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Volumn 72, Issue 3, 2009, Pages 452-474

Thioredoxin targets in plants: The first 30 years

Author keywords

Disulfide proteome; Proteomic approaches; Redox biology; Redox regulation; Thioredoxin; Thioredoxin targets

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; ACETYLORNITHINE AMINOTRANSFERASE; ACONITATE HYDRATASE; ACTIN; ADENOSINE KINASE; ADENOSINE KINASE 1; ADENOSYLHOMOCYSTEINASE; ADENYLATE KINASE; ADENYLOSUCCINATE SYNTHASE; ALANINE AMINOTRANSFERASE; ALCOHOL DEHYDROGENASE; ALDEHYDE OXIDASE; ALDEHYDE REDUCTASE; ALDOSE 1 EPIMERASE; ALLENE OXIDE CYCLASE; ALLYL ALCOHOL DEHYDROGENASE; AMINOTRANSFERASE; AMYLASE; ARGININE METHYLTRANSFERASE; ARGININOSUCCINATE LYASE; ASCORBATE PEROXIDASE; GLUCOSE 1 PHOSPHATE ADENYLYLTRANSFERASE; GLUTAREDOXIN; METHIONINE ADENOSYLTRANSFERASE; MUTANT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; OXIDOREDUCTASE; S ADENOSYLMETHIONINE SYNTHETASE 1; THIOREDOXIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 63549137242     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2008.12.002     Document Type: Review
Times cited : (251)

References (137)
  • 1
    • 42949151399 scopus 로고    scopus 로고
    • The ferredoxin/thioredoxin system of oxygenic photosynthesis
    • Schürmann P., and Buchanan B.B. The ferredoxin/thioredoxin system of oxygenic photosynthesis. Antioxid Redox Signal 10 (2008) 1235-1274
    • (2008) Antioxid Redox Signal , vol.10 , pp. 1235-1274
    • Schürmann, P.1    Buchanan, B.B.2
  • 2
    • 0014200334 scopus 로고
    • Ferredoxin-activated fructose diphosphatase in isolated chloroplasts
    • Buchanan B., Kalberer P., and Arnon D. Ferredoxin-activated fructose diphosphatase in isolated chloroplasts. Biochem Biophys Res Commun 29 (1967) 74-79
    • (1967) Biochem Biophys Res Commun , vol.29 , pp. 74-79
    • Buchanan, B.1    Kalberer, P.2    Arnon, D.3
  • 3
    • 33750604604 scopus 로고    scopus 로고
    • Aspects of the biological redox chemistry of cysteine: from simple redox responses to sophisticated signalling pathways
    • Jacob C., Knight I., and Winyard P. Aspects of the biological redox chemistry of cysteine: from simple redox responses to sophisticated signalling pathways. Biol Chem 387 (2006) 1385-1397
    • (2006) Biol Chem , vol.387 , pp. 1385-1397
    • Jacob, C.1    Knight, I.2    Winyard, P.3
  • 4
    • 36549031664 scopus 로고    scopus 로고
    • Identification of intra- and intermolecular disulphide bonding in the plant mitochondrial proteome by diagonal gel electrophoresis
    • Winger A.M., Taylor N., Heazlewood J., Day D., and Millar A. Identification of intra- and intermolecular disulphide bonding in the plant mitochondrial proteome by diagonal gel electrophoresis. Proteomics 7 (2007) 4158-4170
    • (2007) Proteomics , vol.7 , pp. 4158-4170
    • Winger, A.M.1    Taylor, N.2    Heazlewood, J.3    Day, D.4    Millar, A.5
  • 5
    • 0033582933 scopus 로고    scopus 로고
    • Bridge over troubled waters: sensing stress by disulfide bond formation
    • Aslund F., and Beckwith J. Bridge over troubled waters: sensing stress by disulfide bond formation. Cell 96 (1999) 751-753
    • (1999) Cell , vol.96 , pp. 751-753
    • Aslund, F.1    Beckwith, J.2
  • 7
    • 20344377809 scopus 로고    scopus 로고
    • Proteomic identification of S-nitrosylated proteins in Arabidopsis
    • Lindermayr C., Saalbach G., and Durner J. Proteomic identification of S-nitrosylated proteins in Arabidopsis. Plant Physiol 137 (2005) 921-930
    • (2005) Plant Physiol , vol.137 , pp. 921-930
    • Lindermayr, C.1    Saalbach, G.2    Durner, J.3
  • 8
    • 39149095741 scopus 로고    scopus 로고
    • Proteomic analysis of S-nitrosylated proteins in Arabidopsis thaliana undergoing hypersensitive response
    • Romero-Puertas M., Campostrini N., Mattè A., Righetti P., Perazzolli M., Zolla L., et al. Proteomic analysis of S-nitrosylated proteins in Arabidopsis thaliana undergoing hypersensitive response. Proteomics 8 (2008) 1459-1469
    • (2008) Proteomics , vol.8 , pp. 1459-1469
    • Romero-Puertas, M.1    Campostrini, N.2    Mattè, A.3    Righetti, P.4    Perazzolli, M.5    Zolla, L.6
  • 10
    • 20044367629 scopus 로고    scopus 로고
    • Redox regulation: a broadening horizon
    • Buchanan B.B., and Balmer Y. Redox regulation: a broadening horizon. Annu Rev Plant Biol 56 (2005) 187-220
    • (2005) Annu Rev Plant Biol , vol.56 , pp. 187-220
    • Buchanan, B.B.1    Balmer, Y.2
  • 11
    • 0021456845 scopus 로고
    • Conformational and functional similarities between glutaredoxin and thioredoxins
    • Eklund H., Cambillau C., Sjoberg B.M., Holmgren A., Jornvall H., Hoog J.O., et al. Conformational and functional similarities between glutaredoxin and thioredoxins. EMBO J 3 (1984) 1443-1449
    • (1984) EMBO J , vol.3 , pp. 1443-1449
    • Eklund, H.1    Cambillau, C.2    Sjoberg, B.M.3    Holmgren, A.4    Jornvall, H.5    Hoog, J.O.6
  • 12
    • 78651146370 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B
    • Laurent T.C., Moore E.C., and Reichard P. Enzymatic synthesis of deoxyribonucleotides. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B. J Biol Chem 239 (1964) 3436-3444
    • (1964) J Biol Chem , vol.239 , pp. 3436-3444
    • Laurent, T.C.1    Moore, E.C.2    Reichard, P.3
  • 13
    • 0008062361 scopus 로고
    • Escherichia coli thioredoxin: a subunit of bacteriophage T7 DNA polymerase
    • Mark D.F., and Richardson C.C. Escherichia coli thioredoxin: a subunit of bacteriophage T7 DNA polymerase. Proc Natl Acad Sci USA 73 (1976) 780-784
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 780-784
    • Mark, D.F.1    Richardson, C.C.2
  • 14
    • 0023035960 scopus 로고
    • The role of thioredoxin in filamentous phage assembly. Construction, isolation, and characterization of mutant thioredoxins
    • Russel M., and Model P. The role of thioredoxin in filamentous phage assembly. Construction, isolation, and characterization of mutant thioredoxins. J Biol Chem 261 (1986) 14997-15005
    • (1986) J Biol Chem , vol.261 , pp. 14997-15005
    • Russel, M.1    Model, P.2
  • 15
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • Saitoh M., Nishitoh H., Fujii M., Takeda K., Tobiume K., Sawada Y., et al. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J 17 (1998) 2596-2606
    • (1998) EMBO J , vol.17 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2    Fujii, M.3    Takeda, K.4    Tobiume, K.5    Sawada, Y.6
  • 16
    • 0036119804 scopus 로고    scopus 로고
    • Classification of plant thioredoxins by sequence similarity and intron position
    • Meyer Y., Vignols F., and Reichheld J.P. Classification of plant thioredoxins by sequence similarity and intron position. Methods Enzymol 347 (2002) 394-402
    • (2002) Methods Enzymol , vol.347 , pp. 394-402
    • Meyer, Y.1    Vignols, F.2    Reichheld, J.P.3
  • 17
  • 18
    • 0023641348 scopus 로고
    • Thioredoxin and NADP-thioredoxin reductase from cultured carrot cells
    • Johnson T.C., Cao R.Q., Kung J.E., and Buchanan B.B. Thioredoxin and NADP-thioredoxin reductase from cultured carrot cells. Planta 171 (1987) 321-331
    • (1987) Planta , vol.171 , pp. 321-331
    • Johnson, T.C.1    Cao, R.Q.2    Kung, J.E.3    Buchanan, B.B.4
  • 19
    • 0025726517 scopus 로고
    • Plant thioredoxin h: an animal-like thioredoxin occurring in multiple cell compartments
    • Marcus F., Chamberlain S.H., Chu C., Masiarz F.R., Shin S., Yee B.C., et al. Plant thioredoxin h: an animal-like thioredoxin occurring in multiple cell compartments. Arch Biochem Biophys 287 (1991) 195-198
    • (1991) Arch Biochem Biophys , vol.287 , pp. 195-198
    • Marcus, F.1    Chamberlain, S.H.2    Chu, C.3    Masiarz, F.R.4    Shin, S.5    Yee, B.C.6
  • 22
    • 5144234728 scopus 로고    scopus 로고
    • A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase
    • Gelhaye E., Rouhier N., Gérard J., Jolivet Y., Gualberto J., Navrot N., et al. A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase. Proc Natl Acad Sci USA 101 (2004) 14545-14550
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14545-14550
    • Gelhaye, E.1    Rouhier, N.2    Gérard, J.3    Jolivet, Y.4    Gualberto, J.5    Navrot, N.6
  • 27
    • 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 (1999) 307-316
    • (1999) Gene , vol.240 , pp. 307-316
    • Mestres-Ortega, D.1    Meyer, Y.2
  • 28
    • 0038393110 scopus 로고    scopus 로고
    • Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii
    • Lemaire S.D., Collin V., Keryer E., Quesada A., and Miginiac-Maslow M. Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii. FEBS Lett 543 (2003) 87-92
    • (2003) FEBS Lett , vol.543 , pp. 87-92
    • Lemaire, S.D.1    Collin, V.2    Keryer, E.3    Quesada, A.4    Miginiac-Maslow, M.5
  • 30
    • 11844285694 scopus 로고    scopus 로고
    • AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana
    • Reichheld J.-P., Meyer E., Khafif M., Bonnard G., and Meyer Y. AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana. FEBS Lett 579 (2005) 337-342
    • (2005) FEBS Lett , vol.579 , pp. 337-342
    • Reichheld, J.-P.1    Meyer, E.2    Khafif, M.3    Bonnard, G.4    Meyer, Y.5
  • 31
    • 6344235622 scopus 로고    scopus 로고
    • A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana
    • Serrato A.J., Perez-Ruiz J.M., Spinola M.C., and Cejudo F.J. A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana. J Biol Chem 279 (2004) 43821-43827
    • (2004) J Biol Chem , vol.279 , pp. 43821-43827
    • Serrato, A.J.1    Perez-Ruiz, J.M.2    Spinola, M.C.3    Cejudo, F.J.4
  • 32
    • 33749233825 scopus 로고    scopus 로고
    • Rice NTRC is a high-efficiency redox system for chloroplast protection against oxidative damage
    • Pérez-Ruiz J.M., Spínola M.C., Kirchsteiger K., Moreno J., Sahrawy M., and Cejudo F. Rice NTRC is a high-efficiency redox system for chloroplast protection against oxidative damage. Plant Cell 18 (2006) 2356-2368
    • (2006) Plant Cell , vol.18 , pp. 2356-2368
    • Pérez-Ruiz, J.M.1    Spínola, M.C.2    Kirchsteiger, K.3    Moreno, J.4    Sahrawy, M.5    Cejudo, F.6
  • 33
    • 34247270164 scopus 로고    scopus 로고
    • Unique properties of NADP-thioredoxin reductase C in legumes
    • Alkhalfioui F., Renard M., and Montrichard F. Unique properties of NADP-thioredoxin reductase C in legumes. J Exp Bot 58 (2007) 969-978
    • (2007) J Exp Bot , vol.58 , pp. 969-978
    • Alkhalfioui, F.1    Renard, M.2    Montrichard, F.3
  • 34
    • 0036413565 scopus 로고    scopus 로고
    • The ferredoxin/thioredoxin system: from discovery to molecular structures and beyond
    • Buchanan B., Schürmann P., Wolosiuk R., and Jacquot J. The ferredoxin/thioredoxin system: from discovery to molecular structures and beyond. Photosynth Res 73 (2002) 215-222
    • (2002) Photosynth Res , vol.73 , pp. 215-222
    • Buchanan, B.1    Schürmann, P.2    Wolosiuk, R.3    Jacquot, J.4
  • 36
    • 0017336797 scopus 로고
    • Thioredoxin and glutathione regulate photosynthesis in chloroplasts
    • Wolosiuk R., and Buchanan B. Thioredoxin and glutathione regulate photosynthesis in chloroplasts. Nature 266 (1977) 565-567
    • (1977) Nature , vol.266 , pp. 565-567
    • Wolosiuk, R.1    Buchanan, B.2
  • 37
    • 0000168597 scopus 로고
    • Activation of chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by the ferredoxin/thioredoxin system
    • Wolosiuk R.A., and Buchanan B.B. Activation of chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by the ferredoxin/thioredoxin system. Plant Physiol 61 (1978) 669-671
    • (1978) Plant Physiol , vol.61 , pp. 669-671
    • Wolosiuk, R.A.1    Buchanan, B.B.2
  • 38
    • 0000765807 scopus 로고
    • Role of light in the regulation of chloroplast enzymes
    • Buchanan B.B. Role of light in the regulation of chloroplast enzymes. Annu Rev Plant Physiol 31 (1980) 341-374
    • (1980) Annu Rev Plant Physiol , vol.31 , pp. 341-374
    • Buchanan, B.B.1
  • 39
    • 0017058765 scopus 로고
    • Identification of a protein factor involved in dithiothreitol activation of NADP malate dehydrogenase from French bean leaves
    • Jacquot J.-P., Vidal J.G., and P. Identification of a protein factor involved in dithiothreitol activation of NADP malate dehydrogenase from French bean leaves. FEBS Lett 71 (1976) 223-227
    • (1976) FEBS Lett , vol.71 , pp. 223-227
    • Jacquot, J.-P.1    Vidal, J.G.2    P3
  • 40
    • 0017669183 scopus 로고
    • Regulation of NADP-malate dehydrogenase by the light-actuated ferredoxin/thioredoxin system of chloroplasts
    • Wolosiuk R., Buchanan B., and Crawford N. Regulation of NADP-malate dehydrogenase by the light-actuated ferredoxin/thioredoxin system of chloroplasts. FEBS Lett 81 (1977) 253-258
    • (1977) FEBS Lett , vol.81 , pp. 253-258
    • Wolosiuk, R.1    Buchanan, B.2    Crawford, N.3
  • 41
    • 84981564988 scopus 로고
    • Influence of protein factors on activation of NADP-malate dehydrogenase by dithiothreitol
    • Vidal J., Jacquot J., Gadal P., and Vidal D. Influence of protein factors on activation of NADP-malate dehydrogenase by dithiothreitol. Physiol Plant 42 (1978) 307-314
    • (1978) Physiol Plant , vol.42 , pp. 307-314
    • Vidal, J.1    Jacquot, J.2    Gadal, P.3    Vidal, D.4
  • 42
    • 0019878627 scopus 로고
    • Dark modulation of NADP-dependent malate dehydrogenase and glucose-6-phosphate dehydrogenase in the chloroplast
    • Scheibe R., and Anderson L. Dark modulation of NADP-dependent malate dehydrogenase and glucose-6-phosphate dehydrogenase in the chloroplast. Biochim Biophys Acta 636 (1981) 58-64
    • (1981) Biochim Biophys Acta , vol.636 , pp. 58-64
    • Scheibe, R.1    Anderson, L.2
  • 43
    • 0008782539 scopus 로고
    • Activation of chloroplast ATPase by reduced thioredoxin
    • McKinney D.W., Buchanan B.B., and Wolosiuk R.A. Activation of chloroplast ATPase by reduced thioredoxin. Phytochemistry 17 (1978) 794-795
    • (1978) Phytochemistry , vol.17 , pp. 794-795
    • McKinney, D.W.1    Buchanan, B.B.2    Wolosiuk, R.A.3
  • 44
    • 49149147054 scopus 로고
    • Modulation of coupling factor ATPase activity in intact chloroplasts - the role of the thioredoxin system
    • Mills J., Mitchell P., and Schürmann P. Modulation of coupling factor ATPase activity in intact chloroplasts - the role of the thioredoxin system. FEBS letters 112 (1980) 173-177
    • (1980) FEBS letters , vol.112 , pp. 173-177
    • Mills, J.1    Mitchell, P.2    Schürmann, P.3
  • 45
    • 0030930312 scopus 로고    scopus 로고
    • Link between light and fatty acid synthesis: thioredoxin-linked reductive activation of plastidic acetyl-CoA carboxylase
    • Sasaki Y., Kozaki A., and Hatano M. Link between light and fatty acid synthesis: thioredoxin-linked reductive activation of plastidic acetyl-CoA carboxylase. Proc Nat Acad Sci USA 94 (1997) 11096-11101
    • (1997) Proc Nat Acad Sci USA , vol.94 , pp. 11096-11101
    • Sasaki, Y.1    Kozaki, A.2    Hatano, M.3
  • 46
    • 0033529948 scopus 로고    scopus 로고
    • Mechanism of light regulation of RubisCO: a specific role for the larger RubisCO activase isoform involving reductive activation by thioredoxin-f
    • Zhang N., and Portis Jr. A.R. Mechanism of light regulation of RubisCO: a specific role for the larger RubisCO activase isoform involving reductive activation by thioredoxin-f. Proc Nat Acad Sci USA 96 (1999) 9438-9443
    • (1999) Proc Nat Acad Sci USA , vol.96 , pp. 9438-9443
    • Zhang, N.1    Portis Jr., A.R.2
  • 47
    • 0033966939 scopus 로고    scopus 로고
    • Activation of the potato tuber ADP-glucose pyrophosphorylase by thioredoxin
    • Ballicora M.A., Frueauf J.B., Fu Y., Schürmann P., and Preiss J. Activation of the potato tuber ADP-glucose pyrophosphorylase by thioredoxin. J Biol Chem 275 (2000) 1315-1320
    • (2000) J Biol Chem , vol.275 , pp. 1315-1320
    • Ballicora, M.A.1    Frueauf, J.B.2    Fu, Y.3    Schürmann, P.4    Preiss, J.5
  • 48
    • 0031444519 scopus 로고    scopus 로고
    • Thioredoxins: structure and function in plant cells
    • Jacquot J.-P., Lancelin J.-M., and Meyer Y. Thioredoxins: structure and function in plant cells. New Phytol 136 (1997) 543-570
    • (1997) New Phytol , vol.136 , pp. 543-570
    • Jacquot, J.-P.1    Lancelin, J.-M.2    Meyer, Y.3
  • 49
    • 0032922625 scopus 로고    scopus 로고
    • Regulation of chloroplast enzyme activities by thioredoxins: activation or relief from inhibition?
    • Ruelland E., and Miginiac-Maslow M. Regulation of chloroplast enzyme activities by thioredoxins: activation or relief from inhibition?. Trends Plant Sci 4 (1999) 136-141
    • (1999) Trends Plant Sci , vol.4 , pp. 136-141
    • Ruelland, E.1    Miginiac-Maslow, M.2
  • 51
    • 0001015635 scopus 로고
    • Reduction of purothionin by the wheat seed thioredoxin system
    • Johnson T.C., Wada K., Buchanan B.B., and Holmgren A. Reduction of purothionin by the wheat seed thioredoxin system. Plant Physiol 85 (1987) 446-451
    • (1987) Plant Physiol , vol.85 , pp. 446-451
    • Johnson, T.C.1    Wada, K.2    Buchanan, B.B.3    Holmgren, A.4
  • 53
    • 0000524092 scopus 로고
    • Reduction of castor-seed 2S albumin by thioredoxin
    • Shin S., Wong J.H., Kobrehel K., and Buchanan B.B. Reduction of castor-seed 2S albumin by thioredoxin. Planta 189 (1993) 557-560
    • (1993) Planta , vol.189 , pp. 557-560
    • Shin, S.1    Wong, J.H.2    Kobrehel, K.3    Buchanan, B.B.4
  • 54
    • 0029839611 scopus 로고    scopus 로고
    • New evidence for a role for thioredoxin h in germination and seedling development
    • Lozano R.M., Wong J.H., Yee B.C., Peters A., Kobrehel K., and Buchanan B.B. New evidence for a role for thioredoxin h in germination and seedling development. Planta 200 (1996) 100-106
    • (1996) Planta , vol.200 , pp. 100-106
    • Lozano, R.M.1    Wong, J.H.2    Yee, B.C.3    Peters, A.4    Kobrehel, K.5    Buchanan, B.B.6
  • 55
    • 0034838039 scopus 로고    scopus 로고
    • Redox changes accompanying the degradation of seed storage proteins in germinating rice
    • Yano H., Wong J.H., Cho M.J., and Buchanan B.B. Redox changes accompanying the degradation of seed storage proteins in germinating rice. Plant Cell Physiol 42 (2001) 879-883
    • (2001) Plant Cell Physiol , vol.42 , pp. 879-883
    • Yano, H.1    Wong, J.H.2    Cho, M.J.3    Buchanan, B.B.4
  • 56
    • 0029928068 scopus 로고    scopus 로고
    • Thiocalsin: a thioredoxin-linked, substrate-specific protease dependent on calcium
    • Besse I., Wong J.H., Kobrehel K., and Buchanan B.B. Thiocalsin: a thioredoxin-linked, substrate-specific protease dependent on calcium. Proc Nat Acad Sci USA 93 (1996) 3169-3175
    • (1996) Proc Nat Acad Sci USA , vol.93 , pp. 3169-3175
    • Besse, I.1    Wong, J.H.2    Kobrehel, K.3    Buchanan, B.B.4
  • 57
    • 0025944354 scopus 로고
    • Role of the NADP/thioredoxin system in the reduction of α-amylase and trypsin inhibitor proteins
    • Kobrehel K., Yee B.C., and Buchanan B.B. Role of the NADP/thioredoxin system in the reduction of α-amylase and trypsin inhibitor proteins. J Biol Chem 266 (1991) 16135-16140
    • (1991) J Biol Chem , vol.266 , pp. 16135-16140
    • Kobrehel, K.1    Yee, B.C.2    Buchanan, B.B.3
  • 58
    • 0000579043 scopus 로고
    • Effect of thioredoxin-linked reduction on the activity and stability of the Kunitz and Bowman-Birk soybean inhibitor proteins
    • Jiao J.-A., Yee B.C., Kobrehel K., and Buchanan B.B. Effect of thioredoxin-linked reduction on the activity and stability of the Kunitz and Bowman-Birk soybean inhibitor proteins. J Agric Food Chem 40 (1992) 2333-2336
    • (1992) J Agric Food Chem , vol.40 , pp. 2333-2336
    • Jiao, J.-A.1    Yee, B.C.2    Kobrehel, K.3    Buchanan, B.B.4
  • 59
    • 0027143431 scopus 로고
    • Thioredoxin-linked changes in regulatory properties of barley α-amylase/subtilisin inhibitor protein
    • Jiao J., Yee B.C., Wong J.H., Kobrehel K., and Buchanan B.B. Thioredoxin-linked changes in regulatory properties of barley α-amylase/subtilisin inhibitor protein. Plant Physiol Biochem 31 (1993) 799-804
    • (1993) Plant Physiol Biochem , vol.31 , pp. 799-804
    • Jiao, J.1    Yee, B.C.2    Wong, J.H.3    Kobrehel, K.4    Buchanan, B.B.5
  • 60
    • 0008581550 scopus 로고
    • Thioredoxin-dependent deinhibition of pullulanase of barley malt by inactivation of a specific inhibitor protein
    • Wong J., Jiao J.-A., Kobrehel K., and Buchanan B. Thioredoxin-dependent deinhibition of pullulanase of barley malt by inactivation of a specific inhibitor protein. Plant Physiol 108 (1995) 67
    • (1995) Plant Physiol , vol.108 , pp. 67
    • Wong, J.1    Jiao, J.-A.2    Kobrehel, K.3    Buchanan, B.4
  • 61
    • 0033428817 scopus 로고    scopus 로고
    • Overexpression of thioredoxin h leads to enhanced activity of starch debranching enzyme (pullulanase) in barley grain
    • Cho M.J., Wong J.H., Marx C., Jiang W., Lemaux P.G., and Buchanan B.B. Overexpression of thioredoxin h leads to enhanced activity of starch debranching enzyme (pullulanase) in barley grain. Proc Nat Acad Sci USA 96 (1999) 14641-14646
    • (1999) Proc Nat Acad Sci USA , vol.96 , pp. 14641-14646
    • Cho, M.J.1    Wong, J.H.2    Marx, C.3    Jiang, W.4    Lemaux, P.G.5    Buchanan, B.B.6
  • 62
    • 0037058928 scopus 로고    scopus 로고
    • Transgenic barley grain overexpressing thioredoxin shows evidence that the starchy endosperm communicates with the embryo and the aleurone
    • Wong J.H., Kim Y.-B., Ren P.-H., Cai N., Cho M.-J., Hedden P., et al. Transgenic barley grain overexpressing thioredoxin shows evidence that the starchy endosperm communicates with the embryo and the aleurone. Proc Nat Acad Sci USA 99 (2002) 16325-16330
    • (2002) Proc Nat Acad Sci USA , vol.99 , pp. 16325-16330
    • Wong, J.H.1    Kim, Y.-B.2    Ren, P.-H.3    Cai, N.4    Cho, M.-J.5    Hedden, P.6
  • 63
    • 0030237223 scopus 로고    scopus 로고
    • A self-fertile mutant of Phalaris produces an S protein with reduced thioredoxin activity
    • Li X., Nield J., Hayman D., and Langridge P. A self-fertile mutant of Phalaris produces an S protein with reduced thioredoxin activity. Plant J 10 (1996) 505-513
    • (1996) Plant J , vol.10 , pp. 505-513
    • Li, X.1    Nield, J.2    Hayman, D.3    Langridge, P.4
  • 64
    • 0030249317 scopus 로고    scopus 로고
    • Two members of the thioredoxin-h family interact with the kinase domain of a Brassica S locus receptor kinase
    • Bower M.S., Matias D.D., Fernandes-Carvalho E., Mazzurco M., Gu T., Rothstein S.J., et al. Two members of the thioredoxin-h family interact with the kinase domain of a Brassica S locus receptor kinase. Plant Cell 8 (1996) 1641-1650
    • (1996) Plant Cell , vol.8 , pp. 1641-1650
    • Bower, M.S.1    Matias, D.D.2    Fernandes-Carvalho, E.3    Mazzurco, M.4    Gu, T.5    Rothstein, S.J.6
  • 65
    • 0035826255 scopus 로고    scopus 로고
    • The S-locus receptor kinase is inhibited by thioredoxins and activated by pollen coat proteins
    • Cabrillac D., Cock J.M., Dumas C., and Gaude T. The S-locus receptor kinase is inhibited by thioredoxins and activated by pollen coat proteins. Nature 410 (2001) 220-223
    • (2001) Nature , vol.410 , pp. 220-223
    • Cabrillac, D.1    Cock, J.M.2    Dumas, C.3    Gaude, T.4
  • 66
    • 2942535848 scopus 로고    scopus 로고
    • CITRX thioredoxin interacts with the tomato Cf-9 resistance protein and negatively regulates defence
    • Rivas S., Rougon-Cardoso A., Smoker M., Schauser L., Yoshioka H., and Jones J.D. CITRX thioredoxin interacts with the tomato Cf-9 resistance protein and negatively regulates defence. EMBO J 22 (2004) 2156-2166
    • (2004) EMBO J , vol.22 , pp. 2156-2166
    • Rivas, S.1    Rougon-Cardoso, A.2    Smoker, M.3    Schauser, L.4    Yoshioka, H.5    Jones, J.D.6
  • 67
    • 33645000975 scopus 로고    scopus 로고
    • Induction of thioredoxin is required for nodule development to reduce reactive oxygen species levels in soybean roots
    • Lee M.-Y., Shin K.-H., Kim Y.-K., Suh J.-Y., Gu Y.-Y., Kim M.-R., et al. Induction of thioredoxin is required for nodule development to reduce reactive oxygen species levels in soybean roots. Plant Physiol 139 (2005) 1881-1889
    • (2005) Plant Physiol , vol.139 , pp. 1881-1889
    • Lee, M.-Y.1    Shin, K.-H.2    Kim, Y.-K.3    Suh, J.-Y.4    Gu, Y.-Y.5    Kim, M.-R.6
  • 68
    • 34250661741 scopus 로고    scopus 로고
    • Thioredoxin h5 is required for victorin sensitivity mediated by a CC-NBS-LRR gene in Arabidopsis
    • Sweat T.A., and Wolpert T.J. Thioredoxin h5 is required for victorin sensitivity mediated by a CC-NBS-LRR gene in Arabidopsis. Plant Cell 19 (2007) 673-687
    • (2007) Plant Cell , vol.19 , pp. 673-687
    • Sweat, T.A.1    Wolpert, T.J.2
  • 69
    • 0035836648 scopus 로고    scopus 로고
    • A strategy for the identification of proteins targeted by thioredoxin
    • Yano H., Wong J.H., Lee Y.M., Cho M.J., and Buchanan B.B. A strategy for the identification of proteins targeted by thioredoxin. Proc Nat Acad Sci USA 98 (2001) 4794-4799
    • (2001) Proc Nat Acad Sci USA , vol.98 , pp. 4794-4799
    • Yano, H.1    Wong, J.H.2    Lee, Y.M.3    Cho, M.J.4    Buchanan, B.B.5
  • 70
    • 0038662709 scopus 로고    scopus 로고
    • Thioredoxin and germinating barley: targets and protein redox changes
    • Marx C., Wong J.-H., and Buchanan B. Thioredoxin and germinating barley: targets and protein redox changes. Planta 216 (2003) 454-460
    • (2003) Planta , vol.216 , pp. 454-460
    • Marx, C.1    Wong, J.-H.2    Buchanan, B.3
  • 71
    • 0033959891 scopus 로고    scopus 로고
    • Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities
    • Trebish T., Levitan A., Sofer A., and Danon A. Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities. Mol Cell Biol (2000) 1116-1123
    • (2000) Mol Cell Biol , pp. 1116-1123
    • Trebish, T.1    Levitan, A.2    Sofer, A.3    Danon, A.4
  • 72
    • 0037628370 scopus 로고    scopus 로고
    • Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics
    • Wong J.H., Balmer Y., Cai N., Tanaka C.K., Vensel W.H., Hurkman W.J., et al. Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics. FEBS Letters 547 (2003) 151-156
    • (2003) FEBS Letters , vol.547 , pp. 151-156
    • Wong, J.H.1    Balmer, Y.2    Cai, N.3    Tanaka, C.K.4    Vensel, W.H.5    Hurkman, W.J.6
  • 73
    • 1642409412 scopus 로고    scopus 로고
    • Cy5 maleimide labelling for sensitive detection of free thiols in native protein extracts: identification of seed proteins targeted by barley thioredoxin h isoforms
    • Maeda K., Finnie C., and Svensson B. 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 (2004) 497-507
    • (2004) Biochem J , vol.378 , pp. 497-507
    • Maeda, K.1    Finnie, C.2    Svensson, B.3
  • 75
    • 61349103096 scopus 로고    scopus 로고
    • Identification of thioredoxin protein disulfide targets using a quantitative proteomics approach based on isotope-coded affinity tags
    • Hägglund P., Bunkenborg J., Maeda K., and Svensson B. Identification of thioredoxin protein disulfide targets using a quantitative proteomics approach based on isotope-coded affinity tags. J Proteome Res 7 (2008) 5270-5276
    • (2008) J Proteome Res , vol.7 , pp. 5270-5276
    • Hägglund, P.1    Bunkenborg, J.2    Maeda, K.3    Svensson, B.4
  • 76
    • 0019163962 scopus 로고
    • Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli
    • Kallis G.B., and Holmgren A. Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli. J Biol Chem 255 (1980) 10261-10265
    • (1980) J Biol Chem , vol.255 , pp. 10261-10265
    • Kallis, G.B.1    Holmgren, A.2
  • 77
    • 0029080757 scopus 로고
    • Mixed disulfide intermediates during the reduction of disulfides by Escherichia coli thioredoxin
    • Wynn R., Cocco M.J., and Richards F.M. Mixed disulfide intermediates during the reduction of disulfides by Escherichia coli thioredoxin. Biochemistry 34 (1995) 11807-11813
    • (1995) Biochemistry , vol.34 , pp. 11807-11813
    • Wynn, R.1    Cocco, M.J.2    Richards, F.M.3
  • 78
    • 0029644240 scopus 로고
    • Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF[kappa]B
    • Qin J., Clore G.M., Kennedy W.P., Huth J.R., and Gronenborn A.M. Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF[kappa]B. Structure 3 (1995) 289-297
    • (1995) Structure , vol.3 , pp. 289-297
    • Qin, J.1    Clore, G.M.2    Kennedy, W.P.3    Huth, J.R.4    Gronenborn, A.M.5
  • 79
    • 0030043399 scopus 로고    scopus 로고
    • The molecular pathway for the regulation of phosphoribulokinase by thioredoxin f
    • Brandes H.K., Larimer F.W., and Hartman F.C. The molecular pathway for the regulation of phosphoribulokinase by thioredoxin f. J Biol Chem 271 (1996) 3333-3335
    • (1996) J Biol Chem , vol.271 , pp. 3333-3335
    • Brandes, H.K.1    Larimer, F.W.2    Hartman, F.C.3
  • 80
    • 0035831133 scopus 로고    scopus 로고
    • Heterodimer formation between thioredoxin f and fructose 1,6-bisphosphatase from spinach chloroplasts
    • Balmer Y., and Schürmann P. Heterodimer formation between thioredoxin f and fructose 1,6-bisphosphatase from spinach chloroplasts. FEBS Letters 492 (2001) 58-61
    • (2001) FEBS Letters , vol.492 , pp. 58-61
    • Balmer, Y.1    Schürmann, P.2
  • 81
    • 0033538442 scopus 로고    scopus 로고
    • In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family
    • Verdoucq L., Vignols F., Jacquot J.P., Chartier Y., and Meyer Y. In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. J Biol Chem 274 (1999) 19714-19722
    • (1999) J Biol Chem , vol.274 , pp. 19714-19722
    • Verdoucq, L.1    Vignols, F.2    Jacquot, J.P.3    Chartier, Y.4    Meyer, Y.5
  • 82
    • 0035949574 scopus 로고    scopus 로고
    • Comprehensive survey of proteins targeted by chloroplast thioredoxin
    • Motohashi K., Kondoh A., Stumpp M.T., and Hisabori T. Comprehensive survey of proteins targeted by chloroplast thioredoxin. Proc Nat Acad Sci USA 98 (2001) 11224-11229
    • (2001) Proc Nat Acad Sci USA , vol.98 , pp. 11224-11229
    • Motohashi, K.1    Kondoh, A.2    Stumpp, M.T.3    Hisabori, T.4
  • 83
    • 0003446098 scopus 로고
    • A thioredoxin-mediated activation of glutamine synthetase and glutamate synthase in synchronous Chlorella sorokiniana
    • Tischner R., and Schmidt A. A thioredoxin-mediated activation of glutamine synthetase and glutamate synthase in synchronous Chlorella sorokiniana. Plant Physiol 70 (1982) 113-116
    • (1982) Plant Physiol , vol.70 , pp. 113-116
    • Tischner, R.1    Schmidt, A.2
  • 84
    • 0000886711 scopus 로고
    • Thioredoxin-linked activation of the chloroplast and cytosolic forms of Chlamydomonas reinhardtii glutamine synthase
    • Florencio F.J., Gadal P., and Buchanan B.B. Thioredoxin-linked activation of the chloroplast and cytosolic forms of Chlamydomonas reinhardtii glutamine synthase. Plant Physiol Biochem 31 (1993) 649-655
    • (1993) Plant Physiol Biochem , vol.31 , pp. 649-655
    • Florencio, F.J.1    Gadal, P.2    Buchanan, B.B.3
  • 87
    • 1642371610 scopus 로고    scopus 로고
    • Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts
    • Balmer Y., Koller A., Val G.D., Schürmann P., and Buchanan B.B. Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynth Res 79 (2004) 275-280
    • (2004) Photosynth Res , vol.79 , pp. 275-280
    • Balmer, Y.1    Koller, A.2    Val, G.D.3    Schürmann, P.4    Buchanan, B.B.5
  • 89
    • 0036157915 scopus 로고    scopus 로고
    • Isolation and characterization of a thioredoxin-dependent peroxidase from Chlamydomonas reinhardtii
    • Goyer A., Haslekas C., Miginiac-Maslow M., Klein U., Le Marechal P., Jacquot J.-P., et al. Isolation and characterization of a thioredoxin-dependent peroxidase from Chlamydomonas reinhardtii. Eur J Biochem 269 (2002) 272-282
    • (2002) Eur J Biochem , vol.269 , pp. 272-282
    • Goyer, A.1    Haslekas, C.2    Miginiac-Maslow, M.3    Klein, U.4    Le Marechal, P.5    Jacquot, J.-P.6
  • 90
    • 0346103649 scopus 로고    scopus 로고
    • Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different
    • Lindahl M., and Florencio F.J. Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different. Proc Nat Acad Sci USA 100 (2003) 16107-16112
    • (2003) Proc Nat Acad Sci USA , vol.100 , pp. 16107-16112
    • Lindahl, M.1    Florencio, F.J.2
  • 92
    • 12844253100 scopus 로고    scopus 로고
    • Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803
    • Hosoya-Matsuda N., Motohashi K., Yoshimura H., Nozaki A., Inoue K., Ohmori M., et al. Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803. J Biol Chem 280 (2005) 840-846
    • (2005) J Biol Chem , vol.280 , pp. 840-846
    • Hosoya-Matsuda, N.1    Motohashi, K.2    Yoshimura, H.3    Nozaki, A.4    Inoue, K.5    Ohmori, M.6
  • 93
    • 33748980307 scopus 로고    scopus 로고
    • Selecting thioredoxins for disulphide proteomics: target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp
    • Pérez-Pérez M.E., Florencio F., and Lindahl M. Selecting thioredoxins for disulphide proteomics: target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. Proteomics 6 (2006) S186--S195
    • (2006) Proteomics , vol.6
    • Pérez-Pérez, M.E.1    Florencio, F.2    Lindahl, M.3
  • 95
    • 0035983856 scopus 로고    scopus 로고
    • The plastidic 2-cysteine peroxiredoxin is a target for a thioredoxin involved in the protection of the photosynthetic apparatus against oxidative damage
    • Broin M., Cuine 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 (2002) 1417-1432
    • (2002) Plant Cell , vol.14 , pp. 1417-1432
    • Broin, M.1    Cuine, S.2    Eymery, F.3    Rey, P.4
  • 96
    • 12744274638 scopus 로고    scopus 로고
    • Analysis of the proteins targeted by CDSP32, a plastidic thioredoxin participating in oxidative stress responses
    • Rey P., Cuine S., Eymery F., Garin J., Court M., Jacquot J.-P., et al. Analysis of the proteins targeted by CDSP32, a plastidic thioredoxin participating in oxidative stress responses. Plant J 41 (2005) 31-42
    • (2005) Plant J , vol.41 , pp. 31-42
    • Rey, P.1    Cuine, S.2    Eymery, F.3    Garin, J.4    Court, M.5    Jacquot, J.-P.6
  • 97
    • 0033962438 scopus 로고    scopus 로고
    • Involvement of CDSP 32, a drought-induced thioredoxin, in the response to oxidative stress in potato plants
    • Broin M., Cuine S., Peltier G., and Rey P. Involvement of CDSP 32, a drought-induced thioredoxin, in the response to oxidative stress in potato plants. FEBS Letters 467 (2000) 245-248
    • (2000) FEBS Letters , vol.467 , pp. 245-248
    • Broin, M.1    Cuine, S.2    Peltier, G.3    Rey, P.4
  • 98
    • 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
    • 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 (2006) 35039-35047
    • (2006) J Biol Chem , vol.281 , pp. 35039-35047
    • Motohashi, K.1    Hisabori, T.2
  • 99
    • 0035209897 scopus 로고    scopus 로고
    • HCF164 encodes a thioredoxin-like protein involved in the biogenesis of the cytochrome b(6)f complex in Arabidopsis
    • Lennartz K., Plucken 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 13 (2001) 2539-2551
    • (2001) Plant Cell , vol.13 , pp. 2539-2551
    • Lennartz, K.1    Plucken, H.2    Seidler, A.3    Westhoff, P.4    Bechtold, N.5    Meierhoff, K.6
  • 100
    • 3242791842 scopus 로고    scopus 로고
    • Thioredoxin targets of developing wheat seeds identified by complementary proteomic approaches
    • Wong J.H., Cai N., Balmer Y., Tanaka C.K., Vensel W.H., Hurkman W.J., et al. Thioredoxin targets of developing wheat seeds identified by complementary proteomic approaches. Phytochemistry 65 (2004) 1629-1640
    • (2004) Phytochemistry , vol.65 , 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
  • 101
    • 63549117802 scopus 로고    scopus 로고
    • Bewley JD and Black M (1994), Second edition. Plenum Press, New York and London.
    • Bewley JD and Black M (1994), Vol. Second edition. Plenum Press, New York and London.
  • 102
    • 33646261644 scopus 로고    scopus 로고
    • Proteome of amyloplasts isolated from developing wheat endosperm presents evidence of broad metabolic capability
    • Balmer Y., Vensel W.H., DuPont F.M., Buchanan B.B., and Hurkman W.J. Proteome of amyloplasts isolated from developing wheat endosperm presents evidence of broad metabolic capability. J Exp Bot 57 (2006) 1591-1602
    • (2006) J Exp Bot , vol.57 , pp. 1591-1602
    • Balmer, Y.1    Vensel, W.H.2    DuPont, F.M.3    Buchanan, B.B.4    Hurkman, W.J.5
  • 103
    • 0036743460 scopus 로고    scopus 로고
    • Starch synthesis in potato tubers is regulated by post-translational redox modification of ADP-glucose pyrophosphorylase: a novel regulatory mechanism linking starch synthesis to the sucrose supply
    • Tiessen A., Hendriks J.H.M., Stitt M., Branscheid A., Gibon Y., Farre E.M., et al. Starch synthesis in potato tubers is regulated by post-translational redox modification of ADP-glucose pyrophosphorylase: a novel regulatory mechanism linking starch synthesis to the sucrose supply. Plant Cell 14 (2002) 2191-2213
    • (2002) Plant Cell , vol.14 , pp. 2191-2213
    • Tiessen, A.1    Hendriks, J.H.M.2    Stitt, M.3    Branscheid, A.4    Gibon, Y.5    Farre, E.M.6
  • 104
  • 105
    • 33845968455 scopus 로고    scopus 로고
    • Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin
    • Marchand C., Le Marechal P., Meyer Y., and Decottignies P. Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin. Proteomics 24 (2006) 6528-6537
    • (2006) Proteomics , vol.24 , pp. 6528-6537
    • Marchand, C.1    Le Marechal, P.2    Meyer, Y.3    Decottignies, P.4
  • 106
    • 34447130271 scopus 로고    scopus 로고
    • Thioredoxin-linked proteins are reduced during germination of seeds of Medicago truncatula
    • Alkhalfioui F., Renard M., Vensel W.H., Wong J.H., Tanaka C.K., Hurkman W.J., et al. Thioredoxin-linked proteins are reduced during germination of seeds of Medicago truncatula. Plant Physiol 144 (2007) 1559-1579
    • (2007) Plant Physiol , vol.144 , pp. 1559-1579
    • Alkhalfioui, F.1    Renard, M.2    Vensel, W.H.3    Wong, J.H.4    Tanaka, C.K.5    Hurkman, W.J.6
  • 108
    • 42449087319 scopus 로고    scopus 로고
    • Three thioredoxin targets in the inner envelope membrane of chloroplasts function in protein import and chlorophyll metabolism
    • Bartsch S., Monnet J., Selbach K., Quigley F., Gray J., von Wettstein D., et al. Three thioredoxin targets in the inner envelope membrane of chloroplasts function in protein import and chlorophyll metabolism. Proc Nat Acad Sci USA 105 (2008) 4933-4938
    • (2008) Proc Nat Acad Sci USA , vol.105 , pp. 4933-4938
    • Bartsch, S.1    Monnet, J.2    Selbach, K.3    Quigley, F.4    Gray, J.5    von Wettstein, D.6
  • 109
    • 36048943681 scopus 로고    scopus 로고
    • Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin
    • Mata-Cabana A., Florencio F., and Lindahl M. Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin. Proteomics 7 (2007) 3953-3963
    • (2007) Proteomics , vol.7 , pp. 3953-3963
    • Mata-Cabana, A.1    Florencio, F.2    Lindahl, M.3
  • 111
    • 45249097787 scopus 로고    scopus 로고
    • The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility
    • Ströher E., and Dietz K.J. The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility. Physiol Plant 133 (2008) 566-583
    • (2008) Physiol Plant , vol.133 , pp. 566-583
    • Ströher, E.1    Dietz, K.J.2
  • 112
    • 31344457323 scopus 로고    scopus 로고
    • Disulfide proteome yields a detailed understanding of redox regulations: a model study of thioredoxin-linked reactions in seed germination
    • Yano H., and Kuroda M. Disulfide proteome yields a detailed understanding of redox regulations: a model study of thioredoxin-linked reactions in seed germination. Proteomics 6 (2006) 294-300
    • (2006) Proteomics , vol.6 , pp. 294-300
    • Yano, H.1    Kuroda, M.2
  • 113
    • 14044257165 scopus 로고    scopus 로고
    • Protein thiol modifications visualized in vivo
    • Leichert L.I., and Jakob U. Protein thiol modifications visualized in vivo. PLoS Biol. 2 (2004) e333
    • (2004) PLoS Biol. , vol.2
    • Leichert, L.I.1    Jakob, U.2
  • 114
    • 33744543755 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae proteome of oxidized protein thiols: contrasted functions for the thioredoxin and glutathione pathways
    • Le Moan N., Clement G., Le Maout S., Tacnet F., and Toledano M.B. The Saccharomyces cerevisiae proteome of oxidized protein thiols: contrasted functions for the thioredoxin and glutathione pathways. J Biol Chem 281 (2006) 10420-10430
    • (2006) J Biol Chem , vol.281 , pp. 10420-10430
    • Le Moan, N.1    Clement, G.2    Le Maout, S.3    Tacnet, F.4    Toledano, M.B.5
  • 115
    • 63549133454 scopus 로고    scopus 로고
    • Protein-thiol oxidation, from single proteins to proteome-wide analyses
    • Hancock ed, Humana press. ISBN: 978-1-58829-842-3
    • N. Le Moan, F. Tacnet and M.B. Toledano. Protein-thiol oxidation, from single proteins to proteome-wide analyses. In: Redox-Mediated Signal Transduction 2009; 476. Hancock ed, Humana press. ISBN: 978-1-58829-842-3.
    • (2009) Redox-Mediated Signal Transduction , pp. 476
    • Le Moan, N.1    Tacnet, F.2    Toledano, M.B.3
  • 117
    • 1642363933 scopus 로고    scopus 로고
    • Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli
    • Kumar J.K., Tabor S., and Richardson C.C. Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli. Proc Natl Acad Sci U S A 101 (2004) 3759-3764
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 3759-3764
    • Kumar, J.K.1    Tabor, S.2    Richardson, C.C.3
  • 119
    • 0032539799 scopus 로고    scopus 로고
    • In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae
    • Mouaheb N., Thomas D., Verdoucq L., Monfort P., and Meyer Y. In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 95 (1998) 3312-3317
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 3312-3317
    • Mouaheb, N.1    Thomas, D.2    Verdoucq, L.3    Monfort, P.4    Meyer, Y.5
  • 120
    • 0035142197 scopus 로고    scopus 로고
    • Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin
    • Issakidis-Bourguet E., Mouaheb N., Meyer Y., and Miginiac-Maslow M. Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin. Plant J 25 (2001) 127-135
    • (2001) Plant J , vol.25 , pp. 127-135
    • Issakidis-Bourguet, E.1    Mouaheb, N.2    Meyer, Y.3    Miginiac-Maslow, M.4
  • 121
    • 28044457914 scopus 로고    scopus 로고
    • A yeast two-hybrid knockout strain to explore thioredoxin-interacting proteins in vivo
    • Vignols F., Brehelin C., Surdin-Kerjan Y., Thomas D., and Meyer Y. A yeast two-hybrid knockout strain to explore thioredoxin-interacting proteins in vivo. Proc Natl Acad Sci U S A 102 (2005) 16729-16734
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 16729-16734
    • Vignols, F.1    Brehelin, C.2    Surdin-Kerjan, Y.3    Thomas, D.4    Meyer, Y.5
  • 122
    • 33846845957 scopus 로고    scopus 로고
    • Identification of novel targets of cyanobacterial glutaredoxin
    • Li M., Yang Q., Zhang L., Li H., Cui Y., and Wu Q. Identification of novel targets of cyanobacterial glutaredoxin. Arch Biochem Biophys 458 (2007) 220-228
    • (2007) Arch Biochem Biophys , vol.458 , pp. 220-228
    • Li, M.1    Yang, Q.2    Zhang, L.3    Li, H.4    Cui, Y.5    Wu, Q.6
  • 123
    • 34547698762 scopus 로고    scopus 로고
    • Inactivation of thioredoxin reductases reveals a complex interplay between thioredoxin and glutathione pathways in Arabidopsis development
    • Reichheld J.-P., Khafif M., Riondet C., Droux M., Bonnard G., and Meyer Y. Inactivation of thioredoxin reductases reveals a complex interplay between thioredoxin and glutathione pathways in Arabidopsis development. Plant Cell 19 (2007) 1851-1865
    • (2007) Plant Cell , vol.19 , pp. 1851-1865
    • Reichheld, J.-P.1    Khafif, M.2    Riondet, C.3    Droux, M.4    Bonnard, G.5    Meyer, Y.6
  • 124
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae H.Z., Chung S.J., and Rhee S.G. Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 269 (1994) 27670-27678
    • (1994) J Biol Chem , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 125
    • 20044391221 scopus 로고    scopus 로고
    • Thioredoxin affinity chromatography: a useful method for further understanding the thioredoxin network
    • Hisabori T., Hara S., Fujii T., Yamazaki D., Hosoya-Matsuda N., and Motohashi K. Thioredoxin affinity chromatography: a useful method for further understanding the thioredoxin network. J Exp Bot 56 (2005) 1463-1468
    • (2005) J Exp Bot , vol.56 , pp. 1463-1468
    • Hisabori, T.1    Hara, S.2    Fujii, T.3    Yamazaki, D.4    Hosoya-Matsuda, N.5    Motohashi, K.6
  • 126
    • 0041856169 scopus 로고    scopus 로고
    • Chloroplast cyclophilin is a target protein of thioredoxin. Thiol modulation of the peptidyl-prolyl cis-trans isomerase activity
    • Motohashi K., Koyama F., Nakanishi Y., Ueoka-Nakanishi H., and Hisabori T. Chloroplast cyclophilin is a target protein of thioredoxin. Thiol modulation of the peptidyl-prolyl cis-trans isomerase activity. J Biol Chem 278 (2003) 31848-31852
    • (2003) J Biol Chem , vol.278 , pp. 31848-31852
    • Motohashi, K.1    Koyama, F.2    Nakanishi, Y.3    Ueoka-Nakanishi, H.4    Hisabori, T.5
  • 128
    • 33846393586 scopus 로고    scopus 로고
    • Structural basis for target protein recognition by the protein disulfide reductase thioredoxin
    • Maeda K., Hägglund P., Finnie C., Svensson B., and Henriksen A. Structural basis for target protein recognition by the protein disulfide reductase thioredoxin. Structure 14 (2006) 1701-1710
    • (2006) Structure , vol.14 , pp. 1701-1710
    • Maeda, K.1    Hägglund, P.2    Finnie, C.3    Svensson, B.4    Henriksen, A.5
  • 129
    • 17844411493 scopus 로고    scopus 로고
    • Identification of thioredoxin h-reducible disulphides in proteomes by differential labelling of cysteines: insight into recognition and regulation of proteins in Barley seeds by thioredoxin h
    • Maeda K., Finnie C., and Svensson B. Identification of thioredoxin h-reducible disulphides in proteomes by differential labelling of cysteines: insight into recognition and regulation of proteins in Barley seeds by thioredoxin h. Proteomics 5 (2005) 1634-1644
    • (2005) Proteomics , vol.5 , pp. 1634-1644
    • Maeda, K.1    Finnie, C.2    Svensson, B.3
  • 130
    • 0030041167 scopus 로고    scopus 로고
    • Purification and characterization of α-amylase from poplar leaves
    • Witt W., and Sauter J. Purification and characterization of α-amylase from poplar leaves. Phytochemistry 41 (1996) 365-372
    • (1996) Phytochemistry , vol.41 , pp. 365-372
    • Witt, W.1    Sauter, J.2
  • 131
    • 21644460772 scopus 로고
    • Light and thiol activation of maize leaf glycerate kinase: the stimulating effect of reduced thioredoxins and ATP
    • Kleczkowski L., and Randall D. Light and thiol activation of maize leaf glycerate kinase: the stimulating effect of reduced thioredoxins and ATP. Plant Physiol 79 (1985) 274-277
    • (1985) Plant Physiol , vol.79 , pp. 274-277
    • Kleczkowski, L.1    Randall, D.2
  • 132
    • 33749856059 scopus 로고    scopus 로고
    • Plant methionine sulfoxide reductase A and B multigenic families
    • Rouhier N., Vieira Dos Santos C., Tarrago L., and Rey P. Plant methionine sulfoxide reductase A and B multigenic families. Photosynth Res 89 (2006) 247-262
    • (2006) Photosynth Res , vol.89 , pp. 247-262
    • Rouhier, N.1    Vieira Dos Santos, C.2    Tarrago, L.3    Rey, P.4
  • 133
    • 0027175339 scopus 로고
    • Activation of oxidized cysteine proteinases by thioredoxin-mediated reduction in vitro
    • Part 2
    • Stephen A.G., Powls R., and Beynon R.J. Activation of oxidized cysteine proteinases by thioredoxin-mediated reduction in vitro. Biochem J 291 (1993) 345-347 Part 2
    • (1993) Biochem J , vol.291 , pp. 345-347
    • Stephen, A.G.1    Powls, R.2    Beynon, R.J.3
  • 134
    • 0542362307 scopus 로고
    • Chloroplast phenylalanine ammonia-lyase from spinach leaves
    • Nishizawa A., Wolosiuk R., and Buchanan B. Chloroplast phenylalanine ammonia-lyase from spinach leaves. Planta (1979) 7-12
    • (1979) Planta , pp. 7-12
    • Nishizawa, A.1    Wolosiuk, R.2    Buchanan, B.3
  • 135
    • 0035544109 scopus 로고    scopus 로고
    • Thioredoxin-mediated reductive activation of a protein kinase for the regulatory phosphorylation of C4-form phosphoenolpyruvate carboxylase from maize
    • Saze H., Ueno Y., Hisabori T., Hayashi H., and Izui K. Thioredoxin-mediated reductive activation of a protein kinase for the regulatory phosphorylation of C4-form phosphoenolpyruvate carboxylase from maize. Plant Cell Physiol 42 (2001) 1295-1302
    • (2001) Plant Cell Physiol , vol.42 , pp. 1295-1302
    • Saze, H.1    Ueno, Y.2    Hisabori, T.3    Hayashi, H.4    Izui, K.5
  • 136
    • 0020507081 scopus 로고
    • The isocitrate dehydrogenase from cyanobacteria
    • Papen H., Neuer G., Refaian M., and Bothe H. The isocitrate dehydrogenase from cyanobacteria. Arch Microbiol 134 (1983) 73-79
    • (1983) Arch Microbiol , vol.134 , pp. 73-79
    • Papen, H.1    Neuer, G.2    Refaian, M.3    Bothe, H.4
  • 137
    • 5544272099 scopus 로고
    • A factor-dependent sulfotransferase specific for 3′-phosphoadenosine-5′-phosphosulfate (PAPS) in the cyanobacterium Synechococcus 6301
    • Schmidt A., and Christen U. A factor-dependent sulfotransferase specific for 3′-phosphoadenosine-5′-phosphosulfate (PAPS) in the cyanobacterium Synechococcus 6301. Planta 140 (1978) 239-244
    • (1978) Planta , vol.140 , pp. 239-244
    • Schmidt, A.1    Christen, U.2


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