 is required for victorin sensitivity mediated by a CC-NBS-LRR gene in Arabidopsis. Plant Cell 19: 673-687, 2007. (Pubitemid 46941686)
    • (2007) Plant Cell , vol.19 , Issue.2 , pp. 673-687
    • Sweat, T.A.1    Wolpert, T.J.2
  • 214
    • 37149023158 scopus 로고    scopus 로고
    • Characterization of natural and induced variation in the LOV1 gene, a CC-NB-LRR gene conferring victorin sensitivity and disease susceptibility in Arabidopsis
    • DOI 10.1094/MPMI-21-1-0007
    • Sweat TA, Lorang JM, Bakker EG, and Wolpert TJ. Characterization of natural and induced variation in the LOV1 gene, a CC-NB-LRR gene conferring victorin sensitivity and disease susceptibility in Arabidopsis. MPMI 1: 7-19, 2008. (Pubitemid 350262357)
    • (2008) Molecular Plant-Microbe Interactions , vol.21 , Issue.1 , pp. 7-19
    • Sweat, T.A.1    Lorang, J.M.2    Bakker, E.G.3    Wolpert, T.J.4
  • 215
    • 49649112131 scopus 로고    scopus 로고
    • Plant immunity requires conformational changes of NPR1 via S-nitrosylation and thioredoxins
    • Tada Y, Spoel SH, Pajerowska-Mukhtar K, Mou Z, Song J, and Dong X. Plant immunity requires conformational changes of NPR1 via S-nitrosylation and thioredoxins. Science 321: 952-956, 2008.
    • (2008) Science , vol.321 , pp. 952-956
    • Tada, Y.1    Spoel, S.H.2    Pajerowska-Mukhtar, K.3    Mou, Z.4    Song, J.5    Dong, X.6
  • 216
    • 0038491193 scopus 로고    scopus 로고
    • Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin
    • DOI 10.1074/jbc.M303477200
    • Tamarit J, Belli G, Cabiscol E, Herrero E, and Ros J. Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin. J Biol Chem 278: 25745-25751, 2003. (Pubitemid 36835331)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 25745-25751
    • Tamarit, J.1    Belli, G.2    Cabiscol, E.3    Herrero, E.4    Ros, J.5
  • 217
    • 77949899140 scopus 로고    scopus 로고
    • The thioredoxin-thioredoxin reductase system can function in vivo as an alternative system to reduce oxidized glutathione in Saccharomyces cerevisiae
    • Tan SX, Greetham D, Raeth S, Grant CM, Dawes IW, and Perrone GG. The thioredoxin-thioredoxin reductase system can function in vivo as an alternative system to reduce oxidized glutathione in Saccharomyces cerevisiae. J Biol Chem 285: 6118-6126, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 6118-6126
    • Tan, S.X.1    Greetham, D.2    Raeth, S.3    Grant, C.M.4    Dawes, I.W.5    Perrone, G.G.6
  • 218
  • 219
    • 77952071893 scopus 로고    scopus 로고
    • Plant thioredoxin CDSP32 regenerates 1-cys methionine sulfoxide reductase B activity through the direct reduction of sulfenic acid
    • Tarrago L, Laugier E, Zaffagnini M, Marchand CH, Le Maréchal P, Lemaire SD, and Rey P. Plant thioredoxin CDSP32 regenerates 1-cys methionine sulfoxide reductase B activity through the direct reduction of sulfenic acid. J Biol Chem 285: 14964-14972, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 14964-14972
    • Tarrago, L.1    Laugier, E.2    Zaffagnini, M.3    Marchand, C.H.4    Le Maréchal, P.5    Lemaire, S.D.6    Rey, P.7
  • 220
  • 221
    • 34447518686 scopus 로고    scopus 로고
    • The system biology of thiol redox system in Escherichia coli and yeast: Differential functions in oxidative stress, iron metabolism and DNA synthesis
    • DOI 10.1016/j.febslet.2007.07.002, PII S0014579307007557, Cellular Stress
    • Toledano MB, Kumar C, Le Moan N, Spector D, and Tacnet F. The system biology of thiol redox system in Escherichia coli and yeast: differential functions in oxidative stress, iron metabolism and DNA synthesis. FEBS Lett 581: 3598-3607, 2007. (Pubitemid 47081012)
    • (2007) FEBS Letters , vol.581 , Issue.19 , pp. 3598-3607
    • Toledano, M.B.1    Kumar, C.2    Le Moan, N.3    Spector, D.4    Tacnet, F.5
  • 222
    • 0036435926 scopus 로고    scopus 로고
    • Thioredoxins are required for protection against a reductive stress in the yeast Saccharomyces cerevisiae
    • DOI 10.1046/j.1365-2958.2002.03216.x
    • Trotter EW and Grant CM. Thioredoxins are required for protection against a reductive stress in the yeast Saccharomyces cerevisiae. Mol Microb 46: 869-878, 2002. (Pubitemid 35370032)
    • (2002) Molecular Microbiology , vol.46 , Issue.3 , pp. 869-878
    • Trotter, E.W.1    Grant, C.M.2
  • 223
    • 0037297417 scopus 로고    scopus 로고
    • Non-reciprocal regulation of the redox state of the glutathione- glutaredoxin and thioredoxin systems
    • DOI 10.1038/sj.embor.embor729
    • Trotter EW and Grant CM. Non-reciprocal regulation of the redox state of the glutathione-glutaredoxin and thioredoxin systems. EMBO Rep 4: 184-188, 2003. (Pubitemid 36322161)
    • (2003) EMBO Reports , vol.4 , Issue.2 , pp. 184-188
    • Trotter, E.W.1    Grant, C.M.2
  • 224
    • 13844313006 scopus 로고    scopus 로고
    • Overlapping roles of the cytoplasmic and mitochondrial redox regulatory systems in the yeast Saccharomyces cerevisiae
    • DOI 10.1128/EC.4.2.392-400.2005
    • Trotter EW and Grant CM. Overlapping roles of the cytoplasmic and mitochondrial redox regulatory systems in the yeast Saccharomyces cerevisiae. Eukaryot. Cell 4: 392-400, 2005. (Pubitemid 40257138)
    • (2005) Eukaryotic Cell , vol.4 , Issue.2 , pp. 392-400
    • Trotter, E.W.1    Grant, C.M.2
  • 226
    • 0001613347 scopus 로고    scopus 로고
    • Pathogen-induced changes in the antioxidant status of the apoplast in barley leaves
    • Vanacker H, Carver TLW, and Foyer CH. Pathogen-induced changes in the antioxidant status of the apoplast in barley leaves. Plant Physiol 117: 1103-1114, 1998. (Pubitemid 128652883)
    • (1998) Plant Physiology , vol.117 , Issue.3 , pp. 1103-1114
    • Vanacker, H.1    Carver, T.L.W.2    Foyer, C.H.3
  • 227
    • 0033538442 scopus 로고    scopus 로고
    • Vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family
    • Verdoucq L, Vignols F, Jacquot JP, Chartier Y, and Meyer Y. In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. J Biol Chem 274: 19714-19722, 1999.
    • (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
  • 229
    • 34548503203 scopus 로고    scopus 로고
    • Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B
    • DOI 10.1016/j.febslet.2007.07.081, PII S0014579307008423
    • Vieira Dos Santos C, Laugier E, Tarrago L, Massot V, Issakidis-Bourguet E, Rouhier N, and Rey P. 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. (Pubitemid 47376692)
    • (2007) FEBS Letters , vol.581 , Issue.23 , 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
  • 230
    • 0037799277 scopus 로고    scopus 로고
    • Redox control of Hsp70-co-chaperone interaction revealed by expression of a thioredoxin-like Arabidopsis protein
    • DOI 10.1074/jbc.M210080200
    • Vignols F, Mouaheb N, Thomas D, and Meyer Y. Redox control of Hsp70-Co-chaperone interaction revealed by expression of a thioredoxin-like Arabidopsis protein. J Biol Chem 278: 4516-4523, 2003. (Pubitemid 36800947)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.7 , pp. 4516-4523
    • Vignols, F.1    Mouaheb, N.2    Thomas, D.3    Meyer, Y.4
  • 232
    • 78649560974 scopus 로고    scopus 로고
    • Recruitment of glutathione into the nucleus during cell proliferation adjusts whole-cell redox homeostasis in Arabidopsis thaliana and lowers the oxidative defence shield
    • Vivancos PD, Dong Y, Ziegler K, Markovic J, Pallardó FV, Pellny TK, Verrier PJ, and Foyer CH. Recruitment of glutathione into the nucleus during cell proliferation adjusts whole-cell redox homeostasis in Arabidopsis thaliana and lowers the oxidative defence shield. Plant J 64: 825-838, 2010.
    • (2010) Plant J , vol.64 , pp. 825-838
    • Vivancos, P.D.1    Dong, Y.2    Ziegler, K.3    Markovic, J.4    Pallardó, F.V.5    Pellny, T.K.6    Verrier, P.J.7    Foyer, C.H.8
  • 233
    • 49449109504 scopus 로고    scopus 로고
    • The multiple functions of the thiol-based electron flow pathways of Escherichia coli: Eternal concepts revisited
    • Vlamis-Gardikas A. The multiple functions of the thiol-based electron flow pathways of Escherichia coli: Eternal concepts revisited. Biochim Biophys Acta 1780: 1170-1200, 2008.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 1170-1200
    • Vlamis-Gardikas, A.1
  • 234
    • 45249092528 scopus 로고    scopus 로고
    • Knockout of major leaf ferredoxin reveals new redox-regulatory adaptations in Arabidopsis thaliana
    • DOI 10.1111/j.1399-3054.2008.01112.x
    • Voss I, Koelmann M, Wojtera J, Holtgrefe S, Kitzmann C, Backhausen JE, and Scheibe R. Knockout of major leaf ferredoxin reveals new redox-regulatory adaptations in Arabidopsis thaliana. Physiol Plant 3: 584-598, 2008. (Pubitemid 351841680)
    • (2008) Physiologia Plantarum , vol.133 , Issue.3 , pp. 584-598
    • Voss, I.1    Koelmann, M.2    Wojtera, J.3    Holtgrefe, S.4    Kitzmann, C.5    Backhausen, J.E.6    Scheibe, R.7
  • 235
    • 12744268500 scopus 로고    scopus 로고
    • Differential targeting of GSH1 and GSH2 is achieved by multiple transcription initiation: Implications for the compartmentation of glutathione biosynthesis in the Brassicaceae
    • Wachter A, Wolf S, Steininger H, Bogs J, and Rausch T. Differential targeting of GSH1 and GSH2 is achieved by multiple transcription initiation: implications for the compartmentation of glutathione biosynthesis in the Brassicaceae. Plant J 41: 15-30, 2005.
    • (2005) Plant J , vol.41 , pp. 15-30
    • Wachter, A.1    Wolf, S.2    Steininger, H.3    Bogs, J.4    Rausch, T.5
  • 236
    • 65249163613 scopus 로고    scopus 로고
    • Conserved functions of Arabidopsis and rice CC-type glutaredoxins in flower development and pathogen response
    • Wang Z, Xing S, Birkenbihl RP, and Zachgo S. Conserved functions of Arabidopsis and rice CC-type glutaredoxins in flower development and pathogen response. Mol Plant 2: 323-335, 2009.
    • (2009) Mol Plant , vol.2 , pp. 323-335
    • Wang, Z.1    Xing, S.2    Birkenbihl, R.P.3    Zachgo, S.4
  • 237
    • 0030822030 scopus 로고    scopus 로고
    • Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase
    • DOI 10.1074/jbc.272.43.26985
    • Wenderoth I, Scheibe R, and von Schaewen A. Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase. J Biol Chem 272: 26985-26990, 1997. (Pubitemid 27452652)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.43 , pp. 26985-26990
    • Wenderoth, I.1    Scheibe, R.2    Von Schaewen, A.3
  • 239
    • 0034695550 scopus 로고    scopus 로고
    • Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-κB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain
    • DOI 10.1074/jbc.275.3.1902
    • Witte S, Villalba M, Bi K, Liu Y, Isakov N, and Altman A. Inhibition of the c-Jun N-terminal kinase/AP-1 and NFkappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain. J Biol Chem 275: 1902-1909, 2000. (Pubitemid 30060815)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.3 , pp. 1902-1909
    • Witte, S.1    Villalba, M.2    Bi, K.3    Liu, Y.4    Isakov, N.5    Altman, A.6
  • 240
    • 0017336797 scopus 로고
    • Thioredoxin and glutathione regulate photosynthesis in chloroplasts
    • Wolosiuk RA and Buchanan BB. Thioredoxin and glutathione regulate photosynthesis in chloroplasts. Nature 266: 565-567, 1977. (Pubitemid 8079253)
    • (1977) Nature , vol.266 , Issue.5602 , pp. 565-567
    • Wolosiuk, R.A.1    Buchanan, B.B.2
  • 242
    • 0037628370 scopus 로고    scopus 로고
    • Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics
    • DOI 10.1016/S0014-5793(03)00696-3
    • Wong JH, Balmer Y, Cai N, Tanaka CK, Vensel WH, Hurkman WJ, and Buchanan BB. Unraveling thioredoxinlinked metabolic processes of cereal starchy endosperm using proteomics. FEBS Lett 547: 151-156, 2003. (Pubitemid 36829396)
    • (2003) FEBS Letters , vol.547 , Issue.1-3 , 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
  • 243
    • 3242791842 scopus 로고    scopus 로고
    • Thioredoxin targets of developing wheat seeds identified by complementary proteomic approaches
    • DOI 10.1016/j.phytochem.2004.05.010, PII S0031942204002262
    • Wong JH, Cai N, Balmer Y, Tanaka CK, Vensel WH, Hurkman WJ, and Buchanan BB. Thioredoxin targets of developing wheat seeds identified by complementary proteomic approaches. Phytochemistry 65: 1629-1640, 2004. (Pubitemid 38969943)
    • (2004) Phytochemistry , vol.65 , Issue.11 , pp. 1629-1640
    • Wong, J.H.1    Cai, N.2    Balmer, Y.3    Tanaka, C.K.4    Vensel, W.H.5    Hurkman, W.J.6    Buchanan, B.B.7
  • 244
    • 0028168801 scopus 로고
    • GSH1, which encodes gamma-glutamylcysteine synthetase, is a target gene for yAP-1 transcriptional regulation
    • Wu AL and Moye-Rowley WS. GSH1, which encodes gamma-glutamylcysteine synthetase, is a target gene for yAP-1 transcriptional regulation. Mol Cell Biol 14: 5832-5839, 1994.
    • (1994) Mol Cell Biol , vol.14 , pp. 5832-5839
    • Wu, A.L.1    Moye-Rowley, W.S.2
  • 245
    • 80054870283 scopus 로고    scopus 로고
    • Distinction of thioredoxin transnitrosylation and denitrosylation target proteins by the ICAT quantitative approach
    • Wu C, Parrott AM, Liu T, Jain MR, Yang Y, Sadoshima J, and Li H. Distinction of thioredoxin transnitrosylation and denitrosylation target proteins by the ICAT quantitative approach. J Proteomics 74: 2498-2509, 2011.
    • (2011) J Proteomics , vol.74 , pp. 2498-2509
    • Wu, C.1    Parrott, A.M.2    Liu, T.3    Jain, M.R.4    Yang, Y.5    Sadoshima, J.6    Li, H.7
  • 246
    • 17744384297 scopus 로고    scopus 로고
    • ROXY1, a member of the plant glutaredoxin family, is required for petal development in Arabidopsis thaliana
    • DOI 10.1242/dev.01725
    • Xing S, Rosso MG, and Zachgo S. ROXY1, a member of the plant glutaredoxin family, is required for petal development in Arabidopsis thaliana. Development 132: 1555-1565, 2005. (Pubitemid 40575857)
    • (2005) Development , vol.132 , Issue.7 , pp. 1555-1565
    • Xing, S.1    Rosso, M.G.2    Zachgo, S.3
  • 247
    • 41849125681 scopus 로고    scopus 로고
    • ROXY1 and ROXY2, two Arabidopsis glutaredoxin genes, are required for anther development
    • DOI 10.1111/j.1365-313X.2007.03375.x
    • Xing S and Zachgo S. ROXY1 and ROXY2, two Arabidopsis glutaredoxin genes, are required for anther development. Plant J 53: 790-801, 2008. (Pubitemid 351495871)
    • (2008) Plant Journal , vol.53 , Issue.5 , pp. 790-801
    • Xing, S.1    Zachgo, S.2
  • 248
    • 72249112935 scopus 로고    scopus 로고
    • Ternary protein complex of ferredoxin, ferredoxin: Thioredoxin reductase, and thioredoxin studied by paramagnetic NMR spectroscopy
    • Xu X, Schürmann P, Chung JS, Hass MA, Kim SK, Hirasawa M, Tripathy JN, Knaff DB, and Ubbink M. Ternary protein complex of ferredoxin, ferredoxin: thioredoxin reductase, and thioredoxin studied by paramagnetic NMR spectroscopy. J Am Chem Soc 131: 17576-17582, 2009.
    • (2009) J Am Chem Soc , vol.131 , pp. 17576-17582
    • Xu, X.1    Schürmann, P.2    Chung, J.S.3    Hass, M.A.4    Kim, S.K.5    Hirasawa, M.6    Tripathy, J.N.7    Knaff, D.B.8    Ubbink, M.9
  • 249
    • 1042279801 scopus 로고    scopus 로고
    • Target Proteins of the Cytosolic Thioredoxins in Arabidopsis thaliana
    • DOI 10.1093/pcp/pch019
    • Yamazaki D, Motohashi K, Kasama T, Hara Y, and Hisabori T. Target proteins of the cytosolic thioredoxins in Arabidopsis thaliana. Plant Cell Physiol 45: 18-27, 2004. (Pubitemid 38192330)
    • (2004) Plant and Cell Physiology , vol.45 , Issue.1 , pp. 18-27
    • Yamazaki, D.1    Motohashi, K.2    Kasama, T.3    Hara, Y.4    Hisabori, T.5
  • 252
    • 44049097906 scopus 로고    scopus 로고
    • Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii reveals the unique properties of a chloroplastic CGFS-type glutaredoxin
    • Zaffagnini M, Michelet L, Massot V, Trost P, and Lemaire SD. Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii reveals the unique properties of a chloroplastic CGFS-type glutaredoxin. J Biol Chem 283: 8868-8876, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 8868-8876
    • Zaffagnini, M.1    Michelet, L.2    Massot, V.3    Trost, P.4    Lemaire, S.D.5
  • 255
    • 55249112721 scopus 로고    scopus 로고
    • Subcellular immunocytochemical analysis detects the highest concentrations of glutathione in mitochondria and not in plastids
    • Zechmann B, Mauch F, Sticher L, and Müller M. Subcellular immunocytochemical analysis detects the highest concentrations of glutathione in mitochondria and not in plastids. J Exp Bot 59: 4017-4027, 2008.
    • (2008) J Exp Bot , vol.59 , pp. 4017-4027
    • Zechmann, B.1    Mauch, F.2    Sticher, L.3    Müller, M.4
  • 256
    • 79953103574 scopus 로고    scopus 로고
    • Glutathione synthesis is essential for pollen germination in vitro
    • Zechmann B, Koffler BE, and Russell SD. Glutathione synthesis is essential for pollen germination in vitro. BMC Plant Biol 11: 1-11, 2011.
    • (2011) BMC Plant Biol , vol.11 , pp. 1-11
    • Zechmann, B.1    Koffler, B.E.2    Russell, S.D.3
  • 257
    • 0842285650 scopus 로고    scopus 로고
    • A novel family of transporters mediating the transport of glutathione derivatives in plants
    • DOI 10.1104/pp.103.030940
    • Zhang MY, Bourbouloux A, Cagnac O, Srikanth CV, Rentsch D, Bachhawat AK, and Delrot S. A novel family of transporters mediating the transport of glutathione derivatives in plants. Plant Physiol 134: 482-491, 2004. (Pubitemid 38178719)
    • (2004) Plant Physiology , vol.134 , Issue.1 , pp. 482-491
    • Zhang, M.-Y.1    Bourbouloux, A.2    Cagnac, O.3    Srikanth, C.V.4    Rentsch, D.5    Bachhawat, A.K.6    Delrot, S.7
  • 258
    • 77956631441 scopus 로고    scopus 로고
    • Origin and diversification of land plant CC-type glutaredoxins
    • Ziemann M, Bhave M, and Zachgo S. Origin and diversification of land plant CC-type glutaredoxins. Genome Biol Evol 1: 265-277, 2009.
    • (2009) Genome Biol Evol , vol.1 , pp. 265-277
    • Ziemann, M.1    Bhave, M.2    Zachgo, S.3


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