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Volumn 9, Issue 5, 2019, Pages

Plant defensins: types, mechanism of action and prospects of genetic engineering for enhanced disease resistance in plants

Author keywords

Disease resistance; Genetic engineering; Pathogens; Plant defensins

Indexed keywords

ALKALOID; FLAVONOID; JASMONIC ACID; LIPOSOME; MEMBRANE LIPID; PHOSPHATIDIC ACID; POLYPEPTIDE ANTIBIOTIC AGENT; REACTIVE OXYGEN METABOLITE;

EID: 85065143555     PISSN: 2190572X     EISSN: 21905738     Source Type: Journal    
DOI: 10.1007/s13205-019-1725-5     Document Type: Review
Times cited : (75)

References (112)
  • 1
    • 84855718494 scopus 로고    scopus 로고
    • Stable integration and expression of a plant defensin in tomato confers resistance to fusarium wilt
    • PID: 21844692
    • Abdallah NA, Shah D, Abbas D, Madkour M (2010) Stable integration and expression of a plant defensin in tomato confers resistance to fusarium wilt. GM Crops 1:344–350
    • (2010) GM Crops , vol.1 , pp. 344-350
    • Abdallah, N.A.1    Shah, D.2    Abbas, D.3    Madkour, M.4
  • 2
    • 34547143735 scopus 로고    scopus 로고
    • Arabidopsis thaliana plants expressing human-defensin-2 are more resistant to fungal attack: functional homology between plant and human defensins
    • COI: 1:CAS:528:DC%2BD2sXotFymtL0%3D, PID: 17340092
    • Aerts AM, Thevissen K, Bresseleers SM, Sels J, WoutersP Cammue BPA, François IEJA (2007) Arabidopsis thaliana plants expressing human-defensin-2 are more resistant to fungal attack: functional homology between plant and human defensins. Plant Cell Rep 26:1391–1398
    • (2007) Plant Cell Rep , vol.26 , pp. 1391-1398
    • Aerts, A.M.1    Thevissen, K.2    Bresseleers, S.M.3    Sels, J.4    WoutersP, C.B.P.A.5    François, I.E.J.A.6
  • 3
    • 40949112325 scopus 로고    scopus 로고
    • Plant defensins and virally encoded fungal toxin KP4 inhibit plant root growth
    • COI: 1:CAS:528:DC%2BD2sXhtlOqsLvJ, PID: 17849147
    • Allen A, Snyder AK, Preuss M, Nielsen EE, Shah DM, Smith TJ (2008) Plant defensins and virally encoded fungal toxin KP4 inhibit plant root growth. Planta 227:331–339
    • (2008) Planta , vol.227 , pp. 331-339
    • Allen, A.1    Snyder, A.K.2    Preuss, M.3    Nielsen, E.E.4    Shah, D.M.5    Smith, T.J.6
  • 4
    • 84953388634 scopus 로고    scopus 로고
    • Overexpression of a fusion defensin gene from radish and fenugreek improves resistance against leaf spot diseases caused by Cercospora arachidicola and Phaeoisariopsis personata in peanut
    • COI: 1:CAS:528:DC%2BC2sXjtFOrt7w%3D
    • Bala M, Radhakrishnan A, Kumar A, Mishra GP, Dobraia JR, Kirti PB (2016) Overexpression of a fusion defensin gene from radish and fenugreek improves resistance against leaf spot diseases caused by Cercospora arachidicola and Phaeoisariopsis personata in peanut. Turk J Biol 40:139–149
    • (2016) Turk J Biol , vol.40 , pp. 139-149
    • Bala, M.1    Radhakrishnan, A.2    Kumar, A.3    Mishra, G.P.4    Dobraia, J.R.5    Kirti, P.B.6
  • 5
    • 65349142168 scopus 로고    scopus 로고
    • Functional aspects of the solution structure and dynamics of PAF—a highly-stable anti-fungal protein from Penicillium chrysogenum
    • COI: 1:CAS:528:DC%2BD1MXmt1Cmt78%3D, PID: 19459942
    • Batta G, Barna T, Gaspari Z, Sandor S, Kover KE, Binder U et al (2009) Functional aspects of the solution structure and dynamics of PAF—a highly-stable anti-fungal protein from Penicillium chrysogenum. FEBS J 276:2875–2890
    • (2009) FEBS J , vol.276 , pp. 2875-2890
    • Batta, G.1    Barna, T.2    Gaspari, Z.3    Sandor, S.4    Kover, K.E.5    Binder, U.6
  • 6
    • 0025976182 scopus 로고
    • A new family of small (5 kD) protein inhibitors of insect alpha-amylases from seeds or sorghum (Sorghum bicolor Moench) have sequence homologies with wheat -purothionins
    • COI: 1:CAS:528:DyaK3MXit1CgsLo%3D, PID: 1995329
    • Bloch C JR, Richardson M (1991) A new family of small (5 kD) protein inhibitors of insect alpha-amylases from seeds or sorghum (Sorghum bicolor Moench) have sequence homologies with wheat -purothionins. FEBS Lett 279:101–104
    • (1991) FEBS Lett , vol.279 , pp. 101-104
    • Bloch, C.J.R.1    Richardson, M.2
  • 7
    • 0029347190 scopus 로고
    • Plant defensins: novel antimicrobial peptides as components of the host defence system
    • COI: 1:CAS:528:DyaK2MXnsVags70%3D, PID: 7659744
    • Broekaert WF, Terras FRG, Cammue BPA, Osborn RW (1995) Plant defensins: novel antimicrobial peptides as components of the host defence system. Plant Physiol 108:1353–1358
    • (1995) Plant Physiol , vol.108 , pp. 1353-1358
    • Broekaert, W.F.1    Terras, F.R.G.2    Cammue, B.P.A.3    Osborn, R.W.4
  • 8
    • 11344267777 scopus 로고    scopus 로고
    • Insect antimicrobial peptides: structures, properties and gene regulation
    • COI: 1:CAS:528:DC%2BD2MXjvVOksA%3D%3D, PID: 15638797
    • Bulet P, Stocklin R (2005) Insect antimicrobial peptides: structures, properties and gene regulation. Protein Pept Lett 12:3–11
    • (2005) Protein Pept Lett , vol.12 , pp. 3-11
    • Bulet, P.1    Stocklin, R.2
  • 9
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: from invertebrates to vertebrates
    • COI: 1:CAS:528:DC%2BD2cXjs1yjsr8%3D, PID: 15199962
    • Bulet P, Stöcklin R, Menin L (2004) Anti-microbial peptides: from invertebrates to vertebrates. Immunol Rev 198:169–184
    • (2004) Immunol Rev , vol.198 , pp. 169-184
    • Bulet, P.1    Stöcklin, R.2    Menin, L.3
  • 10
    • 34247641821 scopus 로고    scopus 로고
    • Role of plant lipid transfer proteins in plant cell physiology—a concise review
    • COI: 1:CAS:528:DC%2BD2sXkslegtbg%3D
    • Carvalho AO, Gomes VM (2007) Role of plant lipid transfer proteins in plant cell physiology—a concise review. Peptides 28:1144–1153
    • (2007) Peptides , vol.28 , pp. 1144-1153
    • Carvalho, A.O.1    Gomes, V.M.2
  • 11
    • 0037021614 scopus 로고    scopus 로고
    • A novel defensin encoded by a Mungbean cdna exhibits insecticidal activity against bruchid
    • COI: 1:CAS:528:DC%2BD38Xot1Cltro%3D, PID: 12452641
    • Chen KC, Lin CY, Kuan CC, Sung HY, Chen CS (2002) A novel defensin encoded by a Mungbean cdna exhibits insecticidal activity against bruchid. J Agric Food Chem 50:7258–7263
    • (2002) J Agric Food Chem , vol.50 , pp. 7258-7263
    • Chen, K.C.1    Lin, C.Y.2    Kuan, C.C.3    Sung, H.Y.4    Chen, C.S.5
  • 12
    • 1842783692 scopus 로고    scopus 로고
    • Cloning and Functional Expression of a Mungbean Defensin VrD1 in Pichia pastoris
    • COI: 1:CAS:528:DC%2BD2cXisFaqsbg%3D, PID: 15080630
    • Chen JJ, Chen GH, Hsu HC, Li SS, Chen CS (2004) Cloning and Functional Expression of a Mungbean Defensin VrD1 in Pichia pastoris. J Agric Food Chem 52:2256–2261
    • (2004) J Agric Food Chem , vol.52 , pp. 2256-2261
    • Chen, J.J.1    Chen, G.H.2    Hsu, H.C.3    Li, S.S.4    Chen, C.S.5
  • 13
    • 73349110946 scopus 로고    scopus 로고
    • Combined overexpression of chitinase and defensin genes in transgenic tomato enhances resistance to Botrytis cinerea
    • COI: 1:CAS:528:DC%2BD1MXhsVylu7vK
    • Chen SC, Liu AR, Wang FH, Ahammed GJ (2009) Combined overexpression of chitinase and defensin genes in transgenic tomato enhances resistance to Botrytis cinerea. Afr J Biotechnol 8(20):5182–5188
    • (2009) Afr J Biotechnol , vol.8 , Issue.20 , pp. 5182-5188
    • Chen, S.C.1    Liu, A.R.2    Wang, F.H.3    Ahammed, G.J.4
  • 14
    • 69849107757 scopus 로고    scopus 로고
    • Expression of Br D1, a plant defensin from Brassica rapa, confers resistance against brown plant hopper (Nilaparvata lugens) in transgenic rice
    • COI: 1:CAS:528:DC%2BD1MXhtVGisr3O, PID: 19714315
    • Choi MS, Kim YH, Park HM, Seo BY, Jung JK, Kim ST, Kim MC, Shin DB, Yun HT, Choi IS, Kim CK, Lee JY (2009) Expression of Br D1, a plant defensin from Brassica rapa, confers resistance against brown plant hopper (Nilaparvata lugens) in transgenic rice. Mol Cells 28:131–137
    • (2009) Mol Cells , vol.28 , pp. 131-137
    • Choi, M.S.1    Kim, Y.H.2    Park, H.M.3    Seo, B.Y.4    Jung, J.K.5    Kim, S.T.6    Kim, M.C.7    Shin, D.B.8    Yun, H.T.9    Choi, I.S.10    Kim, C.K.11    Lee, J.Y.12
  • 15
    • 80054910686 scopus 로고    scopus 로고
    • Bioinformatic and molecular characterization of beta-defensins-like peptides isolated from the green lizard Anolis carolinensis
    • COI: 1:CAS:528:DC%2BC3MXhtlOksb7J, PID: 21663758
    • Dalla Valle L, Benato F, Maistro S, Quinzani S, Alibardi L (2012) Bioinformatic and molecular characterization of beta-defensins-like peptides isolated from the green lizard Anolis carolinensis. Dev Comp Immunol 36:222–229
    • (2012) Dev Comp Immunol , vol.36 , pp. 222-229
    • Dalla Valle, L.1    Benato, F.2    Maistro, S.3    Quinzani, S.4    Alibardi, L.5
  • 16
    • 84893966233 scopus 로고    scopus 로고
    • Generation of selectable marker-free transgenic eggplant resistant to Alternaria solani using the R/RS site-specific recombination system
    • COI: 1:CAS:528:DC%2BC3sXhvFeitLrL, PID: 24311155
    • Darwish NA, Khan RS, Ntui VO, Nakamura I, Mii M (2014) Generation of selectable marker-free transgenic eggplant resistant to Alternaria solani using the R/RS site-specific recombination system. Plant Cell Rep 33:411–421
    • (2014) Plant Cell Rep , vol.33 , pp. 411-421
    • Darwish, N.A.1    Khan, R.S.2    Ntui, V.O.3    Nakamura, I.4    Mii, M.5
  • 17
    • 78651247954 scopus 로고    scopus 로고
    • Portrayal of complex dynamic properties of sugarcane defensin 5 by NMR: multiple motions associated with membrane interaction
    • PID: 21220113, COI: 1:CAS:528:DC%2BC3MXksFCkuw%3D%3D
    • de Paula VS, Razzera G, Barreto-Bergter E, Almeida FCL, Valente AP (2011) Portrayal of complex dynamic properties of sugarcane defensin 5 by NMR: multiple motions associated with membrane interaction. Structure 19:26–36
    • (2011) Structure , vol.19 , pp. 26-36
    • de Paula, V.S.1    Razzera, G.2    Barreto-Bergter, E.3    Almeida, F.C.L.4    Valente, A.P.5
  • 18
    • 0032411402 scopus 로고    scopus 로고
    • Cysteine-rich antimicrobial peptides in invertebrates
    • COI: 1:CAS:528:DyaK1MXjtFSmsbw%3D, PID: 10333738
    • Dimarcq JL, Bulet P, Hetru C, Hoffmann J (1998) Cysteine-rich antimicrobial peptides in invertebrates. Biopolymers 47:465–477
    • (1998) Biopolymers , vol.47 , pp. 465-477
    • Dimarcq, J.L.1    Bulet, P.2    Hetru, C.3    Hoffmann, J.4
  • 19
    • 79958042300 scopus 로고    scopus 로고
    • Agrobacterium-mediated transformation of tomato plants expressing defensin gene
    • COI: 1:CAS:528:DC%2BC3MXhtFakurfF
    • El-Siddig MA, El-Hussein AA, Saker MM (2011) Agrobacterium-mediated transformation of tomato plants expressing defensin gene. Inter J of Agric Res 6:323–334
    • (2011) Inter J of Agric Res , vol.6 , pp. 323-334
    • El-Siddig, M.A.1    El-Hussein, A.A.2    Saker, M.M.3
  • 20
    • 11244342346 scopus 로고    scopus 로고
    • Antibacterial activity and specificity of the six human {alpha}-defensins
    • COI: 1:CAS:528:DC%2BD2MXjvVShsQ%3D%3D, PID: 15616305
    • Ericksen B, Wu Z, Lu W, Lehrer RI (2005) Antibacterial activity and specificity of the six human {alpha}-defensins. Antimicrob Agents Chemother 49:269–275
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 269-275
    • Ericksen, B.1    Wu, Z.2    Lu, W.3    Lehrer, R.I.4
  • 21
    • 0032577318 scopus 로고    scopus 로고
    • Determination of the three-dimensional solution structure of Raphanus sativus antifungal protein 1 by 1h nmr
    • COI: 1:CAS:528:DyaK1cXjvVOkt7Y%3D, PID: 9636715
    • Fant F, Vranken W, Broekaert W, Borremans F (1998) Determination of the three-dimensional solution structure of Raphanus sativus antifungal protein 1 by 1h nmr. J Mol Biol 279:257–270
    • (1998) J Mol Biol , vol.279 , pp. 257-270
    • Fant, F.1    Vranken, W.2    Broekaert, W.3    Borremans, F.4
  • 22
    • 0032707644 scopus 로고    scopus 로고
    • The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1 H nuclear magnetic resonance
    • COI: 1:CAS:528:DyaK1MXntFOjsbo%3D, PID: 10591099
    • Fant F, Vranken WF, Borremans FAM (1999) The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1 H nuclear magnetic resonance. Proteins 37:388–403
    • (1999) Proteins , vol.37 , pp. 388-403
    • Fant, F.1    Vranken, W.F.2    Borremans, F.A.M.3
  • 23
    • 85064519620 scopus 로고    scopus 로고
    • Structural motifs in class I and class II plant defensins for phospholipid interactions:intriguing role of ligand binding and modes of action
    • Francisco GCA, Georgina E (2017) Structural motifs in class I and class II plant defensins for phospholipid interactions:intriguing role of ligand binding and modes of action. Francisco and Georgina, J Plant Physiol Pathol 5:1–7
    • (2017) Francisco and Georgina, J Plant Physiol Pathol , vol.5 , pp. 1-7
    • Francisco, G.C.A.1    Georgina, E.2
  • 24
    • 2442473461 scopus 로고    scopus 로고
    • Purification, characterization, and sequencing of a novel type of antimicrobial peptides, Fa-AMP1 and Fa-AMP2, from seeds of buckwheat (Fagopyrum esculentum Moench.)
    • COI: 1:CAS:528:DC%2BD3sXnt1Wnuro%3D
    • Fujimura M, Minami Y, Watanabe K, Tadera K (2003) Purification, characterization, and sequencing of a novel type of antimicrobial peptides, Fa-AMP1 and Fa-AMP2, from seeds of buckwheat (Fagopyrum esculentum Moench.). Biosc Biotechnol Biochem 67:1636–1642
    • (2003) Biosc Biotechnol Biochem , vol.67 , pp. 1636-1642
    • Fujimura, M.1    Minami, Y.2    Watanabe, K.3    Tadera, K.4
  • 25
    • 0141799911 scopus 로고    scopus 로고
    • Defensins antimicrobial peptides of innate immunity
    • COI: 1:CAS:528:DC%2BD3sXmvVWmtLc%3D, PID: 12949495
    • Ganz T (2003) Defensins antimicrobial peptides of innate immunity. Nat Rev Immunol 3:710–720
    • (2003) Nat Rev Immunol , vol.3 , pp. 710-720
    • Ganz, T.1
  • 26
    • 3242778563 scopus 로고    scopus 로고
    • Defensins antimicrobial peptides of vertebrates
    • COI: 1:CAS:528:DC%2BD2cXls1Wlt7s%3D, PID: 15330253
    • Ganz T (2004) Defensins antimicrobial peptides of vertebrates. C R Biol 327:539–549
    • (2004) C R Biol , vol.327 , pp. 539-549
    • Ganz, T.1
  • 27
    • 16844377323 scopus 로고    scopus 로고
    • Defensins and other antimicrobial peptides: a historical perspective and an update
    • COI: 1:CAS:528:DC%2BD2MXjtFyks7w%3D, PID: 15892623
    • Ganz T (2005) Defensins and other antimicrobial peptides: a historical perspective and an update. Comb Chem High Throughput Screen 8:209–217
    • (2005) Comb Chem High Throughput Screen , vol.8 , pp. 209-217
    • Ganz, T.1
  • 28
    • 0022402545 scopus 로고
    • Defensins: natural peptide antibiotics of human neutrophils
    • COI: 1:CAS:528:DyaL2MXlvFCrtro%3D, PID: 2997278
    • Ganz T, Selsted ME, Szklarek D, Harwig SS, Daher K, Bainton DF et al (1985) Defensins: natural peptide antibiotics of human neutrophils. J Clin Invest 76:1427–1435
    • (1985) J Clin Invest , vol.76 , pp. 1427-1435
    • Ganz, T.1    Selsted, M.E.2    Szklarek, D.3    Harwig, S.S.4    Daher, K.5    Bainton, D.F.6
  • 31
    • 84893822697 scopus 로고    scopus 로고
    • Field resistance to Fusarium oxysporum and Verticillium dahliae in transgenic cotton expressing the plant defensin NaD1
    • COI: 1:CAS:528:DC%2BC2cXltFKju7w%3D
    • Gaspar YM, McKenna JA, McGinness BS, Hinch J, Poon S, Connelly AA, Heath RL (2014) Field resistance to Fusarium oxysporum and Verticillium dahliae in transgenic cotton expressing the plant defensin NaD1. J Experiment Bot 65(6):1541–1550
    • (2014) J Experiment Bot , vol.65 , Issue.6 , pp. 1541-1550
    • Gaspar, Y.M.1    McKenna, J.A.2    McGinness, B.S.3    Hinch, J.4    Poon, S.5    Connelly, A.A.6    Heath, R.L.7
  • 32
    • 3543042528 scopus 로고    scopus 로고
    • Computational identification and characterization of novel genes from legumes
    • COI: 1:CAS:528:DC%2BD2cXmtVOrsbc%3D, PID: 15266052
    • Graham MA, Silverstein KAT, Cannon SB, VandenBosch KA (2004) Computational identification and characterization of novel genes from legumes. Plant Physiol 135:1179–1197
    • (2004) Plant Physiol , vol.135 , pp. 1179-1197
    • Graham, M.A.1    Silverstein, K.A.T.2    Cannon, S.B.3    VandenBosch, K.A.4
  • 34
    • 23744462650 scopus 로고    scopus 로고
    • Defensin gene family in Medicago truncatula: structure, expression and induction by signal molecules
    • COI: 1:CAS:528:DC%2BD2MXmt1Wns7Y%3D, PID: 16021402
    • Hanks JN, Snyder AK, Graham MA, Shah RK, Blaylock LA, Harrison MJ, Shah DM (2005) Defensin gene family in Medicago truncatula: structure, expression and induction by signal molecules. Plant Mol Biol 58:385–399
    • (2005) Plant Mol Biol , vol.58 , pp. 385-399
    • Hanks, J.N.1    Snyder, A.K.2    Graham, M.A.3    Shah, R.K.4    Blaylock, L.A.5    Harrison, M.J.6    Shah, D.M.7
  • 35
    • 84880318184 scopus 로고    scopus 로고
    • Identification and mechanism of action of the plant defensin nad1 as a new member of the antifungal drug arsenal against Candida albicans
    • COI: 1:CAS:528:DC%2BC3sXht1WgtLnP, PID: 23689717
    • Hayes BM, Bleackley MR, Wiltshire JL, Anderson MA, Traven A, van der Weerden NL (2013) Identification and mechanism of action of the plant defensin nad1 as a new member of the antifungal drug arsenal against Candida albicans. Antimicrob Agents Chemother 57:3667–3675
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 3667-3675
    • Hayes, B.M.1    Bleackley, M.R.2    Wiltshire, J.L.3    Anderson, M.A.4    Traven, A.5    van der Weerden, N.L.6
  • 36
    • 0026738576 scopus 로고
    • Insect defensins: inducible antibacterial peptides
    • COI: 1:CAS:528:DyaK3sXltFan, PID: 1418378
    • Hoffmann JA, Hetru C (1992) Insect defensins: inducible antibacterial peptides. Immunol Today 13:411–415
    • (1992) Immunol Today , vol.13 , pp. 411-415
    • Hoffmann, J.A.1    Hetru, C.2
  • 37
    • 84860604740 scopus 로고    scopus 로고
    • Agri-environment scheme enhancing ecosystem services: a demonstration of improved biological control in cereal crops
    • Holland JM, Oaten H, Moreby S, Birkett T, Simper J, Southway S, Smith BM (2012) Agri-environment scheme enhancing ecosystem services: a demonstration of improved biological control in cereal crops. Agric Ecosyst Environ 155:147–152
    • (2012) Agric Ecosyst Environ , vol.155 , pp. 147-152
    • Holland, J.M.1    Oaten, H.2    Moreby, S.3    Birkett, T.4    Simper, J.5    Southway, S.6    Smith, B.M.7
  • 38
    • 44349167842 scopus 로고    scopus 로고
    • Antimicrobial, dehydroascorbate reductase, and monodehydroascorbate reductase activities of defensin from sweet potato [ipomoea batatas (l.) lam. ‘Tainong 57’] storage roots
    • COI: 1:CAS:528:DC%2BD1cXksVShtbo%3D, PID: 18393437
    • Huang GJ, Lai HC, Chang YS, Sheu MJ, Lu TL, Huang SS, Lin YH (2008) Antimicrobial, dehydroascorbate reductase, and monodehydroascorbate reductase activities of defensin from sweet potato [ipomoea batatas (l.) lam. ‘Tainong 57'] storage roots. J Agric Food Chem 56:2989–2995
    • (2008) J Agric Food Chem , vol.56 , pp. 2989-2995
    • Huang, G.J.1    Lai, H.C.2    Chang, Y.S.3    Sheu, M.J.4    Lu, T.L.5    Huang, S.S.6    Lin, Y.H.7
  • 39
    • 0037826923 scopus 로고    scopus 로고
    • Structure of Petunia hybrid defensin 1, a novel plant defensin with five disulfide bonds
    • COI: 1:CAS:528:DC%2BD3sXks12nu74%3D
    • Janssen BJ, Schirra HJ, Lay FT, Anderson MA, Craik DJ (2003) Structure of Petunia hybrid defensin 1, a novel plant defensin with five disulfide bonds. Biochem 42:8214–8222
    • (2003) Biochem , vol.42 , pp. 8214-8222
    • Janssen, B.J.1    Schirra, H.J.2    Lay, F.T.3    Anderson, M.A.4    Craik, D.J.5
  • 41
    • 77952241898 scopus 로고    scopus 로고
    • Expression of a plant defensin in rice confers resistance to fungal phytopathogens
    • COI: 1:CAS:528:DC%2BC3cXls12hsr4%3D, PID: 19690975
    • Jha S, Chattoo BB (2010) Expression of a plant defensin in rice confers resistance to fungal phytopathogens. Transgenic Res 19:373–384
    • (2010) Transgenic Res , vol.19 , pp. 373-384
    • Jha, S.1    Chattoo, B.B.2
  • 42
    • 84941940731 scopus 로고    scopus 로고
    • Application of antimicrobial peptides for disease control in plants
    • Jung YJ, Kang KK (2014) Application of antimicrobial peptides for disease control in plants. Plant Breed Biotech 1:1–13
    • (2014) Plant Breed Biotech , vol.1 , pp. 1-13
    • Jung, Y.J.1    Kang, K.K.2
  • 43
    • 85050958497 scopus 로고    scopus 로고
    • Structural and biological features of a novel plant defensin from Brugmansia x candida
    • COI: 1:CAS:528:DC%2BC1cXit1emsbbJ
    • Kaewklom S, Wongchai M, Petvises S, Hanpithakphong W, Aunpad R (2018) Structural and biological features of a novel plant defensin from Brugmansia x candida. PLoS One 13(8):201668
    • (2018) PLoS One , vol.13 , Issue.8
    • Kaewklom, S.1    Wongchai, M.2    Petvises, S.3    Hanpithakphong, W.4    Aunpad, R.5
  • 44
    • 0036949921 scopus 로고    scopus 로고
    • Overexpression of the wasabi defensin gene confers enhanced resistance to blast fungus (Magnaporthe grisea) in transgenic rice
    • COI: 1:CAS:528:DC%2BD38XosVCnt7s%3D, PID: 12582903
    • Kanzaki H, Nirasawa S, Saitoh H (2002) Overexpression of the wasabi defensin gene confers enhanced resistance to blast fungus (Magnaporthe grisea) in transgenic rice. Theor Appl Genet 105:809–814
    • (2002) Theor Appl Genet , vol.105 , pp. 809-814
    • Kanzaki, H.1    Nirasawa, S.2    Saitoh, H.3
  • 45
    • 0036380501 scopus 로고    scopus 로고
    • Enhanced quantitative resistance to Laptosphaeria maculans conferred by expression of a novel antimicrobial peptide in canola (Brassica napus L.)
    • COI: 1:CAS:528:DC%2BD38Xnt1aht78%3D
    • Kazan K, Rusu A, Marcus JP, Goulter KC, Manners JM (2002) Enhanced quantitative resistance to Laptosphaeria maculans conferred by expression of a novel antimicrobial peptide in canola (Brassica napus L.). Mol Breed 10:63–70
    • (2002) Mol Breed , vol.10 , pp. 63-70
    • Kazan, K.1    Rusu, A.2    Marcus, J.P.3    Goulter, K.C.4    Manners, J.M.5
  • 46
    • 33645849555 scopus 로고    scopus 로고
    • Transgenic Potatoes expressing wasabi defensin peptide confer partial resistance to gray mold (Botrytis cinerea)
    • Khan RS, Nishihara M, Yamamura S, Nakamura I, Mii M (2006) Transgenic Potatoes expressing wasabi defensin peptide confer partial resistance to gray mold (Botrytis cinerea). Plant Biotechnol 23:179–183
    • (2006) Plant Biotechnol , vol.23 , pp. 179-183
    • Khan, R.S.1    Nishihara, M.2    Yamamura, S.3    Nakamura, I.4    Mii, M.5
  • 47
    • 64749115376 scopus 로고    scopus 로고
    • Production of transgenic potato exhibiting enhanced resistance to fungal infection and herbicide applications
    • Khan RS, Sjahril R, Nakamura I, Mii M (2008) Production of transgenic potato exhibiting enhanced resistance to fungal infection and herbicide applications. Plant Biotechnol Rep 2:13–20
    • (2008) Plant Biotechnol Rep , vol.2 , pp. 13-20
    • Khan, R.S.1    Sjahril, R.2    Nakamura, I.3    Mii, M.4
  • 48
    • 79952704512 scopus 로고    scopus 로고
    • Production of marker-Free disease-resistant potato using isopentenyl transferase gene as a positive selection marker
    • COI: 1:CAS:528:DC%2BC3MXjtFagt7k%3D, PID: 21184230
    • Khan RS, Ntui VO, Chin DP, Nakamura I, Mii M (2011) Production of marker-Free disease-resistant potato using isopentenyl transferase gene as a positive selection marker. Plant Cell Rep 30:587–597
    • (2011) Plant Cell Rep , vol.30 , pp. 587-597
    • Khan, R.S.1    Ntui, V.O.2    Chin, D.P.3    Nakamura, I.4    Mii, M.5
  • 49
    • 79955933724 scopus 로고    scopus 로고
    • Development of disease resistant marker-free tomato by R/RS site-specific recombination
    • COI: 1:CAS:528:DC%2BC3MXlvFWjsLo%3D, PID: 21293863
    • Khan RS, Nakamura I, Mii M (2011) Development of disease resistant marker-free tomato by R/RS site-specific recombination. Plant Cell Rep 30:1041–1053
    • (2011) Plant Cell Rep , vol.30 , pp. 1041-1053
    • Khan, R.S.1    Nakamura, I.2    Mii, M.3
  • 50
    • 84905907467 scopus 로고    scopus 로고
    • Retransformation of marker-free potato for enhanced resistance against fungal pathogens by pyramiding chitinase and Wasabi Defensin Genes
    • COI: 1:CAS:528:DC%2BC2cXnslWkuro%3D, PID: 24802621
    • Khan RS, Darwish NA, Khattak B, Ntui V, Kong K, Shimomae K et al (2014) Retransformation of marker-free potato for enhanced resistance against fungal pathogens by pyramiding chitinase and Wasabi Defensin Genes. Mol Biotechnol 56:814–823
    • (2014) Mol Biotechnol , vol.56 , pp. 814-823
    • Khan, R.S.1    Darwish, N.A.2    Khattak, B.3    Ntui, V.4    Kong, K.5    Shimomae, K.6
  • 51
    • 33748569152 scopus 로고    scopus 로고
    • Defensin a multifunctional molecule lives up to its versatile name
    • COI: 1:CAS:528:DC%2BD28Xps1Wlsbc%3D, PID: 16908156
    • Kim C, Kaufmann SH (2006) Defensin a multifunctional molecule lives up to its versatile name. Trends Microbiol 14:428–431
    • (2006) Trends Microbiol , vol.14 , pp. 428-431
    • Kim, C.1    Kaufmann, S.H.2
  • 52
    • 84903524638 scopus 로고    scopus 로고
    • Transgenic tobacco and tomato plants expressing Wasabi defensin genes driven by root-specific LjNRT2 and AtNRT2. 1 promoters confer resistance against Fusarium oxysporum
    • COI: 1:CAS:528:DC%2BC2cXitFaqu7%2FK
    • Kong K, Ntui VO, Makabe S, Khan RS, Mii M et al (2014) Transgenic tobacco and tomato plants expressing Wasabi defensin genes driven by root-specific LjNRT2 and AtNRT2. 1 promoters confer resistance against Fusarium oxysporum. Plant Biotechnol 31:89–96
    • (2014) Plant Biotechnol , vol.31 , pp. 89-96
    • Kong, K.1    Ntui, V.O.2    Makabe, S.3    Khan, R.S.4    Mii, M.5
  • 54
    • 13844322064 scopus 로고    scopus 로고
    • Defensins-components of the innate immune system in plants
    • COI: 1:CAS:528:DC%2BD2MXhsVWqtb8%3D
    • Lay FT, Anderson M (2005) Defensins-components of the innate immune system in plants. Curr Pro Pep Sci 6:85–101
    • (2005) Curr Pro Pep Sci , vol.6 , pp. 85-101
    • Lay, F.T.1    Anderson, M.2
  • 55
    • 0346665520 scopus 로고    scopus 로고
    • Isolation and properties of floral defensins from ornamental tobacco and petunia
    • COI: 1:CAS:528:DC%2BD3sXisFels74%3D, PID: 12644678
    • Lay FT, Brugliera F, Anderson MA (2003) Isolation and properties of floral defensins from ornamental tobacco and petunia. Plant Physiol 131:1283–1293
    • (2003) Plant Physiol , vol.131 , pp. 1283-1293
    • Lay, F.T.1    Brugliera, F.2    Anderson, M.A.3
  • 56
    • 84862017137 scopus 로고    scopus 로고
    • Dimerization of plant defensin NaD1 enhances its antifungal activity
    • COI: 1:CAS:528:DC%2BC38Xot1Kjsbw%3D, PID: 22511788
    • Lay FT, Mills GD, Poon IKH, Cowieson NP, Kirby N, Baxter AA et al (2012) Dimerization of plant defensin NaD1 enhances its antifungal activity. J Biol Chem 287:19961–19972
    • (2012) J Biol Chem , vol.287 , pp. 19961-19972
    • Lay, F.T.1    Mills, G.D.2    Poon, I.K.H.3    Cowieson, N.P.4    Kirby, N.5    Baxter, A.A.6
  • 58
    • 4444246692 scopus 로고    scopus 로고
    • Primate defensins
    • COI: 1:CAS:528:DC%2BD2cXnt1CntLk%3D, PID: 15372083
    • Lehrer RI (2004) Primate defensins. Nat Rev Microbiol 2:727–738
    • (2004) Nat Rev Microbiol , vol.2 , pp. 727-738
    • Lehrer, R.I.1
  • 59
    • 79952984045 scopus 로고    scopus 로고
    • Expression of a radish defensin in transgenic wheat confers increased resistance to Fusarium graminearum and Rhizoctonia cerealis
    • COI: 1:CAS:528:DC%2BC3MXivFClur8%3D, PID: 21279533
    • Li Z, Zhou M, Zhang Z, Ren L, Du L, Zhang B, Xu H, Xin Z (2011) Expression of a radish defensin in transgenic wheat confers increased resistance to Fusarium graminearum and Rhizoctonia cerealis. Funct Integr Genomics 11:63–70
    • (2011) Funct Integr Genomics , vol.11 , pp. 63-70
    • Li, Z.1    Zhou, M.2    Zhang, Z.3    Ren, L.4    Du, L.5    Zhang, B.6    Xu, H.7    Xin, Z.8
  • 60
    • 0032548181 scopus 로고    scopus 로고
    • Structure and mapping of the human β-defensin 2 gene and its expression at sites of inflammation
    • COI: 1:CAS:528:DyaK1cXotV2hu70%3D, PID: 9831658
    • Liu L, Wang L, Jia HP, Zhao C, Heng HHQ, Schutte BC, McCray PB, Ganz T (1998) Structure and mapping of the human β-defensin 2 gene and its expression at sites of inflammation. Gene 222:237–244
    • (1998) Gene , vol.222 , pp. 237-244
    • Liu, L.1    Wang, L.2    Jia, H.P.3    Zhao, C.4    Heng, H.H.Q.5    Schutte, B.C.6    McCray, P.B.7    Ganz, T.8
  • 61
    • 0025670589 scopus 로고
    • Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, γ-hordothionin, from barley endosperm
    • COI: 1:CAS:528:DyaK3MXhtlyhtrY%3D
    • Mendez E, Moreno A, Colilla F, Pelaez F, Limas GG, Mendez R, Soriano F, Salinas M, Haro C (1990) Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, γ-hordothionin, from barley endosperm. Euro J Biochem 194:533–539
    • (1990) Euro J Biochem , vol.194 , pp. 533-539
    • Mendez, E.1    Moreno, A.2    Colilla, F.3    Pelaez, F.4    Limas, G.G.5    Mendez, R.6    Soriano, F.7    Salinas, M.8    Haro, C.9
  • 63
    • 84904384965 scopus 로고    scopus 로고
    • Vv-AMP2, a grapevine flower specific defensin capable of Botrytis cinerea growth inhibition: insights into its mode of action
    • COI: 1:CAS:528:DC%2BC2cXhtFOltbfM
    • Nanni V, Schumacher J, Giacomelli L et al (2014) Vv-AMP2, a grapevine flower specific defensin capable of Botrytis cinerea growth inhibition: insights into its mode of action. Plant Pathol 63:899–910
    • (2014) Plant Pathol , vol.63 , pp. 899-910
    • Nanni, V.1    Schumacher, J.2    Giacomelli, L.3
  • 64
    • 77955774480 scopus 로고    scopus 로고
    • Stable integration and expression of wasabi defensin gene in “Egusi” melon (Colocynthis citrullus L.) confers resistance to Fusarium wilt and Alternaria leaf spot
    • COI: 1:CAS:528:DC%2BC3cXhtVahur%2FI, PID: 20552202
    • Ntui VO, Thirukkumaran G, Azadi P, Khan RS, NakamuraI Mii M (2010) Stable integration and expression of wasabi defensin gene in “Egusi” melon (Colocynthis citrullus L.) confers resistance to Fusarium wilt and Alternaria leaf spot. Plant Cell Rep 29:943–954
    • (2010) Plant Cell Rep , vol.29 , pp. 943-954
    • Ntui, V.O.1    Thirukkumaran, G.2    Azadi, P.3    Khan, R.S.4    NakamuraI, M.M.5
  • 65
    • 79952087458 scopus 로고    scopus 로고
    • Increased resistance to fusarium wilt in transgenic tobacco lines co-expressing chitinase and wasabi defensin genes
    • COI: 1:CAS:528:DC%2BC3MXkvVGrtb0%3D
    • Ntui VO, Azadi P, Thirukkumaran G, Khan RS, Chin DP, Nakamura I, Mii M (2011) Increased resistance to fusarium wilt in transgenic tobacco lines co-expressing chitinase and wasabi defensin genes. Plant Pathol 60:221–231
    • (2011) Plant Pathol , vol.60 , pp. 221-231
    • Ntui, V.O.1    Azadi, P.2    Thirukkumaran, G.3    Khan, R.S.4    Chin, D.P.5    Nakamura, I.6    Mii, M.7
  • 69
    • 57349188418 scopus 로고    scopus 로고
    • Novel insights on the mechanism of action of alpha-amylase inhibitors from the plant defensin family
    • COI: 1:CAS:528:DC%2BD1cXhtlCgsbvE, PID: 18498107
    • Pelegrini PB, Lay FT, Murad AM, Anderson MA, Franco OL (2008) Novel insights on the mechanism of action of alpha-amylase inhibitors from the plant defensin family. Proteins 73:719–729
    • (2008) Proteins , vol.73 , pp. 719-729
    • Pelegrini, P.B.1    Lay, F.T.2    Murad, A.M.3    Anderson, M.A.4    Franco, O.L.5
  • 70
    • 84891569071 scopus 로고    scopus 로고
    • Antimicrobial peptides: their history, evolution, and functional promiscuity
    • Wiley, Weinheim
    • Phoenix DA, Dennison SR, Harris F (2013) Antimicrobial peptides: their history, evolution, and functional promiscuity. Antimicrobial Peptides. Wiley, Weinheim, pp 1–38
    • (2013) Antimicrobial Peptides , pp. 1-38
    • Phoenix, D.A.1    Dennison, S.R.2    Harris, F.3
  • 72
    • 50249123189 scopus 로고    scopus 로고
    • Neutrophil-derived defensins as modulators of innate immune function
    • COI: 1:CAS:528:DC%2BD1cXhtFegurjL, PID: 19024344
    • Rehaume L, Hancock RE (2008) Neutrophil-derived defensins as modulators of innate immune function. Crit Rev Immunol 28:185–200
    • (2008) Crit Rev Immunol , vol.28 , pp. 185-200
    • Rehaume, L.1    Hancock, R.E.2
  • 73
    • 19444366409 scopus 로고    scopus 로고
    • On the evolution of invertebrate defensins
    • COI: 1:CAS:528:DC%2BD2MXks1Cmsbs%3D, PID: 15922831
    • Rodriguez de la Vega RC, Possani LD (2005) On the evolution of invertebrate defensins. Trends Genet 21:330–332
    • (2005) Trends Genet , vol.21 , pp. 330-332
    • Rodriguez de la Vega, R.C.1    Possani, L.D.2
  • 74
    • 0035403871 scopus 로고    scopus 로고
    • Antifungal proteins
    • COI: 1:CAS:528:DC%2BD3MXkvFSnt7g%3D, PID: 11425698
    • Selitrennikoff CP (2001) Antifungal proteins. Appl Environ Microbiol 67:2883–2894
    • (2001) Appl Environ Microbiol , vol.67 , pp. 2883-2894
    • Selitrennikoff, C.P.1
  • 75
    • 4444341077 scopus 로고    scopus 로고
    • Theta-defensins: cyclic antimicrobial peptides produced by binary ligation of truncated alpha-defensins
    • COI: 1:CAS:528:DC%2BD2cXnsFGjur4%3D, PID: 15544531
    • Selsted ME (2004) Theta-defensins: cyclic antimicrobial peptides produced by binary ligation of truncated alpha-defensins. Curr Protein Pept Sci 5(5):365–367
    • (2004) Curr Protein Pept Sci , vol.5 , Issue.5 , pp. 365-367
    • Selsted, M.E.1
  • 76
    • 35348940762 scopus 로고    scopus 로고
    • Defensins and Paneth cells in inflammatory bowel disease
    • PID: 17567878
    • Shi J (2007) Defensins and Paneth cells in inflammatory bowel disease. Inflamm Bowel Dis 13:1284–1292
    • (2007) Inflamm Bowel Dis , vol.13 , pp. 1284-1292
    • Shi, J.1
  • 77
    • 26944500600 scopus 로고    scopus 로고
    • Genome organization of more than 300 defensin-like genes in Arabidopsis
    • COI: 1:CAS:528:DC%2BD2MXmtVaqurg%3D, PID: 15955924
    • Silverstein KA, Graham MA, Paape TD, VandenBosch KA (2005) Genome organization of more than 300 defensin-like genes in Arabidopsis. Plant Physiol 138(2):600–610
    • (2005) Plant Physiol , vol.138 , Issue.2 , pp. 600-610
    • Silverstein, K.A.1    Graham, M.A.2    Paape, T.D.3    VandenBosch, K.A.4
  • 78
    • 33645960442 scopus 로고    scopus 로고
    • Antimicrobial peptides with unusual amino acid compositions and unusual structures
    • COI: 1:CAS:528:DC%2BD28XisVWjsLc%3D, PID: 16529559
    • Sitaram N (2006) Antimicrobial peptides with unusual amino acid compositions and unusual structures. Curr Med Chem 13:679–696
    • (2006) Curr Med Chem , vol.13 , pp. 679-696
    • Sitaram, N.1
  • 79
    • 33645881095 scopus 로고    scopus 로고
    • Transgenic Phalaenopsis plants with resistance to Erwinia carotovora produced by introducing wasabi defensin gene using Agrobacterium method
    • COI: 1:CAS:528:DC%2BD28XktlSmsbw%3D
    • Sjahril R, Chin DP, Khan RS, Yamamura S, Nakamura I, Amemiya Y, Mii M (2006) Transgenic Phalaenopsis plants with resistance to Erwinia carotovora produced by introducing wasabi defensin gene using Agrobacterium method. Plant Biotech 23:191–194
    • (2006) Plant Biotech , vol.23 , pp. 191-194
    • Sjahril, R.1    Chin, D.P.2    Khan, R.S.3    Yamamura, S.4    Nakamura, I.5    Amemiya, Y.6    Mii, M.7
  • 80
    • 16644369026 scopus 로고    scopus 로고
    • Purification, characterization and preliminary crystallographic studies of a novel plant defensin from Pachyrrhizu serosus seeds
    • PID: 15159575, COI: 1:CAS:528:DC%2BD2cXkt1Wisr4%3D
    • Song X, Zhou Z, Wang J, Wu F, Gong W (2004) Purification, characterization and preliminary crystallographic studies of a novel plant defensin from Pachyrrhizu serosus seeds. Acta Crystallogr D Biol Crystallogr 60:1121–1124
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1121-1124
    • Song, X.1    Zhou, Z.2    Wang, J.3    Wu, F.4    Gong, W.5
  • 81
    • 78651349903 scopus 로고    scopus 로고
    • Ultra-high resolution crystal structure of a dimeric defensin SPE10
    • COI: 1:CAS:528:DC%2BC3MXnsFWntA%3D%3D, PID: 21192931
    • Song X, Zhang M, Zhou Z, Gong W (2011) Ultra-high resolution crystal structure of a dimeric defensin SPE10. FEBS Lett 585:300–306
    • (2011) FEBS Lett , vol.585 , pp. 300-306
    • Song, X.1    Zhang, M.2    Zhou, Z.3    Gong, W.4
  • 82
    • 4444295137 scopus 로고    scopus 로고
    • Differential Antifungal and Calcium Channel-Blocking Activity among Structurally Related Plant Defensins
    • COI: 1:CAS:528:DC%2BD2cXnt1GgsrY%3D, PID: 15299136
    • Spelbrink RG, Dilmac N, Allen A, Smith TJ, Shah DM, Hockerman GH (2004) Differential Antifungal and Calcium Channel-Blocking Activity among Structurally Related Plant Defensins. Plant Physiol 135(4):2055–2067
    • (2004) Plant Physiol , vol.135 , Issue.4 , pp. 2055-2067
    • Spelbrink, R.G.1    Dilmac, N.2    Allen, A.3    Smith, T.J.4    Shah, D.M.5    Hockerman, G.H.6
  • 83
    • 77954043686 scopus 로고    scopus 로고
    • Plant defensins: defense, development and application
    • COI: 1:CAS:528:DC%2BC3cXms1aju7Y%3D, PID: 20009545
    • Stotz HU, Thomson J, Wang Y (2009) Plant defensins: defense, development and application. Plant Signal Behav 4:1010–1012
    • (2009) Plant Signal Behav , vol.4 , pp. 1010-1012
    • Stotz, H.U.1    Thomson, J.2    Wang, Y.3
  • 84
    • 54049126446 scopus 로고    scopus 로고
    • Transgenic tobacco and peanut plants expressing a mustard defensin show resistance to fungal pathogens
    • COI: 1:CAS:528:DC%2BD1cXht1ChtbbE, PID: 18758784
    • Swathi Anuradha T, Divya K, Jami SK, Kirti PB (2008) Transgenic tobacco and peanut plants expressing a mustard defensin show resistance to fungal pathogens. Plant Cell Rep 27:1777
    • (2008) Plant Cell Rep , vol.27 , pp. 1777
    • Swathi Anuradha, T.1    Divya, K.2    Jami, S.K.3    Kirti, P.B.4
  • 87
    • 0001469527 scopus 로고
    • In vitro antifungal activity of a radish (Raphanus sativus L.) seed protein homologous to nonspecific lipid transfer proteins
    • COI: 1:CAS:528:DyaK38XmsVymu7o%3D, PID: 16653017
    • Terras FR, Goderis IJ, Van Leuven F, Vanderleyden J, Cammue BP, Broekaert WF (1992) In vitro antifungal activity of a radish (Raphanus sativus L.) seed protein homologous to nonspecific lipid transfer proteins. Plant Physiol 100:1055–1058
    • (1992) Plant Physiol , vol.100 , pp. 1055-1058
    • Terras, F.R.1    Goderis, I.J.2    Van Leuven, F.3    Vanderleyden, J.4    Cammue, B.P.5    Broekaert, W.F.6
  • 88
  • 89
    • 0027132885 scopus 로고
    • Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors
    • COI: 1:CAS:528:DyaK2cXltVajsA%3D%3D, PID: 12232024
    • Terras FRG, Schoofs HME, Thevissen K, Osborn R, Vanderleyden J, Cammue BPA, Broekaert WF (1993) Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors. Plant Physiol 103:1311–1319
    • (1993) Plant Physiol , vol.103 , pp. 1311-1319
    • Terras, F.R.G.1    Schoofs, H.M.E.2    Thevissen, K.3    Osborn, R.4    Vanderleyden, J.5    Cammue, B.P.A.6    Broekaert, W.F.7
  • 92
    • 0033981958 scopus 로고    scopus 로고
    • Specific binding sites for an antifungal plant defensin from dahlia (Dahlia merckii) on fungal cells are required for antifungal activity
    • COI: 1:CAS:528:DC%2BD3cXislSgsg%3D%3D, PID: 10656585
    • Thevissen K, Osborn RW, Acland DP, Broekaert WF (2000) Specific binding sites for an antifungal plant defensin from dahlia (Dahlia merckii) on fungal cells are required for antifungal activity. Mol Plant Microbe Interact 13:54–61
    • (2000) Mol Plant Microbe Interact , vol.13 , pp. 54-61
    • Thevissen, K.1    Osborn, R.W.2    Acland, D.P.3    Broekaert, W.F.4
  • 93
    • 12944249531 scopus 로고    scopus 로고
    • A gene encoding a sphingolipid biosynthesis enzyme determines the sensitivity of Saccharomyces cerevisiae to an antifungal plant defensin from dahlia (Dahlia merckii)
    • COI: 1:CAS:528:DC%2BD3cXmtVensb4%3D
    • Thevissen K, Cammue BP, Lemaire K, Winderickx J, Dickson RC, Lester RL, Ferket KK, Van Even F, Parret AH, Broekaert WF (2000) A gene encoding a sphingolipid biosynthesis enzyme determines the sensitivity of Saccharomyces cerevisiae to an antifungal plant defensin from dahlia (Dahlia merckii). Proceed Nat Acad Sci 97:9531–9536
    • (2000) Proceed Nat Acad Sci , vol.97 , pp. 9531-9536
    • Thevissen, K.1    Cammue, B.P.2    Lemaire, K.3    Winderickx, J.4    Dickson, R.C.5    Lester, R.L.6    Ferket, K.K.7    Van Even, F.8    Parret, A.H.9    Broekaert, W.F.10
  • 95
    • 0036886964 scopus 로고    scopus 로고
    • Plant defensins
    • COI: 1:CAS:528:DC%2BD3sXktFOjug%3D%3D, PID: 12447532
    • Thomma BP, Cammue BP, Thevissen K (2002) Plant defensins. Planta 216:193–202
    • (2002) Planta , vol.216 , pp. 193-202
    • Thomma, B.P.1    Cammue, B.P.2    Thevissen, K.3
  • 96
    • 44449149173 scopus 로고    scopus 로고
    • Expression of a synthetic Cry1EC gene for resistance against Spodoptera litura in transgenic peanut (Arachis hypogaea L.)
    • COI: 1:CAS:528:DC%2BD1cXmtFemsrw%3D, PID: 18320194
    • Tiwari S, Mishra DK, Singh A, Singh PK, Tuli R (2008) Expression of a synthetic Cry1EC gene for resistance against Spodoptera litura in transgenic peanut (Arachis hypogaea L.). Plant Cell Rep 27:1017–1025
    • (2008) Plant Cell Rep , vol.27 , pp. 1017-1025
    • Tiwari, S.1    Mishra, D.K.2    Singh, A.3    Singh, P.K.4    Tuli, R.5
  • 97
    • 47249102056 scopus 로고    scopus 로고
    • The plant defensin, nad1, enters the cytoplasm of Fusarium oxysporum hyphae
    • PID: 18339623, COI: 1:CAS:528:DC%2BD1cXlvFyjs7g%3D
    • Van der Weerden NL, Lay FT, Anderson MA (2008) The plant defensin, nad1, enters the cytoplasm of Fusarium oxysporum hyphae. J Biol Chem 283:14445–14452
    • (2008) J Biol Chem , vol.283 , pp. 14445-14452
    • Van der Weerden, N.L.1    Lay, F.T.2    Anderson, M.A.3
  • 98
    • 84953418627 scopus 로고    scopus 로고
    • Expression, affinity purification, and functional characterization of recombinant fusion gene. World Congress on Biotechnol (21–23 March 2011)
    • Vasavirama K, Kirti PB (2011) Expression, affinity purification, and functional characterization of recombinant fusion gene. World Congress on Biotechnol (21–23 March 2011). J Microbial Biochem Technol S1(013): 35.
    • (2011) J Microbial Biochem Technol , Issue.13 , pp. 35
    • Vasavirama, K.1    Kirti, P.B.2
  • 99
    • 84888128035 scopus 로고    scopus 로고
    • Constitutive expression of a fusion gene comprising Trigonella foenum-graecum defensin (Tfgd2) and Raphanus sativus antifungal protein (RsAFP2) confers enhanced disease and insect resistance in transgenic tobacco
    • COI: 1:CAS:528:DC%2BC3sXht1GmurrF
    • Vasavirama K, Kirti PB (2013) Constitutive expression of a fusion gene comprising Trigonella foenum-graecum defensin (Tfgd2) and Raphanus sativus antifungal protein (RsAFP2) confers enhanced disease and insect resistance in transgenic tobacco. Plant Cell Tiss Org Cult 115:309–319
    • (2013) Plant Cell Tiss Org Cult , vol.115 , pp. 309-319
    • Vasavirama, K.1    Kirti, P.B.2
  • 100
    • 85047082639 scopus 로고    scopus 로고
    • Modes of Action of a Bi-domain Plant Defensin MtDef5 Against a Bacterial Pathogen Xanthomonas campestris
    • Velivelli SLS, Islam KT, Hobson E, Shah DM (2018) Modes of Action of a Bi-domain Plant Defensin MtDef5 Against a Bacterial Pathogen Xanthomonas campestris. Front Microbiol 9:934. 10.3389/fmicb.2018.00934
    • (2018) Front Microbiol , vol.9 , pp. 934
    • Velivelli, S.L.S.1    Islam, K.T.2    Hobson, E.3    Shah, D.M.4
  • 101
    • 84906674840 scopus 로고    scopus 로고
    • Antifungal Plant Defensins: Mechanisms of Action and Production
    • PID: 25153857, COI: 1:CAS:528:DC%2BC2cXhs1GhsbvM
    • Vriens K, Bruno PA, Cammue BP, Thevissen K (2014) Antifungal Plant Defensins: Mechanisms of Action and Production. Molecules 19:12280–12303
    • (2014) Molecules , vol.19 , pp. 12280-12303
    • Vriens, K.1    Bruno, P.A.2    Cammue, B.P.3    Thevissen, K.4
  • 102
    • 0032913664 scopus 로고    scopus 로고
    • Constitutive expression of pea defense gene DRR206 confers resistance to blackleg (Leptosphaeria maculans) disease in transgenic canola (Brassica napus)
    • COI: 1:CAS:528:DyaK1MXivVektLg%3D
    • Wang Y, Nowak G, Culley D, Hadwiger LA, Fristensky B (1999) Constitutive expression of pea defense gene DRR206 confers resistance to blackleg (Leptosphaeria maculans) disease in transgenic canola (Brassica napus). Mol Plant-Microbe Interact 12:410–418
    • (1999) Mol Plant-Microbe Interact , vol.12 , pp. 410-418
    • Wang, Y.1    Nowak, G.2    Culley, D.3    Hadwiger, L.A.4    Fristensky, B.5
  • 103
    • 0034613541 scopus 로고    scopus 로고
    • Defense proteins from seed of Cassia fistula include a lipid transfer protein homologue and a protease inhibitory plant defensin
    • COI: 1:CAS:528:DC%2BD3cXovFSltrc%3D, PID: 11074277
    • Wijaya R, Neumann GM, Condron R, Hughes AB, Polya GM (2000) Defense proteins from seed of Cassia fistula include a lipid transfer protein homologue and a protease inhibitory plant defensin. Plant Sci 159:243–255
    • (2000) Plant Sci , vol.159 , pp. 243-255
    • Wijaya, R.1    Neumann, G.M.2    Condron, R.3    Hughes, A.B.4    Polya, G.M.5
  • 104
    • 77958085274 scopus 로고    scopus 로고
    • Describing the mechanism of antimicrobial peptide action with the interfacial activity model
    • COI: 1:CAS:528:DC%2BC3cXhtVGgsLbF
    • Wimley WC (2010) Describing the mechanism of antimicrobial peptide action with the interfacial activity model. ACS ChemBiol 10:905–917
    • (2010) ACS ChemBiol , vol.10 , pp. 905-917
    • Wimley, W.C.1
  • 105
    • 36248957133 scopus 로고    scopus 로고
    • A review of defensins of diverse origins
    • COI: 1:CAS:528:DC%2BD2sXhtlSisbzO
    • Wong JH, Xia L, Ng T (2007) A review of defensins of diverse origins. Curr Prot Peptide Sci 8:446–459
    • (2007) Curr Prot Peptide Sci , vol.8 , pp. 446-459
    • Wong, J.H.1    Xia, L.2    Ng, T.3
  • 106
    • 0030899690 scopus 로고    scopus 로고
    • Crystal structure of Ser-22/Ile-25 form crambin confirms solvent, side chain substate correlations
    • COI: 1:CAS:528:DyaK2sXisFOmsbg%3D, PID: 9092482
    • Yamano A, Heo NH, Teeter MM (1997) Crystal structure of Ser-22/Ile-25 form crambin confirms solvent, side chain substate correlations. J Biol Chem 272:9597–9600
    • (1997) J Biol Chem , vol.272 , pp. 9597-9600
    • Yamano, A.1    Heo, N.H.2    Teeter, M.M.3
  • 107
    • 0036606951 scopus 로고    scopus 로고
    • Mammalian defensins in immunity: more than just microbicidal
    • COI: 1:CAS:528:DC%2BD38XksF2hu7s%3D, PID: 12072367
    • Yang D, Biragyn A, Kwak LW, Oppenheim JJ (2002) Mammalian defensins in immunity: more than just microbicidal. Trends Immunol 23:291–296
    • (2002) Trends Immunol , vol.23 , pp. 291-296
    • Yang, D.1    Biragyn, A.2    Kwak, L.W.3    Oppenheim, J.J.4
  • 108
    • 70349333809 scopus 로고    scopus 로고
    • Expression ofthe Capsicuum annum (Chili) defensin gene in transgenic tomatoes confers enhanced resistance to fungal pathogens
    • COI: 1:CAS:528:DC%2BD1MXosFCqt7o%3D
    • Zainal Z, Marouf E, Ismail I, Fei CK (2009) Expression ofthe Capsicuum annum (Chili) defensin gene in transgenic tomatoes confers enhanced resistance to fungal pathogens. Am J Physiol 4:70–79
    • (2009) Am J Physiol , vol.4 , pp. 70-79
    • Zainal, Z.1    Marouf, E.2    Ismail, I.3    Fei, C.K.4
  • 109
    • 34848836028 scopus 로고    scopus 로고
    • Discovery of six families of fungal defensin-like peptides provides insights into origin and evolution of CSαβ defensins
    • COI: 1:CAS:528:DC%2BD2sXhtFalsbzO, PID: 17675235
    • Zhu S (2008) Discovery of six families of fungal defensin-like peptides provides insights into origin and evolution of CSαβ defensins. Mol Immunol 45:828–838
    • (2008) Mol Immunol , vol.45 , pp. 828-838
    • Zhu, S.1
  • 110
    • 0024381745 scopus 로고
    • Isolation and biological activity of corticostatic peptides (anti-ACTH)
    • COI: 1:CAS:528:DyaL1MXls1OmsLc%3D, PID: 2547596
    • Zhu Q, Bateman A, Singh A, Solomon S (1989) Isolation and biological activity of corticostatic peptides (anti-ACTH). Endocr Res 15:129–149
    • (1989) Endocr Res , vol.15 , pp. 129-149
    • Zhu, Q.1    Bateman, A.2    Singh, A.3    Solomon, S.4
  • 111
    • 34248571984 scopus 로고    scopus 로고
    • Ectopic expressionof Dahlia merckii defensin DmAMP1 improves papaya resistance to Phytophthora palmivora by reducing pathogen vigor
    • COI: 1:CAS:528:DC%2BD2sXltlSrsLw%3D, PID: 17216480
    • Zhu YJ, Agbayani R, Moore PH (2007) Ectopic expressionof Dahlia merckii defensin DmAMP1 improves papaya resistance to Phytophthora palmivora by reducing pathogen vigor. Planta 226:87–97
    • (2007) Planta , vol.226 , pp. 87-97
    • Zhu, Y.J.1    Agbayani, R.2    Moore, P.H.3
  • 112
    • 33747856780 scopus 로고    scopus 로고
    • Discovery of multiple beta-defensin like homologues in teleost fish
    • COI: 1:CAS:528:DC%2BD28Xos12mu7c%3D, PID: 16540171
    • Zou J, Mercier C, Koussounadis A, Secombes C (2007) Discovery of multiple beta-defensin like homologues in teleost fish. Mol Immunol 44:638–647
    • (2007) Mol Immunol , vol.44 , pp. 638-647
    • Zou, J.1    Mercier, C.2    Koussounadis, A.3    Secombes, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.