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Volumn 11, Issue 3, 2010, Pages 210-219

Structural aspects of plant antimicrobial peptides

Author keywords

Antimicrobial peptides; Cyclotides; Defensins; Lipid transfer proteins; Plant; Snakins; Thionins

Indexed keywords

ALPHA DEFENSIN; BETA DEFENSIN; CYCLOTIDE; LIPID TRANSFER PROTEIN; POLYPEPTIDE ANTIBIOTIC AGENT; SCAFFOLD PROTEIN; SNAKIN 1; SNAKIN 2; THIONIN PEPTIDE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 77952632254     PISSN: 13892037     EISSN: None     Source Type: Journal    
DOI: 10.2174/138920310791112093     Document Type: Article
Times cited : (64)

References (94)
  • 1
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand, R.M.; Vogel, H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta, 1999, 1462, 11-28.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 2
    • 34247137266 scopus 로고    scopus 로고
    • Antimicrobial peptides and plant disease control
    • Montesinos, E. Antimicrobial peptides and plant disease control. FEMS Microbiol. Lett., 2007, 270, 1-11.
    • (2007) FEMS Microbiol. Lett , vol.270 , pp. 1-11
    • Montesinos, E.1
  • 3
    • 11244258268 scopus 로고    scopus 로고
    • Plant defense and antimicrobial peptides
    • Castro, M.S.; Fontes, W. Plant defense and antimicrobial peptides. Protein Pept. Lett., 2005, 12, 13-18.
    • (2005) Protein Pept. Lett , vol.12 , pp. 13-18
    • Castro, M.S.1    Fontes, W.2
  • 4
    • 13844322064 scopus 로고    scopus 로고
    • Defensins-components of the innate immune system in plants
    • Lay, F.T.; Anderson, M.A. Defensins-components of the innate immune system in plants. Curr. Protein Pept. Sci., 2005, 6, 85-101.
    • (2005) Curr. Protein Pept. Sci , vol.6 , pp. 85-101
    • Lay, F.T.1    Anderson, M.A.2
  • 6
    • 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. Snakin-2, an antimicrobial peptide from potato whose gene is locally induced by wounding and responds to pathogen infection. Plant Physiol., 2002, 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
  • 7
    • 0001131393 scopus 로고
    • A crystalline protein obtained from a lipoprotein of wheat flour
    • Balls, A.K.; Hale, W.S.; Harris, T.H. A crystalline protein obtained from a lipoprotein of wheat flour. Cereal Chem., 1942, 19, 951-961.
    • (1942) Cereal Chem , vol.19 , pp. 951-961
    • Balls, A.K.1    Hale, W.S.2    Harris, T.H.3
  • 10
    • 34548809144 scopus 로고    scopus 로고
    • Is there a difference in metal ion-based inhibition between members of thionin family: Molecular dynamics simulation study?
    • Oard, S.; Karki, B.; Enright, F. Is there a difference in metal ion-based inhibition between members of thionin family: molecular dynamics simulation study? Biophys. Chem., 2007, 130, 65-75.
    • (2007) Biophys. Chem , vol.130 , pp. 65-75
    • Oard, S.1    Karki, B.2    Enright, F.3
  • 11
    • 18344406534 scopus 로고    scopus 로고
    • Stimulation of prothrombinase activity by the nonapeptide Thr-Trp-Ala-Arg-Asn-Ser-Tyr-Asn-Val, a segment of a plant thionin
    • Osorio e Castro, V.R.; Vernon, L.P. Stimulation of prothrombinase activity by the nonapeptide Thr-Trp-Ala-Arg-Asn-Ser-Tyr-Asn-Val, a segment of a plant thionin. Peptides, 2003, 24, 515-521.
    • (2003) Peptides , vol.24 , pp. 515-521
    • Osorio e Castro, V.R.1    Vernon, L.P.2
  • 12
    • 0022380625 scopus 로고
    • A toxic thionin from Pyrularia pubera: Purification, properties and amino acid sequence
    • Vernon, L.P.; Evett, G.E.; Zeikus, R.D.; Gray, W.R. A toxic thionin from Pyrularia pubera: purification, properties and amino acid sequence. Arch. Biochem. Biophys., 1985, 238, 18-29.
    • (1985) Arch. Biochem. Biophys , vol.238 , pp. 18-29
    • Vernon, L.P.1    Evett, G.E.2    Zeikus, R.D.3    Gray, W.R.4
  • 13
    • 0037432186 scopus 로고    scopus 로고
    • Synthetic and structural studies on Pyrularia pubera thionin: A single-residue mutation enhances activity against Gram-negative bacteria
    • Vila-Perello, M.; Sanchez-Vallet, A.; Garcia-Olmedo, F.; Molina, A.; Andreu, D. Synthetic and structural studies on Pyrularia pubera thionin: a single-residue mutation enhances activity against Gram-negative bacteria. FEBS Lett., 2003, 536, 215-519.
    • (2003) FEBS Lett , vol.536 , pp. 215-519
    • Vila-Perello, M.1    Sanchez-Vallet, A.2    Garcia-Olmedo, F.3    Molina, A.4    Andreu, D.5
  • 14
    • 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. Structural dissection of a highly knotted peptide reveals minimal motif with antimicrobial activity. J. Biol. Chem., 2005, 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
  • 15
    • 0027959528 scopus 로고
    • Organ-specific expression of highly divergent thionin variants that are distinct from the seed-specific crambin in the crucifer Crambe abyssinica
    • Schrader-Fischer, G.; Apel, K. Organ-specific expression of highly divergent thionin variants that are distinct from the seed-specific crambin in the crucifer Crambe abyssinica. Mol. Gen. Genet., 1994, 245, 380-389.
    • (1994) Mol. Gen. Genet , vol.245 , pp. 380-389
    • Schrader-Fischer, G.1    Apel, K.2
  • 17
    • 67349088413 scopus 로고    scopus 로고
    • Plant defensins-prospects for the biological functions and biotechnological properties
    • Carvalho Ade, O.; Gomes, V.M. Plant defensins-prospects for the biological functions and biotechnological properties. Peptides, 2009, 30, 1007-1020.
    • (2009) Peptides , vol.30 , pp. 1007-1020
    • Carvalho Ade, O.1    Gomes, V.M.2
  • 19
    • 0029347190 scopus 로고
    • Plant defensins: Novel antimicrobial peptides as components of the host defense system
    • Broekaert, W.F.; Terras, F.R.; Cammue, B.P.; Osborn, R.W. Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol., 1995, 108, 1353-1358.
    • (1995) Plant Physiol , vol.108 , pp. 1353-1358
    • Broekaert, W.F.1    Terras, F.R.2    Cammue, B.P.3    Osborn, R.W.4
  • 20
    • 0025080513 scopus 로고
    • γ-Purothionins: Amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm
    • Colilla, F.J.; Rocher, A.; Mendez, E. γ-Purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. FEBS Lett., 1990, 270, 191-194.
    • (1990) FEBS Lett , vol.270 , pp. 191-194
    • Colilla, F.J.1    Rocher, A.2    Mendez, E.3
  • 21
    • 0025670589 scopus 로고
    • Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, gamma-hordothionin, from barley endosperm
    • Mendez, E.; Moreno, A.; Colilla, F.; Pelaez, F.; Limas, G.G.; Mendez, R.; Soriano, F.; Salinas, M.; de Haro, C. Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, gamma-hordothionin, from barley endosperm. Eur. J. Biochem., 1990, 194, 533-539.
    • (1990) Eur. 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    de Haro, C.9
  • 22
    • 0025976182 scopus 로고
    • A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds or sorghum (Sorghum bicolar (L) Moench) have sequence homologies with wheat gamma-purothionins
    • Bloch, C., Jr.; Richardson, M. A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds or sorghum (Sorghum bicolar (L) Moench) have sequence homologies with wheat gamma-purothionins. FEBS Lett., 1991, 279, 101-104.
    • (1991) FEBS Lett , vol.279 , pp. 101-104
    • Bloch Jr., C.1    Richardson, M.2
  • 23
    • 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, M.A.; Santoro, J.; Gonzalez, C.; Colilla, F.J.; Mendez, E.; Rico, M. 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, 1993, 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
  • 25
    • 36248957133 scopus 로고    scopus 로고
    • A review of defensins of diverse origins
    • Wong, J.H.; Xia, L.; Ng, T.B. A review of defensins of diverse origins. Curr. Protein Pept. Sci., 2007, 8, 446-459.
    • (2007) Curr. Protein Pept. Sci , vol.8 , pp. 446-459
    • Wong, J.H.1    Xia, L.2    Ng, T.B.3
  • 26
    • 34848836028 scopus 로고    scopus 로고
    • Discovery of six families of fungal defensin-like peptides provides insights into origin and evolution of the CSalphabeta defensins
    • Zhu, S. Discovery of six families of fungal defensin-like peptides provides insights into origin and evolution of the CSalphabeta defensins. Mol. Immunol., 2008, 45, 828-838.
    • (2008) Mol. Immunol , vol.45 , pp. 828-838
    • Zhu, S.1
  • 27
    • 0036257512 scopus 로고    scopus 로고
    • Molecular diversity in gene-encoded, cationic antimicrobial polypeptides
    • Tossi, A.; Sandri, L. Molecular diversity in gene-encoded, cationic antimicrobial polypeptides. Curr. Pharm. Des., 2002, 8, 743-761.
    • (2002) Curr. Pharm. Des , vol.8 , pp. 743-761
    • Tossi, A.1    Sandri, L.2
  • 32
    • 33646807759 scopus 로고    scopus 로고
    • Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids
    • Liu, Y.J.; Cheng, C.S.; Lai, S.M.; Hsu, M.P.; Chen, C.S.; Lyu, P.C. Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids. Proteins, 2006, 63, 777-786.
    • (2006) Proteins , vol.63 , pp. 777-786
    • Liu, Y.J.1    Cheng, C.S.2    Lai, S.M.3    Hsu, M.P.4    Chen, C.S.5    Lyu, P.C.6
  • 33
    • 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
    • Thevissen, K.; Osborn, R.W.; Acland, D.P.; Broekaert, W.F. Specific binding sites for an antifungal plant defensin from Dahlia (Dahlia merckii) on fungal cells are required for antifungal activity. Mol. Plant Microbe Interact., 2000, 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
  • 34
    • 0031238744 scopus 로고    scopus 로고
    • Cadmium leads to stimulated expression of the lipid transfer protein genes in barley: Implications for the involvement of lipid transfer proteins in wax assembly
    • Hollenbach, B.; Schreiber, L.; Hartung, W.; Dietz, K.J. Cadmium leads to stimulated expression of the lipid transfer protein genes in barley: implications for the involvement of lipid transfer proteins in wax assembly. Planta, 1997, 203, 9-19.
    • (1997) Planta , vol.203 , pp. 9-19
    • Hollenbach, B.1    Schreiber, L.2    Hartung, W.3    Dietz, K.J.4
  • 35
    • 0030174964 scopus 로고    scopus 로고
    • New antifungal proteins from sugar beet (Beta vulgaris L.) showing homology to non-specific lipid transfer proteins
    • Nielsen, K.K.; Nielsen, J.E.; Madrid, S.M.; Mikkelsen, J.D. New antifungal proteins from sugar beet (Beta vulgaris L.) showing homology to non-specific lipid transfer proteins. Plant Mol. Biol., 1996, 31, 539-552.
    • (1996) Plant Mol. Biol , vol.31 , pp. 539-552
    • Nielsen, K.K.1    Nielsen, J.E.2    Madrid, S.M.3    Mikkelsen, J.D.4
  • 36
    • 0000876838 scopus 로고    scopus 로고
    • Localization of expression of three cold-induced genes, blt101, blt4. 9, and blt14, in different tissues of the crown and developing leaves of cold-acclimated cultivated barley
    • Pearce, R.S.; Houlston, C.E.; Atherton, K.M.; Rixon, J.E.; Harrison, P.; Hughes, M.A.; Alison Dunn, M. Localization of expression of three cold-induced genes, blt101, blt4. 9, and blt14, in different tissues of the crown and developing leaves of cold-acclimated cultivated barley. Plant Physiol., 1998, 117, 787-795.
    • (1998) Plant Physiol , vol.117 , pp. 787-795
    • Pearce, R.S.1    Houlston, C.E.2    Atherton, K.M.3    Rixon, J.E.4    Harrison, P.5    Hughes, M.A.6    Alison Dunn, M.7
  • 38
    • 0033782344 scopus 로고    scopus 로고
    • Purification and structural characterization of LTP1 polypeptides from beer
    • Jegou, S.; Douliez, J.P.; Molle, D.; Boivin, P.; Marion, D. Purification and structural characterization of LTP1 polypeptides from beer. J. Agric. Food Chem., 2000, 48, 5023-5029.
    • (2000) J. Agric. Food Chem , vol.48 , pp. 5023-5029
    • Jegou, S.1    Douliez, J.P.2    Molle, D.3    Boivin, P.4    Marion, D.5
  • 39
    • 0027568154 scopus 로고
    • A non-specific lipid transfer protein from Arabidopsis is a cell wall protein
    • Thoma, S.; Kaneko, Y.; Somerville, C. A non-specific lipid transfer protein from Arabidopsis is a cell wall protein. Plant J., 1993, 3, 427-436.
    • (1993) Plant J , vol.3 , pp. 427-436
    • Thoma, S.1    Kaneko, Y.2    Somerville, C.3
  • 40
    • 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, P.E. Identification of a lipid transfer protein as the major protein in the surface wax of broccoli (Brassica oleracea) leaves. Arch. Biochem. Biophys., 1994, 311, 460-468.
    • (1994) Arch. Biochem. Biophys , vol.311 , pp. 460-468
    • Pyee, J.1    Yu, H.2    Kolattukudy, P.E.3
  • 41
    • 0035078262 scopus 로고    scopus 로고
    • Disulfide bond assignment, lipid transfer activity and secondary structure of a 7-kDa plant lipid transfer protein, LTP2
    • Douliez, J.P.; Pato, C.; Rabesona, H.; Molle, D.; Marion, D. Disulfide bond assignment, lipid transfer activity and secondary structure of a 7-kDa plant lipid transfer protein, LTP2. Eur. J. Biochem., 2001, 268, 1400-1403.
    • (2001) Eur. J. Biochem , vol.268 , pp. 1400-1403
    • Douliez, J.P.1    Pato, C.2    Rabesona, H.3    Molle, D.4    Marion, D.5
  • 42
    • 0029643949 scopus 로고
    • High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings
    • Shin, D.H.; Lee, J.Y.; Hwang, K.Y.; Kim, K.K.; Suh, S.W. High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings. Structure, 1995, 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
  • 44
    • 0033082341 scopus 로고    scopus 로고
    • Solution structure of a lipid transfer protein extracted from rice seeds. Comparison with homologous proteins
    • Poznanski, J.; Sodano, P.; Suh, S.W.; Lee, J.Y.; Ptak, M.; Vovelle, F. Solution structure of a lipid transfer protein extracted from rice seeds. Comparison with homologous proteins. Eur. J. Biochem., 1999, 259, 692-708.
    • (1999) Eur. J. Biochem , vol.259 , pp. 692-708
    • Poznanski, J.1    Sodano, P.2    Suh, S.W.3    Lee, J.Y.4    Ptak, M.5    Vovelle, F.6
  • 45
    • 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, J.P.; Caille, A.; Marion, D.; Ptak, M.; Vovelle, F. 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., 1994, 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
  • 46
    • 17144404580 scopus 로고    scopus 로고
    • Characterization and structural analyses of non-specific lipid transfer protein 1 from mung bean
    • Lin, K.F.; Liu, Y.N.; Hsu, S.T.; Samuel, D.; Cheng, C.S.; Bonvin, A.M.; Lyu, P.C. Characterization and structural analyses of non-specific lipid transfer protein 1 from mung bean. Biochemistry, 2005, 44, 5703-5712.
    • (2005) Biochemistry , vol.44 , pp. 5703-5712
    • Lin, K.F.1    Liu, Y.N.2    Hsu, S.T.3    Samuel, D.4    Cheng, C.S.5    Bonvin, A.M.6    Lyu, P.C.7
  • 47
    • 33744810845 scopus 로고    scopus 로고
    • Accessibility of tobacco lipid transfer protein cavity revealed by 15N NMR relaxation studies and molecular dynamics simulations
    • Da Silva, P.; Landon, C.; Beltoise, R.; Ponchet, M.; Vovelle, F. Accessibility of tobacco lipid transfer protein cavity revealed by 15N NMR relaxation studies and molecular dynamics simulations. Proteins, 2006, 64, 124-132.
    • (2006) Proteins , vol.64 , pp. 124-132
    • da Silva, P.1    Landon, C.2    Beltoise, R.3    Ponchet, M.4    Vovelle, F.5
  • 48
    • 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, W.F.; Marion, D.; Acland, D.P.; Ptak, M.; Vovelle, F.; Sodano, P. Solution structure of Ace-AMP1, a potent antimicrobial protein extracted from onion seeds: structural analogies with plant nonspecific lipid transfer proteins. Biochemistry, 1998, 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
  • 49
    • 16344384006 scopus 로고    scopus 로고
    • Solution structure of a tobacco lipid transfer protein exhibiting new biophysical and biological features
    • Da Silva, P.; Landon, C.; Industri, B.; Marais, A.; Marion, D.; Ponchet, M.; Vovelle, F. Solution structure of a tobacco lipid transfer protein exhibiting new biophysical and biological features. Proteins, 2005, 59, 356-367.
    • (2005) Proteins , vol.59 , pp. 356-367
    • da Silva, P.1    Landon, C.2    Industri, B.3    Marais, A.4    Marion, D.5    Ponchet, M.6    Vovelle, F.7
  • 51
    • 0038191045 scopus 로고    scopus 로고
    • Refined solution structure of a liganded type 2 wheat nonspecific lipid transfer protein
    • Pons, J.L.; de Lamotte, F.; Gautier, M.F.; Delsuc, M.A. Refined solution structure of a liganded type 2 wheat nonspecific lipid transfer protein. J. Biol. Chem., 2003, 278, 14249-14256.
    • (2003) J. Biol. Chem , vol.278 , pp. 14249-14256
    • Pons, J.L.1    de Lamotte, F.2    Gautier, M.F.3    Delsuc, M.A.4
  • 52
    • 0037144489 scopus 로고    scopus 로고
    • Solution structure of plant nonspecific lipid transfer protein-2 from rice (Oryza sativa)
    • Samuel, D.; Liu, Y.J.; Cheng, C.S.; Lyu, P.C. Solution structure of plant nonspecific lipid transfer protein-2 from rice (Oryza sativa). J. Biol. Chem., 2002, 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
  • 53
    • 0942278892 scopus 로고    scopus 로고
    • Resistance function of rice lipid transfer protein LTP110
    • Ge, X.; Chen, J.; Li, N.; Lin, Y.; Sun, C.; Cao, K. Resistance function of rice lipid transfer protein LTP110. J. Biochem. Mol. Biol., 2003, 36, 603-607.
    • (2003) J. Biochem. Mol. Biol , vol.36 , pp. 603-607
    • Ge, X.1    Chen, J.2    Li, N.3    Lin, Y.4    Sun, C.5    Cao, K.6
  • 55
    • 34548667473 scopus 로고    scopus 로고
    • Post-translational modification of barley LTP1b: The lipid adduct lies in the hydrophobic cavity and alters the protein dynamics
    • Wijesinha-Bettoni, R.; Gao, C.; Jenkins, J.A.; Mackie, A.R.; Wilde, P.J.; Mills, E.N.; Smith, L.J. Post-translational modification of barley LTP1b: the lipid adduct lies in the hydrophobic cavity and alters the protein dynamics. FEBS Lett, 2007, 581, 4557-4561.
    • (2007) FEBS Lett , vol.581 , pp. 4557-4561
    • Wijesinha-Bettoni, R.1    Gao, C.2    Jenkins, J.A.3    Mackie, A.R.4    Wilde, P.J.5    Mills, E.N.6    Smith, L.J.7
  • 56
    • 44449135472 scopus 로고    scopus 로고
    • Comparison of the adsorbed conformation of barley lipid transfer protein at the decane-water and vacuum-water interface: A molecular dynamics simulation
    • Euston, S.R.; Hughes, P.; Naser, M.A.; Westacott, R.E. Comparison of the adsorbed conformation of barley lipid transfer protein at the decane-water and vacuum-water interface: a molecular dynamics simulation. Biomacromolecules, 2008, 9, 1443-1453.
    • (2008) Biomacromolecules , vol.9 , pp. 1443-1453
    • Euston, S.R.1    Hughes, P.2    Naser, M.A.3    Westacott, R.E.4
  • 57
    • 57049132826 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the cooperative adsorption of barley lipid transfer protein and cis-isocohumulone at the vacuum-water interface
    • Euston, S.R.; Hughes, P.; Naser, M.A.; Westacott, R.E. Molecular dynamics simulation of the cooperative adsorption of barley lipid transfer protein and cis-isocohumulone at the vacuum-water interface. Biomacromolecules, 2008, 9, 3024-3032.
    • (2008) Biomacromolecules , vol.9 , pp. 3024-3032
    • Euston, S.R.1    Hughes, P.2    Naser, M.A.3    Westacott, R.E.4
  • 58
    • 38549150372 scopus 로고    scopus 로고
    • Mutagenesis study of rice nonspecific lipid transfer protein 2 reveals residues that contribute to structure and ligand binding
    • Cheng, C.S.; Chen, M.N.; Lai, Y.T.; Chen, T.; Lin, K.F.; Liu, Y.J.; Lyu, P.C. Mutagenesis study of rice nonspecific lipid transfer protein 2 reveals residues that contribute to structure and ligand binding. Proteins, 2008, 70, 695-706.
    • (2008) Proteins , vol.70 , pp. 695-706
    • Cheng, C.S.1    Chen, M.N.2    Lai, Y.T.3    Chen, T.4    Lin, K.F.5    Liu, Y.J.6    Lyu, P.C.7
  • 59
    • 50049131120 scopus 로고    scopus 로고
    • The structure of defective in induced resistance protein of Arabidopsis thaliana, DIR1, reveals a new type of lipid transfer protein
    • Lascombe, M.B.; Bakan, B.; Buhot, N.; Marion, D.; Blein, J.P.; Larue, V.; Lamb, C.; Prange, T. The structure of defective in induced resistance protein of Arabidopsis thaliana, DIR1, reveals a new type of lipid transfer protein. Protein Sci., 2008, 17, 1522-1530.
    • (2008) Protein Sci , vol.17 , pp. 1522-1530
    • Lascombe, M.B.1    Bakan, B.2    Buhot, N.3    Marion, D.4    Blein, J.P.5    Larue, V.6    Lamb, C.7    Prange, T.8
  • 60
    • 0034793341 scopus 로고    scopus 로고
    • Plant cyclotides: Circular, knotted peptide toxins
    • Craik, D.J. Plant cyclotides: circular, knotted peptide toxins. Toxicon, 2001, 39, 1809-1813.
    • (2001) Toxicon , vol.39 , pp. 1809-1813
    • Craik, D.J.1
  • 61
    • 2442715239 scopus 로고    scopus 로고
    • Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: The importance of the cyclic cystine knot
    • Colgrave, M.L.; Craik, D.J. Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: the importance of the cyclic cystine knot. Biochemistry, 2004, 43, 5965-5975.
    • (2004) Biochemistry , vol.43 , pp. 5965-5975
    • Colgrave, M.L.1    Craik, D.J.2
  • 62
    • 0028927655 scopus 로고
    • Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1
    • Saether, O.; Craik, D.J.; Campbell, I.D.; Sletten, K.; Juul, J.; Norman, D.G. Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1. Biochemistry, 1995, 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
  • 63
    • 0000014794 scopus 로고
    • An oxytocic principle found in Oldenlandia affinis DC. An indigenous, Congolese drug "Kalata-Kalata" used to accelerate delivery
    • Gran, L. An oxytocic principle found in Oldenlandia affinis DC. An indigenous, Congolese drug "Kalata-Kalata" used to accelerate delivery. Medd. Nor. Farm. Selsk., 1970, 12, 173-180.
    • (1970) Medd. Nor. Farm. Selsk , vol.12 , pp. 173-180
    • Gran, L.1
  • 65
    • 71849113184 scopus 로고    scopus 로고
    • Cyclotide proteins and precursors from the genus Gloeospermum: Filling a blank spot in the cyclotide map of Violaceae
    • Burman, R.; Gruber, C.W.; Rizzardi, K.; Herrmann, A.; Craik, D.J.; Gupta, M.P.; Goransson, U. Cyclotide proteins and precursors from the genus Gloeospermum: Filling a blank spot in the cyclotide map of Violaceae. Phytochemistry, 2010, 71(1), 13-20.
    • (2010) Phytochemistry , vol.71 , Issue.1 , pp. 13-20
    • Burman, R.1    Gruber, C.W.2    Rizzardi, K.3    Herrmann, A.4    Craik, D.J.5    Gupta, M.P.6    Goransson, U.7
  • 67
    • 33645047649 scopus 로고    scopus 로고
    • Discovery and characterization of a linear cyclotide from Viola odorata: Implications for the processing of circular proteins
    • Ireland, D.C.; Colgrave, M.L.; Nguyencong, P.; Daly, N.L.; Craik, D.J. Discovery and characterization of a linear cyclotide from Viola odorata: implications for the processing of circular proteins. J. Mol. Biol., 2006, 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
  • 68
    • 65949100618 scopus 로고    scopus 로고
    • Circular proteins from Melicytus (Violaceae) refine the conserved protein and gene architecture of cyclotides
    • Trabi, M.; Mylne, J.S.; Sando, L.; Craik, D.J. Circular proteins from Melicytus (Violaceae) refine the conserved protein and gene architecture of cyclotides. Org. Biomol. Chem., 2009, 7, 2378-2388.
    • (2009) Org. Biomol. Chem , vol.7 , pp. 2378-2388
    • Trabi, M.1    Mylne, J.S.2    Sando, L.3    Craik, D.J.4
  • 69
  • 70
    • 70349591891 scopus 로고    scopus 로고
    • Despite a conserved cystine knot motif, different cyclotides have different membrane binding modes
    • Wang, C.K.; Colgrave, M.L.; Ireland, D.C.; Kaas, Q.; Craik, D.J. Despite a conserved cystine knot motif, different cyclotides have different membrane binding modes. Biophys. J., 2009, 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
  • 71
    • 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. Biosynthesis and insecticidal properties of plant cyclotides: the cyclic knotted proteins from Oldenlandia affinis. Proc. Natl. Acad. Sci. USA, 2001, 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
  • 73
    • 57849088141 scopus 로고    scopus 로고
    • Anthelmintic activity of cyclotides: In vitro studies with canine and human hookworms
    • Colgrave, M.L.; Kotze, A.C.; Kopp, S.; McCarthy, J.S.; Coleman, G.T.; Craik, D.J. Anthelmintic activity of cyclotides: In vitro studies with canine and human hookworms. Acta Trop, 2009, 109, 163-166.
    • (2009) Acta Trop , vol.109 , pp. 163-166
    • Colgrave, M.L.1    Kotze, A.C.2    Kopp, S.3    McCarthy, J.S.4    Coleman, G.T.5    Craik, D.J.6
  • 74
    • 33646248365 scopus 로고    scopus 로고
    • The cyclotide family of circular miniproteins: Nature's combinatorial peptide template
    • Craik, D.J.; Cemazar, M.; Wang, C.K.; Daly, N.L. The cyclotide family of circular miniproteins: nature's combinatorial peptide template. Biopolymers, 2006, 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
  • 75
    • 33947359890 scopus 로고    scopus 로고
    • NMR as a tool for elucidating the structures of circular and knotted proteins
    • Craik, D.J.; Daly, N.L. NMR as a tool for elucidating the structures of circular and knotted proteins. Mol. Biosyst., 2007, 3, 257-265.
    • (2007) Mol. Biosyst , vol.3 , pp. 257-265
    • Craik, D.J.1    Daly, N.L.2
  • 76
    • 67449106989 scopus 로고    scopus 로고
    • Combined X-ray and NMR analysis of the stability of the cyclotide cystine knot fold that underpins its insecticidal activity and potential use as a drug scaffold
    • Wang, C.K.; Hu, S.H.; Martin, J.L.; Sjogren, T.; Hajdu, J.; Bohlin, L.; Claeson, P.; Goransson, U.; Rosengren, K.J.; Tang, J.; Tan, N.H.; Craik, D.J. Combined X-ray and NMR analysis of the stability of the cyclotide cystine knot fold that underpins its insecticidal activity and potential use as a drug scaffold. J. Biol. Chem., 2009, 284, 10672-10683.
    • (2009) J. Biol. Chem , vol.284 , pp. 10672-10683
    • Wang, C.K.1    Hu, S.H.2    Martin, J.L.3    Sjogren, T.4    Hajdu, J.5    Bohlin, L.6    Claeson, P.7    Goransson, U.8    Rosengren, K.J.9    Tang, J.10    Tan, N.H.11    Craik, D.J.12
  • 78
    • 34547098170 scopus 로고    scopus 로고
    • A novel plant protein-disulfide isomerase involved in the oxidative folding of cystine knot defense proteins
    • Gruber, C.W.; Cemazar, M.; Clark, R.J.; Horibe, T.; Renda, R.F.; Anderson, M.A.; Craik, D.J. A novel plant protein-disulfide isomerase involved in the oxidative folding of cystine knot defense proteins. J. Biol. Chem., 2007, 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
  • 79
    • 33847385325 scopus 로고    scopus 로고
    • Insecticidal plant cyclotides and related cystine knot toxins
    • Gruber, C.W.; Cemazar, M.; Anderson, M.A.; Craik, D.J. Insecticidal plant cyclotides and related cystine knot toxins. Toxicon, 2007, 49, 561-575.
    • (2007) Toxicon , vol.49 , pp. 561-575
    • Gruber, C.W.1    Cemazar, M.2    Anderson, M.A.3    Craik, D.J.4
  • 81
    • 33751073415 scopus 로고    scopus 로고
    • A novel suite of cyclotides from Viola odorata: Sequence variation and the implications for structure, function and stability
    • Ireland, D.C.; Colgrave, M.L.; Craik, D.J. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability. Biochem. J., 2006, 400, 1-12.
    • (2006) Biochem. J , vol.400 , pp. 1-12
    • Ireland, D.C.1    Colgrave, M.L.2    Craik, D.J.3
  • 83
    • 0033579483 scopus 로고    scopus 로고
    • Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif
    • Craik, D. J.; Daly, N.L.; Bond, T.; Waine, C. Plant cyclotides: a unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. J. Mol. Biol., 1999, 294, 1327-1336.
    • (1999) J. Mol. Biol , vol.294 , pp. 1327-1336
    • Craik, D.J.1    Daly, N.L.2    Bond, T.3    Waine, C.4
  • 84
    • 70349583511 scopus 로고    scopus 로고
    • Discovery, structure and biological activities of cyclotides
    • Daly, N.L.; Rosengren, K.J.; Craik, D.J. Discovery, structure and biological activities of cyclotides. Adv. Drug Deliv. Rev., 2009, 61, 918-930.
    • (2009) Adv. Drug Deliv. Rev , vol.61 , pp. 918-930
    • Daly, N.L.1    Rosengren, K.J.2    Craik, D.J.3
  • 85
    • 0037424506 scopus 로고    scopus 로고
    • Twists, knots, and rings in proteins. Structural definition of the cyclotide framework
    • Rosengren, K.J.; Daly, N.L.; Plan, M.R.; Waine, C.; Craik, D.J. Twists, knots, and rings in proteins. Structural definition of the cyclotide framework. J. Biol. Chem., 2003, 278, 8606-8616.
    • (2003) J. Biol. Chem , vol.278 , pp. 8606-8616
    • Rosengren, K.J.1    Daly, N.L.2    Plan, M.R.3    Waine, C.4    Craik, D.J.5
  • 86
    • 0035933743 scopus 로고    scopus 로고
    • Circular proteins in plants: Solution structure of a novel macrocyclic trypsin inhibitor from Momordica cochinchinensis
    • Felizmenio-Quimio, M.E.; Daly, N.L.; Craik, D.J. Circular proteins in plants: solution structure of a novel macrocyclic trypsin inhibitor from Momordica cochinchinensis. J. Biol. Chem., 2001, 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
  • 90
    • 42249092243 scopus 로고    scopus 로고
    • Overexpression of snakin-1 gene enhances resistance to Rhizoctonia solani and Erwinia carotovora in transgenic potato plants
    • Almasia, N.I.; Bazzini, A.A.; Hopp, H.E.; Vazquez-Rovere, C. Overexpression of snakin-1 gene enhances resistance to Rhizoctonia solani and Erwinia carotovora in transgenic potato plants. Mol. Plant Pathol., 2008, 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
  • 93
    • 0036301039 scopus 로고    scopus 로고
    • Solution structure of Pisum sativum defensin 1 by high resolution NMR: Plant defensins, identical backbone with different mechanisms of action
    • Almeida, M.S.; Cabral, K.M.; Kurtenbach, E.; Almeida, F.C.; Valente, A.P. Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical backbone with different mechanisms of action. J. Mol. Biol., 2002, 315, 749-757.
    • (2002) J. Mol. Biol , vol.315 , pp. 749-757
    • Almeida, M.S.1    Cabral, K.M.2    Kurtenbach, E.3    Almeida, F.C.4    Valente, A.P.5
  • 94
    • 23844519388 scopus 로고    scopus 로고
    • Structure of a liganded type 2 non-specific lipid-transfer protein from wheat and the molecular basis of lipid binding
    • Hoh, F.; Pons, J.L.; Gautier, M.F.; de Lamotte, F.; Dumas, C. Structure of a liganded type 2 non-specific lipid-transfer protein from wheat and the molecular basis of lipid binding. Acta Crystallogr. D Biol. Crystallogr., 2005, 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


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