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2013
S. Sheoran, Pandey, B., Sharma, P., Narwal, S., Singh, R., Sharma, I., and Chatrath, R., In silico comparative analysis and expression profile of antioxidant proteins in plants, vol. 12, pp. 537-551, 2013.
Andriotis VM and Rathjen JP (2006). The Pto kinase of tomato, which regulates plant immunity, is repressed by its myristoylated N terminus. J. Biol. Chem. 281: 26578-26586. http://dx.doi.org/10.1074/jbc.M603197200 PMid:16785235   Asada K (2006). Production and scavenging of reactive oxygen species in chloroplasts and their functions. Plant Physiol. 141: 391-396. http://dx.doi.org/10.1104/pp.106.082040 PMid:16760493 PMCid:1475469   Batistic O, Sorek N, Schultke S, Yalovsky S, et al. (2008). Dual fatty acyl modification determines the localization and plasma membrane targeting of CBL/CIPK Ca2+ signaling complexes in Arabidopsis. Plant Cell 20: 1346-1362. http://dx.doi.org/10.1105/tpc.108.058123 PMid:18502848 PMCid:2438452   Benetka W, Mehlmer N, Maurer-Stroh S, Sammer M, et al. (2008). Experimental testing of predicted myristoylation targets involved in asymmetric cell division and calcium-dependent signalling. Cell Cycle 7: 3709-3719. http://dx.doi.org/10.4161/cc.7.23.7176 PMid:19029837   Bowler C, Van Montagu M and lnzé D (1992). Superoxide dismutase and stress tolerance. Annu. Rev. Plant Physiol. Plant Mol. Biol. 43: 83-116. http://dx.doi.org/10.1146/annurev.pp.43.060192.000503   Bowler C, Neuhaus G, Yamagata H and Chua NH (1994). Cyclic GMP and calcium mediate phytochrome phototransduction. Cell 77: 73-81. http://dx.doi.org/10.1016/0092-8674(94)90236-4   Chothia C and Lesk AM (1986). The relation between the divergence of sequence and structure in proteins. EMBO J. 5: 823-826. PMid:3709526 PMCid:1166865   Dat J, Vandenabeele S, Vranová E, Van Montagu M, et al. (2000). Dual action of the active oxygen species during plant stress responses. Cell Mol. Life Sci. 57: 779-795. http://dx.doi.org/10.1007/s000180050041 PMid:10892343   del Río LA, Sandalio LM, Yanez J and Gomez M (1985). Induction of a manganese-containing superoxide dismutase in leaves of Pisum sativum L. by high nutrient levels of zinc and manganese. J. Inorg. Biochem. 24: 25-34. http://dx.doi.org/10.1016/0162-0134(85)85011-X   Delseny M, Cooke R, Raynal M and Grellet F (1997). The Arabidopsis thaliana cDNA sequencing projects. FEBS Lett. 403: 221-224. http://dx.doi.org/10.1016/S0014-5793(97)00075-6   Edgar RC (2004). MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32: 1792-1797. http://dx.doi.org/10.1093/nar/gkh340 PMid:15034147 PMCid:390337   Gratao PL, Gomes Junior RA, Delite FS, Lea PJ, et al. (2006). Cadmium Toxicity and Tolerance in Plants. Alpha Sciences International Ltd., Oxford.   Hanks SK (2003). Genomic analysis of the eukaryotic protein kinase superfamily: a perspective. Genome Biol. 4: 111. http://dx.doi.org/10.1186/gb-2003-4-5-111 PMid:12734000 PMCid:156577   Hidalgo P, Garreton V, Berrios CG, Ojeda H, et al. (2001). A nuclear casein kinase 2 activity is involved in early events of transcriptional activation induced by salicylic acid in tobacco. Plant Physiol. 125: 396-405. http://dx.doi.org/10.1104/pp.125.1.396 PMid:11154347 PMCid:61020   Ishikawa T, Yoshimura K, Sakai K, Tamoi M, et al. (1998). Molecular characterization and physiological role of a glyoxysome-bound ascorbate peroxidase from spinach. Plant Cell Physiol. 39: 23-34. http://dx.doi.org/10.1093/oxfordjournals.pcp.a029285 PMid:9516999   Ishitani M, Liu J, Halfter U, Kim CS, et al. (2000). SOS3 function in plant salt tolerance requires N-myristoylation and calcium binding. Plant Cell 12: 1667-1678. PMid:11006339 PMCid:149077   Kanematsu S and Asada K (1990). Characteristic amino acid sequences of chloroplast and cytosol isozymes of CuZn- Superoxide dismutase in spinach, rice and horsetail. Plant Cell Physiol. 31: 99-112.   Katyshev AI, Konstantinov I and Kobzev VF (2006). Characterization of Mn- and Cu/Zn-containing superoxide dismutase gene transcripts in Larix gmelinii. Mol. Biol. 40: 372-374. http://dx.doi.org/10.1134/S0026893306020208   Kliebenstein DJ, Monde RA and Last RL (1998). Superoxide dismutase in Arabidopsis: an eclectic enzyme family with disparate regulation and protein localization. Plant Physiol. 118: 637-650. http://dx.doi.org/10.1104/pp.118.2.637 PMid:9765550 PMCid:34840   La Du BN and Zannoni VG (1955). The tyrosine oxidation system of liver. II. Oxidation of p-hydroxyphenylpyruvic acid to homogentisic acid. J. Biol. Chem. 217: 777-787. PMid:13271439   Miyake C, Cao WH and Asada K (1993). Purification and molecular properties of the thylakoid-bound ascorbate peroxidase in spinach chloroplast. Plant Cell Physiol. 34: 881-889.   Moorhead GB, De Wever V, Templeton G and Kerk D (2009). Evolution of protein phosphatases in plants and animals. Biochem J. 417: 401-409. http://dx.doi.org/10.1042/BJ20081986 PMid:19099538   Murao K, Takamiya M, Ono K, Takano H, et al. (2004). Copper deficiency induced expression of Fe-superoxide dismutase gene in Matteuccia struthiopteris. Plant Physiol. Biochem. 42: 143-148. http://dx.doi.org/10.1016/j.plaphy.2003.11.004 PMid:15283130   Noctor G, Veljovic-Jovanovic S and Foyer CH (2000). Peroxide processing in photosynthesis: antioxidant coupling and redox signalling. Philos. Trans. R. Soc. Lond. B Biol. Sci. 355: 1465-1475. http://dx.doi.org/10.1098/rstb.2000.0707 PMid:11128000 PMCid:1692876   Notredame C, Higgins DG and Heringa J (2000). T-Coffee: A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302: 205-217. http://dx.doi.org/10.1006/jmbi.2000.4042 PMid:10964570   Pei J, Kim BH and Grishin NV (2008). PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic Acids Res. 36: 2295-2300. http://dx.doi.org/10.1093/nar/gkn072 PMid:18287115 PMCid:2367709   Rayapureddi JP, Kattamuri C, Chan FH and Hegde RS (2005). Characterization of a plant, tyrosine-specific phosphatase of the aspartyl class. Biochemistry 44: 751-758. http://dx.doi.org/10.1021/bi0481794 PMid:15641802   Resh MD (1999). Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451: 1-16. http://dx.doi.org/10.1016/S0167-4889(99)00075-0   Riera M, Peracchia G and Pages M (2001). Distinctive features of plant protein kinase CK2. Mol. Cell Biochem. 227: 119-127. http://dx.doi.org/10.1023/A:1013141713277 PMid:11827162   Saitou N and Nei M (1987). The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4: 406-425. PMid:3447015   Scandalios JG, Guan L and Polidoros AN (1997). Catalases in Plants: Gene Structure, Properties, Regulation, and Expression. In: Oxidative Stress and the Molecular Biology of Antioxidant Defenses (Scandalios JG, ed.). Cold Spring Harbor Laboratory, New York, 343-406.   Shigeoka S, Ishikawa T, Tamoi M, Miyagawa Y, et al. (2002). Regulation and function of ascorbate peroxidase isozymes. J. Exp. Bot. 53: 1305-1319. http://dx.doi.org/10.1093/jexbot/53.372.1305 PMid:11997377   Spiteri A, Viratelle OM, Raymond P, Rancillac M, et al. (1989). Artifactual origins of cyclic AMP in higher plant tissues. Plant Physiol. 91: 624-628. http://dx.doi.org/10.1104/pp.91.2.624 PMid:16667078 PMCid:1062046   Stone JM and Walker JC (1995). Plant protein kinase families and signal transduction. Plant Physiol. 108: 451-457. http://dx.doi.org/10.1104/pp.108.2.451 PMid:7610156 PMCid:157363   Takahashi Y, Shomura A, Sasaki T and Yano M (2001). Hd6, a rice quantitative trait locus involved in photoperiod sensitivity, encodes the alpha subunit of protein kinase CK2. Proc. Natl. Acad. Sci. U. S. A. 98: 7922-7927. http://dx.doi.org/10.1073/pnas.111136798 PMid:11416158 PMCid:35444   Tamura K, Dudley J, Nei M and Kumar S (2007). MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24: 1596-1599. http://dx.doi.org/10.1093/molbev/msm092 PMid:17488738   Teixeira FK, Menezes-Benavente L, Margis R and Margis-Pinheiro M (2004). Analysis of the molecular evolutionary history of the ascorbate peroxidase gene family: inferences from the rice genome. J. Mol. Evol. 59: 761-770. http://dx.doi.org/10.1007/s00239-004-2666-z PMid:15599508   Van Camp W, Inzé D and Van Montagu M (1997). The regulation and function of tobacco superoxide dismutases. Free Radic. Biol. Med. 23: 515-520. http://dx.doi.org/10.1016/S0891-5849(97)00112-3   Willekens H, Chamnongpol S, Davey M, Schraudner M, et al. (1997). Catalase is a sink for H2O2 and is indispensable for stress defence in C3 plants. EMBO J. 16: 4806-4816. http://dx.doi.org/10.1093/emboj/16.16.4806 PMid:9305623 PMCid:1170116   Wu G, Wilen RW, Robertson AJ and Gusta LV (1996). The electronic plant genes register PGR 96-126 molecular cloning of two wheat (Triticum aestivum) genes (Accession Nos. U69536 (SOD11) and U69632 (SOD12) encoding chloroplast Cu/Zn superoxide dismutases. Plant Physiol. 112: 1736.   Wu G, Robertson AJ, Wilen RW and Gusta LV (1997). Isolation and characterisation of two cDNAs (Accession Nos. U72212 and U73172) encoding mitochondrial manganese superoxide dismutases in wheat. Plant Physiol. 113: 664.   Zamocky M, Jakopitsch C, Furtmuller PG, Dunand C, et al. (2008). The peroxidase-cyclooxygenase superfamily: Reconstructed evolution of critical enzymes of the innate immune system. Proteins 72: 589-605. http://dx.doi.org/10.1002/prot.21950 PMid:18247411   Zvelebil MJ and Baum JO (2008). Understanding Bioinformatics. Garland Science, Taylor & Francis Group, New York and London.
T. - Y. Seng, Singh, R., Faridah, Q. Z., Tan, S. - G., and Alwee, S. S. R. S., Recycling of superfine resolution agarose gel, vol. 12, pp. 2360-2367, 2013.