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Volumn 222, Issue 1, 2005, Pages 192-200

Fungal pathogen-induced changes in the antioxidant systems of leaf peroxisomes from infected tomato plants

Author keywords

Antioxidant defence; Ascorbate glutathione cycle; Botrytis; Lycopersicon; Peroxisomes

Indexed keywords

CELL CULTURE; DETOXIFICATION; ENZYME KINETICS; FUNGI; PLANTS (BOTANY); REDOX REACTIONS;

EID: 26444446941     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00425-005-1514-8     Document Type: Article
Times cited : (150)

References (63)
  • 1
    • 0030900075 scopus 로고    scopus 로고
    • Correlation between changes in cell ascorbate and growth of Lupinus albus seedlings
    • Arrigoni O, Calabrese G, De Gara L, Bitonti MB, Liso R (1997) Correlation between changes in cell ascorbate and growth of Lupinus albus seedlings. J Plant Physiol 150:302-308
    • (1997) J Plant Physiol , vol.150 , pp. 302-308
    • Arrigoni, O.1    Calabrese, G.2    De Gara, L.3    Bitonti, M.B.4    Liso, R.5
  • 3
    • 0005575145 scopus 로고
    • Glutathione reductase
    • Grune, Stratton (eds) New York
    • Beutler E (1975) Glutathione reductase. In: Grune, Stratton (eds) Red cells metabolism, 2nd edn. New York, pp 69-70
    • (1975) Red Cells Metabolism, 2nd Edn. , pp. 69-70
    • Beutler, E.1
  • 4
    • 15944414952 scopus 로고
    • The activities of the photosynthetic carbon cycle enzymes of greening bean leaves
    • Bradbeer JW (1969) The activities of the photosynthetic carbon cycle enzymes of greening bean leaves. New Phytol 68:233-245
    • (1969) New Phytol , vol.68 , pp. 233-245
    • Bradbeer, J.W.1
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0017066115 scopus 로고
    • Enzymatic assay for glutathione
    • Brehe JE, Burch HB (1976) Enzymatic assay for glutathione. Anal Biochem 74:315-319
    • (1976) Anal Biochem , vol.74 , pp. 315-319
    • Brehe, J.E.1    Burch, H.B.2
  • 7
    • 0000285024 scopus 로고
    • Separation of mitochondria from microbodies of Pisum sativum L cv Alaska cotyledons
    • Burgess N, Beakes GW, Thomas DR (1985) Separation of mitochondria from microbodies of Pisum sativum L cv Alaska cotyledons. Planta 166:151-155
    • (1985) Planta , vol.166 , pp. 151-155
    • Burgess, N.1    Beakes, G.W.2    Thomas, D.R.3
  • 9
    • 0032871989 scopus 로고    scopus 로고
    • A gene encoding glutathione peroxidase homologues in Hordeum vulgare (barley)
    • Churin Y, Schilling S, Börner T (1999) A gene encoding glutathione peroxidase homologues in Hordeum vulgare (barley). FEBS Lett 459: 33-38
    • (1999) FEBS Lett , vol.459 , pp. 33-38
    • Churin, Y.1    Schilling, S.2    Börner, T.3
  • 11
    • 0343321564 scopus 로고    scopus 로고
    • L-ascorbic acid metabolism in the ascorbate-deficient Arabidopsis mutant vtc1
    • Conklin PL, Pallanca JE, Last Rl, Smirnoff N (1997) L-ascorbic acid metabolism in the ascorbate-deficient Arabidopsis mutant vtc1. Plant Physiol 115:1277-1285
    • (1997) Plant Physiol , vol.115 , pp. 1277-1285
    • Conklin, P.L.1    Pallanca, J.E.2    Last, Rl.3    Smirnoff, N.4
  • 12
    • 0029119130 scopus 로고
    • Two inducers of plant defense responses, 2,6-dichloroisonicotinic acid and salicylic acid, inhibit catalase activity in tobacco
    • USA
    • Conrath U, Chen Z, Ricigliano JR, Klessig DF (1995) Two inducers of plant defense responses, 2,6-dichloroisonicotinic acid and salicylic acid, inhibit catalase activity in tobacco. Proc Natl Acad Sci USA 92:7143-7147
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 7143-7147
    • Conrath, U.1    Chen, Z.2    Ricigliano, J.R.3    Klessig, D.F.4
  • 13
    • 0031896836 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase is a constituent enzyme of the matrix of peroxisomes in the cotyledons of oilseed plants
    • DOI 10.1046/j.1469-8137.1998.00899x
    • Corpas FJ, Sandalio LM, del Río LA, Trelease RN (1998) Copper-zinc superoxide dismutase is a constituent enzyme of the matrix of peroxisomes in the cotyledons of oilseed plants. New Phytol 138:307-314. DOI 10.1046/j.1469-8137.1998.00899x
    • (1998) New Phytol , vol.138 , pp. 307-314
    • Corpas, F.J.1    Sandalio, L.M.2    Del Río, L.A.3    Trelease, R.N.4
  • 14
    • 0035212728 scopus 로고    scopus 로고
    • Peroxisomes as a source of reactive oxygen species and nitric oxide signal molecules in plant cells
    • Corpas FJ, Barroso JB, del Río LA (2001) Peroxisomes as a source of reactive oxygen species and nitric oxide signal molecules in plant cells. 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
  • 18
    • 77956983868 scopus 로고
    • Leaf senescence: Correlated with increased levels of membrane permeability and lipid peroxidation, and decreased levels of superoxide dismutase and catalase
    • Dhindsa RS, Plumb-Dhindsa P, Thorpe TA (1981) Leaf senescence: correlated with increased levels of membrane permeability and lipid peroxidation, and decreased levels of superoxide dismutase and catalase. J Exp Bot 32:91-101
    • (1981) J Exp Bot , vol.32 , pp. 91-101
    • Dhindsa, R.S.1    Plumb-Dhindsa, P.2    Thorpe, T.A.3
  • 19
    • 0032874587 scopus 로고    scopus 로고
    • Proteolytic cleavage of plant proteins by peroxisomal endoproteases from senescent pea leaves
    • DOI 10.007/s004250050637
    • Distefano S, Palma JS, McCarthy I, del Río LA (1999) Proteolytic cleavage of plant proteins by peroxisomal endoproteases from senescent pea leaves. Planta 209:308-313. DOI 10.007/s004250050637
    • (1999) Planta , vol.209 , pp. 308-313
    • Distefano, S.1    Palma, J.S.2    McCarthy, I.3    Del Río, L.A.4
  • 22
    • 0242309094 scopus 로고    scopus 로고
    • Redox sensing and signalling associated with reactive oxygen in chloroplasts, peroxisomes and mitochondria
    • DOI 10.1034/j.1399-3054.2003.00223.x
    • Foyer CH, Noctor G (2003) Redox sensing and signalling associated with reactive oxygen in chloroplasts, peroxisomes and mitochondria. Physiol Plant 119:355-364. DOI 10.1034/j.1399-3054.2003.00223.x
    • (2003) Physiol Plant , vol.119 , pp. 355-364
    • Foyer, C.H.1    Noctor, G.2
  • 23
    • 0033826053 scopus 로고    scopus 로고
    • Role of reactive oxygen intermediates and cognate redox signaling in disease resistance
    • Grant JJ, Loake GJ (2000) Role of reactive oxygen intermediates and cognate redox signaling in disease resistance. Plant Physiol 124:21-29
    • (2000) Plant Physiol , vol.124 , pp. 21-29
    • Grant, J.J.1    Loake, G.J.2
  • 24
    • 0017819382 scopus 로고
    • A simple spectrophotometric assay for fumarate hydratase in crude tissue extracts
    • Hatch MD (1978) A simple spectrophotometric assay for fumarate hydratase in crude tissue extracts. Anal Biochem 85:271-275
    • (1978) Anal Biochem , vol.85 , pp. 271-275
    • Hatch, M.D.1
  • 25
    • 0345393852 scopus 로고    scopus 로고
    • Entering a new era of research on plant peroxisomes
    • DOI 10.1016/j.pbi.2003.09.012
    • Hayashi M, Nishimura M (2003) Entering a new era of research on plant peroxisomes. Curr Opin Plant Biol 6:577-582. DOI 10.1016/j.pbi.2003.09.012
    • (2003) Curr Opin Plant Biol , vol.6 , pp. 577-582
    • Hayashi, M.1    Nishimura, M.2
  • 26
    • 0034022040 scopus 로고    scopus 로고
    • The effects of ethylene, depressed oxygen, and elevated carbon dioxide on antioxidant profiles of senescing spinach leaves
    • Hodges MD, Forney CF (2000) The effects of ethylene, depressed oxygen, and elevated carbon dioxide on antioxidant profiles of senescing spinach leaves. J Exp Bot 51:645-655
    • (2000) J Exp Bot , vol.51 , pp. 645-655
    • Hodges, M.D.1    Forney, C.F.2
  • 27
    • 0015693372 scopus 로고
    • Glutathione peroxidase in human red cells in health and disease
    • Hopkins J, Tudhope GR (1973) Glutathione peroxidase in human red cells in health and disease. Br J Haematol 25:563-575
    • (1973) Br J Haematol , vol.25 , pp. 563-575
    • Hopkins, J.1    Tudhope, G.R.2
  • 28
    • 0002458223 scopus 로고
    • Purification of dehydroascorbate reductase from spinach and its characterization as a thiol enzyme
    • Hossain MA, Asada K (1984) Purification of dehydroascorbate reductase from spinach and its characterization as a thiol enzyme. Plant Cell Physiol 25:85-92
    • (1984) Plant Cell Physiol , vol.25 , pp. 85-92
    • Hossain, M.A.1    Asada, K.2
  • 29
    • 0037077408 scopus 로고    scopus 로고
    • The role of peroxisomes in the integration of metabolism and evolutionary diversity of photosynthetic organisms
    • Igamberdiev AU, Lea PJ (2002) The role of peroxisomes in the integration of metabolism and evolutionary diversity of photosynthetic organisms. Phytochemistry 60:651-674
    • (2002) Phytochemistry , vol.60 , pp. 651-674
    • Igamberdiev, A.U.1    Lea, P.J.2
  • 30
    • 0040557481 scopus 로고    scopus 로고
    • Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves
    • Jiménez A, Hernández JA, del Río, 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    Río, D.3    Sevilla, F.4
  • 31
    • 0034537491 scopus 로고    scopus 로고
    • Overexpression of Mn-superoxide dismutase in maize leaves leads to increased monodehydroascorbate reductase, dehydroascorbate reductase and glutathione reductase activities
    • Kingston-Smith AH, Foyer CH (2000) Overexpression of Mn-superoxide dismutase in maize leaves leads to increased monodehydroascorbate reductase, dehydroascorbate reductase and glutathione reductase activities. J Exp Bot 51:1867-1877
    • (2000) J Exp Bot , vol.51 , pp. 1867-1877
    • Kingston-Smith, A.H.1    Foyer, C.H.2
  • 32
    • 0030478735 scopus 로고    scopus 로고
    • Alterations in the antioxidative system of suspension-cultured soybean cells (Glycine max) induced by oxidative stress
    • Knörzer OC, Durner J, Böger P (1996) Alterations in the antioxidative system of suspension-cultured soybean cells (Glycine max) induced by oxidative stress. Physiol Plant 97:388-396
    • (1996) Physiol Plant , vol.97 , pp. 388-396
    • Knörzer, O.C.1    Durner, J.2    Böger, P.3
  • 33
    • 0344563460 scopus 로고    scopus 로고
    • The effect of Botrytis cinerea infection on ascorbate-glutathione cycle in tomato leaves
    • Kuźniak E, Skłodowska M (1999) The effect of Botrytis cinerea infection on ascorbate-glutathione cycle in tomato leaves. Plant Sci 148:69-76
    • (1999) Plant Sci , vol.148 , pp. 69-76
    • Kuźniak, E.1    Skłodowska, M.2
  • 34
    • 0035084679 scopus 로고    scopus 로고
    • Ascorbate, glutathione and related enzymes in chloroplasts of tomato leaves infected by Botrytis cinerea
    • Kuźniak E, Skłodowska M (2001) Ascorbate, glutathione and related enzymes in chloroplasts of tomato leaves infected by Botrytis cinerea. Plant Sci 160:723-731
    • (2001) Plant Sci , vol.160 , pp. 723-731
    • Kuźniak, E.1    Skłodowska, M.2
  • 35
    • 1542649629 scopus 로고    scopus 로고
    • The effect of Botrytis cinerea infection on the antioxidant profile of mitochondria from tomato leaves
    • DOI 10.1093/jxb/erh076
    • Kuźniak E, Skłodowska M (2004) The effect of Botrytis cinerea infection on the antioxidant profile of mitochondria from tomato leaves. J Exp Bot 397:605-612. DOI 10.1093/jxb/erh076
    • (2004) J Exp Bot , vol.397 , pp. 605-612
    • Kuźniak, E.1    Skłodowska, M.2
  • 36
    • 0037832556 scopus 로고    scopus 로고
    • Peroxisomal ascorbate peroxidase resides within a subdomain of rough endoplasmic reticulum in wild-type Arabidopsis cells
    • DOI 10.1104/pp. 103.019976
    • Lisenbee CS, Heinze M, Trelease RN (2003) Peroxisomal ascorbate peroxidase resides within a subdomain of rough endoplasmic reticulum in wild-type Arabidopsis cells. Plant Physiol 132:870-882. DOI 10.1104/pp. 103.019976
    • (2003) Plant Physiol , vol.132 , pp. 870-882
    • Lisenbee, C.S.1    Heinze, M.2    Trelease, R.N.3
  • 38
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymatic function for erythrocuprein (hemocuprein)
    • McCord J, Fridovich I (1969) Superoxide dismutase. An enzymatic function for erythrocuprein (hemocuprein). J Biol Chem 244:6049-6055
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.1    Fridovich, I.2
  • 39
    • 0018409235 scopus 로고
    • A simplified assay method of superoxide dismutase activity for clinical use
    • Minami M, Yoshikawa H (1979) A simplified assay method of superoxide dismutase activity for clinical use. Clin Chim Acta 92:337-342
    • (1979) Clin Chim Acta , vol.92 , pp. 337-342
    • Minami, M.1    Yoshikawa, H.2
  • 40
    • 0033823856 scopus 로고    scopus 로고
    • Activities of SOD and the ascorbate-glutathione cycle enzymes in sub-cellular compartments in leaves and roots of the cultivated tomato and its wild salt-tolerant relative Lycopersicon pennellii
    • DOI 10.1034/j.1399-3054.2000.110106.x
    • Mittova V, Volokita M, Guy M, Tal M (2000) Activities of SOD and the ascorbate-glutathione cycle enzymes in sub-cellular compartments in leaves and roots of the cultivated tomato and its wild salt-tolerant relative Lycopersicon pennellii. Physiol Plant 110:42-51. DOI 10.1034/j.1399-3054.2000.110106.x
    • (2000) Physiol Plant , vol.110 , pp. 42-51
    • Mittova, V.1    Volokita, M.2    Guy, M.3    Tal, M.4
  • 41
    • 0034089277 scopus 로고    scopus 로고
    • Evaluation of defence system in chloroplasts to photooxidative stress caused by paraquat using transgenic tobacco plants expressing catalase from Escherichia coli
    • Miyagawa Y, Tamoi M, Shigeoka S (2000) Evaluation of defence system in chloroplasts to photooxidative stress caused by paraquat using transgenic tobacco plants expressing catalase from Escherichia coli. Plant Cell Physiol 41:311-320
    • (2000) Plant Cell Physiol , vol.41 , pp. 311-320
    • Miyagawa, Y.1    Tamoi, M.2    Shigeoka, S.3
  • 42
    • 0032904974 scopus 로고    scopus 로고
    • Induction of rice cytosolic ascorbate peroxidase mRNA by oxidative stress; the involvement of hydrogen peroxide in oxidative stress signaling
    • Morita S, Kaminaka H, Masumura T, Tanaka K (1999) Induction of rice cytosolic ascorbate peroxidase mRNA by oxidative stress; the involvement of hydrogen peroxide in oxidative stress signaling. Plant Cell Physiol 40:417-422
    • (1999) Plant Cell Physiol , vol.40 , pp. 417-422
    • Morita, S.1    Kaminaka, H.2    Masumura, T.3    Tanaka, K.4
  • 43
    • 0030292246 scopus 로고    scopus 로고
    • Biogenesis and membrane properties of peroxisomes: Does the boundary membrane serve and protect?
    • Mullen RT, Trelease RN (1996) Biogenesis and membrane properties of peroxisomes: does the boundary membrane serve and protect? Trends Plant Sci 1:389-394
    • (1996) Trends Plant Sci , vol.1 , pp. 389-394
    • Mullen, R.T.1    Trelease, R.N.2
  • 44
    • 0010282460 scopus 로고
    • Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts
    • Nakano Y, Asada K (1981) Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts. Plant Cell Physiol 22:867-880
    • (1981) Plant Cell Physiol , vol.22 , pp. 867-880
    • Nakano, Y.1    Asada, K.2
  • 45
    • 0036001076 scopus 로고    scopus 로고
    • Hydrogen peroxide and nitric oxide as signalling moleculaes in plants
    • Neill SJ, Desikan R, Clarke A, Hurst RD, Hancock JT (2002) Hydrogen peroxide and nitric oxide as signalling moleculaes in plants. J Exp Bot 53:1237-1247
    • (2002) J Exp Bot , vol.53 , pp. 1237-1247
    • Neill, S.J.1    Desikan, R.2    Clarke, A.3    Hurst, R.D.4    Hancock, J.T.5
  • 46
    • 0029294117 scopus 로고
    • Characterization of a pathogen-induced potato catalase and its systemic expression upon nematode and bacterial infection
    • Niebel A, Heungens K, Barthels N, Inzée D, Van Montagu M, Gheysen G (1995) Characterization of a pathogen-induced potato catalase and its systemic expression upon nematode and bacterial infection. Mol Plant Microbe Interact 8:371-378
    • (1995) Mol Plant Microbe Interact , vol.8 , pp. 371-378
    • Niebel, A.1    Heungens, K.2    Barthels, N.3    Inzée, D.4    Van Montagu, M.5    Gheysen, G.6
  • 47
    • 1042290184 scopus 로고    scopus 로고
    • 2 accumulation in field-grown aspen and birch is linked to foliar ultrastructure and peroxisomal activity
    • DOI 10.1111/j.1469-8137.2003.00981.x
    • 2 accumulation in field-grown aspen and birch is linked to foliar ultrastructure and peroxisomal activity. New Phytol 161:791-799. DOI 10.1111/j.1469-8137.2003.00981.x
    • (2003) New Phytol , vol.161 , pp. 791-799
    • Oksanen, E.1    Häikkiö, E.2    Sober, J.3    Karnosky, D.F.4
  • 48
    • 0032458615 scopus 로고    scopus 로고
    • Peroxisomal manganese superoxide dismutase: Purification and properties of the isozyme from pea leaves
    • DOI 10.1034/j.1399-3054.1998.1040429.x
    • Palma JM, López-Huertas E, Corpas FJ, Sandalio LM, Gómez M, del Río LA (1998) Peroxisomal manganese superoxide dismutase: purification and properties of the isozyme from pea leaves. Physiol Plant 104:720-726. DOI 10.1034/j.1399-3054.1998.1040429.x
    • (1998) Physiol Plant , vol.104 , pp. 720-726
    • Palma, J.M.1    López-Huertas, E.2    Corpas, F.J.3    Sandalio, L.M.4    Gómez, M.5    Del Río, L.A.6
  • 50
    • 0030901644 scopus 로고    scopus 로고
    • Natural senescence of pea leaves: An activated oxygen-mediated function for peroxisomes
    • Pastori GM, del Río LA (1997) Natural senescence of pea leaves: an activated oxygen-mediated function for peroxisomes. Plant Physiol 113:411-418
    • (1997) Plant Physiol , vol.113 , pp. 411-418
    • Pastori, G.M.1    Del Río, L.A.2
  • 51
    • 0038625957 scopus 로고    scopus 로고
    • 2 generation and metabolism in leaf apoplastic fraction of tomato leaves infected with Botrytis cinerea
    • 2 generation and metabolism in leaf apoplastic fraction of tomato leaves infected with Botrytis cinerea. J Phytopathol 151:153-161
    • (2003) J Phytopathol , vol.151 , pp. 153-161
    • Patykowski, J.1    Urbanek, H.2
  • 52
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: Verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • Porra JR, Thompson WA, Kiedermann PE (1989) Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochim Biophys Acta 975:384-394
    • (1989) Biochim Biophys Acta , vol.975 , pp. 384-394
    • Porra, J.R.1    Thompson, W.A.2    Kiedermann, P.E.3
  • 53
    • 0033832732 scopus 로고    scopus 로고
    • The structural properties of plant peroxisomes and their metabolic significance
    • Reumann S (2000) The structural properties of plant peroxisomes and their metabolic significance. Biol Chem 381:639-648
    • (2000) Biol Chem , vol.381 , pp. 639-648
    • Reumann, S.1
  • 55
    • 0003047177 scopus 로고
    • Localization of manganese superoxide dismutase in peroxisomes isolated from Pisum sativum L.
    • Sandalio LM, Palma JM, del Rio 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 Rio, L.A.3
  • 56
    • 0031001627 scopus 로고    scopus 로고
    • Immunocytochemical localization of copper, zinc superoxide dismutase in peroxisomes from watermelon (Citrullus vulgaris Schrad)
    • Sandalio LM, López-Huertas E, Bueno P, del Río LA (1997) Immunocytochemical localization of copper, zinc superoxide dismutase in peroxisomes from watermelon (Citrullus vulgaris Schrad). Free Rad Res 26:187-194
    • (1997) Free Rad Res , vol.26 , pp. 187-194
    • Sandalio, L.M.1    López-Huertas, E.2    Bueno, P.3    Del Río, L.A.4
  • 57
    • 0342656161 scopus 로고    scopus 로고
    • Photoinactivation and protection of glycolate oxidase in vitro and in leaves
    • Schäfer L, Feierabend J (2000) Photoinactivation and protection of glycolate oxidase in vitro and in leaves. Z Naturforsch 55c:361-372
    • (2000) Z Naturforsch , vol.55 C , pp. 361-372
    • Schäfer, L.1    Feierabend, J.2
  • 58
    • 0000545202 scopus 로고
    • Purification of peroxisomes and mitochondria from spinach leaf by Percoll gradient centrifugatuion
    • Schwitzguebel J-P, Siegenthaler P-A (1984) Purification of peroxisomes and mitochondria from spinach leaf by Percoll gradient centrifugatuion. Plant Physiol 75:670-674
    • (1984) Plant Physiol , vol.75 , pp. 670-674
    • Schwitzguebel, J.-P.1    Siegenthaler, P.-A.2
  • 59
    • 0033538442 scopus 로고    scopus 로고
    • In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family
    • Verdoucq L, Vignols F, Jacquot J-P, Chartier Y, Meyer Y (1999) In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. J Biol Chem 274:19714-19722
    • (1999) J Biol Chem , vol.274 , pp. 19714-19722
    • Verdoucq, L.1    Vignols, F.2    Jacquot, J.-P.3    Chartier, Y.4    Meyer, Y.5
  • 62
    • 0030948290 scopus 로고    scopus 로고
    • Oxidative burst: An early plant response to pathogen infection
    • Wojtaszek P (1997) Oxidative burst: an early plant response to pathogen infection. Biochem J 332:681-692
    • (1997) Biochem J , vol.332 , pp. 681-692
    • Wojtaszek, P.1


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