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References
Cramer CL, Edwards K, Dron M, Liang X, Dildine SL, Bolwell GP, Dixon RA, Lamb CJ, Schuch W: Phenylalanine ammonia-lyase gene organization and structure. Plant Mol Biol 12: 367–383 (1989).
Dangle JL, Hauffe KD, Lipphardt S, Hahlbrock K, Scheel D: Parsley protoplasts retain differential responsiveness to u.v. light and fungal elicitor. EMBO J 6: 2551–2556 (1987).
Dixon RA, Dey PM, Lamb CJ: Phytoalexins; enzymology and molecular biology. Adv Ezymol Relat Areas Mol Biol 55: 1–135 (1983).
Edwards K, Cramer CL, Bolwell GP, Dixon RA, Schuch W, Lamb CJ: Rapid transient induction of phenylalamine ammonia-lyase mRNA in elicitor-treated bean cells. Proc Natl Acad Sci USA 82: 6731–6735 (1985).
Hahlbrock K, Scheel D: Physiology and molecular biology of phenylpropanoid metabolism. Annu Rev Plant Physiol Plant Mol Biol 40: 347–369 (1989).
Jones DH: Phenylalanine ammonia-lyase: Regulation of its induction, and its role in plant development. Phytochemistry 23: 1349–1359 (1984).
Joshi CP: Putative polyadenylation signals in nuclear genes of higher plants: A compilation and analysis. Nucl Acids Res 15: 9627–9640 (1987).
Lamb CJ, Lawton MA, Dron M, Dixon RA: Signals and transduction mechanisms for activation of plant defenses against microbial attack. Cell 56: 215–224 (1989).
Liang X, Dron M, Cramer CL, Dixon RA, Lamb CJ: Differential regulation of phenylalanine ammonia-lyase genes during plant development and environmental cues. J Biol Chem 264: 14486–14492 (1989).
Lois R, Dietrich A, Hahlbrock K, Schulz W: A phenylalanine ammonia-lyase gene from parsley: Structure, regulation and identification of elicitor and light responsivecis-acting elements. EMBO J 8: 1641–1648 (1989).
Loschke DC, Hadwiger LA: Effects of light and ofFusarium solani on synthesis and activity of phenylalanine ammonia-lyase in peas. Plant Physiol 68: 680–685 (1981).
Minami E, Ozeki Y, Matsuoka M, Koizuka N, Tanaka Y: Structure and some characterization of the gene for phenylalanine ammonia-lyase from rice plants. Eur J Biochem 185: 19–25 (1989).
Ohl S, Hedrick SA, Chory J, Lamb CJ: Functional properties of a phenylalanine ammonia-lyase promoter fromArabidopsis. Plant Cell 2: 837–848 (1990).
Shiraishi T, Yamada T, Oku H, Yoshioka H: Suppressor production as a key factor for fungal pathogenesis. In: Patil SS, Ouchi S, Mills D, Vance C (eds) Molecular Strategies of Pathogens and Host Plants. Springer-Verlag, New York (1991).
Tanaka Y, Matsuoka M, Yamamoto N, Ohashi Y, Kano-Murakami Y, Ozeki Y: Structure and characterization of a cDNA clone for potato. Plant Physiol 90: 1403–1407 (1989).
Yamada T, Hashimoto H, Shiraishi T, Oku H: Suppression of pisatin, phenylalanine ammonia-lyase mRNA, and chalcone synthase mRNA accumulation by a putative pathogenicity factor from the fungusMycosphaerella pinodes. Mol Plant-Microbe Inter 2: 256–261 (1989).
Yoshioka H, Shiraishi T, Yamada T, Ichinose Y, Oku H: Suppression of pisatin production and ATPase activity in pea plasma membranes by orthovanadate, verapamil and suppressor fromMycosphaerella pinodes. Plant Cell Physiol 31: 1139–1146 (1990).
Yoshioka H, Shiraishi T, Kawamata S, Nasu K, Yamada T, Ichinose Y, Oku H: Orthovanadate suppresses accumulation of phenylalanine ammonia-lyase mRNA and chalcone synthase mRNA in pea epicotyls induced by elicitor fromMycosphaerella pinodes. Plant Cell Physiol, in press.
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Kawamata, S., Yamada, T., Tanaka, Y. et al. Molecular cloning of phenylalanine ammonia-lyase cDNA fromPisum sativum . Plant Mol Biol 20, 167–170 (1992). https://doi.org/10.1007/BF00029163
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DOI: https://doi.org/10.1007/BF00029163