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［1］ Antoniw J F, Ritter C E, Pierpoint W S, et al. Comparison of three pathogenesisrelated proteins from plants of two cultivars of tobacco infected with TMV. Journal of General Virology, 1980, 47: 7987. 
［2］ Van Loon L C, Van Strien E A. The families of pathogenesisrelated proteins, their activities, and comparative analysis of PR1 type proteins. Physiological and Molecular Plant Payhology, 1999, 22: 55855597. 
［3］ Ho V S, Wong J H, Ng T B. A thaumatinlike antifungal protein from the emperor banana. Peptides, 2007, 28: 760766. 
［4］ Selitrennikoff C P. Antifungal proteins. Applied and Environmental Microbiology, 2001, 67: 28832894. 
［5］ Ghosh R, Chakrabarti C. Crystal structure analysis of NP24I: a thaumatinlike protein. Planta, 2008, 228: 883890. 
［6］ Leone P, MenuBouaouiche L, Peumans W J, et al. Resolution of the structure of the allergenic and antifungal banana fruit thaumatin like protein at 1.7 ?. Biochimie, 2006, 88: 4552. 
［7］ Kaneko R, Kitabatake N. Structuresweetness relationshi Pin thaumatin: importance of lysine residues. Chemical Senses, 2001, 26: 167177. 
［8］ Anzlovar S, Serra M D, Dermastia M, et al. Membrane permeabilizing activity of pathogenesisrelated protein linusitin from flax seed. Molecular PlantMicrobe Interactions, 1998, 11: 610617. 
［9］ Koiwa H, Kato H, Nakatsu T, et al. Crystal structure of tobacco PR5d protein at 1.8  resolution reveals a conserved acidic cleft structure in antifungal Thaumatinlike Proteins. Journal of Molecular Biology, 1999, 286: 11371145. 
［10］ Velazhahan R, Muthukrishnan S. Transgenic tobacco plants constitutively overexpressing a rice thaumatinlike protein (PR5) show enhanced resistance to Alternaria alternate. Biologia Plantarum, 2003, 47: 347354. 
［11］ MenuBouaouiche L, Vriet C, Peumans W J, et al. A molecular basis for the endobeta1,3glucanase activity of the thaumatinlike proteins from edible fruits. Biochimie, 2003, 85: 123131. 
［12］ Zechel D L, Withers S G. Dissection of nucleophilic and acidbase catalysis in glycosidases. Current Opinion in Chemical Biology, 2001, 5: 643649. 
［13］ Kim Y S, Park J Y, Kim K S, et al. A thaumatinlike gene in nonclimacteric pepper fruits used as molecular marker in probing disease resistance, ripening, and sugar accumulation. Plant Molecular Biology, 2002, 49: 125135. 
［14］ Vitalia A, Pacinia L, Bordic E, et al. Purification and characterization of an antifungal thaumatinlike protein from Cassia didymobotrya cell culture. Plant Physiology and Biochemistry, 2006, 44: 604610. 
［15］ Klarzynski O, Plesse B, Joubert J M, et al. Linear β1,3 Glucans are elicitors of defense responses in tobacco. Plant Physiology, 2003, 124: 10271037. 
［16］ Looze Y, Boussard P, Huet J, et al. Purification and characterization of a woundinducible thaumatinlike protein from the latex of Carica papaya. Phytochemistry, 2009, 70(8): 970978. 
［17］ Wang H X, Ng T B. Dendrocin, a distinctive antifungal protein from bamboo shoots. Biochemical and Biophysical Research Communications, 2003, 307: 750755. 
［18］ O'Leary S J, Poulis B A, von Aderkas P. Identification of two thaumatinlike proteins (TLPs) in the pollination dro Pof hybrid yew that may play a role in pathogen defence during pollen collection. Tree Physiology, 2007, 27: 16491659. 
［19］ Li W L, Faris J D, Muthukrishnan S, et al. Isolation and characterization of novel cDNA clones of acidic chitinases and β1,3glucanases from wheat spikes infected with Fusarium graminearium. Theoretical and Applied Genetics, 2001, 102: 353362. 
［20］ Pritsch C, Vance C P, Bushnell R W, et al. Systemic expression of defence response genes in wheat spikes as a response to Fusarium graminearum infection. Physiological and Molecular Plant Pathology, 2001, 58: 112. 
［21］ Anand A, Zhou T, Trick H N, et al. Greenhouse and field testing of transgenic wheat plants stably expressing genes for thaumatinlike protein, chitinase and glucanase against Fusarium graminearum. Journal of Experimental Botany, 2003, 54(384): 11011111. 
［22］ Tobias D J, Manoharan M, Pritsch C, et al. Cobombardment, integration and expression of rice chitinase and thaumatinlike protein genes in barley (Hordeum vulgare cv. Conlon). Plant Cell Reports, 2007, 26: 631639. 
［23］ Mackintosh C A, Lewis J, Radmer L E, et al. Overexpression of defense response genes in transgenic wheat enhances resistance to Fusarium head blight. Plant Cell Reports, 2007, 26: 479488. 
［24］ Datta K, Velazhahan R, Oliva N, et al. Overexpression of the cloned rice thaumatinlike protein (PR5) gene in transgenic rice plants enhances environmental friendly resistance to Rhizoctonia sonali causing sheath blight disease. Theoretical and Applied Genetics, 1999, 98: 11381145. 
［25］ Maruthasalam S, Kalpana K, Kumar K K, et al. Pyramiding transgenic resistance in elite indica rice cultivars against the sheath blight and bacterial blight. Plant Cell Reports, 2007, 26: 791804.