메뉴 건너뛰기




Volumn 11, Issue 7, 2006, Pages 329-334

Plant thioredoxins are key actors in the oxidative stress response

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; REACTIVE OXYGEN METABOLITE; THIOREDOXIN;

EID: 33746264833     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2006.05.005     Document Type: Article
Times cited : (289)

References (63)
  • 1
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arnér E.S.J., and Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267 (2000) 6102-6109
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6102-6109
    • Arnér, E.S.J.1    Holmgren, A.2
  • 2
    • 3042658652 scopus 로고    scopus 로고
    • Plant glutaredoxins: still mysterious reducing systems
    • Rouhier N., et al. Plant glutaredoxins: still mysterious reducing systems. Cell. Mol. Life Sci. 61 (2004) 1266-1277
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1266-1277
    • Rouhier, N.1
  • 3
    • 22044451853 scopus 로고    scopus 로고
    • Identification of plant glutaredoxin targets
    • Rouhier N., et al. Identification of plant glutaredoxin targets. Antioxid. Redox Signal. 7 (2005) 919-929
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 919-929
    • Rouhier, N.1
  • 4
    • 29944441650 scopus 로고    scopus 로고
    • Thioredoxins in Arabidopsis and other plants
    • Meyer Y., et al. Thioredoxins in Arabidopsis and other plants. Photosynth. Res. 86 (2005) 419-433
    • (2005) Photosynth. Res. , vol.86 , pp. 419-433
    • Meyer, Y.1
  • 5
    • 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
  • 6
    • 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., et al. Transgenic barley grain overexpressing thioredoxin shows evidence that the starchy endosperm communicates with the embryo and the aleurone. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 16325-16330
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16325-16330
    • Wong, J.H.1
  • 7
    • 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., et al. 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
  • 8
    • 4644304481 scopus 로고    scopus 로고
    • Reactive oxygen gene network of plants
    • Mittler R., et al. Reactive oxygen gene network of plants. Trends Plant Sci. 9 (2004) 490-498
    • (2004) Trends Plant Sci. , vol.9 , pp. 490-498
    • Mittler, R.1
  • 9
    • 12844278044 scopus 로고    scopus 로고
    • The oxidative environment and protein damage
    • Davies M.J. The oxidative environment and protein damage. Biochim. Biophys. Acta 1703 (2005) 93-109
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 93-109
    • Davies, M.J.1
  • 10
    • 0036671827 scopus 로고    scopus 로고
    • Overexpression of human thioredoxin in transgenic mice controls oxidative stress and life span
    • Mitsui A., et al. Overexpression of human thioredoxin in transgenic mice controls oxidative stress and life span. Antioxid. Redox Signal. 4 (2002) 693-696
    • (2002) Antioxid. Redox Signal. , vol.4 , pp. 693-696
    • Mitsui, A.1
  • 11
    • 13444264729 scopus 로고    scopus 로고
    • GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox
    • Zimmermann P., et al. GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox. Plant Physiol. 136 (2004) 2621-2632
    • (2004) Plant Physiol. , vol.136 , pp. 2621-2632
    • Zimmermann, P.1
  • 12
    • 0036619752 scopus 로고    scopus 로고
    • The multigenic family of thioredoxin h in Arabidopsis thaliana: specific expression and stress response
    • Reichheld J.P., et al. The multigenic family of thioredoxin h in Arabidopsis thaliana: specific expression and stress response. Plant Physiol. Biochem. 40 (2002) 685-690
    • (2002) Plant Physiol. Biochem. , vol.40 , pp. 685-690
    • Reichheld, J.P.1
  • 13
    • 16644395716 scopus 로고    scopus 로고
    • Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type
    • Collin V., et al. Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type. Plant Physiol. 136 (2004) 4088-4095
    • (2004) Plant Physiol. , vol.136 , pp. 4088-4095
    • Collin, V.1
  • 14
    • 1642547085 scopus 로고    scopus 로고
    • The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative stress and its W-box-mediated response to pathogen elicitor
    • Laloi C., et al. The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative stress and its W-box-mediated response to pathogen elicitor. Plant Physiol. 134 (2004) 1006-1016
    • (2004) Plant Physiol. , vol.134 , pp. 1006-1016
    • Laloi, C.1
  • 15
    • 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., 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
  • 16
    • 0031885601 scopus 로고    scopus 로고
    • A novel thioredoxin-like protein located in the chloroplast is induced by water deficit in Solanum tuberosum L. plants
    • Rey P., et al. A novel thioredoxin-like protein located in the chloroplast is induced by water deficit in Solanum tuberosum L. plants. Plant J. 13 (1998) 97-107
    • (1998) Plant J. , vol.13 , pp. 97-107
    • Rey, P.1
  • 17
    • 0033962438 scopus 로고    scopus 로고
    • Involvement of CDSP32, a drought-induced thioredoxin, in the response to oxidative stress in potato plants
    • Broin M., et al. Involvement of CDSP32, a drought-induced thioredoxin, in the response to oxidative stress in potato plants. FEBS Lett. 467 (2000) 245-248
    • (2000) FEBS Lett. , vol.467 , pp. 245-248
    • Broin, M.1
  • 18
    • 18744383949 scopus 로고    scopus 로고
    • A novel cis-element that is responsive to oxidative stress regulates three antioxidant defense genes in rice
    • Tsukamoto S., et al. A novel cis-element that is responsive to oxidative stress regulates three antioxidant defense genes in rice. Plant Physiol. 137 (2005) 317-327
    • (2005) Plant Physiol. , vol.137 , pp. 317-327
    • Tsukamoto, S.1
  • 19
    • 0037222255 scopus 로고    scopus 로고
    • Structure, mechanisms and regulation of peroxiredoxins
    • Wood Z.A., et al. Structure, mechanisms and regulation of peroxiredoxins. Trends Biochem. Sci. 28 (2003) 32-40
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 32-40
    • Wood, Z.A.1
  • 20
  • 21
    • 0043011656 scopus 로고    scopus 로고
    • Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization, and activity
    • Brehelin C., et al. Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization, and activity. Plant Physiol. 132 (2003) 2045-2057
    • (2003) Plant Physiol. , vol.132 , pp. 2045-2057
    • Brehelin, C.1
  • 22
    • 0033117456 scopus 로고    scopus 로고
    • Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis. Evidence from transgenic Arabidopsis
    • Baier M., and Dietz K.J. Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis. Evidence from transgenic Arabidopsis. Plant Physiol. 119 (1999) 1407-1414
    • (1999) Plant Physiol. , vol.119 , pp. 1407-1414
    • Baier, M.1    Dietz, K.J.2
  • 23
    • 33644753761 scopus 로고    scopus 로고
    • Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis
    • Lamkemeyer P., et al. Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis. Plant J. 45 (2006) 968-981
    • (2006) Plant J. , vol.45 , pp. 968-981
    • Lamkemeyer, P.1
  • 24
    • 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., et al. Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor. Plant Physiol. 127 (2001) 1299-1309
    • (2001) Plant Physiol. , vol.127 , pp. 1299-1309
    • Rouhier, N.1
  • 25
    • 12744274638 scopus 로고    scopus 로고
    • Analysis of the proteins targeted by CDSP32, a plastidic thioredoxin participating in oxidative stress responses
    • Rey 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
  • 26
    • 2542464938 scopus 로고    scopus 로고
    • Two enzymes in one: two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function
    • Jang H.H., et al. Two enzymes in one: two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function. Cell 117 (2004) 825-835
    • (2004) Cell , vol.117 , pp. 825-835
    • Jang, H.H.1
  • 27
  • 28
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
    • Biteau B., et al. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425 (2003) 980-984
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1
  • 29
    • 10944237769 scopus 로고    scopus 로고
    • Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine
    • Chang T.S., et al. Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. J. Biol. Chem. 279 (2004) 50994-51001
    • (2004) J. Biol. Chem. , vol.279 , pp. 50994-51001
    • Chang, T.S.1
  • 30
    • 0042591328 scopus 로고    scopus 로고
    • Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure
    • König J., et al. Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure. J. Biol. Chem. 278 (2003) 24409-24420
    • (2003) J. Biol. Chem. , vol.278 , pp. 24409-24420
    • König, J.1
  • 31
    • 0029187630 scopus 로고
    • Diversity of glutathione peroxidases
    • Ursini F., et al. Diversity of glutathione peroxidases. Methods Enzymol. 252 (1995) 38-53
    • (1995) Methods Enzymol. , vol.252 , pp. 38-53
    • Ursini, F.1
  • 32
    • 0036094218 scopus 로고    scopus 로고
    • Two GPX-like proteins from Lycopersicon esculentum and Helianthus annuus are antioxidant enzymes with phospholipid hydroperoxide glutathione peroxidase and thioredoxin peroxidase activities
    • Herbette S., et al. Two GPX-like proteins from Lycopersicon esculentum and Helianthus annuus are antioxidant enzymes with phospholipid hydroperoxide glutathione peroxidase and thioredoxin peroxidase activities. Eur. J. Biochem. 269 (2002) 2414-2420
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2414-2420
    • Herbette, S.1
  • 33
    • 0037066696 scopus 로고    scopus 로고
    • A chinese cabbage cDNA with high sequence identity to phospholipid hydroperoxide glutathione peroxidases encodes a novel isoform of thioredoxin-dependent peroxidase
    • Jung B.G., et al. A chinese cabbage cDNA with high sequence identity to phospholipid hydroperoxide glutathione peroxidases encodes a novel isoform of thioredoxin-dependent peroxidase. J. Biol. Chem. 277 (2002) 12572-12578
    • (2002) J. Biol. Chem. , vol.277 , pp. 12572-12578
    • Jung, B.G.1
  • 34
    • 0344237365 scopus 로고    scopus 로고
    • Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated by abiotic stresses through diverse signaling pathways
    • Rodriguez Milla M.A., et al. Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated by abiotic stresses through diverse signaling pathways. Plant J. 36 (2003) 602-615
    • (2003) Plant J. , vol.36 , pp. 602-615
    • Rodriguez Milla, M.A.1
  • 35
    • 0037110454 scopus 로고    scopus 로고
    • 2 receptor and redox-transducer in gene activation
    • 2 receptor and redox-transducer in gene activation. Cell 111 (2002) 471-481
    • (2002) Cell , vol.111 , pp. 471-481
    • Delaunay, A.1
  • 36
    • 0019557182 scopus 로고
    • Enzymatic reduction of protein-bound methionine sulfoxide
    • Brot N., et al. Enzymatic reduction of protein-bound methionine sulfoxide. Proc. Natl. Acad. Sci. U. S. A. 78 (1981) 2155-2158
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 2155-2158
    • Brot, N.1
  • 37
    • 0030955353 scopus 로고    scopus 로고
    • The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo
    • Moskovitz J., et al. The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 9585-9589
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9585-9589
    • Moskovitz, J.1
  • 38
    • 0035966062 scopus 로고    scopus 로고
    • Repair of oxidized proteins. Identification of a new methionine sulfoxide reductase
    • Grimaud R., et al. Repair of oxidized proteins. Identification of a new methionine sulfoxide reductase. J. Biol. Chem. 276 (2001) 48915-48920
    • (2001) J. Biol. Chem. , vol.276 , pp. 48915-48920
    • Grimaud, R.1
  • 39
    • 4444327673 scopus 로고    scopus 로고
    • New targets of Arabidopsis thioredoxins revealed by proteomic analysis
    • Marchand C., et al. New targets of Arabidopsis thioredoxins revealed by proteomic analysis. Proteomics 4 (2004) 2696-2706
    • (2004) Proteomics , vol.4 , pp. 2696-2706
    • Marchand, C.1
  • 40
    • 2442498463 scopus 로고    scopus 로고
    • New thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii
    • Lemaire S.D., et al. New thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 7475-7480
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 7475-7480
    • Lemaire, S.D.1
  • 41
    • 0034070583 scopus 로고    scopus 로고
    • Differential regulation of plastidial and cytosolic isoforms of peptide methionine sulfoxide reductase in Arabidopsis
    • Sadanandom A., et al. Differential regulation of plastidial and cytosolic isoforms of peptide methionine sulfoxide reductase in Arabidopsis. Plant Physiol. 123 (2000) 255-264
    • (2000) Plant Physiol. , vol.123 , pp. 255-264
    • Sadanandom, A.1
  • 42
    • 1842712573 scopus 로고    scopus 로고
    • Arabidopsis peptide methionine sulfoxide reductase2 prevents cellular oxidative damage in long nights
    • Bechtold U., et al. Arabidopsis peptide methionine sulfoxide reductase2 prevents cellular oxidative damage in long nights. Plant Cell 16 (2004) 908-919
    • (2004) Plant Cell , vol.16 , pp. 908-919
    • Bechtold, U.1
  • 43
    • 16544383249 scopus 로고    scopus 로고
    • Investigations into the role of the plastidial peptide methionine sulfoxide reductase in response to oxidative stress in Arabidopsis
    • Romero H.M., et al. Investigations into the role of the plastidial peptide methionine sulfoxide reductase in response to oxidative stress in Arabidopsis. Plant Physiol. 136 (2004) 3784-3794
    • (2004) Plant Physiol. , vol.136 , pp. 3784-3794
    • Romero, H.M.1
  • 44
    • 0036006188 scopus 로고    scopus 로고
    • A peptide methionine sulfoxide reductase highly expressed in photosynthetic tissue in Arabidopsis thaliana can protect the chaperone-like activity of a chloroplast-localized small heat shock protein
    • Gustavsson N., et al. A peptide methionine sulfoxide reductase highly expressed in photosynthetic tissue in Arabidopsis thaliana can protect the chaperone-like activity of a chloroplast-localized small heat shock protein. Plant J. 29 (2002) 545-553
    • (2002) Plant J. , vol.29 , pp. 545-553
    • Gustavsson, N.1
  • 45
    • 26944456370 scopus 로고    scopus 로고
    • The Arabidopsis plastidic methionine sulfoxide reductases B proteins: sequence and activity characteristics, comparison of the expression with plastidic methionine sulfoxide reductase A and induction by photooxidative stress
    • Vieira Dos Santos C., et al. The Arabidopsis plastidic methionine sulfoxide reductases B proteins: sequence and activity characteristics, comparison of the expression with plastidic methionine sulfoxide reductase A and induction by photooxidative stress. Plant Physiol. 138 (2005) 909-922
    • (2005) Plant Physiol. , vol.138 , pp. 909-922
    • Vieira Dos Santos, C.1
  • 46
    • 4244218956 scopus 로고    scopus 로고
    • Stadtman, E.R. et al. (2002) Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism. Mol. Cell. Biochem. 234-235, 3-9
  • 47
    • 0037628370 scopus 로고    scopus 로고
    • Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics
    • Wong J.H., et al. Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics. FEBS Lett. 547 (2003) 151-156
    • (2003) FEBS Lett. , vol.547 , pp. 151-156
    • Wong, J.H.1
  • 48
    • 1042279801 scopus 로고    scopus 로고
    • Target proteins of the cytosolic thioredoxins in Arabidopsis thaliana
    • Yamazaki D., et al. Target proteins of the cytosolic thioredoxins in Arabidopsis thaliana. Plant Cell Physiol. 45 (2004) 18-27
    • (2004) Plant Cell Physiol. , vol.45 , pp. 18-27
    • Yamazaki, D.1
  • 49
    • 10744230621 scopus 로고    scopus 로고
    • Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria
    • Balmer Y., et al. Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 2642-2647
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2642-2647
    • Balmer, Y.1
  • 50
    • 0032539799 scopus 로고    scopus 로고
    • In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae
    • Mouaheb N., et al. 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
  • 51
    • 0035142197 scopus 로고    scopus 로고
    • Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin
    • Issakidis-Bourguet E., et al. Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin. Plant J. 25 (2001) 127-136
    • (2001) Plant J. , vol.25 , pp. 127-136
    • Issakidis-Bourguet, E.1
  • 52
    • 0035983856 scopus 로고    scopus 로고
    • The plastidic 2-Cys-peroxiredoxin is a target for a thioredoxin involved in the protection of the photosynthetic apparatus against oxidative damage
    • Broin M., et al. The plastidic 2-Cys-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
  • 53
    • 0038038526 scopus 로고    scopus 로고
    • Potato plants lacking the CDSP32 plastidic thioredoxin exhibit over-oxidation of the BAS1 2-cys peroxiredoxin and increased lipid peroxidation in thylakoids under photooxidative stress
    • Broin M., and Rey P. Potato plants lacking the CDSP32 plastidic thioredoxin exhibit over-oxidation of the BAS1 2-cys peroxiredoxin and increased lipid peroxidation in thylakoids under photooxidative stress. Plant Physiol. 132 (2003) 1335-1343
    • (2003) Plant Physiol. , vol.132 , pp. 1335-1343
    • Broin, M.1    Rey, P.2
  • 54
    • 1642356888 scopus 로고    scopus 로고
    • Characterization of Arabidopsis mutants for the variable subunit of ferredoxin:thioredoxin reductase
    • Keryer E., et al. Characterization of Arabidopsis mutants for the variable subunit of ferredoxin:thioredoxin reductase. Photosynth. Res. 79 (2004) 265-274
    • (2004) Photosynth. Res. , vol.79 , pp. 265-274
    • Keryer, E.1
  • 55
    • 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., et al. 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
  • 56
    • 13844306891 scopus 로고    scopus 로고
    • Functional specialization of Chlamydomonas reinhardtii cytosolic thioredoxin h1 in the response to alkylation-induced DNA damage
    • Sarkar N., et al. Functional specialization of Chlamydomonas reinhardtii cytosolic thioredoxin h1 in the response to alkylation-induced DNA damage. Eukaryot. Cell 4 (2005) 262-273
    • (2005) Eukaryot. Cell , vol.4 , pp. 262-273
    • Sarkar, N.1
  • 57
    • 0038826955 scopus 로고    scopus 로고
    • Inducers of plant systemic acquired resistance regulate NPR1 function through redox changes
    • Mou Z., et al. Inducers of plant systemic acquired resistance regulate NPR1 function through redox changes. Cell 113 (2003) 935-944
    • (2003) Cell , vol.113 , pp. 935-944
    • Mou, Z.1
  • 58
    • 0034708674 scopus 로고    scopus 로고
    • Disulfide bond formation between RNA binding domains is used to regulate mRNA binding activity of the chloroplast poly(A)-binding protein
    • Fong C.L., et al. Disulfide bond formation between RNA binding domains is used to regulate mRNA binding activity of the chloroplast poly(A)-binding protein. J. Biol. Chem. 275 (2000) 8275-8278
    • (2000) J. Biol. Chem. , vol.275 , pp. 8275-8278
    • Fong, C.L.1
  • 59
    • 0346366724 scopus 로고    scopus 로고
    • Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction
    • Gelhaye E., et al. Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction. FEBS Lett. 555 (2003) 443-448
    • (2003) FEBS Lett. , vol.555 , pp. 443-448
    • Gelhaye, E.1
  • 60
    • 0035949574 scopus 로고    scopus 로고
    • Comprehensive survey of proteins target by chloroplast thioredoxin
    • Motohashi K., et al. Comprehensive survey of proteins target by chloroplast thioredoxin. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 11224-11229
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11224-11229
    • Motohashi, K.1
  • 61
    • 0037422610 scopus 로고    scopus 로고
    • Proteomics give insight into the regulatory function of chloroplast thioredoxins
    • Balmer Y., et al. Proteomics give insight into the regulatory function of chloroplast thioredoxins. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 370-375
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 370-375
    • Balmer, Y.1
  • 62
    • 0037930284 scopus 로고    scopus 로고
    • The Arabidopsis plastidial thioredoxins: new functions and new insights into specificity
    • Collin V., et al. The Arabidopsis plastidial thioredoxins: new functions and new insights into specificity. J. Biol. Chem. 278 (2003) 23747-23752
    • (2003) J. Biol. Chem. , vol.278 , pp. 23747-23752
    • Collin, V.1
  • 63
    • 16844368306 scopus 로고    scopus 로고
    • The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress
    • Finkemeier I., et al. The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress. J. Biol. Chem. 280 (2005) 12168-12180
    • (2005) J. Biol. Chem. , vol.280 , pp. 12168-12180
    • Finkemeier, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.