메뉴 건너뛰기




Volumn 57, Issue 7, 2016, Pages 1364-1376

ROS generation in peroxisomes and its role in cell signaling

Author keywords

Cell metabolism; Hydrogen peroxide (H2O2); Peroxisomes; ROS generation; ROS signaling; Superoxide radicals (O2 )

Indexed keywords

ANTIOXIDANT; REACTIVE OXYGEN METABOLITE;

EID: 84982067582     PISSN: 00320781     EISSN: 14719053     Source Type: Journal    
DOI: 10.1093/pcp/pcw076     Document Type: Review
Times cited : (271)

References (148)
  • 1
    • 0033513358 scopus 로고    scopus 로고
    • The water-water cycle in chloroplasts: Scavenging of active oxygens and dissipation of excess photons
    • Asada, K. (1999) The water-water cycle in chloroplasts: scavenging of active oxygens and dissipation of excess photons. Annu. Rev. Plant Physiol. Plant Mol. Biol. 50:601-639.
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 601-639
    • Asada, K.1
  • 2
    • 33745662408 scopus 로고    scopus 로고
    • Production and scavenging of reactive oxygen species in chloroplasts and their functions
    • Asada, K. (2006) Production and scavenging of reactive oxygen species in chloroplasts and their functions. Plant Physiol. 141:391-396.
    • (2006) Plant Physiol. , vol.141 , pp. 391-396
    • Asada, K.1
  • 3
    • 0015882208 scopus 로고
    • Subcellular location of superoxide dismutase in spinach leaves and preparation and properties of crystalline spinach superoxide dismutase
    • Asada, K., Urano, M. and Takahashi, M. (1973) Subcellular location of superoxide dismutase in spinach leaves and preparation and properties of crystalline spinach superoxide dismutase. Eur. J. Biochem. 36:257-266.
    • (1973) Eur. J. Biochem. , vol.36 , pp. 257-266
    • Asada, K.1    Urano, M.2    Takahashi, M.3
  • 4
    • 44349182030 scopus 로고    scopus 로고
    • Proteomic analysis of highly purified peroxisomes from etiolated soybean cotyledons
    • Arai, Y., Hayashi, M. and Nishimura, M. (2008) Proteomic analysis of highly purified peroxisomes from etiolated soybean cotyledons. Plant Cell Physiol. 49:526-539.
    • (2008) Plant Cell Physiol. , vol.49 , pp. 526-539
    • Arai, Y.1    Hayashi, M.2    Nishimura, M.3
  • 6
    • 84897423636 scopus 로고    scopus 로고
    • ROS as key players in plant stress signalling
    • Baxter, A., Mittler, R. and Suzuki, N. (2014) ROS as key players in plant stress signalling. J. Exp. Bot. 65:1229-1240.
    • (2014) J. Exp. Bot. , vol.65 , pp. 1229-1240
    • Baxter, A.1    Mittler, R.2    Suzuki, N.3
  • 9
    • 0000796913 scopus 로고
    • Ascorbate free radical reduction by glyoxysomal membranes
    • Bowditch, M. Y. and Donaldson, R. P. (1990) Ascorbate free radical reduction by glyoxysomal membranes. Plant Physiol. 94:531-537.
    • (1990) Plant Physiol. , vol.94 , pp. 531-537
    • Bowditch, M.Y.1    Donaldson, R.P.2
  • 10
    • 0029328498 scopus 로고
    • Peroxisomal copper, zinc superoxide dismutase: Characterization of the isoenzyme from watermelon cotyledons
    • Bueno, P., Varela, J., Giménez-Gallego, G. and del Río, L. A. (1995) Peroxisomal copper, zinc superoxide dismutase: characterization of the isoenzyme from watermelon cotyledons. Plant Physiol. 108:1151-1160.
    • (1995) Plant Physiol. , vol.108 , pp. 1151-1160
    • Bueno, P.1    Varela, J.2    Giménez-Gallego, G.3    Del Río, L.A.4
  • 12
    • 40749153546 scopus 로고    scopus 로고
    • Peroxisome proliferation, wound-activated responses and expression of peroxisome-associated genes are cross-regulated but uncoupled in Arabidopsis thaliana
    • Castillo, M. C., Sandalio, L. M., del Río, L. A. and León, J. (2008) Peroxisome proliferation, wound-activated responses and expression of peroxisome-associated genes are cross-regulated but uncoupled in Arabidopsis thaliana. Plant Cell Environ. 31:492-505.
    • (2008) Plant Cell Environ. , vol.31 , pp. 492-505
    • Castillo, M.C.1    Sandalio, L.M.2    Del Río, L.A.3    León, J.4
  • 13
    • 84942235155 scopus 로고    scopus 로고
    • Ripening of pepper (Capsicum annuum) fruit is characterized by an enhancement of protein tyrosine nitration
    • Chaki, M., Álvarez de Morales, P., Ruiz, C., Begara-Morales, J. C., Barroso, J. B., Corpas, F. J., et al. (2015) Ripening of pepper (Capsicum annuum) fruit is characterized by an enhancement of protein tyrosine nitration. Ann. Bot. 116:637-647.
    • (2015) Ann. Bot. , vol.116 , pp. 637-647
    • Chaki, M.1    Álvarez De Morales, P.2    Ruiz, C.3    Begara-Morales, J.C.4    Barroso, J.B.5    Corpas, F.J.6
  • 14
    • 15944411822 scopus 로고    scopus 로고
    • Salt-induced expression of peroxisome-associated genes requires components of the ethylene, jasmonate and abscisic acid signalling pathways
    • Charlton, W. L., Matsui, K., Johnson, B., Graham, I., Ohme-Takagi, M. and Baker, A. (2005) Salt-induced expression of peroxisome-associated genes requires components of the ethylene, jasmonate and abscisic acid signalling pathways. Plant Cell Environ. 28:513-524.
    • (2005) Plant Cell Environ. , vol.28 , pp. 513-524
    • Charlton, W.L.1    Matsui, K.2    Johnson, B.3    Graham, I.4    Ohme-Takagi, M.5    Baker, A.6
  • 15
    • 84942249810 scopus 로고    scopus 로고
    • Unravelling how plants benefit from ROS and NO reactions, while resisting oxidative stress
    • Considine, M. J., Sandalio, L. M. and Foyer, C. H. (2015) Unravelling how plants benefit from ROS and NO reactions, while resisting oxidative stress. Ann. Bot. 116:469-473.
    • (2015) Ann. Bot. , vol.116 , pp. 469-473
    • Considine, M.J.1    Sandalio, L.M.2    Foyer, C.H.3
  • 16
    • 84945470559 scopus 로고    scopus 로고
    • 2 in plant peroxisomes?
    • 2 in plant peroxisomes? Plant Biol. 17:1099-1103.
    • (2015) Plant Biol. , vol.17 , pp. 1099-1103
    • Corpas, F.J.1
  • 17
    • 84891500515 scopus 로고    scopus 로고
    • -) is endogenously produced in Arabidopsis peroxisomes and is overproduced under cadmium stress
    • -) is endogenously produced in Arabidopsis peroxisomes and is overproduced under cadmium stress. Ann. Bot. 113:87-96.
    • (2014) Ann. Bot. , vol.113 , pp. 87-96
    • Corpas, F.J.1    Barroso, J.B.2
  • 18
    • 84925042309 scopus 로고    scopus 로고
    • Reactive sulfur species (RSS): Possible new players in the oxidative metabolism of plant peroxisomes
    • Corpas, F. J. and Barroso, J. B. (2015) Reactive sulfur species (RSS): possible new players in the oxidative metabolism of plant peroxisomes. Front. Plant Sci. 6:116.
    • (2015) Front. Plant Sci. , vol.6 , pp. 116
    • Corpas, F.J.1    Barroso, J.B.2
  • 20
    • 0035212728 scopus 로고    scopus 로고
    • Peroxisomes as a source of reactive oxygen species and nitric oxide signal molecules
    • Corpas, F. J., Barroso, J. B. and del Río, L. A. (2001) Peroxisomes as a source of reactive oxygen species and nitric oxide signal molecules. Trends Plant Sci. 6:145-150.
    • (2001) Trends Plant Sci. , vol.6 , pp. 145-150
    • Corpas, F.J.1    Barroso, J.B.2    Del Río, L.A.3
  • 21
    • 71049127138 scopus 로고    scopus 로고
    • Peroxisomes as key organelles in the metabolism of reactive oxygen species, reactive nitrogen species, and reactive sulfur species in plants
    • Edited by Terlecky, S. R. and Titorenko, V. I, Research Signpost, Kerala, India
    • Corpas, F. J., Barroso, J. B., Palma, J. M. and del Río, L. A. (2009) Peroxisomes as key organelles in the metabolism of reactive oxygen species, reactive nitrogen species, and reactive sulfur species in plants. In Emergent Functions of the Peroxisome. Edited by Terlecky, S. R. and Titorenko, V. I. pp. 97-124. Research Signpost, Kerala, India.
    • (2009) Emergent Functions of the Peroxisome , pp. 97-124
    • Corpas, F.J.1    Barroso, J.B.2    Palma, J.M.3    Del Río, L.A.4
  • 23
    • 0032759685 scopus 로고    scopus 로고
    • Peroxisomal NADP-dependent isocitrate dehydrogenase. Characterization and activity regulation during natural senescence
    • Corpas, F. J., Barroso, J. B., Sandalio, L. M., Palma, J. M., Lupiáñez, J. A. and del Río, L. A. (1999) Peroxisomal NADP-dependent isocitrate dehydrogenase. Characterization and activity regulation during natural senescence. Plant Physiol. 121:921-928.
    • (1999) Plant Physiol. , vol.121 , pp. 921-928
    • Corpas, F.J.1    Barroso, J.B.2    Sandalio, L.M.3    Palma, J.M.4    Lupiáñez, J.A.5    Del Río, L.A.6
  • 25
    • 33747834591 scopus 로고    scopus 로고
    • The expression of different superoxide dismutase forms is cell-type dependent in olive (Olea europaea L.) leaves
    • Corpas, F. J., Fernández-Ocaña, A., Carreras, A., Valderrama, R., Luque, F., Esteban, F. J., et al (2006) The expression of different superoxide dismutase forms is cell-type dependent in olive (Olea europaea L.) leaves. Plant Cell Physiol. 47:984-994.
    • (2006) Plant Cell Physiol. , vol.47 , pp. 984-994
    • Corpas, F.J.1    Fernández-Ocaña, A.2    Carreras, A.3    Valderrama, R.4    Luque, F.5    Esteban, F.J.6
  • 26
    • 77949716151 scopus 로고
    • Metabolism of activated oxygen in peroxisomes from two Pisum sativum L. Cultivars with different sensitivity to sodium chloride
    • Corpas, F. J., Gómez, M., Hernández, J. A. and del Río, L. A. (1993a) Metabolism of activated oxygen in peroxisomes from two Pisum sativum L. cultivars with different sensitivity to sodium chloride. J. Plant Physiol. 141:160-165.
    • (1993) J. Plant Physiol. , vol.141 , pp. 160-165
    • Corpas, F.J.1    Gómez, M.2    Hernández, J.A.3    Del Río, L.A.4
  • 27
    • 0027180149 scopus 로고
    • Evidence for the presence of proteolytic activity in peroxisomes
    • Corpas, F. J., Palma, J. M., Gómez, M. and del Río, L. A. (1993b) 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    Gómez, M.3    Del Río, L.A.4
  • 28
    • 48949099436 scopus 로고    scopus 로고
    • Peroxisomal xanthine oxidoreductase: Characterization of the enzyme from pea (Pisum sativum L.) leaves
    • Corpas, F. J., Palma, J. M., Sandalio, L. M., Valderrama, R., Barroso, J. B. and del Río, L. A. (2008) Peroxisomal xanthine oxidoreductase: characterization of the enzyme from pea (Pisum sativum L.) leaves. J. Plant Physiol. 165:1319-1330.
    • (2008) J. Plant Physiol. , vol.165 , pp. 1319-1330
    • Corpas, F.J.1    Palma, J.M.2    Sandalio, L.M.3    Valderrama, R.4    Barroso, J.B.5    Del Río, L.A.6
  • 31
    • 0013897667 scopus 로고
    • Peroxisomes (microbodies and related particles)
    • De Duve, C. and Baudhuin, P. (1966) Peroxisomes (microbodies and related particles). Physiol. Rev. 46:323-357.
    • (1966) Physiol. Rev. , vol.46 , pp. 323-357
    • De Duve, C.1    Baudhuin, P.2
  • 32
    • 78751630784 scopus 로고    scopus 로고
    • Peroxisomes as a cellular source of reactive nitrogen species signal molecules
    • del Río, L. A. (2011) Peroxisomes as a cellular source of reactive nitrogen species signal molecules. Arch. Biochem. Biophys. 506:1-11.
    • (2011) Arch. Biochem. Biophys. , vol.506 , pp. 1-11
    • Del Río, L.A.1
  • 34
    • 84938144547 scopus 로고    scopus 로고
    • ROS and RNS in plant physiology: An overview
    • del Río, L. A. (2015) ROS and RNS in plant physiology: an overview. J. Exp. Bot. 66:2827-2837.
    • (2015) J. Exp. Bot. , vol.66 , pp. 2827-2837
    • Del Río, L.A.1
  • 35
    • 84930243147 scopus 로고    scopus 로고
    • Function of peroxisomes as a cellular source of nitric oxide and other reactive nitrogen species
    • Edited by Khan, M. N., Mobin, M., Mohammad, F. and Corpas, F. J, Springer International Publishing, Switzerland
    • del Río, L. A., Corpas, F. J., Barroso, J. B., López-Huertas, E. and Palma, J. M. (2014) Function of peroxisomes as a cellular source of nitric oxide and other reactive nitrogen species. In Nitric Oxide in Plants: Metabolism and Role in Stress Physiology. Edited by Khan, M. N., Mobin, M., Mohammad, F. and Corpas, F. J. pp. 33-55. Springer International Publishing, Switzerland.
    • (2014) Nitric Oxide in Plants: Metabolism and Role in Stress Physiology , pp. 33-55
    • Del Río, L.A.1    Corpas, F.J.2    Barroso, J.B.3    López-Huertas, E.4    Palma, J.M.5
  • 38
    • 0028887672 scopus 로고
    • Production of superoxide radicals in glyoxysomal membranes from castor bean endosperm
    • del Río, L. A. and Donaldson, R. P. (1995) Production of superoxide radicals in glyoxysomal membranes from castor bean endosperm. J. Plant Physiol. 146:283-287.
    • (1995) J. Plant Physiol. , vol.146 , pp. 283-287
    • Del Río, L.A.1    Donaldson, R.P.2
  • 40
    • 0000691592 scopus 로고
    • Immunocytochemical evidence for a peroxisomal localization of manganese superoxide dismutase in leaf protoplasts from a higher plant
    • del Río, L. A., Lyon, D. S., Olah, I., Glick, B. and Salin, M. L. (1983) Immunocytochemical evidence for a peroxisomal localization of manganese superoxide dismutase in leaf protoplasts from a higher plant. Planta 158:216-224.
    • (1983) Planta , vol.158 , pp. 216-224
    • Del Río, L.A.1    Lyon, D.S.2    Olah, I.3    Glick, B.4    Salin, M.L.5
  • 43
    • 0242585515 scopus 로고    scopus 로고
    • Mitochondrial and peroxisomal manganese superoxide dismutase: Differential expression during leaf senescence
    • del Río, L. A., Sandalio, L. M., Altomare, D. A. and Zilinskas, B. A. (2003a) Mitochondrial and peroxisomal manganese superoxide dismutase: differential expression during leaf senescence. J. Exp. Bot. 54:923-933.
    • (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
  • 44
    • 33745675163 scopus 로고    scopus 로고
    • Reactive oxygen species and reactive nitrogen species in peroxisomes. Production, scavenging, and role in cell signaling
    • del Río, L. A., Sandalio, L. M., Corpas, F. J., Palma, J. M. and Barroso, J. B. (2006) Reactive oxygen species and reactive nitrogen species in peroxisomes. Production, scavenging, and role in cell signaling. Plant Physiol. 141:330-335.
    • (2006) Plant Physiol. , vol.141 , pp. 330-335
    • Del Río, L.A.1    Sandalio, L.M.2    Corpas, F.J.3    Palma, J.M.4    Barroso, J.B.5
  • 45
    • 0025087348 scopus 로고
    • A new cellular function for peroxisomes related to oxygen free radicals?
    • del Río, L. A., Sandalio, L. M. and Palma, J. M. (1990) A new cellular function for peroxisomes related to oxygen free radicals? Experientia 46:989-992.
    • (1990) Experientia , vol.46 , pp. 989-992
    • Del Río, L.A.1    Sandalio, L.M.2    Palma, J.M.3
  • 47
    • 48949120153 scopus 로고    scopus 로고
    • Light induces peroxisome proliferation in Arabidopsis seedlings through the photoreceptor phytochrome A, the transcription factor HY5 HOMOLOG, and the peroxisomal protein PEROXIN11B
    • Desai, M. and Hu, J. (2008) Light induces peroxisome proliferation in Arabidopsis seedlings through the photoreceptor phytochrome A, the transcription factor HY5 HOMOLOG, and the peroxisomal protein PEROXIN11B. Plant Physiol. 146:1117-1127.
    • (2008) Plant Physiol. , vol.146 , pp. 1117-1127
    • Desai, M.1    Hu, J.2
  • 48
    • 0142057021 scopus 로고    scopus 로고
    • Plant peroxiredoxins
    • Dietz, K. J. (2003) Plant peroxiredoxins. Annu. Rev. Plant Biol. 54:93-107.
    • (2003) Annu. Rev. Plant Biol. , vol.54 , pp. 93-107
    • Dietz, K.J.1
  • 49
    • 0030681367 scopus 로고    scopus 로고
    • Characterization of endopeptidases from plant peroxisomes
    • Distefano, S., Palma, J. M. Gómez, M. and del Río, L. A. (1997) Characterization of endopeptidases from plant peroxisomes. Biochem. J. 327:399-405.
    • (1997) Biochem. J. , vol.327 , pp. 399-405
    • Distefano, S.1    Palma, J.M.2    Gómez, M.3    Del Río, L.A.4
  • 50
    • 0032874587 scopus 로고    scopus 로고
    • Proteolytic cleavage of plant proteins by peroxisomal endoproteases from senescent pea leaves
    • Distefano, S., Palma, J. M., McCarthy, I. and del Río, L. A. (1999) Proteolytic cleavage of plant proteins by peroxisomal endoproteases from senescent pea leaves. Planta 209:308-313.
    • (1999) Planta , vol.209 , pp. 308-313
    • Distefano, S.1    Palma, J.M.2    McCarthy, I.3    Del Río, L.A.4
  • 51
    • 64949203222 scopus 로고    scopus 로고
    • Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily
    • Dixon, D. P., Hawkins, T., Hussey, P. J. and Edwards, R. (2009) Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily. J. Exp. Bot. 60:1207-1218.
    • (2009) J. Exp. Bot. , vol.60 , pp. 1207-1218
    • Dixon, D.P.1    Hawkins, T.2    Hussey, P.J.3    Edwards, R.4
  • 53
    • 70350618069 scopus 로고    scopus 로고
    • Sub-cellular distribution of glutathione in an Arabidopsis mutant (vtc1) deficient in ascorbate
    • 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.
    • (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
  • 54
    • 67651049051 scopus 로고    scopus 로고
    • Photorespiratory metabolism: Genes, mutants, energetic, and redox signaling
    • Foyer, C. H., Bloom, A. J., Queval, G. and Noctor, G. (2009) Photorespiratory metabolism: genes, mutants, energetic, and redox signaling. Annu. Rev. Plant Biol. 60:455-484.
    • (2009) Annu. Rev. Plant Biol. , vol.60 , pp. 455-484
    • Foyer, C.H.1    Bloom, A.J.2    Queval, G.3    Noctor, G.4
  • 55
    • 26844496737 scopus 로고    scopus 로고
    • Oxidant and antioxidant signaling in plants: A re-evaluation of the concept of oxidative stress in a physiological context
    • Foyer, C. H. and Noctor, G. (2005) Oxidant and antioxidant signaling in plants: a re-evaluation of the concept of oxidative stress in a physiological context. Plant Cell Environ. 28:1056-1071.
    • (2005) Plant Cell Environ. , vol.28 , pp. 1056-1071
    • Foyer, C.H.1    Noctor, G.2
  • 56
    • 78650988662 scopus 로고    scopus 로고
    • Ascorbate and glutathione: The heart of the redox hub
    • Foyer, C. H. and Noctor, G. (2011) Ascorbate and glutathione: the heart of the redox hub. Plant Physiol. 155:2-18.
    • (2011) Plant Physiol. , vol.155 , pp. 2-18
    • Foyer, C.H.1    Noctor, G.2
  • 57
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich, I. (1995) Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64:97-112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 58
    • 84864050485 scopus 로고    scopus 로고
    • Role of peroxisomes in ROS/RNS-metabolism: Implications for human disease
    • Fransen, M., Nordgren, M., Wang, B. and Apanasets, O. (2012) Role of peroxisomes in ROS/RNS-metabolism: implications for human disease. Biochim. Biophys. Acta 1822:1363-1373.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1363-1373
    • Fransen, M.1    Nordgren, M.2    Wang, B.3    Apanasets, O.4
  • 59
    • 84946215987 scopus 로고    scopus 로고
    • Posttranslational protein modifications in plant metabolism
    • Friso, G. and van Wijk, K. J. (2015) Posttranslational protein modifications in plant metabolism. Plant Physiol. 169:1469-1487.
    • (2015) Plant Physiol. , vol.169 , pp. 1469-1487
    • Friso, G.1    Van Wijk, K.J.2
  • 61
    • 0242486385 scopus 로고    scopus 로고
    • Arabidopsis NDK1 is a component of ROS signaling by interacting with three catalases
    • Fukumatsu, Y., Yabe, N. and Hasunuma, K. (2003) Arabidopsis NDK1 is a component of ROS signaling by interacting with three catalases. Plant Cell Physiol. 44:982-989.
    • (2003) Plant Cell Physiol. , vol.44 , pp. 982-989
    • Fukumatsu, Y.1    Yabe, N.2    Hasunuma, K.3
  • 63
    • 0345393852 scopus 로고    scopus 로고
    • Entering a new era of research on plant peroxisomes
    • Hayashi, M. and Nishimura, M. (2003) Entering a new era of research on plant peroxisomes. Curr. Opin. Plant Biol. 6:577-582.
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 577-582
    • Hayashi, M.1    Nishimura, M.2
  • 64
    • 0035958005 scopus 로고    scopus 로고
    • Antioxidant system within yeast peroxisome. Biochemical and physiological characterization of CbPmp20 in the methylotrophic yeast Candida boidinii
    • Horiguchi, H., Yurimoto, H., Kato, N. and Sakai, Y. (2001) Antioxidant system within yeast peroxisome. Biochemical and physiological characterization of CbPmp20 in the methylotrophic yeast Candida boidinii. J. Biol. Chem. 276:14279-14288.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14279-14288
    • Horiguchi, H.1    Yurimoto, H.2    Kato, N.3    Sakai, Y.4
  • 66
    • 79954432514 scopus 로고    scopus 로고
    • Redox pioneer: Professor Irwin Fridovich
    • Imlay, J. A. (2011) Redox pioneer: Professor Irwin Fridovich. Antiox. Redox Signal. 14:335-340.
    • (2011) Antiox. Redox Signal. , vol.14 , pp. 335-340
    • Imlay, J.A.1
  • 68
    • 0031950765 scopus 로고    scopus 로고
    • Molecular characterization and physiological role of a glyoxysome-bound ascorbate peroxidase from spinach
    • Ishikawa, T., Yoshimura, K., Sakai, K., Tamoi, M., Takeda, T. and Shigeoka, S. (1998) Molecular characterization and physiological role of a glyoxysome-bound ascorbate peroxidase from spinach. Plant Cell Physiol. 39:23-34.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 23-34
    • Ishikawa, T.1    Yoshimura, K.2    Sakai, K.3    Tamoi, M.4    Takeda, T.5    Shigeoka, S.6
  • 69
    • 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
  • 71
    • 84882302938 scopus 로고    scopus 로고
    • Defining the plant peroxisomal proteome: From Arabidopsis to rice
    • Kaur, N. and Hu, J. (2011) Defining the plant peroxisomal proteome: from Arabidopsis to rice. Front. Plant Sci. 2:103.
    • (2011) Front. Plant Sci. , vol.2 , pp. 103
    • Kaur, N.1    Hu, J.2
  • 72
    • 84888869119 scopus 로고    scopus 로고
    • Peroxisomes and photomorphogenesis
    • Kaur, N., Li, J. and Hu, J. (2013) Peroxisomes and photomorphogenesis. Subcell. Biochem. 69:195-211.
    • (2013) Subcell. Biochem. , vol.69 , pp. 195-211
    • Kaur, N.1    Li, J.2    Hu, J.3
  • 74
    • 0033553562 scopus 로고    scopus 로고
    • Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry
    • Kirkman, H. N., Rolfo, M., Ferraris, A. M. and Gaetani, G. F. (1999) Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry. J. Biol. Chem. 274:13908-13914.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13908-13914
    • Kirkman, H.N.1    Rolfo, M.2    Ferraris, A.M.3    Gaetani, G.F.4
  • 75
    • 84921311178 scopus 로고    scopus 로고
    • Compartment specific changes of the antioxidative status in Arabidopsis thaliana during salt stress
    • Koffler, B. E., Luschin-Ebengreuth, N. and Zechmann, B. (2015) Compartment specific changes of the antioxidative status in Arabidopsis thaliana during salt stress. J. Plant Biol. 58:8-16.
    • (2015) J. Plant Biol. , vol.58 , pp. 8-16
    • Koffler, B.E.1    Luschin-Ebengreuth, N.2    Zechmann, B.3
  • 76
    • 33644839692 scopus 로고    scopus 로고
    • Arabidopsis thaliana subcellular responses to compatible Erysiphe cichoracearum infections
    • Koh, S., André, A., Edwards, H., Ehrhardt, D. and Somerville, S. (2005) Arabidopsis thaliana subcellular responses to compatible Erysiphe cichoracearum infections. Plant J. 44:516-529.
    • (2005) Plant J. , vol.44 , pp. 516-529
    • Koh, S.1    André, A.2    Edwards, H.3    Ehrhardt, D.4    Somerville, S.5
  • 77
    • 26444446941 scopus 로고    scopus 로고
    • Fungal pathogen-induced changes in the antioxidant systems of leaf peroxisomes from infected tomato plants
    • Kużniak, E. and Sklodowska, M. (2005) Fungal pathogen-induced changes in the antioxidant systems of leaf peroxisomes from infected tomato plants. Planta 222:192-200.
    • (2005) Planta , vol.222 , pp. 192-200
    • Kuzniak, E.1    Sklodowska, M.2
  • 79
    • 31044448350 scopus 로고    scopus 로고
    • Peroxisomal monodydroascorbate reductase: Genomic clone characterization and functional analysis under environmental stress conditions
    • Leterrier, M., Corpas, F. J., Barroso, J. B., Sandalio, L. M. and del Río, L. A. (2005) Peroxisomal monodydroascorbate reductase: genomic clone characterization and functional analysis under environmental stress conditions. Plant Physiol. 138:2111-2123.
    • (2005) Plant Physiol. , vol.138 , pp. 2111-2123
    • Leterrier, M.1    Corpas, F.J.2    Barroso, J.B.3    Sandalio, L.M.4    Del Río, L.A.5
  • 80
    • 63149168967 scopus 로고    scopus 로고
    • Peroxisome associated-matrix protein degradation in Arabidopsis
    • Lingard, M., Monroe-Augustus, M. and Bartel, B. (2009) Peroxisome associated-matrix protein degradation in Arabidopsis. Proc. Natl. Acad. Sci. USA 106:4561-4566.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4561-4566
    • Lingard, M.1    Monroe-Augustus, M.2    Bartel, B.3
  • 81
    • 31044444190 scopus 로고    scopus 로고
    • Arabidopsis peroxisomes possess functionally redundant membrane and matrix isoforms of monodehydroascorbate reductase
    • Lisenbee, C. S., Lingard, M. J. and Trelease, R. N. (2005) Arabidopsis peroxisomes possess functionally redundant membrane and matrix isoforms of monodehydroascorbate reductase. Plant J. 43:900-914.
    • (2005) Plant J. , vol.43 , pp. 900-914
    • Lisenbee, C.S.1    Lingard, M.J.2    Trelease, R.N.3
  • 82
    • 0039552192 scopus 로고    scopus 로고
    • Characterization of membrane polypeptides from pea leaf peroxisomes involved in superoxide radical generation
    • López-Huertas, E., Corpas, F. J., Sandalio, L. M. and del Río, L. A. (1999) Characterization of membrane polypeptides from pea leaf peroxisomes involved in superoxide radical generation. Biochem. J. 337:531-536.
    • (1999) Biochem. J. , vol.337 , pp. 531-536
    • López-Huertas, E.1    Corpas, F.J.2    Sandalio, L.M.3    Del Río, L.A.4
  • 84
    • 84928566985 scopus 로고    scopus 로고
    • Characterization of antioxidant enzymes and peroxisomes of olive (Olea europaea L.) fruits
    • López-Huertas, E. and del Río, L. A. (2014) Characterization of antioxidant enzymes and peroxisomes of olive (Olea europaea L.) fruits. J. Plant Physiol. 171:1463-1471.
    • (2014) J. Plant Physiol. , vol.171 , pp. 1463-1471
    • López-Huertas, E.1    Del Río, L.A.2
  • 85
    • 0036010197 scopus 로고    scopus 로고
    • Distribution and characterization of peroxisomes in Arabidopsis by visualization with GFP: Dynamic morphology and actin-dependent movement
    • Mano, S., Nakamori, C., Hayashi, M., Kato, A., Kondo, M. and Nishimura, M. (2002) Distribution and characterization of peroxisomes in Arabidopsis by visualization with GFP: dynamic morphology and actin-dependent movement. Plant Cell Physiol. 43:331-341.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 331-341
    • Mano, S.1    Nakamori, C.2    Hayashi, M.3    Kato, A.4    Kondo, M.5    Nishimura, M.6
  • 86
    • 0346687502 scopus 로고    scopus 로고
    • Peroxisomes from pepper fruits (Capsicum annuum L.): Purification, characterization and antioxidant activity
    • Mateos, R. M., León, A. M., Sandalio, L. M., Gómez, M., del Río, L. A. and Palma, J. M. (2003) Peroxisomes from pepper fruits (Capsicum annuum L.): purification, characterization and antioxidant activity. J. Plant Physiol. 160:1507-1516.
    • (2003) J. Plant Physiol. , vol.160 , pp. 1507-1516
    • Mateos, R.M.1    León, A.M.2    Sandalio, L.M.3    Gómez, M.4    Del Río, L.A.5    Palma, J.M.6
  • 87
    • 0036006052 scopus 로고    scopus 로고
    • Simultaneous visualization of peroxisomes and cytoskeletal elements reveals actin and not microtubule-based peroxisome motility in plants
    • Mathur, J., Mathur, N. and Hulskamp, M. (2002) Simultaneous visualization of peroxisomes and cytoskeletal elements reveals actin and not microtubule-based peroxisome motility in plants. Plant Physiol. 128:1031-1045.
    • (2002) Plant Physiol. , vol.128 , pp. 1031-1045
    • Mathur, J.1    Mathur, N.2    Hulskamp, M.3
  • 89
    • 85028128429 scopus 로고    scopus 로고
    • Role of peroxisomes in the oxidative injury induced by 2, 4-dichlorophenoxyacetic acid in leaves of pea plants
    • McCarthy, I., Gómez, M., del Río, L. A. and Palma, J. M. (2011) Role of peroxisomes in the oxidative injury induced by 2, 4-dichlorophenoxyacetic acid in leaves of pea plants. Biol. Plant. 55:485-492.
    • (2011) Biol. Plant. , vol.55 , pp. 485-492
    • McCarthy, I.1    Gómez, M.2    Del Río, L.A.3    Palma, J.M.4
  • 91
    • 84864630234 scopus 로고    scopus 로고
    • Plant catalases: Peroxisomal redox guardians
    • Mhamdi, A., Noctor, G. and Baker, A. (2012) Plant catalases: peroxisomal redox guardians. Arch. Biochem. Biophys. 525:181-194.
    • (2012) Arch. Biochem. Biophys. , vol.525 , pp. 181-194
    • Mhamdi, A.1    Noctor, G.2    Baker, A.3
  • 93
    • 77949673517 scopus 로고    scopus 로고
    • Salt stress causes peroxisome proliferation, but inducing peroxisome proliferation does not improve NaCl tolerance in Arabidopsis thaliana
    • Mitsuya, S., El Shami, M., Sparkes, I. A., Charlton, W. L., de Marcos, L. C., Johnson, B., et al. (2010) Salt stress causes peroxisome proliferation, but inducing peroxisome proliferation does not improve NaCl tolerance in Arabidopsis thaliana. PLoS One 5:e9408.
    • (2010) PLoS One , vol.5 , pp. e9408
    • Mitsuya, S.1    El Shami, M.2    Sparkes, I.A.3    Charlton, W.L.4    De Marcos, L.C.5    Johnson, B.6
  • 95
    • 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
    • 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.
    • (2004) J. Exp. Bot. , vol.55 , pp. 1105-1113
    • Mittova, V.1    Guy, M.2    Tal, M.3    Volokita, M.4
  • 96
    • 84899869292 scopus 로고    scopus 로고
    • Singlet oxygen signatures are detected independent of light or chloroplasts in response to multiple stresses
    • Mor, A., Koh, E., Weiner, L., Rosenwasser, S., Sibony-Benyamini, H. and Fluhr, R (2014) Singlet oxygen signatures are detected independent of light or chloroplasts in response to multiple stresses. Plant Physiol. 165:249-261.
    • (2014) Plant Physiol. , vol.165 , pp. 249-261
    • Mor, A.1    Koh, E.2    Weiner, L.3    Rosenwasser, S.4    Sibony-Benyamini, H.5    Fluhr, R.6
  • 97
    • 53749088668 scopus 로고    scopus 로고
    • Bridging the gap between plant and mammalian polyamine catabolism: A novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis
    • Moschou, P. N., Sanmartin, M., Andriopoulou, A. H., Rojo, E., Sanchez-Serrano, J. J., Kalliopi, K., et al. (2008) Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis. Plant Physiol. 147:1845-1857.
    • (2008) Plant Physiol. , vol.147 , pp. 1845-1857
    • Moschou, P.N.1    Sanmartin, M.2    Andriopoulou, A.H.3    Rojo, E.4    Sanchez-Serrano, J.J.5    Kalliopi, K.6
  • 98
    • 20444458610 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation induces carbonylation of peroxisomal proteins and loss of enzymatic activities
    • Nguyen, A. T., Donaldson, R. P. (2005) Metal-catalyzed oxidation induces carbonylation of peroxisomal proteins and loss of enzymatic activities. Arch. Biochem. Biophys. 439:25-31.
    • (2005) Arch. Biochem. Biophys. , vol.439 , pp. 25-31
    • Nguyen, A.T.1    Donaldson, R.P.2
  • 99
    • 33745642032 scopus 로고    scopus 로고
    • Expression of a peroxisome proliferator-activated receptor gene (xPPARα) from Xenopus laevis in tobacco (Nicotiana tabacum) plants
    • Nila, A. G., Sandalio, L. M., Lopez, M. G., Gomez, M., del Río, LA. and Gomez-Lim, M. A. (2006) Expression of a peroxisome proliferator-activated receptor gene (xPPARα) from Xenopus laevis in tobacco (Nicotiana tabacum) plants. Planta 224:569-581.
    • (2006) Planta , vol.224 , pp. 569-581
    • Nila, A.G.1    Sandalio, L.M.2    Lopez, M.G.3    Gomez, M.4    Del Río, L.A.5    Gomez-Lim, M.A.6
  • 100
    • 33845285532 scopus 로고    scopus 로고
    • Plant peroxisomes as a source of signalling molecules
    • Nyathi, Y. and Baker, A. (2006) Plant peroxisomes as a source of signalling molecules. Biochim. Biophys. Acta 1763:1478-1495.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1478-1495
    • Nyathi, Y.1    Baker, A.2
  • 101
    • 0029830579 scopus 로고    scopus 로고
    • Intra- and extra-cellular localization of 'cytosolic' CuZn-superoxide dismutase in spinach leaf and hypocotyls
    • Ogawa, K., Kanematsu, S. and Asada, K. (1996) Intra- and extra-cellular localization of 'cytosolic' CuZn-superoxide dismutase in spinach leaf and hypocotyls. Plant Cell Physiol. 37:790-799.
    • (1996) Plant Cell Physiol. , vol.37 , pp. 790-799
    • Ogawa, K.1    Kanematsu, S.2    Asada, K.3
  • 102
    • 84863983857 scopus 로고    scopus 로고
    • Involvement of glutathione peroxidase 1 in growth and peroxisome formation in Saccharomyces cerevisiae in oleic acid medium
    • Ohdate, T. and Inoue, Y. (2012) Involvement of glutathione peroxidase 1 in growth and peroxisome formation in Saccharomyces cerevisiae in oleic acid medium. Biochim. Biophys. Acta 1821:1295-1305.
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 1295-1305
    • Ohdate, T.1    Inoue, Y.2
  • 103
    • 84942165980 scopus 로고    scopus 로고
    • Physical interaction between peroxisomes and chloroplasts elucidated by in situ laser analysis
    • Oikawa, K., Matsunaga, S., Mano, S., Kondo, M., Yamada K., Hayashi, M., et al. (2015) Physical interaction between peroxisomes and chloroplasts elucidated by in situ laser analysis. Nat. Plants 1:15035.
    • (2015) Nat. Plants , vol.1 , pp. 15035
    • Oikawa, K.1    Matsunaga, S.2    Mano, S.3    Kondo, M.4    Yamada, K.5    Hayashi, M.6
  • 104
    • 1042290184 scopus 로고    scopus 로고
    • 2 accumulation in field-grown aspen and birch is linked to foliar ultrastructure and peroxisomal activity
    • 2 accumulation in field-grown aspen and birch is linked to foliar ultrastructure and peroxisomal activity. New Phytol. 161:791-799.
    • (2003) New Phytol. , vol.161 , pp. 791-799
    • Oksanen, E.1    Haikio, E.2    Sober, J.3    Karnosky, D.F.4
  • 105
    • 66149173521 scopus 로고    scopus 로고
    • Proteome of plant peroxisomes: New perspectives on the role of these organelles in cell biology
    • Palma, J. M., Corpas, F. J. and del Río, LA. (2009) Proteome of plant peroxisomes: new perspectives on the role of these organelles in cell biology. Proteomics 9:2301-2312.
    • (2009) Proteomics , vol.9 , pp. 2301-2312
    • Palma, J.M.1    Corpas, F.J.2    Del Río, L.A.3
  • 106
    • 0025801196 scopus 로고
    • Peroxisome proliferation and oxidative stress mediated by activated oxygen species in plant peroxisomes
    • Palma, J. M., Garrido, M., Rodríguez-García, M. I. and del Río, LA. (1991) Peroxisome proliferation and oxidative stress mediated by activated oxygen species in plant peroxisomes. Arch. Biochem. Biophys. 287:68-74
    • (1991) Arch. Biochem. Biophys. , vol.287 , pp. 68-74
    • Palma, J.M.1    Garrido, M.2    Rodríguez-García, M.I.3    Del Río, L.A.4
  • 107
    • 0001018812 scopus 로고
    • Increased levels of peroxisomal active oxygen-related enzymes in copper-tolerant pea plants
    • Palma, J. M., Gomez, M., Yañez, J. and del Río, LA. (1987) Increased levels of peroxisomal active oxygen-related enzymes in copper-tolerant pea plants. Plant Physiol. 85:570-574.
    • (1987) Plant Physiol. , vol.85 , pp. 570-574
    • Palma, J.M.1    Gomez, M.2    Yañez, J.3    Del Río, L.A.4
  • 108
    • 0032458615 scopus 로고    scopus 로고
    • Peroxisomal manganese superoxide dismutase: Purification and properties of the isozyme from pea leaves
    • Palma, J. M., Lopez-Huertas E., Corpas, F. J., Sandalio, L. M., Gomez, M. and del Río, LA. (1998) Peroxisomal manganese superoxide dismutase: purification and properties of the isozyme from pea leaves. Physiol. Plant. 104:720-726.
    • (1998) Physiol. Plant. , vol.104 , pp. 720-726
    • Palma, J.M.1    Lopez-Huertas, E.2    Corpas, F.J.3    Sandalio, L.M.4    Gomez, M.5    Del Río, L.A.6
  • 110
    • 84942241397 scopus 로고    scopus 로고
    • Physiology of pepper fruit and the metabolism of antioxidants: Chloroplasts, mitochondria and peroxisomes
    • Palma, J. M., Sevilla, F., Jiménez, A., del Río, L. A., Corpas, F. J., Álvarez de Morales, P., et al. (2015) Physiology of pepper fruit and the metabolism of antioxidants: chloroplasts, mitochondria and peroxisomes. Ann. Bot. 116:627-636.
    • (2015) Ann. Bot. , vol.116 , pp. 627-636
    • Palma, J.M.1    Sevilla, F.2    Jiménez, A.3    Del Río, L.A.4    Corpas, F.J.5    Álvarez De Morales, P.6
  • 111
    • 73349108064 scopus 로고    scopus 로고
    • Peroxisomal localization of Mn-SOD enzyme in Saccharomyces cerevisiae yeasts: In silico analysis
    • Petrova, V., Uzunov, Z. and Kujumdzieva, A. (2009) Peroxisomal localization of Mn-SOD enzyme in Saccharomyces cerevisiae yeasts: in silico analysis. Biotechnol. Biotechnol. Equip. 23:1531-1536.
    • (2009) Biotechnol. Biotechnol. Equip. , vol.23 , pp. 1531-1536
    • Petrova, V.1    Uzunov, Z.2    Kujumdzieva, A.3
  • 112
  • 113
    • 84888871901 scopus 로고    scopus 로고
    • Proteome analysis of peroxisomes from etiolated Arabidopsis seedlings identifies a peroxisomal protease involved in β-oxidation and development
    • Quan, S., Yang, P., Cassin-Ross, G., Kaur, N., Switzenberg, R., Aung, K., et al. (2013) Proteome analysis of peroxisomes from etiolated Arabidopsis seedlings identifies a peroxisomal protease involved in β-oxidation and development. Plant Physiol. 163:1518-1538.
    • (2013) Plant Physiol. , vol.163 , pp. 1518-1538
    • Quan, S.1    Yang, P.2    Cassin-Ross, G.3    Kaur, N.4    Switzenberg, R.5    Aung, K.6
  • 114
    • 0020002341 scopus 로고
    • Hepatic and renal effects of peroxisome proliferators: Biological implications
    • Reddy, J. K., Warren, J. R., Reddy, M. K. and Lalwani, N. D. (1982) Hepatic and renal effects of peroxisome proliferators: biological implications. Ann. NY Acad. Sci. 386:81-110.
    • (1982) Ann. NY Acad. Sci. , vol.386 , pp. 81-110
    • Reddy, J.K.1    Warren, J.R.2    Reddy, M.K.3    Lalwani, N.D.4
  • 115
    • 79955030496 scopus 로고    scopus 로고
    • Toward a definition of the complete proteome of plant peroxisomes: Where experimental proteomics must be complemented by bioinformatics
    • Reumann, S. (2011) Toward a definition of the complete proteome of plant peroxisomes: where experimental proteomics must be complemented by bioinformatics. Proteomics 11:1764-1779.
    • (2011) Proteomics , vol.11 , pp. 1764-1779
    • Reumann, S.1
  • 116
    • 37249016441 scopus 로고    scopus 로고
    • Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting peptides, metabolic pathways and defense mechanisms
    • Reumann, S., Babujee, L., Ma, C., Wienkoop, S., Siemsen, T., Antonicelli, G. E., et al. (2007) Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting peptides, metabolic pathways and defense mechanisms. Plant Cell 19:3170-3193.
    • (2007) Plant Cell , vol.19 , pp. 3170-3193
    • Reumann, S.1    Babujee, L.2    Ma, C.3    Wienkoop, S.4    Siemsen, T.5    Antonicelli, G.E.6
  • 117
    • 66149148256 scopus 로고    scopus 로고
    • In-depth proteome analysis of Arabidopsis leaf peroxisomes combined with in vivo subcellular targeting verification indicates novel metabolic and regulatory functions of peroxisomes
    • Reumann, S., Quan, S., Aung, K., Yang, P., Manandhar-Shrestha, K., Holbrook D., et al. (2009) In-depth proteome analysis of Arabidopsis leaf peroxisomes combined with in vivo subcellular targeting verification indicates novel metabolic and regulatory functions of peroxisomes. Plant Physiol. 150:125-143.
    • (2009) Plant Physiol. , vol.150 , pp. 125-143
    • Reumann, S.1    Quan, S.2    Aung, K.3    Yang, P.4    Manandhar-Shrestha, K.5    Holbrook, D.6
  • 118
    • 84907398766 scopus 로고    scopus 로고
    • 2, 4-Dichlorophenoxyacetic acid promotes S-nitrosylation and oxidation of actin affecting cytoskeleton and peroxisomal dynamics
    • Rodríguez-Serrano, M., Pazmiño, D. M., Sparkes, I., Rochetti, A., Hawes, C., Romero-Puertas, M. C., et al. (2014) 2, 4-Dichlorophenoxyacetic acid promotes S-nitrosylation and oxidation of actin affecting cytoskeleton and peroxisomal dynamics. J. Exp. Bot. 65:4783-4793.
    • (2014) J. Exp. Bot. , vol.65 , pp. 4783-4793
    • Rodríguez-Serrano, M.1    Pazmiño, D.M.2    Sparkes, I.3    Rochetti, A.4    Hawes, C.5    Romero-Puertas, M.C.6
  • 119
    • 34548457672 scopus 로고    scopus 로고
    • Peroxisomal membrane manganese superoxide dismutase: Characterization of the isozyme from watermelon (Citrullus lanatus Schrad.) cotyledons
    • Rodríguez-Serrano, M., Romero-Puertas, M. C., Pastori, G. M., Corpas, F. J., Sandalio, L. M., del Río, L. A., et al. (2007) Peroxisomal membrane manganese superoxide dismutase: characterization of the isozyme from watermelon (Citrullus lanatus Schrad.) cotyledons. J. Exp. Bot. 58:2417-2427.
    • (2007) J. Exp. Bot. , vol.58 , pp. 2417-2427
    • Rodríguez-Serrano, M.1    Romero-Puertas, M.C.2    Pastori, G.M.3    Corpas, F.J.4    Sandalio, L.M.5    Del Río, L.A.6
  • 121
    • 84863230574 scopus 로고    scopus 로고
    • Glycolate oxidase modulates reactive oxygen species-mediated signal transduction during nonhost resistance in Nicotiana benthamiana and Arabidopsis
    • Rojas, C. M., Senthil-Kumar, M., Wang, K., Ryu C. M., Kaundal, A. and Mysore, K. (2012) Glycolate oxidase modulates reactive oxygen species-mediated signal transduction during nonhost resistance in Nicotiana benthamiana and Arabidopsis. Plant Cell 24:336-352.
    • (2012) Plant Cell , vol.24 , pp. 336-352
    • Rojas, C.M.1    Senthil-Kumar, M.2    Wang, K.3    Ryu, C.M.4    Kaundal, A.5    Mysore, K.6
  • 122
    • 4544233001 scopus 로고    scopus 로고
    • Reactive oxygen species-mediated enzymatic systems involved in the oxidative action of 2, 4-dichlorophenoxyacetic acid
    • Romero-Puertas, M. C., McCarthy, I., Gómez, M., Sandalio, L. M., Corpas, F. J., del Río, L. A., et al. (2004b) Reactive oxygen species-mediated enzymatic systems involved in the oxidative action of 2, 4-dichlorophenoxyacetic acid. Plant Cell Environ. 27:1135-1148.
    • (2004) Plant Cell Environ. , vol.27 , pp. 1135-1148
    • Romero-Puertas, M.C.1    McCarthy, I.2    Gómez, M.3    Sandalio, L.M.4    Corpas, F.J.5    Del Río, L.A.6
  • 123
  • 129
    • 84940676027 scopus 로고    scopus 로고
    • Reactive oxygen and reactive nitrogen signaling networks in plants
    • Sandalio, LM. and Foyer, C. H. (eds.) (2015) Reactive oxygen and reactive nitrogen signaling networks in plants. J. Exp. Bot. 66:2827-3000.
    • (2015) J. Exp. Bot. , vol.66 , pp. 2827-3000
    • Sandalio, L.M.1    Foyer, C.H.2
  • 130
    • 0003047177 scopus 로고
    • Localization of manganese superoxide dismutase in peroxisomes isolated from Pisum sativum L
    • Sandalio, L. M., Palma, J. M. and del Río, LA. (1987) Localization of manganese superoxide dismutase in peroxisomes isolated from Pisum sativum L. Plant Sci. 51:1-8.
    • (1987) Plant Sci. , vol.51 , pp. 1-8
    • Sandalio, L.M.1    Palma, J.M.2    Del Río, L.A.3
  • 133
    • 84938913588 scopus 로고    scopus 로고
    • Peroxisomes sense and respond to environmental cues by regulating ROS and RNS signaling networks
    • Sandalio LM. and Romero-Puertas, M. C. (2015) Peroxisomes sense and respond to environmental cues by regulating ROS and RNS signaling networks. Ann. Bot. 116:475-485.
    • (2015) Ann. Bot. , vol.116 , pp. 475-485
    • Sandalio, L.M.1    Romero-Puertas, M.C.2
  • 134
    • 0002316172 scopus 로고
    • Products of biological nitrogen fixation in higher plants: Synthesis, transport, and metabolism
    • Schubert, K. R. (1986) Products of biological nitrogen fixation in higher plants: synthesis, transport, and metabolism. Annu. Rev. Plant Physiol. 37:539-574.
    • (1986) Annu. Rev. Plant Physiol. , vol.37 , pp. 539-574
    • Schubert, K.R.1
  • 135
    • 0000276965 scopus 로고
    • Characterization of a manganese superoxide dismutase from the higher plant Pisum sativum L
    • Sevilla, F., Lopez-Gorge, J. and del Río, LA. (1982) Characterization of a manganese superoxide dismutase from the higher plant Pisum sativum L. Plant Physiol. 70:1321-1326.
    • (1982) Plant Physiol. , vol.70 , pp. 1321-1326
    • Sevilla, F.1    Lopez-Gorge, J.2    Del Río, L.A.3
  • 136
    • 84905797315 scopus 로고    scopus 로고
    • Role of plant peroxisomes in protection against herbivores
    • Shabab, M. (2013) Role of plant peroxisomes in protection against herbivores. Subcell. Biochem. 69:315-328.
    • (2013) Subcell. Biochem. , vol.69 , pp. 315-328
    • Shabab, M.1
  • 137
    • 84903818940 scopus 로고    scopus 로고
    • Ectopic over-expression of peroxisomal ascorbate peroxidase (SbpAPX) gene confers salt stress tolerance in transgenic peanut (Arachis hypogaea)
    • Singh, N., Mishra, A. and Jha, B. (2014) Ectopic over-expression of peroxisomal ascorbate peroxidase (SbpAPX) gene confers salt stress tolerance in transgenic peanut (Arachis hypogaea). Gene 547:119-125.
    • (2014) Gene , vol.547 , pp. 119-125
    • Singh, N.1    Mishra, A.2    Jha, B.3
  • 139
    • 79751472085 scopus 로고    scopus 로고
    • Peroxisome metabolism and cellular aging
    • Titorenko, V. I. and Terlecky, S. R. (2011) Peroxisome metabolism and cellular aging. Traffic 12:252-259.
    • (2011) Traffic , vol.12 , pp. 252-259
    • Titorenko, V.I.1    Terlecky, S.R.2
  • 141
    • 63649146772 scopus 로고    scopus 로고
    • Singlet oxygen in plants: Production, detoxification and signaling
    • Triantaphylides, C. and Havaux, M. (2009) Singlet oxygen in plants: production, detoxification and signaling. Trends Plant Sci. 14:219-228.
    • (2009) Trends Plant Sci. , vol.14 , pp. 219-228
    • Triantaphylides, C.1    Havaux, M.2
  • 142
    • 33744960001 scopus 로고    scopus 로고
    • The dehydrogenase-mediated recycling of NADPH is a key antioxidant system against salt-induced oxidative stress in olive plants
    • Valderrama, R., Corpas, F. J., Carreras, A., Gomez-Rodríguez, M. V., Chaki, M., Pedrajas, J. R., et al. (2006) The dehydrogenase-mediated recycling of NADPH is a key antioxidant system against salt-induced oxidative stress in olive plants. Plant Cell Environ. 29:1449-1459.
    • (2006) Plant Cell Environ. , vol.29 , pp. 1449-1459
    • Valderrama, R.1    Corpas, F.J.2    Carreras, A.3    Gomez-Rodríguez, M.V.4    Chaki, M.5    Pedrajas, J.R.6
  • 144
    • 77949774450 scopus 로고    scopus 로고
    • Subcellular and tissue localization of NAD kinases from Arabidopsis: Compartmentalization of de novo NADP biosynthesis
    • Waller, J. C., Dhanoa, P. K., Schumann, U., Mullen, RT. and Snedden, W. A. (2010) Subcellular and tissue localization of NAD kinases from Arabidopsis: compartmentalization of de novo NADP biosynthesis. Planta 231:305-317.
    • (2010) Planta , vol.231 , pp. 305-317
    • Waller, J.C.1    Dhanoa, P.K.2    Schumann, U.3    Mullen, R.T.4    Snedden, W.A.5
  • 145
    • 84920274916 scopus 로고    scopus 로고
    • Redox regulated peroxisome homeostasis
    • Wang, X., Li, S., Liu, Y. and Ma, C. (2015) Redox regulated peroxisome homeostasis. Redox Biol. 4:104-108.
    • (2015) Redox Biol. , vol.4 , pp. 104-108
    • Wang, X.1    Li, S.2    Liu, Y.3    Ma, C.4
  • 146
    • 84864035138 scopus 로고    scopus 로고
    • Metabolic functions and biogenesis of peroxisomes in health and disease
    • Waterham, H. R. and Wanders, R. J. A. (2012) Metabolic functions and biogenesis of peroxisomes in health and disease. Biochim. Biophys. Acta 1822:1325-1508.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1325-1508
    • Waterham, H.R.1    Wanders, R.J.A.2
  • 147
    • 84860495899 scopus 로고    scopus 로고
    • Synthesis and signalling by small, redox active molecules in the plant immune response
    • Yun, B. W., Spoel, S. H. and Loake, G. J. (2012) Synthesis and signalling by small, redox active molecules in the plant immune response. Biochim. Biophys. Acta 1820:770-776.
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 770-776
    • Yun, B.W.1    Spoel, S.H.2    Loake, G.J.3
  • 148
    • 55249112721 scopus 로고    scopus 로고
    • Subcellular immunocytochemical analysis detects the highest concentrations of glutathione in mitochondria and not in plastids
    • Zechmann, B., Mauch, F., Sticher, L and Muller, M. (2008) Subcellular immunocytochemical analysis detects the highest concentrations of glutathione in mitochondria and not in plastids. J. Exp. Bot. 59:4017-4027.
    • (2008) J. Exp. Bot. , vol.59 , pp. 4017-4027
    • Zechmann, B.1    Mauch, F.2    Sticher, L.3    Muller, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.