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Volumn , Issue , 2007, Pages 25-52

Plant Thiol Enzymes and Thiol Homestasis in Relation to Thiol-dependent Redox Regulation and Oxidative Stress

Author keywords

Chloroplast; Oxidative stress; Plant thiol enzymes; Proteins; Sulfur

Indexed keywords


EID: 27644516893     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470988565.ch2     Document Type: Chapter
Times cited : (23)

References (113)
  • 1
    • 0028388161 scopus 로고
    • Transcripts encoding an oleosin and a dormancy-related protein are present in both the aleurone layer and the embryo of developing barley (Hordeum vulgare L.) seeds
    • Aalen, R.B., Opsahl-Fernstad, H.G., Linnestad, C. and Olsen, O.A. (1994) 'Transcripts encoding an oleosin and a dormancy-related protein are present in both the aleurone layer and the embryo of developing barley (Hordeum vulgare L.) seeds', The Plant Journal 5, 385-396.
    • (1994) The Plant Journal , vol.5 , pp. 385-396
    • Aalen, R.B.1    Opsahl-Fernstad, H.G.2    Linnestad, C.3    Olsen, O.A.4
  • 2
    • 0030695902 scopus 로고    scopus 로고
    • Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria
    • Åslund, F., Berndt, K.D. and Holmgren, A. (1997) 'Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria', Journal of Biological Chemistry 272, 30780-30786.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 30780-30786
    • Åslund, F.1    Berndt, K.D.2    Holmgren, A.3
  • 3
    • 0028061437 scopus 로고
    • Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant
    • Åslund, F., Ehn, B., Miranda-Vizuete, A., Pueyo, C. and Holmgren, A. (1994) 'Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant', Proceedings of the National Academy of Sciences USA 91, 9813-9817.
    • (1994) Proceedings of the National Academy of Sciences USA , vol.91 , pp. 9813-9817
    • Åslund, F.1    Ehn, B.2    Miranda-Vizuete, A.3    Pueyo, C.4    Holmgren, A.5
  • 4
    • 0029924163 scopus 로고    scopus 로고
    • Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis
    • Åslund, F., Nordstrand, K., Berndt, K.D. et al. (1996) 'Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis', Journal of Biological Chemistry 271, 6736-6745.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 6736-6745
    • Åslund, F.1    Nordstrand, K.2    Berndt, K.D.3
  • 5
    • 0031194690 scopus 로고    scopus 로고
    • The plant 2-Cys peroxiredoxin BAS1 is a nuclear-encoded chloroplast protein: its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants
    • Baier, M. and Dietz, K.J. (1997) 'The plant 2-Cys peroxiredoxin BAS1 is a nuclear-encoded chloroplast protein: its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants', The Plant Journal 12, 179-190.
    • (1997) The Plant Journal , vol.12 , pp. 179-190
    • Baier, M.1    Dietz, K.J.2
  • 6
    • 0033117456 scopus 로고    scopus 로고
    • Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis. Evidence from transgenic Arabidopsis
    • Baier, M. and Dietz, K.J. (1999) 'Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis. Evidence from transgenic Arabidopsis', Plant Physiology 119, 1407-1414.
    • (1999) Plant Physiology , vol.119 , pp. 1407-1414
    • Baier, M.1    Dietz, K.J.2
  • 7
    • 0033788736 scopus 로고    scopus 로고
    • Antisense suppression of 2-Cys peroxiredoxin in Arabidopsis specifically enhances the activities and expression of enzymes associated with ascorbate metabolism but not glutathione metabolism
    • Baier, M., Noctor, G., Foyer, C.H. and Dietz, K.J. (2000) 'Antisense suppression of 2-Cys peroxiredoxin in Arabidopsis specifically enhances the activities and expression of enzymes associated with ascorbate metabolism but not glutathione metabolism', Plant Physiology 124, 823-832.
    • (2000) Plant Physiology , vol.124 , pp. 823-832
    • Baier, M.1    Noctor, G.2    Foyer, C.H.3    Dietz, K.J.4
  • 8
    • 4644371980 scopus 로고    scopus 로고
    • The photosynthetic electron transport and ABA balance 2-Cys peroxiredoxin A promoter activity
    • Baier, M., Ströher, E. and Dietz, K.J. (2004) 'The photosynthetic electron transport and ABA balance 2-Cys peroxiredoxin A promoter activity', Plant Cell Physiology 45(8), 997-1006.
    • (2004) Plant Cell Physiology , vol.45 , Issue.8 , pp. 997-1006
    • Baier, M.1    Ströher, E.2    Dietz, K.J.3
  • 9
    • 1642371610 scopus 로고    scopus 로고
    • Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts
    • Balmer,Y., Koller, A., del Val, G., Schürmann, P. and Buchanan, B. (2004a) 'Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts', Photosynthesis Research 79, 275-280.
    • (2004) Photosynthesis Research , vol.79 , pp. 275-280
    • Balmer, Y.1    Koller, A.2    del Val, G.3    Schürmann, P.4    Buchanan, B.5
  • 10
    • 10744230621 scopus 로고    scopus 로고
    • Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria
    • Balmer,Y.,Vensel,W.H., Tanaka, C.K. et al. (2004b) 'Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria', Proceedings of the National Academy of Sciences USA 101, 2642-2647.
    • (2004) Proceedings of the National Academy of Sciences USA , vol.101 , pp. 2642-2647
    • Balmer, Y.1    Vensel, W.H.2    Tanaka, C.K.3
  • 11
    • 0036302168 scopus 로고    scopus 로고
    • Plant thioredoxins: the multiplicity conundrum
    • Baumann, U. and Juttner, J. (2002) 'Plant thioredoxins: the multiplicity conundrum', Cellular Molecular Life Science 59, 1042-1057.
    • (2002) Cellular Molecular Life Science , vol.59 , pp. 1042-1057
    • Baumann, U.1    Juttner, J.2
  • 12
    • 0001514394 scopus 로고
    • Glutathione metabolism in plants
    • in Sulfur Nutrition and Assimilation in Higher Plants (ed. L.J. De Kok, I. Stulen, H. Rennenberg, C. Brunold and W.E. Rauser), SPB Academic Publishing, The Hague
    • Bergmann, L. and Rennenberg, H. (1993) Glutathione metabolism in plants, in Sulfur Nutrition and Assimilation in Higher Plants (ed. L.J. De Kok, I. Stulen, H. Rennenberg, C. Brunold and W.E. Rauser), SPB Academic Publishing, The Hague, pp. 109-124.
    • (1993) , pp. 109-124
    • Bergmann, L.1    Rennenberg, H.2
  • 13
    • 0032493355 scopus 로고    scopus 로고
    • Glutaredoxin function for the carboxylterminal domain of the plant-type 5'-adenylylsulfate reductase
    • Bick, J.A., Åslund, F., Chen,Y.C. and Leustek, T. (1998) Glutaredoxin function for the carboxylterminal domain of the plant-type 5'-adenylylsulfate reductase', Proceedings of the National Academy of Sciences USA 95, 8404-8409.
    • (1998) Proceedings of the National Academy of Sciences USA , vol.95 , pp. 8404-8409
    • Bick, J.A.1    Åslund, F.2    Chen, Y.C.3    Leustek, T.4
  • 14
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
    • Biteau, B., Labarre, J. and Toledano, M.B. (2003) 'ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin', Nature 425, 980-984.
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 15
    • 12144286702 scopus 로고    scopus 로고
    • Cytosolic, mitochondrial thioredoxins and thioredoxin reductases in Arabidopsis thaliana
    • Bréhélin, C., Laloi, C., Setterdahl, A.T., Knaff, D.B. and Meyer, Y. (2004) 'Cytosolic, mitochondrial thioredoxins and thioredoxin reductases in Arabidopsis thaliana', Photosynthesis Research 79, 295-304.
    • (2004) Photosynthesis Research , vol.79 , pp. 295-304
    • Bréhélin, C.1    Laloi, C.2    Setterdahl, A.T.3    Knaff, D.B.4    Meyer, Y.5
  • 16
    • 0043011656 scopus 로고    scopus 로고
    • Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization, and activity
    • Bréhélin, C., Meyer, E.H., de Souris, J.P., Bonnard, G. and Meyer, Y. (2003) 'Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization, and activity', Plant Physiology 132, 2045-2057.
    • (2003) Plant Physiology , vol.132 , pp. 2045-2057
    • Bréhélin, C.1    Meyer, E.H.2    de Souris, J.P.3    Bonnard, G.4    Meyer, Y.5
  • 17
    • 84957958139 scopus 로고
    • Oxidation of thiols
    • in The Chemistry of Thiol Group, Part 2, Chapter 17 (ed. S. Patai), John Wiley & Sons, London
    • Capozzi, G. and Modena, G. (1974) Oxidation of thiols, in The Chemistry of Thiol Group, Part 2, Chapter 17 (ed. S. Patai), John Wiley & Sons, London, pp. 785-839.
    • (1974) , pp. 785-839
    • Capozzi, G.1    Modena, G.2
  • 18
    • 0000650850 scopus 로고    scopus 로고
    • Molecular cloning, expression, and functional characterization of a 2Cys-peroxiredoxin in Chinese cabbage
    • Cheong, N.E., Choi,Y.O., Lee, K.O. et al. (1999) 'Molecular cloning, expression, and functional characterization of a 2Cys-peroxiredoxin in Chinese cabbage', Plant Molecular Biology 40, 825-834.
    • (1999) Plant Molecular Biology , vol.40 , pp. 825-834
    • Cheong, N.E.1    Choi, Y.O.2    Lee, K.O.3
  • 19
    • 0033583798 scopus 로고    scopus 로고
    • Cloning and expression of a new isotype of the peroxiredoxin gene in Chinese cabbage and its comparison to 2-Cys peroxiredoxin isolated from the same plant
    • Choi, H.Y.O., Cheong, N.E., Lee, K.O. et al. (1999) 'Cloning and expression of a new isotype of the peroxiredoxin gene in Chinese cabbage and its comparison to 2-Cys peroxiredoxin isolated from the same plant', Biochemical and Biophysical Research Communication 258, 768-771.
    • (1999) Biochemical and Biophysical Research Communication , vol.258 , pp. 768-771
    • Choi, H.Y.O.1    Cheong, N.E.2    Lee, K.O.3
  • 20
    • 0037930284 scopus 로고    scopus 로고
    • The Arabidopsis plastidial thioredoxins: new functions and new insights into specificity
    • Collin, V., Issakidis-Bourguet, E., Marchand, C. et al. (2003) 'The Arabidopsis plastidial thioredoxins: new functions and new insights into specificity', Journal of Biological Chemistry 278, 23747-23752.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 23747-23752
    • Collin, V.1    Issakidis-Bourguet, E.2    Marchand, C.3
  • 21
    • 0034597012 scopus 로고    scopus 로고
    • H2O2 sensing through oxidation of the Yap1 transcription factor
    • Delaunay, A., Isnard, A.D. and Toledano, M.B. (2000) 'H2O2 sensing through oxidation of the Yap1 transcription factor', EMBO Journal 19, 5157-5166.
    • (2000) EMBO Journal , vol.19 , pp. 5157-5166
    • Delaunay, A.1    Isnard, A.D.2    Toledano, M.B.3
  • 22
    • 0037110454 scopus 로고    scopus 로고
    • A thiol peroxidase is an H2O2-acceptor and redox-transducer in gene activation
    • Delaunay, A., Pflieger, D., Barrault, M.B., Vinh, J. and Toledano, M. (2002) 'A thiol peroxidase is an H2O2-acceptor and redox-transducer in gene activation', Cell 111, 471-481.
    • (2002) Cell , vol.111 , pp. 471-481
    • Delaunay, A.1    Pflieger, D.2    Barrault, M.B.3    Vinh, J.4    Toledano, M.5
  • 24
    • 0345306681 scopus 로고    scopus 로고
    • Redox control, redox signaling and redox homeostasis in plant cells
    • Dietz, K.J. (2003b) 'Redox control, redox signaling and redox homeostasis in plant cells', International Review of Cytology 228, 141-193.
    • (2003) International Review of Cytology , vol.228 , pp. 141-193
    • Dietz, K.J.1
  • 25
    • 0036001082 scopus 로고    scopus 로고
    • The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation
    • Dietz, K.J., Horling, F., König, J. and Baier, M. (2002a) 'The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation', Journal of Experimental Botany 53, 1321-1329.
    • (2002) Journal of Experimental Botany , vol.53 , pp. 1321-1329
    • Dietz, K.J.1    Horling, F.2    König, J.3    Baier, M.4
  • 27
    • 1642450637 scopus 로고    scopus 로고
    • Redox regulation: an introduction
    • Dietz, K.J. and Scheibe, R. (2004) 'Redox regulation: an introduction', Physiologia Plantarum 120, 1-3.
    • (2004) Physiologia Plantarum , vol.120 , pp. 1-3
    • Dietz, K.J.1    Scheibe, R.2
  • 28
    • 33644781038 scopus 로고    scopus 로고
    • The role of peroxiredoxins in oxygenic photosynthesis of cyanobacteria and higher plants: peroxide detoxification or redox sensing?
    • in Photoprotection, Photoinhibition, Gene Regulation, and Environment (ed. B. Demmig-Adams, W. Adams and A. Mattoo), Kluwer Academic Press, in press
    • Dietz, K.J., Stork, T., Finkemeier, I. et al. (2005) The role of peroxiredoxins in oxygenic photosynthesis of cyanobacteria and higher plants: peroxide detoxification or redox sensing?, in Photoprotection, Photoinhibition, Gene Regulation, and Environment (ed. B. Demmig-Adams, W. Adams and A. Mattoo), Kluwer Academic Press, in press.
    • (2005)
    • Dietz, K.J.1    Stork, T.2    Finkemeier, I.3
  • 30
    • 0037163126 scopus 로고    scopus 로고
    • Functional divergence in the glutathione transferase superfamily in plants
    • Dixon, D.P., Davis, B.G. and Edwards, R. (2002) 'Functional divergence in the glutathione transferase superfamily in plants', Journal of Biological Chemistry 277, 30859-30869.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 30859-30869
    • Dixon, D.P.1    Davis, B.G.2    Edwards, R.3
  • 31
    • 0002422436 scopus 로고
    • Mineral metabolism
    • in Plant Biochemistry (ed. J. Bonner and J.E. Varner), Academic Press, London, Orlando
    • Epstein, E. (1965) Mineral metabolism, in Plant Biochemistry (ed. J. Bonner and J.E. Varner), Academic Press, London, Orlando, pp. 438-466.
    • (1965) , pp. 438-466
    • Epstein, E.1
  • 33
    • 84889289079 scopus 로고    scopus 로고
    • New insights into the antioxidant defence of mitochondria: the type II peroxiredoxin F (Prx IIF)
    • Finkemeier, I., Lamkemeyer, P., Kandlbinder, A., Baier, M. and Dietz, K.J. (2003b) 'New insights into the antioxidant defence of mitochondria: the type II peroxiredoxin F (Prx IIF)', Free Radical Research 37(Suppl.), 21-22.
    • (2003) Free Radical Research , vol.37 , Issue.SUPPL , pp. 21-22
    • Finkemeier, I.1    Lamkemeyer, P.2    Kandlbinder, A.3    Baier, M.4    Dietz, K.J.5
  • 34
    • 0141679346 scopus 로고    scopus 로고
    • Identity and functions of CxxC-derived motifs
    • Fomenko, D.E. and Gladyshev, V.N. (2003) 'Identity and functions of CxxC-derived motifs', Biochemistry 42, 11214-11225.
    • (2003) Biochemistry , vol.42 , pp. 11214-11225
    • Fomenko, D.E.1    Gladyshev, V.N.2
  • 35
    • 18344390036 scopus 로고    scopus 로고
    • Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes
    • Fratelli, M., Demol, H., Puype, M. et al. (2002) 'Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes', Proceedings of the National Academy of Sciences USA 99, 3505-3510.
    • (2002) Proceedings of the National Academy of Sciences USA , vol.99 , pp. 3505-3510
    • Fratelli, M.1    Demol, H.2    Puype, M.3
  • 36
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: building bridges in protein folding
    • Freedman, R.B., Hirst, T.R. and Tuite, M.F. (1994) 'Protein disulphide isomerase: building bridges in protein folding', Trends in Biochemical Science 19, 331-336.
    • (1994) Trends in Biochemical Science , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 37
    • 0036198797 scopus 로고    scopus 로고
    • Protein disulfide isomerases exploit synergy between catalytic and specific binding domains
    • Freedman, R.B., Klappa, P. and Ruddock, L.W. (2002) 'Protein disulfide isomerases exploit synergy between catalytic and specific binding domains', EMBO Reports 3(2), 136-140.
    • (2002) EMBO Reports , vol.3 , Issue.2 , pp. 136-140
    • Freedman, R.B.1    Klappa, P.2    Ruddock, L.W.3
  • 38
    • 0001669835 scopus 로고
    • Sulfur amino acids in plants
    • in The Biochemistry of Plants, Vol. 5 (ed. B.J. Miflin), Academic Press, New York
    • Giovanelli, J., Mudd, S.H. and Datko, A.H. (1980) Sulfur amino acids in plants, in The Biochemistry of Plants, Vol. 5 (ed. B.J. Miflin), Academic Press, New York, pp. 453-505.
    • (1980) , pp. 453-505
    • Giovanelli, J.1    Mudd, S.H.2    Datko, A.H.3
  • 39
    • 0001068301 scopus 로고
    • Phytochelatins, the heavy metal binding peptides from plants, are synthesized from glutathione by a specific γ-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase)
    • Grill, E., Löffler, S., Winnacker, E.L. and Zenk, M.H. (1989) 'Phytochelatins, the heavy metal binding peptides from plants, are synthesized from glutathione by a specific γ-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase)', Proceedings of the National Academy of Sciences USA 86, 6338-6342.
    • (1989) Proceedings of the National Academy of Sciences USA , vol.86 , pp. 6338-6342
    • Grill, E.1    Löffler, S.2    Winnacker, E.L.3    Zenk, M.H.4
  • 40
    • 0035844694 scopus 로고    scopus 로고
    • Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and x-ray crystallography
    • Harris, J.R., Schroder, E., Isupov, M.N. et al. (2001) 'Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and x-ray crystallography', Biochimica et Biophysica Acta 1547(2), 221-234.
    • (2001) Biochimica et Biophysica Acta , vol.1547 , Issue.2 , pp. 221-234
    • Harris, J.R.1    Schroder, E.2    Isupov, M.N.3
  • 41
    • 0346038797 scopus 로고    scopus 로고
    • ABI3 mediates expression of the peroxiredoxin antioxidant AtPER1 gene and induction by oxidative stress
    • Haslekas, C., Grini, P.E., Nordgard, S.H. et al. (2003a) 'ABI3 mediates expression of the peroxiredoxin antioxidant AtPER1 gene and induction by oxidative stress', Plant Molecular Biology 53(3), 313-326.
    • (2003) Plant Molecular Biology , vol.53 , Issue.3 , pp. 313-326
    • Haslekas, C.1    Grini, P.E.2    Nordgard, S.H.3
  • 42
    • 0344066300 scopus 로고    scopus 로고
    • Seed 1-cysteine peroxiredoxin antioxidants are not involved in dormancy, but contribute to inhibition of germination during stress
    • Haslekas, C., Viken, M.K., Grini, P.E. et al. (2003b) 'Seed 1-cysteine peroxiredoxin antioxidants are not involved in dormancy, but contribute to inhibition of germination during stress', Plant Physiology 133(3), 1148-1157.
    • (2003) Plant Physiology , vol.133 , Issue.3 , pp. 1148-1157
    • Haslekas, C.1    Viken, M.K.2    Grini, P.E.3
  • 45
    • 0035786229 scopus 로고    scopus 로고
    • Redox-regulation of the expression of the peroxidedetoxifying chloroplast 2-Cys peroxiredoxin in the liverwort Riccia fluitans
    • Horling, F., Baier, M. and Dietz, K.J. (2001) 'Redox-regulation of the expression of the peroxidedetoxifying chloroplast 2-Cys peroxiredoxin in the liverwort Riccia fluitans', Planta 214, 304-313.
    • (2001) Planta , vol.214 , pp. 304-313
    • Horling, F.1    Baier, M.2    Dietz, K.J.3
  • 46
    • 0036619345 scopus 로고    scopus 로고
    • Type II peroxiredoxin C, a member of the peroxiredoxin family of Arabidopsis thaliana: its expression and activity in comparison with other peroxiredoxins
    • Horling, F., König, J. and Dietz, K.J. (2002) 'Type II peroxiredoxin C, a member of the peroxiredoxin family of Arabidopsis thaliana: its expression and activity in comparison with other peroxiredoxins', Plant Physiology and Biochemistry 40(6-8), 491-499.
    • (2002) Plant Physiology and Biochemistry , vol.40 , Issue.6-8 , pp. 491-499
    • Horling, F.1    König, J.2    Dietz, K.J.3
  • 47
    • 0037252527 scopus 로고    scopus 로고
    • Divergent light-, ascorbate-and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis
    • Horling, F., Lamkemeyer, P., König, J. et al. (2003) 'Divergent light-, ascorbate-and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis', Plant Physiology 131, 317-325.
    • (2003) Plant Physiology , vol.131 , pp. 317-325
    • Horling, F.1    Lamkemeyer, P.2    König, J.3
  • 48
    • 0032066054 scopus 로고    scopus 로고
    • A common position-dependent mechanism controls cell-type patterning and GLABRA2 regulation in the root and hypocotyl epidermis of Arabidopsis
    • Hung, C.Y., Lin,Y., Zhang, M., Pollock, S., Marks, M.D. and Schiefelbein, J. (1998) 'A common position-dependent mechanism controls cell-type patterning and GLABRA2 regulation in the root and hypocotyl epidermis of Arabidopsis', Plant Physiology 117, 73-84.
    • (1998) Plant Physiology , vol.117 , pp. 73-84
    • Hung, C.Y.1    Lin, Y.2    Zhang, M.3    Pollock, S.4    Marks, M.D.5    Schiefelbein, J.6
  • 49
    • 0043199342 scopus 로고    scopus 로고
    • The sugar-metabolic enzymes aldolase and triosephosphate isomerase are targets of glutathionylation in Arabidopsis thaliana: detection using biotinylated glutathione
    • Ito, H., Iwabuchi, M. and Ogawa, K. (2003) 'The sugar-metabolic enzymes aldolase and triosephosphate isomerase are targets of glutathionylation in Arabidopsis thaliana: detection using biotinylated glutathione', Plant Cell Physiology 44(7), 655-660.
    • (2003) Plant Cell Physiology , vol.44 , Issue.7 , pp. 655-660
    • Ito, H.1    Iwabuchi, M.2    Ogawa, K.3
  • 50
    • 0031444519 scopus 로고    scopus 로고
    • Tansley review No. 94: Thioredoxins: structure and function in plant cells
    • Jacquot, J.P., Lancelin, J.M. and Meyer,Y. (1997) 'Tansley review No. 94: Thioredoxins: structure and function in plant cells', New Phytologist 136, 543-570.
    • (1997) New Phytologist , vol.136 , pp. 543-570
    • Jacquot, J.P.1    Lancelin, J.M.2    Meyer, Y.3
  • 51
    • 0028354036 scopus 로고
    • Arabidopsis thaliana NADPH thioredoxin reductase: cDNA characterization and expression of the recombinant protein in Escherichia coli
    • Jacquot, J.P., Riveramadrid, R., Marinho, P. et al. (1994) 'Arabidopsis thaliana NADPH thioredoxin reductase: cDNA characterization and expression of the recombinant protein in Escherichia coli', Journal of Molecular Biology 235(4), 1357-1363.
    • (1994) Journal of Molecular Biology , vol.235 , Issue.4 , pp. 1357-1363
    • Jacquot, J.P.1    Riveramadrid, R.2    Marinho, P.3
  • 52
    • 0034723165 scopus 로고    scopus 로고
    • Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin-comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/alkyl hydroperoxide peroxidaseC (AhpC) family
    • Jeong, W., Cha, M.K. and Kim, I.H. (2000) 'Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin-comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/alkyl hydroperoxide peroxidaseC (AhpC) family', Journal of Biological Chemistry 275, 2924-2930.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 2924-2930
    • Jeong, W.1    Cha, M.K.2    Kim, I.H.3
  • 53
    • 0037452951 scopus 로고    scopus 로고
    • Thiol regulation of the thylakoid electron transport chain-a missing link in the regulation of photosynthesis
    • Johnson, G.N. (2003) 'Thiol regulation of the thylakoid electron transport chain-a missing link in the regulation of photosynthesis', Biochemistry 42, 3040-3044.
    • (2003) Biochemistry , vol.42 , pp. 3040-3044
    • Johnson, G.N.1
  • 54
    • 1642424390 scopus 로고    scopus 로고
    • The antioxidant status of photosynthesizing leaves under nutrient deficiency: redox regulation, gene expression and antioxidant activity in Arabidopsis thaliana
    • Kandlbinder, A., Finkemeier, I.,Wormuth, D., Hanitzsch, M. and Dietz, K.J. (2004) 'The antioxidant status of photosynthesizing leaves under nutrient deficiency: redox regulation, gene expression and antioxidant activity in Arabidopsis thaliana', Physiologia Plantarum 120, 63-73.
    • (2004) Physiologia Plantarum , vol.120 , pp. 63-73
    • Kandlbinder, A.1    Finkemeier, I.2    Wormuth, D.3    Hanitzsch, M.4    Dietz, K.J.5
  • 55
    • 0031452439 scopus 로고    scopus 로고
    • Protein disulfide isomerase as a regulator of chloroplast translational activity
    • Kim, J. and Mayfield, S.P. (1997) 'Protein disulfide isomerase as a regulator of chloroplast translational activity', Science 278, 1954-1957.
    • (1997) Science , vol.278 , pp. 1954-1957
    • Kim, J.1    Mayfield, S.P.2
  • 56
    • 0037013155 scopus 로고    scopus 로고
    • OxyR: a molecular code for redox regulated signalling
    • Kim, S.O., Merchant, K., Nudelman, R. et al. (2002) 'OxyR: a molecular code for redox regulated signalling', Cell 109, 383-396.
    • (2002) Cell , vol.109 , pp. 383-396
    • Kim, S.O.1    Merchant, K.2    Nudelman, R.3
  • 57
    • 0034306117 scopus 로고    scopus 로고
    • A novel peroxiredoxin of the plant Sedum limeare is a homologue of Escherichia coli bacterioferritin comigratory protein (Bcp)
    • Kong, W., Shiota, S., Shi, Y., Nakayama, H. and Nakayama, K. (2000) 'A novel peroxiredoxin of the plant Sedum limeare is a homologue of Escherichia coli bacterioferritin comigratory protein (Bcp)', Biochemical Journal 351, 107-114.
    • (2000) Biochemical Journal , vol.351 , pp. 107-114
    • Kong, W.1    Shiota, S.2    Shi, Y.3    Nakayama, H.4    Nakayama, K.5
  • 58
    • 0037117488 scopus 로고    scopus 로고
    • The plant-specific function of 2-Cys peroxiredoxinmediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux
    • König, J., Baier, M., Horling, F. et al. (2002) 'The plant-specific function of 2-Cys peroxiredoxinmediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux', Proceedings of the National Academy of Sciences USA 99, 5738-5743.
    • (2002) Proceedings of the National Academy of Sciences USA , vol.99 , pp. 5738-5743
    • König, J.1    Baier, M.2    Horling, F.3
  • 59
    • 0042591328 scopus 로고    scopus 로고
    • Reaction mechanism of plant 2-Cys peroxiredoxin: role of the C terminus and the quaternary structure
    • König, J., Lotte, K., Plessow, R., Brockhinke, A., Baier, M. and Dietz, K.J. (2003) 'Reaction mechanism of plant 2-Cys peroxiredoxin: role of the C terminus and the quaternary structure', Journal of Biological Chemistry 278, 24409-24420.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 24409-24420
    • König, J.1    Lotte, K.2    Plessow, R.3    Brockhinke, A.4    Baier, M.5    Dietz, K.J.6
  • 60
    • 0037199969 scopus 로고    scopus 로고
    • Functional knockout of the adenosine 5'-phosphosulfate reductase genes revives an old route of sulfate assimilation
    • Koprivova, A., Meyer, A.J., Schween, G., Herschbach, C., Reski, R. and Kopriva, S. (2002) 'Functional knockout of the adenosine 5'-phosphosulfate reductase genes revives an old route of sulfate assimilation', Journal of Biological Chemistry 277, 32195-32201.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 32195-32201
    • Koprivova, A.1    Meyer, A.J.2    Schween, G.3    Herschbach, C.4    Reski, R.5    Kopriva, S.6
  • 61
    • 0034896388 scopus 로고    scopus 로고
    • Light-induced short-term adaptation mechanisms under redox control in the PS II-LHCII supercomplex: LHC II state transitions and PS II repair cycle
    • Kruse, O. (2001) 'Light-induced short-term adaptation mechanisms under redox control in the PS II-LHCII supercomplex: LHC II state transitions and PS II repair cycle', Naturwissenschaften 88(7), 284-292.
    • (2001) Naturwissenschaften , vol.88 , Issue.7 , pp. 284-292
    • Kruse, O.1
  • 63
    • 28544442038 scopus 로고    scopus 로고
    • The role of peroxiredoxin Q in the antioxidant defence system of the chloroplast
    • Lamkemeyer, P., Finkemeier, I., Kandlbinder, A., Baier, M. and Dietz, K.J. (2003) 'The role of peroxiredoxin Q in the antioxidant defence system of the chloroplast', Free Radical Research 37(Suppl.), 40.
    • (2003) Free Radical Research , vol.37 , Issue.SUPPL , pp. 40
    • Lamkemeyer, P.1    Finkemeier, I.2    Kandlbinder, A.3    Baier, M.4    Dietz, K.J.5
  • 64
    • 1342304902 scopus 로고    scopus 로고
    • Defining the plant disulfide proteome
    • Lee, K., Lee, J., Kim,Y. et al. (2004) 'Defining the plant disulfide proteome', Electrophoresis 25, 532-541.
    • (2004) Electrophoresis , vol.25 , pp. 532-541
    • Lee, K.1    Lee, J.2    Kim, Y.3
  • 65
    • 1642286959 scopus 로고    scopus 로고
    • The glutaredoxin family in oxygenic photosynthetic organisms
    • Lemaire, S.D. (2004) 'The glutaredoxin family in oxygenic photosynthetic organisms', Photosynthesis Research 79, 305-318.
    • (2004) Photosynthesis Research , vol.79 , pp. 305-318
    • Lemaire, S.D.1
  • 66
    • 0033583039 scopus 로고    scopus 로고
    • New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductase
    • Lillig, C.H., Prior, A., Schwenn, J.D. et al. (1999) 'New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductase', Journal of Biological Chemistry 274, 7695-7698.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 7695-7698
    • Lillig, C.H.1    Prior, A.2    Schwenn, J.D.3
  • 67
    • 0037296184 scopus 로고    scopus 로고
    • Redox regulation of chloroplast transcription
    • Link, G. (2003) 'Redox regulation of chloroplast transcription', Antioxidants and Redox Signaling 5, 79-88.
    • (2003) Antioxidants and Redox Signaling , vol.5 , pp. 79-88
    • Link, G.1
  • 68
    • 0030329947 scopus 로고    scopus 로고
    • Identification of a meristem L1 layerspecific gene in Arabidopsis that is expressed during embryonic pattern formation and defines a new class of homeobox genes
    • Lu, P., Porat, R., Nadeau, J.A. and O'Neill, S.D. (1996) 'Identification of a meristem L1 layerspecific gene in Arabidopsis that is expressed during embryonic pattern formation and defines a new class of homeobox genes', The Plant Cell 8, 2155-2168.
    • (1996) The Plant Cell , vol.8 , pp. 2155-2168
    • Lu, P.1    Porat, R.2    Nadeau, J.A.3    O'Neill, S.D.4
  • 70
    • 0029165589 scopus 로고
    • Thioredoxin-a fold for all reasons
    • Martin, J.L. (1995) 'Thioredoxin-a fold for all reasons', Structure 3, 245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 71
    • 0032735140 scopus 로고    scopus 로고
    • The Arabidopsis thaliana genome encodes at least four thioredoxin m and a new prokaryotic-like thioredoxin
    • Mestres-Ortega, D. and Meyer,Y. (1999) 'The Arabidopsis thaliana genome encodes at least four thioredoxin m and a new prokaryotic-like thioredoxin', Gene 240, 307-316.
    • (1999) Gene , vol.240 , pp. 307-316
    • Mestres-Ortega, D.1    Meyer, Y.2
  • 72
    • 0033214489 scopus 로고    scopus 로고
    • Plant thioredoxins and glutaredoxins: identity and putative roles
    • Meyer,Y.,Verdoucq, L. and Vignols, F. (1999) 'Plant thioredoxins and glutaredoxins: identity and putative roles', Trends in Plant Science 4, 388-394.
    • (1999) Trends in Plant Science , vol.4 , pp. 388-394
    • Meyer, Y.1    Verdoucq, L.2    Vignols, F.3
  • 73
  • 74
    • 0029142983 scopus 로고
    • Identification and localization of the first glutaredoxin in leaves of a higher plant
    • Morell, S., Follmann, H. and Häberlein, I. (1995) 'Identification and localization of the first glutaredoxin in leaves of a higher plant', FEBS Letters 369, 149-152.
    • (1995) FEBS Letters , vol.369 , pp. 149-152
    • Morell, S.1    Follmann, H.2    Häberlein, I.3
  • 76
    • 0032539799 scopus 로고    scopus 로고
    • In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae
    • Mouaheb, N., Thoma, D., Verdoucq, L., Monfort, P. and Meyer, Y. (1998) 'In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae', Proceedings of the National Academy of Sciences USA 95, 3312-3317.
    • (1998) Proceedings of the National Academy of Sciences USA , vol.95 , pp. 3312-3317
    • Mouaheb, N.1    Thoma, D.2    Verdoucq, L.3    Monfort, P.4    Meyer, Y.5
  • 77
    • 0036935750 scopus 로고    scopus 로고
    • A novel stress-inducible antioxidant enzyme identified in the resurrection plant Xerophyta viscosa Baker
    • Mowda, S.B., Thomson, J.A, Farrant, J.M. and Mundree, S.G. (2002) 'A novel stress-inducible antioxidant enzyme identified in the resurrection plant Xerophyta viscosa Baker', Planta 215, 716-726.
    • (2002) Planta , vol.215 , pp. 716-726
    • Mowda, S.B.1    Thomson, J.A.2    Farrant, J.M.3    Mundree, S.G.4
  • 80
    • 0035983613 scopus 로고    scopus 로고
    • Common components, networks, and pathways of crosstolerance to stress. The central role of "redox" and abscisic acid-mediated controls
    • Pastori, G.M. and Foyer, C.H. (2002) 'Common components, networks, and pathways of crosstolerance to stress. The central role of "redox" and abscisic acid-mediated controls', Plant Physiology 129, 460-468.
    • (2002) Plant Physiology , vol.129 , pp. 460-468
    • Pastori, G.M.1    Foyer, C.H.2
  • 81
    • 0037267882 scopus 로고    scopus 로고
    • Chloroplast redox signals: how photosynthesis controls its own genes
    • Pfannschmidt, T. (2003) 'Chloroplast redox signals: how photosynthesis controls its own genes', Trends in Plant Science 8, 33-41.
    • (2003) Trends in Plant Science , vol.8 , pp. 33-41
    • Pfannschmidt, T.1
  • 82
    • 0035367291 scopus 로고    scopus 로고
    • Distribution of protein disulphide isomerase in rat liver mitochondria
    • Rigobello, M.P., Donella-Deana, A., Cesaro, L. and Bindoli, A. (2001) 'Distribution of protein disulphide isomerase in rat liver mitochondria', Biochemical Journal 356, 567-570.
    • (2001) Biochemical Journal , vol.356 , pp. 567-570
    • Rigobello, M.P.1    Donella-Deana, A.2    Cesaro, L.3    Bindoli, A.4
  • 83
    • 1942501872 scopus 로고    scopus 로고
    • The Arabidopsis cyclophilin gene family
    • Romano, P,G.N., Horton, P. and Gray, J.E. (2004) 'The Arabidopsis cyclophilin gene family', Plant Physiology 134, 1268-1282.
    • (2004) Plant Physiology , vol.134 , pp. 1268-1282
    • Romano, P.G.N.1    Horton, P.2    Gray, J.E.3
  • 84
    • 1642465526 scopus 로고    scopus 로고
    • Active site mutagenesis and phospholipid hydroperoxide reductase activity of poplar type II peroxiredoxin
    • Rouhier, N., Gelhaye, E., Corbier, C. and Jacquot, J.P. (2004a) 'Active site mutagenesis and phospholipid hydroperoxide reductase activity of poplar type II peroxiredoxin', Physiologia Plantarum 120, 57-62.
    • (2004) Physiologia Plantarum , vol.120 , pp. 57-62
    • Rouhier, N.1    Gelhaye, E.2    Corbier, C.3    Jacquot, J.P.4
  • 85
    • 12144287638 scopus 로고    scopus 로고
    • Poplar peroxiredoxin Q: a thioredoxin-linked chloroplast antioxidant functional in pathogen defense
    • Rouhier, N., Gelhaye, E., Gualberto, J.M. et al. (2004b) 'Poplar peroxiredoxin Q: a thioredoxin-linked chloroplast antioxidant functional in pathogen defense', Plant Physiology 134, 1027-1038.
    • (2004) Plant Physiology , vol.134 , pp. 1027-1038
    • Rouhier, N.1    Gelhaye, E.2    Gualberto, J.M.3
  • 86
    • 84889438259 scopus 로고    scopus 로고
    • Identification of plant glutaredoxin targets
    • Antioxidants and Redox Signaling, in press
    • Rouhier, N., Gelhaye, E., Villarejo, A. et al. (2004c) 'Identification of plant glutaredoxin targets', Antioxidants and Redox Signaling, in press.
    • (2004)
    • Rouhier, N.1    Gelhaye, E.2    Villarejo, A.3
  • 87
    • 0035202123 scopus 로고    scopus 로고
    • Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor
    • Rouhier, N., Gelhaye, E., Sautiere, P.E. et al. (2001) 'Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor', Plant Physiology 127, 1299-1309.
    • (2001) Plant Physiology , vol.127 , pp. 1299-1309
    • Rouhier, N.1    Gelhaye, E.2    Sautiere, P.E.3
  • 88
    • 0036914442 scopus 로고    scopus 로고
    • Plant peroxiredoxins: alternative hydroperoxide scavenging enzymes
    • Rouhier, N. and Jacquot, J.P. (2002) 'Plant peroxiredoxins: alternative hydroperoxide scavenging enzymes', Photosynthesis Research 74, 259-268.
    • (2002) Photosynthesis Research , vol.74 , pp. 259-268
    • Rouhier, N.1    Jacquot, J.P.2
  • 90
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer, F.Q. and Buettner, G.R. (2001) 'Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple', Free Radicals in Biology and Medicine 30, 1191-1212.
    • (2001) Free Radicals in Biology and Medicine , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 91
    • 12044250534 scopus 로고
    • Redox modulation of chloroplast enzymes. A common principle for individual control
    • Scheibe, R. (1991) 'Redox modulation of chloroplast enzymes. A common principle for individual control', Plant Physiology 96, 1-3.
    • (1991) Plant Physiology , vol.96 , pp. 1-3
    • Scheibe, R.1
  • 92
    • 1642424402 scopus 로고    scopus 로고
    • Malate valves to balance cellular energy supply
    • Scheibe, R. (2004) 'Malate valves to balance cellular energy supply', Physiologia Plantarum 120(1), 21-26.
    • (2004) Physiologia Plantarum , vol.120 , Issue.1 , pp. 21-26
    • Scheibe, R.1
  • 94
    • 0004217575 scopus 로고
    • Biochemical Calculations
    • John Wiley, New York
    • Segel, I.H. (1976) Biochemical Calculations, John Wiley, New York.
    • (1976)
    • Segel, I.H.1
  • 95
  • 96
    • 0033166877 scopus 로고    scopus 로고
    • The dormancyrelated peroxiredoxin anti-oxidant, PER1, is localized to the nucleus of barley embryo and aleurone cells
    • Stacy, R.A.P., Nordeng, T.W., Culianez-Macia, F.A. and Aalen, R.B. (1999) 'The dormancyrelated peroxiredoxin anti-oxidant, PER1, is localized to the nucleus of barley embryo and aleurone cells', The Plant Journal 19(1), 1-8.
    • (1999) The Plant Journal , vol.19 , Issue.1 , pp. 1-8
    • Stacy, R.A.P.1    Nordeng, T.W.2    Culianez-Macia, F.A.3    Aalen, R.B.4
  • 97
    • 0025214474 scopus 로고
    • Transcriptional regulator of oxidative stressinducible genes; direct activation by oxidation
    • Storz, G., Tartaglia, L.A. and Ames, B.N. (1990) 'Transcriptional regulator of oxidative stressinducible genes; direct activation by oxidation', Science 248, 189-194.
    • (1990) Science , vol.248 , pp. 189-194
    • Storz, G.1    Tartaglia, L.A.2    Ames, B.N.3
  • 98
    • 0346003769 scopus 로고    scopus 로고
    • The impact of oxidative stress on Arabidopsis mitochondria
    • Sweetlove, L.J., Heazlewood, J.L., Herald, V. et al. (2002) 'The impact of oxidative stress on Arabidopsis mitochondria', The Plant Journal 32, 891-904.
    • (2002) The Plant Journal , vol.32 , pp. 891-904
    • Sweetlove, L.J.1    Heazlewood, J.L.2    Herald, V.3
  • 99
    • 1842376834 scopus 로고    scopus 로고
    • Cloning of the cDNA for glutaredoxin, an abundant sieve-tube exudate protein from Ricinus communis L. and characterization of the glutathione-dependent thiol-reduction system in sieve tubes
    • Szederkenyi, J., Komor, E. and Schobert, C. (1997) 'Cloning of the cDNA for glutaredoxin, an abundant sieve-tube exudate protein from Ricinus communis L. and characterization of the glutathione-dependent thiol-reduction system in sieve tubes', Planta 202, 349-356.
    • (1997) Planta , vol.202 , pp. 349-356
    • Szederkenyi, J.1    Komor, E.2    Schobert, C.3
  • 100
    • 0038491193 scopus 로고    scopus 로고
    • Biochemical characterization of yeast mitochondrial GRX5 monothiol glutaredoxin
    • Tamarit, J., Belli, G., Cabiscol, E., Herrero, E. and Ros, J. (2003) 'Biochemical characterization of yeast mitochondrial GRX5 monothiol glutaredoxin', Journal of Biological Chemistry 278, 25745-25751.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 25745-25751
    • Tamarit, J.1    Belli, G.2    Cabiscol, E.3    Herrero, E.4    Ros, J.5
  • 101
    • 0037309444 scopus 로고    scopus 로고
    • Co-induction of glutathione-S-transferases and multidrug resistance associated protein by xenobiotics in wheat
    • Theodoulou, F.L., Clark, I.M., He, X.L., Pallett, K.E., Cole, D.J. and Hallahan, D.L. (2003) 'Co-induction of glutathione-S-transferases and multidrug resistance associated protein by xenobiotics in wheat', Pest Management Science 59, 202-214.
    • (2003) Pest Management Science , vol.59 , pp. 202-214
    • Theodoulou, F.L.1    Clark, I.M.2    He, X.L.3    Pallett, K.E.4    Cole, D.J.5    Hallahan, D.L.6
  • 102
    • 0033959891 scopus 로고    scopus 로고
    • Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities
    • Trebitsh, T., Levitan, A., Sofer, A. and Danon, A. (2000) 'Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities', Molecular Cell Biology 20, 1116-1123.
    • (2000) Molecular Cell Biology , vol.20 , pp. 1116-1123
    • Trebitsh, T.1    Levitan, A.2    Sofer, A.3    Danon, A.4
  • 105
    • 1642384633 scopus 로고    scopus 로고
    • Ferredoxin: thioredoxin reductase: disulfide reduction catalyzed via novel site-specific [4Fe-4S]cluster chemistry
    • Walters, E.M. and Johnson, M.K. (2004) 'Ferredoxin: thioredoxin reductase: disulfide reduction catalyzed via novel site-specific [4Fe-4S]cluster chemistry', Photosynthesis Research 79, 249-264.
    • (2004) Photosynthesis Research , vol.79 , pp. 249-264
    • Walters, E.M.1    Johnson, M.K.2
  • 106
    • 1642547105 scopus 로고    scopus 로고
    • Regulation of redox homeostasis in the yeast Saccharomyces cerevisiae
    • Wheeler, G.L. and Grant, C.M. (2004) 'Regulation of redox homeostasis in the yeast Saccharomyces cerevisiae', Physiologia Plantarum 120, 12-20.
    • (2004) Physiologia Plantarum , vol.120 , pp. 12-20
    • Wheeler, G.L.1    Grant, C.M.2
  • 107
    • 0000957432 scopus 로고
    • Subcellular volumes and metabolite concentrations in barley leaves
    • Winter, H., Robinson, D.G. and Heldt, H.W. (1993) 'Subcellular volumes and metabolite concentrations in barley leaves', Planta 191(2), 180-190.
    • (1993) Planta , vol.191 , Issue.2 , pp. 180-190
    • Winter, H.1    Robinson, D.G.2    Heldt, H.W.3
  • 108
    • 0037197672 scopus 로고    scopus 로고
    • Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins
    • Wood, Z.A., Poole, L.B., Hantgan, R.R. and Karplus, P.A. (2002) 'Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins', Biochemistry 41, 5493-5504.
    • (2002) Biochemistry , vol.41 , pp. 5493-5504
    • Wood, Z.A.1    Poole, L.B.2    Hantgan, R.R.3    Karplus, P.A.4
  • 111
    • 0031034725 scopus 로고    scopus 로고
    • Both isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A212
    • Yao,Y., Zhou,Y. and Wang, C. (1997) 'Both isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A212', EMBO Journal 16, 651-658.
    • (1997) EMBO Journal , vol.16 , pp. 651-658
    • Yao, Y.1    Zhou, Y.2    Wang, C.3
  • 112
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Åslund, F. and Storz, G. (1998) 'Activation of the OxyR transcription factor by reversible disulfide bond formation', Science 279, 1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Åslund, F.2    Storz, G.3
  • 113
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the E. coli response to hydrogen peroxide
    • Zheng, M.,Wang, X., Templeton, L.J., Smulski, D.R., LaRossa, R.A. and Storz, G. (2001) 'DNA microarray-mediated transcriptional profiling of the E. coli response to hydrogen peroxide', Journal of Bacteriology 183, 4562-4570.
    • (2001) Journal of Bacteriology , vol.183 , pp. 4562-4570
    • Zheng, M.1    Wang, X.2    Templeton, L.J.3    Smulski, D.R.4    LaRossa, R.A.5    Storz, G.6


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