메뉴 건너뛰기




Volumn 235, Issue 1-4, 2009, Pages 3-15

Peroxiredoxins: A less studied component of hydrogen peroxide detoxification in photosynthetic organisms

Author keywords

Antioxidant; Hydrogen peroxides; Nutrient deficiency; Oxidative stress; Peroxiredoxin; Reactive oxygen species

Indexed keywords

HYDROGEN PEROXIDE; PEROXIREDOXIN;

EID: 62949245620     PISSN: 0033183X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00709-009-0032-0     Document Type: Review
Times cited : (117)

References (93)
  • 1
    • 0028388161 scopus 로고
    • Transcripts encoding an oleosin and a dormancy-related protein are present in both the aleurone layer and the embryo of developing barley (Hordeum vulgare L.) seeds
    • RB Aalen HG Opsahl-Festad C Linnestad OA Olsen 1994 Transcripts encoding an oleosin and a dormancy-related protein are present in both the aleurone layer and the embryo of developing barley (Hordeum vulgare L.) seeds Plant J 5 385 396
    • (1994) Plant J , vol.5 , pp. 385-396
    • Aalen, R.B.1    Opsahl-Festad, H.G.2    Linnestad, C.3    Olsen, O.A.4
  • 2
    • 0034730977 scopus 로고    scopus 로고
    • The water-water cycle as alternative photon and electron sinks
    • K Asada 2000 The water-water cycle as alternative photon and electron sinks Philos Trans R Soc 355 1419 1430
    • (2000) Philos Trans R Soc , vol.355 , pp. 1419-1430
    • Asada, K.1
  • 3
    • 0030175109 scopus 로고    scopus 로고
    • Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases
    • M Baier K-J Dietz 1996 Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent 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
  • 4
    • 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
    • M Baier K-J Dietz 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
  • 5
    • 0033117456 scopus 로고    scopus 로고
    • Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis: Evidence from transgenic Arabidopsis thaliana
    • M Baier K-J Dietz 1999 Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis: evidence from transgenic Arabidopsis thaliana Plant Physiol 119 1407 1414
    • (1999) Plant Physiol , vol.119 , pp. 1407-1414
    • Baier, M.1    Dietz, K.-J.2
  • 6
    • 0033788736 scopus 로고    scopus 로고
    • Antisense suppression of 2-Cys peroxiredoxin in Arabidopsis thaliana specifically enhances the activities and expression of enzymes associated with ascorbate metabolism, but not glutathione metabolism
    • M Baier G Noctor CH Foyer K-J Dietz 2000 Antisense suppression of 2-Cys peroxiredoxin in Arabidopsis thaliana 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
    • Baier, M.1    Noctor, G.2    Foyer, C.H.3    Dietz, K.-J.4
  • 7
    • 17644386166 scopus 로고    scopus 로고
    • Human mitochondrial peroxiredoxin 5 protects from mitochondrial DNA damages induced by hydrogen peroxide
    • I Banmeyer C Marchand A Clipe B Knoops 2005 Human mitochondrial peroxiredoxin 5 protects from mitochondrial DNA damages induced by hydrogen peroxide FEBS Lett 579 2327 2333
    • (2005) FEBS Lett , vol.579 , pp. 2327-2333
    • Banmeyer, I.1    Marchand, C.2    Clipe, A.3    Knoops, B.4
  • 8
    • 33745713185 scopus 로고    scopus 로고
    • Cloning, overexpression, purification and preliminary crystallographic studies of a mitochondrial type II peroxiredoxin from Pisum sativum
    • S Barranco-Medina FJ López-Jaramillo L Bernier-Villamor F Sevilla JJ Lázaro 2006 Cloning, overexpression, purification and preliminary crystallographic studies of a mitochondrial type II peroxiredoxin from Pisum sativum Acta Crystall F 62 695 698
    • (2006) Acta Crystall F , vol.62 , pp. 695-698
    • Barranco-Medina, S.1    López-Jaramillo, F.J.2    Bernier-Villamor, L.3    Sevilla, F.4    Lázaro, J.J.5
  • 10
    • 46849118983 scopus 로고    scopus 로고
    • Thermodynamics of the dimer-decamer transition of reduced human and plant 2-Cys peroxiredoxin
    • S Barranco-Medina S Kakorin JJ Lázaro K-J Dietz 2008 Thermodynamics of the dimer-decamer transition of reduced human and plant 2-Cys peroxiredoxin Biochemistry 47 7196 7204
    • (2008) Biochemistry , vol.47 , pp. 7196-7204
    • Barranco-Medina, S.1    Kakorin, S.2    Lázaro, J.J.3    Dietz, K.-J.4
  • 11
    • 2142856869 scopus 로고    scopus 로고
    • Cloning of cDNA encoding a thioredoxin peroxidase (PTx) homolog from winter rye (Secale cereale L.) (Accession no
    • T Berberich M Vebeler J Feierabend 1998 Cloning of cDNA encoding a thioredoxin peroxidase (PTx) homolog from winter rye (Secale cereale L.) (Accession no AF076920). Plant Physiol Plant Gene Reg 118 98 167
    • (1998) AF076920). Plant Physiol Plant Gene Reg , vol.118 , pp. 98-167
    • Berberich, T.1    Vebeler, M.2    Feierabend, J.3
  • 12
    • 0043011656 scopus 로고    scopus 로고
    • Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: Similar sequences for divergent gene expression, protein localization, and activity
    • C Brehelin EH Meyer JP de Souris G Bonnard Y Meyer 2003 Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization, and activity Plant Physiol 132 2045 2057
    • (2003) Plant Physiol , vol.132 , pp. 2045-2057
    • Brehelin, C.1    Meyer, E.H.2    De Souris, J.P.3    Bonnard, G.4    Meyer, Y.5
  • 13
    • 0027323871 scopus 로고
    • Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae
    • HZ Chae I-H Kim K Kim SG Rhee 1993 Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae J Biol Chem 268 16815 16821
    • (1993) J Biol Chem , vol.268 , pp. 16815-16821
    • Chae, H.Z.1    Kim, I.-H.2    Kim, K.3    Rhee, S.G.4
  • 14
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • HZ Chae SJ Chung SG Rhee 1994 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
  • 15
    • 0000385805 scopus 로고    scopus 로고
    • Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin
    • HZ Chae SW Kang SG Rhee 1999 Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin Methods Enzymol 300 219 226
    • (1999) Methods Enzymol , vol.300 , pp. 219-226
    • Chae, H.Z.1    Kang, S.W.2    Rhee, S.G.3
  • 17
    • 0031945918 scopus 로고    scopus 로고
    • Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution
    • HJ Choi SW Kang CH Yang SG Rhee SE Ryu 1998 Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution Nat Struct Biol 5 400 406
    • (1998) Nat Struct Biol , vol.5 , pp. 400-406
    • Choi, H.J.1    Kang, S.W.2    Yang, C.H.3    Rhee, S.G.4    Ryu, S.E.5
  • 21
    • 0035943382 scopus 로고    scopus 로고
    • Crystal structure of human peroxiredoxin5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution
    • JP Declercq C Evrard A Clippe D Vander Stricht A Bernard B Knoops 2001 Crystal structure of human peroxiredoxin5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution J Mol Biol 311 751 759
    • (2001) J Mol Biol , vol.311 , pp. 751-759
    • Declercq, J.P.1    Evrard, C.2    Clippe, A.3    Vander Stricht, D.4    Bernard, A.5    Knoops, B.6
  • 22
  • 23
    • 0036001082 scopus 로고    scopus 로고
    • The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation
    • K-J Dietz F Horling J Konig M Baier 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    Konig, J.3    Baier, M.4
  • 27
    • 16844368306 scopus 로고    scopus 로고
    • The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress
    • I Finkemeier M Goodman P Lamkemeyer A Kandlbinder LJ Sweetlove K-J Dietz 2005 The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress J Biol Chem 280 12168 12180
    • (2005) J Biol Chem , vol.280 , pp. 12168-12180
    • Finkemeier, I.1    Goodman, M.2    Lamkemeyer, P.3    Kandlbinder, A.4    Sweetlove, L.J.5    Dietz, K.-J.6
  • 28
    • 0033932601 scopus 로고    scopus 로고
    • Oxygen processing in photosynthesis: Regulation and signaling
    • CH Foyer G Noctor 2000 Oxygen processing in photosynthesis: regulation and signaling New Phytol 146 359 388
    • (2000) New Phytol , vol.146 , pp. 359-388
    • Foyer, C.H.1    Noctor, G.2
  • 29
    • 0036287739 scopus 로고    scopus 로고
    • Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein
    • J Fujii Y Ikeda 2002 Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein Redox Rep 7 1 8
    • (2002) Redox Rep , vol.7 , pp. 1-8
    • Fujii, J.1    Ikeda, Y.2
  • 31
    • 45249116783 scopus 로고    scopus 로고
    • Functional analysis and expression characteristics of chloroplastic PrxIIE
    • doi: 10.1111/j.1399-3054.2008.01097.x
    • Gama F, Bréhélin C, Gelhaye E, Meyer Y, Jacquot J-P, Rey P, Rouhier N (2008) Functional analysis and expression characteristics of chloroplastic PrxIIE. Physiol Plant 133:599-610. doi: 10.1111/j.1399-3054.2008. 01097.x
    • (2008) Physiol Plant , vol.133 , pp. 599-610
    • Gama, F.1    Bréhélin, C.2    Gelhaye, E.3    Meyer, Y.4    Jacquot, J.-P.5    Rey, P.6    Rouhier, N.7
  • 33
    • 0032055342 scopus 로고    scopus 로고
    • The expression of a peroxiredoxin antioxidant gene, AtPer1, in Arabidopsis thaliana is seed-specific and related to dormancy
    • C Haslekas RA Stacy V Nygaard FA Culianez-Macia RB Aalen 1998 The expression of a peroxiredoxin antioxidant gene, AtPer1, 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
  • 34
    • 0033607229 scopus 로고    scopus 로고
    • Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product
    • S Hirotsu Y Abe K Okada N Nigahara H Hori T Nishino T Hakaoshina 1999 Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product Proc Natl Acad Sci USA 96 12333 12338
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12333-12338
    • Hirotsu, S.1    Abe, Y.2    Okada, K.3    Nigahara, N.4    Hori, H.5    Nishino, T.6    Hakaoshina, T.7
  • 36
    • 0035786229 scopus 로고    scopus 로고
    • Redox-regulation of the expression of the peroxide-detoxifying chloroplast 2-cys peroxiredoxin in the liverwort Riccia fluitans
    • F Horling M Baier KJ Dietz 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
  • 37
    • 0036619345 scopus 로고    scopus 로고
    • Type II peroxiredoxin C, a member of the peroxiredoxin family of Arabidopsis thaliana: Its expression and activity in comparison with other peroxiredoxins
    • F Horling J Konig K-J Dietz 2002 Type II peroxiredoxin C, a member of the peroxiredoxin family of Arabidopsis thaliana: its expression and activity in comparison with other peroxiredoxins Plant Physiol Biochem 40 491 499
    • (2002) Plant Physiol Biochem , vol.40 , pp. 491-499
    • Horling, F.1    Konig, J.2    Dietz, K.-J.3
  • 38
    • 0037252527 scopus 로고    scopus 로고
    • Divergent light-, ascorbate- and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis
    • F Horling P Lamkemeyer J Konig I Finkemeier A Kandlbinder M Baier K-J Dietz 2003 Divergent light-, ascorbate- and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis Plant Physiol 131 317 325
    • (2003) Plant Physiol , vol.131 , pp. 317-325
    • Horling, F.1    Lamkemeyer, P.2    Konig, J.3    Finkemeier, I.4    Kandlbinder, A.5    Baier, M.6    Dietz, K.-J.7
  • 39
    • 12844253100 scopus 로고    scopus 로고
    • Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803
    • N Hosoya-Matsuda K Motohashi H Yoshimura A Nozaki K Inoue M Ohmori T Hisabori 2005 Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803 J Biol Chem 280 840 846
    • (2005) J Biol Chem , vol.280 , pp. 840-846
    • Hosoya-Matsuda, N.1    Motohashi, K.2    Yoshimura, H.3    Nozaki, A.4    Inoue, K.5    Ohmori, M.6    Hisabori, T.7
  • 40
    • 0027130651 scopus 로고
    • 2 specificity factor of ribulose 1,5-bisphosphate carboxylase-oxygenase in intact leaves of sunflower
    • 2 specificity factor of ribulose 1,5-bisphosphate carboxylase-oxygenase in intact leaves of sunflower J Exp Bot 44 1635 1641
    • (1993) J Exp Bot , vol.44 , pp. 1635-1641
    • Jacob, J.1    Lawlor, D.W.2
  • 41
    • 0000300772 scopus 로고    scopus 로고
    • Purification and characterization of a second type thioredoxin peroxidase (Type II TPx) from Saccharomyces cerevisiae
    • JS Jeong SJ Kwon SW Kang SG Rhee K Kim 1999 Purification and characterization of a second type thioredoxin peroxidase (Type II TPx) from Saccharomyces cerevisiae Biochemistry 38 776 783
    • (1999) Biochemistry , vol.38 , pp. 776-783
    • Jeong, J.S.1    Kwon, S.J.2    Kang, S.W.3    Rhee, S.G.4    Kim, K.5
  • 42
    • 1642424390 scopus 로고    scopus 로고
    • The antioxidant status of photosynthesizing leaves under nutrient deficiency: Redox regulation, gene expression and antioxidant activity in Arabidopsis thaliana
    • A Kandlbinder I Finkemeier D Wormuth M Hanitzsch K-J Dietz 2004 The antioxidant status of photosynthesizing leaves under nutrient deficiency: redox regulation, gene expression and antioxidant activity in Arabidopsis thaliana Physiol Plant 120 63 73
    • (2004) Physiol Plant , vol.120 , pp. 63-73
    • Kandlbinder, A.1    Finkemeier, I.2    Wormuth, D.3    Hanitzsch, M.4    Dietz, K.-J.5
  • 43
    • 0141746553 scopus 로고    scopus 로고
    • Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha
    • SW Kang HZ Chae MS Seo K Kim IC Baines SG Rhee 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
  • 44
    • 24644445236 scopus 로고    scopus 로고
    • A peroxiredoxin Q homolog from gentians is involved in both resistance against fungal disease and oxidative stress
    • A Kiba M Nishihara N Tsukatani T Nakatsuka Y Kato S Yamamura 2005 A peroxiredoxin Q homolog from gentians is involved in both resistance against fungal disease and oxidative stress Plant Cell Physiol 46 1007 1015
    • (2005) Plant Cell Physiol , vol.46 , pp. 1007-1015
    • Kiba, A.1    Nishihara, M.2    Tsukatani, N.3    Nakatsuka, T.4    Kato, Y.5    Yamamura, S.6
  • 46
    • 0033959934 scopus 로고    scopus 로고
    • Bundle sheath proteins are more sensitive to oxidative damage than those of the mesophyll in maize leaves exposed to paraquat or low temperatures
    • AH Kingston-Smith CH Foyer 2000 Bundle sheath proteins are more sensitive to oxidative damage than those of the mesophyll in maize leaves exposed to paraquat or low temperatures J Exp Bot 51 123 130
    • (2000) J Exp Bot , vol.51 , pp. 123-130
    • Kingston-Smith, A.H.1    Foyer, C.H.2
  • 47
    • 0032450522 scopus 로고    scopus 로고
    • Inactivation by gene disruption of 2-Cysteine peroxiredoxin in Synechocystis sp. PCC 6803 leads to increased stress sensitivity
    • B Klughammer M Baier K-J Dietz 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
  • 50
    • 0034306117 scopus 로고    scopus 로고
    • A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp)
    • W Kong S Shiota Y Shi H Nakayama K Nakayama 2000 A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp) Biochem J 351 107 114
    • (2000) Biochem J , vol.351 , pp. 107-114
    • Kong, W.1    Shiota, S.2    Shi, Y.3    Nakayama, H.4    Nakayama, K.5
  • 51
    • 0037117488 scopus 로고    scopus 로고
    • The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux
    • J Konig M Baier F Horling U Kahmann G Harris P Schurmann K-J Dietz 2002 The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux Proc Natl Acad Sci USA 99 5738 5743
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5738-5743
    • Konig, J.1    Baier, M.2    Horling, F.3    Kahmann, U.4    Harris, G.5    Schurmann, P.6    Dietz, K.-J.7
  • 52
    • 0042591328 scopus 로고    scopus 로고
    • Reaction mechanism of plant 2-Cys peroxiredoxin- Role of the C terminus and the quaternary structure
    • J Konig K Lotte R Plessow A Brockhinke M Baier K-J Dietz 2003 Reaction mechanism of plant 2-Cys peroxiredoxin- Role of the C terminus and the quaternary structure J Biol Chem 278 24409 24420
    • (2003) J Biol Chem , vol.278 , pp. 24409-24420
    • Konig, J.1    Lotte, K.2    Plessow, R.3    Brockhinke, A.4    Baier, M.5    Dietz, K.-J.6
  • 53
    • 38349127603 scopus 로고    scopus 로고
    • Modulation of copper toxicity-induced oxidative damage by excess supply of iron in maize plants
    • P Kumar RK Tewari PN Sharma 2008 Modulation of copper toxicity-induced oxidative damage by excess supply of iron in maize plants Plant Cell Rep 27 399 409
    • (2008) Plant Cell Rep , vol.27 , pp. 399-409
    • Kumar, P.1    Tewari, R.K.2    Sharma, P.N.3
  • 55
    • 33846295570 scopus 로고    scopus 로고
    • Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions
    • M Laxa J König K-J Dietz A Kandlbinder 2007 Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions Biochem J 401 287 297
    • (2007) Biochem J , vol.401 , pp. 287-297
    • Laxa, M.1    König, J.2    Dietz, K.-J.3    Kandlbinder, A.4
  • 57
    • 0034603781 scopus 로고    scopus 로고
    • FePER1, a gene encoding an evolutionary conserved 1-Cys peroxiredoxin in buckwheat (Fagopyrum esculentum Moench), is expressed in a seed-specific manner and induced during seed germination
    • ML Lewis K Miki T Ueda 2000 FePER1, a gene encoding an evolutionary 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
  • 58
    • 33645960112 scopus 로고    scopus 로고
    • Functional differentiation of bundle sheath and mesophyll maize chloroplasts determined by comparative proteomics
    • W Majeran Y Cai Q Sun KJ van Wijk 2005 Functional differentiation of bundle sheath and mesophyll maize chloroplasts determined by comparative proteomics Plant Cell 17 3111 3140
    • (2005) Plant Cell , vol.17 , pp. 3111-3140
    • Majeran, W.1    Cai, Y.2    Sun, Q.3    Van Wijk, K.J.4
  • 59
    • 0033928555 scopus 로고    scopus 로고
    • Analysis by two-dimensional electrophoresis of the effect of salt stress on the polypeptide patterns in roots of a salt-tolerant and a salt-sensitive cultivar of wheat
    • T Majoul K Chahed E Zamiti L Ouelhazi R Ghrir 2000 Analysis by two-dimensional electrophoresis of the effect of salt stress on the polypeptide patterns in roots of a salt-tolerant and a salt-sensitive cultivar of wheat Electrophoresis 21 2562 2565
    • (2000) Electrophoresis , vol.21 , pp. 2562-2565
    • Majoul, T.1    Chahed, K.2    Zamiti, E.3    Ouelhazi, L.4    Ghrir, R.5
  • 61
    • 0036935750 scopus 로고    scopus 로고
    • A novel stress-inducible antioxidant enzyme identified from the resurrection plant Xerophyta viscosa Baker
    • SB Mowla JA Thomson JM Farrant SG Mundree 2002 A novel stress-inducible antioxidant enzyme identified from the resurrection plant Xerophyta viscosa Baker Planta 215 716 726
    • (2002) Planta , vol.215 , pp. 716-726
    • Mowla, S.B.1    Thomson, J.A.2    Farrant, J.M.3    Mundree, S.G.4
  • 62
    • 36048942406 scopus 로고    scopus 로고
    • Comparative quantitative proteomics to investigate the remodeling of bioenergetic pathways under iron deficiency in Chlamydomonas reinhardtii
    • B Naumann A Busch J Allmer E Ostendorf M Zeller H Kirchhoff M Hippler 2007 Comparative quantitative proteomics to investigate the remodeling of bioenergetic pathways under iron deficiency in Chlamydomonas reinhardtii Proteomics 21 3964 3979
    • (2007) Proteomics , vol.21 , pp. 3964-3979
    • Naumann, B.1    Busch, A.2    Allmer, J.3    Ostendorf, E.4    Zeller, M.5    Kirchhoff, H.6    Hippler, M.7
  • 63
    • 33845631208 scopus 로고    scopus 로고
    • Plant glutathione peroxidases are functional peroxiredoxins distributed in several subcellular compartments and regulated during biotic and abiotic stresses
    • N Navrot V Collin J Gualberto E Gelhaye M Hirasawa P Rey DB Knaff E Issakidis J-P Jacquot N Rouhier 2006 Plant glutathione peroxidases are functional peroxiredoxins distributed in several subcellular compartments and regulated during biotic and abiotic stresses Plant Physiol 142 1364 1379
    • (2006) Plant Physiol , vol.142 , pp. 1364-1379
    • Navrot, N.1    Collin, V.2    Gualberto, J.3    Gelhaye, E.4    Hirasawa, M.5    Rey, P.6    Knaff, D.B.7    Issakidis, E.8    Jacquot, J.-P.9    Rouhier, N.10
  • 64
    • 0034730972 scopus 로고    scopus 로고
    • Peroxide processing in photosynthesis: Antioxidant coupling and redox signaling
    • G Noctor Veljovic-Jovanovics CH Foyer 2000 Peroxide processing in photosynthesis: antioxidant coupling and redox signaling Philos Trans R Soc Lond Ser B 355 1465 1475
    • (2000) Philos Trans R Soc Lond Ser B , vol.355 , pp. 1465-1475
    • Noctor, G.1    Veljovic-Jovanovics2    Foyer, C.H.3
  • 65
    • 0034717135 scopus 로고    scopus 로고
    • Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin wiyh thioredoxin peroxidase activity
    • JR Pedrajas A Miranda-Vizuete N Javanmardy JA Gustafsson G Spyrou 2000 Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin wiyh thioredoxin peroxidase activity J Biol Chem 275 16296 16301
    • (2000) J Biol Chem , vol.275 , pp. 16296-16301
    • Pedrajas, J.R.1    Miranda-Vizuete, A.2    Javanmardy, N.3    Gustafsson, J.A.4    Spyrou, G.5
  • 66
    • 33947311809 scopus 로고    scopus 로고
    • Regulation of peroxiredoxin expression versus expression of Halliwell-Asada-Cycle enzymes during early seedling development of Arabidopsis thaliana
    • A Pena-Ahumada U Kahmann K-J Dietz M Baier 2006 Regulation of peroxiredoxin expression versus expression of Halliwell-Asada-Cycle enzymes during early seedling development of Arabidopsis thaliana Photosynth Res 89 99 112
    • (2006) Photosynth Res , vol.89 , pp. 99-112
    • Pena-Ahumada, A.1    Kahmann, U.2    Dietz, K.-J.3    Baier, M.4
  • 69
    • 33750576724 scopus 로고    scopus 로고
    • The Prx Q protein of Arabidopsis thaliana is a member of the luminal chloroplast proteome
    • UA Petersson T Kieselbach JG Garcia-Cerdan WP Schroder 2006 The Prx Q protein of Arabidopsis thaliana is a member of the luminal chloroplast proteome FEBS Lett 580 6055 6061
    • (2006) FEBS Lett , vol.580 , pp. 6055-6061
    • Petersson, U.A.1    Kieselbach, T.2    Garcia-Cerdan, J.G.3    Schroder, W.P.4
  • 70
    • 58149131296 scopus 로고    scopus 로고
    • An antioxidant redox system in the nucleus of wheat seed cells suffering oxidative stress
    • P Pulido R Cazalis FJ Cejudo 2009 An antioxidant redox system in the nucleus of wheat seed cells suffering oxidative stress Plant J 57 132 145
    • (2009) Plant J , vol.57 , pp. 132-145
    • Pulido, P.1    Cazalis, R.2    Cejudo, F.J.3
  • 72
    • 33846427352 scopus 로고    scopus 로고
    • The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response
    • P Rey N Becuwe M-B Barrault D Rumean M Havanx B Biteau MB Toledano 2007 The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response Plant J 49 505 514
    • (2007) Plant J , vol.49 , pp. 505-514
    • Rey, P.1    Becuwe, N.2    Barrault, M.-B.3    Rumean, D.4    Havanx, M.5    Biteau, B.6    Toledano, M.B.7
  • 74
    • 0036914442 scopus 로고    scopus 로고
    • Plant peroxiredoxins: Alternative hydroperoxide scavenging enzymes
    • N Rouhier J-P Jacquot 2002 Plant peroxiredoxins: alternative hydroperoxide scavenging enzymes Photosynth Res 74 259 268
    • (2002) Photosynth Res , vol.74 , pp. 259-268
    • Rouhier, N.1    Jacquot, J.-P.2
  • 77
    • 23844543308 scopus 로고    scopus 로고
    • Acclimation of unicellular cyanobacteria to macronutrient deficiency: Emerge of a complex network of cellular responses
    • R Schwarz K Forchhammer 2005 Acclimation of unicellular cyanobacteria to macronutrient deficiency: emerge of a complex network of cellular responses Mol Microbiol 151 2503 2514
    • (2005) Mol Microbiol , vol.151 , pp. 2503-2514
    • Schwarz, R.1    Forchhammer, K.2
  • 78
    • 0001015125 scopus 로고    scopus 로고
    • Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
    • MS Seo SW Kang K Kim IC Baines TH Lee SG Rhee 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
  • 79
    • 6344235622 scopus 로고    scopus 로고
    • A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana
    • AJ Serrato JM Pérez-Ruiz MC Spínola FJ Cejudo 2004 A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana J Biol Chem 279 43821 43827
    • (2004) J Biol Chem , vol.279 , pp. 43821-43827
    • Serrato, A.J.1    Pérez-Ruiz, J.M.2    Spínola, M.C.3    Cejudo, F.J.4
  • 80
    • 0032557638 scopus 로고    scopus 로고
    • Inhibition of ascorbate peroxidase under oxidative stress in tobacco having bacterial catalase in chloroplasts
    • T Shikanai T Takeda H Yamauchi S Sano KI Tomizawa A Yakota S Shigeoka 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    Yakota, A.6    Shigeoka, S.7
  • 81
    • 2942592057 scopus 로고    scopus 로고
    • Hydrogen peroxide mediates plant root cell response to nutrient deprivation
    • R Shin DP Schachtman 2004 Hydrogen peroxide mediates plant root cell response to nutrient deprivation Proc Natl Acad Sci USA 101 8827 8832
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8827-8832
    • Shin, R.1    Schachtman, D.P.2
  • 82
    • 0030237516 scopus 로고    scopus 로고
    • A peroxiredoxin antioxidant is encoded by a dormancy-related gene, Per1, expressed during late development in the aleurone and embryo of barley grains
    • RA Stacy E Munthe T Steinum B Sharma RB Aalen 1996 A peroxiredoxin antioxidant is encoded by a dormancy-related gene, Per1, 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
  • 83
    • 0033166877 scopus 로고    scopus 로고
    • The dormancy-related peroxiredoxin anti-oxidant, PER 1, is localized to the nucleus of barley embryo and aleurone cells
    • RA Stacy TW Nordeng FA Culianez-Macia RB Aalen 1999 The dormancy-related peroxiredoxin anti-oxidant, PER 1, 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
  • 84
    • 28544436837 scopus 로고    scopus 로고
    • Bioinformatic analysis of the genomes of the cyanobacteria Synechocystis sp. PCC 6803 and Synechocystis elongatus PCC 7942 for the presence of peroxiredoxins and the transcript regulation under stress
    • T Stork KP Michel E Pistorius K-J Dietz 2005 Bioinformatic analysis of the genomes of the cyanobacteria Synechocystis sp. PCC 6803 and Synechocystis elongatus PCC 7942 for the presence of peroxiredoxins and the transcript regulation under stress J Exp Bot 56 3193 3206
    • (2005) J Exp Bot , vol.56 , pp. 3193-3206
    • Stork, T.1    Michel, K.P.2    Pistorius, E.3    Dietz, K.-J.4
  • 85
    • 0024604234 scopus 로고
    • An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: Genetic characterization and cloning of ahp
    • G Storz FS Jacobson LA Tartaglia RW Morgan LA Silveira BN Ames 1989 An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp J Bacteriol 171 2049 2055
    • (1989) J Bacteriol , vol.171 , pp. 2049-2055
    • Storz, G.1    Jacobson, F.S.2    Tartaglia, L.A.3    Morgan, R.W.4    Silveira, L.A.5    Ames, B.N.6
  • 86
    • 26444485613 scopus 로고    scopus 로고
    • Signs of oxidative stress in the chlorotic leaves of iron starved plants
    • RK Tewari P Kumar Neetu PN Sharma 2005 Signs of oxidative stress in the chlorotic leaves of iron starved plants Plant Sci 169 1037 1045
    • (2005) Plant Sci , vol.169 , pp. 1037-1045
    • Tewari, R.K.1    Kumar, P.2    Neetu3    Sharma, P.N.4
  • 87
    • 33646402077 scopus 로고    scopus 로고
    • Antioxidant responses to enhanced generation of superoxide anion radical and hydrogen peroxide in the copper-stressed mulberry plants
    • RK Tewari P Kumar PN Sharma 2006 Antioxidant responses to enhanced generation of superoxide anion radical and hydrogen peroxide in the copper-stressed mulberry plants Planta 223 1145 1153
    • (2006) Planta , vol.223 , pp. 1145-1153
    • Tewari, R.K.1    Kumar, P.2    Sharma, P.N.3
  • 88
    • 3543127836 scopus 로고    scopus 로고
    • Relationship between copper- and zinc- induced oxidative stress and proline accumulation in Scenedesmus sp
    • BN Tripathi JP Gaur 2004 Relationship between copper- and zinc- induced oxidative stress and proline accumulation in Scenedesmus sp Planta 219 397 404
    • (2004) Planta , vol.219 , pp. 397-404
    • Tripathi, B.N.1    Gaur, J.P.2
  • 89
    • 28444433696 scopus 로고    scopus 로고
    • Oxidative stress in Scenedesmus sp. during short- and long term exposure to Cu and Zn
    • BN Tripathi SK Mehta A Amar JP Gaur 2006 Oxidative stress in Scenedesmus sp. during short- and long term exposure to Cu and Zn Chemosphere 62 538 544
    • (2006) Chemosphere , vol.62 , pp. 538-544
    • Tripathi, B.N.1    Mehta, S.K.2    Amar, A.3    Gaur, J.P.4
  • 90
    • 0033538442 scopus 로고    scopus 로고
    • In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family
    • L Verdoucq F Vignol J-P Jacquot Y Chartier Y Meyer 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    Vignol, F.2    Jacquot, J.-P.3    Chartier, Y.4    Meyer, Y.5
  • 91
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • ZA Wood LB Poole PA Karplus 2003 Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling Science 300 650 653
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.