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Volumn , Issue , 2013, Pages 29-51

Innate immunity in plants: The role of antimicrobial peptides

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EID: 84942501061     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-0348-0541-4_2     Document Type: Chapter
Times cited : (46)

References (154)
  • 1
    • 34548511597 scopus 로고    scopus 로고
    • The antifungal activity of RsAFP2, a plant defensin from Raphanus sativus involves the induction of reactive oxygen species in Candida albicans
    • Aerts A, Francois IEJA, Meertt EMK, Li Q-T, Cammue BPA, Thevissen K (2007) The antifungal activity of RsAFP2, a plant defensin from Raphanus sativus involves the induction of reactive oxygen species in Candida albicans. J Mol Microbiol Biotechnol 13:243-247
    • (2007) J Mol Microbiol Biotechnol , vol.13 , pp. 243-247
    • Aerts, A.1    Francois, I.E.J.A.2    Meertt, E.M.K.3    Li, Q.-T.4    Cammue, B.P.A.5    Thevissen, K.6
  • 2
    • 40949112325 scopus 로고    scopus 로고
    • Plant defensins and virally encoded fungal toxin KP4 inhibit plant root growth
    • Allan 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
    • Allan, A.1    Snyder, A.K.2    Preuss, M.3    Nielsen, E.E.4    Shah, D.M.5    Smith, T.J.6
  • 3
    • 42249092243 scopus 로고    scopus 로고
    • Overexpression of snakin-1 gene enhances resistance to Rhizoctonia solani and Erwinia carotovora in transgenic potato plants
    • Almasia NI, Bazzini AA, Hopp HE, Vazquez-Rovere C (2008) Overexpression of snakin-1 gene enhances resistance to Rhizoctonia solani and Erwinia carotovora in transgenic potato plants. Mol Plant Pathol 9:329-338
    • (2008) Mol Plant Pathol , vol.9 , pp. 329-338
    • Almasia, N.I.1    Bazzini, A.A.2    Hopp, H.E.3    Vazquez-Rovere, C.4
  • 4
    • 79952333130 scopus 로고    scopus 로고
    • Silencing of host basal defense response-related gene expression increases susceptibility of Nicotiana benthamiana to Clavibacter michiganensis subsp. michiganensis
    • Balaji V, Sessa G, Smart CD (2010) Silencing of host basal defense response-related gene expression increases susceptibility of Nicotiana benthamiana to Clavibacter michiganensis subsp. michiganensis. Phytopathology 101:349-357
    • (2010) Phytopathology , vol.101 , pp. 349-357
    • Balaji, V.1    Sessa, G.2    Smart, C.D.3
  • 5
    • 0001131393 scopus 로고
    • A crystalline protein obtained from a lipoprotein of wheat flour
    • Balls AK, Hale WS, Harris TH (1942) A crystalline protein obtained from a lipoprotein of wheat flour. Cereal Chem 19:279-288
    • (1942) Cereal Chem , vol.19 , pp. 279-288
    • Balls, A.K.1    Hale, W.S.2    Harris, T.H.3
  • 7
    • 0030002724 scopus 로고    scopus 로고
    • Polypeptide signaling for plant defensive genes exhibits analogies to defense signaling in animals
    • Bergey DR, Howe GA, Ryan CA (1996) Polypeptide signaling for plant defensive genes exhibits analogies to defense signaling in animals. Proc Natl Acad Sci USA 93:12053-12058
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12053-12058
    • Bergey, D.R.1    Howe, G.A.2    Ryan, C.A.3
  • 8
    • 0036006046 scopus 로고    scopus 로고
    • Snakin-2, an antimicrobial peptide from potato whose gene is locally induced by wounding and responds to pathogen infection
    • Berrocal-Lobo M, Segura A, Moreno M, Lopez G, Garcia-Olmedo F, Molina A (2002) Snakin-2, an antimicrobial peptide from potato whose gene is locally induced by wounding and responds to pathogen infection. Plant Physiol 128:951-961
    • (2002) Plant Physiol , vol.128 , pp. 951-961
    • Berrocal-Lobo, M.1    Segura, A.2    Moreno, M.3    Lopez, G.4    Garcia-Olmedo, F.5    Molina, A.6
  • 10
    • 0025976182 scopus 로고
    • A new family of small (5 kD) protein inhibitors of insect alpha- amylases from seeds of sorghum (Sorghum bicolor Moench) have sequence homologies with wheat gamma-purothionins
    • Bloch C Jr, Richardson M (1991) A new family of small (5 kD) protein inhibitors of insect alpha- amylases from seeds of sorghum (Sorghum bicolor Moench) have sequence homologies with wheat gamma-purothionins. FEBS Lett 279:101-104
    • (1991) FEBS Lett , vol.279 , pp. 101-104
    • Bloch, C.1    Richardson, M.2
  • 11
    • 0017366834 scopus 로고
    • Rat liver proteins capable of transferring phosphatidylethanolamine. Purification and transfer activity for other phospholipids and cholesterol
    • Bloj B, Zilversmit DB (1977) Rat liver proteins capable of transferring phosphatidylethanolamine. Purification and transfer activity for other phospholipids and cholesterol. J Biol Chem 252:1613-1619
    • (1977) J Biol Chem , vol.252 , pp. 1613-1619
    • Bloj, B.1    Zilversmit, D.B.2
  • 13
    • 0001709760 scopus 로고
    • Leaf-specific thionins of barley-a novel class of cell wall proteins toxic to plant-pathogenic fungi and possibly involved in the defence mechanism of plants
    • Bohlmann H, Clausen S, Behnke S, Giese H, Hiller C, Reimann-Philipp U, Schrader G, Barkholt V, Apel K (1988) Leaf-specific thionins of barley-a novel class of cell wall proteins toxic to plant-pathogenic fungi and possibly involved in the defence mechanism of plants. EMBO J 7:1559-1565
    • (1988) EMBO J , vol.7 , pp. 1559-1565
    • Bohlmann, H.1    Clausen, S.2    Behnke, S.3    Giese, H.4    Hiller, C.5    Reimann-Philipp, U.6    Schrader, G.7    Barkholt, V.8    Apel, K.9
  • 14
    • 0032561506 scopus 로고    scopus 로고
    • Wounding and chemicals induce expression of the Arabidopsis thaliana gene Thi2.1, encoding a fungal defense thionin, via the octadecanoid pathway
    • Bohlmann H, Vignutelli A, Hilpert B, Miersch O, Wasternack C, Apel K (1998) Wounding and chemicals induce expression of the Arabidopsis thaliana gene Thi2.1, encoding a fungal defense thionin, via the octadecanoid pathway. FEBS Lett 437:281-286
    • (1998) FEBS Lett , vol.437 , pp. 281-286
    • Bohlmann, H.1    Vignutelli, A.2    Hilpert, B.3    Miersch, O.4    Wasternack, C.5    Apel, K.6
  • 16
    • 0038459120 scopus 로고    scopus 로고
    • A role for the GCC-box in jasmonate-mediated activation of the PDF1.2 gene of Arabidopsis
    • Brown RL, Kazan K, McGrath KC, Maclean DJ, Manners JM (2003) A role for the GCC-box in jasmonate-mediated activation of the PDF1.2 gene of Arabidopsis. Plant Physiol 132:1020-1032
    • (2003) Plant Physiol , vol.132 , pp. 1020-1032
    • Brown, R.L.1    Kazan, K.2    McGrath, K.C.3    Maclean, D.J.4    Manners, J.M.5
  • 17
    • 0027395308 scopus 로고
    • Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: A structural motif common to toxic arthropod proteins
    • Bruix M, Jimenez MA, Santoro J, Gonzalez C, Colilla FJ, Mendez E, Rico M (1993) Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: a structural motif common to toxic arthropod proteins. Biochemistry 32:715-724
    • (1993) Biochemistry , vol.32 , pp. 715-724
    • Bruix, M.1    Jimenez, M.A.2    Santoro, J.3    Gonzalez, C.4    Colilla, F.J.5    Mendez, E.6    Rico, M.7
  • 19
    • 0029743043 scopus 로고    scopus 로고
    • A computer-based systematic survey reveals the predominance of small inverted-repeat elements in wild-type rice genes
    • Bureau TE, Ronald PC, Wessler SR (1996) A computer-based systematic survey reveals the predominance of small inverted-repeat elements in wild-type rice genes. Proc Natl Acad Sci USA 93:8524-8529
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8524-8529
    • Bureau, T.E.1    Ronald, P.C.2    Wessler, S.R.3
  • 23
    • 0028168377 scopus 로고
    • A novel alphaamylase inhibitor from amaranth (Amaranthus hypocondriacus) seeds
    • Chagolla-Lopez A, Blanco-Labra A, Patthy A, Sanchez R, Pongor S (1994) A novel alphaamylase inhibitor from amaranth (Amaranthus hypocondriacus) seeds. J Biol Chem 269:23675-23680
    • (1994) J Biol Chem , vol.269 , pp. 23675-23680
    • Chagolla-Lopez, A.1    Blanco-Labra, A.2    Patthy, A.3    Sanchez, R.4    Pongor, S.5
  • 24
    • 0033199578 scopus 로고    scopus 로고
    • The crystal structure of a wheat nonspecific lipid transfer protein (ns-LTP1) complexed with two molecules of phospholipid at 2.1 A resolution
    • Charvolin D, Douliez JP, Marion D, Cohen-Addad C, Pebay-Peyroula E (1999) The crystal structure of a wheat nonspecific lipid transfer protein (ns-LTP1) complexed with two molecules of phospholipid at 2.1 A resolution. Eur J Biochem 264:562-568
    • (1999) Eur J Biochem , vol.264 , pp. 562-568
    • Charvolin, D.1    Douliez, J.P.2    Marion, D.3    Cohen-Addad, C.4    Pebay-Peyroula, E.5
  • 25
    • 40949116336 scopus 로고    scopus 로고
    • Plastid omega3-fatty acid desaturase-dependent accumulation of a systemic acquired resistance inducing activity in petiole exudates of Arabidopsis thaliana is independent of jasmonic acid
    • Chaturvedi R, Krothapalli K, Makandar R, Nandi A, Sparks AA, Roth MR, Welti R, Shah J (2008) Plastid omega3-fatty acid desaturase-dependent accumulation of a systemic acquired resistance inducing activity in petiole exudates of Arabidopsis thaliana is independent of jasmonic acid. Plant J 54:106-117
    • (2008) Plant J , vol.54 , pp. 106-117
    • Chaturvedi, R.1    Krothapalli, K.2    Makandar, R.3    Nandi, A.4    Sparks, A.A.5    Roth, M.R.6    Welti, R.7    Shah, J.8
  • 26
    • 32644451112 scopus 로고    scopus 로고
    • Cycloviolacin H4, a hydrophobic cyclotide from Viola hederaceae
    • Chen B, Colgrave ML, Wang C, Craik DJ (2006) Cycloviolacin H4, a hydrophobic cyclotide from Viola hederaceae. J Nat Prod 69:23-28
    • (2006) J Nat Prod , vol.69 , pp. 23-28
    • Chen, B.1    Colgrave, M.L.2    Wang, C.3    Craik, D.J.4
  • 28
    • 0010626198 scopus 로고
    • Effect on small laboratory animals of the injection of the crystalline hydrochloride of a sulfur protein from wheat flour
    • Coulson EJ, Harris TH, Axelrod B (1942) Effect on small laboratory animals of the injection of the crystalline hydrochloride of a sulfur protein from wheat flour. Cereal Chem 19:301-307
    • (1942) Cereal Chem , vol.19 , pp. 301-307
    • Coulson, E.J.1    Harris, T.H.2    Axelrod, B.3
  • 29
    • 33646248365 scopus 로고    scopus 로고
    • The cyclotide family of circular miniproteins: Nature's combinatorial peptide template
    • Craik DJ, Cemazar M, Wang CK, Daly NL (2006) The cyclotide family of circular miniproteins: nature's combinatorial peptide template. Biopolymers 84:250-266
    • (2006) Biopolymers , vol.84 , pp. 250-266
    • Craik, D.J.1    Cemazar, M.2    Wang, C.K.3    Daly, N.L.4
  • 30
    • 0029328535 scopus 로고
    • Cloning and characterization of two cDNA clones encoding seed-specific antimicrobial peptides from Mirabilis jalapa L
    • De Bolle MF, Eggermont K, Duncan RE, Osborn RW, Terras FR, Broekaert WF (1995) Cloning and characterization of two cDNA clones encoding seed-specific antimicrobial peptides from Mirabilis jalapa L. Plant Mol Biol 28:713-721
    • (1995) Plant Mol Biol , vol.28 , pp. 713-721
    • De Bolle, M.F.1    Eggermont, K.2    Duncan, R.E.3    Osborn, R.W.4    Terras, F.R.5    Broekaert, W.F.6
  • 31
    • 0030220499 scopus 로고    scopus 로고
    • Antimicrobial peptides from Mirabilis jalapa and Amaranthus caudatus: Expression, processing, localization and biological activity in transgenic tobacco
    • De Bolle MF, Osborn RW, Goderis IJ, Noe L, Acland D, Hart CA, Torrekens S, Van Leuven F, Broekaert WF (1996) Antimicrobial peptides from Mirabilis jalapa and Amaranthus caudatus: expression, processing, localization and biological activity in transgenic tobacco. Plant Mol Biol 31:993-1008
    • (1996) Plant Mol Biol , vol.31 , pp. 993-1008
    • De Bolle, M.F.1    Osborn, R.W.2    Goderis, I.J.3    Noe, L.4    Acland, D.5    Hart, C.A.6    Torrekens, S.7    Van Leuven, F.8    Broekaert, W.F.9
  • 34
    • 0034817848 scopus 로고    scopus 로고
    • Binding of two mono-acylated lipid monomers by the barley lipid transfer protein, LTP1, as viewed by fluorescence, isothermal titration calorimetry and molecular modelling
    • Douliez JP, Jegou S, Pato C, Molle D, Tran V, Marion D (2001) Binding of two mono-acylated lipid monomers by the barley lipid transfer protein, LTP1, as viewed by fluorescence, isothermal titration calorimetry and molecular modelling. Eur J Biochem 268:384-388
    • (2001) Eur J Biochem , vol.268 , pp. 384-388
    • Douliez, J.P.1    Jegou, S.2    Pato, C.3    Molle, D.4    Tran, V.5    Marion, D.6
  • 35
    • 0034738520 scopus 로고    scopus 로고
    • Steady-state tyrosine fluorescence to study the lipidbinding properties of a wheat non-specific lipid-transfer protein (nsLTP1)
    • Douliez JP, Michon T, Marion D (2000) Steady-state tyrosine fluorescence to study the lipidbinding properties of a wheat non-specific lipid-transfer protein (nsLTP1). Biochim Biophys Acta 1467:65-72
    • (2000) Biochim Biophys Acta , vol.1467 , pp. 65-72
    • Douliez, J.P.1    Michon, T.2    Marion, D.3
  • 37
    • 0029411206 scopus 로고
    • An Arabidopsis thaliana thionin gene is inducible via a signal transduction pathway different from that for pathogenesis-related proteins
    • Epple P, Apel K, Bohlmann H (1995) An Arabidopsis thaliana thionin gene is inducible via a signal transduction pathway different from that for pathogenesis-related proteins. Plant Physiol 109:813-820
    • (1995) Plant Physiol , vol.109 , pp. 813-820
    • Epple, P.1    Apel, K.2    Bohlmann, H.3
  • 38
    • 0031128435 scopus 로고    scopus 로고
    • Overexpression of an endogenous thionin enhances resistance of Arabidopsis against Fusarium oxysporum
    • Epple P, Apel K, Bohlmann H (1997) Overexpression of an endogenous thionin enhances resistance of Arabidopsis against Fusarium oxysporum. Plant Cell 9:509-520
    • (1997) Plant Cell , vol.9 , pp. 509-520
    • Epple, P.1    Apel, K.2    Bohlmann, H.3
  • 39
    • 0033136465 scopus 로고    scopus 로고
    • Plants have a sensitive perception system for the most conserved domain of bacterial flagellin
    • Felix G, Duran JD, Volko S, Boller T (1999) Plants have a sensitive perception system for the most conserved domain of bacterial flagellin. Plant J 18:265-276
    • (1999) Plant J , vol.18 , pp. 265-276
    • Felix, G.1    Duran, J.D.2    Volko, S.3    Boller, T.4
  • 40
    • 0035933743 scopus 로고    scopus 로고
    • Circular proteins in plants: Solution structure of a novel macrocyclic trypsin inhibitor from Momordica cochinchinensis
    • Felizmenio-Quimio ME, Daly NL, Craik DJ (2001) Circular proteins in plants: solution structure of a novel macrocyclic trypsin inhibitor from Momordica cochinchinensis. J Biol Chem 276:22875-22882
    • (2001) J Biol Chem , vol.276 , pp. 22875-22882
    • Felizmenio-Quimio, M.E.1    Daly, N.L.2    Craik, D.J.3
  • 45
    • 0035842069 scopus 로고    scopus 로고
    • Molecular scaffold of a new pokeweed antifungal peptide deduced by 1H nuclear magnetic resonance
    • Gao GH, Liu W, Dai JX, Wang JF, Hu Z, Zhang Y, Wang DC (2001a) Molecular scaffold of a new pokeweed antifungal peptide deduced by 1H nuclear magnetic resonance. Int J Biol Macromol 29:251-258
    • (2001) Int J Biol Macromol , vol.29 , pp. 251-258
    • Gao, G.H.1    Liu, W.2    Dai, J.X.3    Wang, J.F.4    Hu, Z.5    Zhang, Y.6    Wang, D.C.7
  • 46
    • 0035909081 scopus 로고    scopus 로고
    • Solution structure of PAFP-S: A new knottin-type antifungal peptide from the seeds of Phytolacca americana
    • Gao GH, Liu W, Dai JX, Wang JF, Hu Z, Zhang Y, Wang DC (2001b) Solution structure of PAFP-S: a new knottin-type antifungal peptide from the seeds of Phytolacca americana. Biochemistry 40:10973-10978
    • (2001) Biochemistry , vol.40 , pp. 10973-10978
    • Gao, G.H.1    Liu, W.2    Dai, J.X.3    Wang, J.F.4    Hu, Z.5    Zhang, Y.6    Wang, D.C.7
  • 47
  • 48
    • 0043268759 scopus 로고    scopus 로고
    • Preliminary study on the structural basis of the antifungal activity of a rice lipid transfer protein
    • Ge X, Chen J, Sun C, Cao K (2003) Preliminary study on the structural basis of the antifungal activity of a rice lipid transfer protein. Protein Eng 16:387-390
    • (2003) Protein Eng , vol.16 , pp. 387-390
    • Ge, X.1    Chen, J.2    Sun, C.3    Cao, K.4
  • 50
    • 0027973368 scopus 로고
    • Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers
    • Gincel E, Simorre JP, Caille A, Marion D, Ptak M, Vovelle F (1994) Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers. Eur J Biochem 226:413-422
    • (1994) Eur J Biochem , vol.226 , pp. 413-422
    • Gincel, E.1    Simorre, J.P.2    Caille, A.3    Marion, D.4    Ptak, M.5    Vovelle, F.6
  • 51
    • 0030005766 scopus 로고    scopus 로고
    • Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds
    • Gomar J, Petit MC, Sodano P, Sy D, Marion D, Kader JC, Vovelle F, Ptak M (1996) Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds. Protein Sci 5:565-577
    • (1996) Protein Sci , vol.5 , pp. 565-577
    • Gomar, J.1    Petit, M.C.2    Sodano, P.3    Sy, D.4    Marion, D.5    Kader, J.C.6    Vovelle, F.7    Ptak, M.8
  • 53
    • 42449112866 scopus 로고    scopus 로고
    • Defensin-like genes: Genomic perspectives on a diverse superfamily in plants
    • Graham MA, Silverstein KAT, VandenBosch KA (2008) Defensin-like genes: genomic perspectives on a diverse superfamily in plants. Crop Sci 48:S3-S11
    • (2008) Crop Sci , vol.48 , pp. S3-S11
    • Graham, M.A.1    Silverstein, K.A.T.2    VandenBosch, K.A.3
  • 54
    • 34547098170 scopus 로고    scopus 로고
    • A novel plant protein-disulfide isomerase involved in the oxidative folding of cystine knot defense proteins
    • Gruber CW, Cemazar M, Clark RJ, Horibe T, Renda RF, Anderson MA, Craik DJ (2007) A novel plant protein-disulfide isomerase involved in the oxidative folding of cystine knot defense proteins. J Biol Chem 282:20435-20446
    • (2007) J Biol Chem , vol.282 , pp. 20435-20446
    • Gruber, C.W.1    Cemazar, M.2    Clark, R.J.3    Horibe, T.4    Renda, R.F.5    Anderson, M.A.6    Craik, D.J.7
  • 56
    • 0030909499 scopus 로고    scopus 로고
    • Structural and evolutionary relationships among chitinases of flowering plants
    • Hamel F, Boivin R, Tremblay C, Bellemare G (1997) Structural and evolutionary relationships among chitinases of flowering plants. J Mol Evol 44:614-624
    • (1997) J Mol Evol , vol.44 , pp. 614-624
    • Hamel, F.1    Boivin, R.2    Tremblay, C.3    Bellemare, G.4
  • 58
    • 23844519388 scopus 로고    scopus 로고
    • Structure of a liganded type 2 nonspecific lipid-transfer protein from wheat and the molecular basis of lipid binding
    • Hoh F, Pons JL, Gautier MF, de Lamotte F, Dumas C (2005) Structure of a liganded type 2 nonspecific lipid-transfer protein from wheat and the molecular basis of lipid binding. Acta Crystallogr D Biol Crystallogr 61:397-406
    • (2005) Acta Crystallogr D Biol Crystallogr , vol.61 , pp. 397-406
    • Hoh, F.1    Pons, J.L.2    Gautier, M.F.3    de Lamotte, F.4    Dumas, C.5
  • 59
    • 33745589774 scopus 로고    scopus 로고
    • An endogenous peptide signal in Arabidopsis activates components of the innate immune response
    • Huffaker A, Pearce G, Ryan CA (2006) An endogenous peptide signal in Arabidopsis activates components of the innate immune response. Proc Natl Acad Sci USA 103:10098-10103
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10098-10103
    • Huffaker, A.1    Pearce, G.2    Ryan, C.A.3
  • 60
    • 34447645226 scopus 로고    scopus 로고
    • Endogenous peptide defense signals in Arabidopsis differentially amplify signaling for the innate immune response
    • Huffaker A, Ryan CA (2007) Endogenous peptide defense signals in Arabidopsis differentially amplify signaling for the innate immune response. Proc Natl Acad Sci USA 104:10732-10736
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 10732-10736
    • Huffaker, A.1    Ryan, C.A.2
  • 61
    • 33645047649 scopus 로고    scopus 로고
    • Discovery and characterization of a linear cyclotide from Viola odorata: Implications for the processing of circular proteins
    • Ireland DC, Colgrave ML, Nguyencong P, Daly NL, Craik DJ (2006) Discovery and characterization of a linear cyclotide from Viola odorata: implications for the processing of circular proteins. J Mol Biol 357:1522-1535
    • (2006) J Mol Biol , vol.357 , pp. 1522-1535
    • Ireland, D.C.1    Colgrave, M.L.2    Nguyencong, P.3    Daly, N.L.4    Craik, D.J.5
  • 63
    • 0027666351 scopus 로고
    • The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity
    • Iseli B, Boller T, Neuhaus JM (1993) The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity. Plant Physiol 103:221-226
    • (1993) Plant Physiol , vol.103 , pp. 221-226
    • Iseli, B.1    Boller, T.2    Neuhaus, J.M.3
  • 64
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway CA (1989) Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb Symp Quant Biol 54:1-13
    • (1989) Cold Spring Harb Symp Quant Biol , vol.54 , pp. 1-13
    • Janeway, C.A.1
  • 65
    • 0035845584 scopus 로고    scopus 로고
    • Biosynthesis and insecticidal properties of plant cyclotides: The cyclic knotted proteins from Oldenlandia affinis
    • Jennings C, West J, Waine C, Craik D, Anderson M (2001) Biosynthesis and insecticidal properties of plant cyclotides: the cyclic knotted proteins from Oldenlandia affinis. Proc Natl Acad Sci USA 98:10614-10619
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10614-10619
    • Jennings, C.1    West, J.2    Waine, C.3    Craik, D.4    Anderson, M.5
  • 66
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • Jones JDG, Dangl JL (2006) The plant immune system. Nature 444:323-329
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.G.1    Dangl, J.L.2
  • 70
    • 0021402150 scopus 로고
    • Purification and characterization of a spinach-leaf protein capable of transferring phospholipids from liposomes to mitochondria or chloroplasts
    • Kader JC, Julienne M, Vergnolle C (1984) Purification and characterization of a spinach-leaf protein capable of transferring phospholipids from liposomes to mitochondria or chloroplasts. Eur J Biochem 139:411-416
    • (1984) Eur J Biochem , vol.139 , pp. 411-416
    • Kader, J.C.1    Julienne, M.2    Vergnolle, C.3
  • 71
    • 0030060895 scopus 로고    scopus 로고
    • Physiological and molecular characteristics of elicitin-induced systemic acquired resistance in tobacco
    • Keller H, Blein JP, Bonnet P, Ricci P (1996) Physiological and molecular characteristics of elicitin-induced systemic acquired resistance in tobacco. Plant Physiol 110:365-376
    • (1996) Plant Physiol , vol.110 , pp. 365-376
    • Keller, H.1    Blein, J.P.2    Bonnet, P.3    Ricci, P.4
  • 74
    • 54849422795 scopus 로고    scopus 로고
    • Expression and functional characterization of the plant antimicrobial snakin-1 and defensin recombinant proteins
    • Kovalskaya N, Hammond RW (2009) Expression and functional characterization of the plant antimicrobial snakin-1 and defensin recombinant proteins. Protein Expr Purif 63:12-17
    • (2009) Protein Expr Purif , vol.63 , pp. 12-17
    • Kovalskaya, N.1    Hammond, R.W.2
  • 75
    • 0025940134 scopus 로고
    • Co- and post-translational processing of the hevein preproprotein of latex of the rubber tree (Hevea brasiliensis)
    • Lee HI, Broekaert WF, Raikhel NV (1991) Co- and post-translational processing of the hevein preproprotein of latex of the rubber tree (Hevea brasiliensis). J Biol Chem 266:15944-15948
    • (1991) J Biol Chem , vol.266 , pp. 15944-15948
    • Lee, H.I.1    Broekaert, W.F.2    Raikhel, N.V.3
  • 76
    • 0032548996 scopus 로고    scopus 로고
    • Rice non-specific lipid transfer protein: The 1.6 A crystal structure in the unliganded state reveals a small hydrophobic cavity
    • Lee JY, Min K, Cha H, Shin DH, Hwang KY, Suh SW (1998) Rice non-specific lipid transfer protein: the 1.6 A crystal structure in the unliganded state reveals a small hydrophobic cavity. J Mol Biol 276:437-448
    • (1998) J Mol Biol , vol.276 , pp. 437-448
    • Lee, J.Y.1    Min, K.2    Cha, H.3    Shin, D.H.4    Hwang, K.Y.5    Suh, S.W.6
  • 77
    • 0031700043 scopus 로고    scopus 로고
    • Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins
    • Lerche MH, Poulsen FM (1998) Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins. Protein Sci 7:2490-2498
    • (1998) Protein Sci , vol.7 , pp. 2490-2498
    • Lerche, M.H.1    Poulsen, F.M.2
  • 78
    • 34250887046 scopus 로고    scopus 로고
    • Structure-based protein engineering for alpha-amylase inhibitory activity of plant defensin
    • Lin KF, Lee TR, Tsai PH, Hsu MP, Chen CS, Lyu PC (2007) Structure-based protein engineering for alpha-amylase inhibitory activity of plant defensin. Proteins 68:530-540
    • (2007) Proteins , vol.68 , pp. 530-540
    • Lin, K.F.1    Lee, T.R.2    Tsai, P.H.3    Hsu, M.P.4    Chen, C.S.5    Lyu, P.C.6
  • 79
    • 0037179714 scopus 로고    scopus 로고
    • A putative lipid transfer protein involved in systemic resistance signalling in Arabidopsis
    • Maldonado AM, Doerner P, Dixon RA, Lamb CJ, Cameron RK (2002) A putative lipid transfer protein involved in systemic resistance signalling in Arabidopsis. Nature 419:399-403
    • (2002) Nature , vol.419 , pp. 399-403
    • Maldonado, A.M.1    Doerner, P.2    Dixon, R.A.3    Lamb, C.J.4    Cameron, R.K.5
  • 81
    • 0001008022 scopus 로고
    • Functional implications of the subcellular localization of ethylene- induced chitinase and beta-1,3-glucanase in bean leaves
    • Mauch F, Staehelin LA (1989) Functional implications of the subcellular localization of ethylene- induced chitinase and beta-1,3-glucanase in bean leaves. Plant Cell 1:447-457
    • (1989) Plant Cell , vol.1 , pp. 447-457
    • Mauch, F.1    Staehelin, L.A.2
  • 82
    • 0025670589 scopus 로고
    • Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, gamma-thionin, from barley endosperm
    • Mendez E, Moreno A, Colilla F, Pelaez R, Limas GG, Mendez R, Soriano F, Salinas M, de Haro C (1990) Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, gamma-thionin, from barley endosperm. Eur J Biochem 194:533-539
    • (1990) Eur J Biochem , vol.194 , pp. 533-539
    • Mendez, E.1    Moreno, A.2    Colilla, F.3    Pelaez, R.4    Limas, G.G.5    Mendez, R.6    Soriano, F.7    Salinas, M.8    de Haro, C.9
  • 84
    • 0032483319 scopus 로고    scopus 로고
    • Systemic induction of an Arabidopsis plant defensin gene promoter by tobacco mosaic virus and jasmonic acid in transgenic tobacco
    • Mitter N, Kazan K, Way HM, Broekaert WF, Manners JM (1998) Systemic induction of an Arabidopsis plant defensin gene promoter by tobacco mosaic virus and jasmonic acid in transgenic tobacco. Plant Sci 136:169-180
    • (1998) Plant Sci , vol.136 , pp. 169-180
    • Mitter, N.1    Kazan, K.2    Way, H.M.3    Broekaert, W.F.4    Manners, J.M.5
  • 85
    • 60649083575 scopus 로고    scopus 로고
    • Phloem sap of tomato plants contains a DIR1 putative ortholog
    • Mitton FM, Pinedo ML, de la Canal L (2009) Phloem sap of tomato plants contains a DIR1 putative ortholog. J Plant Physiol 166:543-547
    • (2009) J Plant Physiol , vol.166 , pp. 543-547
    • Mitton, F.M.1    Pinedo, M.L.2    de la Canal, L.3
  • 86
    • 0027722868 scopus 로고
    • Developmental and pathogen-induced expression of three barley genes encoding lipid transfer proteins
    • Molina A, Garcia-Olmedo F (1993) Developmental and pathogen-induced expression of three barley genes encoding lipid transfer proteins. Plant J 4:983-991
    • (1993) Plant J , vol.4 , pp. 983-991
    • Molina, A.1    Garcia-Olmedo, F.2
  • 87
    • 0031239810 scopus 로고    scopus 로고
    • Enhanced tolerance to bacterial pathogens caused by the transgenic expression of barley lipid transfer protein LTP2
    • Molina A, Garcia-Olmedo F (1997) Enhanced tolerance to bacterial pathogens caused by the transgenic expression of barley lipid transfer protein LTP2. Plant J 12:669-675
    • (1997) Plant J , vol.12 , pp. 669-675
    • Molina, A.1    Garcia-Olmedo, F.2
  • 88
    • 0027507001 scopus 로고
    • Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens
    • Molina A, Segura A, Garcia-Olmedo F (1993) Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens. FEBS Lett 316:119-122
    • (1993) FEBS Lett , vol.316 , pp. 119-122
    • Molina, A.1    Segura, A.2    Garcia-Olmedo, F.3
  • 89
    • 0037532487 scopus 로고    scopus 로고
    • Ethylene and jasmonic acid signaling affect the NPR1-independent expression of defense genes without impacting resistance to Pseudomonas syringae and Peronospora parasitica in the Arabidopsis ssil mutant
    • Nandi A, Kachroo P, Fukushige H, Hildebrand DF, Klessig DF, Shah J (2003) Ethylene and jasmonic acid signaling affect the NPR1-independent expression of defense genes without impacting resistance to Pseudomonas syringae and Peronospora parasitica in the Arabidopsis ssil mutant. Mol Plant-Microbe Interact 16:588-599
    • (2003) Mol Plant-Microbe Interact , vol.16 , pp. 588-599
    • Nandi, A.1    Kachroo, P.2    Fukushige, H.3    Hildebrand, D.F.4    Klessig, D.F.5    Shah, J.6
  • 90
    • 1042290708 scopus 로고    scopus 로고
    • The Arabidopsis thaliana dihydroxyacetone phosphate reductase gene SUPPRESSSOR OF FATTY ACID DESATURASE DEFICIENCY1 is required for glycerolipid metabolism and for the activation of systemic acquired resistance
    • Nandi A, Welti R, Shah J (2004) The Arabidopsis thaliana dihydroxyacetone phosphate reductase gene SUPPRESSSOR OF FATTY ACID DESATURASE DEFICIENCY1 is required for glycerolipid metabolism and for the activation of systemic acquired resistance. Plant Cell 16:465-477
    • (2004) Plant Cell , vol.16 , pp. 465-477
    • Nandi, A.1    Welti, R.2    Shah, J.3
  • 91
    • 0037066461 scopus 로고    scopus 로고
    • Recognition and rejection of self in plant reproduction
    • Nasrallah JB (2002) Recognition and rejection of self in plant reproduction. Science 296:305-308
    • (2002) Science , vol.296 , pp. 305-308
    • Nasrallah, J.B.1
  • 92
    • 33947651152 scopus 로고    scopus 로고
    • SA-inducible Arabidopsis glutaredoxin interacts with TGA factors and suppresses JA-responsive PDF1.2 transcription
    • Ndamukong I, Abdallat AA, Thurow C, Fode B, Zander M, Weigel R, Gatz C (2007) SA-inducible Arabidopsis glutaredoxin interacts with TGA factors and suppresses JA-responsive PDF1.2 transcription. Plant J 50:128-139
    • (2007) Plant J , vol.50 , pp. 128-139
    • Ndamukong, I.1    Abdallat, A.A.2    Thurow, C.3    Fode, B.4    Zander, M.5    Weigel, R.6    Gatz, C.7
  • 93
    • 0031048304 scopus 로고    scopus 로고
    • Characterization of a new antifungal chitin-binding peptide from sugar beet leaves
    • Nielsen KK, Nielsen JE, Madrid SM, Mikkelsen JD (1997) Characterization of a new antifungal chitin-binding peptide from sugar beet leaves. Plant Physiol 113:83-91
    • (1997) Plant Physiol , vol.113 , pp. 83-91
    • Nielsen, K.K.1    Nielsen, J.E.2    Madrid, S.M.3    Mikkelsen, J.D.4
  • 94
    • 0031801556 scopus 로고    scopus 로고
    • Antagonistic effect of salicylic acid and jasmonic acid on the expression of pathogenesis-related (PR) protein genes in wounded mature tobacco leaves
    • Niki T, Mitsuhara I, Seo S, Ohtsubo N, Ohashi Y (1998) Antagonistic effect of salicylic acid and jasmonic acid on the expression of pathogenesis-related (PR) protein genes in wounded mature tobacco leaves. Plant Cell Physiol 39:500-507
    • (1998) Plant Cell Physiol , vol.39 , pp. 500-507
    • Niki, T.1    Mitsuhara, I.2    Seo, S.3    Ohtsubo, N.4    Ohashi, Y.5
  • 95
    • 84912165303 scopus 로고
    • The relation of a "globulin" component of wheat flower to purothionin
    • Nimmo CC, O'Sullivan MT, Bernardin JE (1968) The relation of a "globulin" component of wheat flower to purothionin. Cereal Chem 45:28-36
    • (1968) Cereal Chem , vol.45 , pp. 28-36
    • Nimmo, C.C.1    O'Sullivan, M.T.2    Bernardin, J.E.3
  • 98
    • 77952632254 scopus 로고    scopus 로고
    • Structural aspects of plant antimicrobial peptides
    • Padovan L, Scocchi M, Tossi A (2010) Structural aspects of plant antimicrobial peptides. Curr Protein Pept Sci 11:210-219
    • (2010) Curr Protein Pept Sci , vol.11 , pp. 210-219
    • Padovan, L.1    Scocchi, M.2    Tossi, A.3
  • 100
    • 0036241388 scopus 로고    scopus 로고
    • Effects of acylation on the structure, lipid binding, and transfer activity of wheat lipid transfer protein
    • Pato C, Tran V, Marion D, Douliez JP (2002) Effects of acylation on the structure, lipid binding, and transfer activity of wheat lipid transfer protein. J Protein Chem 21:195-201
    • (2002) J Protein Chem , vol.21 , pp. 195-201
    • Pato, C.1    Tran, V.2    Marion, D.3    Douliez, J.P.4
  • 101
    • 55949094265 scopus 로고    scopus 로고
    • Structure-activity studies of AtPep1, a plant peptide signal involved in the innate immune response
    • Pearce G, Yamaguchi Y, Munske G, Ryan CA (2008) Structure-activity studies of AtPep1, a plant peptide signal involved in the innate immune response. Peptides 29:2083-2089
    • (2008) Peptides , vol.29 , pp. 2083-2089
    • Pearce, G.1    Yamaguchi, Y.2    Munske, G.3    Ryan, C.A.4
  • 102
    • 57349188418 scopus 로고    scopus 로고
    • Novel insights on the mechanism of action of alpha-amylase inhibitors from the plant defensin family
    • 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
  • 103
    • 72949124488 scopus 로고    scopus 로고
    • The Medicago truncatula N5 gene encoding a root-specific lipid transfer protein is required for the symbiotic interaction with Sinorhizobium meliloti
    • Pii Y, Astegno A, Peroni E, Zaccardelli M, Pandolfini T, Crimi M (2009) The Medicago truncatula N5 gene encoding a root-specific lipid transfer protein is required for the symbiotic interaction with Sinorhizobium meliloti. Mol Plant Microbe Interact 22:1577-1587
    • (2009) Mol Plant Microbe Interact , vol.22 , pp. 1577-1587
    • Pii, Y.1    Astegno, A.2    Peroni, E.3    Zaccardelli, M.4    Pandolfini, T.5    Crimi, M.6
  • 104
    • 77954992376 scopus 로고    scopus 로고
    • Signaling LTPs: A new plant LTPs sub-family
    • Pii Y, Pandolfini T, Crimi M (2010) Signaling LTPs: a new plant LTPs sub-family? Plant Signal Behav 5:594-597
    • (2010) Plant Signal Behav , vol.5 , pp. 594-597
    • Pii, Y.1    Pandolfini, T.2    Crimi, M.3
  • 106
    • 0028363877 scopus 로고
    • Identification of a lipid transfer protein as the major protein in the surface wax of broccoli (Brassica oleracea) leaves
    • Pyee J, Yu H, Kolattukudy PE (1994) Identification of a lipid transfer protein as the major protein in the surface wax of broccoli (Brassica oleracea) leaves. Arch Biochem Biophys 311:460-468
    • (1994) Arch Biochem Biophys , vol.311 , pp. 460-468
    • Pyee, J.1    Yu, H.2    Kolattukudy, P.E.3
  • 107
    • 47549084504 scopus 로고    scopus 로고
    • PR-13/Thionin but not PR-1 mediates bacterial resistance in Nicotiana attenuata in nature, and neither influences herbivore resistance
    • Rayapuram C, Wu J, Haas C, Baldwin IT (2008) PR-13/Thionin but not PR-1 mediates bacterial resistance in Nicotiana attenuata in nature, and neither influences herbivore resistance. Mol Plant Microbe Interact 21:988-1000
    • (2008) Mol Plant Microbe Interact , vol.21 , pp. 988-1000
    • Rayapuram, C.1    Wu, J.2    Haas, C.3    Baldwin, I.T.4
  • 108
    • 0031020926 scopus 로고    scopus 로고
    • Processing of thionin precursors in barley leaves by a vacuolar proteinase
    • Romero A, Alamillo JM, Garcia-Olmedo F (1997) Processing of thionin precursors in barley leaves by a vacuolar proteinase. Eur J Biochem 243:202-208
    • (1997) Eur J Biochem , vol.243 , pp. 202-208
    • Romero, A.1    Alamillo, J.M.2    Garcia-Olmedo, F.3
  • 109
    • 33747070536 scopus 로고    scopus 로고
    • Expression of the lipid transfer protein Ace-AMP1 in transgenic wheat enhances antifungal activity and defense responses
    • Roy-Barman S, Sautter C, Chattoo BB (2006) Expression of the lipid transfer protein Ace-AMP1 in transgenic wheat enhances antifungal activity and defense responses. Transgenic Res 15:435-446
    • (2006) Transgenic Res , vol.15 , pp. 435-446
    • Roy-Barman, S.1    Sautter, C.2    Chattoo, B.B.3
  • 110
    • 0028927655 scopus 로고
    • Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1
    • Saether O, Craik DJ, Campbell ID, Sletten K, Juul J, Norman DG (1995) Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1. Biochemistry 34:4147-4158
    • (1995) Biochemistry , vol.34 , pp. 4147-4158
    • Saether, O.1    Craik, D.J.2    Campbell, I.D.3    Sletten, K.4    Juul, J.5    Norman, D.G.6
  • 111
    • 0037144489 scopus 로고    scopus 로고
    • Solution structure of plant nonspecific lipid transfer protein-2 from rice (Oryza sativa)
    • Samuel D, Liu YJ, Cheng CS, Lyu PC (2002) Solution structure of plant nonspecific lipid transfer protein-2 from rice (Oryza sativa). J Biol Chem 277:35267-35273
    • (2002) J Biol Chem , vol.277 , pp. 35267-35273
    • Samuel, D.1    Liu, Y.J.2    Cheng, C.S.3    Lyu, P.C.4
  • 113
    • 21644442843 scopus 로고    scopus 로고
    • Diversification and alteration of recognition specificity of the pollen ligand SP11/SCR in self-incompatibility of Brassica and Raphanus
    • Sato Y, Okamoto S, Nishio T (2004) Diversification and alteration of recognition specificity of the pollen ligand SP11/SCR in self-incompatibility of Brassica and Raphanus. Plant Cell 16:3230-3241
    • (2004) Plant Cell , vol.16 , pp. 3230-3241
    • Sato, Y.1    Okamoto, S.2    Nishio, T.3
  • 114
    • 0033213989 scopus 로고    scopus 로고
    • Epithelial antimicrobial peptides: Innate local host response elements
    • Schröder J-M (1999) Epithelial antimicrobial peptides: innate local host response elements. Cell Mol Life Sci 56:32-46
    • (1999) Cell Mol Life Sci , vol.56 , pp. 32-46
    • Schröder, J.-M.1
  • 115
    • 48049084745 scopus 로고    scopus 로고
    • News from the frontline: Recent insights into PAMP-triggered immunity in plants
    • Schwessinger B, Zipfel C (2008) News from the frontline: recent insights into PAMP-triggered immunity in plants. Curr Opin Plant Biol 11:389-395
    • (2008) Curr Opin Plant Biol , vol.11 , pp. 389-395
    • Schwessinger, B.1    Zipfel, C.2
  • 116
    • 0027358813 scopus 로고
    • Purification and antipathogenic activity of lipid transfer proteins (LTPs) from the leaves of Arabidopsis and spinach
    • Segura A, Moreno M, Garcia-Olmedo F (1993) Purification and antipathogenic activity of lipid transfer proteins (LTPs) from the leaves of Arabidopsis and spinach. FEBS Lett 332:243-246
    • (1993) FEBS Lett , vol.332 , pp. 243-246
    • Segura, A.1    Moreno, M.2    Garcia-Olmedo, F.3
  • 118
    • 68149112475 scopus 로고    scopus 로고
    • Plants under attack: Systemic signals in defence
    • Shah J (2009) Plants under attack: systemic signals in defence. Curr Opin Plant Biol 12:459-464
    • (2009) Curr Opin Plant Biol , vol.12 , pp. 459-464
    • Shah, J.1
  • 119
    • 0029643949 scopus 로고
    • High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings
    • Shin DH, Lee JY, Hwang KY, Kim KK, Suh SW (1995) High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings. Structure 3:189-199
    • (1995) Structure , vol.3 , pp. 189-199
    • Shin, D.H.1    Lee, J.Y.2    Hwang, K.Y.3    Kim, K.K.4    Suh, S.W.5
  • 124
    • 67849114035 scopus 로고    scopus 로고
    • A defensin from tomato with dual function in defence and development
    • Stotz HU, Wang Y, Spence B (2009) A defensin from tomato with dual function in defence and development. Plant Mol Biol 71:131-143
    • (2009) Plant Mol Biol , vol.71 , pp. 131-143
    • Stotz, H.U.1    Wang, Y.2    Spence, B.3
  • 126
    • 34249056827 scopus 로고    scopus 로고
    • Mechanism of action of cytotoxic cyclotides: Cycloviolacin O2 disrupts lipid membranes
    • Svangard E, Burman R, Gunasekera S, Lovborg H, Gullbo J, Goransson U (2007) Mechanism of action of cytotoxic cyclotides: cycloviolacin O2 disrupts lipid membranes. J Nat Prod 70:643-647
    • (2007) J Nat Prod , vol.70 , pp. 643-647
    • Svangard, E.1    Burman, R.2    Gunasekera, S.3    Lovborg, H.4    Gullbo, J.5    Goransson, U.6
  • 127
    • 0033529942 scopus 로고    scopus 로고
    • An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides
    • Tam JP, Lu YA, Yang JL, Chiu KW (1999) An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides. Proc Natl Acad Sci USA 96:8913-8918
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8913-8918
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3    Chiu, K.W.4
  • 128
    • 0032539972 scopus 로고    scopus 로고
    • Solution structure of Ace-AMP1, a potent antimicrobial protein extracted from onion seeds. Structural analogies with plant nonspecific lipid transfer proteins
    • Tassin S, Broekaert WF, Marion D, Acland DP, Ptak M, Vovelle F, Sodano P (1998) Solution structure of Ace-AMP1, a potent antimicrobial protein extracted from onion seeds. Structural analogies with plant nonspecific lipid transfer proteins. Biochemistry 37:3623-3637
    • (1998) Biochemistry , vol.37 , pp. 3623-3637
    • Tassin, S.1    Broekaert, W.F.2    Marion, D.3    Acland, D.P.4    Ptak, M.5    Vovelle, F.6    Sodano, P.7
  • 129
    • 0001469527 scopus 로고
    • In vitro antifungal activity of a radish (Raphanus sativus L.) seed protein homologous to nonspecific lipid transfer proteins
    • 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
  • 133
    • 0031465590 scopus 로고    scopus 로고
    • Specific, high affinity binding sites for an antifungal plant defensin on Neurospora crassa hyphae and microsomal membranes
    • Thevissen K, Osborn RW, Acland DP, Broekaert WF (1997) Specific, high affinity binding sites for an antifungal plant defensin on Neurospora crassa hyphae and microsomal membranes. J Biol Chem 272:32176-32181
    • (1997) J Biol Chem , vol.272 , pp. 32176-32181
    • Thevissen, K.1    Osborn, R.W.2    Acland, D.P.3    Broekaert, W.F.4
  • 134
    • 0032751756 scopus 로고    scopus 로고
    • Permeabilization of fungal membranes by plant defensins inhibits fungal growth
    • Thevissen K, Terras FR, Broekaert WF (1999) Permeabilization of fungal membranes by plant defensins inhibits fungal growth. Appl Environ Microbiol 65:5451-5458
    • (1999) Appl Environ Microbiol , vol.65 , pp. 5451-5458
    • Thevissen, K.1    Terras, F.R.2    Broekaert, W.F.3
  • 136
    • 0028428501 scopus 로고
    • Tissue-specific expression of a gene encoding a cell wall-localized lipid transfer protein from Arabidopsis
    • Thoma S, Hecht U, Kippers A, Botella J, De Vries S, Somerville C (1994) Tissue-specific expression of a gene encoding a cell wall-localized lipid transfer protein from Arabidopsis. Plant Physiol 105:35-45
    • (1994) Plant Physiol , vol.105 , pp. 35-45
    • Thoma, S.1    Hecht, U.2    Kippers, A.3    Botella, J.4    De Vries, S.5    Somerville, C.6
  • 137
    • 0032430834 scopus 로고    scopus 로고
    • Separate jasmonate-dependent and salicylate-dependent defense-response pathways in Arabidopsis are essential for resistance to distinct microbial pathogens
    • Thomma B, Eggermont K, Penninckx I, Mauch-Mani B, Vogelsang R, Cammue B, Broekaert W (1998) Separate jasmonate-dependent and salicylate-dependent defense-response pathways in Arabidopsis are essential for resistance to distinct microbial pathogens. Proc Natl Acad Sci USA 95:15107-15111
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15107-15111
    • Thomma, B.1    Eggermont, K.2    Penninckx, I.3    Mauch-Mani, B.4    Vogelsang, R.5    Cammue, B.6    Broekaert, W.7
  • 138
    • 0032126924 scopus 로고    scopus 로고
    • Tissue-specific expression of plant defensin genes PDF2.1 and PDF2.2 in Arabidopsis thaliana
    • Thomma BPHJ, Broekaert WF (1998) Tissue-specific expression of plant defensin genes PDF2.1 and PDF2.2 in Arabidopsis thaliana. Plant Physiol Biochem 36:533-537
    • (1998) Plant Physiol Biochem , vol.36 , pp. 533-537
    • Thomma, B.P.H.J.1    Broekaert, W.F.2
  • 139
    • 4043175614 scopus 로고    scopus 로고
    • Tissue-specific expression of head-to-tail cyclized miniproteins in Violaceae and structure determination of the root cyclotide Viola hederacea root cyclotide1
    • Trabi M, Craik DJ (2004) Tissue-specific expression of head-to-tail cyclized miniproteins in Violaceae and structure determination of the root cyclotide Viola hederacea root cyclotide1. Plant Cell 16:2204-2216
    • (2004) Plant Cell , vol.16 , pp. 2204-2216
    • Trabi, M.1    Craik, D.J.2
  • 141
    • 0026554314 scopus 로고
    • Nonspecific lipid transfer protein in castor bean cotyledon cells: Subcellular localization and a possible role in lipid metabolism
    • Tsuboi S, Osafune T, Tsugeki R, Nishimura M, Yamada M (1992) Nonspecific lipid transfer protein in castor bean cotyledon cells: subcellular localization and a possible role in lipid metabolism. J Biochem 111:500-508
    • (1992) J Biochem , vol.111 , pp. 500-508
    • Tsuboi, S.1    Osafune, T.2    Tsugeki, R.3    Nishimura, M.4    Yamada, M.5
  • 143
    • 78549295936 scopus 로고    scopus 로고
    • Permeabilization of fungal hyphae by the plant defensin NaD1 occurs through a cell wall-dependent process
    • van der Weerden NL, Hancock RE, Anderson MA (2010) Permeabilization of fungal hyphae by the plant defensin NaD1 occurs through a cell wall-dependent process. J Biol Chem 285:37513-37520
    • (2010) J Biol Chem , vol.285 , pp. 37513-37520
    • van der Weerden, N.L.1    Hancock, R.E.2    Anderson, M.A.3
  • 144
    • 85029561620 scopus 로고    scopus 로고
    • The plant defensin NaD1 enters the cytoplasm of Fusarium oxysporum hyphae
    • van der Weerden NL, Lay FT, Anderson MA (2008) The plant defensin NaD1 enters the cytoplasm of Fusarium oxysporum hyphae. J Biol Chem 13:13
    • (2008) J Biol Chem , vol.13 , pp. 13
    • van der Weerden, N.L.1    Lay, F.T.2    Anderson, M.A.3
  • 145
    • 12544251245 scopus 로고    scopus 로고
    • Structural dissection of a highly knotted peptide reveals minimal motif with antimicrobial activity
    • Vila-Perello M, Sanchez-Vallet A, Garcia-Olmedo F, Molina A, Andreu D (2005) Structural dissection of a highly knotted peptide reveals minimal motif with antimicrobial activity. J Biol Chem 280:1661-1668
    • (2005) J Biol Chem , vol.280 , pp. 1661-1668
    • Vila-Perello, M.1    Sanchez-Vallet, A.2    Garcia-Olmedo, F.3    Molina, A.4    Andreu, D.5
  • 146
    • 70349591891 scopus 로고    scopus 로고
    • Despite a conserved cystine knot motif, different cyclotides have different membrane binding modes
    • Wang CK, Colgrave ML, Ireland DC, Kaas Q, Craik DJ (2009) Despite a conserved cystine knot motif, different cyclotides have different membrane binding modes. Biophys J 97:1471-1481
    • (2009) Biophys J , vol.97 , pp. 1471-1481
    • Wang, C.K.1    Colgrave, M.L.2    Ireland, D.C.3    Kaas, Q.4    Craik, D.J.5
  • 149
    • 0034613541 scopus 로고    scopus 로고
    • Defense proteins from seed of Cassia fistula include a lipid transfer protein homologue and a protease inhibitory plant defensin
    • 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
  • 150
    • 77950343795 scopus 로고    scopus 로고
    • PEPR2 is a second receptor for the Pep1 and Pep2 peptides and contributes to defense responses in Arabidopsis
    • Yamaguchi Y, Huffaker A, Bryan AC, Tax FE, Ryan CA (2010) PEPR2 is a second receptor for the Pep1 and Pep2 peptides and contributes to defense responses in Arabidopsis. Plant Cell 22:508-522
    • (2010) Plant Cell , vol.22 , pp. 508-522
    • Yamaguchi, Y.1    Huffaker, A.2    Bryan, A.C.3    Tax, F.E.4    Ryan, C.A.5
  • 152
    • 67849130752 scopus 로고    scopus 로고
    • The chitin-binding capability of Cy-AMP1 from cycad is essential to antifungal activity
    • Yokoyama S, Iida Y, Kawasaki Y, Minami Y, Watanabe K, Yagi F (2009) The chitin-binding capability of Cy-AMP1 from cycad is essential to antifungal activity. J Pept Sci 15:492-497
    • (2009) J Pept Sci , vol.15 , pp. 492-497
    • Yokoyama, S.1    Iida, Y.2    Kawasaki, Y.3    Minami, Y.4    Watanabe, K.5    Yagi, F.6
  • 153
    • 55949098106 scopus 로고    scopus 로고
    • Purification, characterization, and sequencing of antimicrobial peptides, Cy-AMP1, Cy-AMP2, and Cy-AMP3, from the Cycad (Cycas revoluta) seeds
    • Yokoyama S, Kato K, Koba A, Minami Y, Watanabe K, Yagi F (2008) Purification, characterization, and sequencing of antimicrobial peptides, Cy-AMP1, Cy-AMP2, and Cy-AMP3, from the Cycad (Cycas revoluta) seeds. Peptides 29:2110-2117
    • (2008) Peptides , vol.29 , pp. 2110-2117
    • Yokoyama, S.1    Kato, K.2    Koba, A.3    Minami, Y.4    Watanabe, K.5    Yagi, F.6
  • 154
    • 73849141151 scopus 로고    scopus 로고
    • Arabidopsis thaliana class-II TGA transcription factors are essential activators of jasmonic acid/ethylene-induced defense responses
    • Zander M, La Camera S, Lamotte O, Metraux JP, Gatz C (2009) Arabidopsis thaliana class-II TGA transcription factors are essential activators of jasmonic acid/ethylene-induced defense responses. Plant J 61:200-210
    • (2009) Plant J , vol.61 , pp. 200-210
    • Zander, M.1    La Camera, S.2    Lamotte, O.3    Metraux, J.P.4    Gatz, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.