메뉴 건너뛰기




Volumn 4, Issue NOV, 2013, Pages

Dissecting the integrative antioxidant and redox systems in plant mitochondria. Effect of stress and S-nitrosylation

Author keywords

Abiotic stress; Ascorbate glutathione cycle; Mitochondria; Peroxiredoxin; S nitrosylation; Signaling; Sulfiredoxin; Thioredoxin

Indexed keywords


EID: 84900874461     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2013.00460     Document Type: Review
Times cited : (71)

References (244)
  • 1
    • 84878003949 scopus 로고    scopus 로고
    • The transcription factor Nrf2 promotes survival by enhancing the expression of uncoupling protein 3 under conditions of oxidative stress
    • doi: 10.1016/j.freeradbiomed.2013.04.007
    • Anedda, A., López-Bernardo, E., Acosta-Iborra, B., Suleiman, M. S., Landázuri, M. O., and Cadenas, S. (2013). The transcription factor Nrf2 promotes survival by enhancing the expression of uncoupling protein 3 under conditions of oxidative stress. Free Radic. Biol. Med. 61, 395-407. doi: 10.1016/j.freeradbiomed.2013.04.007
    • (2013) Free Radic. Biol. Med. , vol.61 , pp. 395-407
    • Anedda, A.1    López-Bernardo, E.2    Acosta-Iborra, B.3    Suleiman, M.S.4    Landázuri, M.O.5    Cadenas, S.6
  • 2
    • 69949167171 scopus 로고
    • Enhanced tolerance to photooxidative stress of transgenic Nicotiana tabacum with high chloroplastic glutathione reductase activity
    • Aono, M., Kubo, A., Saji, H., Tanaka, K., and Kondo, N. (1993). Enhanced tolerance to photooxidative stress of transgenic Nicotiana tabacum with high chloroplastic glutathione reductase activity. Plant Cell Physiol. 34, 129-135.
    • (1993) Plant Cell Physiol. , vol.34 , pp. 129-135
    • Aono, M.1    Kubo, A.2    Saji, H.3    Tanaka, K.4    Kondo, N.5
  • 3
    • 0001662170 scopus 로고
    • Ascorbate free radical reductase: A key enzyme of the ascorbic acid system
    • doi: 10.1016/0014-5793(81)80729-6
    • Arrigoni, O., Dipierro, S., and Borranccino, G. (1981). Ascorbate free radical reductase: a key enzyme of the ascorbic acid system. FEBS Lett. 125, 242-244. doi: 10.1016/0014-5793(81)80729-6
    • (1981) FEBS Lett. , vol.125 , pp. 242-244
    • Arrigoni, O.1    Dipierro, S.2    Borranccino, G.3
  • 4
    • 57249097070 scopus 로고    scopus 로고
    • Biotechnological approach of improving plant salt tolerance using antioxidants as markers
    • doi: 10.1016/j.biotechadv.2008.09.003
    • Ashraf, M. (2009). Biotechnological approach of improving plant salt tolerance using antioxidants as markers. Biotech. Adv. 27, 84-93. doi: 10.1016/j.biotechadv.2008.09.003
    • (2009) Biotech. Adv. , vol.27 , pp. 84-93
    • Ashraf, M.1
  • 5
    • 80052414829 scopus 로고    scopus 로고
    • S-nitrosylation: An emerging post-translational protein modification in plants
    • doi: 10.1016/j.plantsci.2011.02.011
    • Astier, J., Rasul, S., Koen, E., Manzoor, H., Besson-Bard, A., Lamotte, O., et al. (2011). S-nitrosylation: an emerging post-translational protein modification in plants. Plant Sci. 181, 527-533. doi: 10.1016/j.plantsci.2011.02.011
    • (2011) Plant Sci. , vol.181 , pp. 527-533
    • Astier, J.1    Rasul, S.2    Koen, E.3    Manzoor, H.4    Besson-Bard, A.5    Lamotte, O.6
  • 6
    • 38949087227 scopus 로고    scopus 로고
    • Long-term effects of mild salt stress on growth, ion accumulation and superoxide dismutase expression on Arabidopsis rosette leaves
    • doi: 10.1111/j.1399-3054.2007.01009.x
    • Attia, H., Arnaud, N., Karray, N., and Lachaâl, M. (2008). Long-term effects of mild salt stress on growth, ion accumulation and superoxide dismutase expression on Arabidopsis rosette leaves. Physiol. Plant. 132, 293-305. doi: 10.1111/j.1399-3054.2007.01009.x
    • (2008) Physiol. Plant. , vol.132 , pp. 293-305
    • Attia, H.1    Arnaud, N.2    Karray, N.3    Lachaâl, M.4
  • 7
    • 1542381052 scopus 로고    scopus 로고
    • Enhanced tolerance to salt stress and water deficit by overexpressing superoxide dismutase in tobacco (Nicotiana tabacum) chloroplasts
    • doi: 10.1016/j.plantsci.2003.12.007
    • Badawi, G. H., Yamauchi, Y., Shimada, E., Sasaki, R., Kawano, N., Tanaka, K., et al. (2004). Enhanced tolerance to salt stress and water deficit by overexpressing superoxide dismutase in tobacco (Nicotiana tabacum) chloroplasts. Plant Sci. 166, 919-928. doi: 10.1016/j.plantsci.2003.12.007
    • (2004) Plant Sci. , vol.166 , pp. 919-928
    • Badawi, G.H.1    Yamauchi, Y.2    Shimada, E.3    Sasaki, R.4    Kawano, N.5    Tanaka, K.6
  • 8
    • 0030175109 scopus 로고    scopus 로고
    • Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases
    • doi: 10.1007/BF00042228
    • Baier, M., and Dietz, K. J. (1996). Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases. Plant Mol. Biol. 31, 553-564. doi: 10.1007/BF00042228
    • (1996) Plant Mol. Biol. , vol.31 , pp. 553-564
    • Baier, M.1    Dietz, K.J.2
  • 9
    • 10744230621 scopus 로고    scopus 로고
    • Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria
    • doi: 10.1073/pnas.0308583101
    • Balmer, Y., Vensel, W. H., Tanaka, C. K., Hurkman, W. J., Gelhaye, E., Rouhier, N., et al. (2004). Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria. Proc. Natl. Acad. Sci. U.S.A. 101, 2642-2647. doi: 10.1073/pnas.0308583101
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2642-2647
    • Balmer, Y.1    Vensel, W.H.2    Tanaka, C.K.3    Hurkman, W.J.4    Gelhaye, E.5    Rouhier, N.6
  • 10
    • 46849118983 scopus 로고    scopus 로고
    • Thermodynamics of the dimmer-decamer transition of reduced human and plant 2-Cys peroxiredoxin
    • doi: 10.1021/bi8002956
    • Barranco-Medina, S., Kakorin, S., Lázaro, J. J., and Dietz, K. J. (2008a). Thermodynamics of the dimmer-decamer transition of reduced human and plant 2-Cys peroxiredoxin. Biochemistry 47, 7196-7204. doi: 10.1021/bi8002956
    • (2008) Biochemistry , vol.47 , pp. 7196-7204
    • Barranco-Medina, S.1    Kakorin, S.2    Lázaro, J.J.3    Dietz, K.J.4
  • 11
    • 51749120178 scopus 로고    scopus 로고
    • Hexameric oligomerization of mitochondrial peroxiredoxin PrxIIF and formation of an ultrahigh affinity complex with its electron donor thioredoxin Trx-o
    • doi: 10.1093/jxb/ern177
    • Barranco-Medina, S., Krell, T., Bernier-Villamor, L., Sevilla, F., Lázaro, J. J., and Dietz, K. J. (2008b). Hexameric oligomerization of mitochondrial peroxiredoxin PrxIIF and formation of an ultrahigh affinity complex with its electron donor thioredoxin Trx-o. J. Exp. Bot. 59, 3259-3269. doi: 10.1093/jxb/ern177
    • (2008) J. Exp. Bot. , vol.59 , pp. 3259-3269
    • Barranco-Medina, S.1    Krell, T.2    Bernier-Villamor, L.3    Sevilla, F.4    Lázaro, J.J.5    Dietz, K.J.6
  • 12
    • 35048824792 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum
    • doi: 10.1016/j.plaphy.2007.07.017
    • Barranco-Medina, S., Krell, T., Finkemeier, I., Sevilla, F., Lazaro, J. J., and Dietz, K. J. (2007). Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum. Plant Physiol. Biochem. 45, 729-739. doi: 10.1016/j.plaphy.2007.07.017
    • (2007) Plant Physiol. Biochem. , vol.45 , pp. 729-739
    • Barranco-Medina, S.1    Krell, T.2    Finkemeier, I.3    Sevilla, F.4    Lazaro, J.J.5    Dietz, K.J.6
  • 13
    • 67349155642 scopus 로고    scopus 로고
    • The oligomeric conformation of peroxiredoxins links redox state to function
    • doi: 10.1016/j.febslet.2009.05.029
    • Barranco-Medina, S., Lázaro, J. J., and Dietz, K. J. (2009). The oligomeric conformation of peroxiredoxins links redox state to function. FEBS Lett. 583, 1809-1816. doi: 10.1016/j.febslet.2009.05.029
    • (2009) FEBS Lett. , vol.583 , pp. 1809-1816
    • Barranco-Medina, S.1    Lázaro, J.J.2    Dietz, K.J.3
  • 14
    • 33745713185 scopus 로고    scopus 로고
    • Cloning, overexpression, purification and preliminary crystallographic studies of a mitochondrial type II peroxiredoxin from Pisum sativum
    • doi: 10.1107/S1744309106023451
    • Barranco-Medina, S., López-Jaramillo, F. J., Bernier-Villamor, L., Sevilla, F., and Lázaro, J. J. (2006). Cloning, overexpression, purification and preliminary crystallographic studies of a mitochondrial type II peroxiredoxin from Pisum sativum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62, 696-698. doi: 10.1107/S1744309106023451
    • (2006) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.62 , pp. 696-698
    • Barranco-Medina, S.1    López-Jaramillo, F.J.2    Bernier-Villamor, L.3    Sevilla, F.4    Lázaro, J.J.5
  • 15
    • 0034126442 scopus 로고    scopus 로고
    • Ascorbate biosynthesis in mitochondria is linked to the electron transport chain between complexes III and IV
    • doi: 10.1104/pp.123.1.335
    • Bartoli, C. G., Pastori, G. M., and Foyer, C. H. (2000). Ascorbate biosynthesis in mitochondria is linked to the electron transport chain between complexes III and IV. Plant Physiol. 123, 335-344. doi: 10.1104/pp.123.1.335
    • (2000) Plant Physiol. , vol.123 , pp. 335-344
    • Bartoli, C.G.1    Pastori, G.M.2    Foyer, C.H.3
  • 16
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: Implications for mitochondrial redox regulation and antioxidant defense
    • doi: 10.1074/jbc.M408011200
    • Beer, S. M., Taylor, E. R., Brown, S. E., Dahm, C. C., Costa, N. J., Runswick, M. J., et al. (2004). Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant defense. J. Biol. Chem. 279, 47939-47951. doi: 10.1074/jbc.M408011200
    • (2004) J. Biol. Chem. , vol.279 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6
  • 17
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • 1158265
    • Benhar, M., Forrester, M. T., Hess, D. T., and Stamler, J. S. (2008). Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320, 1050-1054.1158265
    • (2008) Science , vol.320 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 18
    • 70349466515 scopus 로고    scopus 로고
    • Protein denitrosylation: Enzymatic mechanisms and cellular functions
    • doi: 10.1038/nrm2764. Epub 2009 Sep 9
    • Benhar, M., Forrester, M. T., and Stamler, J. S. (2009). Protein denitrosylation: enzymatic mechanisms and cellular functions. Nat. Rev. Mol. Cell Biol. 10, 721-732. doi: 10.1038/nrm2764. Epub 2009 Sep 9
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 721-732
    • Benhar, M.1    Forrester, M.T.2    Stamler, J.S.3
  • 19
    • 5144228043 scopus 로고    scopus 로고
    • Cloning and characterization of a 2-Cys peroxiredoxin from Pisum sativum
    • doi: 10.1093/jxb/erh238
    • Bernier-Villamor, L., Navarro, E., Sevilla, F., and Lázaro, J. J. (2004). Cloning and characterization of a 2-Cys peroxiredoxin from Pisum sativum. J. Exp. Bot. 55, 2191-2199. doi: 10.1093/jxb/erh238
    • (2004) J. Exp. Bot. , vol.55 , pp. 2191-2199
    • Bernier-Villamor, L.1    Navarro, E.2    Sevilla, F.3    Lázaro, J.J.4
  • 20
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
    • doi: 10.1038/nature02075
    • Biteau, B., Labarre, J., and Toledano, M. B. (2003). ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425, 980-984. doi: 10.1038/nature02075
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 21
    • 77952055233 scopus 로고    scopus 로고
    • Reactive oxygen species and nitric oxide in plant mitochondria: Origin and redundant regulatory systems
    • doi: 10.1111/j.1399-3054.2009.01340.x
    • Blokhina, O., and Fagerstedt, K. V. (2010). Reactive oxygen species and nitric oxide in plant mitochondria: origin and redundant regulatory systems. Physiol. Plant. 138, 447-462. doi: 10.1111/j.1399-3054.2009.01340.x
    • (2010) Physiol. Plant. , vol.138 , pp. 447-462
    • Blokhina, O.1    Fagerstedt, K.V.2
  • 22
    • 80051578564 scopus 로고    scopus 로고
    • A eukaryotic-like sulfiredoxin involved in oxidative stress responses and in the reduction of the sulfinic form of 2-Cys peroxiredoxin in the cyanobacterium Anabaena PCC 7120
    • doi: 10.1111/j.1469-8137.2011.03774.x
    • Boileau, C., Emele, L., Brochier-Armanet, C., Janicki, A., Zhang, C. C., and Lafiti, A. (2011). A eukaryotic-like sulfiredoxin involved in oxidative stress responses and in the reduction of the sulfinic form of 2-Cys peroxiredoxin in the cyanobacterium Anabaena PCC 7120. New Phytol. 191, 1108-1118. doi: 10.1111/j.1469-8137.2011.03774.x
    • (2011) New Phytol. , vol.191 , pp. 1108-1118
    • Boileau, C.1    Emele, L.2    Brochier-Armanet, C.3    Janicki, A.4    Zhang, C.C.5    Lafiti, A.6
  • 23
    • 80052612768 scopus 로고    scopus 로고
    • Role of peroxidases in the compensation of cytosolic ascorbate peroxidase knockdown in rice plants under abiotic stress
    • doi: 10.1111/j.1365-3040.2011.02366.x
    • Bonifacio, A., Martins, M. O., Ribeiro, C. W., Fontenele, A. V., Carvalho, F. E., Margis-Pinheiro, M., et al. (2011). Role of peroxidases in the compensation of cytosolic ascorbate peroxidase knockdown in rice plants under abiotic stress. Plant Cell Environ. 34, 1705-1722. doi: 10.1111/j.1365-3040.2011.02366.x
    • (2011) Plant Cell Environ. , vol.34 , pp. 1705-1722
    • Bonifacio, A.1    Martins, M.O.2    Ribeiro, C.W.3    Fontenele, A.V.4    Carvalho, F.E.5    Margis-Pinheiro, M.6
  • 24
    • 33644850178 scopus 로고    scopus 로고
    • ABA-induced NO generation and stomatal closure in Arabidopsis are dependent on H2O2 synthesis
    • doi: 10.1111/j.1365-313X.2005.02615.x
    • Bright, J., Desikan, R., Hancock, J. T., Weir, I. S., and Neill, S. J. (2006). ABA-induced NO generation and stomatal closure in Arabidopsis are dependent on H2O2 synthesis. Plant J. 45, 113-122. doi: 10.1111/j.1365-313X.2005.02615.x
    • (2006) Plant J. , vol.45 , pp. 113-122
    • Bright, J.1    Desikan, R.2    Hancock, J.T.3    Weir, I.S.4    Neill, S.J.5
  • 25
    • 2142815107 scopus 로고    scopus 로고
    • Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD
    • doi: 10.1126/science.1095569
    • Budanov, A. V., Sablina, A. A., Feinstein, E., Koonin, E., V., and Chumacov, P. M. (2004). Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD. Science 304, 596-600. doi: 10.1126/science.1095569
    • (2004) Science , vol.304 , pp. 596-600
    • Budanov, A.V.1    Sablina, A.A.2    Feinstein, E.3    Koonin, E.V.4    Chumacov, P.M.5
  • 26
    • 22844442461 scopus 로고    scopus 로고
    • Thioredoxin: Friend or foe in human disease?
    • doi: 10.1016/j.tips.2005.06.005
    • Burke-Gaffney, A., Callister, M. E. J., and Nakamura, H. (2005). Thioredoxin: friend or foe in human disease? Trends Pharmacol. Sci. 26, 398-404. doi: 10.1016/j.tips.2005.06.005
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 398-404
    • Burke-Gaffney, A.1    Callister, M.E.J.2    Nakamura, H.3
  • 27
    • 23144452633 scopus 로고    scopus 로고
    • Interaction between photorespiration and respiration in transgenic potato plants with antisense reduction in glycine decarboxylase
    • doi: 10.1007/s00425-005-1505-9
    • Bykova, N. V., Keerberg, O., Pärnik, T., Bauwe, H., and Gardeström, P. (2005). Interaction between photorespiration and respiration in transgenic potato plants with antisense reduction in glycine decarboxylase. Planta 222, 130-140. doi: 10.1007/s00425-005-1505-9
    • (2005) Planta , vol.222 , pp. 130-140
    • Bykova, N.V.1    Keerberg, O.2    Pärnik, T.3    Bauwe, H.4    Gardeström, P.5
  • 30
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • doi: 10.1073/pnas.91.15.7017
    • Chae, H. Z., Robinson, K., Poole, L. B., Church, G., Storz, G., and Rhee, S. G. (1994). Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc. Natl. Acad. Sci. U.S.A. 91, 7017-7021. doi: 10.1073/pnas.91.15.7017
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robinson, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 31
    • 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
    • doi: 10.1074/jbc.M409482200
    • Chang, T. S., Jeong, W., Wooh, H. A., Lee, S. M., Park, S., and Rhee, S. G. (2004). 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, 50994-51001. doi: 10.1074/jbc.M409482200
    • (2004) J. Biol. Chem. , vol.279 , pp. 50994-51001
    • Chang, T.S.1    Jeong, W.2    Wooh, H.A.3    Lee, S.M.4    Park, S.5    Rhee, S.G.6
  • 32
    • 0037031939 scopus 로고    scopus 로고
    • Overexpressed human mitochondrial thioredoxin confers resistance to oxidant-induced apoptosis in human osteosarcoma cells
    • doi: 10.1074/jbc.M202026200
    • Chen, Y., Cai, J., Murphy, T. J., and Jones, D. P. (2002). Overexpressed human mitochondrial thioredoxin confers resistance to oxidant-induced apoptosis in human osteosarcoma cells. J. Biol. Chem. 277, 33242-33248. doi: 10.1074/jbc.M202026200
    • (2002) J. Biol. Chem. , vol.277 , pp. 33242-33248
    • Chen, Y.1    Cai, J.2    Murphy, T.J.3    Jones, D.P.4
  • 33
    • 0141510042 scopus 로고    scopus 로고
    • Regeneration of peroxiredoxins during recovery after oxidative stress
    • doi: 10.1074/jbc.M305161200
    • Chevallet, M., Wagner, E., Luche, S., van Dorsselaer, A., Leize-Wagner, E., and Rabilloud, T. (2003). Regeneration of peroxiredoxins during recovery after oxidative stress. J. Biol. Chem. 278, 37146-37153. doi: 10.1074/jbc.M305161200
    • (2003) J. Biol. Chem. , vol.278 , pp. 37146-37153
    • Chevallet, M.1    Wagner, E.2    Luche, S.3    van Dorsselaer, A.4    Leize-Wagner, E.5    Rabilloud, T.6
  • 34
    • 0344875538 scopus 로고    scopus 로고
    • Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants
    • doi: 10.1074/jbc.M307525200
    • Chew, O., Whelan, J., and Millar, A. H. (2003). Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants. J. Biol. Chem. 278, 46869-46877. doi: 10.1074/jbc.M307525200
    • (2003) J. Biol. Chem. , vol.278 , pp. 46869-46877
    • Chew, O.1    Whelan, J.2    Millar, A.H.3
  • 35
    • 33746589081 scopus 로고    scopus 로고
    • Alternative oxidases in Arabidopsis: A comparative analysis of differential expression in the gene family provides new insights into function of nonphosphorylating bypasses
    • doi: 10.1016/j.bbabio.2006.03.009
    • Clifton, R., Millar, A. H., and Whelan, J. (2006). Alternative oxidases in Arabidopsis: a comparative analysis of differential expression in the gene family provides new insights into function of nonphosphorylating bypasses. Biochim. Biophys. Acta 1757, 730-741. doi: 10.1016/j.bbabio.2006.03.009
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 730-741
    • Clifton, R.1    Millar, A.H.2    Whelan, J.3
  • 36
    • 16644395716 scopus 로고    scopus 로고
    • Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type
    • doi: 10.1104/pp.104.052233
    • Collin, V., Lamkemeyer, P., Miginiac-Maslow, M., Hirasawa, M., Knaff, D. B., Dietz, K. J., et al. (2004). Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type. Plant Physiol. 136, 4088-4095. doi: 10.1104/pp.104.052233
    • (2004) Plant Physiol. , vol.136 , pp. 4088-4095
    • Collin, V.1    Lamkemeyer, P.2    Miginiac-Maslow, M.3    Hirasawa, M.4    Knaff, D.B.5    Dietz, K.J.6
  • 38
    • 84880613812 scopus 로고    scopus 로고
    • Current overview of S-nitrosoglutathione (GSNO) in higher plants
    • doi:10.3389/fpls.2013.00126. doi: 10.3389/fpls.2013.00126
    • Corpas, F. J., Alché, J. D., and Barroso, J. B. (2013). Current overview of S-nitrosoglutathione (GSNO) in higher plants. Front. Plant Sci. 4:126. doi:10.3389/fpls.2013.00126. doi: 10.3389/fpls.2013.00126
    • (2013) Front. Plant Sci. , vol.4 , pp. 126
    • Corpas, F.J.1    Alché, J.D.2    Barroso, J.B.3
  • 39
    • 0027180149 scopus 로고
    • Evidence for the presence of proteolytic activity in peroxisomes
    • Corpas, F. J., Palma, J. M., and del Río, L. A. (1993). Evidence for the presence of proteolytic activity in peroxisomes. Eur. J. Cell Biol. 61, 81-85.
    • (1993) Eur. J. Cell Biol. , vol.61 , pp. 81-85
    • Corpas, F.J.1    Palma, J.M.2    del Río, L.A.3
  • 40
    • 0039486980 scopus 로고
    • Manipulation of glutathione reductase in transgenic plants: Implications for plants' responses to environmental stress
    • doi: 10.1017/S0269727000014081
    • Creissen, G. P., Broadbent, P., Kular, B., Reynolds, H., Wellburn, A. R., and Mullineaux, P. M. (1994). Manipulation of glutathione reductase in transgenic plants: implications for plants' responses to environmental stress. Proc. R. Soc. Edinb. Biol. Sci. 102, 167-175. doi: 10.1017/S0269727000014081
    • (1994) Proc. R. Soc. Edinb. Biol. Sci. , vol.102 , pp. 167-175
    • Creissen, G.P.1    Broadbent, P.2    Kular, B.3    Reynolds, H.4    Wellburn, A.R.5    Mullineaux, P.M.6
  • 41
    • 0029347014 scopus 로고
    • Simultaneous targeting of pea glutathione reductase and of a bacterial fusion protein to chloroplasts and mitochondria in transgenic tobacco
    • doi: 10.1046/j.1365-313X.1995.08020167.x
    • Creissen, G. P., Reynolds, H., Xue, Y., and Mullineaux, P. (1995). Simultaneous targeting of pea glutathione reductase and of a bacterial fusion protein to chloroplasts and mitochondria in transgenic tobacco. Plant J. 8, 167-175. doi: 10.1046/j.1365-313X.1995.08020167.x
    • (1995) Plant J. , vol.8 , pp. 167-175
    • Creissen, G.P.1    Reynolds, H.2    Xue, Y.3    Mullineaux, P.4
  • 42
    • 84861481905 scopus 로고    scopus 로고
    • Alternative oxidase modulates leaf mitochondrial concentrations of superoxide and nitric oxide
    • doi: 10.1111/j.1469-8137.2012.04166.x
    • Cvetkovska, M., and Vanlerberghe, G. C. (2012). Alternative oxidase modulates leaf mitochondrial concentrations of superoxide and nitric oxide. New Phytol. 195, 32-39. doi: 10.1111/j.1469-8137.2012.04166.x
    • (2012) New Phytol. , vol.195 , pp. 32-39
    • Cvetkovska, M.1    Vanlerberghe, G.C.2
  • 43
    • 70350594364 scopus 로고    scopus 로고
    • Effects of different NaCl concentration on the antioxidant enzymes in oilseed rape (Brassica napus L.) seedlings
    • doi: 10.1007/s10725-009-9402-z
    • Dai, Q., Chen, C., Feng, B., Liu, T. T., Tian, X., Gong, Y. Y., et al. (2009). Effects of different NaCl concentration on the antioxidant enzymes in oilseed rape (Brassica napus L.) seedlings. Plant Growth Regul. 59, 273-278. doi: 10.1007/s10725-009-9402-z
    • (2009) Plant Growth Regul. , vol.59 , pp. 273-278
    • Dai, Q.1    Chen, C.2    Feng, B.3    Liu, T.T.4    Tian, X.5    Gong, Y.Y.6
  • 45
    • 0003026935 scopus 로고    scopus 로고
    • The cyanide-resistant oxidase: To inhibit or not to inhibit, that is the question
    • doi: 10.1104/pp.110.1.1
    • Day, D. A., Krab, K., Lambers, H., Moore, A. L., Siedow, J. N., Wagner, A. M., et al. (1996). The cyanide-resistant oxidase: to inhibit or not to inhibit, that is the question. Plant Physiol. 110, 1-2. doi: 10.1104/pp.110.1.1
    • (1996) Plant Physiol. , vol.110 , pp. 1-2
    • Day, D.A.1    Krab, K.2    Lambers, H.3    Moore, A.L.4    Siedow, J.N.5    Wagner, A.M.6
  • 46
    • 1842716716 scopus 로고    scopus 로고
    • Nitric oxide and nitric oxide synthase activity in plants
    • doi: 10.1016/j.phytochem.2004.02.001
    • del Río, L. A., Corpas, F. J., and Barroso, J. B. (2004). Nitric oxide and nitric oxide synthase activity in plants. Phytochemistry 65, 783-792. doi: 10.1016/j.phytochem.2004.02.001
    • (2004) Phytochemistry , vol.65 , pp. 783-792
    • del Río, L.A.1    Corpas, F.J.2    Barroso, J.B.3
  • 47
    • 0036001078 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidant systems and nitric oxide in peroxisomes
    • doi: 10.1093/jexbot/53.372.1255
    • del Río, L. A., Corpas, F. J., Sandalio, L. M., Palma, J. M., Gómez, M., and Barroso, J. B. (2002). Reactive oxygen species, antioxidant systems and nitric oxide in peroxisomes. J. Exp. Bot. 53, 1255-1272. doi: 10.1093/jexbot/53.372.1255
    • (2002) J. Exp. Bot. , vol.53 , pp. 1255-1272
    • del Río, L.A.1    Corpas, F.J.2    Sandalio, L.M.3    Palma, J.M.4    Gómez, M.5    Barroso, J.B.6
  • 50
    • 0242585515 scopus 로고    scopus 로고
    • Mitochondrial and peroxisomal manganese superoxide dismutase: Differential expression during leaf senescence
    • doi: 10.1093/jxb/erg091
    • del Río, L. A., Sandalio, L. M., Altomare, D. A., and Zilinskas, B. A. (2003). Mitochondrial and peroxisomal manganese superoxide dismutase: differential expression during leaf senescence. J. Exp. Bot. 54; 923-933. doi: 10.1093/jxb/erg091
    • (2003) J. Exp. Bot. , vol.54 , pp. 923-933
    • del Río, L.A.1    Sandalio, L.M.2    Altomare, D.A.3    Zilinskas, B.A.4
  • 51
    • 0026672522 scopus 로고
    • Metabolism of oxygen radicals in peroxisomes and cellular implications
    • doi: 10.1016/0891-5849(92)90150-F
    • del Río, L. A., Sandalio, L. M., Palma, J. M., Bueno, P., and Corpas, F. J. (1992). Metabolism of oxygen radicals in peroxisomes and cellular implications. Free Radic. Biol. Med. 13, 557-580. doi: 10.1016/0891-5849(92)90150-F
    • (1992) Free Radic. Biol. Med. , vol.13 , pp. 557-580
    • del Río, L.A.1    Sandalio, L.M.2    Palma, J.M.3    Bueno, P.4    Corpas, F.J.5
  • 52
    • 33750996449 scopus 로고    scopus 로고
    • Hydrogen peroxide, nitric oxide and cytosolic ascorbate peroxidase at the crossroad between defence and cell death
    • doi: 10.1111/j.1365-313X.2006.02919.x
    • de Pinto, M. C., Paradiso, A., Leonetti, P., and de Gara, L. (2006). Hydrogen peroxide, nitric oxide and cytosolic ascorbate peroxidase at the crossroad between defence and cell death. Plant J. 48, 784-795. doi: 10.1111/j.1365-313X.2006.02919.x
    • (2006) Plant J. , vol.48 , pp. 784-795
    • de Pinto, M.C.1    Paradiso, A.2    Leonetti, P.3    de Gara, L.4
  • 53
    • 77957930036 scopus 로고    scopus 로고
    • A nuclear glutathione cycle within the cell cycle
    • doi: 10.1042/BJ20100409
    • Diaz Vivancos, P., Wolff, T., Markovic, J., Pallardó, F. V., and Foyer, C. H. (2010). A nuclear glutathione cycle within the cell cycle. Biochem. J. 431, 169-178. doi: 10.1042/BJ20100409
    • (2010) Biochem. J. , vol.431 , pp. 169-178
    • Diaz Vivancos, P.1    Wolff, T.2    Markovic, J.3    Pallardó, F.V.4    Foyer, C.H.5
  • 54
    • 33745617040 scopus 로고    scopus 로고
    • The function of peroxiredoxin in plant organelle redox metabolism
    • doi: 10.1093/jxb/erj160
    • Dietz, K. J., Jacob, S., Oelze, M. L., Laxa, M., Tognetti, V., de Miranda, S. B., et al. (2006). The function of peroxiredoxin in plant organelle redox metabolism. J. Exp. Bot. 57, 1697-1709. doi: 10.1093/jxb/erj160
    • (2006) J. Exp. Bot. , vol.57 , pp. 1697-1709
    • Dietz, K.J.1    Jacob, S.2    Oelze, M.L.3    Laxa, M.4    Tognetti, V.5    de Miranda, S.B.6
  • 55
    • 77953116477 scopus 로고    scopus 로고
    • Salt-induced expression of genes related to Na+/K+ and ROS homeostasis in leaves of salt-resistant and salt-sensitive poplar species
    • doi: 10.1007/s11103-010-9612-9
    • Ding, M., Hou, P., Shen, X., Wang, M., Deng, S., Sun, J., et al. (2010). Salt-induced expression of genes related to Na+/K+ and ROS homeostasis in leaves of salt-resistant and salt-sensitive poplar species. Plant Mol. Biol. 73, 251-269. doi: 10.1007/s11103-010-9612-9
    • (2010) Plant Mol. Biol. , vol.73 , pp. 251-269
    • Ding, M.1    Hou, P.2    Shen, X.3    Wang, M.4    Deng, S.5    Sun, J.6
  • 56
    • 33746264833 scopus 로고    scopus 로고
    • Plant thioredoxins are key actors in the oxidative stress response
    • doi: 10.1016/j.tplants.2006.05.005
    • Dos Santos, C. V., and Rey, P. (2006). Plant thioredoxins are key actors in the oxidative stress response. Trends Plant Sci. 11, 329-334. doi: 10.1016/j.tplants.2006.05.005
    • (2006) Trends Plant Sci. , vol.11 , pp. 329-334
    • Dos Santos, C.V.1    Rey, P.2
  • 57
    • 0035212268 scopus 로고    scopus 로고
    • The glycine decarboxylase system: A fascinating complex
    • doi: 10.1016/S1360-1385(01)01892-1
    • Douce, R., Bourguignon, J., Neuburger, M., and Rébeillé, F. (2001). The glycine decarboxylase system: a fascinating complex. Trends Plant Sci. 6, 167-176. doi: 10.1016/S1360-1385(01)01892-1
    • (2001) Trends Plant Sci. , vol.6 , pp. 167-176
    • Douce, R.1    Bourguignon, J.2    Neuburger, M.3    Rébeillé, F.4
  • 58
    • 84877924814 scopus 로고    scopus 로고
    • Dual localized mitochondrial and nuclear proteins as gene expression regulators in plants?
    • doi: 10.3389/fpls.2012.00221
    • Duchêne, A. M., and Giegé, P. (2012). Dual localized mitochondrial and nuclear proteins as gene expression regulators in plants? Front. Plant Sci. 3:221. doi: 10.3389/fpls.2012.00221
    • (2012) Front. Plant Sci. , vol.3 , pp. 221
    • Duchêne, A.M.1    Giegé, P.2
  • 59
    • 33646377888 scopus 로고    scopus 로고
    • Respiratory chain supracomplexes in the plant mitochondria membrane
    • doi: 10.1016/j.tplants.2006.03.007
    • Dudkina, N. V., Heinemeyer, J., Sunderhaus, S., Boekema, E. J., and Braun, H. P. (2006). Respiratory chain supracomplexes in the plant mitochondria membrane. Trends Plant Sci. 11, 232-240. doi: 10.1016/j.tplants.2006.03.007
    • (2006) Trends Plant Sci. , vol.11 , pp. 232-240
    • Dudkina, N.V.1    Heinemeyer, J.2    Sunderhaus, S.3    Boekema, E.J.4    Braun, H.P.5
  • 60
    • 13544263241 scopus 로고    scopus 로고
    • Crystal structure and resolution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: A new insight into the peroxiredoxin oligomerism
    • doi: 10.1021/bi048226s
    • Echalier, A., Trivelli, X., Corbier, C., Rouhier, N., Walker, O., Tsan, P., et al. (2005). Crystal structure and resolution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism. Biochemistry 44, 1755-1767. doi: 10.1021/bi048226s
    • (2005) Biochemistry , vol.44 , pp. 1755-1767
    • Echalier, A.1    Trivelli, X.2    Corbier, C.3    Rouhier, N.4    Walker, O.5    Tsan, P.6
  • 61
    • 0001008314 scopus 로고
    • Subcellular distribution of multiple forms of glutathione reductase in leaves of pea (Pisum sativum L.)
    • doi: 10.1007/BF00194008
    • Edwards, E. A., Rawsthorne, S., and Mullineux, P. M. (1990). Subcellular distribution of multiple forms of glutathione reductase in leaves of pea (Pisum sativum L.). Planta 180, 278-284. doi: 10.1007/BF00194008
    • (1990) Planta , vol.180 , pp. 278-284
    • Edwards, E.A.1    Rawsthorne, S.2    Mullineux, P.M.3
  • 62
    • 33947208011 scopus 로고    scopus 로고
    • Overexpression of monodehydroascorbate reductase in transgenic tobacco confers enhanced tolerance to ozone, salt and polyethylene glycol stresses
    • doi: 10.1007/s00425-006-0417-7
    • Eltayeb, A. E., Kawano, N., Badawi, G. H., Kaminaka, H., Sanekata, T., Shibahara, T., et al. (2007). Overexpression of monodehydroascorbate reductase in transgenic tobacco confers enhanced tolerance to ozone, salt and polyethylene glycol stresses. Planta 225, 1255-1264. doi: 10.1007/s00425-006-0417-7
    • (2007) Planta , vol.225 , pp. 1255-1264
    • Eltayeb, A.E.1    Kawano, N.2    Badawi, G.H.3    Kaminaka, H.4    Sanekata, T.5    Shibahara, T.6
  • 63
    • 79952209397 scopus 로고    scopus 로고
    • Transgenic potato overexpressing Arabidopsis cytosolic AtDHAR1 showed higher tolerance to herbicide, drought and salt stresses
    • doi: 10.1270/jsbbs.61.3
    • Eltayeb, A. E., Yamamoto, S., Habora, M. E. E., Yin, L., Tsujimoto, H., and Tanaka, K. (2011). Transgenic potato overexpressing Arabidopsis cytosolic AtDHAR1 showed higher tolerance to herbicide, drought and salt stresses. Breed. Sci. 61, 3-10. doi: 10.1270/jsbbs.61.3
    • (2011) Breed. Sci. , vol.61 , pp. 3-10
    • Eltayeb, A.E.1    Yamamoto, S.2    Habora, M.E.E.3    Yin, L.4    Tsujimoto, H.5    Tanaka, K.6
  • 64
    • 1842523326 scopus 로고    scopus 로고
    • Crystal structure of a dimeric oxidized form of human peroxiredoxin 5
    • doi: 10.1016/j.jmb.2004.02.017
    • Evrard, C., Capron, A., Marchand, C., Clippe, A., Wattiez, R., Soumillion, P., et al. (2004). Crystal structure of a dimeric oxidized form of human peroxiredoxin 5. J. Mol. Biol. 337, 1079-1090. doi: 10.1016/j.jmb.2004.02.017
    • (2004) J. Mol. Biol. , vol.337 , pp. 1079-1090
    • Evrard, C.1    Capron, A.2    Marchand, C.3    Clippe, A.4    Wattiez, R.5    Soumillion, P.6
  • 65
    • 84855895599 scopus 로고    scopus 로고
    • Proteomics investigation of endogenous S-nitrosylation in Arabidopsis
    • doi: 10.1016/j.bbrc.2011.11.036
    • Fares, A., Rossignol, M., and Peltier, J. B. (2011). Proteomics investigation of endogenous S-nitrosylation in Arabidopsis. Biochem. Biophys. Res. Commun. 416, 331-336. doi: 10.1016/j.bbrc.2011.11.036
    • (2011) Biochem. Biophys. Res. Commun. , vol.416 , pp. 331-336
    • Fares, A.1    Rossignol, M.2    Peltier, J.B.3
  • 66
    • 70350618069 scopus 로고    scopus 로고
    • Sub-cellular distribution of glutathione in an Arabidopsis mutant (vtc1) deficient in ascorbate
    • doi: 10.1016/j.jplph.2009.06.006
    • Fernández-García, N., Martí, M. C., Jiménez, A., Sevilla, F., and Olmos, E. (2009). Sub-cellular distribution of glutathione in an Arabidopsis mutant (vtc1) deficient in ascorbate. J. Plant Physiol. 166, 2004-2012. doi: 10.1016/j.jplph.2009.06.006
    • (2009) J. Plant Physiol. , vol.166 , pp. 2004-2012
    • Fernández-García, N.1    Martí, M.C.2    Jiménez, A.3    Sevilla, F.4    Olmos, E.5
  • 67
    • 33845434556 scopus 로고    scopus 로고
    • Consequences of MnSOD interactions with nitric oxide: Nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide
    • doi: 10.1080/10715760600944296
    • Filipovic, M. R., Stanic, D., Raicevic, S., Spasic, M., and Niketic, V. (2007). Consequences of MnSOD interactions with nitric oxide: nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide. Free Radic. Res. 4, 62-72. doi: 10.1080/10715760600944296
    • (2007) Free Radic. Res. , vol.4 , pp. 62-72
    • Filipovic, M.R.1    Stanic, D.2    Raicevic, S.3    Spasic, M.4    Niketic, V.5
  • 68
    • 79956217269 scopus 로고    scopus 로고
    • Effect of drought and rewatering on the cellular status and antioxidant response of Medicago truncatula plants
    • doi: 10.4161/psb.6.2.14633
    • Filipou, P., Antoniou, C., and Fotopoulus, V. (2011). Effect of drought and rewatering on the cellular status and antioxidant response of Medicago truncatula plants. Plant Signal. Behav. 6, 270-277. doi: 10.4161/psb.6.2.14633
    • (2011) Plant Signal. Behav. , vol.6 , pp. 270-277
    • Filipou, P.1    Antoniou, C.2    Fotopoulus, V.3
  • 69
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • doi: 10.1083/jcb.201102095
    • Finkel, T. (2011). Signal transduction by reactive oxygen species. J. Cell Biol. 194, 7-15. doi: 10.1083/jcb.201102095
    • (2011) J. Cell Biol. , vol.194 , pp. 7-15
    • Finkel, T.1
  • 70
    • 16844368306 scopus 로고    scopus 로고
    • The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress
    • doi: 10.1074/jbc.M413189200
    • Finkemeier, I., Goodman, M., Lankemeyer, P., Kandlbinder, A., Sweetlove, L. J., and Dietz, K. J. (2005). The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress. J. Biol. Chem. 280, 12168-12180. doi: 10.1074/jbc.M413189200
    • (2005) J. Biol. Chem. , vol.280 , pp. 12168-12180
    • Finkemeier, I.1    Goodman, M.2    Lankemeyer, P.3    Kandlbinder, A.4    Sweetlove, L.J.5    Dietz, K.J.6
  • 71
    • 0003121376 scopus 로고
    • Presence of glutathione and glutathione reductase in chloroplasts: A proposed role in ascorbic acid metabolism
    • doi: 10.1007/BF00386001
    • Foyer, C. H., and Halliwell, B. (1976). Presence of glutathione and glutathione reductase in chloroplasts: a proposed role in ascorbic acid metabolism. Planta 133, 21-25. doi: 10.1007/BF00386001
    • (1976) Planta , vol.133 , pp. 21-25
    • Foyer, C.H.1    Halliwell, B.2
  • 72
    • 25844468618 scopus 로고    scopus 로고
    • Redox homeostasis and antioxidant signaling: A metabolic interface between stress perception and physiological responses
    • doi: 10.1105/tpc.105.033589
    • Foyer, C. H., and Noctor, G. (2005). Redox homeostasis and antioxidant signaling: a metabolic interface between stress perception and physiological responses. Plant Cell 17, 1866-1875. doi: 10.1105/tpc.105.033589
    • (2005) Plant Cell , vol.17 , pp. 1866-1875
    • Foyer, C.H.1    Noctor, G.2
  • 73
    • 0242309094 scopus 로고    scopus 로고
    • Redox sensing and signalling associated with reactive oxygen in chloroplasts, peroxisomes and mitochondria
    • doi: 10.1034/j.1399-3054.2003.00223.x
    • Foyer, C. H., and Noctor, G. (2003). Redox sensing and signalling associated with reactive oxygen in chloroplasts, peroxisomes and mitochondria. Physiol. Plant. 119, 355-364. doi: 10.1034/j.1399-3054.2003.00223.x
    • (2003) Physiol. Plant. , vol.119 , pp. 355-364
    • Foyer, C.H.1    Noctor, G.2
  • 74
    • 60749136076 scopus 로고    scopus 로고
    • Redox regulation in photosynthetic organisms: Signaling, acclimation, and practical implications
    • doi: 10.1089/ars.2008.2177
    • Foyer, C. H., and Noctor, G. (2009). Redox regulation in photosynthetic organisms: Signaling, acclimation, and practical implications. Antioxid. Redox Signal. 11, 861-905. doi: 10.1089/ars.2008.2177
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 861-905
    • Foyer, C.H.1    Noctor, G.2
  • 75
    • 78650988662 scopus 로고    scopus 로고
    • Ascorbate and glutathione: The heart of the redox hub
    • doi: 10.1104/pp.110.167569
    • Foyer, C. H., and Noctor, G. (2011). Ascorbate and glutathione: the heart of the redox hub. Plant Physiol. 155, 2-18. doi: 10.1104/pp.110.167569
    • (2011) Plant Physiol. , vol.155 , pp. 2-18
    • Foyer, C.H.1    Noctor, G.2
  • 76
    • 0029410773 scopus 로고
    • Overexpression of glutathione reductase but not glutathione synthetase leads to increases in antioxidant capacity and resistance to photoinhibition in poplar trees
    • doi: 10.1104/pp.109.3.1047
    • Foyer, C. H., Souriau, N., Perret, S., Lelandais, M., Kunert, K. J., Pruvost, C., et al. (1995). Overexpression of glutathione reductase but not glutathione synthetase leads to increases in antioxidant capacity and resistance to photoinhibition in poplar trees. Plant Physiol. 109, 1047-1057. doi: 10.1104/pp.109.3.1047
    • (1995) Plant Physiol. , vol.109 , pp. 1047-1057
    • Foyer, C.H.1    Souriau, N.2    Perret, S.3    Lelandais, M.4    Kunert, K.J.5    Pruvost, C.6
  • 77
    • 80052338563 scopus 로고    scopus 로고
    • The hunt for plant nitric oxide synthase (NOS): Is one really needed?
    • doi: 10.1016/j.plantsci.2011.07.014
    • Fröhlich, A., and Durner, J. (2011). The hunt for plant nitric oxide synthase (NOS): is one really needed? Plant Sci. 181, 401-404. doi: 10.1016/j.plantsci.2011.07.014
    • (2011) Plant Sci. , vol.181 , pp. 401-404
    • Fröhlich, A.1    Durner, J.2
  • 78
    • 33845644110 scopus 로고    scopus 로고
    • The mitochondrial type II peroxiredoxin from poplar
    • doi: 10.1111/j.1399-3054.2006.00785.x
    • Gama, O., Keech, F., Eymery, F., Finkemeier, I., Gelhaye, E., Gardeström, P., et al. (2007). The mitochondrial type II peroxiredoxin from poplar. Physiol. Plant. 129, 196-206. doi: 10.1111/j.1399-3054.2006.00785.x
    • (2007) Physiol. Plant. , vol.129 , pp. 196-206
    • Gama, O.1    Keech, F.2    Eymery, F.3    Finkemeier, I.4    Gelhaye, E.5    Gardeström, P.6
  • 79
    • 5144234728 scopus 로고    scopus 로고
    • A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase
    • doi: 10.1073/pnas.0405282101
    • Gelhaye, E., Rouhier, N., Gérard, J., Jolivet, Y., Gualberto, J., Navrot, N., et al. (2004). A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase. Proc. Natl. Acad. Sci. U.S.A. 101, 14545-14550. doi: 10.1073/pnas.0405282101
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 14545-14550
    • Gelhaye, E.1    Rouhier, N.2    Gérard, J.3    Jolivet, Y.4    Gualberto, J.5    Navrot, N.6
  • 80
    • 16644384217 scopus 로고    scopus 로고
    • The plant thioredoxin system
    • doi: 10.1007/s00018-004-4296-4
    • Gelhaye, E., Rouhier, N., Navrot, N., and Jaquot, J. P. (2005). The plant thioredoxin system. Cell. Mol. Life Sci. 62, 24-35. doi: 10.1007/s00018-004-4296-4
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 24-35
    • Gelhaye, E.1    Rouhier, N.2    Navrot, N.3    Jaquot, J.P.4
  • 81
    • 78049474352 scopus 로고    scopus 로고
    • Reactive oxygen species and antioxidant machinery in abiotic stress tolerance in crop plants
    • doi: 10.1016/j.plaphy.2010.08.016
    • Gill, S. S., and Tuteja, N. (2010). Reactive oxygen species and antioxidant machinery in abiotic stress tolerance in crop plants. Plant Physiol. Biochem. 48, 909-930. doi: 10.1016/j.plaphy.2010.08.016
    • (2010) Plant Physiol. Biochem. , vol.48 , pp. 909-930
    • Gill, S.S.1    Tuteja, N.2
  • 82
    • 67650173467 scopus 로고    scopus 로고
    • The transcription factor ABI4 is a regulator of mitochondrial retrograde expression of alternative oxidase1a
    • doi: 10.1104/pp.109.139782
    • Giraud, E., Van Aken, O., Ho, L. H. M., and Whelan, J. (2009). The transcription factor ABI4 is a regulator of mitochondrial retrograde expression of alternative oxidase1a. Plant Physiol. 150, 1286-1296. doi: 10.1104/pp.109.139782
    • (2009) Plant Physiol. , vol.150 , pp. 1286-1296
    • Giraud, E.1    Van Aken, O.2    Ho, L.H.M.3    Whelan, J.4
  • 83
    • 0142256789 scopus 로고    scopus 로고
    • Differential response of antioxidative enzymes of chloroplasts and mitochondria to long-term NaCl stress of pea plants
    • doi: 10.1080/10715769900301261
    • Gómez, J. M., Hernández, J. A., Jiménez, A., del Río, L. A., and Sevilla, F. (1999). Differential response of antioxidative enzymes of chloroplasts and mitochondria to long-term NaCl stress of pea plants. Free Radic. Res. 31, S11-S18. doi: 10.1080/10715769900301261
    • (1999) Free Radic. Res. , vol.31
    • Gómez, J.M.1    Hernández, J.A.2    Jiménez, A.3    del Río, L.A.4    Sevilla, F.5
  • 84
    • 0347317990 scopus 로고    scopus 로고
    • Location and effects of long-term NaCl stress on superoxide dismutase and ascorbate peroxidase isoenzymes of pea (Pisum sativum cv. Puget) chloroplasts
    • doi: 10.1093/jxb/erh013
    • Gómez, J. M., Jiménez, A., Olmos, E., and Sevilla, F. (2004). Location and effects of long-term NaCl stress on superoxide dismutase and ascorbate peroxidase isoenzymes of pea (Pisum sativum cv. Puget) chloroplasts. J. Exp. Bot. 55, 119-130. doi: 10.1093/jxb/erh013
    • (2004) J. Exp. Bot. , vol.55 , pp. 119-130
    • Gómez, J.M.1    Jiménez, A.2    Olmos, E.3    Sevilla, F.4
  • 85
    • 0345802562 scopus 로고    scopus 로고
    • Nitric oxide production in tobacco leaf cells: A generalized stress response?
    • doi: 10.1046/j.1365-3040.2003.01101.x
    • Gould, K. S., Lamotte, O., Klinuer, A., Pugin, A., and Wendehenne, D. (2003). Nitric oxide production in tobacco leaf cells: a generalized stress response? Plant Cell Environ. 26, 1851-1862. doi: 10.1046/j.1365-3040.2003.01101.x
    • (2003) Plant Cell Environ. , vol.26 , pp. 1851-1862
    • Gould, K.S.1    Lamotte, O.2    Klinuer, A.3    Pugin, A.4    Wendehenne, D.5
  • 86
    • 30644480616 scopus 로고    scopus 로고
    • Arabidopsis nitric oxide synthase1 is targeted to mitochondria and protects against oxidative damage and dark-induced senescence
    • doi: 10.1105/tpc.105.037770
    • Guo, F. Q., and Crawford, N. M. (2005). Arabidopsis nitric oxide synthase1 is targeted to mitochondria and protects against oxidative damage and dark-induced senescence. Plant Cell 17, 3436-3450. doi: 10.1105/tpc.105.037770
    • (2005) Plant Cell , vol.17 , pp. 3436-3450
    • Guo, F.Q.1    Crawford, N.M.2
  • 87
    • 78650858812 scopus 로고    scopus 로고
    • Protein S-nitrosylation in plants: Photorespiratory metabolism and NO signaling
    • jc1. doi: 10.1126/scisignal.2001404
    • Gupta, K. J. (2011). Protein S-nitrosylation in plants: photorespiratory metabolism and NO signaling. Sci. Signal. 4, jc1. doi: 10.1126/scisignal.2001404
    • (2011) Sci. Signal. , vol.4
    • Gupta, K.J.1
  • 88
    • 79957962052 scopus 로고    scopus 로고
    • The anoxic plant mitochondrion as a nitrite: NO reductase
    • doi: 10.1016/j.mito.2011.03.005
    • Gupta, K. J., and Igamberdiev, A. U. (2011). The anoxic plant mitochondrion as a nitrite: NO reductase. Mitochondrion 11, 537-543. doi: 10.1016/j.mito.2011.03.005
    • (2011) Mitochondrion , vol.11 , pp. 537-543
    • Gupta, K.J.1    Igamberdiev, A.U.2
  • 89
    • 80052406379 scopus 로고    scopus 로고
    • The emerging roles of nitric oxide (NO) in plant mitochondria
    • doi: 10.1016/j.plantsci.2011.03.018
    • Gupta, K. J., Igamberdiev, A. U., Manjunatha, G., Segu, S., Moran, J. F., Neelawarne, B., et al. (2011). The emerging roles of nitric oxide (NO) in plant mitochondria. Plant Sci. 181, 520-526. doi: 10.1016/j.plantsci.2011.03.018
    • (2011) Plant Sci. , vol.181 , pp. 520-526
    • Gupta, K.J.1    Igamberdiev, A.U.2    Manjunatha, G.3    Segu, S.4    Moran, J.F.5    Neelawarne, B.6
  • 90
    • 77952893977 scopus 로고    scopus 로고
    • Production and scavenging of nitric oxide by barley root mitochondria
    • doi: 10.1093/pcp/pcq022
    • Gupta, K. J., and Kaiser, W. M. (2010). Production and scavenging of nitric oxide by barley root mitochondria. Plant Cell Physiol. 51, 576-584. doi: 10.1093/pcp/pcq022
    • (2010) Plant Cell Physiol. , vol.51 , pp. 576-584
    • Gupta, K.J.1    Kaiser, W.M.2
  • 91
    • 0034958914 scopus 로고    scopus 로고
    • Mitochondrial adaptations to NaCl. Complex I is protected by anti-oxidants and small heat shock proteins, whereas Complex II is protected by proline and betaine
    • doi: 10.1104/pp.126.3.1266
    • Hamilton, E. W., and Heckathorn, S. A. (2001). Mitochondrial adaptations to NaCl. Complex I is protected by anti-oxidants and small heat shock proteins, whereas Complex II is protected by proline and betaine. Plant Physiol. 126, 1266-1274. doi: 10.1104/pp.126.3.1266
    • (2001) Plant Physiol. , vol.126 , pp. 1266-1274
    • Hamilton, E.W.1    Heckathorn, S.A.2
  • 92
    • 84886728414 scopus 로고    scopus 로고
    • Plant mitochondrial retrograde signaling: Translational modifications enter the stage
    • doi: 10.3389/fpls.2012.00253
    • Hartl, M., and Finkemeier, I. (2012). Plant mitochondrial retrograde signaling: translational modifications enter the stage. Front. Plant Sci. 3:253. doi: 10.3389/fpls.2012.00253
    • (2012) Front. Plant Sci. , vol.3 , pp. 253
    • Hartl, M.1    Finkemeier, I.2
  • 94
    • 78649490845 scopus 로고    scopus 로고
    • Antioxidant-enzyme system as selection criteria for salt tolerance in forage sorghum genotypes (Sorghum bicolor L. Moench)
    • in eds M. Ashraf, M. Ozturk, and H. R. Athar (The Netherlands: Springer), doi: 10.1007/978-1-4020-9065-3_3
    • Hefny, M., and Abdel-Kader, D. Z. (2009). "Antioxidant-enzyme system as selection criteria for salt tolerance in forage sorghum genotypes (Sorghum bicolor L. Moench), " in Salinity and Water Stress, eds M. Ashraf, M. Ozturk, and H. R. Athar (The Netherlands: Springer), 25-36. doi: 10.1007/978-1-4020-9065-3_3
    • (2009) Salinity and Water Stress , pp. 25-36
    • Hefny, M.1    Abdel-Kader, D.Z.2
  • 95
    • 84989714866 scopus 로고
    • Salt-induced oxidative stress mediated by activated oxygen species in pea leaf mitochondria
    • doi: 10.1111/j.1399-3054.1993.tb01792.x
    • Hernández, J. A., Corpas, F. J., Gómez, M., del Río, L. A., and Sevilla, F. (1993). Salt-induced oxidative stress mediated by activated oxygen species in pea leaf mitochondria. Physiol. Plant. 89, 103-108. doi: 10.1111/j.1399-3054.1993.tb01792.x
    • (1993) Physiol. Plant. , vol.89 , pp. 103-108
    • Hernández, J.A.1    Corpas, F.J.2    Gómez, M.3    del Río, L.A.4    Sevilla, F.5
  • 96
    • 0035193531 scopus 로고    scopus 로고
    • Antioxidant systems and O2-/H2O2 production in the apoplast of pea leaves. Its relation with salt-induced necrotic lesions in minor veins
    • doi: 10.1104/pp.010188
    • Hernández, J. A., Ferrer, M. A., Jiménez, A., Barceló, A. R., and Sevilla, F. (2001). Antioxidant systems and O2-/H2O2 production in the apoplast of pea leaves. Its relation with salt-induced necrotic lesions in minor veins. Plant Physiol. 127, 817-831. doi: 10.1104/pp.010188
    • (2001) Plant Physiol. , vol.127 , pp. 817-831
    • Hernández, J.A.1    Ferrer, M.A.2    Jiménez, A.3    Barceló, A.R.4    Sevilla, F.5
  • 97
    • 18744424713 scopus 로고    scopus 로고
    • Tolerance of pea (Pisum sativum L.) to long-term salt stress is associated with induction of antioxidant defenses
    • doi: 10.1046/j.1365-3040.2000.00602.x
    • Hernández, J. A., Jiménez, A., Mullineaux, P., and Sevilla, F. (2000). Tolerance of pea (Pisum sativum L.) to long-term salt stress is associated with induction of antioxidant defenses. Plant Cell Environ. 23, 853-862. doi: 10.1046/j.1365-3040.2000.00602.x
    • (2000) Plant Cell Environ. , vol.23 , pp. 853-862
    • Hernández, J.A.1    Jiménez, A.2    Mullineaux, P.3    Sevilla, F.4
  • 99
    • 84856834347 scopus 로고    scopus 로고
    • Regulation by S-nitrosylation of protein post-translational modification
    • doi: 10.1074/jbc.R111.285742
    • Hess, D. T., and Stamler, J. S. (2012). Regulation by S-nitrosylation of protein post-translational modification. J. Biol. Chem. 287, 4411-4418. doi: 10.1074/jbc.R111.285742
    • (2012) J. Biol. Chem. , vol.287 , pp. 4411-4418
    • Hess, D.T.1    Stamler, J.S.2
  • 100
    • 0030936568 scopus 로고    scopus 로고
    • AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1
    • doi: 10.1073/pnas.94.8.3633
    • Hirota, K., Matsui, M., Iwata, S., Nishiyama, A., Mori, K., and Yodoi, J. (1997). AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc. Natl. Acad. Sci. U.S.A. 94, 3633-3638. doi: 10.1073/pnas.94.8.3633
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 3633-3638
    • Hirota, K.1    Matsui, M.2    Iwata, S.3    Nishiyama, A.4    Mori, K.5    Yodoi, J.6
  • 101
    • 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
    • doi: 10.1016/S0981-9428(02)01396-7
    • 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 Physiol. Biochem. 40, 491-499. doi: 10.1016/S0981-9428(02)01396-7
    • (2002) Plant Physiol. Biochem. , vol.40 , pp. 491-499
    • Horling, F.1    König, J.2    Dietz, K.-J.3
  • 102
    • 0037252527 scopus 로고    scopus 로고
    • Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis
    • doi: 10.1104/pp.010017
    • Horling, F., Lamkemeyer, P., König, J., Finkemeier, I., Kandlbinder, A., Baier, M., et al. (2003). Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis. Plant Physiol. 131, 317-325. doi: 10.1104/pp.010017
    • (2003) Plant Physiol. , vol.131 , pp. 317-325
    • Horling, F.1    Lamkemeyer, P.2    König, J.3    Finkemeier, I.4    Kandlbinder, A.5    Baier, M.6
  • 103
    • 0036944847 scopus 로고    scopus 로고
    • Nitric oxide induces transcriptional activation of the nitric oxide-tolerant alternative oxidase in Arabidopsis suspension cells
    • doi: 10.1007/s00425-002-0828-z
    • Huang, X., von Rad, U., and Durner, J. (2002). Nitric oxide induces transcriptional activation of the nitric oxide-tolerant alternative oxidase in Arabidopsis suspension cells. Planta 215, 914-923. doi: 10.1007/s00425-002-0828-z
    • (2002) Planta , vol.215 , pp. 914-923
    • Huang, X.1    von Rad, U.2    Durner, J.3
  • 105
    • 79551690479 scopus 로고    scopus 로고
    • The dual targeted plant sulfiredoxin retroreduces the sulfinic form of atypical mitochondrial peroxiredoxin
    • doi: 10.1104/pp.110.166504
    • Iglesias-Baena, I., Barranco-Medina, S., Sevilla, F., and Lázaro, J. J. (2011). The dual targeted plant sulfiredoxin retroreduces the sulfinic form of atypical mitochondrial peroxiredoxin. Plant Physiol. 155, 944-955. doi: 10.1104/pp.110.166504
    • (2011) Plant Physiol. , vol.155 , pp. 944-955
    • Iglesias-Baena, I.1    Barranco-Medina, S.2    Sevilla, F.3    Lázaro, J.J.4
  • 106
    • 78649851541 scopus 로고    scopus 로고
    • Wheat mitochondrial proteomes provide new links between antioxidant defense and plant salinity tolerance
    • doi: 10.1021/pr1007834
    • Jacoby, R. P., Millar, A. H., and Taylor, N. L. (2010). Wheat mitochondrial proteomes provide new links between antioxidant defense and plant salinity tolerance. J. Proteome Res. 9, 6595-6604. doi: 10.1021/pr1007834
    • (2010) J. Proteome Res. , vol.9 , pp. 6595-6604
    • Jacoby, R.P.1    Millar, A.H.2    Taylor, N.L.3
  • 107
    • 77952031014 scopus 로고    scopus 로고
    • Reactive oxygen species in abiotic stress signaling
    • doi: 10.1111/j.1399-3054.2009.01321.x
    • Jaspers, P. J., and Kangasjärvi, J. (2010). Reactive oxygen species in abiotic stress signaling. Physiol. Plant. 139, 405-413. doi: 10.1111/j.1399-3054.2009.01321.x
    • (2010) Physiol. Plant. , vol.139 , pp. 405-413
    • Jaspers, P.J.1    Kangasjärvi, J.2
  • 108
    • 33744919853 scopus 로고    scopus 로고
    • Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin
    • doi: 10.1074/jbc.M511082200
    • Jeong, W., Park, S. J., Chang, T. S., Lee, D. Y., and Rhee, G. S. (2006). Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin. J. Biol. Chem. 281, 14400-14407. doi: 10.1074/jbc.M511082200
    • (2006) J. Biol. Chem. , vol.281 , pp. 14400-14407
    • Jeong, W.1    Park, S.J.2    Chang, T.S.3    Lee, D.Y.4    Rhee, G.S.5
  • 109
    • 36848998855 scopus 로고    scopus 로고
    • Comparative proteomic analysis of NaCl stress-responsive proteins in Arabidopsis roots
    • doi: 10.1093/jxb/erm207
    • Jiang, Y., Yang, B., Harris, N. S., and Deyholos, M. K. (2007). Comparative proteomic analysis of NaCl stress-responsive proteins in Arabidopsis roots. J. Exp. Bot. 58, 3591-3607. doi: 10.1093/jxb/erm207
    • (2007) J. Exp. Bot. , vol.58 , pp. 3591-3607
    • Jiang, Y.1    Yang, B.2    Harris, N.S.3    Deyholos, M.K.4
  • 110
    • 0040557481 scopus 로고    scopus 로고
    • Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves
    • Jiménez, A., Hernández, J. A., del Río, L. A., and Sevilla, F. (1997). Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves. Plant Physiol. 114, 275-284.
    • (1997) Plant Physiol. , vol.114 , pp. 275-284
    • Jiménez, A.1    Hernández, J.A.2    del Río, L.A.3    Sevilla, F.4
  • 111
    • 7944239352 scopus 로고    scopus 로고
    • Role of the ascorbate-glutathione cycle of mitochondria and peroxisomes in the senescence of pea leaves
    • doi: 10.1104/pp.118.4.1327
    • Jiménez, A., Hernández, J. A., Pastori, G., del Río, L. A., and Sevilla, F. (1998). Role of the ascorbate-glutathione cycle of mitochondria and peroxisomes in the senescence of pea leaves. Plant Physiol. 118, 1327-1335. doi: 10.1104/pp.118.4.1327
    • (1998) Plant Physiol. , vol.118 , pp. 1327-1335
    • Jiménez, A.1    Hernández, J.A.2    Pastori, G.3    del Río, L.A.4    Sevilla, F.5
  • 112
    • 38749116271 scopus 로고    scopus 로고
    • The peroxiredoxin repair proteins
    • doi: 10.1007/978-1-4020-6051-9_6
    • Jönsson, T. J., and Lowther, W. T. (2007). The peroxiredoxin repair proteins. Subcell. Biochem. 44, 115-141. doi: 10.1007/978-1-4020-6051-9_6
    • (2007) Subcell. Biochem. , vol.44 , pp. 115-141
    • Jönsson, T.J.1    Lowther, W.T.2
  • 113
    • 53049083629 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid in peroxiredoxin by sulfiredoxin proceeds directly through a sulfinic phosphoryl ester intermediate
    • doi: 10.1074/jbc.M803244200
    • Jönsson, T. J., Murray, M. S., Johnson, L. C., and Lowther, W. T. (2008). Reduction of cysteine sulfinic acid in peroxiredoxin by sulfiredoxin proceeds directly through a sulfinic phosphoryl ester intermediate. J. Biol. Chem. 283, 23846-23851. doi: 10.1074/jbc.M803244200
    • (2008) J. Biol. Chem. , vol.283 , pp. 23846-23851
    • Jönsson, T.J.1    Murray, M.S.2    Johnson, L.C.3    Lowther, W.T.4
  • 114
    • 0033383169 scopus 로고    scopus 로고
    • Differential gene expression of rice superoxide dismutase isoforms to oxidative and environmental stresses
    • doi: 10.1080/10715769900301541
    • Kaminaka, H., Morita, S., Tokumoto, M., Masumura, T., and Tanaka, K. (1999). Differential gene expression of rice superoxide dismutase isoforms to oxidative and environmental stresses. Free Radic. Res. 31, S219-S225. doi: 10.1080/10715769900301541
    • (1999) Free Radic. Res. , vol.31
    • Kaminaka, H.1    Morita, S.2    Tokumoto, M.3    Masumura, T.4    Tanaka, K.5
  • 115
    • 38749122130 scopus 로고    scopus 로고
    • Structural survey of the peroxiredoxins
    • doi: 10.1007/978-1-4020-6051-9_3
    • Karplus, P. A., and Hall A. (2007). Structural survey of the peroxiredoxins. Subcell. Biochem. 44, 41-60. doi: 10.1007/978-1-4020-6051-9_3
    • (2007) Subcell. Biochem. , vol.44 , pp. 41-60
    • Karplus, P.A.1    Hall, A.2
  • 116
    • 0023929362 scopus 로고
    • The isolation and purification of a specific "protector" protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed function oxidation system
    • Kim, K., Kim, I. H., and Lee, K.-Y. (1988). The isolation and purification of a specific "protector" protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed function oxidation system. J. Biol. Chem. 263, 4704-4711.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4704-4711
    • Kim, K.1    Kim, I.H.2    Lee, K.-Y.3
  • 117
    • 0037059057 scopus 로고    scopus 로고
    • RNA interference-mediated silencing of Sod2 in Drosophila leads to early adult-onset mortality and elevated endogenous oxidative stress
    • doi: 10.1073/pnas.252342899
    • Kirby, K., Hu, J., Hilliker, A. J., and Phillips, J. P. (2002). RNA interference-mediated silencing of Sod2 in Drosophila leads to early adult-onset mortality and elevated endogenous oxidative stress. Proc. Natl. Acad. Sci. U.S.A. 99, 16162-16167. doi: 10.1073/pnas.252342899
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16162-16167
    • Kirby, K.1    Hu, J.2    Hilliker, A.J.3    Phillips, J.P.4
  • 118
    • 84861709976 scopus 로고    scopus 로고
    • NADPH thioredoxin reductase C is localized in plastids of photosynthetic and nonphotosynthetic tissues and is involved in lateral root formation in Arabidopsis thaliana
    • doi: 10.1105/tpc.111.092304
    • Kirchsteiger, K., Ferrández, J., Pascual, M. B., González, M., and Cejudo, F. J. (2012). NADPH thioredoxin reductase C is localized in plastids of photosynthetic and nonphotosynthetic tissues and is involved in lateral root formation in Arabidopsis thaliana. Plant Cell 24, 1534-1548. doi: 10.1105/tpc.111.092304
    • (2012) Plant Cell , vol.24 , pp. 1534-1548
    • Kirchsteiger, K.1    Ferrández, J.2    Pascual, M.B.3    González, M.4    Cejudo, F.J.5
  • 119
    • 0037117488 scopus 로고    scopus 로고
    • The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy photosynthetic electron flux
    • doi: 10.1073/pnas.072644999
    • König, J., Baier, M., Horling, F., Kahmann, U., Harris, G., Schürman, P., et al. (2002). The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy photosynthetic electron flux. Proc. Natl. Acad. Sci. U.S.A. 99, 5738-5743. doi: 10.1073/pnas.072644999
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5738-5743
    • König, J.1    Baier, M.2    Horling, F.3    Kahmann, U.4    Harris, G.5    Schürman, P.6
  • 120
    • 0042591328 scopus 로고    scopus 로고
    • Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure
    • doi: 10.1074/jbc.M301145200
    • 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. J. Biol. Chem. 278, 24409-24420. doi: 10.1074/jbc.M301145200
    • (2003) J. Biol. Chem. , vol.278 , pp. 24409-24420
    • König, J.1    Lotte, K.2    Plessow, R.3    Brockhinke, A.4    Baier, M.5    Dietz, K.J.6
  • 122
    • 77956704183 scopus 로고    scopus 로고
    • Arabidopsis root growth dependence on glutathione is linked to auxin transport
    • doi: 10.1007/s00299-010-0902-0
    • Koprivova, A., Mugford, S. T., and Kopriva, S. (2010). Arabidopsis root growth dependence on glutathione is linked to auxin transport. Plant Cell Rep. 29, 1157-1167. doi: 10.1007/s00299-010-0902-0
    • (2010) Plant Cell Rep. , vol.29 , pp. 1157-1167
    • Koprivova, A.1    Mugford, S.T.2    Kopriva, S.3
  • 123
    • 84893728188 scopus 로고    scopus 로고
    • Nitric oxide-based protein modification: Formation and site-specificity of protein S-nitrosylation
    • doi: 10.3389/fpls.2013.00137. doi: 10.3389/fpls.2013.00137
    • Kovacs, I., and Lindermayr, C. (2013). Nitric oxide-based protein modification: formation and site-specificity of protein S-nitrosylation. Front. Plant Sci. 4:137. doi: 10.3389/fpls.2013.00137. doi: 10.3389/fpls.2013.00137
    • (2013) Front. Plant Sci. , vol.4 , pp. 137
    • Kovacs, I.1    Lindermayr, C.2
  • 124
    • 33745284271 scopus 로고    scopus 로고
    • Constitutive expression of the human peroxiredoxin V gene contributes to protection of the genome from oxidative DNA lesions and to suppression of transcription of noncoding DNA
    • doi: 10.1111/j.1742-4658.2006.05265.x
    • Kropotov, A., Serikov, V., Suh, J., Smirnova, A., Bashkirov, V., Zhivotovsky, B., et al. (2006). Constitutive expression of the human peroxiredoxin V gene contributes to protection of the genome from oxidative DNA lesions and to suppression of transcription of noncoding DNA. FEBS J. 273, 2607-2617. doi: 10.1111/j.1742-4658.2006.05265.x
    • (2006) FEBS J. , vol.273 , pp. 2607-2617
    • Kropotov, A.1    Serikov, V.2    Suh, J.3    Smirnova, A.4    Bashkirov, V.5    Zhivotovsky, B.6
  • 125
    • 0035923520 scopus 로고    scopus 로고
    • Identification and characterization of a mitochondrial thioredoxin system in plants
    • doi: 10.1073/pnas.241340898
    • Laloi, C., Rayapuram, N., Chartier, Y., Grienenberger, J. M., Bonnard, G., and Meyer, Y. (2001). Identification and characterization of a mitochondrial thioredoxin system in plants. Proc. Natl. Acad. Sci. U.S.A. 98, 14144-14149. doi: 10.1073/pnas.241340898
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14144-14149
    • Laloi, C.1    Rayapuram, N.2    Chartier, Y.3    Grienenberger, J.M.4    Bonnard, G.5    Meyer, Y.6
  • 126
    • 66649083142 scopus 로고    scopus 로고
    • Galactonolactone dehydrogenase requires a redox-sensitive thiol for optimal production of vitamin C
    • doi: 10.1104/pp.109.136929
    • Leferink, N. G. H., van Duijn, E., Barendregt, A., Heck, A. J. R., and van Berkel, W. J. H. (2009). Galactonolactone dehydrogenase requires a redox-sensitive thiol for optimal production of vitamin C. Plant Physiol. 150, 596-605. doi: 10.1104/pp.109.136929
    • (2009) Plant Physiol. , vol.150 , pp. 596-605
    • Leferink, N.G.H.1    van Duijn, E.2    Barendregt, A.3    Heck, A.J.R.4    van Berkel, W.J.H.5
  • 127
    • 84866160686 scopus 로고    scopus 로고
    • Retrograde signaling in plants: From simple to complex scenarios
    • doi: 10.3389/fpls.2012.00135
    • Leister, D. (2012). Retrograde signaling in plants: from simple to complex scenarios. Front. Plant Sci. 3:135. doi: 10.3389/fpls.2012.00135
    • (2012) Front. Plant Sci. , vol.3 , pp. 135
    • Leister, D.1
  • 128
    • 68149114331 scopus 로고    scopus 로고
    • NO signals in the haze. Nitric oxide signalling in plant defence
    • doi: 10.1016/j.pbi.2009.05.012
    • Leitner, M., Vandelle, E., Gaupels, F., Bellin, D., and Delledonne, M. (2009). NO signals in the haze. Nitric oxide signalling in plant defence. Curr. Opin. Plant Biol. 12, 451-458. doi: 10.1016/j.pbi.2009.05.012
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 451-458
    • Leitner, M.1    Vandelle, E.2    Gaupels, F.3    Bellin, D.4    Delledonne, M.5
  • 129
    • 20344377809 scopus 로고    scopus 로고
    • Proteomic identification of S-nitrosylated proteins in Arabidopsis
    • doi: 10.1104/pp.104.058719
    • Lindermayr, C., Saalbach, G., and Durner, J. (2005). Proteomic identification of S-nitrosylated proteins in Arabidopsis. Plant Physiol. 137, 921-930. doi: 10.1104/pp.104.058719
    • (2005) Plant Physiol. , vol.137 , pp. 921-930
    • Lindermayr, C.1    Saalbach, G.2    Durner, J.3
  • 130
    • 33645074141 scopus 로고    scopus 로고
    • Molecular and functional characterization of sulfiredoxin homologs from higher plants
    • doi: 10.1038/sj.cr.7310036
    • Liu, X. P., Liu, X. Y., Zhang, J., Xia, Z. L., Liu, X., Qin, H. J., et al. (2006). Molecular and functional characterization of sulfiredoxin homologs from higher plants. Cell Res. 16, 287-296. doi: 10.1038/sj.cr.7310036
    • (2006) Cell Res. , vol.16 , pp. 287-296
    • Liu, X.P.1    Liu, X.Y.2    Zhang, J.3    Xia, Z.L.4    Liu, X.5    Qin, H.J.6
  • 131
    • 34548570056 scopus 로고    scopus 로고
    • Two rice cytosolic ascorbate peroxidases differentially improve salt tolerance in transgenic Arabidopsis
    • doi: 10.1007/s00299-007-0395-7
    • Lu, Z., Liu, D., and Liu, S. (2007). Two rice cytosolic ascorbate peroxidases differentially improve salt tolerance in transgenic Arabidopsis. Plant Cell Rep. 26, 1909-1917. doi: 10.1007/s00299-007-0395-7
    • (2007) Plant Cell Rep. , vol.26 , pp. 1909-1917
    • Lu, Z.1    Liu, D.2    Liu, S.3
  • 132
    • 84872647922 scopus 로고    scopus 로고
    • Response of mitochondrial antioxidant system and respiratory pathways to reactive nitrogen species in pea leaves
    • doi: 10.1111/j.1399-3054.2012.01654.x
    • Martí, M. C., Florez-Sarasa, I., Camejo, D., Pallol, B., Ortiz, A., Ribas-Carbó, M., et al. (2012). Response of mitochondrial antioxidant system and respiratory pathways to reactive nitrogen species in pea leaves. Physiol. Plant. 147, 194-206. doi: 10.1111/j.1399-3054.2012.01654.x
    • (2012) Physiol. Plant. , vol.147 , pp. 194-206
    • Martí, M.C.1    Florez-Sarasa, I.2    Camejo, D.3    Pallol, B.4    Ortiz, A.5    Ribas-Carbó, M.6
  • 133
    • 79960534184 scopus 로고    scopus 로고
    • Response of the mitochondrial antioxidant redox system and respiration to salinity in pea plants
    • doi: 10.1093/jxb/err076
    • Martí, M. C., Florez-Sarasa, I., Camejo, D., Ribas-Carbó, M., Lázaro, J. J., Sevilla, F., et al. (2011). Response of the mitochondrial antioxidant redox system and respiration to salinity in pea plants. J. Exp. Bot. 62, 3863-3874. doi: 10.1093/jxb/err076
    • (2011) J. Exp. Bot. , vol.62 , pp. 3863-3874
    • Martí, M.C.1    Florez-Sarasa, I.2    Camejo, D.3    Ribas-Carbó, M.4    Lázaro, J.J.5    Sevilla, F.6
  • 134
    • 66649118574 scopus 로고    scopus 로고
    • Mitochondrial and nuclear localization of a novel pea thioredoxin: Identification of its mitochondrial target proteins
    • doi: 10.1104/pp.109.138073
    • Martí, M. C., Olmos, E., Calvete, J. J., Díaz, I., Barranc-Medina, S., Whelan, J., et al. (2009). Mitochondrial and nuclear localization of a novel pea thioredoxin: identification of its mitochondrial target proteins. Plant Physiol. 150, 646-657. doi: 10.1104/pp.109.138073
    • (2009) Plant Physiol. , vol.150 , pp. 646-657
    • Martí, M.C.1    Olmos, E.2    Calvete, J.J.3    Díaz, I.4    Barranc-Medina, S.5    Whelan, J.6
  • 135
    • 0033529335 scopus 로고    scopus 로고
    • The alternative oxidase lowers mitochondrial reactive oxygen production in plant cells
    • doi: 10.1073/pnas.96.14.8271
    • Maxwell, D. P., Wang, Y., and McIntosh, L. (1999). The alternative oxidase lowers mitochondrial reactive oxygen production in plant cells. Proc. Natl. Acad. Sci. U.S.A. 96, 8271-8276. doi: 10.1073/pnas.96.14.8271
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 8271-8276
    • Maxwell, D.P.1    Wang, Y.2    McIntosh, L.3
  • 136
    • 1242300119 scopus 로고    scopus 로고
    • Salt stress induces altered expression of genes encoding antioxidant enzymes in seedlings of a Brazilian indica rice (Oryza sativa L.)
    • doi: 10.1016/j.plantsci.2003.10.001
    • Menezes-Benavente, L., Teixeira, F. K., Kamei, C. L. A., and Margis-Pinheiro, M. (2004). Salt stress induces altered expression of genes encoding antioxidant enzymes in seedlings of a Brazilian indica rice (Oryza sativa L.). Plant Sci. 166, 323-331. doi: 10.1016/j.plantsci.2003.10.001
    • (2004) Plant Sci. , vol.166 , pp. 323-331
    • Menezes-Benavente, L.1    Teixeira, F.K.2    Kamei, C.L.A.3    Margis-Pinheiro, M.4
  • 137
    • 84865411350 scopus 로고    scopus 로고
    • Thioredoxin and glutaredoxin systems in plants: Molecular mechanisms, crosstalks, and functional significance
    • doi: 10.1089/ars.2011.4327
    • Meyer, Y., Belin, C., Delorme-Hinoux, V., Reichheld, J. P., Riondet, C., and Meyer, Y. (2012). Thioredoxin and glutaredoxin systems in plants: molecular mechanisms, crosstalks, and functional significance. Antioxid. Redox Signal. 17, 1124-1160. doi: 10.1089/ars.2011.4327
    • (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    Meyer, Y.6
  • 138
    • 33644818614 scopus 로고    scopus 로고
    • Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine
    • doi: 10.1038/nchembio720
    • Mitchell, D. A., and Marletta, M. A. (2005). Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine. Nat. Chem. Biol. 1, 154-158. doi: 10.1038/nchembio720
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 154-158
    • Mitchell, D.A.1    Marletta, M.A.2
  • 139
    • 0034844069 scopus 로고    scopus 로고
    • Unraveling the role of mitochondria during oxidative stress in plants
    • doi: 10.1080/152165401753311735
    • Millar, A. H., Considine, M. J., Day, D. A., and Whelan, J. (2001). Unraveling the role of mitochondria during oxidative stress in plants. IUBMB Life 51, 201-205. doi: 10.1080/152165401753311735
    • (2001) IUBMB Life , vol.51 , pp. 201-205
    • Millar, A.H.1    Considine, M.J.2    Day, D.A.3    Whelan, J.4
  • 140
    • 0030566801 scopus 로고    scopus 로고
    • Nitric oxide inhibits the cytochrome oxidase but not the alternative oxidase of plant mitochondria
    • doi: 10.1016/S0014-5793(96)01230-6
    • Millar, A. H., and Day, D. A. (1996). Nitric oxide inhibits the cytochrome oxidase but not the alternative oxidase of plant mitochondria. FEBS Lett. 398, 155-158. doi: 10.1016/S0014-5793(96)01230-6
    • (1996) FEBS Lett. , vol.398 , pp. 155-158
    • Millar, A.H.1    Day, D.A.2
  • 141
    • 0142183502 scopus 로고    scopus 로고
    • Control of ascorbate synthesis by respiration and its implications for stress responses
    • doi: 10.1104/pp.103.028399
    • Millar, A. H., Mittova, V., Kiddle, G., Heazlewood, J. L., Bartoli, C. G., Theodoulou, F. L., et al. (2003). Control of ascorbate synthesis by respiration and its implications for stress responses. Plant Physiol. 133, 443-447. doi: 10.1104/pp.103.028399
    • (2003) Plant Physiol. , vol.133 , pp. 443-447
    • Millar, A.H.1    Mittova, V.2    Kiddle, G.3    Heazlewood, J.L.4    Bartoli, C.G.5    Theodoulou, F.L.6
  • 142
    • 79955639890 scopus 로고    scopus 로고
    • Organization and regulation of mitochondrial respiration in plants
    • doi: 10.1146/annurev-arplant-042110-103857
    • Millar, A. H., Whelan, J., Soole, K. L., and Day, D. A. (2011). Organization and regulation of mitochondrial respiration in plants. Annu. Rev. Plant Biol. 62, 79-104. doi: 10.1146/annurev-arplant-042110-103857
    • (2011) Annu. Rev. Plant Biol. , vol.62 , pp. 79-104
    • Millar, A.H.1    Whelan, J.2    Soole, K.L.3    Day, D.A.4
  • 144
    • 66649095648 scopus 로고    scopus 로고
    • Prediction of dual protein targeting to plant organelles
    • doi: 10.1111/j.1469-8137.2009.02832.x
    • Mitschke, J., Fuss, J., Blum, T., Höglund, A., Reski, R., Kohlbacher, O., et al. (2009). Prediction of dual protein targeting to plant organelles. New Phytol. 183, 224-235. doi: 10.1111/j.1469-8137.2009.02832.x
    • (2009) New Phytol. , vol.183 , pp. 224-235
    • Mitschke, J.1    Fuss, J.2    Blum, T.3    Höglund, A.4    Reski, R.5    Kohlbacher, O.6
  • 145
    • 2442444152 scopus 로고    scopus 로고
    • Salinity up-regulates the antioxidative system in root mitochondria and peroxisomes of the wild salt-tolerant tomato species Lycopersicon pennellii
    • doi: 10.1093/jxb/erh113
    • Mittova, V., Guy, M., Tal, M., and Volokita, M. (2004). Salinity up-regulates the antioxidative system in root mitochondria and peroxisomes of the wild salt-tolerant tomato species Lycopersicon pennellii. J. Exp. Bot. 55, 1105-1113. doi: 10.1093/jxb/erh113
    • (2004) J. Exp. Bot. , vol.55 , pp. 1105-1113
    • Mittova, V.1    Guy, M.2    Tal, M.3    Volokita, M.4
  • 146
    • 0037708395 scopus 로고    scopus 로고
    • Up-regulation of the leaf mitochondrial and peroxisomal antioxidative systems in response to salt-induced oxidative stress in the wild salt-tolerant tomato species Lycopersicon pennellii
    • doi: 10.1046/j.1365-3040.2003.01016.x
    • Mittova, V., Tal, M., Volokita, M., and Guy, M. (2003). Up-regulation of the leaf mitochondrial and peroxisomal antioxidative systems in response to salt-induced oxidative stress in the wild salt-tolerant tomato species Lycopersicon pennellii. Plant Cell Environ. 26, 845-856. doi: 10.1046/j.1365-3040.2003.01016.x
    • (2003) Plant Cell Environ. , vol.26 , pp. 845-856
    • Mittova, V.1    Tal, M.2    Volokita, M.3    Guy, M.4
  • 147
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitocondria and oxidative stress: Electron transport, NADPH turnover and metabolism of reactive oxygen species
    • doi: 10.1146/annurev.arplant.52.1.561
    • Moller, I. M. (2001). Plant mitocondria and oxidative stress: electron transport, NADPH turnover and metabolism of reactive oxygen species. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52, 561-591. doi: 10.1146/annurev.arplant.52.1.561
    • (2001) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.52 , pp. 561-591
    • Moller, I.M.1
  • 148
    • 50649115800 scopus 로고    scopus 로고
    • Decrease in manganese superoxide dismutase leads to reduced root growth and affects tricarboxylic acid cycle flux and mitochondrial redox homeostasis
    • doi: 10.1104/pp.107.113613
    • Morgan, M. J., Lehmann, M., Schwarzländer, M., Baxter, C. J., Sienkiewicz-Porzucek, A., Williams, T. C. R., et al. (2008). Decrease in manganese superoxide dismutase leads to reduced root growth and affects tricarboxylic acid cycle flux and mitochondrial redox homeostasis. Plant Physiol. 147, 101-114. doi: 10.1104/pp.107.113613
    • (2008) Plant Physiol. , vol.147 , pp. 101-114
    • Morgan, M.J.1    Lehmann, M.2    Schwarzländer, M.3    Baxter, C.J.4    Sienkiewicz-Porzucek, A.5    Williams, T.C.R.6
  • 149
    • 29944447039 scopus 로고    scopus 로고
    • Glutathione, photosynthesis and the redox regulation of stress-responsive gene expression
    • doi: 10.1007/s11120-005-8811-8
    • Mullineaux, P. M., and Rausch, T. (2005). Glutathione, photosynthesis and the redox regulation of stress-responsive gene expression. Photosynth. Res. 86, 459-474. doi: 10.1007/s11120-005-8811-8
    • (2005) Photosynth. Res. , vol.86 , pp. 459-474
    • Mullineaux, P.M.1    Rausch, T.2
  • 150
    • 84871752316 scopus 로고    scopus 로고
    • The impact of global change factors on redox signaling underpinning stress tolerance
    • doi: 10.1104/pp.112.205690
    • Munné-Bosch, S., Queval, G., and Foyer, C. H. (2013). The impact of global change factors on redox signaling underpinning stress tolerance. Plant Physiol. 161, 5-19. doi: 10.1104/pp.112.205690
    • (2013) Plant Physiol. , vol.161 , pp. 5-19
    • Munné-Bosch, S.1    Queval, G.2    Foyer, C.H.3
  • 151
    • 0038715782 scopus 로고    scopus 로고
    • Nitric oxide signalling in plants
    • doi: 10.1046/j.1469-8137.2003.00804.x
    • Neill, S. J., Desikan, R., and Hancock, J. T. (2003). Nitric oxide signalling in plants. New Phytol. 159, 11-35. doi: 10.1046/j.1469-8137.2003.00804.x
    • (2003) New Phytol. , vol.159 , pp. 11-35
    • Neill, S.J.1    Desikan, R.2    Hancock, J.T.3
  • 152
    • 33847613456 scopus 로고    scopus 로고
    • Mitochondrial redox biology and homeostasis in plants
    • doi: 10.1016/j.tplants.2007.01.005
    • Noctor, G., De Paepe, R., and Foyer, C. H. (2007). Mitochondrial redox biology and homeostasis in plants. Trends Plant Sci. 12, 125-134. doi: 10.1016/j.tplants.2007.01.005
    • (2007) Trends Plant Sci. , vol.12 , pp. 125-134
    • Noctor, G.1    De Paepe, R.2    Foyer, C.H.3
  • 153
    • 0031735647 scopus 로고    scopus 로고
    • Ascorbate and glutathione: Keeping active oxygen under control
    • doi: 10.1146/annurev.arplant.49.1.249
    • Noctor, G., and Foyer, C. H. (1998). Ascorbate and glutathione: keeping active oxygen under control. Annu. Rev. Plant Physiol. Plant Mol. Biol. 49, 249-279. doi: 10.1146/annurev.arplant.49.1.249
    • (1998) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.49 , pp. 249-279
    • Noctor, G.1    Foyer, C.H.2
  • 155
    • 67649279837 scopus 로고    scopus 로고
    • Sulfiredoxin translocation into mitochondria plays a crucial role in reducing hyperoxidized peroxiredoxin III
    • doi: 10.1074/jbc.M808981200
    • Noh, Y. H., Baek, J. Y., Jeong, W., Rhee, S. G., and Chang, T. S. (2009). Sulfiredoxin translocation into mitochondria plays a crucial role in reducing hyperoxidized peroxiredoxin III. J. Biol. Chem. 284, 8470-8477. doi: 10.1074/jbc.M808981200
    • (2009) J. Biol. Chem. , vol.284 , pp. 8470-8477
    • Noh, Y.H.1    Baek, J.Y.2    Jeong, W.3    Rhee, S.G.4    Chang, T.S.5
  • 156
    • 0036348737 scopus 로고    scopus 로고
    • The use of multiple transcription starts causes the dual targeting of Arabidopsis putative monodehydroascorbate reductase to both mitochondria and chloroplasts
    • doi: 10.1093/pcp/pcf103
    • Obara, K., Sumi, K., and Fukuda, H. (2002). The use of multiple transcription starts causes the dual targeting of Arabidopsis putative monodehydroascorbate reductase to both mitochondria and chloroplasts. Plant Cell Physiol. 43, 697-705. doi: 10.1093/pcp/pcf103
    • (2002) Plant Cell Physiol. , vol.43 , pp. 697-705
    • Obara, K.1    Sumi, K.2    Fukuda, H.3
  • 157
    • 0028192180 scopus 로고
    • Induction of several antioxidant enzymes in the selection of a salt-tolerant cell-line of Pisum sativum
    • doi: 10.1016/S0176-1617(11)82142-5
    • Olmos, E., Hernández, J. A., Sevilla, F., and Hellín, E. (1994). Induction of several antioxidant enzymes in the selection of a salt-tolerant cell-line of Pisum sativum. J. Plant Physiol. 144, 594-598. doi: 10.1016/S0176-1617(11)82142-5
    • (1994) J. Plant Physiol. , vol.144 , pp. 594-598
    • Olmos, E.1    Hernández, J.A.2    Sevilla, F.3    Hellín, E.4
  • 158
    • 79251566511 scopus 로고    scopus 로고
    • Circadian clocks in human red blood cells
    • doi: 10.1038/nature09702
    • O'Neill, J. S., and Reddy, A. B. (2011). Circadian clocks in human red blood cells. Nature 469, 498-504. doi: 10.1038/nature09702
    • (2011) Nature , vol.469 , pp. 498-504
    • O'Neill, J.S.1    Reddy, A.B.2
  • 159
  • 160
    • 0034106709 scopus 로고    scopus 로고
    • The control of ascorbic acid synthesis and turnover pea seedlings
    • doi: 10.1093/jexbot/51.345.669
    • Pallanca, J. E., and Smirnoff, N. (2000). The control of ascorbic acid synthesis and turnover pea seedlings. J. Exp. Bot. 51, 669-674. doi: 10.1093/jexbot/51.345.669
    • (2000) J. Exp. Bot. , vol.51 , pp. 669-674
    • Pallanca, J.E.1    Smirnoff, N.2
  • 161
    • 33745605509 scopus 로고    scopus 로고
    • Antioxidative enzymes from chloroplasts, mitochondria and peroxisomes during leaf senescence of nodulated pea plants
    • doi: 10.1093/jxb/erj191
    • Palma, J. M., Jiménez, A., Sandalio, L. M., Corpas, F. J., Lundqvist, M., Gómez, M., et al. (2006). Antioxidative enzymes from chloroplasts, mitochondria and peroxisomes during leaf senescence of nodulated pea plants. J. Exp. Bot. 57, 1747-1758. doi: 10.1093/jxb/erj191
    • (2006) J. Exp. Bot. , vol.57 , pp. 1747-1758
    • Palma, J.M.1    Jiménez, A.2    Sandalio, L.M.3    Corpas, F.J.4    Lundqvist, M.5    Gómez, M.6
  • 162
    • 77949534774 scopus 로고    scopus 로고
    • Regulation of plant glycine decarboxylase by S-nitrosylation and glutathionylation
    • doi: 10.1104/pp.109.152579
    • Palmieri, M. C., Lindermayr, C., Bauwe, H., Steinhauser, C., and Durner, J. (2010). Regulation of plant glycine decarboxylase by S-nitrosylation and glutathionylation. Plant Physiol. 152, 1514-1528. doi: 10.1104/pp.109.152579
    • (2010) Plant Physiol. , vol.152 , pp. 1514-1528
    • Palmieri, M.C.1    Lindermayr, C.2    Bauwe, H.3    Steinhauser, C.4    Durner, J.5
  • 163
    • 78049372675 scopus 로고    scopus 로고
    • Overexpresion of 2-Cys peroxiredoxin in prokariotes: Cyanobacterial 2-Cys peroxiredoxins sensitive to oxidative stress
    • doi: 10.1074/jbc.M110.160465
    • Pascual, M. B., Mata-Cabana, A., Florencio, F. J., Lindahl, M., and Cejudo, F. J. (2010). Overexpresion of 2-Cys peroxiredoxin in prokariotes: cyanobacterial 2-Cys peroxiredoxins sensitive to oxidative stress. J. Biol. Chem. 285, 34485-34492. doi: 10.1074/jbc.M110.160465
    • (2010) J. Biol. Chem. , vol.285 , pp. 34485-34492
    • Pascual, M.B.1    Mata-Cabana, A.2    Florencio, F.J.3    Lindahl, M.4    Cejudo, F.J.5
  • 164
    • 33846841016 scopus 로고    scopus 로고
    • Possible plant mitochondria involvement in cell adaptation to drought stress. A case study: Durum wheat mitochondria
    • doi: 10.1093/jxb/erl273
    • Pastore, D., Trono, D., Laus, M. N., Di Fonzo, N., and Flagella, Z. (2007). Possible plant mitochondria involvement in cell adaptation to drought stress. A case study: durum wheat mitochondria. J. Exp. Bot. 58, 195-210. doi: 10.1093/jxb/erl273
    • (2007) J. Exp. Bot. , vol.58 , pp. 195-210
    • Pastore, D.1    Trono, D.2    Laus, M.N.3    Di Fonzo, N.4    Flagella, Z.5
  • 165
    • 33749233825 scopus 로고    scopus 로고
    • Rice NTRC is a high-efficiency redox system for chloroplast protection against oxidative damage
    • doi: 10.1105/tpc.106.041541
    • Pérez-Ruiz, J. M., Spinola, M. C., Kirchsteiger, K., Moreno, J., Sahrawy, M., and Cejudo, F. J. (2006). Rice NTRC is a high-efficiency redox system for chloroplast protection against oxidative damage. Plant Cell 18, 2356-2368. doi: 10.1105/tpc.106.041541
    • (2006) Plant Cell , vol.18 , pp. 2356-2368
    • Pérez-Ruiz, J.M.1    Spinola, M.C.2    Kirchsteiger, K.3    Moreno, J.4    Sahrawy, M.5    Cejudo, F.J.6
  • 166
    • 57749094920 scopus 로고    scopus 로고
    • L-Galactono-1,4-lactone dehydrogenase is required for the accumulation of plant respiratory complex I
    • doi: 10.1074/jbc.M805320200
    • Pineau, B., Layoune, O., Danon, A., and De Paepe, R. (2008). L-Galactono-1,4-lactone dehydrogenase is required for the accumulation of plant respiratory complex I. J. Biol. Chem. 283, 32500-32505. doi: 10.1074/jbc.M805320200
    • (2008) J. Biol. Chem. , vol.283 , pp. 32500-32505
    • Pineau, B.1    Layoune, O.2    Danon, A.3    De Paepe, R.4
  • 167
    • 14844289535 scopus 로고    scopus 로고
    • Nitric oxide emission from tobacco leaves and cell suspensions: Rate limiting factors and evidence for their involvement of mitochondrial electron transport
    • doi: 10.1111/j.1365-313X.2005.02335.x
    • Planchet, E., Gupta, K. J., Sonoda, M., and Kaiser, W. M. (2005). Nitric oxide emission from tobacco leaves and cell suspensions: rate limiting factors and evidence for their involvement of mitochondrial electron transport. Plant J. 41 732-743. doi: 10.1111/j.1365-313X.2005.02335.x
    • (2005) Plant J. , vol.41 , pp. 732-743
    • Planchet, E.1    Gupta, K.J.2    Sonoda, M.3    Kaiser, W.M.4
  • 168
    • 0029986691 scopus 로고    scopus 로고
    • Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles
    • doi: 10.1006/abbi.1996.0146
    • Poderoso, J. J., Carreras, M. C., Lisdero, C., Riobó, N., Schöpfer, F., and Boveris, A. (1996). Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles. Arch. Biochem. Biophys. 328, 85-92. doi: 10.1006/abbi.1996.0146
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 85-92
    • Poderoso, J.J.1    Carreras, M.C.2    Lisdero, C.3    Riobó, N.4    Schöpfer, F.5    Boveris, A.6
  • 169
    • 0036619384 scopus 로고    scopus 로고
    • Ascorbate and glutathione: Guardians of the cell cycle, partners in crime?
    • doi: 10.1016/S0981-9428(02)01414-6
    • Potters, G., De Gara, L., Asard, H., and Horemans, N. (2002). Ascorbate and glutathione: guardians of the cell cycle, partners in crime? Plant Physiol. Biochem. 40, 537-548. doi: 10.1016/S0981-9428(02)01414-6
    • (2002) Plant Physiol. Biochem. , vol.40 , pp. 537-548
    • Potters, G.1    De Gara, L.2    Asard, H.3    Horemans, N.4
  • 170
    • 34247562746 scopus 로고    scopus 로고
    • How can organellar protein N-terminal sequences be dual targeting sigmals? In silico analysis and mutagenesis approach
    • doi: 10.1016/j.jmb.2007.03.015
    • Pujol, C., Maréchal-Drouard, L., and Duchêne, A. M. (2007). How can organellar protein N-terminal sequences be dual targeting sigmals? In silico analysis and mutagenesis approach. J. Mol. Biol. 369, 356-367. doi: 10.1016/j.jmb.2007.03.015
    • (2007) J. Mol. Biol. , vol.369 , pp. 356-367
    • Pujol, C.1    Maréchal-Drouard, L.2    Duchêne, A.M.3
  • 171
    • 58149131296 scopus 로고    scopus 로고
    • An antioxidant redox system in the nucleus of wheat seed cells suffering oxidative stress
    • doi: 10.1111/j.1365-313X.2008.03675.x
    • Pulido, P., Cazalis, R., and Cejudo, F. J. (2009). An antioxidant redox system in the nucleus of wheat seed cells suffering oxidative stress. Plant J. 57, 132-145. doi: 10.1111/j.1365-313X.2008.03675.x
    • (2009) Plant J. , vol.57 , pp. 132-145
    • Pulido, P.1    Cazalis, R.2    Cejudo, F.J.3
  • 172
    • 77956568987 scopus 로고    scopus 로고
    • Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts
    • doi: 10.1093/jxb/erq218
    • Pulido, P., Spinola, M. C., Kirchsteiger, K., Guinea, M., Pascual, M. B., Sahrawy, M., et al. (2010). Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts. J. Exp. Bot. 61, 4043-4054. doi: 10.1093/jxb/erq218
    • (2010) J. Exp. Bot. , vol.61 , pp. 4043-4054
    • Pulido, P.1    Spinola, M.C.2    Kirchsteiger, K.3    Guinea, M.4    Pascual, M.B.5    Sahrawy, M.6
  • 173
    • 20044388711 scopus 로고    scopus 로고
    • Legume nodule senescence: Roles for redox and hormone signalling in the orchestration of the natural aging process
    • doi: 10.1111/j.1469-8137.2004.01285.x
    • Puppo, A., Groten, K., Bastian, F., Carzaniga, R., Soussi, M., Lucas, M. M., et al. (2005). Legume nodule senescence: roles for redox and hormone signalling in the orchestration of the natural aging process. New Phytol. 165, 683-701. doi: 10.1111/j.1469-8137.2004.01285.x
    • (2005) New Phytol. , vol.165 , pp. 683-701
    • Puppo, A.1    Groten, K.2    Bastian, F.3    Carzaniga, R.4    Soussi, M.5    Lucas, M.M.6
  • 174
    • 70450267629 scopus 로고    scopus 로고
    • Alternative oxidase: A defence against metabolic fluctuations?
    • doi: 10.1111/j.1399-3054.2009.01252.x
    • Rasmusson, A. G., Fernie, A. R., and van Dongen, J. T. (2009). Alternative oxidase: a defence against metabolic fluctuations? Physiol. Plant. 137, 371-382. doi: 10.1111/j.1399-3054.2009.01252.x
    • (2009) Physiol. Plant. , vol.137 , pp. 371-382
    • Rasmusson, A.G.1    Fernie, A.R.2    van Dongen, J.T.3
  • 175
    • 84989674612 scopus 로고
    • NAD(P)H dehydrogenases on the inner surface of the inner mitochondrial membrane studied using insideout submitochondriral particles
    • doi: 10.1111/j.1399-3054.1991.tb00106.x
    • Rasmusson, A. G., and Moller, I. M. (1991). NAD(P)H dehydrogenases on the inner surface of the inner mitochondrial membrane studied using insideout submitochondriral particles. Physiol. Plant. 83, 357-365. doi: 10.1111/j.1399-3054.1991.tb00106.x
    • (1991) Physiol. Plant. , vol.83 , pp. 357-365
    • Rasmusson, A.G.1    Moller, I.M.2
  • 176
    • 77953280824 scopus 로고    scopus 로고
    • Involvement of mitochondria in the control of plant cell NAD(P)H reduction levels
    • doi: 10.1042/BST0380661
    • Rasmusson, A. G., and Wallström, S. V. (2010). Involvement of mitochondria in the control of plant cell NAD(P)H reduction levels. Biochem. Soc. Trans. 38, 661-666. doi: 10.1042/BST0380661
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 661-666
    • Rasmusson, A.G.1    Wallström, S.V.2
  • 177
    • 11844285694 scopus 로고    scopus 로고
    • AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana
    • doi: 10.1016/j.febslet.2004.11.094
    • Reichheld, J. P., Meyer, E., Khafif, M., Bonnard, G., and Meyer, Y. (2005). AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana. FEBS Lett. 579, 337-342. doi: 10.1016/j.febslet.2004.11.094
    • (2005) FEBS Lett. , vol.579 , pp. 337-342
    • Reichheld, J.P.1    Meyer, E.2    Khafif, M.3    Bonnard, G.4    Meyer, Y.5
  • 178
    • 33846427352 scopus 로고    scopus 로고
    • The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response
    • doi: 10.1111/j.1365-313X.2006.02969.x
    • Rey, P., Becuwe, N., Barrault, M. B., Rumeau, D., Havaux, M., Biteau, B., et al. (2007). The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response. Plant J. 49, 505-514. doi: 10.1111/j.1365-313X.2006.02969.x
    • (2007) Plant J. , vol.49 , pp. 505-514
    • Rey, P.1    Becuwe, N.2    Barrault, M.B.3    Rumeau, D.4    Havaux, M.5    Biteau, B.6
  • 179
    • 33745631769 scopus 로고    scopus 로고
    • H2O2, a necessary evil for cell signalling
    • doi: 10.1126/science.1130481
    • Rhee, S. G. (2006). H2O2, a necessary evil for cell signalling. Science 312, 1882-1883. doi: 10.1126/science.1130481
    • (2006) Science , vol.312 , pp. 1882-1883
    • Rhee, S.G.1
  • 180
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: A historical overview and speculative preview of novel mechanism and emerging concepts in cell signalling
    • doi: 10.1016/j.freeradbiomed.2005.02.026
    • Rhee, S. G., Chae, H. Z., and Kim, K. (2005). Peroxiredoxins: a historical overview and speculative preview of novel mechanism and emerging concepts in cell signalling. Free Radic. Biol. Med. 38, 1543-1552. doi: 10.1016/j.freeradbiomed.2005.02.026
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 181
    • 33947188157 scopus 로고    scopus 로고
    • Mitochondrial retrograde regulation in plants
    • doi: 10.1016/j.mito.2007.01.002
    • Rhoads, D. M., and Subbaiah, C. C. (2007). Mitochondrial retrograde regulation in plants. Mitochondrion 7, 177-194. doi: 10.1016/j.mito.2007.01.002
    • (2007) Mitochondrion , vol.7 , pp. 177-194
    • Rhoads, D.M.1    Subbaiah, C.C.2
  • 182
    • 25444468110 scopus 로고    scopus 로고
    • The application of the oxygen-isotope technique to assess respiratory pathway partitioning
    • Plant Respiration: from Cell to Ecosystem, eds H. Lambers and M. Ribas-Carbó (The Netherlands: Springer)
    • Ribas-Carbó, M., Robinson, S. A., and Giles, L. (2005). "The application of the oxygen-isotope technique to assess respiratory pathway partitioning, " in Advances in Photosynthesis and Respiration. Plant Respiration: from Cell to Ecosystem, eds H. Lambers and M. Ribas-Carbó (The Netherlands: Springer), 18, 31-42.
    • (2005) Advances in Photosynthesis and Respiration. , vol.18 , pp. 31-42
    • Ribas-Carbó, M.1    Robinson, S.A.2    Giles, L.3
  • 183
    • 66149143498 scopus 로고    scopus 로고
    • Cellular response of pea plants to cadmium toxicity: Cross talk between reactive oxygen species, nitric oxide, and calcium
    • doi: 10.1104/pp.108.131524
    • Rodríguez-Serrano, M., Romero-Puertas, M. C., Pazmiño, D. M., Testillano, P. S., Risueño, M. C., Del Río, L. A., et al. (2009). Cellular response of pea plants to cadmium toxicity: cross talk between reactive oxygen species, nitric oxide, and calcium. Plant Physiol. 150, 229-243. doi: 10.1104/pp.108.131524
    • (2009) Plant Physiol. , vol.150 , pp. 229-243
    • Rodríguez-Serrano, M.1    Romero-Puertas, M.C.2    Pazmiño, D.M.3    Testillano, P.S.4    Risueño, M.C.5    Del Río, L.A.6
  • 184
    • 39149095741 scopus 로고    scopus 로고
    • Proteomic analysis of S-nitrosylated proteins in Arabidopsis thaliana undergoing hypersensitive response
    • doi: 10.1002/pmic.200700536
    • Romero-Puertas, M. C., Campostrini, N., Mattè, A., Righetti, P. G., Perazzolli, M., Zolla, L., et al. (2008). Proteomic analysis of S-nitrosylated proteins in Arabidopsis thaliana undergoing hypersensitive response. Proteomics 8, 1459-1469. doi: 10.1002/pmic.200700536
    • (2008) Proteomics , vol.8 , pp. 1459-1469
    • Romero-Puertas, M.C.1    Campostrini, N.2    Mattè, A.3    Righetti, P.G.4    Perazzolli, M.5    Zolla, L.6
  • 185
    • 39149133106 scopus 로고    scopus 로고
    • S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration
    • doi: 10.1105/tpc.107.055061
    • Romero-Puertas, M. C., Laxa, M., and Delledonne, M. (2007). S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration. Plant Cell 19, 4120-4130. doi: 10.1105/tpc.107.055061
    • (2007) Plant Cell , vol.19 , pp. 4120-4130
    • Romero-Puertas, M.C.1    Laxa, M.2    Delledonne, M.3
  • 186
    • 0037134534 scopus 로고    scopus 로고
    • Glutaredoxin-dependent peroxiredoxin from poplar: Protein-protein interaction and catalytic mechanism
    • doi: 10.1074/jbc.M111489200
    • Rouhier, N., Gelhaye, E., and Jacquot, J. P. (2002). Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism. J. Biol. Chem. 277, 13609-13614. doi: 10.1074/jbc.M111489200
    • (2002) J. Biol. Chem. , vol.277 , pp. 13609-13614
    • Rouhier, N.1    Gelhaye, E.2    Jacquot, J.P.3
  • 187
    • 18844398674 scopus 로고    scopus 로고
    • The plant multigenic family of thiol peroxidases
    • doi: 10.1016/j.freeradbiomed.2004.07.037
    • Rouhier, N., and Jacquot, J. P. (2005). The plant multigenic family of thiol peroxidases. Free Radic. Biol. Med. 38, 1413-1421. doi: 10.1016/j.freeradbiomed.2004.07.037
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1413-1421
    • Rouhier, N.1    Jacquot, J.P.2
  • 188
    • 42949085825 scopus 로고    scopus 로고
    • The role of glutathione in photosynthetic organisms: Emerging functions for glutaredoxins and glutathionylation
    • doi: 10.1146/annurev.arplant.59.032607.092811
    • Rouhier, N., Lemaire, S. D., and Jacquot, J. P. (2008). The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation. Annu. Rev. Plant Biol. 59, 143-166. doi: 10.1146/annurev.arplant.59.032607.092811
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 143-166
    • Rouhier, N.1    Lemaire, S.D.2    Jacquot, J.P.3
  • 189
    • 70450240741 scopus 로고    scopus 로고
    • Catalytic mechanism of sulfiredoxin from Saccharomyces cerevisiae passes through an oxidized disusfide sulfiredoxin intermediate that is reduced by thioredoxin
    • doi: 10.1074/jbc.M109.035352
    • Roussel, X., Kriznik, A., Richard, C., Rauel-Clermont, S., and Branlsant, G. (2009). Catalytic mechanism of sulfiredoxin from Saccharomyces cerevisiae passes through an oxidized disusfide sulfiredoxin intermediate that is reduced by thioredoxin. J. Biol. Chem. 284, 33048-33055. doi: 10.1074/jbc.M109.035352
    • (2009) J. Biol. Chem. , vol.284 , pp. 33048-33055
    • Roussel, X.1    Kriznik, A.2    Richard, C.3    Rauel-Clermont, S.4    Branlsant, G.5
  • 190
    • 59849108144 scopus 로고    scopus 로고
    • Effects of salt stress on the expression of antioxidant genes and proteins in the model legume Lotus japonicas
    • doi: 10.1111/j.1469-8137.2008.02718.x
    • Rubio, M. C., Bustos-Sanmamed, P., Clemente, M. R., and Becana, M. (2009). Effects of salt stress on the expression of antioxidant genes and proteins in the model legume Lotus japonicas. New Phytol. 181, 851-859. doi: 10.1111/j.1469-8137.2008.02718.x
    • (2009) New Phytol. , vol.181 , pp. 851-859
    • Rubio, M.C.1    Bustos-Sanmamed, P.2    Clemente, M.R.3    Becana, M.4
  • 191
    • 0036293238 scopus 로고    scopus 로고
    • Changes in antioxidant activity in sub-cellular fractions of tolerant and susceptible wheat genotypes in response to long-term salt stress
    • doi: 10.1016/S0168-9452(02)00037-7
    • Sairam, R. K., and Srivastava, G. C. (2002). Changes in antioxidant activity in sub-cellular fractions of tolerant and susceptible wheat genotypes in response to long-term salt stress. Plant Sci. 162, 897-904. doi: 10.1016/S0168-9452(02)00037-7
    • (2002) Plant Sci. , vol.162 , pp. 897-904
    • Sairam, R.K.1    Srivastava, G.C.2
  • 192
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • doi: 10.1093/emboj/17.9.2596
    • Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., et al. (1998). Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J. 17, 2596-2606. doi: 10.1093/emboj/17.9.2596
    • (1998) EMBO J. , vol.17 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2    Fujii, M.3    Takeda, K.4    Tobiume, K.5    Sawada, Y.6
  • 193
    • 84877037648 scopus 로고    scopus 로고
    • Mitochondrial energy and redox signaling in plants
    • doi: 10.1089/ars.2012.5104
    • Schwarzländer, M., and Finkemeier, I. (2013). Mitochondrial energy and redox signaling in plants. Antioxid. Redox Signal. 18, 2122-2144. doi: 10.1089/ars.2012.5104
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 2122-2144
    • Schwarzländer, M.1    Finkemeier, I.2
  • 194
    • 0001015125 scopus 로고    scopus 로고
    • Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
    • doi: 10.1074/jbc.M001943200
    • Seo, M. S., Kang, S. W., Kim, K., Baines, I. C., Lee, T. H., and Rhee, S. G. (2000). Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. J. Biol. Chem. 275, 20346-20354. doi: 10.1074/jbc.M001943200
    • (2000) J. Biol. Chem. , vol.275 , pp. 20346-20354
    • Seo, M.S.1    Kang, S.W.2    Kim, K.3    Baines, I.C.4    Lee, T.H.5    Rhee, S.G.6
  • 195
    • 0042209787 scopus 로고    scopus 로고
    • Type-H Thioredoxins accumulate in the nucleus of developing wheat seed tissues suffering oxidative stress
    • doi: 10.1007/s00425-003-1009-4
    • Serrato, A. J., and Cejudo, F. J. (2003). Type-H Thioredoxins accumulate in the nucleus of developing wheat seed tissues suffering oxidative stress. Planta 217, 392-399. doi: 10.1007/s00425-003-1009-4
    • (2003) Planta , vol.217 , pp. 392-399
    • Serrato, A.J.1    Cejudo, F.J.2
  • 196
    • 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
    • doi: 10.1023/A:1010697331184
    • Serrato, A. J., Crespo, J. L., Florencio, F. J., and Cejudo, F. J. (2001). Characterization of two thioredoxins h with predominant localization in the nucleus of aleurone and scutellum cells of germinating wheat seeds. Plant Mol. Biol. 46, 361-371. doi: 10.1023/A:1010697331184
    • (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
  • 197
    • 6344235622 scopus 로고    scopus 로고
    • A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana
    • doi: 10.1074/jbc.M404696200
    • Serrato, A. J., Pérez-Ruiz, J. M., Spínola, M. C., and Cejudo, F. J. (2004). A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana. J. Biol. Chem. 279, 43821-43827. doi: 10.1074/jbc.M404696200
    • (2004) J. Biol. Chem. , vol.279 , pp. 43821-43827
    • Serrato, A.J.1    Pérez-Ruiz, J.M.2    Spínola, M.C.3    Cejudo, F.J.4
  • 198
    • 0000276965 scopus 로고
    • Characterization of a manganese superoxide dismutase from the higher plant Pisum sativum
    • doi: 10.1104/pp.70.5.1321
    • Sevilla, F., López-Gorgé, J., and del Río, L. A. (1982). Characterization of a manganese superoxide dismutase from the higher plant Pisum sativum. Plant Physiol. 70, 1321-1326. doi: 10.1104/pp.70.5.1321
    • (1982) Plant Physiol. , vol.70 , pp. 1321-1326
    • Sevilla, F.1    López-Gorgé, J.2    del Río, L.A.3
  • 199
    • 26444507306 scopus 로고    scopus 로고
    • Drought induces oxidative stress and enhances the activities of antioxidant enzymes in growing rice seedlings
    • doi: 10.1007/s10725-005-0002-2
    • Sharma, P., and Dubey, R. S. (2005). Drought induces oxidative stress and enhances the activities of antioxidant enzymes in growing rice seedlings. Plant Growth Regul. 46, 209-221. doi: 10.1007/s10725-005-0002-2
    • (2005) Plant Growth Regul. , vol.46 , pp. 209-221
    • Sharma, P.1    Dubey, R.S.2
  • 200
    • 70450225552 scopus 로고    scopus 로고
    • Manipulation of alternative oxidase can influence salt tolerance in Arabidopsis thaliana
    • doi: 10.1111/j.1399-3054.2009.01305.x
    • Smith, C. A., Melino, V. J., Sweetman, C., and Soole, K. L. (2009). Manipulation of alternative oxidase can influence salt tolerance in Arabidopsis thaliana. Physiol. Plant. 137, 459-472. doi: 10.1111/j.1399-3054.2009.01305.x
    • (2009) Physiol. Plant. , vol.137 , pp. 459-472
    • Smith, C.A.1    Melino, V.J.2    Sweetman, C.3    Soole, K.L.4
  • 201
    • 33845682100 scopus 로고    scopus 로고
    • Dehydroascorbate reduction in plant mitochondria is coupled to the respiratory electron transfer chain
    • doi: 10.1111/j.1399-3054.2006.00810.x
    • Szarka, A., Horemans, N., Kovacs, Z., Gróf, P., Mayer, M., and Bánhegyi, G. (2007). Dehydroascorbate reduction in plant mitochondria is coupled to the respiratory electron transfer chain. Physiol. Plant. 129, 225-232. doi: 10.1111/j.1399-3054.2006.00810.x
    • (2007) Physiol. Plant. , vol.129 , pp. 225-232
    • Szarka, A.1    Horemans, N.2    Kovacs, Z.3    Gróf, P.4    Mayer, M.5    Bánhegyi, G.6
  • 202
    • 79957664930 scopus 로고    scopus 로고
    • Ascorbic acid is a key participant during the interactions between chloroplasts and mitochondria to optimize photosynthesis and protect against photoinhibition
    • doi: 10.1007/s12038-011-9000-x
    • Talla, S., Riazunnisa, K., Padmavathi, L., Sunil, B., Rajsheel, P., and Raghavendra, A. S. (2011). Ascorbic acid is a key participant during the interactions between chloroplasts and mitochondria to optimize photosynthesis and protect against photoinhibition. J. Biosci. 36, 163-173. doi: 10.1007/s12038-011-9000-x
    • (2011) J. Biosci. , vol.36 , pp. 163-173
    • Talla, S.1    Riazunnisa, K.2    Padmavathi, L.3    Sunil, B.4    Rajsheel, P.5    Raghavendra, A.S.6
  • 203
    • 0033615664 scopus 로고    scopus 로고
    • Salt tolerance of transgenic rice overexpression yeast mitochondrial Mn-SOD in chloroplasts
    • doi: 10.1016/S0168-9452(99)00133-8
    • Tanaka, K., Hibino, T., Hayashi, Y., Tanaka, A., Kishitani, S., Takabe, T., et al. (1999). Salt tolerance of transgenic rice overexpression yeast mitochondrial Mn-SOD in chloroplasts. Plant Sci. 148, 131-138. doi: 10.1016/S0168-9452(99)00133-8
    • (1999) Plant Sci. , vol.148 , pp. 131-138
    • Tanaka, K.1    Hibino, T.2    Hayashi, Y.3    Tanaka, A.4    Kishitani, S.5    Takabe, T.6
  • 204
    • 18444365267 scopus 로고    scopus 로고
    • Thioredoxin-2 (TRX-2) is an essential gene regulating mitochondria dependent apoptosis
    • doi: 10.1093/emboj/21.7.1695
    • Tanaka, T., Hosoi, F., Yamaguchi-Iwai, Y., Nakamura, H., Masutani, H., Ueda, S., et al. (2002). Thioredoxin-2 (TRX-2) is an essential gene regulating mitochondria dependent apoptosis. EMBO J. 21, 1695-1703. doi: 10.1093/emboj/21.7.1695
    • (2002) EMBO J. , vol.21 , pp. 1695-1703
    • Tanaka, T.1    Hosoi, F.2    Yamaguchi-Iwai, Y.3    Nakamura, H.4    Masutani, H.5    Ueda, S.6
  • 205
    • 71949124535 scopus 로고    scopus 로고
    • Proteomics reveals the overlapping roles of hydrogen peroxide and nitric oxide in the acclimation of citrus plants to salinity
    • doi: 10.1111/j.1365-313X.2009.04000.x
    • Tanou, G., Job, C., Rajjou, L., Arc, E., Belghazi, M., Diamantidis, G., et al. (2009). Proteomics reveals the overlapping roles of hydrogen peroxide and nitric oxide in the acclimation of citrus plants to salinity. Plant J. 60, 795-804. doi: 10.1111/j.1365-313X.2009.04000.x
    • (2009) Plant J. , vol.60 , pp. 795-804
    • Tanou, G.1    Job, C.2    Rajjou, L.3    Arc, E.4    Belghazi, M.5    Diamantidis, G.6
  • 206
    • 0037490142 scopus 로고    scopus 로고
    • Reversible glutathionylation of complex I increases mitochondrial superoxide formation
    • doi: 10.1074/jbc.M209359200
    • Taylor, E. R., Hurrell, F., Shannon, R. J., Lin, T. K., Hirst, J., and Murphy, M. P. (2003). Reversible glutathionylation of complex I increases mitochondrial superoxide formation. J. Biol. Chem. 278, 19603-19610. doi: 10.1074/jbc.M209359200
    • (2003) J. Biol. Chem. , vol.278 , pp. 19603-19610
    • Taylor, E.R.1    Hurrell, F.2    Shannon, R.J.3    Lin, T.K.4    Hirst, J.5    Murphy, M.P.6
  • 207
    • 63549119436 scopus 로고    scopus 로고
    • Abiotic environmental stress induced changes in the Arabidopsis thaliana chloroplast, mitochondria and peroxisome proteomes
    • doi: 10.1016/j.jprot.2008.11.006
    • Taylor, N. L., Tan, Y.-F., Jacoby, R. P., and Millar, A. H. (2009). Abiotic environmental stress induced changes in the Arabidopsis thaliana chloroplast, mitochondria and peroxisome proteomes. J. Proteomics 72, 367-378. doi: 10.1016/j.jprot.2008.11.006
    • (2009) J. Proteomics , vol.72 , pp. 367-378
    • Taylor, N.L.1    Tan, Y.-F.2    Jacoby, R.P.3    Millar, A.H.4
  • 208
    • 33745355254 scopus 로고    scopus 로고
    • Rice ascorbate peroxidase gene family encodes functionally diverse isoforms localized in different subcellular compartments
    • doi: 10.1007/s00425-005-0214-8
    • Teixeira, F. K., Menezes-Benavente, L., Galvao, V. C., Margis, R., and Margis-Pinheiro, M. (2006). Rice ascorbate peroxidase gene family encodes functionally diverse isoforms localized in different subcellular compartments. Planta 224, 300-314. doi: 10.1007/s00425-005-0214-8
    • (2006) Planta , vol.224 , pp. 300-314
    • Teixeira, F.K.1    Menezes-Benavente, L.2    Galvao, V.C.3    Margis, R.4    Margis-Pinheiro, M.5
  • 209
    • 79959935916 scopus 로고    scopus 로고
    • Peroxiredoxins and NADPH-dependent thioredoxin systems in the model legume Lotus japonicas
    • doi: 10.1104/pp.111.177196
    • Tovar-Méndez, A., Matamoros, M. A., Bustos-Sanmamed, P., Dietz, K. J., Cejudo, F. J., Rouhier, N., et al. (2011). Peroxiredoxins and NADPH-dependent thioredoxin systems in the model legume Lotus japonicas. Plant Physiol. 156, 1535-1547. doi: 10.1104/pp.111.177196
    • (2011) Plant Physiol. , vol.156 , pp. 1535-1547
    • Tovar-Méndez, A.1    Matamoros, M.A.2    Bustos-Sanmamed, P.3    Dietz, K.J.4    Cejudo, F.J.5    Rouhier, N.6
  • 210
    • 62949245620 scopus 로고    scopus 로고
    • Peroxiredoxins: A less studied component of hydrogen peroxide detoxification in photosynthetic organisms
    • doi: 10.1007/s00709-009-0032-0
    • Tripathi, B. N., Bhatt, I., and Dietz, K. J. (2009). Peroxiredoxins: a less studied component of hydrogen peroxide detoxification in photosynthetic organisms. Protoplasma 235, 3-15. doi: 10.1007/s00709-009-0032-0
    • (2009) Protoplasma , vol.235 , pp. 3-15
    • Tripathi, B.N.1    Bhatt, I.2    Dietz, K.J.3
  • 211
    • 1842529224 scopus 로고    scopus 로고
    • The uncoupling protein and the potassium channel are activated by hyperosmotic stress in mitochondria from durum wheat seedlings
    • doi: 10.1111/j.1365-3040.2003.01162.x
    • Trono, D., Flagella, Z., Laus, M. N., Di Fonzo, N., and Pastore, D. (2004). The uncoupling protein and the potassium channel are activated by hyperosmotic stress in mitochondria from durum wheat seedlings. Plant Cell Environ. 27, 437-448. doi: 10.1111/j.1365-3040.2003.01162.x
    • (2004) Plant Cell Environ. , vol.27 , pp. 437-448
    • Trono, D.1    Flagella, Z.2    Laus, M.N.3    Di Fonzo, N.4    Pastore, D.5
  • 212
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • doi: 10.1113/jphysiol.2003.049478
    • Turrens, J. F. (2003). Mitochondrial formation of reactive oxygen species. J. Physiol. (Lond.) 552, 335-344. doi: 10.1113/jphysiol.2003.049478
    • (2003) J. Physiol. (Lond.) , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 213
    • 33645013085 scopus 로고    scopus 로고
    • Regulation of plant alternative oxidase activity: A tale of two cysteines
    • doi: 10.1016/j.bbabio.2005.12.005
    • Umbach, A. L., Ng, V. S., and Siedow, J. N. (2006). Regulation of plant alternative oxidase activity: a tale of two cysteines. Biochim. Biophys. Acta 1757, 135-142. doi: 10.1016/j.bbabio.2005.12.005
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 135-142
    • Umbach, A.L.1    Ng, V.S.2    Siedow, J.N.3
  • 214
    • 33745624267 scopus 로고    scopus 로고
    • Roles for redox regulation in leaf senescence in pea plants grown in different sources of nitrogen nutrition
    • doi: 10.1093/jxb/erl012
    • Vanacker, H., Sandalio, L. M., Jiménez, A., Palma, J. M., Corpas, F. J., Meseger, V., et al. (2006). Roles for redox regulation in leaf senescence in pea plants grown in different sources of nitrogen nutrition. J. Exp. Bot. 57, 1735-1745. doi: 10.1093/jxb/erl012
    • (2006) J. Exp. Bot. , vol.57 , pp. 1735-1745
    • Vanacker, H.1    Sandalio, L.M.2    Jiménez, A.3    Palma, J.M.4    Corpas, F.J.5    Meseger, V.6
  • 215
    • 70450260721 scopus 로고    scopus 로고
    • Alternative oxidase: A target and regulator of stress response
    • doi: 10.1111/j.1399-3054.2009.01240.x
    • Van Aken, O., Giraud, E., Clifton, R., and Whelan, J. (2009a). Alternative oxidase: a target and regulator of stress response. Physiol. Plant. 137, 354-361. doi: 10.1111/j.1399-3054.2009.01240.x
    • (2009) Physiol. Plant. , vol.137 , pp. 354-361
    • Van Aken, O.1    Giraud, E.2    Clifton, R.3    Whelan, J.4
  • 216
    • 71249116157 scopus 로고    scopus 로고
    • Defining the mitochondrial stress response in Arabidopsis thaliana
    • doi: 10.1093/mp/ssp053
    • Van Aken, O., Zhang, B., Carrie, C., Uggalla, V., Paynter, E., Giraud, E., et al. (2009b). Defining the mitochondrial stress response in Arabidopsis thaliana. Mol. Plant 2, 1310-1324. doi: 10.1093/mp/ssp053
    • (2009) Mol. Plant , vol.2 , pp. 1310-1324
    • Van Aken, O.1    Zhang, B.2    Carrie, C.3    Uggalla, V.4    Paynter, E.5    Giraud, E.6
  • 217
    • 0034879767 scopus 로고    scopus 로고
    • The role of active oxygen species in plant signal transduction
    • doi: 10.1016/S0168-9452(01)00452-6
    • Van Breusegem, F., Vranová, E., Dat, J. F., and Inzé, D. (2001). The role of active oxygen species in plant signal transduction. Plant Sci. 161, 405-414. doi: 10.1016/S0168-9452(01)00452-6
    • (2001) Plant Sci. , vol.161 , pp. 405-414
    • Van Breusegem, F.1    Vranová, E.2    Dat, J.F.3    Inzé, D.4
  • 218
    • 80052419041 scopus 로고    scopus 로고
    • Peroxynitrite formation and function in plants
    • doi: 10.1016/j.plantsci.2011.05.002
    • Vandelle, E., and Delledonne, M. (2011). Peroxynitrite formation and function in plants. Plant Sci. 181, 534-539. doi: 10.1016/j.plantsci.2011.05.002
    • (2011) Plant Sci. , vol.181 , pp. 534-539
    • Vandelle, E.1    Delledonne, M.2
  • 219
    • 61449184625 scopus 로고    scopus 로고
    • Deletion of the mitochondrial superoxide dismutase sod-2 extends lifespan in Caenorhabditis elegans
    • doi: 10.1371/journal.pgen.1000361
    • Van Raamsdonk, J. M., and Hekimi, S. (2009). Deletion of the mitochondrial superoxide dismutase sod-2 extends lifespan in Caenorhabditis elegans. PLoS Genet. 5:1000361. doi: 10.1371/journal.pgen.1000361
    • (2009) PLoS Genet. , vol.5 , pp. 1000361
    • Van Raamsdonk, J.M.1    Hekimi, S.2
  • 220
    • 34147210988 scopus 로고    scopus 로고
    • Hydrogen peroxide sensing and signaling
    • doi: 10.1016/j.molcel.2007.03.016
    • Veal, E. A., Day, A. M., and Morgan, B. A. (2007). Hydrogen peroxide sensing and signaling. Mol. Cell. 26, 1-14. doi: 10.1016/j.molcel.2007.03.016
    • (2007) Mol. Cell. , vol.26 , pp. 1-14
    • Veal, E.A.1    Day, A.M.2    Morgan, B.A.3
  • 221
    • 21144440053 scopus 로고    scopus 로고
    • A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway
    • doi: 10.1073/pnas.0503251102
    • Vivancos, A. P., Castillo, E. A., Biteau, B., Nicot, C., Ayté, J., Toledano, M. B., et al. (2005). A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway. Proc. Natl. Acad. Sci. U.S.A. 102, 8875-8880. doi: 10.1073/pnas.0503251102
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 8875-8880
    • Vivancos, A.P.1    Castillo, E.A.2    Biteau, B.3    Nicot, C.4    Ayté, J.5    Toledano, M.B.6
  • 222
    • 77950870073 scopus 로고    scopus 로고
    • Enhanced salt tolerance of transgenic poplar plants expressing a manganese superoxide dismutase from Tamarix androssowii
    • doi: 10.1007/s11033-009-9884-9
    • Wang, Y., Qu, G. Z., Li, H. Y., Wu, Y. J., Wang, C., Liu, G. F., et al. (2010a). Enhanced salt tolerance of transgenic poplar plants expressing a manganese superoxide dismutase from Tamarix androssowii. Mol. Biol. Rep. 37, 1119-1124. doi: 10.1007/s11033-009-9884-9
    • (2010) Mol. Biol. Rep. , vol.37 , pp. 1119-1124
    • Wang, Y.1    Qu, G.Z.2    Li, H.Y.3    Wu, Y.J.4    Wang, C.5    Liu, G.F.6
  • 223
    • 77952898429 scopus 로고    scopus 로고
    • Increased vitamin C content accompanied by an enhanced recycling pathway confers oxidative stress tolerance in Arabidopsis
    • doi: 10.1111/j.1744-7909.2010.00921.x
    • Wang, Z., Xiao, Y., Chen, W., Tang, K., and Zhang, L. (2010b). Increased vitamin C content accompanied by an enhanced recycling pathway confers oxidative stress tolerance in Arabidopsis. J. Integr. Plant Biol. 52, 400-409. doi: 10.1111/j.1744-7909.2010.00921.x
    • (2010) J. Integr. Plant Biol. , vol.52 , pp. 400-409
    • Wang, Z.1    Xiao, Y.2    Chen, W.3    Tang, K.4    Zhang, L.5
  • 224
    • 70349854477 scopus 로고    scopus 로고
    • Ectopic expression of Mn-SOD in Lycopersicon esculentum leads to enhanced tolerance to salt and oxidative stress
    • Wang, Y., Wisniewski, M., Meilan, R., Uratsu, S. L., Cui, M., Dandekar, A., et al. (2007). Ectopic expression of Mn-SOD in Lycopersicon esculentum leads to enhanced tolerance to salt and oxidative stress. J. Appl. Horticul. 9, 3-8.
    • (2007) J. Appl. Horticul. , vol.9 , pp. 3-8
    • Wang, Y.1    Wisniewski, M.2    Meilan, R.3    Uratsu, S.L.4    Cui, M.5    Dandekar, A.6
  • 225
    • 3543092741 scopus 로고    scopus 로고
    • Transgenic Arabidopsis overexpressing Mn-SOD enhanced salt-tolerance
    • doi: 10.1016/j.plantsci.2004.03.032
    • Wang, Y., Ying, Y., Chen, J., and Wang, X. (2004). Transgenic Arabidopsis overexpressing Mn-SOD enhanced salt-tolerance. Plant Sci. 67, 671-677. doi: 10.1016/j.plantsci.2004.03.032
    • (2004) Plant Sci. , vol.67 , pp. 671-677
    • Wang, Y.1    Ying, Y.2    Chen, J.3    Wang, X.4
  • 226
    • 45949090961 scopus 로고    scopus 로고
    • Mechanisms of salt tolerance in transgenic Arabidopsis thaliana carrying a peroxisomal ascorbate peroxidase gene from barley
    • doi: 10.1016/S1002-0160(08)60039-9
    • Wei-Feng, X., Wei-Ming, S., Ueda, A., and Takabe, T. (2008). Mechanisms of salt tolerance in transgenic Arabidopsis thaliana carrying a peroxisomal ascorbate peroxidase gene from barley. Pedosphere 18, 486-495. doi: 10.1016/S1002-0160(08)60039-9
    • (2008) Pedosphere , vol.18 , pp. 486-495
    • Wei-Feng, X.1    Wei-Ming, S.2    Ueda, A.3    Takabe, T.4
  • 227
    • 84855469557 scopus 로고    scopus 로고
    • Bcl-2 is a novel interacting partner for the 2-oxoglutarate carrier and a key regulator of mitochondrial glutathione
    • doi: 10.1016/j.freeradbiomed.2011.10.495
    • Wilkins, H. M., Marquardt, K., Lash, L. H., and Linseman, D. A. (2012). Bcl-2 is a novel interacting partner for the 2-oxoglutarate carrier and a key regulator of mitochondrial glutathione. Free Radic. Biol. Med. 52, 410-419. doi: 10.1016/j.freeradbiomed.2011.10.495
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 410-419
    • Wilkins, H.M.1    Marquardt, K.2    Lash, L.H.3    Linseman, D.A.4
  • 228
    • 41849130604 scopus 로고    scopus 로고
    • Nitric oxide synthesis and signaling in plants
    • doi: 10.1111/j.1365-3040.2007.01761.x
    • Wilson, I. D., Neill, S. J., and Hancock, J. T. (2008). Nitric oxide synthesis and signaling in plants. Plant Cell Environ. 31, 622-631. doi: 10.1111/j.1365-3040.2007.01761.x
    • (2008) Plant Cell Environ. , vol.31 , pp. 622-631
    • Wilson, I.D.1    Neill, S.J.2    Hancock, J.T.3
  • 229
    • 36549031664 scopus 로고    scopus 로고
    • Identification of intra-and intermolecular disulphide bonding in the plant mitochondrial proteome by diagonal gel electrophoresis
    • doi: 10.1002/pmic.200700209
    • Winger, A. M., Taylor, N. L., Heazlewood, J. L., Day, D. A., and Millar, A. H. (2007). Identification of intra-and intermolecular disulphide bonding in the plant mitochondrial proteome by diagonal gel electrophoresis. Proteomics 7, 4158-4170. doi: 10.1002/pmic.200700209
    • (2007) Proteomics , vol.7 , pp. 4158-4170
    • Winger, A.M.1    Taylor, N.L.2    Heazlewood, J.L.3    Day, D.A.4    Millar, A.H.5
  • 230
    • 60749125535 scopus 로고    scopus 로고
    • Sestrin 2 is not a reductase for cysteine sulfinic acid of peroxiredoxins
    • doi: 10.1089/ars.2008.2360
    • Woo, H. A., Bae, S. H., Park, S., and Rhee, S. G. (2009). Sestrin 2 is not a reductase for cysteine sulfinic acid of peroxiredoxins. Antioxid. Redox Signal. 11, 730-745. doi: 10.1089/ars.2008.2360
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 730-745
    • Woo, H.A.1    Bae, S.H.2    Park, S.3    Rhee, S.G.4
  • 231
    • 13544272571 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins
    • doi: 10.1074/jbc.C400496200
    • Woo, H. A., Jeong, W., Chang, T. S., Park, K. J., Park, S. J., Yang, J. S., et al. (2005). Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins. J. Biol. Chem. 280, 3125-3128. doi: 10.1074/jbc.C400496200
    • (2005) J. Biol. Chem. , vol.280 , pp. 3125-3128
    • Woo, H.A.1    Jeong, W.2    Chang, T.S.3    Park, K.J.4    Park, S.J.5    Yang, J.S.6
  • 232
    • 0346850874 scopus 로고    scopus 로고
    • Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid. Inmunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence
    • doi: 10.1074/jbc.C300428200
    • Woo, H. A., Kang, S. W., Kim, H. K., Yang, K. S., Chae, H. Z., and Rhee, S. G. (2003). Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid. Inmunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence. J. Biol. Chem. 278, 47361-47364. doi: 10.1074/jbc.C300428200
    • (2003) J. Biol. Chem. , vol.278 , pp. 47361-47364
    • Woo, H.A.1    Kang, S.W.2    Kim, H.K.3    Yang, K.S.4    Chae, H.Z.5    Rhee, S.G.6
  • 233
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signalling
    • doi: 10.1126/science.1080405
    • Wood, Z. A., Poole, L. B., and Karplus, P. A. (2003). Peroxiredoxin evolution and the regulation of hydrogen peroxide signalling. Science 300, 650-653. doi: 10.1126/science.1080405
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 234
    • 42449103989 scopus 로고    scopus 로고
    • Coordination of gene expression between organellar and nuclear genomes
    • doi: 10.1038/nrg2348
    • Woodson, J. D., and Chory, J. (2008). Coordination of gene expression between organellar and nuclear genomes. Nat. Rev. Genet. 9, 383-395. doi: 10.1038/nrg2348
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 383-395
    • Woodson, J.D.1    Chory, J.2
  • 235
    • 80053005317 scopus 로고    scopus 로고
    • Thioredoxin 1-mediated post-translational modifications: Reduction, transnitrosylation, denitrosylation, and related proteomics methodologies
    • doi: 10.1089/ars.2010.3831
    • Wu, C., Parrott, A. M., Fu, C., Liu, T., Marino, S. M., Gladyshev, V. N., et al. (2011). Thioredoxin 1-mediated post-translational modifications: reduction, transnitrosylation, denitrosylation, and related proteomics methodologies. Antioxid. Redox Signal. 15, 2565-2604. doi: 10.1089/ars.2010.3831
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 2565-2604
    • Wu, C.1    Parrott, A.M.2    Fu, C.3    Liu, T.4    Marino, S.M.5    Gladyshev, V.N.6
  • 236
    • 68149162554 scopus 로고    scopus 로고
    • Nitrite reduction and superoxide-dependent nitric oxide degradation by Arabidopsis mitochondria: Influence of external NAD(P)H dehydrogenases and alternative oxidase in the control of nitric oxide levels
    • doi: 10.1016/j.niox.2009.06.003
    • Wulff, A., Oliveira, H. C., Saviani, E. E., and Salgado, I. (2009). Nitrite reduction and superoxide-dependent nitric oxide degradation by Arabidopsis mitochondria: influence of external NAD(P)H dehydrogenases and alternative oxidase in the control of nitric oxide levels. Nitric Oxide 21, 132-139. doi: 10.1016/j.niox.2009.06.003
    • (2009) Nitric Oxide , vol.21 , pp. 132-139
    • Wulff, A.1    Oliveira, H.C.2    Saviani, E.E.3    Salgado, I.4
  • 237
    • 0032486405 scopus 로고    scopus 로고
    • Inactivation of human manganese-superoxide dismutase by peroxynitrite is caused by exclusive nitration of tyrosine 34 to 3-nitrotyrosine
    • doi: 10.1074/jbc.273.23.14085
    • Yamakura, F., Taka, H., Fujimura, T., and Murayama, K. (1998). Inactivation of human manganese-superoxide dismutase by peroxynitrite is caused by exclusive nitration of tyrosine 34 to 3-nitrotyrosine. J. Biol. Chem. 273, 14085-14089. doi: 10.1074/jbc.273.23.14085
    • (1998) J. Biol. Chem. , vol.273 , pp. 14085-14089
    • Yamakura, F.1    Taka, H.2    Fujimura, T.3    Murayama, K.4
  • 238
    • 77950140755 scopus 로고    scopus 로고
    • Transcription profiles of genes encoding catalase an ascorbate peroxidase in rice leaf tissues under salinity
    • doi: 10.1626/pps.13.164
    • Yamane, K., Mitsuya, S., Taniguchi, M., and Miyake, H. (2010). Transcription profiles of genes encoding catalase an ascorbate peroxidase in rice leaf tissues under salinity. Plant Prod. Sci. 13, 164-168. doi: 10.1626/pps.13.164
    • (2010) Plant Prod. Sci. , vol.13 , pp. 164-168
    • Yamane, K.1    Mitsuya, S.2    Taniguchi, M.3    Miyake, H.4
  • 239
    • 0037064080 scopus 로고    scopus 로고
    • Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid
    • doi: 10.1074/jbc.M206626200
    • Yang, K. S., Kang, S. W., Woo, H. A., Hwang, S. C., Chae, H. Z., Kim, K., et al. (2002). Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J. Biol. Chem. 277, 38029-38036. doi: 10.1074/jbc.M206626200
    • (2002) J. Biol. Chem. , vol.277 , pp. 38029-38036
    • Yang, K.S.1    Kang, S.W.2    Woo, H.A.3    Hwang, S.C.4    Chae, H.Z.5    Kim, K.6
  • 240
    • 0034942538 scopus 로고    scopus 로고
    • Mitochondrial alternative oxidase acts to dampen the generation of active oxygen species during a period of rapid respiration induced to support a high rate of nutrient uptake
    • doi: 10.1034/j.1399-3054.2001.1120305.x
    • Yip, J. Y. H., and Vanlerberghe, G. C. (2001). Mitochondrial alternative oxidase acts to dampen the generation of active oxygen species during a period of rapid respiration induced to support a high rate of nutrient uptake. Physiol. Plant. 112, 327-337. doi: 10.1034/j.1399-3054.2001.1120305.x
    • (2001) Physiol. Plant. , vol.112 , pp. 327-337
    • Yip, J.Y.H.1    Vanlerberghe, G.C.2
  • 241
    • 84878846165 scopus 로고    scopus 로고
    • Systematic Exploration of thioredoxin target proteins in plant mitochondria
    • doi: 10.1093/pcp/pct037
    • Yoshida, K., Noguchi, K., Motohashi, K., and Hisabori, T. (2013). Systematic Exploration of thioredoxin target proteins in plant mitochondria. Plant Cell Physiol. 54, 875-892. doi: 10.1093/pcp/pct037
    • (2013) Plant Cell Physiol. , vol.54 , pp. 875-892
    • Yoshida, K.1    Noguchi, K.2    Motohashi, K.3    Hisabori, T.4
  • 242
    • 84856753212 scopus 로고    scopus 로고
    • Glutathionylation in the photosynthetic model organism Chlamydomonas reinhardtii: A proteomic survey
    • doi: 10.1074/mcp.M111.014142
    • Zaffagnini, M., Bedhomme, M., Groni, H., Marchand, C. H., Puppo, C., Gontero, B., et al. (2012a). Glutathionylation in the photosynthetic model organism Chlamydomonas reinhardtii: a proteomic survey. Mol. Cell. Proteomics 11, 1-15. doi: 10.1074/mcp.M111.014142
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 1-15
    • Zaffagnini, M.1    Bedhomme, M.2    Groni, H.3    Marchand, C.H.4    Puppo, C.5    Gontero, B.6
  • 243
    • 84856719860 scopus 로고    scopus 로고
    • Redox regulation in photosynthetic organisms: Focus on glutathionylation
    • doi: 10.1089/ars.2011.4255
    • Zaffagnini, M., Bedhomme, M., Marchand, C. H., Morisse, S., Trost, P., and Lemaire, S. D. (2012b). Redox regulation in photosynthetic organisms: focus on glutathionylation. Antioxid. Redox Signal. 16, 567-586. doi: 10.1089/ars.2011.4255
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 567-586
    • Zaffagnini, M.1    Bedhomme, M.2    Marchand, C.H.3    Morisse, S.4    Trost, P.5    Lemaire, S.D.6
  • 244
    • 69349088862 scopus 로고    scopus 로고
    • Exogenous nitric oxide improves seed germination in wheat against mitochondrial oxidative damage induced by high salinity
    • doi: 10.1016/j.envexpbot.2009.05.002
    • Zheng, C., Jiang, D., Liu, F., Dai, T., Liu, W., Jing, Q., et al. (2009). Exogenous nitric oxide improves seed germination in wheat against mitochondrial oxidative damage induced by high salinity. Environ. Exp. Bot. 67, 222-227. doi: 10.1016/j.envexpbot.2009.05.002
    • (2009) Environ. Exp. Bot. , vol.67 , pp. 222-227
    • Zheng, C.1    Jiang, D.2    Liu, F.3    Dai, T.4    Liu, W.5    Jing, Q.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.