메뉴 건너뛰기




Volumn 8, Issue 12, 2013, Pages

Characterization of a pathogen induced thaumatin-like protein gene AdTLP from Arachis diogoi, a wild peanut

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; CYSTEINE; HYDROGEN PEROXIDE; RECOMBINANT PROTEIN; SODIUM CHLORIDE; THAUMATIN; THAUMATIN LIKE PROTEIN; UNCLASSIFIED DRUG;

EID: 84893186402     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0083963     Document Type: Article
Times cited : (106)

References (61)
  • 1
    • 0000555489 scopus 로고    scopus 로고
    • Pathogenesis-Related Proteins and Plant Defense
    • G CarrollP Tudzynski. Springer Berlin Heidelberg
    • Kombrink E, Somssich IE (1997) Pathogenesis-Related Proteins and Plant Defense. In: G CarrollP Tudzynski. Plant Relationships: Springer Berlin Heidelberg. pp. 107-128
    • (1997) Plant Relationships , pp. 107-128
    • Kombrink, E.1    Somssich, I.E.2
  • 2
    • 33750967667 scopus 로고    scopus 로고
    • A pathogenesis related protein, AhPR10 from peanut: An insight of its mode of antifungal activity
    • DOI 10.1007/s00425-006-0344-7
    • Chadha P, Das RH (2006) A pathogenesis related protein, AhPR10 from peanut: an insight of its mode of antifungal activity. Planta 225: 213-222. doi:10.1007/s00425-006-0344-7. PubMed: 16832688. (Pubitemid 44749617)
    • (2006) Planta , vol.225 , Issue.1 , pp. 213-222
    • Chadha, P.1    Das, R.H.2
  • 3
    • 33748941620 scopus 로고    scopus 로고
    • Significance of inducible defense-related proteins in infected plants
    • DOI 10.1146/annurev.phyto.44.070505.143425
    • van Loon LC, Rep M, Pieterse CM (2006) Significance of inducible defense-related proteins in infected plants. Annu Rev Phytopathol 44: 135-162. doi:10.1146/annurev.phyto.44.070505.143425. PubMed: 16602946. (Pubitemid 44435701)
    • (2006) Annual Review of Phytopathology , vol.44 , pp. 135-162
    • Van Loon, L.C.1    Rep, M.2    Pieterse, C.M.J.3
  • 4
    • 0022454902 scopus 로고
    • A tobacco mosaic virus-induced tobacco protein is homologous to the sweet-tasting protein thaumatin
    • doi:10.1038/321531a0. PubMed: 3713832
    • Cornelissen BJ, Hooft van Huijsduijnen RA, Bol JF (1986) A tobacco mosaic virus-induced tobacco protein is homologous to the sweet-tasting protein thaumatin. Nature 321: 531-532. doi:10.1038/321531a0. PubMed: 3713832.
    • (1986) Nature , vol.321 , pp. 531-532
    • Cornelissen, B.J.1    Hooft Van Huijsduijnen, R.A.2    Bol, J.F.3
  • 5
    • 77952423798 scopus 로고    scopus 로고
    • The superfamily of thaumatin-like proteins: Its origin, evolution, and expression towards biological function
    • doi:10.1007/s00299-010-0826-8. PubMed: 20204373
    • Liu JJ, Sturrock R, Ekramoddoullah AK (2010) The superfamily of thaumatin-like proteins: its origin, evolution, and expression towards biological function. Plant Cell Rep 29: 419-436. doi:10.1007/s00299-010-0826-8. PubMed: 20204373.
    • (2010) Plant Cell Rep , vol.29 , pp. 419-436
    • Liu, J.J.1    Sturrock, R.2    Ekramoddoullah, A.K.3
  • 6
    • 57649103090 scopus 로고    scopus 로고
    • Molecular characterization of a novel soybean gene encoding a neutral PR-5 protein induced by high-salt stress
    • doi:10.1016/j.plaphy.2008.09.012. PubMed: 19010689
    • Tachi H, Fukuda-Yamada K, Kojima T, Shiraiwa M, Takahara H (2009) Molecular characterization of a novel soybean gene encoding a neutral PR-5 protein induced by high-salt stress. Plant Physiol Biochem 47: 73-79. doi:10.1016/j.plaphy.2008.09.012. PubMed: 19010689.
    • (2009) Plant Physiol Biochem , vol.47 , pp. 73-79
    • Tachi, H.1    Fukuda-Yamada, K.2    Kojima, T.3    Shiraiwa, M.4    Takahara, H.5
  • 7
    • 85056341695 scopus 로고    scopus 로고
    • The PR-5 family: Thaumatin like protein in plants
    • Datta Sk, Muthukrishnan S, editors. CRC press Boca Raton
    • Velazhahan R, Datta KS, Muthukrishnan S (1999) The PR-5 family: thaumatin like protein in plants. In: Datta Sk, Muthukrishnan S, editors. Pathogenesis-related proteins in plants. CRC press Boca Raton. pp. 107-129
    • (1999) Pathogenesis-related Proteins in Plants , pp. 107-129
    • Velazhahan, R.1    Datta, K.S.2    Muthukrishnan, S.3
  • 8
    • 70749108682 scopus 로고    scopus 로고
    • Biochemical and structural characterization of TLXI, the Triticum aestivum L. Thaumatin-like xylanase inhibitor
    • doi:10.1080/14756360802321831. PubMed: 18951281
    • Fierens E, Gebruers K, Voet AR, De Maeyer M, Courtin CM et al. (2009) Biochemical and structural characterization of TLXI, the Triticum aestivum L. thaumatin-like xylanase inhibitor. J Enzyme Inhib Med Chem 24: 646-654. doi:10.1080/14756360802321831. PubMed: 18951281.
    • (2009) J Enzyme Inhib Med Chem , vol.24 , pp. 646-654
    • Fierens, E.1    Gebruers, K.2    Voet, A.R.3    De Maeyer, M.4    Courtin, C.M.5
  • 9
    • 0033819987 scopus 로고    scopus 로고
    • Characterization of an apoplastic basic thaumatin-like protein from recalcitrant chestnut seeds
    • doi:10.1034/j.1399-3054.2000.110205.x
    • Garcia-Casado G, Collada C, Allona I, Soto A, Casado R et al. (2000) Characterization of an apoplastic basic thaumatin-like protein from recalcitrant chestnut seeds. Physiologia Plantarum 110: 172-180. doi:10.1034/j.1399-3054. 2000.110205.x.
    • (2000) Physiologia Plantarum , vol.110 , pp. 172-180
    • Garcia-Casado, G.1    Collada, C.2    Allona, I.3    Soto, A.4    Casado, R.5
  • 10
    • 0037423689 scopus 로고    scopus 로고
    • Isolation of a large thaumatin-like antifungal protein from seeds of the Kweilin chestnut Castanopsis chinensis
    • doi:10.1016/S0006-291X(02)02998-4. PubMed: 12565869
    • Chu KT, Ng TB (2003) Isolation of a large thaumatin-like antifungal protein from seeds of the Kweilin chestnut Castanopsis chinensis. Biochem Biophys Res Commun 301: 364-370. doi:10.1016/S0006-291X(02)02998-4. PubMed: 12565869.
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 364-370
    • Chu, K.T.1    Ng, T.B.2
  • 11
    • 33847345120 scopus 로고    scopus 로고
    • A thaumatin-like antifungal protein from the emperor banana
    • DOI 10.1016/j.peptides.2007.01.005, PII S0196978107000022
    • Ho VS, Wong JH, Ng TB (2007) A thaumatin-like antifungal protein from the emperor banana. Peptides 28: 760-766. doi:10.1016/j.peptides.2007.01.005. PubMed: 17306420. (Pubitemid 46349330)
    • (2007) Peptides , vol.28 , Issue.4 , pp. 760-766
    • Ho, V.S.M.1    Wong, J.H.2    Ng, T.B.3
  • 12
    • 33846617384 scopus 로고    scopus 로고
    • Molecular, biochemical and structural characterization of osmotin-like protein from black nightshade (Solanum nigrum)
    • DOI 10.1016/j.jplph.2006.01.006, PII S0176161706000526
    • Jami SK, Swathi Anuradha T, Guruprasad L, Kirti PB (2007) Molecular, biochemical and structural characterization of osmotin-like protein from black nightshade (Solanum nigrum). J Plant Physiol 164: 238-252. doi:10.1016/j.jplph. 2006.01.006. PubMed: 16542753. (Pubitemid 46186587)
    • (2007) Journal of Plant Physiology , vol.164 , Issue.3 , pp. 238-252
    • Jami, S.K.1    Swathi, A.T.2    Guruprasad, L.3    Kirti, P.B.4
  • 13
    • 0025063227 scopus 로고
    • Zeamatin, an antifungal protein from maize with membrane-permeabilizing activity
    • Roberts WK, Selitrennikoff CP (1990) Zeamatin, an antifungal protein from maize with membrane-permeabilizing activity. Journal of General Microbiology 136: 1771-1778. doi:10.1099/00221287-136-9-1771. (Pubitemid 20291277)
    • (1990) Journal of General Microbiology , vol.136 , Issue.9 , pp. 1771-1778
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 14
    • 0033180204 scopus 로고    scopus 로고
    • Some thaumatin-like proteins hydrolyse polymeric beta-1,3-glucans
    • doi:10.1046/j.1365-313X.1999.00551.x. PubMed: 10504569
    • Grenier J, Potvin C, Trudel J, Asselin A (1999) Some thaumatin-like proteins hydrolyse polymeric beta-1,3-glucans. Plant J 19: 473-480. doi:10.1046/j.1365-313X.1999.00551.x. PubMed: 10504569.
    • (1999) Plant J , vol.19 , pp. 473-480
    • Grenier, J.1    Potvin, C.2    Trudel, J.3    Asselin, A.4
  • 16
    • 12744261386 scopus 로고    scopus 로고
    • Overexpression of rice TLPD34 enhances dollar-spot resistance in transgenic bentgrass
    • doi:10.1016/j.plantsci.2004.09.032
    • Fu D, Tisserat NA, Xiao Y, Settle D, Muthukrishnan S et al. (2005) Overexpression of rice TLPD34 enhances dollar-spot resistance in transgenic bentgrass. Plant Sciences 168: 671-680. doi:10.1016/j.plantsci.2004.09.032.
    • (2005) Plant Sciences , vol.168 , pp. 671-680
    • Fu, D.1    Tisserat, N.A.2    Xiao, Y.3    Settle, D.4    Muthukrishnan, S.5
  • 18
    • 0029411516 scopus 로고
    • Antifreeze proteins in winter rye are similar to pathogenesis-related proteins
    • Hon WC, Griffith M, Mlynarz A, Kwok YC, Yang DS (1995) Antifreeze proteins in winter rye are similar to pathogenesis-related proteins. Plant Physiol 109: 879-889. doi:10.1104/pp.109.3.879. PubMed: 8552719. (Pubitemid 3009553)
    • (1995) Plant Physiology , vol.109 , Issue.3 , pp. 879-889
    • Hon W.-Ching1    Griffith, M.2    Mlynarz, A.3    Kwok, Y.C.4    Yang, D.S.5
  • 19
    • 0031127606 scopus 로고    scopus 로고
    • Two isoforms of NP24: A thaumatin-like protein in tomato fruit
    • doi:10.1016/S0031-9422(96)00667-X. PubMed: 9115696
    • Pressey R (1997) Two isoforms of NP24: a thaumatin-like protein in tomato fruit. Phytochemistry 44: 1241-1245. doi:10.1016/S0031-9422(96)00667-X. PubMed: 9115696.
    • (1997) Phytochemistry , vol.44 , pp. 1241-1245
    • Pressey, R.1
  • 20
    • 0041920777 scopus 로고    scopus 로고
    • Potential of wild species for genetic enhancement of some semi-arid food crops
    • DOI 10.1023/A:1025055018954
    • Kameswara Rao N, Reddy LJ, Bramel PJ (2003) Potential of wild species for genetic enhancement of some semi-arid food crops. Genetic Resources and Crop Evolution 50: 707-721. doi:10.1023/A:1025055018954. (Pubitemid 37078288)
    • (2003) Genetic Resources and Crop Evolution , vol.50 , Issue.7 , pp. 707-721
    • Rao, N.K.1    Reddy, L.J.2    Bramel, P.J.3
  • 21
    • 0034920910 scopus 로고    scopus 로고
    • Resistance of wild Arachis species to late leaf spot and rust in greenhouse trials
    • Pande S, Rao JN (2001) Resistance of wild Arachis species to late leaf spot and rust in greenhouse trials. Plant Disease 85: 851-855. doi:10.1094/PDIS.2001.85.8.851. (Pubitemid 32686472)
    • (2001) Plant Disease , vol.85 , Issue.8 , pp. 851-855
    • Pande, S.1    Narayana, R.J.2
  • 22
    • 79952043686 scopus 로고    scopus 로고
    • Differential gene expression in Arachis diogoi upon interaction with peanut late leaf spot pathogen, Phaeoisariopsis personata and characterization of a pathogen induced cyclophilin
    • doi:10.1007/s11103-011-9747-3. PubMed: 21298396
    • Kumar KR, Kirti PB (2011) Differential gene expression in Arachis diogoi upon interaction with peanut late leaf spot pathogen, Phaeoisariopsis personata and characterization of a pathogen induced cyclophilin. Plant Mol Biol 75: 497-513. doi:10.1007/s11103-011-9747-3. PubMed: 21298396.
    • (2011) Plant Mol Biol , vol.75 , pp. 497-513
    • Kumar, K.R.1    Kirti, P.B.2
  • 23
    • 17844363007 scopus 로고    scopus 로고
    • cDNA cloning, functional expression and antifungal activities of a dimeric plant defensin SPE10 from Pachyrrhizus erosus seeds
    • DOI 10.1007/s11103-004-6637-y
    • Song X, Wang J, Wu F, Li X, Teng M et al. (2005) cDNA cloning, functional expression and antifungal activities of a dimeric plant defensin SPE10 from Pachyrrhizus erosus seeds. Plant Mol Biol 57: 13-20. doi:10.1007/s11103-004- 6637-y. PubMed: 15821865. (Pubitemid 40580439)
    • (2005) Plant Molecular Biology , vol.57 , Issue.1 , pp. 13-20
    • Song, X.1    Wang, J.2    Wu, F.3    Li, X.4    Teng, M.5    Gong, W.6
  • 24
    • 53249121477 scopus 로고    scopus 로고
    • Prokaryotic expression of a constitutively expressed Tephrosia villosa defensin and its potent antifungal activity
    • doi:10.1007/s00253-008-1648-2. PubMed: 18726095
    • Vijayan S, Guruprasad L, Kirti PB (2008) Prokaryotic expression of a constitutively expressed Tephrosia villosa defensin and its potent antifungal activity. Appl Microbiol Biotechnol 80: 1023-1032. doi:10.1007/s00253-008-1648- 2. PubMed: 18726095.
    • (2008) Appl Microbiol Biotechnol , vol.80 , pp. 1023-1032
    • Vijayan, S.1    Guruprasad, L.2    Kirti, P.B.3
  • 25
    • 67649833824 scopus 로고    scopus 로고
    • Purification and characterization of a wound-inducible thaumatin-like protein from the latex of Carica papaya
    • doi:10.1016/j.phytochem.2009.05.005. PubMed: 19527911
    • Looze Y, Boussard P, Huet J, Vandenbusche G, Azarkan M et al. (2009) Purification and characterization of a wound-inducible thaumatin-like protein from the latex of Carica papaya. Phytochemistry 70: 970-978. doi:10.1016/j.phytochem.2009.05.005. PubMed: 19527911.
    • (2009) Phytochemistry , vol.70 , pp. 970-978
    • Looze, Y.1    Boussard, P.2    Huet, J.3    Vandenbusche, G.4    Azarkan, M.5
  • 26
    • 37049182668 scopus 로고
    • A simple and general method for transferring genes into plants
    • doi:10.1126/science.227.4691.1229. PubMed: 17757866
    • Horsch RB, Fry JE, Hoffmann NL, Eichholtz D, Rogers SG et al. (1985) A simple and general method for transferring genes into plants. Science 227: 1229-1230. doi:10.1126/science.227.4691.1229. PubMed: 17757866.
    • (1985) Science , vol.227 , pp. 1229-1230
    • Horsch, R.B.1    Fry, J.E.2    Hoffmann, N.L.3    Eichholtz, D.4    Rogers, S.G.5
  • 27
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts: Polyphenoloxidase in Beta vulgaris
    • doi:10.1104/pp.24.1.1. PubMed: 16654194
    • Arnon DI (1949) Copper enzymes in isolated chloroplasts: polyphenoloxidase in Beta vulgaris. Plant Physiol 24: 1-15. doi:10.1104/pp.24.1. 1. PubMed: 16654194.
    • (1949) Plant Physiol , vol.24 , pp. 1-15
    • Arnon, D.I.1
  • 28
    • 0014276153 scopus 로고
    • Photoperoxidation in isolated chloroplasts. I. Kinetics and stoichiometry of fatty acid peroxidation
    • doi:10.1016/0003-9861(68)90654-1. PubMed: 5655425
    • Heath RL, Packer L (1968) Photoperoxidation in isolated chloroplasts. I. Kinetics and stoichiometry of fatty acid peroxidation. Arch Biochem Biophys 125: 189-198. doi:10.1016/0003-9861(68)90654-1. PubMed: 5655425.
    • (1968) Arch Biochem Biophys , vol.125 , pp. 189-198
    • Heath, R.L.1    Packer, L.2
  • 29
    • 0033031144 scopus 로고    scopus 로고
    • Over-expression of the cloned rice thaumatin-like protein (PR-5) gene in transgenic rice plants enhances environmental friendly resistance to Rhizoctonia solani causing sheath blight disease
    • DOI 10.1007/s001220051178
    • Datta K, Velazhahan R, Oliva N, Ona I, Mew T et al. (1999) Overexpression of the cloned rice thaumatin-like protein (PR-5) gene in transgenic rice plants enhances environmental friendly resistance to Rhizoctonia solani causing sheath blight disease. Theoretical and Applied Genetics 98: 1138-1145. doi:10.1007/s001220051178. (Pubitemid 29245244)
    • (1999) Theoretical and Applied Genetics , vol.98 , Issue.6-7 , pp. 1138-1145
    • Datta, K.1    Velazhahan, R.2    Oliva, N.3    Ona, I.4    Mew, T.5    Khush, G.S.6    Muthukrishnan, S.7    Datta, S.K.8
  • 30
    • 79952440469 scopus 로고    scopus 로고
    • High-efficiency transformation and selective tolerance against biotic and abiotic stress in mulberry, Morus indica cv. K2, by constitutive and inducible expression of tobacco osmotin
    • doi:10.1007/s11248-010-9405-6. PubMed: 20549349
    • Das M, Chauhan H, Chhibbar A, Rizwanul Haq QM, Khurana P (2011) High-efficiency transformation and selective tolerance against biotic and abiotic stress in mulberry, Morus indica cv. K2, by constitutive and inducible expression of tobacco osmotin. Transgenic Res 20: 231-246. doi:10.1007/s11248- 010-9405-6. PubMed: 20549349.
    • (2011) Transgenic Res , vol.20 , pp. 231-246
    • Das, M.1    Chauhan, H.2    Chhibbar, A.3    Rizwanul Haq, Q.M.4    Khurana, P.5
  • 31
    • 77956175012 scopus 로고    scopus 로고
    • Overexpression of osmotin gene confers tolerance to salt and drought stresses in transgenic tomato (Solanum lycopersicum L.)
    • Goel D, Singh AK, Yadav V, Babbar SB, Bansal KC (2010) Overexpression of osmotin gene confers tolerance to salt and drought stresses in transgenic tomato (Solanum lycopersicum L.). Protoplasma 245: 133-141
    • (2010) Protoplasma , vol.245 , pp. 133-141
    • Goel, D.1    Singh, A.K.2    Yadav, V.3    Babbar, S.B.4    Bansal, K.C.5
  • 33
    • 77954693064 scopus 로고    scopus 로고
    • Characterization of a pathogenesis-related thaumatin-like protein gene TaPR5 from wheat induced by stripe rust fungus
    • doi:10.1111/j.1399-3054.2009.01338.x. PubMed: 20059734
    • Wang X, Tang C, Deng L, Cai G, Liu X et al. (2010) Characterization of a pathogenesis-related thaumatin-like protein gene TaPR5 from wheat induced by stripe rust fungus. Physiol Plant 139: 27-38. doi:10.1111/j.1399-3054.2009. 01338.x. PubMed: 20059734.
    • (2010) Physiol Plant , vol.139 , pp. 27-38
    • Wang, X.1    Tang, C.2    Deng, L.3    Cai, G.4    Liu, X.5
  • 34
    • 79952046893 scopus 로고    scopus 로고
    • Purification and characterization of a CkTLP protein from Cynanchum komarovii seeds that confers antifungal activity
    • doi:10.1371/journal.pone.0016930. PubMed: 21364945
    • Wang Q, Li F, Zhang X, Zhang Y, Hou Y et al. (2011) Purification and characterization of a CkTLP protein from Cynanchum komarovii seeds that confers antifungal activity. PLOS ONE 6: e16930. doi:10.1371/journal.pone.0016930. PubMed: 21364945.
    • (2011) PLOS ONE , vol.6
    • Wang, Q.1    Li, F.2    Zhang, X.3    Zhang, Y.4    Hou, Y.5
  • 35
    • 74149093105 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a thaumatin-like protein-encoding cDNA from rough lemon
    • doi:10.1016/j.pmpp.2009.07.001
    • Kim B-G, Fukumoto T, Tatano S, Gomi K, Ohtani K et al. (2009) Molecular cloning and characterization of a thaumatin-like protein-encoding cDNA from rough lemon. Physiological and Molecular Plant Pathology 74: 3-10. doi:10.1016/j.pmpp.2009.07.001.
    • (2009) Physiological and Molecular Plant Pathology , vol.74 , pp. 3-10
    • Kim, B.-G.1    Fukumoto, T.2    Tatano, S.3    Gomi, K.4    Ohtani, K.5
  • 36
    • 0033575874 scopus 로고    scopus 로고
    • First chromatographic isolation of an antifungal thaumatin-like protein from French bean legumes and demonstration of its antifungal activity
    • DOI 10.1006/bbrc.1999.1166
    • Ye XY, Wang HX, Ng TB (1999) First chromatographic isolation of an antifungal thaumatin-like protein from French bean legumes and demonstration of its antifungal activity. Biochem Biophys Res Commun 263: 130-134. doi:10.1006/bbrc.1999.1166. PubMed: 10486265. (Pubitemid 29443651)
    • (1999) Biochemical and Biophysical Research Communications , vol.263 , Issue.1 , pp. 130-134
    • Ye, X.Y.1    Wang, H.X.2    Ng, T.B.3
  • 37
    • 33750954916 scopus 로고    scopus 로고
    • Purification and characterization of an antifungal thaumatin-like protein from Cassia didymobotrya cell culture
    • DOI 10.1016/j.plaphy.2006.09.008, PII S0981942806001306
    • Vitali A, Pacini L, Bordi E, De Mori P, Pucillo L et al. (2006) Purification and characterization of an antifungal thaumatin-like protein from Cassia didymobotrya cell culture. Plant Physiol Biochem 44: 604-610. doi:10.1016/j.plaphy.2006.09.008. PubMed: 17056265. (Pubitemid 44739304)
    • (2006) Plant Physiology and Biochemistry , vol.44 , Issue.10 , pp. 604-610
    • Vitali, A.1    Pacini, L.2    Bordi, E.3    De Mori, P.4    Pucillo, L.5    Maras, B.6    Botta, B.7    Brancaccio, A.8    Giardina, B.9
  • 38
    • 0001207381 scopus 로고    scopus 로고
    • Some Fungi Express β-1,3-Glucanases Similar to Thaumatin-like Proteins
    • doi:10.2307/3761579
    • Grenier J, Potvin C, Asselin A (2000) Some Fungi Express β-1,3-Glucanases Similar to Thaumatin-like Proteins. Mycologia 92: 841-848. doi:10.2307/3761579.
    • (2000) Mycologia , vol.92 , pp. 841-848
    • Grenier, J.1    Potvin, C.2    Asselin, A.3
  • 39
    • 0842270131 scopus 로고    scopus 로고
    • Transgenic Tobacco Plants Constitutively Overexpressing a Rice Thaumatin-like Protein (PR-5) Show Enhanced Resistance to Alternaria alternata
    • Velazhahan R, Muthukrishnan S (2003) Transgenic Tobacco Plants Constitutively Overexpressing a Rice Thaumatin-like Protein (PR-5) Show Enhanced Resistance to Alternaria alternata. Biologia Plantarum 47: 347-354.
    • (2003) Biologia Plantarum , vol.47 , pp. 347-354
    • Velazhahan, R.1    Muthukrishnan, S.2
  • 40
    • 77249158303 scopus 로고    scopus 로고
    • A thaumatin-like protein gene involved in cotton fiber secondary cell wall development enhances resistance against Verticillium dahliae and other stresses in transgenic tobacco
    • doi: 10.1016/j.bbrc.2010.01.069. PubMed: 20097164
    • Munis MF, Tu L, Deng F, Tan J, Xu L et al. (2010) A thaumatin-like protein gene involved in cotton fiber secondary cell wall development enhances resistance against Verticillium dahliae and other stresses in transgenic tobacco. Biochem Biophys Res Commun 393: 38-44. doi: 10.1016/j.bbrc.2010.01.069. PubMed: 20097164.
    • (2010) Biochem Biophys Res Commun , vol.393 , pp. 38-44
    • Munis, M.F.1    Tu, L.2    Deng, F.3    Tan, J.4    Xu, L.5
  • 42
    • 0036258690 scopus 로고    scopus 로고
    • Abscisic acid- and cold-induced thaumatin-like protein in winter wheat has an antifungal activity against snow mould, Microdochium nivale
    • DOI 10.1034/j.1399-3054.2002.1150112.x
    • Kuwabara C, Takezawa D, Shimada T, Hamada T, Fujikawa S et al. (2002) Abscisic acid- and cold-induced thaumatin-like protein in winter wheat has an antifungal activity against snow mould, Microdochium nivale. Physiol Plant 115: 101-110. doi:10.1034/j.1399-3054.2002.1150112.x. PubMed: 12010473. (Pubitemid 34564991)
    • (2002) Physiologia Plantarum , vol.115 , Issue.1 , pp. 101-110
    • Kuwabara, C.1    Takezawa, D.2    Shimada, T.3    Hamada, T.4    Fujikawa, S.5    Arakawa, K.6
  • 43
    • 33947508750 scopus 로고    scopus 로고
    • Thaumatin gene confers resistance to fungal pathogens as well as tolerance to abiotic stresses in transgenic tobacco plants
    • DOI 10.1007/s10535-007-0026-8
    • Rajam MV, Chandola N, Saiprasad Goud P, Singh D, Kashyap V et al. (2007) Thaumatin gene confers resistance to fungal pathogens as well as tolerance to abiotic stresses in transgenic tobacco plants. Biologia Plantarum 51: 135-141. doi:10.1007/s10535-007-0026-8. (Pubitemid 46464798)
    • (2007) Biologia Plantarum , vol.51 , Issue.1 , pp. 135-141
    • Rajam, M.V.1    Chandola, N.2    Goud, P.S.3    Singh, D.4    Kashyap, V.5    Choudhary, M.L.6    Sihachakr, D.7
  • 44
    • 14844342962 scopus 로고    scopus 로고
    • Understanding and improving salt tolerance in plants
    • Chinnusamy V, Jagendorf A, Zhu J-K (2005) Understanding and Improving Salt Tolerance in Plants. Crop Sci 45: 437-448. doi:10.2135/cropsci2005.0437. (Pubitemid 40350959)
    • (2005) Crop Science , vol.45 , Issue.2 , pp. 437-448
    • Chinnusamy, V.1    Jagendorf, A.2    Zhu, J.-K.3
  • 45
    • 79952933352 scopus 로고    scopus 로고
    • Prunus domestica pathogenesis-related protein-5 activates the defense response pathway and enhances the resistance to fungal infection
    • doi:10.1371/journal.pone.0017973. PubMed: 21448276
    • El-kereamy A, El-sharkawy I, Ramamoorthy R, Taheri A, Errampalli D et al. (2011) Prunus domestica pathogenesis-related protein-5 activates the defense response pathway and enhances the resistance to fungal infection. PLOS ONE 6: e17973. doi:10.1371/journal.pone.0017973. PubMed: 21448276.
    • (2011) PLOS ONE , vol.6
    • El-kereamy, A.1    El-sharkawy, I.2    Ramamoorthy, R.3    Taheri, A.4    Errampalli, D.5
  • 46
    • 84882878200 scopus 로고    scopus 로고
    • Overexpression of Camellia sinensis thaumatin-like protein, CsTLP in potato confers enhanced resistance to Macrophomina phaseolina and Phytophthora infestans infection
    • doi:10.1007/s12033-012-9603-y. PubMed: 23086453
    • Acharya K, Pal AK, Gulati A, Kumar S, Singh AK et al. (2013) Overexpression of Camellia sinensis thaumatin-like protein, CsTLP in potato confers enhanced resistance to Macrophomina phaseolina and Phytophthora infestans infection. Mol Biotechnol 54: 609-622. doi:10.1007/s12033-012-9603-y. PubMed: 23086453.
    • (2013) Mol Biotechnol , vol.54 , pp. 609-622
    • Acharya, K.1    Pal, A.K.2    Gulati, A.3    Kumar, S.4    Singh, A.K.5
  • 47
    • 33750616022 scopus 로고    scopus 로고
    • The effect of thaumatin gene overexpression on the properties of H(+)-ATPase from the plasmalemma of potato tuber cells
    • PubMed: 17022457
    • Ladyzhenskaia EP, Korableva NP (2006) The effect of thaumatin gene overexpression on the properties of H(+)-ATPase from the plasmalemma of potato tuber cells. Prikl Biokhim Mikrobiol 42: 462-467. PubMed: 17022457.
    • (2006) Prikl Biokhim Mikrobiol , vol.42 , pp. 462-467
    • Ladyzhenskaia, E.P.1    Korableva, N.P.2
  • 48
    • 33745674717 scopus 로고    scopus 로고
    • Lentinula edodes tlg1 encodes a thaumatin-like protein that is involved in lentinan degradation and fruiting body senescence
    • DOI 10.1104/pp.106.076679
    • Sakamoto Y, Watanabe H, Nagai M, Nakade K, Takahashi M et al. (2006) Lentinula edodes tlg1 encodes a thaumatin-like protein that is involved in lentinan degradation and fruiting body senescence. Plant Physiol 141: 793-801. doi:10.1104/pp.106.076679. PubMed: 16648221. (Pubitemid 43974571)
    • (2006) Plant Physiology , vol.141 , Issue.2 , pp. 793-801
    • Sakamoto, Y.1    Watanabe, H.2    Nagai, M.3    Nakade, K.4    Takahashi, M.5    Sato, T.6
  • 49
    • 40849130959 scopus 로고    scopus 로고
    • Molecular and functional profiling of Arabidopsis pathogenesis-related genes: Insights into their roles in salt response of seed germination
    • DOI 10.1093/pcp/pcn011
    • Seo PJ, Lee AK, Xiang F, Park CM (2008) Molecular and functional profiling of Arabidopsis pathogenesis-related genes: insights into their roles in salt response of seed germination. Plant Cell Physiol 49: 334-344. doi:10.1093/pcp/pcn011. PubMed: 18203731. (Pubitemid 351398306)
    • (2008) Plant and Cell Physiology , vol.49 , Issue.3 , pp. 334-344
    • Seo, P.J.1    Lee, A.-K.2    Xiang, F.3    Park, C.-M.4
  • 50
    • 33845663650 scopus 로고    scopus 로고
    • Involvement of the octadecanoid pathway in bluegreen aphid resistance in Medicago truncatula
    • DOI 10.1094/MPMI-20-0082
    • Gao LL, Anderson JP, Klingler JP, Nair RM, Edwards OR et al. (2007) Involvement of the octadecanoid pathway in bluegreen aphid resistance in Medicago truncatula. Mol Plant Microbe Interact 20: 82-93. doi:10.1094/MPMI-20- 0082. PubMed: 17249425. (Pubitemid 44956914)
    • (2007) Molecular Plant-Microbe Interactions , vol.20 , Issue.1 , pp. 82-93
    • Gao, L.-L.1    Anderson, J.P.2    Klingler, J.P.3    Nair, R.M.4    Edwards, O.R.5    Singh, K.B.6
  • 51
    • 34247267225 scopus 로고    scopus 로고
    • Arabidopsis transcriptome changes in response to phloem-feeding silverleaf whitefly nymphs. Similarities and distinctions in responses to aphids
    • DOI 10.1104/pp.106.090662
    • Kempema LA, Cui X, Holzer FM, Walling LL (2007) Arabidopsis transcriptome changes in response to phloem-feeding silverleaf whitefly nymphs. Similarities and distinctions in responses to aphids. Plant Physiol 143: 849-865. PubMed: 17189325. (Pubitemid 46940978)
    • (2007) Plant Physiology , vol.143 , Issue.2 , pp. 849-865
    • Kempema, L.A.1    Cui, X.2    Holzer, F.M.3    Walling, L.L.4
  • 52
    • 34247195585 scopus 로고    scopus 로고
    • Silverleaf whitefly induces salicylic acid defenses and suppresses effectual jasmonic acid defenses
    • DOI 10.1104/pp.106.090035
    • Zarate SI, Kempema LA, Walling LL (2007) Silverleaf whitefly induces salicylic acid defenses and suppresses effectual jasmonic acid defenses. Plant Physiol 143: 866-875. PubMed: 17189328. (Pubitemid 46940979)
    • (2007) Plant Physiology , vol.143 , Issue.2 , pp. 866-875
    • Zarate, S.I.1    Kempema, L.A.2    Walling, L.L.3
  • 53
    • 79958150758 scopus 로고    scopus 로고
    • Comparative transcription profiling analyses of maize reveals candidate defensive genes for seedling resistance against corn earworm
    • doi:10.1007/s00438-011-0626-z. PubMed: 21556895
    • Johnson ET, Dowd PF, Liu ZL, Musser RO (2011) Comparative transcription profiling analyses of maize reveals candidate defensive genes for seedling resistance against corn earworm. Mol Genet Genomics 285: 517-525. doi:10.1007/s00438-011-0626-z. PubMed: 21556895.
    • (2011) Mol Genet Genomics , vol.285 , pp. 517-525
    • Johnson, E.T.1    Dowd, P.F.2    Liu, Z.L.3    Musser, R.O.4
  • 54
    • 66749174020 scopus 로고    scopus 로고
    • Analysis of the poplar phloem proteome and its response to leaf wounding
    • doi:10.1021/pr800968r. PubMed: 19245218
    • Dafoe NJ, Zamani A, Ekramoddoullah AK, Lippert D, Bohlmann J et al. (2009) Analysis of the poplar phloem proteome and its response to leaf wounding. J Proteome Res 8: 2341-2350. doi:10.1021/pr800968r. PubMed: 19245218.
    • (2009) J Proteome Res , vol.8 , pp. 2341-2350
    • Dafoe, N.J.1    Zamani, A.2    Ekramoddoullah, A.K.3    Lippert, D.4    Bohlmann, J.5
  • 55
    • 0035131401 scopus 로고    scopus 로고
    • Bifunctional α-amylase/trypsin inhibitor activity previously ascribed to the 22 KDa TL protein, resided in a contaminant protein of 14 KDa
    • Gómez-Leyva JF, Blanco-Labra A (2001) Bifunctional α-amylase/trypsin inhibitor activity previously ascribed to the 22 KDa TL protein, resided in a contaminant protein of 14 KDa. J Plant Physiol 158: 177-183. doi:10.1078/0176-1617-00191. (Pubitemid 32161060)
    • (2001) Journal of Plant Physiology , vol.158 , Issue.2 , pp. 177-183
    • Gomez-Leyva, J.F.1    Blanco-Labra, A.2
  • 56
    • 0036164521 scopus 로고    scopus 로고
    • Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases
    • doi:10.1046/j.0014-2956.2001.02656.x. PubMed: 11856298
    • Franco OL, Rigden DJ, Melo FR, Grossi-De-Sá MF (2002) Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases. Eur J Biochem 269: 397-412. doi:10.1046/j.0014-2956.2001.02656.x. PubMed: 11856298.
    • (2002) Eur J Biochem , vol.269 , pp. 397-412
    • Franco, O.L.1    Rigden, D.J.2    Melo, F.R.3    Grossi-De-Sá, M.F.4
  • 57
    • 0031115122 scopus 로고    scopus 로고
    • Identification of Chitinase and Osmotin-Like Protein as Actin-Binding Proteins in Suspension-Cultured Potato Cells
    • Takemoto D, Furuse K, Doke N, Kawakita K (1997) Identification of chitinase and osmotin-like protein as actin-binding proteins in suspension-cultured potato cells. Plant Cell Physiol 38: 441-448. doi: 10.1093/oxfordjournals.pcp.a029187. PubMed: 9177030. (Pubitemid 127467259)
    • (1997) Plant and Cell Physiology , vol.38 , Issue.4 , pp. 441-448
    • Takemoto, D.1    Furuse, K.2    Doke, N.3    Kawakita, K.4
  • 58
    • 0034013346 scopus 로고    scopus 로고
    • Cytokinin-binding proteins from tobacco callus share homology with osmotin-like protein and an endochitinase
    • Kobayashi K, Fukuda M, Igarashi D, Sunaoshi M (2000) Cytokinin-binding proteins from tobacco callus share homology with osmotin-like protein and an endochitinase. Plant Cell Physiol 41: 148-157. doi:10.1093/pcp/41.2.148. PubMed: 10795308. (Pubitemid 30146831)
    • (2000) Plant and Cell Physiology , vol.41 , Issue.2 , pp. 148-157
    • Kobayashi, K.1    Fukuda, M.2    Igarashi, D.3    Sunaoshi, M.4
  • 59
    • 27944472736 scopus 로고    scopus 로고
    • In vitro and in planta interaction evidence between Nicotiana tabacum thaumatin-like protein 1 (TLP1) and Cucumber mosaic virus proteins
    • DOI 10.1007/s11103-005-2619-y
    • Kim MJ, Ham BK, Kim HR, Lee IJ, Kim YJ et al. (2005) In vitro and in planta interaction evidence between Nicotiana tabacum thaumatin-like protein 1 (TLP1) and cucumber mosaic virus proteins. Plant Mol Biol 59: 981-994. doi:10.1007/s11103-005-2619-y. PubMed: 16307370. (Pubitemid 41677680)
    • (2005) Plant Molecular Biology , vol.59 , Issue.6 , pp. 981-994
    • Kim, M.J.1    Ham, B.-K.2    Kim, H.R.3    Lee, I.-J.4    Kim, Y.J.5    Ryu, K.H.6    Park, Y.I.7    Paek, K.-H.8
  • 60
    • 0033738420 scopus 로고    scopus 로고
    • Chitinase genes responsive to cold encode antifreeze proteins in winter cereals
    • doi:10.1104/pp.124.3.1251. PubMed: 11080301
    • Yeh S, Moffatt BA, Griffith M, Xiong F, Yang DS et al. (2000) Chitinase genes responsive to cold encode antifreeze proteins in winter cereals. Plant Physiol 124: 1251-1264. doi:10.1104/pp.124.3.1251. PubMed: 11080301.
    • (2000) Plant Physiol , vol.124 , pp. 1251-1264
    • Yeh, S.1    Moffatt, B.A.2    Griffith, M.3    Xiong, F.4    Yang, D.S.5
  • 61
    • 33746106845 scopus 로고    scopus 로고
    • Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions
    • DOI 10.1038/nbt1224, PII NBT1224
    • Doxey AC, Yaish MW, Griffith M, McConkey BJ (2006) Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions. Nat Biotechnol 24: 852-855. doi:10.1038/nbt1224. PubMed: 16823370. (Pubitemid 44086628)
    • (2006) Nature Biotechnology , vol.24 , Issue.7 , pp. 852-855
    • Doxey, A.C.1    Yaish, M.W.2    Griffith, M.3    McConkey, B.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.