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Volumn 243, Issue , 2016, Pages 84-95

Nuclear thiol redox systems in plants

Author keywords

Glutaredoxin; Glutathione; Nucleus; Thiol; Thioredoxin

Indexed keywords

GLUTAREDOXIN; GLUTATHIONE; ISOPROTEIN; PLANT PROTEIN; THIOL DERIVATIVE; THIOREDOXIN;

EID: 84949895774     PISSN: 01689452     EISSN: 18732259     Source Type: Journal    
DOI: 10.1016/j.plantsci.2015.12.002     Document Type: Review
Times cited : (51)

References (126)
  • 2
    • 0023886170 scopus 로고
    • DNA damage and oxygen radical toxicity
    • Imlay J.A., Linn S. DNA damage and oxygen radical toxicity. Science 1988, 240:1302-1309.
    • (1988) Science , vol.240 , pp. 1302-1309
    • Imlay, J.A.1    Linn, S.2
  • 3
    • 3242715114 scopus 로고    scopus 로고
    • Reactive oxygen species: metabolism, oxidative stress, and signal transduction
    • Apel K., Hirt H. Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Annu. Rev. Plant Biol. 2004, 55:373-399.
    • (2004) Annu. Rev. Plant Biol. , vol.55 , pp. 373-399
    • Apel, K.1    Hirt, H.2
  • 4
    • 84901032866 scopus 로고    scopus 로고
    • Development of roGFP2-derived redox probes for measurement of the glutathione redox potential in the cytosol of severely glutathione-deficient rml1 seedlings
    • Aller I., Rouhier N., Meyer A.J. Development of roGFP2-derived redox probes for measurement of the glutathione redox potential in the cytosol of severely glutathione-deficient rml1 seedlings. Front. Plant Sci. 2013, 4:1-12.
    • (2013) Front. Plant Sci. , vol.4 , pp. 1-12
    • Aller, I.1    Rouhier, N.2    Meyer, A.J.3
  • 5
    • 60749136076 scopus 로고    scopus 로고
    • Redox regulation in photosynthetic organisms: signaling, acclimation, and practical implications
    • Foyer C.H., Noctor G. Redox regulation in photosynthetic organisms: signaling, acclimation, and practical implications. Antioxid. Redox Signal. 2009, 11:861-905.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 861-905
    • Foyer, C.H.1    Noctor, G.2
  • 6
    • 34250849635 scopus 로고    scopus 로고
    • Oxidative modifications to cellular components in plants
    • Møller I.M., Jensen P.E., Hansson A. Oxidative modifications to cellular components in plants. Annu. Rev. Plant Biol. 2007, 58:459-481.
    • (2007) Annu. Rev. Plant Biol. , vol.58 , pp. 459-481
    • Møller, I.M.1    Jensen, P.E.2    Hansson, A.3
  • 7
    • 34249810365 scopus 로고    scopus 로고
    • Diverse subcellular locations of cryptogein-induced reactive oxygen species production in tobacco bright yellow- 2cells
    • Ashtamker C., Kiss V., Sagi M., Davydov O., Fluhr R. Diverse subcellular locations of cryptogein-induced reactive oxygen species production in tobacco bright yellow- 2cells. Plant Physiol. 2007, 143:1817-1826.
    • (2007) Plant Physiol. , vol.143 , pp. 1817-1826
    • Ashtamker, C.1    Kiss, V.2    Sagi, M.3    Davydov, O.4    Fluhr, R.5
  • 8
    • 77649250810 scopus 로고    scopus 로고
    • Nuclear redox signaling
    • Lukosz M., et al. Nuclear redox signaling. Antioxid. Redox Signal. 2010, 12:713-742.
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 713-742
    • Lukosz, M.1
  • 10
    • 44849141142 scopus 로고    scopus 로고
    • Protein thiol modification by peroxynitrite anion and nitric oxide donors
    • Landino L.M. Protein thiol modification by peroxynitrite anion and nitric oxide donors. Methods Enzymol. 2008, 440:95-109.
    • (2008) Methods Enzymol. , vol.440 , pp. 95-109
    • Landino, L.M.1
  • 11
    • 84856719860 scopus 로고    scopus 로고
    • Redox regulation in photosynthetic organisms: focus on glutathionylation
    • Zaffagnini M., et al. Redox regulation in photosynthetic organisms: focus on glutathionylation. Antioxid. Redox Signal. 2012, 16:567-586.
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 567-586
    • Zaffagnini, M.1
  • 12
    • 79751494167 scopus 로고    scopus 로고
    • The language of nitric oxide signalling
    • Baudouin E. The language of nitric oxide signalling. Plant Biol. (Stuttg.) 2011, 13:233-242.
    • (2011) Plant Biol. (Stuttg.) , vol.13 , pp. 233-242
    • Baudouin, E.1
  • 14
    • 42949085825 scopus 로고    scopus 로고
    • The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation
    • Rouhier N., Lemaire S.D., Jacquot J.-P. The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation. Annu. Rev. Plant Biol. 2008, 59:143-166.
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 143-166
    • Rouhier, N.1    Lemaire, S.D.2    Jacquot, J.-P.3
  • 15
  • 18
    • 0344875538 scopus 로고    scopus 로고
    • Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants
    • Chew O., Whelan J., Millar A.H. Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants. J. Biol. Chem. 2003, 278:46869-46877.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46869-46877
    • Chew, O.1    Whelan, J.2    Millar, A.H.3
  • 19
    • 67049156798 scopus 로고    scopus 로고
    • The NADPH-dependent thioredoxin system constitutes a functional backup for cytosolic glutathione reductase in Arabidopsis
    • Marty L., et al. The NADPH-dependent thioredoxin system constitutes a functional backup for cytosolic glutathione reductase in Arabidopsis. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:9109-9114.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 9109-9114
    • Marty, L.1
  • 20
    • 77956622614 scopus 로고    scopus 로고
    • Arabidopsis glutathione reductase 1 is dually targeted to peroxisomes and the cytosol
    • Kataya A.R.A., Reumann S. Arabidopsis glutathione reductase 1 is dually targeted to peroxisomes and the cytosol. Plant Signal. Behav. 2010, 5:171-175.
    • (2010) Plant Signal. Behav. , vol.5 , pp. 171-175
    • Kataya, A.R.A.1    Reumann, S.2
  • 21
    • 58149131296 scopus 로고    scopus 로고
    • An antioxidant redox system in the nucleus of wheat seed cells suffering oxidative stress
    • Pulido P., Cazalis R., Cejudo F.J. An antioxidant redox system in the nucleus of wheat seed cells suffering oxidative stress. Plant J. 2009, 57:132-145.
    • (2009) Plant J. , vol.57 , pp. 132-145
    • Pulido, P.1    Cazalis, R.2    Cejudo, F.J.3
  • 22
    • 84891780708 scopus 로고    scopus 로고
    • NTR/NRX define a new thioredoxin system in the nucleus of Arabidopsis thaliana cells
    • Marchal C., et al. NTR/NRX define a new thioredoxin system in the nucleus of Arabidopsis thaliana cells. Mol. Plant 2014, 7:30-44.
    • (2014) Mol. Plant , vol.7 , pp. 30-44
    • Marchal, C.1
  • 23
    • 63549137242 scopus 로고    scopus 로고
    • Thioredoxin targets in plants: the first 30 years
    • Montrichard F., et al. Thioredoxin targets in plants: the first 30 years. J. Proteom. 2009, 72:452-474.
    • (2009) J. Proteom. , vol.72 , pp. 452-474
    • Montrichard, F.1
  • 24
    • 0034906367 scopus 로고    scopus 로고
    • Quantitative in vivo measurement of glutathione in Arabidopsis cells
    • Meyer A.J., May M.J., Fricker M. Quantitative in vivo measurement of glutathione in Arabidopsis cells. Plant J 2001, 27:67-78.
    • (2001) Plant J , vol.27 , pp. 67-78
    • Meyer, A.J.1    May, M.J.2    Fricker, M.3
  • 26
    • 0036914544 scopus 로고    scopus 로고
    • Control of demand-driven biosynthesis of glutathione in green Arabidopsis suspension culture cells
    • Meyer A.J., Fricker M.D. Control of demand-driven biosynthesis of glutathione in green Arabidopsis suspension culture cells. Plant Physiol. 2002, 130:1927-1937.
    • (2002) Plant Physiol. , vol.130 , pp. 1927-1937
    • Meyer, A.J.1    Fricker, M.D.2
  • 27
    • 77957274966 scopus 로고    scopus 로고
    • Subcellular compartmentation of glutathione in dicotyledonous plants
    • Zechmann B., Müller M. Subcellular compartmentation of glutathione in dicotyledonous plants. Protoplasma 2010, 246:15-24.
    • (2010) Protoplasma , vol.246 , pp. 15-24
    • Zechmann, B.1    Müller, M.2
  • 28
    • 78650721484 scopus 로고    scopus 로고
    • Immunocytochemical determination of the subcellular distribution of ascorbate in plants
    • Zechmann B., Stumpe M., Mauch F. Immunocytochemical determination of the subcellular distribution of ascorbate in plants. Planta 2011, 233:1-12.
    • (2011) Planta , vol.233 , pp. 1-12
    • Zechmann, B.1    Stumpe, M.2    Mauch, F.3
  • 29
    • 36349007756 scopus 로고    scopus 로고
    • Redox-sensitive GFP in Arabidopsis thaliana is a quantitative biosensor for the redox potential of the cellular glutathione redox buffer
    • Meyer A.J., et al. Redox-sensitive GFP in Arabidopsis thaliana is a quantitative biosensor for the redox potential of the cellular glutathione redox buffer. Plant J. 2007, 52:973-986.
    • (2007) Plant J. , vol.52 , pp. 973-986
    • Meyer, A.J.1
  • 30
    • 48549102564 scopus 로고    scopus 로고
    • Confocal imaging of glutathione redox potential in living plant cells
    • Schwarzländer M., et al. Confocal imaging of glutathione redox potential in living plant cells. J. Microsc. 2008, 231:299-316.
    • (2008) J. Microsc. , vol.231 , pp. 299-316
    • Schwarzländer, M.1
  • 31
    • 84921565222 scopus 로고    scopus 로고
    • Low glutathione regulates gene expression and the redox potentials of the nucleus and cytosol in Arabidopsis thaliana
    • Schnaubelt D., et al. Low glutathione regulates gene expression and the redox potentials of the nucleus and cytosol in Arabidopsis thaliana. Plant Cell Environ. 2015, 38:266-279.
    • (2015) Plant Cell Environ. , vol.38 , pp. 266-279
    • Schnaubelt, D.1
  • 32
    • 76649113436 scopus 로고    scopus 로고
    • Plant homologs of the Plasmodium falciparum chloroquine-resistance transporter, PfCRT, are required for glutathione homeostasis and stress responses
    • Maughan S.C., et al. Plant homologs of the Plasmodium falciparum chloroquine-resistance transporter, PfCRT, are required for glutathione homeostasis and stress responses. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:2331-2336.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 2331-2336
    • Maughan, S.C.1
  • 33
    • 84891540793 scopus 로고    scopus 로고
    • Plastid-localized glutathione reductase2-regulated glutathione redox status is essential for Arabidopsis root apical meristem maintenance
    • Yu X., et al. Plastid-localized glutathione reductase2-regulated glutathione redox status is essential for Arabidopsis root apical meristem maintenance. Plant Cell 2013, 25:4451-4468.
    • (2013) Plant Cell , vol.25 , pp. 4451-4468
    • Yu, X.1
  • 34
    • 0027210070 scopus 로고
    • ATP-dependent glutathione S-conjugate export pump in the vacuolar membrane of plants
    • Martinoia E., Gril E., Tommasini R., Kreuz K., Amrhein N. ATP-dependent glutathione S-conjugate export pump in the vacuolar membrane of plants. Nature 1993, 346:247-249.
    • (1993) Nature , vol.346 , pp. 247-249
    • Martinoia, E.1    Gril, E.2    Tommasini, R.3    Kreuz, K.4    Amrhein, N.5
  • 35
    • 84872687926 scopus 로고    scopus 로고
    • Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis
    • Morgan B., et al. Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis. Nat. Chem. Biol. 2013, 9:119-125.
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 119-125
    • Morgan, B.1
  • 36
    • 84906545328 scopus 로고    scopus 로고
    • A conserved mitochondrial ATP-binding cassette transporter exports glutathione polysulfide for cytosolic metal cofactor assembly
    • Schaedler T.A., et al. A conserved mitochondrial ATP-binding cassette transporter exports glutathione polysulfide for cytosolic metal cofactor assembly. J. Biol. Chem. 2014, 289:23264-23274.
    • (2014) J. Biol. Chem. , vol.289 , pp. 23264-23274
    • Schaedler, T.A.1
  • 37
    • 84885194018 scopus 로고    scopus 로고
    • Regulating the redox gatekeeper: vacuolar sequestration puts glutathione disulfide in its place
    • Noctor G., Mhamdi A., Queval G., Foyer C.H. Regulating the redox gatekeeper: vacuolar sequestration puts glutathione disulfide in its place. Plant Physiol. 2013, 163:665-671.
    • (2013) Plant Physiol. , vol.163 , pp. 665-671
    • Noctor, G.1    Mhamdi, A.2    Queval, G.3    Foyer, C.H.4
  • 38
    • 79958839612 scopus 로고    scopus 로고
    • Development of glutathione-deficient embryos in Arabidopsis is influenced by the maternal level of glutathione
    • Lim B., Meyer A.J., Cobbett C.S. Development of glutathione-deficient embryos in Arabidopsis is influenced by the maternal level of glutathione. Plant Biol. (Stuttg.) 2011, 13:693-697.
    • (2011) Plant Biol. (Stuttg.) , vol.13 , pp. 693-697
    • Lim, B.1    Meyer, A.J.2    Cobbett, C.S.3
  • 39
    • 33847185842 scopus 로고    scopus 로고
    • A redox cycle within the cell cycle: ring in the old with the new
    • Menon S.G., Goswami P.C. A redox cycle within the cell cycle: ring in the old with the new. Oncogene 2007, 26:1101-1109.
    • (2007) Oncogene , vol.26 , pp. 1101-1109
    • Menon, S.G.1    Goswami, P.C.2
  • 40
    • 78649560974 scopus 로고    scopus 로고
    • Recruitment of glutathione into the nucleus during cell proliferation adjusts whole-cell redox homeostasis in Arabidopsis thaliana and lowers the oxidative defence shield: recruitment of GSH into the nucleus
    • Diaz Vivancos P., et al. Recruitment of glutathione into the nucleus during cell proliferation adjusts whole-cell redox homeostasis in Arabidopsis thaliana and lowers the oxidative defence shield: recruitment of GSH into the nucleus. Plant J. 2010, 64:825-838.
    • (2010) Plant J. , vol.64 , pp. 825-838
    • Diaz Vivancos, P.1
  • 42
    • 68149137165 scopus 로고    scopus 로고
    • The depletion of nuclear glutathione impairs cell proliferation in 3t3 fibroblasts
    • Markovic J., et al. The depletion of nuclear glutathione impairs cell proliferation in 3t3 fibroblasts. PLoS One 2009, 4:e6413.
    • (2009) PLoS One , vol.4 , pp. e6413
    • Markovic, J.1
  • 43
    • 77954356493 scopus 로고    scopus 로고
    • Fluorescent protein-based redox probes
    • Meyer A.J., Dick T.P. Fluorescent protein-based redox probes. Antioxid. Redox Signal. 2010, 13:621-650.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 621-650
    • Meyer, A.J.1    Dick, T.P.2
  • 44
    • 84881487280 scopus 로고    scopus 로고
    • Redox-sensitive YFP sensors for monitoring dynamic compartment-specific glutathione redox state
    • Banach-Latapy A., et al. Redox-sensitive YFP sensors for monitoring dynamic compartment-specific glutathione redox state. Free Rad. Biol. Med. 2013, 65:436-445.
    • (2013) Free Rad. Biol. Med. , vol.65 , pp. 436-445
    • Banach-Latapy, A.1
  • 45
    • 84865411350 scopus 로고    scopus 로고
    • Thioredoxin and glutaredoxin systems in plants: molecular mechanisms, crosstalks, and functional significance
    • Meyer Y., Belin C., Delorme- Hinoux V., Reichheld J.-P., Riondet C. Thioredoxin and glutaredoxin systems in plants: molecular mechanisms, crosstalks, and functional significance. Antioxid. Redox Signal. 2012, 17:1124-1160.
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 1124-1160
    • Meyer, Y.1    Belin, C.2    Delorme-Hinoux, V.3    Reichheld, J.-P.4    Riondet, C.5
  • 46
    • 38349028576 scopus 로고    scopus 로고
    • Expression pattern of human glutaredoxin 2 isoforms: identification and characterization of two testis/cancer cell- specific isoforms
    • Lönn M.E., et al. Expression pattern of human glutaredoxin 2 isoforms: identification and characterization of two testis/cancer cell- specific isoforms. Antioxid. Redox Signal. 2008, 10:547-558.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 547-558
    • Lönn, M.E.1
  • 47
    • 84921611752 scopus 로고    scopus 로고
    • A comprehensive study of thiol reduction gene expression under stress conditions in Arabidopsis thaliana
    • Belin C., et al. A comprehensive study of thiol reduction gene expression under stress conditions in Arabidopsis thaliana. Plant Cell Environ. 2015, 38:299-314.
    • (2015) Plant Cell Environ. , vol.38 , pp. 299-314
    • Belin, C.1
  • 48
    • 17744384297 scopus 로고    scopus 로고
    • ROXY1, a member of the plant glutaredoxin family, is required for petal development in Arabidopsis thaliana
    • Xing S., Rosso M.G., Zachgo S. ROXY1, a member of the plant glutaredoxin family, is required for petal development in Arabidopsis thaliana. Development 2005, 132:1555-1565.
    • (2005) Development , vol.132 , pp. 1555-1565
    • Xing, S.1    Rosso, M.G.2    Zachgo, S.3
  • 49
    • 41849125681 scopus 로고    scopus 로고
    • ROXY1 and ROXY2, two Arabidopsis glutaredoxin genes, are required for anther development
    • Xing S., Zachgo S. ROXY1 and ROXY2, two Arabidopsis glutaredoxin genes, are required for anther development. Plant J. 2008, 53:790-801.
    • (2008) Plant J. , vol.53 , pp. 790-801
    • Xing, S.1    Zachgo, S.2
  • 50
    • 78249288758 scopus 로고    scopus 로고
    • Arabidopsis basic leucine-zipper transcription factors TGA9 and TGA10 interact with floral glutaredoxins ROXY1 and ROXY2 and are redundantly required for anther development
    • Murmu J., et al. Arabidopsis basic leucine-zipper transcription factors TGA9 and TGA10 interact with floral glutaredoxins ROXY1 and ROXY2 and are redundantly required for anther development. Plant Physiol. 2010, 154:1492-1504.
    • (2010) Plant Physiol. , vol.154 , pp. 1492-1504
    • Murmu, J.1
  • 51
    • 64749114849 scopus 로고    scopus 로고
    • Nuclear activity of ROXY1, a glutaredoxin interacting with TGA factors, is required for petal development in Arabidopsis thaliana
    • Li S., et al. Nuclear activity of ROXY1, a glutaredoxin interacting with TGA factors, is required for petal development in Arabidopsis thaliana. Plant Cell 2009, 21:429-441.
    • (2009) Plant Cell , vol.21 , pp. 429-441
    • Li, S.1
  • 52
    • 51549091920 scopus 로고    scopus 로고
    • Global identification of DELLA target genes during Arabidopsis flower development
    • Hou X., et al. Global identification of DELLA target genes during Arabidopsis flower development. Plant Physiol. 2008, 147:1126-1142.
    • (2008) Plant Physiol. , vol.147 , pp. 1126-1142
    • Hou, X.1
  • 53
    • 33947651152 scopus 로고    scopus 로고
    • SA-inducible Arabidopsis glutaredoxin interacts with TGA factors and suppresses JA-responsive PDF1. 2 transcription: interaction of glutaredoxin with TGA factors
    • Ndamukong I., et al. SA-inducible Arabidopsis glutaredoxin interacts with TGA factors and suppresses JA-responsive PDF1. 2 transcription: interaction of glutaredoxin with TGA factors. Plant J. 2007, 50:128-139.
    • (2007) Plant J. , vol.50 , pp. 128-139
    • Ndamukong, I.1
  • 54
    • 84859053740 scopus 로고    scopus 로고
    • Somatic and reproductive cell development in rice anther is regulated by a putative glutaredoxin
    • Hong L., et al. Somatic and reproductive cell development in rice anther is regulated by a putative glutaredoxin. Plant Cell 2012, 24:577-588.
    • (2012) Plant Cell , vol.24 , pp. 577-588
    • Hong, L.1
  • 55
    • 84923031711 scopus 로고    scopus 로고
    • A maize glutaredoxin gene, abphyl2, regulates shoot meristem size and phyllotaxy
    • Yang F., et al. A maize glutaredoxin gene, abphyl2, regulates shoot meristem size and phyllotaxy. Plant Cell 2015, 27:121-131.
    • (2015) Plant Cell , vol.27 , pp. 121-131
    • Yang, F.1
  • 56
    • 41949108097 scopus 로고    scopus 로고
    • Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters
    • Bandyopadhyay S., et al. Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters. EMBO J. 2008, 27:1122-1133.
    • (2008) EMBO J. , vol.27 , pp. 1122-1133
    • Bandyopadhyay, S.1
  • 57
    • 84926145301 scopus 로고    scopus 로고
    • Arabidopsis glutaredoxin S17 and its partner, the nuclear factor Y subunit C11/negative cofactor 2α, contribute to maintenance of the shoot apical meristem under long-day photoperiod
    • Knuesting J., et al. Arabidopsis glutaredoxin S17 and its partner, the nuclear factor Y subunit C11/negative cofactor 2α, contribute to maintenance of the shoot apical meristem under long-day photoperiod. Plant Physiol. 2015, 167:1643-1658.
    • (2015) Plant Physiol. , vol.167 , pp. 1643-1658
    • Knuesting, J.1
  • 58
    • 84946593620 scopus 로고    scopus 로고
    • The mitochondrial monothiol glutaredoxin S15 is essential for iron-sulfur protein maturation in Arabidopsis thaliana
    • Moseler A., et al. The mitochondrial monothiol glutaredoxin S15 is essential for iron-sulfur protein maturation in Arabidopsis thaliana. Proc. Natl. Acad. Sci. U. S. A. 2015, 112:13735-13740.
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. 13735-13740
    • Moseler, A.1
  • 59
    • 84865749453 scopus 로고    scopus 로고
    • Ectopic expression of Arabidopsis glutaredoxin AtGRXS17 enhances thermotolerance in tomato: ectopic expression of AtGRXS17 in tomato
    • Wu Q., et al. Ectopic expression of Arabidopsis glutaredoxin AtGRXS17 enhances thermotolerance in tomato: ectopic expression of AtGRXS17 in tomato. Plant Biotechnol. J. 2012, 10:945-955.
    • (2012) Plant Biotechnol. J. , vol.10 , pp. 945-955
    • Wu, Q.1
  • 60
    • 79958013653 scopus 로고    scopus 로고
    • Arabidopsis monothiol glutaredoxin, AtGRXS17, is critical for temperature-dependent postembryonic growth and development via modulating auxin response
    • Cheng N.-H., et al. Arabidopsis monothiol glutaredoxin, AtGRXS17, is critical for temperature-dependent postembryonic growth and development via modulating auxin response. J. Biol. Chem. 2011, 286:20398-20406.
    • (2011) J. Biol. Chem. , vol.286 , pp. 20398-20406
    • Cheng, N.-H.1
  • 61
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill R. Function and biogenesis of iron-sulphur proteins. Nature 2009, 460:831-838.
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 62
    • 84855350829 scopus 로고    scopus 로고
    • A dicotyledon-specific glutaredoxin GRXC1 family with dimer-dependent redox regulation is functionally redundant with GRXC2
    • Riondet C., et al. A dicotyledon-specific glutaredoxin GRXC1 family with dimer-dependent redox regulation is functionally redundant with GRXC2. Plant Cell Environ. 2012, 35:360-373.
    • (2012) Plant Cell Environ. , vol.35 , pp. 360-373
    • Riondet, C.1
  • 63
    • 0033913980 scopus 로고    scopus 로고
    • Nucleoredoxin, glutaredoxin, and thioredoxin differentially regulate NF-kappaB, AP-1, and CREB activation in HEK293 cells
    • Hirota K., et al. Nucleoredoxin, glutaredoxin, and thioredoxin differentially regulate NF-kappaB, AP-1, and CREB activation in HEK293 cells. Biochem. Biophys. Res. Commun. 2000, 274:177-182.
    • (2000) Biochem. Biophys. Res. Commun. , vol.274 , pp. 177-182
    • Hirota, K.1
  • 64
    • 0034928212 scopus 로고    scopus 로고
    • Characterization of two thioredoxins h with predominant localization in the nucleus of aleurone and scutellum cells of germinating wheat seeds
    • Serrato A.J., Crespo J.L., Florencio F.J., Cejudo F.J. Characterization of two thioredoxins h with predominant localization in the nucleus of aleurone and scutellum cells of germinating wheat seeds. Plant Mol. Biol. 2001, 46:361-371.
    • (2001) Plant Mol. Biol. , vol.46 , pp. 361-371
    • Serrato, A.J.1    Crespo, J.L.2    Florencio, F.J.3    Cejudo, F.J.4
  • 65
    • 0037108728 scopus 로고    scopus 로고
    • Cloning of thioredoxin h reductase and characterization of the thioredoxin reductase-thioredoxin h system from wheat
    • Serrato A., Perez-Ruiz J., Cejudo F. Cloning of thioredoxin h reductase and characterization of the thioredoxin reductase-thioredoxin h system from wheat. Biochem. J. 2002, 367:491-497.
    • (2002) Biochem. J. , vol.367 , pp. 491-497
    • Serrato, A.1    Perez-Ruiz, J.2    Cejudo, F.3
  • 66
    • 0042209787 scopus 로고    scopus 로고
    • Type-h thioredoxins accumulate in the nucleus of developing wheat seed tissues suffering oxidative stress
    • Serrato A.J., Cejudo F.J. Type-h thioredoxins accumulate in the nucleus of developing wheat seed tissues suffering oxidative stress. Planta 2003, 217:392-399.
    • (2003) Planta , vol.217 , pp. 392-399
    • Serrato, A.J.1    Cejudo, F.J.2
  • 67
    • 13844306891 scopus 로고    scopus 로고
    • Functional specialization of Chlamydomonas reinhardtii cytosolic thioredoxin h1 in the response to alkylation-induced DNA damage
    • Sarkar N., Lemaire S., Wu- Scharf D., Issakidis-Bourguet E., Cerutti H. Functional specialization of Chlamydomonas reinhardtii cytosolic thioredoxin h1 in the response to alkylation-induced DNA damage. Eukaryot. Cell 2005, 4:262-273.
    • (2005) Eukaryot. Cell , vol.4 , pp. 262-273
    • Sarkar, N.1    Lemaire, S.2    Wu-Scharf, D.3    Issakidis-Bourguet, E.4    Cerutti, H.5
  • 68
    • 66649118574 scopus 로고    scopus 로고
    • Mitochondrial and nuclear localization of a novel pea thioredoxin: identification of its mitochondrial target proteins
    • Martí M.C., et al. Mitochondrial and nuclear localization of a novel pea thioredoxin: identification of its mitochondrial target proteins. Plant Physiol. 2009, 150:646-657.
    • (2009) Plant Physiol. , vol.150 , pp. 646-657
    • Martí, M.C.1
  • 69
    • 0031081787 scopus 로고    scopus 로고
    • Cloning and characterization of the nucleoredoxin gene that encodes a novel nuclear protein related to thioredoxin
    • Kurooka H., et al. Cloning and characterization of the nucleoredoxin gene that encodes a novel nuclear protein related to thioredoxin. Genomics 1997, 39:331-339.
    • (1997) Genomics , vol.39 , pp. 331-339
    • Kurooka, H.1
  • 70
    • 65249109913 scopus 로고    scopus 로고
    • Comparative genomic study of the thioredoxin family in photosynthetic organisms with emphasis on Populus trichocarpa
    • Chibani K., Wingsle G., Jacquot J.-P., Gelhaye E., Rouhier N. Comparative genomic study of the thioredoxin family in photosynthetic organisms with emphasis on Populus trichocarpa. Mol. Plant 2009, 2:308-322.
    • (2009) Mol. Plant , vol.2 , pp. 308-322
    • Chibani, K.1    Wingsle, G.2    Jacquot, J.-P.3    Gelhaye, E.4    Rouhier, N.5
  • 71
    • 0032197184 scopus 로고    scopus 로고
    • A novel nuclear member of the thioredoxin superfamily
    • Laughner B.J., Sehnke P.C., Ferl R.J. A novel nuclear member of the thioredoxin superfamily. Plant Physiol. 1998, 118:987-996.
    • (1998) Plant Physiol. , vol.118 , pp. 987-996
    • Laughner, B.J.1    Sehnke, P.C.2    Ferl, R.J.3
  • 72
    • 33646858497 scopus 로고    scopus 로고
    • The thioredoxin-related redox-regulating protein nucleoredoxin inhibits Wnt-β-catenin signalling through dishevelled
    • Funato Y., Michiue T., Asashima M., Miki H. The thioredoxin-related redox-regulating protein nucleoredoxin inhibits Wnt-β-catenin signalling through dishevelled. Nature Cell Biol. 2006, 8:501-508.
    • (2006) Nature Cell Biol. , vol.8 , pp. 501-508
    • Funato, Y.1    Michiue, T.2    Asashima, M.3    Miki, H.4
  • 73
    • 70149108590 scopus 로고    scopus 로고
    • Penetration of the stigma and style elicits a novel transcriptome in pollen tubes, pointing to genes critical for growth in a pistil
    • Qin Y., et al. Penetration of the stigma and style elicits a novel transcriptome in pollen tubes, pointing to genes critical for growth in a pistil. PLoS Genet. 2009, 5:e1000621.
    • (2009) PLoS Genet. , vol.5 , pp. e1000621
    • Qin, Y.1
  • 74
    • 84883149749 scopus 로고    scopus 로고
    • Constitutively elevated salicylic acid levels alter photosynthesis and oxidative state but not growth in transgenic Populus
    • Xue L.-J., et al. Constitutively elevated salicylic acid levels alter photosynthesis and oxidative state but not growth in transgenic Populus. Plant Cell 2013, 25:2714-2730.
    • (2013) Plant Cell , vol.25 , pp. 2714-2730
    • Xue, L.-J.1
  • 75
    • 4644318801 scopus 로고    scopus 로고
    • An alternative splicing variant of the selenoprotein thioredoxin reductase is a modulator of estrogen signaling
    • Damdimopoulos A.E., Miranda-Vizuete A., Treuter E., Gustafsson J.-A., Spyrou G. An alternative splicing variant of the selenoprotein thioredoxin reductase is a modulator of estrogen signaling. J. Biol. Chem. 2004, 279:38721-38729.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38721-38729
    • Damdimopoulos, A.E.1    Miranda-Vizuete, A.2    Treuter, E.3    Gustafsson, J.-A.4    Spyrou, G.5
  • 76
    • 0035923520 scopus 로고    scopus 로고
    • Identification and characterization of a mitochondrial thioredoxin system in plants
    • Laloi C., et al. Identification and characterization of a mitochondrial thioredoxin system in plants. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:14144-14149.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 14144-14149
    • Laloi, C.1
  • 77
    • 11844285694 scopus 로고    scopus 로고
    • AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana
    • Reichheld J.-P., Meyer E., Khafif M., Bonnard G., Meyer Y. AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana. FEBS Lett. 2005, 579:337-342.
    • (2005) FEBS Lett. , vol.579 , pp. 337-342
    • Reichheld, J.-P.1    Meyer, E.2    Khafif, M.3    Bonnard, G.4    Meyer, Y.5
  • 78
    • 0033166877 scopus 로고    scopus 로고
    • The dormancy-related peroxiredoxin anti-oxidant, PER1, is localized to the nucleus of barley embryo and aleurone cells
    • Stacy R.A., Nordeng T.W., Culiáñez-Macià F.A., Aalen R.B. The dormancy-related peroxiredoxin anti-oxidant, PER1, is localized to the nucleus of barley embryo and aleurone cells. Plant J. 1999, 19:1-8.
    • (1999) Plant J. , vol.19 , pp. 1-8
    • Stacy, R.A.1    Nordeng, T.W.2    Culiáñez-Macià, F.A.3    Aalen, R.B.4
  • 80
    • 84881478663 scopus 로고    scopus 로고
    • Histone H3 glutathionylation in proliferating mammalian cells destabilizes nucleosomal structure
    • García-Giménez J.L., et al. Histone H3 glutathionylation in proliferating mammalian cells destabilizes nucleosomal structure. Antioxid. Redox Signal. 2013, 19:1305-1320.
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 1305-1320
    • García-Giménez, J.L.1
  • 81
    • 84906794586 scopus 로고    scopus 로고
    • Histone H3 dynamics in plant cell cycle and development
    • Otero S., Desvoyes B., Gutierrez C. Histone H3 dynamics in plant cell cycle and development. Cytogenet. Genome Res. 2014, 143:114-124.
    • (2014) Cytogenet. Genome Res. , vol.143 , pp. 114-124
    • Otero, S.1    Desvoyes, B.2    Gutierrez, C.3
  • 82
    • 84896292959 scopus 로고    scopus 로고
    • A redox-resistant sirtuin-1 mutant protects against hepatic metabolic and oxidant stress
    • Shao D., et al. A redox-resistant sirtuin-1 mutant protects against hepatic metabolic and oxidant stress. J. Biol. Chem. 2014, 289:7293-7306.
    • (2014) J. Biol. Chem. , vol.289 , pp. 7293-7306
    • Shao, D.1
  • 83
    • 52149108919 scopus 로고    scopus 로고
    • S-Nitrosylation of histone deacetylase 2 induces chromatin remodelling in neurons
    • Nott A., Watson P.M., Robinson J.D., Crepaldi L., Riccio A. S-Nitrosylation of histone deacetylase 2 induces chromatin remodelling in neurons. Nature 2008, 455:411-415.
    • (2008) Nature , vol.455 , pp. 411-415
    • Nott, A.1    Watson, P.M.2    Robinson, J.D.3    Crepaldi, L.4    Riccio, A.5
  • 84
    • 0344066300 scopus 로고    scopus 로고
    • Seed 1-cysteine peroxiredoxin antioxidants are not involved in dormancy, but contribute to inhibition of germination during seed stress
    • Haleskas C., et al. Seed 1-cysteine peroxiredoxin antioxidants are not involved in dormancy, but contribute to inhibition of germination during seed stress. Plant Physiol. 2003, 133:1148-1157.
    • (2003) Plant Physiol. , vol.133 , pp. 1148-1157
    • Haleskas, C.1
  • 85
    • 4444311612 scopus 로고    scopus 로고
    • Two cysteines in plant R2R3 MYB domains participate in REDOX-dependent DNA binding
    • Heine G.F., Hernandez J.M., Grotewold E. Two cysteines in plant R2R3 MYB domains participate in REDOX-dependent DNA binding. J. Biol. Chem. 2004, 279:37878-37885.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37878-37885
    • Heine, G.F.1    Hernandez, J.M.2    Grotewold, E.3
  • 86
    • 84865028379 scopus 로고    scopus 로고
    • Redox-mediated mechanisms regulate DNA binding activity of the G-group of basic region leucine zipper (bZIP) transcription factors in Arabidopsis
    • Shaikhali J., et al. Redox-mediated mechanisms regulate DNA binding activity of the G-group of basic region leucine zipper (bZIP) transcription factors in Arabidopsis. J. Biol. Chem. 2012, 287:27510-27525.
    • (2012) J. Biol. Chem. , vol.287 , pp. 27510-27525
    • Shaikhali, J.1
  • 87
    • 35449001522 scopus 로고    scopus 로고
    • Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins
    • Comelli R.N., Gonzalez D.H. Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins. Arch. Biochem. Biophys. 2007, 467:41-47.
    • (2007) Arch. Biochem. Biophys. , vol.467 , pp. 41-47
    • Comelli, R.N.1    Gonzalez, D.H.2
  • 88
    • 84879733323 scopus 로고    scopus 로고
    • Redox modulation of plant developmental regulators from the class I TCP transcription factor family
    • Viola I.L., Güttlein L.N., Gonzalez D.H. Redox modulation of plant developmental regulators from the class I TCP transcription factor family. Plant Physiol. 2013, 162:1434-1447.
    • (2013) Plant Physiol. , vol.162 , pp. 1434-1447
    • Viola, I.L.1    Güttlein, L.N.2    Gonzalez, D.H.3
  • 89
    • 82755176105 scopus 로고    scopus 로고
    • The ROXY1C-terminal L**LL motif is essential for the interaction with TGA transcription factors
    • Li S., Gutsche N., Zachgo S. The ROXY1C-terminal L**LL motif is essential for the interaction with TGA transcription factors. Plant Physiol. 2011, 157:2056-2068.
    • (2011) Plant Physiol. , vol.157 , pp. 2056-2068
    • Li, S.1    Gutsche, N.2    Zachgo, S.3
  • 90
    • 84865577760 scopus 로고    scopus 로고
    • Repression of the Arabidopsis thaliana jasmonic acid/ethylene-induced defense pathway by TGA-Interacting glutaredoxins depends on their C-terminal ALWL motif
    • Zander M., Chen S., Imkampe J., Thurow C., Gatz C. Repression of the Arabidopsis thaliana jasmonic acid/ethylene-induced defense pathway by TGA-Interacting glutaredoxins depends on their C-terminal ALWL motif. Mol. Plant 2012, 5:831-840.
    • (2012) Mol. Plant , vol.5 , pp. 831-840
    • Zander, M.1    Chen, S.2    Imkampe, J.3    Thurow, C.4    Gatz, C.5
  • 91
    • 78650171927 scopus 로고    scopus 로고
    • Engineered mutated glutaredoxins mimicking peculiar plant class III glutaredoxins bind iron-sulfur centers and possess reductase activity
    • Couturier J., Didierjean C., Jacquot J.-P., Rouhier N. Engineered mutated glutaredoxins mimicking peculiar plant class III glutaredoxins bind iron-sulfur centers and possess reductase activity. Biochem. Biophys. Res. Comm. 2010, 403:435-441.
    • (2010) Biochem. Biophys. Res. Comm. , vol.403 , pp. 435-441
    • Couturier, J.1    Didierjean, C.2    Jacquot, J.-P.3    Rouhier, N.4
  • 92
    • 49649112131 scopus 로고    scopus 로고
    • Plant immunity requires conformational charges of NPR1 via S-nitrosylation and thioredoxins
    • Tada Y., et al. Plant immunity requires conformational charges of NPR1 via S-nitrosylation and thioredoxins. Science 2008, 321:952-956.
    • (2008) Science , vol.321 , pp. 952-956
    • Tada, Y.1
  • 93
    • 0038826955 scopus 로고    scopus 로고
    • Inducers of plant systemic acquired resistance regulate NPR1 function through redox changes
    • Mou Z., Fan W., Dong X. Inducers of plant systemic acquired resistance regulate NPR1 function through redox changes. Cell 2003, 113:935-944.
    • (2003) Cell , vol.113 , pp. 935-944
    • Mou, Z.1    Fan, W.2    Dong, X.3
  • 94
    • 84922391695 scopus 로고    scopus 로고
    • Selective protein denitrosylation activity of thioredoxin-h5 modulates plant immunity
    • Kneeshaw S., Gelineau S., Tada Y., Loake G.J., Spoel S.H. Selective protein denitrosylation activity of thioredoxin-h5 modulates plant immunity. Mol. Cell 2014, 56:153-162.
    • (2014) Mol. Cell , vol.56 , pp. 153-162
    • Kneeshaw, S.1    Gelineau, S.2    Tada, Y.3    Loake, G.J.4    Spoel, S.H.5
  • 95
    • 0033033724 scopus 로고    scopus 로고
    • Interaction of NPR1 with basic leucine zipper protein transcription factors that bind sequences required for salicylic acid induction of the PR-1 gene
    • Zhang Y., Fan W., Kinkema M., Li X., Dong X. Interaction of NPR1 with basic leucine zipper protein transcription factors that bind sequences required for salicylic acid induction of the PR-1 gene. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:6523-6528.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6523-6528
    • Zhang, Y.1    Fan, W.2    Kinkema, M.3    Li, X.4    Dong, X.5
  • 96
    • 0141746099 scopus 로고    scopus 로고
    • The Arabidopsis NPR1 disease resistance protein is a novel cofactor that confers redox regulation of DNA binding activity to the basic domain/leucine zipper transcription factor TGA1
    • Després C., et al. The Arabidopsis NPR1 disease resistance protein is a novel cofactor that confers redox regulation of DNA binding activity to the basic domain/leucine zipper transcription factor TGA1. Plant Cell 2003, 15:2181-2191.
    • (2003) Plant Cell , vol.15 , pp. 2181-2191
    • Després, C.1
  • 97
    • 71549116712 scopus 로고    scopus 로고
    • Glutaredoxins in development and stress responses of plants
    • Li S., Zachgo S. Glutaredoxins in development and stress responses of plants. Adv. Bot. Res. 2009, 52:333-361.
    • (2009) Adv. Bot. Res. , vol.52 , pp. 333-361
    • Li, S.1    Zachgo, S.2
  • 98
    • 84934443529 scopus 로고    scopus 로고
    • Identification of Thioredoxin Target Disulfides Using Isotope-Coded Affinity Tags
    • Humana Press, Totowa, NJ, J.V. Jorrin-Novo, S. Komatsu, W. Weckwerth, S. Wienkoop (Eds.)
    • Hägglund P., Bunkenborg J., Maeda K., Finnie C., Svensson B. Identification of Thioredoxin Target Disulfides Using Isotope-Coded Affinity Tags. Plant Proteomics 2014, 677-685. Humana Press, Totowa, NJ. J.V. Jorrin-Novo, S. Komatsu, W. Weckwerth, S. Wienkoop (Eds.).
    • (2014) Plant Proteomics , pp. 677-685
    • Hägglund, P.1    Bunkenborg, J.2    Maeda, K.3    Finnie, C.4    Svensson, B.5
  • 99
    • 3242791842 scopus 로고    scopus 로고
    • Thioredoxin targets of developing wheat seeds identified by complementary proteomic approaches
    • Wong J.H., et al. Thioredoxin targets of developing wheat seeds identified by complementary proteomic approaches. Phytochemistry 2004, 65:1629-1640.
    • (2004) Phytochemistry , vol.65 , pp. 1629-1640
    • Wong, J.H.1
  • 100
    • 34447130271 scopus 로고    scopus 로고
    • Thioredoxin-linked proteins are reduced during germination of Medicago truncatula seeds
    • Alkhalfioui F., et al. Thioredoxin-linked proteins are reduced during germination of Medicago truncatula seeds. Plant Physiol. 2007, 144:1559-1579.
    • (2007) Plant Physiol. , vol.144 , pp. 1559-1579
    • Alkhalfioui, F.1
  • 101
    • 79959226194 scopus 로고    scopus 로고
    • On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control
    • Sirover M.A. On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control. Biochim. Biophys. Acta 2011, 1810:741-751.
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 741-751
    • Sirover, M.A.1
  • 102
    • 84904720579 scopus 로고    scopus 로고
    • Thioredoxin and glutaredoxin-mediated redox regulation of ribonucleotide reductase
    • Sengupta R., Holmgren A. Thioredoxin and glutaredoxin-mediated redox regulation of ribonucleotide reductase. World J. Biol. Chem. 2014, 5:68-74.
    • (2014) World J. Biol. Chem. , vol.5 , pp. 68-74
    • Sengupta, R.1    Holmgren, A.2
  • 103
    • 1942501872 scopus 로고    scopus 로고
    • The Arabidopsis cyclophilin gene family
    • Romano P.G., Horton P., Gray J.E. The Arabidopsis cyclophilin gene family. Plant Physiol. 2004, 134:1268-1282.
    • (2004) Plant Physiol. , vol.134 , pp. 1268-1282
    • Romano, P.G.1    Horton, P.2    Gray, J.E.3
  • 104
    • 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. 2004, 101:7475-7480.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 7475-7480
    • Lemaire, S.D.1
  • 105
    • 0038699131 scopus 로고    scopus 로고
    • The small GTPase ran: interpreting the signs
    • Quimby B.B., Dasso M. The small GTPase ran: interpreting the signs. Curr. Opin. Cell Biol. 2003, 15:338-344.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 338-344
    • Quimby, B.B.1    Dasso, M.2
  • 106
    • 84875380058 scopus 로고    scopus 로고
    • Plant 14-3-3 proteins as spiders in a web of phosphorylation
    • Boer A.H., van de Kleeff P.J.M., Gao J. Plant 14-3-3 proteins as spiders in a web of phosphorylation. Protoplasma 2013, 250:425-440.
    • (2013) Protoplasma , vol.250 , pp. 425-440
    • Boer, A.H.1    van de Kleeff, P.J.M.2    Gao, J.3
  • 107
    • 22044451853 scopus 로고    scopus 로고
    • Identification of plant glutaredoxin targets
    • Rouhier N., et al. Identification of plant glutaredoxin targets. Antioxid. Redox Signal. 2005, 7:919-929.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 919-929
    • Rouhier, N.1
  • 109
    • 80051505726 scopus 로고    scopus 로고
    • Plant cell nucleolus as a hot spot for iron
    • Roschzttardtz H., et al. Plant cell nucleolus as a hot spot for iron. J. Biol. Chem. 2011, 286:27863-27866.
    • (2011) J. Biol. Chem. , vol.286 , pp. 27863-27866
    • Roschzttardtz, H.1
  • 110
    • 0037799277 scopus 로고    scopus 로고
    • Redox control of Hsp70-co-chaperone interaction revealed by expression of a thioredoxin-like Arabidopsis protein
    • Vignols F., Mouaheb N., Thomas D., Meyer Y. Redox control of Hsp70-co-chaperone interaction revealed by expression of a thioredoxin-like Arabidopsis protein. J. Biol. Chem. 2003, 278:4516-4523.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4516-4523
    • Vignols, F.1    Mouaheb, N.2    Thomas, D.3    Meyer, Y.4
  • 111
    • 84555209313 scopus 로고    scopus 로고
    • Glutaredoxin GRXS13 plays a key role in protection against photooxidative stress in Arabidopsis
    • Laporte D., et al. Glutaredoxin GRXS13 plays a key role in protection against photooxidative stress in Arabidopsis. J. Exp. Bot. 2012, 63:503-515.
    • (2012) J. Exp. Bot. , vol.63 , pp. 503-515
    • Laporte, D.1
  • 112
    • 84864006177 scopus 로고    scopus 로고
    • Hypoxia triggers meiotic fate acquisition in maize
    • Kelliher T., Walbot V. Hypoxia triggers meiotic fate acquisition in maize. Science 2012, 337:345-348.
    • (2012) Science , vol.337 , pp. 345-348
    • Kelliher, T.1    Walbot, V.2
  • 113
    • 34547698762 scopus 로고    scopus 로고
    • Inactivation of thioredoxin reductases reveals a complex interplay between thioredoxin and glutathione pathways in Arabidopsis development
    • Reichheld J.-P., et al. Inactivation of thioredoxin reductases reveals a complex interplay between thioredoxin and glutathione pathways in Arabidopsis development. Plant Cell 2007, 19:1851-1865.
    • (2007) Plant Cell , vol.19 , pp. 1851-1865
    • Reichheld, J.-P.1
  • 114
    • 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. 2003, 547:151-156.
    • (2003) FEBS Lett. , vol.547 , pp. 151-156
    • Wong, J.H.1
  • 115
    • 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., 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. 2004, 378:497-507.
    • (2004) Biochem. J. , vol.378 , pp. 497-507
    • Maeda, K.1    Finnie, C.2    Svensson, B.3
  • 116
    • 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 2004, 4:2696-2706.
    • (2004) Proteomics , vol.4 , pp. 2696-2706
    • Marchand, C.1
  • 117
    • 33845968455 scopus 로고    scopus 로고
    • Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin
    • Marchand C., Le Maréchal P., Meyer Y., Decottignies P. Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin. Proteomics 2006, 6:6528-6537.
    • (2006) Proteomics , vol.6 , pp. 6528-6537
    • Marchand, C.1    Le Maréchal, P.2    Meyer, Y.3    Decottignies, P.4
  • 118
    • 53149120984 scopus 로고    scopus 로고
    • Redox regulation of Ran GTPase
    • Heo J. Redox regulation of Ran GTPase. Biochem. Biophys. Res. Comm. 2008, 376:568-572.
    • (2008) Biochem. Biophys. Res. Comm. , vol.376 , pp. 568-572
    • Heo, J.1
  • 119
    • 84879710644 scopus 로고    scopus 로고
    • Arabidopsis thaliana: proliferating cell nuclear antigen 1 and 2 possibly form homo- and hetero-trimeric complexes in the plant cell
    • Strzalka W., Aggarwal C. Arabidopsis thaliana: proliferating cell nuclear antigen 1 and 2 possibly form homo- and hetero-trimeric complexes in the plant cell. Plant Signal. Behav. 2013, 8:e24837.
    • (2013) Plant Signal. Behav. , vol.8 , pp. e24837
    • Strzalka, W.1    Aggarwal, C.2
  • 120
    • 84877044940 scopus 로고    scopus 로고
    • Nuclear accumulation of cytosolic glyceraldehyde-3-phosphate dehydrogenase in cadmium-stressed Arabidopsis roots
    • Vescovi M., et al. Nuclear accumulation of cytosolic glyceraldehyde-3-phosphate dehydrogenase in cadmium-stressed Arabidopsis roots. Plant Physiol. 2013, 162:333-346.
    • (2013) Plant Physiol. , vol.162 , pp. 333-346
    • Vescovi, M.1
  • 121
    • 84876544295 scopus 로고    scopus 로고
    • SUBA3: a database for integrating experimentation and prediction to define the SUBcellular location of proteins in Arabidopsis
    • Tanz S.K., et al. SUBA3: a database for integrating experimentation and prediction to define the SUBcellular location of proteins in Arabidopsis. Nucleic Acids Res. 2013, 41:1185-1191.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 1185-1191
    • Tanz, S.K.1
  • 122
    • 0038271813 scopus 로고    scopus 로고
    • An Arabidopsis ran-binding protein, AtRanBP1c, is a co-activator of Ran GTPase-activating protein and requires the C-terminus for its cytoplasmic localization
    • Kim S.-H., Roux S.J. An Arabidopsis ran-binding protein, AtRanBP1c, is a co-activator of Ran GTPase-activating protein and requires the C-terminus for its cytoplasmic localization. Planta 2003, 216:1047-1052.
    • (2003) Planta , vol.216 , pp. 1047-1052
    • Kim, S.-H.1    Roux, S.J.2
  • 123
    • 0031463930 scopus 로고    scopus 로고
    • Localization of 14-3-3 proteins in the nuclei of Arabidopsis and maize
    • Bihn E.A., Paul A.L., Wang S.W., Erdos G.W., Ferl R.J. Localization of 14-3-3 proteins in the nuclei of Arabidopsis and maize. Plant J. 1997, 12:1439-1445.
    • (1997) Plant J. , vol.12 , pp. 1439-1445
    • Bihn, E.A.1    Paul, A.L.2    Wang, S.W.3    Erdos, G.W.4    Ferl, R.J.5
  • 124
    • 84864327019 scopus 로고    scopus 로고
    • Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro
    • Bedhomme M., et al. Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro. Biochem. J. 2012, 445:337-347.
    • (2012) Biochem. J. , vol.445 , pp. 337-347
    • Bedhomme, M.1
  • 125
    • 84881253817 scopus 로고    scopus 로고
    • Mechanisms of nitrosylation and denitrosylation of cytoplasmic glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana
    • Zaffagnini M., et al. Mechanisms of nitrosylation and denitrosylation of cytoplasmic glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana. J. Biol. Chem. 2013, 288:22777-22789.
    • (2013) J. Biol. Chem. , vol.288 , pp. 22777-22789
    • Zaffagnini, M.1
  • 126
    • 33846295570 scopus 로고    scopus 로고
    • Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP 20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions
    • Laxa M., König J., Dietz K.-J., Kandlbinder A. Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP 20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions. Biochem. J. 2007, 401:287-297.
    • (2007) Biochem. J. , vol.401 , pp. 287-297
    • Laxa, M.1    König, J.2    Dietz, K.-J.3    Kandlbinder, A.4


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