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Volumn 191, Issue 1, 2011, Pages 234-250

Ascorbate peroxidase-related (APx-R) is a new heme-containing protein functionally associated with ascorbate peroxidase but evolutionarily divergent

Author keywords

Antioxidant; Ascorbate peroxidase; H2O2 scavenging; Heme peroxidase; Peroxidase; Redox; Single copy gene

Indexed keywords

ANTIOXIDANT; ASCORBATE PEROXIDASE; MESSENGER RNA; PEROXIDASE; VEGETABLE PROTEIN;

EID: 79957919995     PISSN: 0028646X     EISSN: 14698137     Source Type: Journal    
DOI: 10.1111/j.1469-8137.2011.03659.x     Document Type: Article
Times cited : (60)

References (48)
  • 3
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantification of microgram quantities of protein utilizing principle of protein-dye binding
    • Bradford MM. 1976. Rapid and sensitive method for quantification of microgram quantities of protein utilizing principle of protein-dye binding. Analytical Biochemistry 72: 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 84989748915 scopus 로고
    • Effect of aluminum on lipid-peroxidation, superoxide-dismutase, catalase and peroxidase-activities in root-tips of soybean (Glycine max)
    • Cakmak I, Horst WJ. 1991. Effect of aluminum on lipid-peroxidation, superoxide-dismutase, catalase and peroxidase-activities in root-tips of soybean (Glycine max). Physiologia Plantarum 83: 463-468.
    • (1991) Physiologia Plantarum , vol.83 , pp. 463-468
    • Cakmak, I.1    Horst, W.J.2
  • 5
    • 33747879976 scopus 로고    scopus 로고
    • Hydrogen peroxide concentrations in leaves under natural conditions
    • Cheeseman JM. 2006. Hydrogen peroxide concentrations in leaves under natural conditions. Journal of Experimental Botany 57: 2435-2444.
    • (2006) Journal of Experimental Botany , vol.57 , pp. 2435-2444
    • Cheeseman, J.M.1
  • 6
    • 33745314723 scopus 로고
    • Ascorbate peroxidase in tea leaves - occurrence of 2 isozymes and the differences in their enzymatic and molecular properties
    • Chen GX, Asada K. 1989. Ascorbate peroxidase in tea leaves - occurrence of 2 isozymes and the differences in their enzymatic and molecular properties. Plant and Cell Physiology 30: 987-998.
    • (1989) Plant and Cell Physiology , vol.30 , pp. 987-998
    • Chen, G.X.1    Asada, K.2
  • 7
    • 33748347060 scopus 로고    scopus 로고
    • A highly efficient transient protoplast system for analyzing defence gene expression and protein-protein interactions in rice
    • Chen SB, Tao LZ, Zeng LR, Vega-Sanchez ME, Umemura K, Wang GL. 2006. A highly efficient transient protoplast system for analyzing defence gene expression and protein-protein interactions in rice. Molecular Plant Pathology 7: 417-427.
    • (2006) Molecular Plant Pathology , vol.7 , pp. 417-427
    • Chen, S.B.1    Tao, L.Z.2    Zeng, L.R.3    Vega-Sanchez, M.E.4    Umemura, K.5    Wang, G.L.6
  • 8
    • 0033708105 scopus 로고    scopus 로고
    • Molecular evolution of the myeloperoxidase family
    • Daiyasu H, Toh H. 2000. Molecular evolution of the myeloperoxidase family. Journal of Molecular Evolution 51: 433-445.
    • (2000) Journal of Molecular Evolution , vol.51 , pp. 433-445
    • Daiyasu, H.1    Toh, H.2
  • 9
    • 33846823909 scopus 로고
    • Particle mesh Ewald - an N Log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L. 1993. Particle mesh Ewald - an N Log(N) method for Ewald sums in large systems. Journal of Chemical Physics 98: 10089-10092.
    • (1993) Journal of Chemical Physics , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 11
    • 70349334103 scopus 로고    scopus 로고
    • Phylogenetic inference under varying proportions of indel-induced alignment gaps
    • doi: .
    • Dwivedi B, Gadagkar SR. 2009. Phylogenetic inference under varying proportions of indel-induced alignment gaps. BMC Evolutionary Biology. doi: .
    • (2009) BMC Evolutionary Biology
    • Dwivedi, B.1    Gadagkar, S.R.2
  • 12
    • 0002668438 scopus 로고
    • Soluble ascorbate peroxidase from potato-tubers
    • Elia MR, Borraccino G, Dipierro S. 1992. Soluble ascorbate peroxidase from potato-tubers. Plant Science 85: 17-21.
    • (1992) Plant Science , vol.85 , pp. 17-21
    • Elia, M.R.1    Borraccino, G.2    Dipierro, S.3
  • 13
    • 0347994106 scopus 로고    scopus 로고
    • Refinement of homology-based protein structures by molecular dynamics simulation techniques
    • Fan H, Mark AE. 2004. Refinement of homology-based protein structures by molecular dynamics simulation techniques. Protein Science 13: 211-220.
    • (2004) Protein Science , vol.13 , pp. 211-220
    • Fan, H.1    Mark, A.E.2
  • 14
    • 0003814339 scopus 로고    scopus 로고
    • Composição e ph de soluções nutritivas para estudos fisiológicos e de seleção de plantas em condições nutricionais adversas
    • Furlani AMC, Furlani PR. 1998. Composição e ph de soluções nutritivas para estudos fisiológicos e de seleção de plantas em condições nutricionais adversas, Technical bulletin Instituto Agronomico de Campinas 121: 1-34.
    • (1998) Technical bulletin Instituto Agronomico de Campinas , vol.121 , pp. 1-34
    • Furlani, A.M.C.1    Furlani, P.R.2
  • 16
    • 0033543516 scopus 로고    scopus 로고
    • Hydroperoxide assay with the ferric-xylenol orange complex
    • Gay C, Collins J, Gebicki JM. 1999. Hydroperoxide assay with the ferric-xylenol orange complex. Analytical Biochemistry 273: 149-155.
    • (1999) Analytical Biochemistry , vol.273 , pp. 149-155
    • Gay, C.1    Collins, J.2    Gebicki, J.M.3
  • 17
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • Guindon S, Gascuel O. 2003. A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Systematic Biology 52: 696-704.
    • (2003) Systematic Biology , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 19
    • 0025188055 scopus 로고
    • Structural homology among the peroxidase enzyme family revealed by hydrophobic cluster analysis
    • Henrissat B, Saloheimo M, Lavaitte S, Knowles JKC. 1990. Structural homology among the peroxidase enzyme family revealed by hydrophobic cluster analysis. Proteins 8: 215-217.
    • (1990) Proteins , vol.8 , pp. 215-217
    • Henrissat, B.1    Saloheimo, M.2    Lavaitte, S.3    Knowles, J.K.C.4
  • 22
    • 0001015272 scopus 로고
    • Cytosolic ascorbate peroxidase in seedlings and leaves of maize (Zea mays)
    • Koshiba T. 1993. Cytosolic ascorbate peroxidase in seedlings and leaves of maize (Zea mays). Plant and Cell Physiology 34: 713-721.
    • (1993) Plant and Cell Physiology , vol.34 , pp. 713-721
    • Koshiba, T.1
  • 26
    • 2342577446 scopus 로고    scopus 로고
    • Simple RNAi vectors for stable and transient suppression of gene function in rice
    • Miki D, Shimamoto K. 2004. Simple RNAi vectors for stable and transient suppression of gene function in rice. Plant and Cell Physiology 45: 490-495.
    • (2004) Plant and Cell Physiology , vol.45 , pp. 490-495
    • Miki, D.1    Shimamoto, K.2
  • 27
    • 0000121196 scopus 로고
    • Purification and characterization of pea cytosolic ascorbate peroxidase
    • Mittler R, Zilinskas BA. 1991. Purification and characterization of pea cytosolic ascorbate peroxidase. Plant Physiology 97: 962-968.
    • (1991) Plant Physiology , vol.97 , pp. 962-968
    • Mittler, R.1    Zilinskas, B.A.2
  • 28
  • 30
    • 34247111250 scopus 로고    scopus 로고
    • Prokaryotic origins of the non-animal peroxidase superfamily and organelle-mediated transmission to eukaryotes
    • Passardi F, Bakalovic N, Teixeira FK, Margis-Pinheiro M, Penel C, Dunand C. 2007a. Prokaryotic origins of the non-animal peroxidase superfamily and organelle-mediated transmission to eukaryotes. Genomics 89: 567-579.
    • (2007) Genomics , vol.89 , pp. 567-579
    • Passardi, F.1    Bakalovic, N.2    Teixeira, F.K.3    Margis-Pinheiro, M.4    Penel, C.5    Dunand, C.6
  • 31
    • 23644437138 scopus 로고    scopus 로고
    • Peroxidases have more functions than a swiss army knife
    • Passardi F, Cosio C, Penel C, Dunand C. 2005. Peroxidases have more functions than a swiss army knife. Plant Cell Reports 24: 255-265.
    • (2005) Plant Cell Reports , vol.24 , pp. 255-265
    • Passardi, F.1    Cosio, C.2    Penel, C.3    Dunand, C.4
  • 33
    • 0028335867 scopus 로고
    • Characterization and crystallization of recombinant pea cytosolic ascorbate peroxidase
    • Patterson WR, Poulos TL. 1994. Characterization and crystallization of recombinant pea cytosolic ascorbate peroxidase. Journal of Biological Chemistry 269: 17020-17024.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 17020-17024
    • Patterson, W.R.1    Poulos, T.L.2
  • 36
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A, Blundell TL. 1993. Comparative protein modeling by satisfaction of spatial restraints. Journal of Molecular Biology 234: 779-815.
    • (1993) Journal of Molecular Biology , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 38
    • 34547781750 scopus 로고    scopus 로고
    • Mega4: molecular evolutionary genetics analysis (mega) software version 4.0
    • Tamura K, Dudley J, Nei M, Kumar S. 2007. Mega4: molecular evolutionary genetics analysis (mega) software version 4.0. Molecular Biology and Evolution 24: 1596-1599.
    • (2007) Molecular Biology and Evolution , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 39
    • 0036845757 scopus 로고    scopus 로고
    • Plant Rac-like GTPases are activated by auxin and mediate auxin-responsive gene expression
    • Tao LZ, Cheung AY, Wu HM. 2002. Plant Rac-like GTPases are activated by auxin and mediate auxin-responsive gene expression. Plant Cell 14: 2745-2760.
    • (2002) Plant Cell , vol.14 , pp. 2745-2760
    • Tao, L.Z.1    Cheung, A.Y.2    Wu, H.M.3
  • 40
    • 33745355254 scopus 로고    scopus 로고
    • Rice ascorbate peroxidase gene family encodes functionally diverse isoforms localized in different subcellular compartments
    • Teixeira FK, Menezes-Benavente L, Galvao VC, Margis R, Margis-Pinheiro M. 2006. Rice ascorbate peroxidase gene family encodes functionally diverse isoforms localized in different subcellular compartments. Planta 224: 300-314.
    • (2006) Planta , vol.224 , pp. 300-314
    • Teixeira, F.K.1    Menezes-Benavente, L.2    Galvao, V.C.3    Margis, R.4    Margis-Pinheiro, M.5
  • 41
    • 11944274967 scopus 로고    scopus 로고
    • Analysis of the molecular evolutionary history of the ascorbate peroxidase gene family: inferences from the rice genome
    • Teixeira FK, Menezes-Benavente L, Margis R, Margis-Pinheiro M. 2004. Analysis of the molecular evolutionary history of the ascorbate peroxidase gene family: inferences from the rice genome. Journal of Molecular Evolution 59: 761-770.
    • (2004) Journal of Molecular Evolution , vol.59 , pp. 761-770
    • Teixeira, F.K.1    Menezes-Benavente, L.2    Margis, R.3    Margis-Pinheiro, M.4
  • 42
    • 0027968068 scopus 로고
    • Clustal w: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. 1994. Clustal w: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Research 22: 4673-4680.
    • (1994) Nucleic Acids Research , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 46
    • 60249083823 scopus 로고    scopus 로고
    • Autophagy plays a role in chloroplast degradation during senescence in individually darkened leaves
    • Wada S, Ishida H, Izumi M, Yoshimoto K, Ohsumi Y, Mae T, Makino A. 2009. Autophagy plays a role in chloroplast degradation during senescence in individually darkened leaves. Plant Physiology 149: 885-893.
    • (2009) Plant Physiology , vol.149 , pp. 885-893
    • Wada, S.1    Ishida, H.2    Izumi, M.3    Yoshimoto, K.4    Ohsumi, Y.5    Mae, T.6    Makino, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.