메뉴 건너뛰기




Volumn 4, Issue 8, 2005, Pages 1122-1133

Differential impact of environmental stresses of the pea mitochondrial proteome

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; HEAT SHOCK PROTEIN; HERBICIDE; LIPID; MITOCHONDRIAL PROTEIN; PROTEOME; THIOCTIC ACID; VEGETABLE PROTEIN;

EID: 24044461712     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M400210-MCP200     Document Type: Article
Times cited : (230)

References (55)
  • 1
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman, E. R. (1992) Protein oxidation and aging. Science 257, 1220-1224
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 2
    • 2542431031 scopus 로고    scopus 로고
    • Progression and specificity of protein oxidation in the life cycle of Arabidopsis thaliana
    • Johansson, E., Olsson, O., and Nystrom, T. (2004) Progression and specificity of protein oxidation in the life cycle of Arabidopsis thaliana. J. Biol. Chem. 279, 22204-22208
    • (2004) J. Biol. Chem. , vol.279 , pp. 22204-22208
    • Johansson, E.1    Olsson, O.2    Nystrom, T.3
  • 3
    • 3242776324 scopus 로고    scopus 로고
    • Identification of oxidised proteins in the matrix of rice leaf mitochondria by immunoprecipitation and two-dimensional liquid chromatography-tandem mass spectrometry
    • Kristensen, B. K., Askerlund, P., Bykova, N. V., Egsgaard, H., and Møller, I. M. (2004) Identification of oxidised proteins in the matrix of rice leaf mitochondria by immunoprecipitation and two-dimensional liquid chromatography-tandem mass spectrometry. Phytochemistry 65, 1839-1851
    • (2004) Phytochemistry , vol.65 , pp. 1839-1851
    • Kristensen, B.K.1    Askerlund, P.2    Bykova, N.V.3    Egsgaard, H.4    Møller, I.M.5
  • 5
    • 0038820056 scopus 로고    scopus 로고
    • Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins
    • Taylor, S. W., Fahy, E., Murray, J., Capaldi, R. A., and Ghosh, S. S. (2003) Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins. J. Biol. Chem. 278, 19587-19590
    • (2003) J. Biol. Chem. , vol.278 , pp. 19587-19590
    • Taylor, S.W.1    Fahy, E.2    Murray, J.3    Capaldi, R.A.4    Ghosh, S.S.5
  • 6
    • 0141706702 scopus 로고    scopus 로고
    • Protein tyrosine nitration in the mitochondria from diabetic mouse heart. Implications to dysfunctional mitochondria in diabetes
    • Turko, I. V., Li, L., Aulak, K. S., Stuehr, D. J., Chang, J. Y., and Murad, F. (2003) Protein tyrosine nitration in the mitochondria from diabetic mouse heart. Implications to dysfunctional mitochondria in diabetes. J. Biol. Chem. 278, 33972-33977
    • (2003) J. Biol. Chem. , vol.278 , pp. 33972-33977
    • Turko, I.V.1    Li, L.2    Aulak, K.S.3    Stuehr, D.J.4    Chang, J.Y.5    Murad, F.6
  • 7
    • 0037044794 scopus 로고    scopus 로고
    • Environmental stress causes oxidative damage to plant mitochondria leading to inhibition of glycine decarboxylase
    • Taylor, N. L., Day, D. A., and Millar, A. H. (2002) Environmental stress causes oxidative damage to plant mitochondria leading to inhibition of glycine decarboxylase. J. Biol. Chem. 277, 42663-42668
    • (2002) J. Biol. Chem. , vol.277 , pp. 42663-42668
    • Taylor, N.L.1    Day, D.A.2    Millar, A.H.3
  • 8
    • 1342286842 scopus 로고    scopus 로고
    • Inhibition of Krebs cycle and activation of glyoxylate cycle in the course of chronological aging of Saccharomyces cerevisiae. Compensatory role of succinate oxidation
    • Samokhvalov, V., Ignatov, V., and Kondrashova, M. (2004) Inhibition of Krebs cycle and activation of glyoxylate cycle in the course of chronological aging of Saccharomyces cerevisiae. Compensatory role of succinate oxidation. Biochimie (Paris) 86, 39-46
    • (2004) Biochimie (Paris) , vol.86 , pp. 39-46
    • Samokhvalov, V.1    Ignatov, V.2    Kondrashova, M.3
  • 11
    • 0036138947 scopus 로고    scopus 로고
    • A subset of newly synthesized polypeptides in mitochondria from human endothelial cells exposed to hydroperoxide stress
    • Mitsumoto, A., Takeuchi, A., Okawa, K., and Nakagawa, Y. (2002) A subset of newly synthesized polypeptides in mitochondria from human endothelial cells exposed to hydroperoxide stress. Free Radic. Biol. Med. 32, 22-37
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 22-37
    • Mitsumoto, A.1    Takeuchi, A.2    Okawa, K.3    Nakagawa, Y.4
  • 12
    • 0023679752 scopus 로고
    • Mitochondria contain a proteolytic system which can recognize and degrade oxidatively-denatured proteins
    • Marcillat, O., Zhang, Y., Lin, S. W., and Davies, K. J. (1988) Mitochondria contain a proteolytic system which can recognize and degrade oxidatively-denatured proteins. Biochem. J. 254, 677-683
    • (1988) Biochem. J. , vol.254 , pp. 677-683
    • Marcillat, O.1    Zhang, Y.2    Lin, S.W.3    Davies, K.J.4
  • 13
  • 14
    • 10644296999 scopus 로고    scopus 로고
    • Mitochondrial protein oxidation in yeast mutants lacking Mn or CuZn superoxide dismutase. Evidence that MnSOD and CuZnSOD have both unique and overlapping functions in protecting mitochondrial proteins from oxidative damage
    • O'Brien, K. M., Dirmeier, R., Engle, M., and Poyton, R. O. (2004) Mitochondrial protein oxidation in yeast mutants lacking Mn or CuZn superoxide dismutase. Evidence that MnSOD and CuZnSOD have both unique and overlapping functions in protecting mitochondrial proteins from oxidative damage. J. Biol. Chem. 279, 51817-51827
    • (2004) J. Biol. Chem. , vol.279 , pp. 51817-51827
    • O'Brien, K.M.1    Dirmeier, R.2    Engle, M.3    Poyton, R.O.4
  • 15
    • 0028002821 scopus 로고
    • A low molecular mass heat-shock protein is localized to higher plant mitochondria
    • Lenne, C., and Douce, R. (1994) A low molecular mass heat-shock protein is localized to higher plant mitochondria. Plant Physiol. 105, 1255-1261
    • (1994) Plant Physiol. , vol.105 , pp. 1255-1261
    • Lenne, C.1    Douce, R.2
  • 16
    • 0032005909 scopus 로고    scopus 로고
    • Accumulation of small heat shock proteins, including mitochondrial HSP22, induced by oxidative stress and adaptive response in tomato cells
    • Banzet, N., Richaud, C., Deveaux, Y., Kazmaier, M., Gagnon, J., and Triantaphylidès, C. (1998) Accumulation of small heat shock proteins, including mitochondrial HSP22, induced by oxidative stress and adaptive response in tomato cells. Plant J. 13, 519-527
    • (1998) Plant J. , vol.13 , pp. 519-527
    • Banzet, N.1    Richaud, C.2    Deveaux, Y.3    Kazmaier, M.4    Gagnon, J.5    Triantaphylidès, C.6
  • 18
    • 0030821356 scopus 로고    scopus 로고
    • Regulation of heat shock gene induction and expression during Drosophila development
    • Michaud, S., Marin, R., and Tanguay, R. M. (1997) Regulation of heat shock gene induction and expression during Drosophila development. Cell. Mol. Life Sci. 53, 104-113
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 104-113
    • Michaud, S.1    Marin, R.2    Tanguay, R.M.3
  • 19
    • 2442649342 scopus 로고    scopus 로고
    • Overexpression of the small mitochondrial Hsp22 extends Drosophila life span and increases resistance to oxidative stress
    • Morrow, G., Samson, M., Michaud, S., and Tanguay, R. M. (2004) Overexpression of the small mitochondrial Hsp22 extends Drosophila life span and increases resistance to oxidative stress. FASEB J. 18, 598-599
    • (2004) FASEB J. , vol.18 , pp. 598-599
    • Morrow, G.1    Samson, M.2    Michaud, S.3    Tanguay, R.M.4
  • 20
    • 6344286028 scopus 로고    scopus 로고
    • Decreased lifespan in the absence of expression of the mitochondrial small heat shock protein Hsp22 in Drosophila
    • Morrow, G., Battistini, S., Zhang, P., and Tanguay, R. M. (2004) Decreased lifespan in the absence of expression of the mitochondrial small heat shock protein Hsp22 in Drosophila. J. Biol. Chem. 279, 43382-43385
    • (2004) J. Biol. Chem. , vol.279 , pp. 43382-43385
    • Morrow, G.1    Battistini, S.2    Zhang, P.3    Tanguay, R.M.4
  • 21
    • 0038705126 scopus 로고    scopus 로고
    • Leaf mitochondria modulate whole cell redox homeostasis, set antioxidant capacity, and determine stress resistance through altered signaling and diurnal regulation
    • Dutilleul, C., Garmier, M., Noctor, G., Mathieu, C., Chetrit, P., Foyer, C. H., and de Paepe, R. (2003) Leaf mitochondria modulate whole cell redox homeostasis, set antioxidant capacity, and determine stress resistance through altered signaling and diurnal regulation. Plant Cell 15, 1212-1226
    • (2003) Plant Cell , vol.15 , pp. 1212-1226
    • Dutilleul, C.1    Garmier, M.2    Noctor, G.3    Mathieu, C.4    Chetrit, P.5    Foyer, C.H.6    de Paepe, R.7
  • 22
    • 2442698814 scopus 로고    scopus 로고
    • Mitochondrial respiratory deficiencies signal up-regulation of genes for heat shock proteins
    • Kuzmin, E. V., Karpova, O. V., Elthon, T. E., and Newton, K. J. (2004) Mitochondrial respiratory deficiencies signal up-regulation of genes for heat shock proteins. J. Biol. Chem. 279, 20672-20677
    • (2004) J. Biol. Chem. , vol.279 , pp. 20672-20677
    • Kuzmin, E.V.1    Karpova, O.V.2    Elthon, T.E.3    Newton, K.J.4
  • 23
    • 1542318096 scopus 로고    scopus 로고
    • Initiation of neuronal damage by complex I deficiency and oxidative stress in Parkinson's disease
    • Tretter, L., Sipos, I., and Adam-Vizi, V. (2004) Initiation of neuronal damage by complex I deficiency and oxidative stress in Parkinson's disease. Neurochem. Res. 29, 569-577
    • (2004) Neurochem. Res. , vol.29 , pp. 569-577
    • Tretter, L.1    Sipos, I.2    Adam-Vizi, V.3
  • 24
    • 1042268861 scopus 로고    scopus 로고
    • Mitochondrial complex I mutations in Caenorhabditis elegans produce cytochrome c oxidase deficiency, oxidative stress and vitamin-responsive lactic acidosis
    • Grad, L. I., and Lemire, B. D. (2004) Mitochondrial complex I mutations in Caenorhabditis elegans produce cytochrome c oxidase deficiency, oxidative stress and vitamin-responsive lactic acidosis. Hum. Mol. Genet. 13, 303-314
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 303-314
    • Grad, L.I.1    Lemire, B.D.2
  • 25
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: Electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • Møller, I. M. (2001) Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52, 561-591
    • (2001) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.52 , pp. 561-591
    • Møller, I.M.1
  • 26
    • 0034717135 scopus 로고    scopus 로고
    • Mitochondria of Saccharomyces cerevisiae contain one conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity
    • Pedrajas, J. R., Miranda-Vizuete, A., Javanmardy, N., Gustafsson, J. A., and Spyrou, G. (2000) Mitochondria of Saccharomyces cerevisiae contain one conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity. J. Biol. Chem. 275, 16296-16301
    • (2000) J. Biol. Chem. , vol.275 , pp. 16296-16301
    • Pedrajas, J.R.1    Miranda-Vizuete, A.2    Javanmardy, N.3    Gustafsson, J.A.4    Spyrou, G.5
  • 27
    • 0035469416 scopus 로고    scopus 로고
    • The mitochondrial antioxidant defence system and its response to oxidative stress
    • Rabilloud, T., Heller, M., Rigobello, M. P., Bindoli, A., Aebersold, R., and Lunardi, J. (2001) The mitochondrial antioxidant defence system and its response to oxidative stress. Proteomics 1, 1105-1110
    • (2001) Proteomics , vol.1 , pp. 1105-1110
    • Rabilloud, T.1    Heller, M.2    Rigobello, M.P.3    Bindoli, A.4    Aebersold, R.5    Lunardi, J.6
  • 29
    • 0344875538 scopus 로고    scopus 로고
    • Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants
    • Chew, O., Whelan, J., 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
    • (2003) J. Biol. Chem. , vol.278 , pp. 46869-46877
    • Chew, O.1    Whelan, J.2    Millar, A.H.3
  • 32
    • 0038066347 scopus 로고    scopus 로고
    • Molecular responses to drought, salinity and frost: Common and different paths for plant protection
    • Seki, M., Kamei, A., Yamaguchi-Shinozaki, K., and Shinozaki, K. (2003) Molecular responses to drought, salinity and frost: common and different paths for plant protection. Curr. Opin. Biotechnol. 14, 194-199
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 194-199
    • Seki, M.1    Kamei, A.2    Yamaguchi-Shinozaki, K.3    Shinozaki, K.4
  • 33
    • 0038643713 scopus 로고    scopus 로고
    • Environmental stresses inhibit and stimulate different protein import pathways in plant mitochondria
    • Taylor, N. L., Rudhe, C., Hulett, J. M., Lithgow, T., Glaser, E., Day, D. A., Millar, A. H., and Whelan, J. (2003) Environmental stresses inhibit and stimulate different protein import pathways in plant mitochondria. FEBS Lett. 547, 125-130
    • (2003) FEBS Lett. , vol.547 , pp. 125-130
    • Taylor, N.L.1    Rudhe, C.2    Hulett, J.M.3    Lithgow, T.4    Glaser, E.5    Day, D.A.6    Millar, A.H.7    Whelan, J.8
  • 34
    • 0033030036 scopus 로고    scopus 로고
    • Improving the thiobarbituric acid-reactive-substances assay for estimating lipid peroxidation in plant tissues containing anthocyanin and other interfering compounds
    • Hodges, D. M., DeLong, J. M., Forney, C. F., and Prange, R. K. (1999) Improving the thiobarbituric acid-reactive-substances assay for estimating lipid peroxidation in plant tissues containing anthocyanin and other interfering compounds. Planta 207, 604-611
    • (1999) Planta , vol.207 , pp. 604-611
    • Hodges, D.M.1    DeLong, J.M.2    Forney, C.F.3    Prange, R.K.4
  • 35
    • 0000636038 scopus 로고
    • Biochemical characterization of chlorophyll-free mitochondria from pea leaves
    • Day, D. A., Neuburger, M., and Douce, R. (1985) Biochemical characterization of chlorophyll-free mitochondria from pea leaves. Aust. J. Plant Physiol. 12, 219-228
    • (1985) Aust. J. Plant Physiol. , vol.12 , pp. 219-228
    • Day, D.A.1    Neuburger, M.2    Douce, R.3
  • 36
    • 0029010327 scopus 로고
    • Activation of glycine decarboxylase in pea leaf mitochondria by ATP
    • Zhang, Q., and Wiskich, J. T. (1995) Activation of glycine decarboxylase in pea leaf mitochondria by ATP. Arch. Biochem. Biophys. 320, 250-256
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 250-256
    • Zhang, Q.1    Wiskich, J.T.2
  • 37
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson, G. L. (1977) A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83, 346-356
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 38
    • 0030111226 scopus 로고    scopus 로고
    • New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria
    • Jansch, L., Kruft, V., Schmitz, U. K., and Braun, H. P. (1996) New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria. Plant J. 9, 357-368
    • (1996) Plant J. , vol.9 , pp. 357-368
    • Jansch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 39
    • 0042232493 scopus 로고    scopus 로고
    • Thermal acclimation and the dynamic response of plant respiration to temperature
    • Atkin, O. K., and Tjoelker, M. G. (2003) Thermal acclimation and the dynamic response of plant respiration to temperature. Trends Plant Sci. 8, 343-351
    • (2003) Trends Plant Sci. , vol.8 , pp. 343-351
    • Atkin, O.K.1    Tjoelker, M.G.2
  • 41
  • 42
    • 0842270043 scopus 로고    scopus 로고
    • Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins
    • Heazlewood, J. L., Tonti-Filippini, J. S., Gout, A. M., Day, D. A., Whelan, J., and Millar, A. H. (2004) Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. Plant Cell 16, 241-256
    • (2004) Plant Cell , vol.16 , pp. 241-256
    • Heazlewood, J.L.1    Tonti-Filippini, J.S.2    Gout, A.M.3    Day, D.A.4    Whelan, J.5    Millar, A.H.6
  • 43
    • 0035851122 scopus 로고    scopus 로고
    • A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage
    • Sturtz, L. A., Diekert, K., Jensen, L. T., Lill, R., and Culotta, V. C. (2001) A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. J. Biol. Chem. 276, 38084-38089
    • (2001) J. Biol. Chem. , vol.276 , pp. 38084-38089
    • Sturtz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Culotta, V.C.5
  • 44
    • 0141786914 scopus 로고    scopus 로고
    • New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II
    • Eubel, H., Jansch, L., and Braun, H. P. (2003) New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II. Plant Physiol. 133, 274-286
    • (2003) Plant Physiol. , vol.133 , pp. 274-286
    • Eubel, H.1    Jansch, L.2    Braun, H.P.3
  • 45
    • 12344323931 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c oxidase and succinate dehydrogenase complexes contain plant-specific subunits
    • Millar, A. H., Eubel, H., Jänsch, L., Kruft, V., Heazlewood, J. L., and Braun, H. P. (2004) Mitochondrial cytochrome c oxidase and succinate dehydrogenase complexes contain plant-specific subunits. Plant Mol. Biol. 56, 77-89
    • (2004) Plant Mol. Biol. , vol.56 , pp. 77-89
    • Millar, A.H.1    Eubel, H.2    Jänsch, L.3    Kruft, V.4    Heazlewood, J.L.5    Braun, H.P.6
  • 46
    • 0034978178 scopus 로고    scopus 로고
    • Heat stress response in pea involves interaction of mitochondrial nucleoside diphosphate kinase with a novel 86-kilodalton protein
    • Escobar Galvis, M. L., Marttila, S., Hakansson, G., Forsberg, J., and Knorpp, C. (2001) Heat stress response in pea involves interaction of mitochondrial nucleoside diphosphate kinase with a novel 86-kilodalton protein. Plant Physiol. 126, 69-77
    • (2001) Plant Physiol. , vol.126 , pp. 69-77
    • Escobar Galvis, M.L.1    Marttila, S.2    Hakansson, G.3    Forsberg, J.4    Knorpp, C.5
  • 47
    • 0037459118 scopus 로고    scopus 로고
    • Insertion of hydrophobic membrane proteins into the inner mitochondrial membrane - A guided tour
    • Rehling, P., Pfanner, N., and Meisinger, C. (2003) Insertion of hydrophobic membrane proteins into the inner mitochondrial membrane - a guided tour. J. Mol. Biol. 326, 639-657
    • (2003) J. Mol. Biol. , vol.326 , pp. 639-657
    • Rehling, P.1    Pfanner, N.2    Meisinger, C.3
  • 48
    • 0035839601 scopus 로고    scopus 로고
    • In vivo modifications of the maize mitochondrial small heat stress protein, HSP22
    • Lund, A. A., Rhoads, D. M., Lund, A. L., Cerny, R. L., and Elthon, T. E. (2001) In vivo modifications of the maize mitochondrial small heat stress protein, HSP22. J. Biol. Chem. 276, 29924-29929
    • (2001) J. Biol. Chem. , vol.276 , pp. 29924-29929
    • Lund, A.A.1    Rhoads, D.M.2    Lund, A.L.3    Cerny, R.L.4    Elthon, T.E.5
  • 49
    • 3943071150 scopus 로고    scopus 로고
    • Cytochrome c-mediated apoptosis
    • Jiang, X., and Wang, X. (2004) Cytochrome c-mediated apoptosis. Annu. Rev. Biochem. 73, 87-106
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 87-106
    • Jiang, X.1    Wang, X.2
  • 50
    • 0034871674 scopus 로고    scopus 로고
    • The PET1-CMS mitochondrial mutation in sunflower is associated with premature programmed cell death and cytochrome c release
    • Balk, J., and Leaver, C. J. (2001) The PET1-CMS mitochondrial mutation in sunflower is associated with premature programmed cell death and cytochrome c release. Plant Cell 13, 1803-1818
    • (2001) Plant Cell , vol.13 , pp. 1803-1818
    • Balk, J.1    Leaver, C.J.2
  • 51
    • 3242774742 scopus 로고    scopus 로고
    • A proteomic analysis of plant programmed cell death
    • Swidzinski, J. A., Leaver, C. J., and Sweetlove, L. J. (2004) A proteomic analysis of plant programmed cell death. Phytochemistry 65, 1829-1838
    • (2004) Phytochemistry , vol.65 , pp. 1829-1838
    • Swidzinski, J.A.1    Leaver, C.J.2    Sweetlove, L.J.3
  • 52
    • 0034192503 scopus 로고    scopus 로고
    • Does the plant mitochondrion integrate cellular stress and regulate programmed cell death?
    • Jones, A. (2000) Does the plant mitochondrion integrate cellular stress and regulate programmed cell death? Trends Plant Sci. 5, 225-230
    • (2000) Trends Plant Sci. , vol.5 , pp. 225-230
    • Jones, A.1
  • 53
    • 0036001079 scopus 로고    scopus 로고
    • Active oxygen and cell death in cereal aleurone cells
    • Fath, A., Bethke, P., Beligni, V., and Jones, R. (2002) Active oxygen and cell death in cereal aleurone cells. J. Exp. Bot. 53, 1273-1282
    • (2002) J. Exp. Bot. , vol.53 , pp. 1273-1282
    • Fath, A.1    Bethke, P.2    Beligni, V.3    Jones, R.4
  • 54
    • 8444244951 scopus 로고    scopus 로고
    • The mitochondrion - An organelle commonly involved in programmed cell death in Arabidopsis thaliana
    • Yao, N., Eisfelder, B. J., Marvin, J., and Greenberg, J. T. (2004) The mitochondrion - an organelle commonly involved in programmed cell death in Arabidopsis thaliana. Plant J. 40, 596-610
    • (2004) Plant J. , vol.40 , pp. 596-610
    • Yao, N.1    Eisfelder, B.J.2    Marvin, J.3    Greenberg, J.T.4
  • 55
    • 0942298545 scopus 로고    scopus 로고
    • Endogenous mitochondrial oxidative stress: Neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice
    • Hinerfeld, D., Traini, M. D., Weinberger, R. P., Cochran, B., Doctrow, S. R., Harry, J., and Melov, S. (2004) Endogenous mitochondrial oxidative stress: neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice. J. Neurochem. 88, 657-667
    • (2004) J. Neurochem. , vol.88 , pp. 657-667
    • Hinerfeld, D.1    Traini, M.D.2    Weinberger, R.P.3    Cochran, B.4    Doctrow, S.R.5    Harry, J.6    Melov, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.