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Volumn 80, Issue 6, 2012, Pages 659-671

Identification of superoxide production by Arabidopsis thaliana aldehyde oxidases AAO1 and AAO3

Author keywords

AAO1; AAO3; Abscisic acid; Aldehyde oxidase; Reactive oxygen species; Superoxide

Indexed keywords

AAO1 PROTEIN, ARABIDOPSIS; AAO3 PROTEIN, ARABIDOPSIS; ALDEHYDE; ALDEHYDE OXIDASE; ARABIDOPSIS PROTEIN; HYDROGEN PEROXIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; RECOMBINANT PROTEIN; SUPEROXIDE;

EID: 84870241093     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11103-012-9975-1     Document Type: Article
Times cited : (22)

References (83)
  • 1
    • 0001307066 scopus 로고
    • Endogenous gibberellin and abscisic acid content as related to senescence of detached lettuce leaves
    • Aharoni N, Richmond AE (1978) Endogenous gibberellin and abscisic acid content as related to senescence of detached lettuce leaves. Plant Physiol 62: 224-228.
    • (1978) Plant Physiol , vol.62 , pp. 224-228
    • Aharoni, N.1    Richmond, A.E.2
  • 2
    • 0032463418 scopus 로고    scopus 로고
    • Aldehyde oxidase in wild type and abal mutant leaves of Nicotiana plumbaginifolia
    • Akaba S, Leydecker MT, Moureaux T, Oritani T, Koshiba T (1998) Aldehyde oxidase in wild type and abal mutant leaves of Nicotiana plumbaginifolia. Plant Cell Physiol 39: 1281-1286.
    • (1998) Plant Cell Physiol , vol.39 , pp. 1281-1286
    • Akaba, S.1    Leydecker, M.T.2    Moureaux, T.3    Oritani, T.4    Koshiba, T.5
  • 4
    • 0001472397 scopus 로고
    • Transmembrane electron transport in plasma membrane vesicles loaded with an NADH-generating system or ascorbate
    • Askerlund P, Larsson C (1991) Transmembrane electron transport in plasma membrane vesicles loaded with an NADH-generating system or ascorbate. Plant Physiol 96: 1178-1184.
    • (1991) Plant Physiol , vol.96 , pp. 1178-1184
    • Askerlund, P.1    Larsson, C.2
  • 5
    • 0019487878 scopus 로고
    • Superoxide production by an unusual aldehyde oxidase in guinea pig granulocytes. Characterization and cytochemical localization
    • Badwey JA, Robinson JM, Karnovsky MJ, Karnovsky ML (1981) Superoxide production by an unusual aldehyde oxidase in guinea pig granulocytes. Characterization and cytochemical localization. J Biol Chem 256: 3479-3486.
    • (1981) J Biol Chem , vol.256 , pp. 3479-3486
    • Badwey, J.A.1    Robinson, J.M.2    Karnovsky, M.J.3    Karnovsky, M.L.4
  • 6
    • 0343674523 scopus 로고    scopus 로고
    • Distribution of the Mo-enzymes aldehyde oxidase, xanthine dehydrogenase and nitrate reductase in maize (Zea mays L.) nodal roots as affected by nitrogen and salinity
    • Barabás KN, Omarov RT, Erdei L, Lips HS (2000) Distribution of the Mo-enzymes aldehyde oxidase, xanthine dehydrogenase and nitrate reductase in maize (Zea mays L.) nodal roots as affected by nitrogen and salinity. Plant Sci 155: 49-58.
    • (2000) Plant Sci , vol.155 , pp. 49-58
    • Barabás, K.N.1    Omarov, R.T.2    Erdei, L.3    Lips, H.S.4
  • 7
    • 33747833649 scopus 로고    scopus 로고
    • Both abscisic acid (ABA)-dependent and ABA-independent pathways govern the induction of NCED3, AAO3 and ABA1 in response to salt stress
    • Barrero JM, Rodríguez PL, Quesada V, Piqueras P, Ponce MR, Micol JL (2006) Both abscisic acid (ABA)-dependent and ABA-independent pathways govern the induction of NCED3, AAO3 and ABA1 in response to salt stress. Plant Cell Environ 29: 2000-2008.
    • (2006) Plant Cell Environ , vol.29 , pp. 2000-2008
    • Barrero, J.M.1    Rodríguez, P.L.2    Quesada, V.3    Piqueras, P.4    Ponce, M.R.5    Micol, J.L.6
  • 8
    • 0035798636 scopus 로고    scopus 로고
    • ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana
    • Bittner F, Oreb M, Mendel RR (2001) ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana. J Biol Chem 276: 40381-40384.
    • (2001) J Biol Chem , vol.276 , pp. 40381-40384
    • Bittner, F.1    Oreb, M.2    Mendel, R.R.3
  • 9
    • 0000736219 scopus 로고    scopus 로고
    • Comparative biochemistry of the oxidative burst produced by rose and french bean cells reveals two distinct mechanisms
    • Bolwell GP, Davies DR, Gerrish C, Auh CK, Murphy TM (1998) Comparative biochemistry of the oxidative burst produced by rose and french bean cells reveals two distinct mechanisms. Plant Physiol 116: 1379-1385.
    • (1998) Plant Physiol , vol.116 , pp. 1379-1385
    • Bolwell, G.P.1    Davies, D.R.2    Gerrish, C.3    Auh, C.K.4    Murphy, T.M.5
  • 10
    • 0001451391 scopus 로고
    • Cucumber seedling indoleacetaldehyde oxidase
    • Bower PJ, Brown HM, Purves WK (1978) Cucumber seedling indoleacetaldehyde oxidase. Plant Physiol 61: 107-110.
    • (1978) Plant Physiol , vol.61 , pp. 107-110
    • Bower, P.J.1    Brown, H.M.2    Purves, W.K.3
  • 11
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation 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
  • 12
    • 72149101510 scopus 로고    scopus 로고
    • Oxidative half-reaction of Arabidopsis thaliana sulfite oxidase: generation of superoxide by a peroxisomal enzyme
    • Byrne RS, Hänsch R, Mendel RR, Hille R (2009) Oxidative half-reaction of Arabidopsis thaliana sulfite oxidase: generation of superoxide by a peroxisomal enzyme. J Biol Chem 284: 35479-35484.
    • (2009) J Biol Chem , vol.284 , pp. 35479-35484
    • Byrne, R.S.1    Hänsch, R.2    Mendel, R.R.3    Hille, R.4
  • 13
    • 0029794132 scopus 로고    scopus 로고
    • A decade of molecular biology of retinoic acid receptors
    • Chambon P (1996) A decade of molecular biology of retinoic acid receptors. Faseb J 10: 940-954.
    • (1996) Faseb J , vol.10 , pp. 940-954
    • Chambon, P.1
  • 16
    • 17644408065 scopus 로고    scopus 로고
    • Aldehyde oxidase (AO) in the root nodules of Lupinus albus and Medicago truncatula: identification of AO in meristematic and infection zones
    • Fedorova E, Redondo FJ, Koshiba T, Pueyo JJ, de Felipe MR, Lucas MM (2005) Aldehyde oxidase (AO) in the root nodules of Lupinus albus and Medicago truncatula: identification of AO in meristematic and infection zones. Mol Plant Microbe Interact 18: 405-413.
    • (2005) Mol Plant Microbe Interact , vol.18 , pp. 405-413
    • Fedorova, E.1    Redondo, F.J.2    Koshiba, T.3    Pueyo, J.J.4    de Felipe, M.R.5    Lucas, M.M.6
  • 17
    • 0015919626 scopus 로고
    • Purification and properties of the aldehyde oxidases from hog and rabbit livers
    • Felsted RL, Chu AE, Chaykin S (1973) Purification and properties of the aldehyde oxidases from hog and rabbit livers. J Biol Chem 248: 2580-2587.
    • (1973) J Biol Chem , vol.248 , pp. 2580-2587
    • Felsted, R.L.1    Chu, A.E.2    Chaykin, S.3
  • 18
    • 0037954564 scopus 로고    scopus 로고
    • Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology
    • Garattini E, Mendel RR, Romao MJ, Wright R, Terao M (2003) Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology. Biochem J 372: 15-32.
    • (2003) Biochem J , vol.372 , pp. 15-32
    • Garattini, E.1    Mendel, R.R.2    Romao, M.J.3    Wright, R.4    Terao, M.5
  • 19
    • 42449117257 scopus 로고    scopus 로고
    • Mammalian aldehyde oxidases: genetics, evolution and biochemistry
    • Garattini E, Fratelli M, Terao M (2008) Mammalian aldehyde oxidases: genetics, evolution and biochemistry. Cell Mol Life Sci 65: 1019-1048.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1019-1048
    • Garattini, E.1    Fratelli, M.2    Terao, M.3
  • 20
    • 2442636773 scopus 로고    scopus 로고
    • Two new alleles of the abscisic aldehyde oxidase 3 gene reveal its role in abscisic acid biosynthesis in seeds
    • González-Guzmán M, Abia D, Salinas J, Serrano R, Rodríguez PL (2004) Two new alleles of the abscisic aldehyde oxidase 3 gene reveal its role in abscisic acid biosynthesis in seeds. Plant Physiol 135: 325-333.
    • (2004) Plant Physiol , vol.135 , pp. 325-333
    • González-Guzmán, M.1    Abia, D.2    Salinas, J.3    Serrano, R.4    Rodríguez, P.L.5
  • 21
    • 0023037533 scopus 로고
    • Aldehyde oxidase from rabbit liver: specificity toward purines and their analogs
    • Hall WW, Krenitsky TA (1986) Aldehyde oxidase from rabbit liver: specificity toward purines and their analogs. Arch Biochem Biophys 251: 36-46.
    • (1986) Arch Biochem Biophys , vol.251 , pp. 36-46
    • Hall, W.W.1    Krenitsky, T.A.2
  • 22
    • 33646589680 scopus 로고    scopus 로고
    • Plant sulfite oxidase as novel producer of H2O2: combination of enzyme catalysis with a subsequent non-enzymatic reaction step
    • Hänsch R, Lang C, Riebeseel E, Lindigkeit R, Gessler A, Rennenberg H, Mendel RR (2006) Plant sulfite oxidase as novel producer of H2O2: combination of enzyme catalysis with a subsequent non-enzymatic reaction step. J Biol Chem 281: 6884-6888.
    • (2006) J Biol Chem , vol.281 , pp. 6884-6888
    • Hänsch, R.1    Lang, C.2    Riebeseel, E.3    Lindigkeit, R.4    Gessler, A.5    Rennenberg, H.6    Mendel, R.R.7
  • 23
    • 0037105296 scopus 로고    scopus 로고
    • Structure and function of xanthine oxidoreductase: where are we now?
    • Harrison R (2002) Structure and function of xanthine oxidoreductase: where are we now? Free Radic Biol Med 33: 774-797.
    • (2002) Free Radic Biol Med , vol.33 , pp. 774-797
    • Harrison, R.1
  • 24
    • 1842741259 scopus 로고    scopus 로고
    • Tandem orientation of duplicated xanthine dehydrogenase genes from Arabidopsis thaliana: differential gene expression and enzyme activities
    • Hesberg C, Hansch, R, Mendel RR, Bittner F (2004) Tandem orientation of duplicated xanthine dehydrogenase genes from Arabidopsis thaliana: differential gene expression and enzyme activities. J Biol Chem 279: 13547-13554.
    • (2004) J Biol Chem , vol.279 , pp. 13547-13554
    • Hesberg, C.1    Hansch, R.2    Mendel, R.R.3    Bittner, F.4
  • 25
    • 0000273676 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • Hille R (1996) The mononuclear molybdenum enzymes. Chem Rev 96: 2757-2816.
    • (1996) Chem Rev , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 26
    • 9944248111 scopus 로고    scopus 로고
    • Molybdenum-containing hydroxylases
    • Hille R (2005) Molybdenum-containing hydroxylases. Arch Biochem Biophys 433: 107-116.
    • (2005) Arch Biochem Biophys , vol.433 , pp. 107-116
    • Hille, R.1
  • 27
    • 79952752115 scopus 로고    scopus 로고
    • Molybdenum enzymes in higher organisms
    • Hille R, Nishino T, Bittner F (2011) Molybdenum enzymes in higher organisms. Coord Chem Rev 255: 1179-1205.
    • (2011) Coord Chem Rev , vol.255 , pp. 1179-1205
    • Hille, R.1    Nishino, T.2    Bittner, F.3
  • 28
    • 0032499987 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of three molybdenum cofactor hydroxylases in Arabidopsis thaliana
    • Hoff T, Frandsen GI, Rocher A, Mundy J (1998) Biochemical and genetic characterization of three molybdenum cofactor hydroxylases in Arabidopsis thaliana. Biochim Biophys Acta 1398: 397-402.
    • (1998) Biochim Biophys Acta , vol.1398 , pp. 397-402
    • Hoff, T.1    Frandsen, G.I.2    Rocher, A.3    Mundy, J.4
  • 29
    • 0000305842 scopus 로고
    • The reduction of cytochrome c by xanthine oxidase
    • Horecker BL, Heppel LA (1949) The reduction of cytochrome c by xanthine oxidase. J Biol Chem 178: 683-690.
    • (1949) J Biol Chem , vol.178 , pp. 683-690
    • Horecker, B.L.1    Heppel, L.A.2
  • 30
    • 0033560621 scopus 로고    scopus 로고
    • Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli
    • Huang DY, Furukawa A, Ichikawa Y (1999) Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli. Arch Biochem Biophys 364: 264-272.
    • (1999) Arch Biochem Biophys , vol.364 , pp. 264-272
    • Huang, D.Y.1    Furukawa, A.2    Ichikawa, Y.3
  • 31
    • 0036894171 scopus 로고    scopus 로고
    • Water stress-induced abscisic acid accumulation triggers the increased generation of reactive oxygen species and up-regulates the activities of antioxidant enzymes in maize leaves
    • Jiang M, Zhang J (2002) Water stress-induced abscisic acid accumulation triggers the increased generation of reactive oxygen species and up-regulates the activities of antioxidant enzymes in maize leaves. J Exp Bot 53: 2401-2410.
    • (2002) J Exp Bot , vol.53 , pp. 2401-2410
    • Jiang, M.1    Zhang, J.2
  • 32
    • 0034052745 scopus 로고    scopus 로고
    • Functional expression of two Arabidopsis aldehyde oxidases in the yeast Pichia pastoris
    • Koiwai H, Akaba S, Seo M, Komano T, Koshiba T (2000) Functional expression of two Arabidopsis aldehyde oxidases in the yeast Pichia pastoris. J Biochem 127: 659-664.
    • (2000) J Biochem , vol.127 , pp. 659-664
    • Koiwai, H.1    Akaba, S.2    Seo, M.3    Komano, T.4    Koshiba, T.5
  • 33
    • 1942437592 scopus 로고    scopus 로고
    • Tissue-specific localization of an abscisic acid biosynthetic enzyme, AAO3, in Arabidopsis
    • Koiwai H, Nakaminami K, Seo M, Mitsuhashi W, Toyomasu T, Koshiba T (2004) Tissue-specific localization of an abscisic acid biosynthetic enzyme, AAO3, in Arabidopsis. Plant Physiol 134: 1697-1707.
    • (2004) Plant Physiol , vol.134 , pp. 1697-1707
    • Koiwai, H.1    Nakaminami, K.2    Seo, M.3    Mitsuhashi, W.4    Toyomasu, T.5    Koshiba, T.6
  • 34
    • 0030028266 scopus 로고    scopus 로고
    • Purification and properties of flavin- and molybdenum-containing aldehyde oxidase from coleoptiles of maize
    • Koshiba T, Saito E, Ono N, Yamamoto N, Sato M (1996) Purification and properties of flavin- and molybdenum-containing aldehyde oxidase from coleoptiles of maize. Plant Physiol 110: 781-789.
    • (1996) Plant Physiol , vol.110 , pp. 781-789
    • Koshiba, T.1    Saito, E.2    Ono, N.3    Yamamoto, N.4    Sato, M.5
  • 35
  • 36
    • 33947723940 scopus 로고    scopus 로고
    • Characterization of superoxide production from aldehyde oxidase: an important source of oxidants in biological tissues
    • Kundu TK, Hille R, Velayutham M, Zweier JL (2007) Characterization of superoxide production from aldehyde oxidase: an important source of oxidants in biological tissues. Arch Biochem Biophys 460: 113-121.
    • (2007) Arch Biochem Biophys , vol.460 , pp. 113-121
    • Kundu, T.K.1    Hille, R.2    Velayutham, M.3    Zweier, J.L.4
  • 37
    • 84859385695 scopus 로고    scopus 로고
    • Aldehyde oxidase functions as a superoxide generating NADH oxidase: an important redox regulated pathway of cellular oxygen radical formation
    • Kundu TK, Velayutham M, Zweier JL (2012) Aldehyde oxidase functions as a superoxide generating NADH oxidase: an important redox regulated pathway of cellular oxygen radical formation. Biochemistry 51: 2930-2939.
    • (2012) Biochemistry , vol.51 , pp. 2930-2939
    • Kundu, T.K.1    Velayutham, M.2    Zweier, J.L.3
  • 38
    • 0028171293 scopus 로고
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell 79: 583-593.
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.3    Lamb, C.4
  • 39
    • 0024286471 scopus 로고
    • Role of hydrogen peroxide in the cytotoxicity of the xanthine/xanthine oxidase system
    • Link EM, Riley PA (1988) Role of hydrogen peroxide in the cytotoxicity of the xanthine/xanthine oxidase system. Biochem J 249: 391-399.
    • (1988) Biochem J , vol.249 , pp. 391-399
    • Link, E.M.1    Riley, P.A.2
  • 41
    • 0030926247 scopus 로고    scopus 로고
    • Tomato flacca mutant is impaired in ABA aldehyde oxidase and xanthine dehydrogenase activities
    • Marin E, Marion-Poll A (1997) Tomato flacca mutant is impaired in ABA aldehyde oxidase and xanthine dehydrogenase activities. Plant Phys Biochem 35: 369-372.
    • (1997) Plant Phys Biochem , vol.35 , pp. 369-372
    • Marin, E.1    Marion-Poll, A.2
  • 42
    • 49749184695 scopus 로고
    • The microestimation of succinate and the extinction coefficient of cytochrome c
    • Massey V (1959) The microestimation of succinate and the extinction coefficient of cytochrome c. Biochim Biophys Acta 34: 255-256.
    • (1959) Biochim Biophys Acta , vol.34 , pp. 255-256
    • Massey, V.1
  • 43
    • 75949101148 scopus 로고
    • On the mechanism of inactivation of xanthine oxidase by cyanide
    • Massey V, Edmondson D (1970) On the mechanism of inactivation of xanthine oxidase by cyanide. J Biol Chem 244: 1682-1691.
    • (1970) J Biol Chem , vol.244 , pp. 1682-1691
    • Massey, V.1    Edmondson, D.2
  • 45
    • 0034597312 scopus 로고    scopus 로고
    • Molecular cloning and expression patterns of three putative functional aldehyde oxidase genes and isolation of two aldehyde oxidase pseudogenes in tomato
    • Min X, Okada K, Brockmann B, Koshiba T, Kamiya Y (2000) Molecular cloning and expression patterns of three putative functional aldehyde oxidase genes and isolation of two aldehyde oxidase pseudogenes in tomato. Biochim Biophys Acta 1493: 337-341.
    • (2000) Biochim Biophys Acta , vol.1493 , pp. 337-341
    • Min, X.1    Okada, K.2    Brockmann, B.3    Koshiba, T.4    Kamiya, Y.5
  • 46
    • 0028903713 scopus 로고
    • Evidence for free radical generation due to NADH oxidation by aldehyde oxidase during ethanol metabolism
    • Mira L, Maia L, Barreira L, Manso CF (1995) Evidence for free radical generation due to NADH oxidation by aldehyde oxidase during ethanol metabolism. Arch Biochem Biophys 318: 53-58.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 53-58
    • Mira, L.1    Maia, L.2    Barreira, L.3    Manso, C.F.4
  • 48
    • 0024556882 scopus 로고
    • The nicotinamide adenine dinucleotide-binding site of chicken liver xanthine dehydrogenase. Evidence for alteration of the redox potential of the flavin by NAD binding or modification of the NAD-binding site and isolation of a modified peptide
    • Nishino T, Nishino T (1989) The nicotinamide adenine dinucleotide-binding site of chicken liver xanthine dehydrogenase. Evidence for alteration of the redox potential of the flavin by NAD binding or modification of the NAD-binding site and isolation of a modified peptide. J Biol Chem 264: 5468-5473.
    • (1989) J Biol Chem , vol.264 , pp. 5468-5473
    • Nishino, T.1    Nishino, T.2
  • 49
    • 0038284875 scopus 로고    scopus 로고
    • Aldehyde oxidase isoforms and subunit composition in roots of barley as affected by ammonium and nitrate
    • Omarov R, Draeger D, Tischner R, Lips H (2003) Aldehyde oxidase isoforms and subunit composition in roots of barley as affected by ammonium and nitrate. Physiol Plant 117: 337-342.
    • (2003) Physiol Plant , vol.117 , pp. 337-342
    • Omarov, R.1    Draeger, D.2    Tischner, R.3    Lips, H.4
  • 50
    • 15644377647 scopus 로고    scopus 로고
    • TAO1, a representative of the molybdenum cofactor containing hydroxylases from tomato
    • Ori N, Eshed Y, Pinto P, Paran I, Zamir D, Fluhr R (1997) TAO1, a representative of the molybdenum cofactor containing hydroxylases from tomato. J Biol Chem 272: 1019-1025.
    • (1997) J Biol Chem , vol.272 , pp. 1019-1025
    • Ori, N.1    Eshed, Y.2    Pinto, P.3    Paran, I.4    Zamir, D.5    Fluhr, R.6
  • 52
    • 67649500149 scopus 로고    scopus 로고
    • Identification of a novel E3 ubiquitin ligase that is required for suppression of premature senescence in Arabidopsis
    • Raab S, Drechsel G, Zarepour M, Hartung W, Koshiba T, Bittner F, Hoth S (2009) Identification of a novel E3 ubiquitin ligase that is required for suppression of premature senescence in Arabidopsis. Plant J 59: 39-51.
    • (2009) Plant J , vol.59 , pp. 39-51
    • Raab, S.1    Drechsel, G.2    Zarepour, M.3    Hartung, W.4    Koshiba, T.5    Bittner, F.6    Hoth, S.7
  • 53
    • 84989742281 scopus 로고
    • Metabolism of indole-3-acetaldehyde. III. Some characteristics of the aldehyde oxidase from Avena coleoptiles
    • Rajagopal R (1971) Metabolism of indole-3-acetaldehyde. III. Some characteristics of the aldehyde oxidase from Avena coleoptiles. Physiol Plant 24: 272-281.
    • (1971) Physiol Plant , vol.24 , pp. 272-281
    • Rajagopal, R.1
  • 54
    • 0037008194 scopus 로고    scopus 로고
    • Reactive oxygen species in the elongation zone of maize leaves are necessary for leaf extension
    • Rodríguez AA, Grunberg KA, Taleisnik EL (2002) Reactive oxygen species in the elongation zone of maize leaves are necessary for leaf extension. Plant Phys 129: 1627-1632.
    • (2002) Plant Phys , vol.129 , pp. 1627-1632
    • Rodríguez, A.A.1    Grunberg, K.A.2    Taleisnik, E.L.3
  • 55
    • 0344824014 scopus 로고    scopus 로고
    • Convergent neofunctionalization by positive Darwinian selection after ancient recurrent duplications of the xanthine dehydrogenase gene
    • Rodríguez-Trelles F, Tarrío R, Ayala FJ (2003) Convergent neofunctionalization by positive Darwinian selection after ancient recurrent duplications of the xanthine dehydrogenase gene. Proc Natl Acad Sci USA 100: 13413-13417.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13413-13417
    • Rodríguez-Trelles, F.1    Tarrío, R.2    Ayala, F.J.3
  • 56
    • 23144451444 scopus 로고    scopus 로고
    • Oxidative stress: molecular perception and transduction of signals triggering antioxidant gene defenses
    • Scandalios JG (2005) Oxidative stress: molecular perception and transduction of signals triggering antioxidant gene defenses. Braz J Med Biol Res 38: 995-1014.
    • (2005) Braz J Med Biol Res , vol.38 , pp. 995-1014
    • Scandalios, J.G.1
  • 57
    • 0035030687 scopus 로고    scopus 로고
    • Release of reactive oxygen intermediates (superoxide radicals, hydrogen peroxide, and hydroxyl radicals) and peroxidase in germinating radish seeds controlled by light, gibberellin, and abscisic acid
    • Schopfer P, Plachy C, Frahry G (2001) Release of reactive oxygen intermediates (superoxide radicals, hydrogen peroxide, and hydroxyl radicals) and peroxidase in germinating radish seeds controlled by light, gibberellin, and abscisic acid. Plant Physiol 125: 1591-1602.
    • (2001) Plant Physiol , vol.125 , pp. 1591-1602
    • Schopfer, P.1    Plachy, C.2    Frahry, G.3
  • 59
  • 60
    • 0031992097 scopus 로고    scopus 로고
    • Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana
    • Seo M, Akaba S, Oritani T, Delarue M, Bellini C, Caboche M, Koshiba T (1998) Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana. Plant Physiol 116: 687-693.
    • (1998) Plant Physiol , vol.116 , pp. 687-693
    • Seo, M.1    Akaba, S.2    Oritani, T.3    Delarue, M.4    Bellini, C.5    Caboche, M.6    Koshiba, T.7
  • 63
    • 11144345842 scopus 로고    scopus 로고
    • Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene family revealed a major role of AAO3 in ABA biosynthesis in seeds
    • Seo M, Aoki H, Koiwai H, Kamiya Y, Nambara E, Koshiba T (2004) Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene family revealed a major role of AAO3 in ABA biosynthesis in seeds. Plant Cell Physiol 45: 1694-1703.
    • (2004) Plant Cell Physiol , vol.45 , pp. 1694-1703
    • Seo, M.1    Aoki, H.2    Koiwai, H.3    Kamiya, Y.4    Nambara, E.5    Koshiba, T.6
  • 64
    • 0025324230 scopus 로고
    • The role of aldehyde oxidase in ethanol-induced hepatic lipid peroxidation in the rat
    • Shaw S, Jayatilleke E (1990) The role of aldehyde oxidase in ethanol-induced hepatic lipid peroxidation in the rat. Biochem J 268: 579-583.
    • (1990) Biochem J , vol.268 , pp. 579-583
    • Shaw, S.1    Jayatilleke, E.2
  • 66
    • 0000774435 scopus 로고
    • Abscisic aldehyde is an intermediate in the enzymatic conversion of xanthoxin to abscisic acid in Phaseolus vulgaris L. leaves
    • Sindhu RK, Griffin DH, Walton DC (1990) Abscisic aldehyde is an intermediate in the enzymatic conversion of xanthoxin to abscisic acid in Phaseolus vulgaris L. leaves. Plant Physiol 93: 689-694.
    • (1990) Plant Physiol , vol.93 , pp. 689-694
    • Sindhu, R.K.1    Griffin, D.H.2    Walton, D.C.3
  • 67
    • 2442626687 scopus 로고    scopus 로고
    • Xanthine dehydrogenase and aldehyde oxidase impact plant hormone homeostasis and affect fruit size in 'Hass' avocado
    • Taylor NJ, Cowan AK (2004) Xanthine dehydrogenase and aldehyde oxidase impact plant hormone homeostasis and affect fruit size in 'Hass' avocado. J Plant Res 117: 121-130.
    • (2004) J Plant Res , vol.117 , pp. 121-130
    • Taylor, N.J.1    Cowan, A.K.2
  • 68
    • 0035824605 scopus 로고    scopus 로고
    • Purification of the aldehyde oxidase homolog 1 (AOH1) protein and cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identification of a novel molybdo-flavoprotein gene cluster on mouse chromosome 1
    • Terao M, Kurosaki M, Marini M, Vanoni MA, Saltini G, Bonetto V, Bastone A, Federico C, Saccone S, Fanelli R, Salmona M, Garattini E (2001) Purification of the aldehyde oxidase homolog 1 (AOH1) protein and cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identification of a novel molybdo-flavoprotein gene cluster on mouse chromosome 1. J Biol Chem 276: 46347-46363.
    • (2001) J Biol Chem , vol.276 , pp. 46347-46363
    • Terao, M.1    Kurosaki, M.2    Marini, M.3    Vanoni, M.A.4    Saltini, G.5    Bonetto, V.6    Bastone, A.7    Federico, C.8    Saccone, S.9    Fanelli, R.10    Salmona, M.11    Garattini, E.12
  • 69
    • 0029155859 scopus 로고
    • Properties of rabbit liver aldehyde oxidase and the relationship of the enzyme to xanthine oxidase and dehydrogenase
    • Turner NA, Doyle WA, Ventom AM, Bray RC (1995) Properties of rabbit liver aldehyde oxidase and the relationship of the enzyme to xanthine oxidase and dehydrogenase. Eur J Biochem 232: 646-657.
    • (1995) Eur J Biochem , vol.232 , pp. 646-657
    • Turner, N.A.1    Doyle, W.A.2    Ventom, A.M.3    Bray, R.C.4
  • 70
    • 80052419041 scopus 로고    scopus 로고
    • Peroxynitrite formation and function in plants
    • Vandelle E, Delledonne M (2011) Peroxynitrite formation and function in plants. Plant Sci 181: 534-539.
    • (2011) Plant Sci , vol.181 , pp. 534-539
    • Vandelle, E.1    Delledonne, M.2
  • 71
    • 18044390885 scopus 로고    scopus 로고
    • Before and beyond ABA: upstream sensing and internal signals that determine ABA accumulation and response under abiotic stress
    • Verslues PE, Zhu JK (2005) Before and beyond ABA: upstream sensing and internal signals that determine ABA accumulation and response under abiotic stress. Biochem Soc Trans 33: 375-379.
    • (2005) Biochem Soc Trans , vol.33 , pp. 375-379
    • Verslues, P.E.1    Zhu, J.K.2
  • 72
    • 43449092870 scopus 로고    scopus 로고
    • Guard-cell signalling for hydrogen peroxide and abscisic acid
    • Wang P, Song CP (2008) Guard-cell signalling for hydrogen peroxide and abscisic acid. New Phytol 178: 703-718.
    • (2008) New Phytol , vol.178 , pp. 703-718
    • Wang, P.1    Song, C.P.2
  • 73
    • 0031006120 scopus 로고    scopus 로고
    • Simple methods for the preparation of enantiomerically pure abscisic acid (ABA) analogues from (S)-(+)-ABA
    • Ward DE, Gai Y (1997) Simple methods for the preparation of enantiomerically pure abscisic acid (ABA) analogues from (S)-(+)-ABA. Synth Commun 24: 2133-2142.
    • (1997) Synth Commun , vol.24 , pp. 2133-2142
    • Ward, D.E.1    Gai, Y.2
  • 75
    • 0141787888 scopus 로고    scopus 로고
    • Regulation of abscisic acid biosynthesis
    • Xiong L, Zhu JK (2003) Regulation of abscisic acid biosynthesis. Plant Physiol 133: 29-36.
    • (2003) Plant Physiol , vol.133 , pp. 29-36
    • Xiong, L.1    Zhu, J.K.2
  • 76
    • 21244461224 scopus 로고    scopus 로고
    • The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have distinct reactive oxygen species signatures and are induced by drought and abscisic acid
    • Yesbergenova Z, Yang G, Oron E, Soffer D, Flur R, Sagi M (2005) The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have distinct reactive oxygen species signatures and are induced by drought and abscisic acid. Plant J 42: 862-876.
    • (2005) Plant J , vol.42 , pp. 862-876
    • Yesbergenova, Z.1    Yang, G.2    Oron, E.3    Soffer, D.4    Flur, R.5    Sagi, M.6
  • 77
    • 0022344589 scopus 로고
    • Guinea pig liver aldehyde oxidase as a sulfoxide reductase: its purification and characterization
    • Yoshihara S, Tatsumi K (1985) Guinea pig liver aldehyde oxidase as a sulfoxide reductase: its purification and characterization. Arch Biochem Biophys 242: 213-224.
    • (1985) Arch Biochem Biophys , vol.242 , pp. 213-224
    • Yoshihara, S.1    Tatsumi, K.2
  • 78
    • 75949096163 scopus 로고    scopus 로고
    • Xanthine dehydrogenase AtXDH1 from Arabidopsis thaliana is a potent producer of superoxide anions via its NADH oxidase activity
    • Zarepour M, Kaspari K, Stagge S, Rethmeier R, Mendel RR, Bittner F (2010) Xanthine dehydrogenase AtXDH1 from Arabidopsis thaliana is a potent producer of superoxide anions via its NADH oxidase activity. Plant Mol Biol 72: 301-310.
    • (2010) Plant Mol Biol , vol.72 , pp. 301-310
    • Zarepour, M.1    Kaspari, K.2    Stagge, S.3    Rethmeier, R.4    Mendel, R.R.5    Bittner, F.6
  • 79
    • 0034945810 scopus 로고    scopus 로고
    • Transport and accumulation rates of abscisic acid and aldehyde oxidase activity in Pisum sativum L. in response to suboptimal growth conditions
    • Zdunek E, Lips SH (2001) Transport and accumulation rates of abscisic acid and aldehyde oxidase activity in Pisum sativum L. in response to suboptimal growth conditions. J Exp Bot 52: 1269-1276.
    • (2001) J Exp Bot , vol.52 , pp. 1269-1276
    • Zdunek, E.1    Lips, S.H.2
  • 80
    • 38549135863 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression analysis of three aldehyde oxidase genes from Pisum sativum L
    • Zdunek-Zastocka E (2008) Molecular cloning, characterization and expression analysis of three aldehyde oxidase genes from Pisum sativum L. Plant Physiol Biochem 46: 19-28.
    • (2008) Plant Physiol Biochem , vol.46 , pp. 19-28
    • Zdunek-Zastocka, E.1
  • 81
    • 2942528831 scopus 로고    scopus 로고
    • Activity and protein level of AO isoforms in pea plants (Pisum sativum L.) during vegetative development and in response to stress conditions
    • Zdunek-Zastocka E, Omarov RT, Koshiba T, Lips HS (2004) Activity and protein level of AO isoforms in pea plants (Pisum sativum L.) during vegetative development and in response to stress conditions. J Exp Bot 55: 1361-1369.
    • (2004) J Exp Bot , vol.55 , pp. 1361-1369
    • Zdunek-Zastocka, E.1    Omarov, R.T.2    Koshiba, T.3    Lips, H.S.4
  • 82
    • 0034872870 scopus 로고    scopus 로고
    • Hydrogen peroxide is involved in abscisic acid-induced stomatal closure in Vicia faba
    • Zhang X, Zhang L, Dong F, Gao J, Galbraith DW, Song CP (2001) Hydrogen peroxide is involved in abscisic acid-induced stomatal closure in Vicia faba. Plant Physiol 126: 1438-1448.
    • (2001) Plant Physiol , vol.126 , pp. 1438-1448
    • Zhang, X.1    Zhang, L.2    Dong, F.3    Gao, J.4    Galbraith, D.W.5    Song, C.P.6
  • 83
    • 33646567818 scopus 로고    scopus 로고
    • Senescence-specific regulation of catalases in Arabidopsis thaliana (L.) Heynh
    • Zimmermann P, Heinlein C, Orendi G, Zentgraf U (2006) Senescence-specific regulation of catalases in Arabidopsis thaliana (L.) Heynh. Plant Cell Environ 29: 1049-1060.
    • (2006) Plant Cell Environ , vol.29 , pp. 1049-1060
    • Zimmermann, P.1    Heinlein, C.2    Orendi, G.3    Zentgraf, U.4


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