메뉴 건너뛰기




Volumn 1827, Issue 3, 2013, Pages 239-247

Modulation of mitochondrial activity by S-nitrosoglutathione reductase in Arabidopsis thaliana transgenic cell lines

Author keywords

Alternative oxidase; Arabidopsis thaliana; GSNO reductase; Nitric oxide; Respiratory chain; Uncoupling protein

Indexed keywords

MITOCHONDRIAL PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); S NITROSOGLUTATHIONE; SUCCINATE DEHYDROGENASE (UBIQUINONE); UNCOUPLING PROTEIN 1; UNCOUPLING PROTEIN 2;

EID: 84871987593     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2012.11.011     Document Type: Article
Times cited : (40)

References (69)
  • 2
    • 79953296231 scopus 로고    scopus 로고
    • The therapeutic potential of targeting endogenous inhibitors of nitric oxide synthesis
    • J. Leiper, and M. Nandi The therapeutic potential of targeting endogenous inhibitors of nitric oxide synthesis Nat. Rev. Drug Discov. 10 2011 277 291
    • (2011) Nat. Rev. Drug Discov. , vol.10 , pp. 277-291
    • Leiper, J.1    Nandi, M.2
  • 3
    • 0033977815 scopus 로고    scopus 로고
    • Nitric oxide stimulates seed germination and de-etiolation, and inhibits hypocotyl elongation, three light-inducible responses in plants
    • M.V. Beligni, and L. Lamattina Nitric oxide stimulates seed germination and de-etiolation, and inhibits hypocotyl elongation, three light-inducible responses in plants Planta 210 2000 215 221
    • (2000) Planta , vol.210 , pp. 215-221
    • Beligni, M.V.1    Lamattina, L.2
  • 4
    • 47249117861 scopus 로고    scopus 로고
    • Floral transition and nitric oxide emission during flower development in Arabidopsis thaliana is affected in nitrate reductase-deficient plants
    • K. Seligman, E.E. Saviani, H.C. Oliveira, C.A.F. Pinto-Maglio, and I. Salgado Floral transition and nitric oxide emission during flower development in Arabidopsis thaliana is affected in nitrate reductase-deficient plants Plant Cell Physiol. 49 2008 1112 1121
    • (2008) Plant Cell Physiol. , vol.49 , pp. 1112-1121
    • Seligman, K.1    Saviani, E.E.2    Oliveira, H.C.3    Pinto-Maglio, C.A.F.4    Salgado, I.5
  • 5
    • 21244453184 scopus 로고    scopus 로고
    • Nitrite as the major source of nitric oxide production by Arabidopsis thaliana in response to Pseudomonas syringae
    • L.V. Modolo, O. Augusto, I.M.G. Almeida, J.R. Magalhaes, and I. Salgado Nitrite as the major source of nitric oxide production by Arabidopsis thaliana in response to Pseudomonas syringae FEBS Lett. 579 2005 3814 3820
    • (2005) FEBS Lett. , vol.579 , pp. 3814-3820
    • Modolo, L.V.1    Augusto, O.2    Almeida, I.M.G.3    Magalhaes, J.R.4    Salgado, I.5
  • 6
    • 79960260496 scopus 로고    scopus 로고
    • Role of nitric oxide in tolerance of plants to abiotic stress
    • M.H. Siddiqui, M.H. Al-Whaibi, and M.O. Basalah Role of nitric oxide in tolerance of plants to abiotic stress Protoplasma 248 2011 447 455
    • (2011) Protoplasma , vol.248 , pp. 447-455
    • Siddiqui, M.H.1    Al-Whaibi, M.H.2    Basalah, M.O.3
  • 7
    • 77957824005 scopus 로고    scopus 로고
    • Redox regulation of the NPR1-TGA1 system of Arabidopsis thaliana by nitric oxide
    • C. Lindermayr, S. Sell, B. Müller, D. Leister, and J. Durner Redox regulation of the NPR1-TGA1 system of Arabidopsis thaliana by nitric oxide Plant Cell 22 2010 2894 2907
    • (2010) Plant Cell , vol.22 , pp. 2894-2907
    • Lindermayr, C.1    Sell, S.2    Müller, B.3    Leister, D.4    Durner, J.5
  • 8
    • 33745643840 scopus 로고    scopus 로고
    • Cross talk between reactive nitrogen and oxygen species during the hypersensitive disease resistance response
    • F. Zaninotto, S. La Camera, A. Polverari, and M. Delledonne Cross talk between reactive nitrogen and oxygen species during the hypersensitive disease resistance response Plant Physiol. 141 2006 379 383
    • (2006) Plant Physiol. , vol.141 , pp. 379-383
    • Zaninotto, F.1    La Camera, S.2    Polverari, A.3    Delledonne, M.4
  • 10
    • 20344377809 scopus 로고    scopus 로고
    • Proteomic identification of S-nitrosylated proteins in Arabidopsis
    • C. Lindermayr, G. Saalbach, and J. Durner Proteomic identification of S-nitrosylated proteins in Arabidopsis Plant Physiol. 137 2005 921 930
    • (2005) Plant Physiol. , vol.137 , pp. 921-930
    • Lindermayr, C.1    Saalbach, G.2    Durner, J.3
  • 11
    • 77955492720 scopus 로고    scopus 로고
    • Identification of S-nitrosated mitochondrial proteins by S-nitrosothiol difference in gel electrophoresis (SNO-DIGE): Implications for the regulation of mitochondrial function by reversible S-nitrosation
    • E.T. Chouchani, T.R. Hurd, S.M. Nadtochiy, P.S. Brookes, I.M. Fearnley, K.S. Lilley, K.S. Lilley, R.A.J. Smith, and M.P. Murphy Identification of S-nitrosated mitochondrial proteins by S-nitrosothiol difference in gel electrophoresis (SNO-DIGE): implications for the regulation of mitochondrial function by reversible S-nitrosation Biochem. J. 430 2010 49 59
    • (2010) Biochem. J. , vol.430 , pp. 49-59
    • Chouchani, E.T.1    Hurd, T.R.2    Nadtochiy, S.M.3    Brookes, P.S.4    Fearnley, I.M.5    Lilley, K.S.6    Lilley, K.S.7    Smith, R.A.J.8    Murphy, M.P.9
  • 12
    • 28044464985 scopus 로고
    • Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases
    • M.W. Cleeter, J.M. Cooper, V.M. Darley-Usmar, S. Moncada, and A.H. Schapira Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases FEBS Lett. 345 1994 50 54
    • (1994) FEBS Lett. , vol.345 , pp. 50-54
    • Cleeter, M.W.1    Cooper, J.M.2    Darley-Usmar, V.M.3    Moncada, S.4    Schapira, A.H.5
  • 13
    • 0030566801 scopus 로고    scopus 로고
    • Nitric oxide inhibits the cytochrome oxidase but not the alternative oxidase of plant mitochondria
    • A.H. Millar, and D.A. Day Nitric oxide inhibits the cytochrome oxidase but not the alternative oxidase of plant mitochondria FEBS Lett. 398 1996 155 158
    • (1996) FEBS Lett. , vol.398 , pp. 155-158
    • Millar, A.H.1    Day, D.A.2
  • 15
    • 0029963244 scopus 로고    scopus 로고
    • Rapid reduction of nitric oxide by mitochondria, and reversible inhibition of mitochondrial respiration by nitric oxide
    • V. Borutaité, and G.C. Brown Rapid reduction of nitric oxide by mitochondria, and reversible inhibition of mitochondrial respiration by nitric oxide Biochem. J. 315 1996 295 299
    • (1996) Biochem. J. , vol.315 , pp. 295-299
    • Borutaité, V.1    Brown, G.C.2
  • 17
    • 33745603712 scopus 로고    scopus 로고
    • S-nitrosothiol inhibition of mitochondrial complex i causes a reversible increase in mitochondrial hydrogen peroxide production
    • V. Borutaite, and G.C. Brown S-nitrosothiol inhibition of mitochondrial complex I causes a reversible increase in mitochondrial hydrogen peroxide production Biochim. Biophys. Acta 1757 2006 562 566
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 562-566
    • Borutaite, V.1    Brown, G.C.2
  • 18
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: Crucial role of S-nitrosylation of mitochondrial complex i and protective action of glutathione
    • E. Clementi, G.C. Brown, M. Feelisch, and S. Moncada Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione Proc. Natl. Acad. Sci. U. S. A. 95 1998 7631 7636
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 20
    • 77952055233 scopus 로고    scopus 로고
    • Reactive oxygen species and nitric oxide in plant mitochondria: Origin and redundant regulatory systems
    • O. Blokhina, and K.V. Fagerstedt Reactive oxygen species and nitric oxide in plant mitochondria: origin and redundant regulatory systems Physiol. Plant. 138 2010 447 462
    • (2010) Physiol. Plant. , vol.138 , pp. 447-462
    • Blokhina, O.1    Fagerstedt, K.V.2
  • 21
    • 78651413976 scopus 로고    scopus 로고
    • Integrative response of plant mitochondrial electron transport chain to nitrogen source
    • T. Hachiya, and K. Noguchi Integrative response of plant mitochondrial electron transport chain to nitrogen source Plant Cell Rep. 30 2011 195 204
    • (2011) Plant Cell Rep. , vol.30 , pp. 195-204
    • Hachiya, T.1    Noguchi, K.2
  • 22
    • 78650888657 scopus 로고    scopus 로고
    • Regulation of thermogenesis in plants: The interaction of alternative oxidase and plant uncoupling mitochondrial protein
    • Y. Zhu, J. Lu, J. Wang, F. Chen, F. Leng, and H. Li Regulation of thermogenesis in plants: the interaction of alternative oxidase and plant uncoupling mitochondrial protein J. Integr. Plant Biol. 53 2011 7 13
    • (2011) J. Integr. Plant Biol. , vol.53 , pp. 7-13
    • Zhu, Y.1    Lu, J.2    Wang, J.3    Chen, F.4    Leng, F.5    Li, H.6
  • 23
    • 79960484330 scopus 로고    scopus 로고
    • Alterations in the mitochondrial alternative NAD(P)H Dehydrogenase NDB4 lead to changes in mitochondrial electron transport chain composition, plant growth and response to oxidative stress
    • C. Smith, M. Barthet, V. Melino, P. Smith, D. Day, and K. Soole Alterations in the mitochondrial alternative NAD(P)H Dehydrogenase NDB4 lead to changes in mitochondrial electron transport chain composition, plant growth and response to oxidative stress Plant Cell Physiol. 52 2011 1222 1237
    • (2011) Plant Cell Physiol. , vol.52 , pp. 1222-1237
    • Smith, C.1    Barthet, M.2    Melino, V.3    Smith, P.4    Day, D.5    Soole, K.6
  • 24
    • 0036944847 scopus 로고    scopus 로고
    • Nitric oxide induces transcriptional activation of the nitric oxide-tolerant alternative oxidase in Arabidopsis suspension cells
    • X. Huang, U. von Rad, and J. Durner Nitric oxide induces transcriptional activation of the nitric oxide-tolerant alternative oxidase in Arabidopsis suspension cells Planta 215 2002 914 923
    • (2002) Planta , vol.215 , pp. 914-923
    • Huang, X.1    Von Rad, U.2    Durner, J.3
  • 25
    • 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
    • A. Wulff, H.C. Oliveira, E.E. Saviani, and I. Salgado 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 2009 132 139
    • (2009) Nitric Oxide , vol.21 , pp. 132-139
    • Wulff, A.1    Oliveira, H.C.2    Saviani, E.E.3    Salgado, I.4
  • 26
    • 84861481905 scopus 로고    scopus 로고
    • Alternative oxidase modulates leaf mitochondrial concentrations of superoxide and nitric oxide
    • M. Cvetkovska, and G.C. Vanlerberghe Alternative oxidase modulates leaf mitochondrial concentrations of superoxide and nitric oxide New Phytol. 195 2012 32 39
    • (2012) New Phytol. , vol.195 , pp. 32-39
    • Cvetkovska, M.1    Vanlerberghe, G.C.2
  • 27
    • 70450237830 scopus 로고    scopus 로고
    • Is the maintenance of homeostatic mitochondrial signaling during stress a physiological role for alternative oxidase?
    • G.C. Vanlerberghe, M. Cvetkovska, and J. Wang Is the maintenance of homeostatic mitochondrial signaling during stress a physiological role for alternative oxidase? Physiol. Plant. 137 2009 392 406
    • (2009) Physiol. Plant. , vol.137 , pp. 392-406
    • Vanlerberghe, G.C.1    Cvetkovska, M.2    Wang, J.3
  • 28
    • 43049095110 scopus 로고    scopus 로고
    • Nitric oxide degradation by potato tuber mitochondria: Evidence for the involvement of external NAD(P)H dehydrogenases
    • H.C. de Oliveira, A. Wulff, E.E. Saviani, and I. Salgado Nitric oxide degradation by potato tuber mitochondria: evidence for the involvement of external NAD(P)H dehydrogenases Biochim. Biophys. Acta 1777 2008 470 476
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 470-476
    • De Oliveira, H.C.1    Wulff, A.2    Saviani, E.E.3    Salgado, I.4
  • 30
    • 1642451708 scopus 로고    scopus 로고
    • Overexpression of plant uncoupling mitochondrial protein in transgenic tobacco increases tolerance to oxidative stress
    • M. Brandalise, I.G. Maia, J. Borecký, A.E. Vercesi, and P. Arruda Overexpression of plant uncoupling mitochondrial protein in transgenic tobacco increases tolerance to oxidative stress J. Bioenerg. Biomembr. 35 2003 203 209
    • (2003) J. Bioenerg. Biomembr. , vol.35 , pp. 203-209
    • Brandalise, M.1    Maia, I.G.2    Borecký, J.3    Vercesi, A.E.4    Arruda, P.5
  • 32
    • 0033080394 scopus 로고    scopus 로고
    • S-nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitrosoglutathione
    • Y. Ji, T.P. Akerboom, H. Sies, and J.A. Thomas S-nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitrosoglutathione Arch. Biochem. Biophys. 362 1999 67 78
    • (1999) Arch. Biochem. Biophys. , vol.362 , pp. 67-78
    • Ji, Y.1    Akerboom, T.P.2    Sies, H.3    Thomas, J.A.4
  • 33
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • L. Liu, A. Hausladen, M. Zeng, L. Que, J. Heitman, and J.S. Stamler A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans Nature 410 2001 490 494
    • (2001) Nature , vol.410 , pp. 490-494
    • Liu, L.1    Hausladen, A.2    Zeng, M.3    Que, L.4    Heitman, J.5    Stamler, J.S.6
  • 34
    • 0032522535 scopus 로고    scopus 로고
    • S-nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme
    • D.E. Jensen, G.K. Belka, and G.C. Du Bois S-nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme Biochem. J. 331 1998 659 668
    • (1998) Biochem. J. , vol.331 , pp. 659-668
    • Jensen, D.E.1    Belka, G.K.2    Du Bois, G.C.3
  • 35
    • 0042510382 scopus 로고    scopus 로고
    • Enhanced formaldehyde detoxification by overexpression of glutathione-dependent formaldehyde dehydrogenase from Arabidopsis
    • H. Achkor, M. Díaz, M.R. Ferna, J.A. Biosca, X. Pares, and M.C. Martínez Enhanced formaldehyde detoxification by overexpression of glutathione-dependent formaldehyde dehydrogenase from Arabidopsis Plant Physiol. 132 2003 2248 2255
    • (2003) Plant Physiol. , vol.132 , pp. 2248-2255
    • Achkor, H.1    Díaz, M.2    Ferna, M.R.3    Biosca, J.A.4    Pares, X.5    Martínez, M.C.6
  • 36
    • 34250665400 scopus 로고    scopus 로고
    • S-nitrosoglutathione reductase affords protection against pathogens in Arabidopsis, both locally and systemically
    • C. Rustérucci, M.C. Espunya, M. Díaz, M. Chabannes, and M.C. Martínez S-nitrosoglutathione reductase affords protection against pathogens in Arabidopsis, both locally and systemically Plant Physiol. 143 2007 1282 1292
    • (2007) Plant Physiol. , vol.143 , pp. 1282-1292
    • Rustérucci, C.1    Espunya, M.C.2    Díaz, M.3    Chabannes, M.4    Martínez, M.C.5
  • 38
    • 48249090109 scopus 로고    scopus 로고
    • Modulation of nitrosative stress by S-nitrosoglutathione reductase is critical for thermotolerance and plant growth in Arabidopsis
    • U. Lee, C. Wie, B.O. Fernandez, M. Feelisch, and E. Vierling Modulation of nitrosative stress by S-nitrosoglutathione reductase is critical for thermotolerance and plant growth in Arabidopsis Plant Cell 20 2008 786 802
    • (2008) Plant Cell , vol.20 , pp. 786-802
    • Lee, U.1    Wie, C.2    Fernandez, B.O.3    Feelisch, M.4    Vierling, E.5
  • 39
    • 71749115983 scopus 로고    scopus 로고
    • The Arabidopsis PARAQUAT RESISTANT2 gene encodes an S-nitrosoglutathione reductase that is a key regulator of cell death
    • R. Chen, S. Sun, C. Wang, Y. Li, Y. Liang, F. An, C. Li, H. Dong, X. Yang, J. Zhang, and J. Zuo The Arabidopsis PARAQUAT RESISTANT2 gene encodes an S-nitrosoglutathione reductase that is a key regulator of cell death Cell Res. 19 2009 1377 1387
    • (2009) Cell Res. , vol.19 , pp. 1377-1387
    • Chen, R.1    Sun, S.2    Wang, C.3    Li, Y.4    Liang, Y.5    An, F.6    Li, C.7    Dong, H.8    Yang, X.9    Zhang, J.10    Zuo, J.11
  • 40
    • 84860481279 scopus 로고    scopus 로고
    • Regulation of mitochondrial processes by protein S-nitrosylation
    • C.A. Piantadosi Regulation of mitochondrial processes by protein S-nitrosylation Biochim. Biophys. Acta 1820 2012 712 721
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 712-721
    • Piantadosi, C.A.1
  • 41
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bio assays with tobacco tissue cultures
    • T. Murashige, and F. Skoog A revised medium for rapid growth and bio assays with tobacco tissue cultures Physiol. Plant. 15 1962 473 479
    • (1962) Physiol. Plant. , vol.15 , pp. 473-479
    • Murashige, T.1    Skoog, F.2
  • 42
    • 0037181505 scopus 로고    scopus 로고
    • Arabidopsis glutathione-dependent formaldehyde desydrogenase is an S-nitrosoglutathione reductase
    • A. Sakamoto, M. Ueda, and H. Morikawa Arabidopsis glutathione-dependent formaldehyde desydrogenase is an S-nitrosoglutathione reductase FEBS Lett. 515 2002 20 24
    • (2002) FEBS Lett. , vol.515 , pp. 20-24
    • Sakamoto, A.1    Ueda, M.2    Morikawa, H.3
  • 43
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 44
    • 37049066149 scopus 로고
    • A scheme for the colorimetric determination of microgram amounts of thiols
    • B. Saville A scheme for the colorimetric determination of microgram amounts of thiols Analyst 83 1958 670 672
    • (1958) Analyst , vol.83 , pp. 670-672
    • Saville, B.1
  • 45
    • 0037073738 scopus 로고    scopus 로고
    • Interfering with nitric oxide measurements. 4,5-diaminofluorescein reacts with dehydroascorbic acid and ascorbic acid
    • X. Zhang, W.S. Kim, N. Hatcher, K. Potgieter, L.L. Moroz, R. Gillette, and J.V. Sweedler Interfering with nitric oxide measurements. 4,5-diaminofluorescein reacts with dehydroascorbic acid and ascorbic acid J. Biol. Chem. 277 2002 48472 48478
    • (2002) J. Biol. Chem. , vol.277 , pp. 48472-48478
    • Zhang, X.1    Kim, W.S.2    Hatcher, N.3    Potgieter, K.4    Moroz, L.L.5    Gillette, R.6    Sweedler, J.V.7
  • 46
    • 11944258348 scopus 로고    scopus 로고
    • Measurement of nitric oxide by 4,5-diaminofluorescein without interferences
    • X. Ye, W.-S. Kim, S.S. Rubakhin, and J.V. Sweedler Measurement of nitric oxide by 4,5-diaminofluorescein without interferences Analyst 129 2004 1200 1205
    • (2004) Analyst , vol.129 , pp. 1200-1205
    • Ye, X.1    Kim, W.-S.2    Rubakhin, S.S.3    Sweedler, J.V.4
  • 47
    • 36949011847 scopus 로고    scopus 로고
    • Isolation of mitochondria from embryogenic cultures of Picea abies (L.) Karst. and Abies cephalonica Loud.: Characterization of a K+(ATP) channel
    • E. Petrussa, A. Bertolini, J. Krajnáková, V. Casolo, F. Macrì, and A. Vianello Isolation of mitochondria from embryogenic cultures of Picea abies (L.) Karst. and Abies cephalonica Loud.: characterization of a K+(ATP) channel Plant Cell Rep. 27 2008 137 146
    • (2008) Plant Cell Rep. , vol.27 , pp. 137-146
    • Petrussa, E.1    Bertolini, A.2    Krajnáková, J.3    Casolo, V.4    MacRì, F.5    Vianello, A.6
  • 48
    • 0000087998 scopus 로고
    • Purification, characterization and storage of mitochondria from Jerusalem artichoke tubers
    • A.C. Lindén, and I.M. Moller Purification, characterization and storage of mitochondria from Jerusalem artichoke tubers Physiol. Plant. 72 1988 265 270
    • (1988) Physiol. Plant. , vol.72 , pp. 265-270
    • Lindén, A.C.1    Moller, I.M.2
  • 51
    • 0031899561 scopus 로고    scopus 로고
    • Fatty acid-mediated uncoupling of potato tuber mitochondria
    • E.E. Saviani, and I.S. Martins Fatty acid-mediated uncoupling of potato tuber mitochondria IUBMB Life 44 1998 833 839
    • (1998) IUBMB Life , vol.44 , pp. 833-839
    • Saviani, E.E.1    Martins, I.S.2
  • 52
    • 68949155541 scopus 로고    scopus 로고
    • Differential gene expression profiles of the mitochondrial respiratory components in illuminated Arabidopsis leaves
    • K. Yoshida, and K. Noguchi Differential gene expression profiles of the mitochondrial respiratory components in illuminated Arabidopsis leaves Plant Cell Physiol. 50 2009 1449 1462
    • (2009) Plant Cell Physiol. , vol.50 , pp. 1449-1462
    • Yoshida, K.1    Noguchi, K.2
  • 54
    • 81055143827 scopus 로고    scopus 로고
    • Detection and quantification of S-nitrosoglutathione (GSNO) in pepper (Capsicum annuum L.) plant organs by LC-ES/MS
    • M. Airaki, L. Sánchez-Moreno, M. Leterrier, J.B. Barroso, J.M. Palma, and F.J. Corpas Detection and quantification of S-nitrosoglutathione (GSNO) in pepper (Capsicum annuum L.) plant organs by LC-ES/MS Plant Cell Physiol. 52 2011 2006 2015
    • (2011) Plant Cell Physiol. , vol.52 , pp. 2006-2015
    • Airaki, M.1    Sánchez-Moreno, L.2    Leterrier, M.3    Barroso, J.B.4    Palma, J.M.5    Corpas, F.J.6
  • 56
    • 33645721277 scopus 로고    scopus 로고
    • Modification of intracellular levels of glutathione-dependent formaldehyde dehydrogenase alters glutathione homeostasis and root development
    • M.C. Espunya, M. Diaz, J. Moreno-Romero, and M.C. Martinez Modification of intracellular levels of glutathione-dependent formaldehyde dehydrogenase alters glutathione homeostasis and root development Plant Cell Environ. 29 2006 1002 1011
    • (2006) Plant Cell Environ. , vol.29 , pp. 1002-1011
    • Espunya, M.C.1    Diaz, M.2    Moreno-Romero, J.3    Martinez, M.C.4
  • 57
    • 79957940923 scopus 로고    scopus 로고
    • Nitric oxide enhances desiccation tolerance of recalcitrant Antiaris toxicaria seeds via protein S-nitrosylation and carbonylation
    • X. Bai, L. Yang, M. Tian, J. Chen, J. Shi, Y. Yang, and X. Hu Nitric oxide enhances desiccation tolerance of recalcitrant Antiaris toxicaria seeds via protein S-nitrosylation and carbonylation PLoS One 6 2011 e20714
    • (2011) PLoS One , vol.6 , pp. 20714
    • Bai, X.1    Yang, L.2    Tian, M.3    Chen, J.4    Shi, J.5    Yang, Y.6    Hu, X.7
  • 61
    • 1342329794 scopus 로고    scopus 로고
    • Nitric oxide functions as a signal in salt resistance in the calluses from two ecotypes of reed
    • L. Zhao, F. Zhang, J. Guo, Y. Yang, B. Li, and L. Zhang Nitric oxide functions as a signal in salt resistance in the calluses from two ecotypes of reed Plant Physiol. 134 2004 849 857
    • (2004) Plant Physiol. , vol.134 , pp. 849-857
    • Zhao, L.1    Zhang, F.2    Guo, J.3    Yang, Y.4    Li, B.5    Zhang, L.6
  • 64
    • 25444469412 scopus 로고    scopus 로고
    • Mitochondrial metabolism of reactive oxygen species
    • A.Y. Andreyev, Y.E. Kushnareva, and A.A. Starkov Mitochondrial metabolism of reactive oxygen species Biochemistry 70 2005 200 214
    • (2005) Biochemistry , vol.70 , pp. 200-214
    • Andreyev, A.Y.1    Kushnareva, Y.E.2    Starkov, A.A.3
  • 65
    • 0036244508 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite interactions with mitochondria
    • R. Radi, A. Cassina, and R. Hodara Nitric oxide and peroxynitrite interactions with mitochondria Biol. Chem. 383 2002 401 409
    • (2002) Biol. Chem. , vol.383 , pp. 401-409
    • Radi, R.1    Cassina, A.2    Hodara, R.3
  • 66
    • 77953067310 scopus 로고    scopus 로고
    • The expression, function and regulation of mitochondrial alternative oxidase under biotic stresses
    • H. Feng, K. Sun, M. Li, H. Li, X. Li, Y. Li, and Y. Wang The expression, function and regulation of mitochondrial alternative oxidase under biotic stresses Mol. Plant Pathol. 11 2010 429 440
    • (2010) Mol. Plant Pathol. , vol.11 , pp. 429-440
    • Feng, H.1    Sun, K.2    Li, M.3    Li, H.4    Li, X.5    Li, Y.6    Wang, Y.7
  • 68
    • 36049029610 scopus 로고    scopus 로고
    • Low oxygen sensing and balancing in plant seeds: A role for nitric oxide
    • L. Borisjuk, D. Macherel, A. Benamar, U. Wobus, and H. Rolletschek Low oxygen sensing and balancing in plant seeds: a role for nitric oxide New Phytol. 176 2007 813 823
    • (2007) New Phytol. , vol.176 , pp. 813-823
    • Borisjuk, L.1    MacHerel, D.2    Benamar, A.3    Wobus, U.4    Rolletschek, H.5
  • 69
    • 0035860428 scopus 로고    scopus 로고
    • Functional reconstitution of Arabidopsis thaliana plant uncoupling mitochondrial protein (AtPUMP1) expressed in Escherichia coli
    • J. Borecký, I.G. Maia, A.D.T. Costa, P. Jezek, H. Chaimovich, P.B.M. de Andrade, A.E. Vercesi, and P. Arruda Functional reconstitution of Arabidopsis thaliana plant uncoupling mitochondrial protein (AtPUMP1) expressed in Escherichia coli FEBS Lett. 505 2001 240 244
    • (2001) FEBS Lett. , vol.505 , pp. 240-244
    • Borecký, J.1    Maia, I.G.2    Costa, A.D.T.3    Jezek, P.4    Chaimovich, H.5    De Andrade, P.B.M.6    Vercesi, A.E.7    Arruda, P.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.