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Volumn 74, Issue 3, 2002, Pages 259-268

Plant peroxiredoxins: Alternative hydroperoxide scavenging enzymes

Author keywords

Chloroplast; Detoxification; Oxidative stress; Peroxiredoxin; Seed

Indexed keywords


EID: 0036914442     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1021218932260     Document Type: Article
Times cited : (74)

References (53)
  • 1
    • 0033513358 scopus 로고    scopus 로고
    • The water-water cycle in chloroplasts: Scavenging of active oxygen and dissipation of excess photons
    • Asada K (1999) The water-water cycle in chloroplasts: Scavenging of active oxygen 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
    • 0030175109 scopus 로고    scopus 로고
    • Primary structure and expression of plant homologues of animal and fungal thioredoxindependent peroxide reductases and bacterial alkyl hydroperoxide reductases
    • Baier M and Dietz KJ (1996) Primary structure and expression of plant homologues of animal and fungal thioredoxindependent peroxide reductases and bacterial alkyl hydroperoxide reductases. Plant Mol Biol 31: 553-564
    • (1996) Plant Mol Biol , vol.31 , pp. 553-564
    • Baier, M.1    Dietz, K.J.2
  • 3
    • 0031194690 scopus 로고    scopus 로고
    • The plant 2-Cys peroxiredoxin BAS1 is a nuclear-encoded chloroplast protein: Its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants
    • Baier M and Dietz KJ (1997) The plant 2-Cys peroxiredoxin BAS1 is a nuclear-encoded chloroplast protein: Its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants. Plant J 12: 179-190
    • (1997) Plant J , vol.12 , pp. 179-190
    • Baier, M.1    Dietz, K.J.2
  • 4
    • 0033117456 scopus 로고    scopus 로고
    • Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis. Evidence from transgenic Arabidopsis
    • Baier M and Dietz KJ (1999a) Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis. Evidence from transgenic Arabidopsis. Plant Physiol 119: 1407-1414
    • (1999) Plant Physiol , vol.119 , pp. 1407-1414
    • Baier, M.1    Dietz, K.J.2
  • 5
    • 0033005699 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductases; the way out of the oxidative breakdown of lipids in chloroplasts
    • Baier M and Dietz KJ (1999b) Alkyl hydroperoxide reductases; the way out of the oxidative breakdown of lipids in chloroplasts. Trends Plant Sci 4: 166-168
    • (1999) Trends Plant Sci , vol.4 , pp. 166-168
    • Baier, M.1    Dietz, K.J.2
  • 6
    • 0033788736 scopus 로고    scopus 로고
    • Antisense suppression of 2-cysteine peroxiredoxin in Arabidopsis specifically enhances the activities and expression of enzymes associated with ascorbate metabolism but not glutathione metabolism
    • Baler M, Noctor G, Foyer CH and Dietz KJ (2000) Antisense suppression of 2-cysteine peroxiredoxin in Arabidopsis specifically enhances the activities and expression of enzymes associated with ascorbate metabolism but not glutathione metabolism. Plant Physiol 124: 823-832
    • (2000) Plant Physiol , vol.124 , pp. 823-832
    • Baler, M.1    Noctor, G.2    Foyer, C.H.3    Dietz, K.J.4
  • 7
    • 0035823608 scopus 로고    scopus 로고
    • Cloning and characterization of three differentially expressed peroxidoxin genes from Leishmania chagasi. Evidence for an enzymatic detoxification of hydroxyl radicals
    • Barr SD and Gedamu L (2001) Cloning and characterization of three differentially expressed peroxidoxin genes from Leishmania chagasi. Evidence for an enzymatic detoxification of hydroxyl radicals. J Biol Chem 276: 34279-34287
    • (2001) J Biol Chem , vol.276 , pp. 34279-34287
    • Barr, S.D.1    Gedamu, L.2
  • 8
    • 0035425182 scopus 로고    scopus 로고
    • Thioredoxin peroxidase-1 (peroxiredoxin-1) is increased in thioredoxin-1 transfected cells and results in enhanced protection against apoptosis caused by hydrogen peroxide but not by other agents including dexamethasone, etoposide, and doxombicin
    • Berggren MI, Husbeck B, Samulitis B, Baker AF, Gallegos A and Powis G (2001) Thioredoxin peroxidase-1 (peroxiredoxin-1) is increased in thioredoxin-1 transfected cells and results in enhanced protection against apoptosis caused by hydrogen peroxide but not by other agents including dexamethasone, etoposide, and doxombicin. Arch Biochem Biophys 2001 392: 103-109
    • (2001) Arch Biochem Biophys 2001 , vol.392 , pp. 103-109
    • Berggren, M.I.1    Husbeck, B.2    Samulitis, B.3    Baker, A.F.4    Gallegos, A.5    Powis, G.6
  • 9
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial perox iredoxins
    • Bryk R, Griffin P and Nathan C (2000) Peroxynitrite reductase activity of bacterial perox iredoxins. Nature 407: 211-215
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 10
    • 0028229670 scopus 로고
    • Dimerization of thiol-specific antioxidant and the essential role of cysteine 47
    • Chae HZ, Uhm TB and Rhee SG (1994a) Dimerization of thiol-specific antioxidant and the essential role of cysteine 47. Proc Natl Acad Sci USA 91: 7022-7026
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7022-7026
    • Chae, H.Z.1    Uhm, T.B.2    Rhee, S.G.3
  • 11
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae HZ, Chung SJ and Rhee SG (1994b) Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 269: 27670-27678
    • (1994) J Biol Chem , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 12
    • 0001445231 scopus 로고    scopus 로고
    • Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin
    • Chae HZ, Kim HJ, Kang SW and Rhee SG (1999) Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin. Diabetes Res Clin Pract 45: 101-112
    • (1999) Diabetes Res Clin Pract , vol.45 , pp. 101-112
    • Chae, H.Z.1    Kim, H.J.2    Kang, S.W.3    Rhee, S.G.4
  • 13
    • 0032060482 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase subunit C (AhpC) protects bacterial and human cells against reactive nitrogen intermediates
    • Chen L, Xie QW and Nathan C (1998) Alkyl hydroperoxide reductase subunit C (AhpC) protects bacterial and human cells against reactive nitrogen intermediates. Mol Cell 1: 795-805
    • (1998) Mol Cell , vol.1 , pp. 795-805
    • Chen, L.1    Xie, Q.W.2    Nathan, C.3
  • 15
    • 0033583798 scopus 로고    scopus 로고
    • Cloning and expression of a new isotype of the peroxiredoxin gene of Chinese cabbage and its comparison to 2Cys-peroxiredoxin isolated from the same plant
    • Choi YO, Cheong NE, Lee KO, Jung BG, Hong CH, Jeong JH, Chi YH, Kim K, Cho MJ and Lee SY (1999) Cloning and expression of a new isotype of the peroxiredoxin gene of Chinese cabbage and its comparison to 2Cys-peroxiredoxin isolated from the same plant. Biochem Biophys Res 258: 768-771
    • (1999) Biochem Biophys Res , vol.258 , pp. 768-771
    • Choi, Y.O.1    Cheong, N.E.2    Lee, K.O.3    Jung, B.G.4    Hong, C.H.5    Jeong, J.H.6    Chi, Y.H.7    Kim, K.8    Cho, M.J.9    Lee, S.Y.10
  • 16
    • 0036001082 scopus 로고    scopus 로고
    • The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation
    • Dietz KJ, Horling F, König J and Baier M (2002) The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation. J Exp Bot 53: 1321-1329
    • (2002) J Exp Bot , vol.53 , pp. 1321-1329
    • Dietz, K.J.1    Horling, F.2    König, J.3    Baier, M.4
  • 17
    • 0033932601 scopus 로고    scopus 로고
    • Oxygen processing in photosynthesis: Regulation and signalling
    • Foyer CH and Noctor G (2000) Oxygen processing in photosynthesis: Regulation and signalling. New Phytol 146: 359-388
    • (2000) New Phytol , vol.146 , pp. 359-388
    • Foyer, C.H.1    Noctor, G.2
  • 18
    • 0034932192 scopus 로고    scopus 로고
    • Molecular characterisation of a bean chloroplastic 2-Cys peroxiredoxin
    • Genot G, Wintz H, Houlné G and Jamet E (2001) Molecular characterisation of a bean chloroplastic 2-Cys peroxiredoxin. Plant physiol Biochem 39: 449-459
    • (2001) Plant Physiol Biochem , vol.39 , pp. 449-459
    • Genot, G.1    Wintz, H.2    Houlné, G.3    Jamet, E.4
  • 20
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell B and Gutteridge JM (1990) Role of free radicals and catalytic metal ions in human disease: An overview. Methods Enzymol 186: 1-85
    • (1990) Methods Enzymol , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.2
  • 21
    • 0032055342 scopus 로고    scopus 로고
    • The expression of a peroxiredoxin antioxidant gene, AtPerl, in Arabidopsis thaliana is seed-specific and related to dormancy
    • Haslekas C, Stacy RA, Nygaard V, Culianez-Macia FA and Aalen RB (1998) The expression of a peroxiredoxin antioxidant gene, AtPerl, in Arabidopsis thaliana is seed-specific and related to dormancy. Plant Mol Biol 36: 833-845
    • (1998) Plant Mol Biol , vol.36 , pp. 833-845
    • Haslekas, C.1    Stacy, R.A.2    Nygaard, V.3    Culianez-Macia, F.A.4    Aalen, R.B.5
  • 22
    • 0036094218 scopus 로고    scopus 로고
    • Two GPX-like proteins from Lycopersicon esculentum and Helianthus annuus are antioxidant enzymes with phospholipid hydroperoxide glutathione peroxidase and thioredoxin peroxidase activities
    • Herbette S, Lenne C, Leblanc N, Julien JL, Drevet JR and Roeckel-Drevet P (2002) Two GPX-like proteins from Lycopersicon esculentum and Helianthus annuus are antioxidant enzymes with phospholipid hydroperoxide glutathione peroxidase and thioredoxin peroxidase activities. Eur J Biochem 269: 2414-2420
    • (2002) Eur J Biochem , vol.269 , pp. 2414-2420
    • Herbette, S.1    Lenne, C.2    Leblanc, N.3    Julien, J.L.4    Drevet, J.R.5    Roeckel-Drevet, P.6
  • 23
    • 0035786229 scopus 로고    scopus 로고
    • Redox-regulation of the expression of the peroxide-detoxifying chloroplast 2-cys peroxiredoxin in the liverwort Riccia fluitans
    • Horling F, Baier M and Dietz KJ (2001) Redox-regulation of the expression of the peroxide-detoxifying chloroplast 2-cys peroxiredoxin in the liverwort Riccia fluitans. Planta 214: 304-313
    • (2001) Planta , vol.214 , pp. 304-313
    • Horling, F.1    Baier, M.2    Dietz, K.J.3
  • 24
    • 0034723165 scopus 로고    scopus 로고
    • Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide peroxidase C (AhpC) family
    • Jeong W, Cha MK and Kim IH (2000) Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide peroxidase C (AhpC) family. J Biol Chem 275: 2924-2930
    • (2000) J Biol Chem , vol.275 , pp. 2924-2930
    • Jeong, W.1    Cha, M.K.2    Kim, I.H.3
  • 25
    • 0037066696 scopus 로고    scopus 로고
    • A Chinese cabbage cDNA with high sequence identity to phospholipid hydroperoxide glutathione peroxidases encodes a novel isoform of thioredoxin-dependent peroxidase
    • Jung BG, Lee KO, Lee SS, Chi YH, Jang HH, Kang SS, Lee K, Lim D, Yoon SC, Yun DJ, Inoue Y, Cho MJ and Lee SY (2002) A Chinese cabbage cDNA with high sequence identity to phospholipid hydroperoxide glutathione peroxidases encodes a novel isoform of thioredoxin-dependent peroxidase. J Biol Chem 277: 12572-12578
    • (2002) J Biol Chem , vol.277 , pp. 12572-12578
    • Jung, B.G.1    Lee, K.O.2    Lee, S.S.3    Chi, Y.H.4    Jang, H.H.5    Kang, S.S.6    Lee, K.7    Lim, D.8    Yoon, S.C.9    Yun, D.J.10    Inoue, Y.11    Cho, M.J.12    Lee, S.Y.13
  • 26
    • 0141746553 scopus 로고    scopus 로고
    • Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha
    • Kang SW, Chae HZ, Seo MS, Kim K, Baines IC and Rhee SG (1998) Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha. J Biol Chem 273: 6297-6302
    • (1998) J Biol Chem , vol.273 , pp. 6297-6302
    • Kang, S.W.1    Chae, H.Z.2    Seo, M.S.3    Kim, K.4    Baines, I.C.5    Rhee, S.G.6
  • 27
    • 0032450522 scopus 로고    scopus 로고
    • Inactivation by gene disruption of 2-cysteine-peroxiredoxin in Synechocystis sp. PCC 6803 leads to increased stress sensitivity
    • Klughammer B, Baier M and Dietz KJ (1998) Inactivation by gene disruption of 2-cysteine-peroxiredoxin in Synechocystis sp. PCC 6803 leads to increased stress sensitivity. Physiol Plant 104: 699-706
    • (1998) Physiol Plant , vol.104 , pp. 699-706
    • Klughammer, B.1    Baier, M.2    Dietz, K.J.3
  • 29
    • 0034306117 scopus 로고    scopus 로고
    • A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp)
    • Kong W, Shiota S, Shi Y, Nakayama H and Nakayama K (2000) A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp). Biochem J351: 107-114
    • (2000) Biochem J , vol.351 , pp. 107-114
    • Kong, W.1    Shiota, S.2    Shi, Y.3    Nakayama, H.4    Nakayama, K.5
  • 30
    • 0037117488 scopus 로고    scopus 로고
    • The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redoxhierarchy of photosynthetic electron flux
    • König J, Baier M, Horling F, Kahmann U, Harris G, Schurmann P and Dietz KJ (2002) The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redoxhierarchy of photosynthetic electron flux. Proc Natl Acad Sci USA. 99: 5738-5743
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5738-5743
    • König, J.1    Baier, M.2    Horling, F.3    Kahmann, U.4    Harris, G.5    Schurmann, P.6    Dietz, K.J.7
  • 31
    • 0034640460 scopus 로고    scopus 로고
    • Catalases and thioredoxin peroxidase protect Saccharomyces cerevisiae against Ca(2+)-induced mitochondrial membrane permeabilization and cell death
    • Kowaltowski AJ, Vercesi AE, Rhee SG and Netto LE (2000) Catalases and thioredoxin peroxidase protect Saccharomyces cerevisiae against Ca(2+)-induced mitochondrial membrane permeabilization and cell death. FEBS Lett 473: 177-182
    • (2000) FEBS Lett , vol.473 , pp. 177-182
    • Kowaltowski, A.J.1    Vercesi, A.E.2    Rhee, S.G.3    Netto, L.E.4
  • 33
    • 0034624199 scopus 로고    scopus 로고
    • Rice 1Cys-peroxiredoxin over-expressed in transgenic tobacco does not maintain dormancy but enhances antioxidant activity
    • Lee KO, Jang HH, Jung BG, Chi YH, Lee JY, Choi YO, Lee JR, Lim CO, Cho MJ and Lee SY (2000) Rice 1Cys-peroxiredoxin over-expressed in transgenic tobacco does not maintain dormancy but enhances antioxidant activity. FEBS Lett 486: 103-106
    • (2000) FEBS Lett , vol.486 , pp. 103-106
    • Lee, K.O.1    Jang, H.H.2    Jung, B.G.3    Chi, Y.H.4    Lee, J.Y.5    Choi, Y.O.6    Lee, J.R.7    Lim, C.O.8    Cho, M.J.9    Lee, S.Y.10
  • 34
  • 35
    • 0034603781 scopus 로고    scopus 로고
    • FePer 1, a gene encoding an evolutionarily conserved 1-Cys peroxiredoxin in buckwheat (Fagopyrum esculentum Moench), is expressed in a seed-specific manner and induced during seed germination
    • Lewis ML, Miki K and Ueda T (2000) FePer 1, a gene encoding an evolutionarily conserved 1-Cys peroxiredoxin in buckwheat (Fagopyrum esculentum Moench), is expressed in a seed-specific manner and induced during seed germination. Gene 246: 81-91
    • (2000) Gene , vol.246 , pp. 81-91
    • Lewis, M.L.1    Miki, K.2    Ueda, T.3
  • 36
    • 0032570772 scopus 로고    scopus 로고
    • Sequence analysis of the tryparedoxin peroxidase gene from Crithidia fasciculata and its functional expression in Escherichia coli
    • Montemartini M, Nogoceke E, Singh M, Steinert P, Flohe L and Kalisz HM (1998) Sequence analysis of the tryparedoxin peroxidase gene from Crithidia fasciculata and its functional expression in Escherichia coli. J Biol Chem 273: 4864-4871
    • (1998) J Biol Chem , vol.273 , pp. 4864-4871
    • Montemartini, M.1    Nogoceke, E.2    Singh, M.3    Steinert, P.4    Flohe, L.5    Kalisz, H.M.6
  • 37
    • 0035949574 scopus 로고    scopus 로고
    • Comprehensive survey of proteins targeted by chloroplast thioredoxin
    • Motohashi K, Kondoh A, Stumpp MT and Hisabori T (2001) Comprehensive survey of proteins targeted by chloroplast thioredoxin. Proc Natl Acad Sci USA 98: 11224-11229
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11224-11229
    • Motohashi, K.1    Kondoh, A.2    Stumpp, M.T.3    Hisabori, T.4
  • 39
    • 0025033314 scopus 로고
    • Antisense RNA of the latent period gene (MER5) inhibits the differentiation of murine erythroleukemia cells
    • Nemoto Y, Yamamoto T, Takada S, Matsui Y and Obinata M (1990) Antisense RNA of the latent period gene (MER5) inhibits the differentiation of murine erythroleukemia cells. Gene 91: 261-265
    • (1990) Gene , vol.91 , pp. 261-265
    • Nemoto, Y.1    Yamamoto, T.2    Takada, S.3    Matsui, Y.4    Obinata, M.5
  • 40
    • 0031735647 scopus 로고    scopus 로고
    • Ascorbate and glutathione: Keeping active oxygen under control
    • Noctor G and Foyer CH (1998) Ascorbate and glutathione: Keeping active oxygen under control. Annu Rev Plant Physiol Plant Mol Biol 49: 249-279
    • (1998) Annu Rev Plant Physiol Plant Mol Biol , vol.49 , pp. 249-279
    • Noctor, G.1    Foyer, C.H.2
  • 41
    • 0033525509 scopus 로고    scopus 로고
    • Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae
    • Pedrajas JR, Kosmidou E, Miranda-Vizuete A, Gustafsson JA, Wright AP and Spyrou G (1999) Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae. J Biol Chem 274: 6366-6373
    • (1999) J Biol Chem , vol.274 , pp. 6366-6373
    • Pedrajas, J.R.1    Kosmidou, E.2    Miranda-Vizuete, A.3    Gustafsson, J.A.4    Wright, A.P.5    Spyrou, G.6
  • 42
    • 0030066091 scopus 로고    scopus 로고
    • Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction
    • Poole LB (1996) Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction. Biochemistry 35: 65-75
    • (1996) Biochemistry , vol.35 , pp. 65-75
    • Poole, L.B.1
  • 43
    • 0027247446 scopus 로고
    • A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing hoinology with amoebic and bacterial proteins
    • Prosperi MT, Ferbus D, Karczinski I and Goubin G (1993) A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing hoinology with amoebic and bacterial proteins. J Biol Chem 268: 11050-11056
    • (1993) J Biol Chem , vol.268 , pp. 11050-11056
    • Prosperi, M.T.1    Ferbus, D.2    Karczinski, I.3    Goubin, G.4
  • 44
    • 0037065722 scopus 로고    scopus 로고
    • An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum
    • Reynolds CM, Meyer J and Poole LB (2002) An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum. Biochemistry 41: 1990-2001
    • (2002) Biochemistry , vol.41 , pp. 1990-2001
    • Reynolds, C.M.1    Meyer, J.2    Poole, L.B.3
  • 45
    • 0035202123 scopus 로고    scopus 로고
    • Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor
    • Rouhier N, Gelhaye E, Sautière PE, Brun A, Laurent P, Tagu D, de Fay E, Meyer Y and Jacquot JP (2001) Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor. Plant Physiol 127: 1299-1309
    • (2001) Plant Physiol , vol.127 , pp. 1299-1309
    • Rouhier, N.1    Gelhaye, E.2    Sautière, P.E.3    Brun, A.4    Laurent, P.5    Tagu, D.6    De Fay, E.7    Meyer, Y.8    Jacquot, J.P.9
  • 46
    • 0037134534 scopus 로고    scopus 로고
    • Glutaredoxin-dependent Peroxiredoxin from Poplar. Protein-protein interaction and catalytic mechanism
    • Rouhier N, Gelhaye E and Jacquot JP (2002) Glutaredoxin-dependent Peroxiredoxin from Poplar. Protein-protein interaction and catalytic mechanism. J Biol Chem 277: 13609-13614
    • (2002) J Biol Chem , vol.277 , pp. 13609-13614
    • Rouhier, N.1    Gelhaye, E.2    Jacquot, J.P.3
  • 47
    • 0001015125 scopus 로고    scopus 로고
    • Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
    • Seo MS, Kang SW, Kim K, Baines IC, Lee TH and Rhee SG (2000) Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. J Biol Chem 275: 20346-20354
    • (2000) J Biol Chem , vol.275 , pp. 20346-20354
    • Seo, M.S.1    Kang, S.W.2    Kim, K.3    Baines, I.C.4    Lee, T.H.5    Rhee, S.G.6
  • 48
    • 0032557638 scopus 로고    scopus 로고
    • Inhibition of ascorbate peroxidase under oxidative stress in tobacco having bacterial catalase in chloroplasts
    • Shikanai T, Takeda T, Yamauchi H, Sano S, Tomizawa KI, Yokota A and Shigeoka S (1998) Inhibition of ascorbate peroxidase under oxidative stress in tobacco having bacterial catalase in chloroplasts. FEBS Lett 428: 47-51
    • (1998) FEBS Lett , vol.428 , pp. 47-51
    • Shikanai, T.1    Takeda, T.2    Yamauchi, H.3    Sano, S.4    Tomizawa, K.I.5    Yokota, A.6    Shigeoka, S.7
  • 49
    • 0030237516 scopus 로고    scopus 로고
    • A peroxiredoxin antioxidant is encoded by a dormancy-related gene, Perl, expressed during late development in the aleurone and embryo of barley grains
    • Stacy RA, Munthe E, Steinum T, Sharma B and Aalen RB (1996) A peroxiredoxin antioxidant is encoded by a dormancy-related gene, Perl, expressed during late development in the aleurone and embryo of barley grains. Plant Mol Biol 31: 1205-1216
    • (1996) Plant Mol Biol , vol.31 , pp. 1205-1216
    • Stacy, R.A.1    Munthe, E.2    Steinum, T.3    Sharma, B.4    Aalen, R.B.5
  • 50
    • 0033166877 scopus 로고    scopus 로고
    • The dormancy-related peroxiredoxin anti-oxidant, PER1, is localized to the nucleus of barley embryo and aleurone cells
    • Stacy RA, Nordeng TW, Culianez-Macia FA and Aalen RB (1999) The dormancy-related peroxiredoxin anti-oxidant, PER1, is localized to the nucleus of barley embryo and aleurone cells. Plant J 19: 1-8
    • (1999) Plant J , vol.19 , pp. 1-8
    • Stacy, R.A.1    Nordeng, T.W.2    Culianez-Macia, F.A.3    Aalen, R.B.4
  • 51
    • 0035877729 scopus 로고    scopus 로고
    • Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling
    • Vergauwen B, Pauwels F, Jacquemotte F, Meyer TE, Cusanovich MA, Bartsch RG and Van Beeumen JJ (2001) Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. J Biol Chem 276: 20890-20897
    • (2001) J Biol Chem , vol.276 , pp. 20890-20897
    • Vergauwen, B.1    Pauwels, F.2    Jacquemotte, F.3    Meyer, T.E.4    Cusanovich, M.A.5    Bartsch, R.G.6    Van Beeumen, J.J.7
  • 53
    • 0030692005 scopus 로고    scopus 로고
    • Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2
    • Zhang P, Liu B, Kang SW, Seo MS, Rhee SG and Obeid LM (1997) Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2. J Biol Chem 272: 30615-30618
    • (1997) J Biol Chem , vol.272 , pp. 30615-30618
    • Zhang, P.1    Liu, B.2    Kang, S.W.3    Seo, M.S.4    Rhee, S.G.5    Obeid, L.M.6


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