메뉴 건너뛰기




Volumn 90, Issue 11-12, 2008, Pages 1667-1673

Seed defensins of barnyard grass Echinochloa crusgalli (L.) Beauv.

Author keywords

Antifungal activity; Defensins; Echinochloa crusgalli (L.) Beauv; Triticum kiharae Dorof. et Migusch; Weeds

Indexed keywords

DEFENSIN;

EID: 55349099842     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2008.06.007     Document Type: Article
Times cited : (46)

References (40)
  • 5
    • 44049091618 scopus 로고    scopus 로고
    • Hidden weapons of microbial destruction in plant genomes
    • 10.1186/gb-2007-8-9-225
    • Manners J.M. Hidden weapons of microbial destruction in plant genomes. Genome Biol. 8 (2007) 225 10.1186/gb-2007-8-9-225
    • (2007) Genome Biol. , vol.8 , pp. 225
    • Manners, J.M.1
  • 6
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat. Rev. Microbiol. 3 (2005) 238-250
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 7
    • 0036257512 scopus 로고    scopus 로고
    • Molecular diversity in gene-encoded, cationic antimicrobial polypeptides
    • Tossi A., and Sandri L. Molecular diversity in gene-encoded, cationic antimicrobial polypeptides. Curr. Pharm. Des. 8 (2002) 743-761
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 743-761
    • Tossi, A.1    Sandri, L.2
  • 8
    • 0025976182 scopus 로고
    • A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds of sorghum (Sorghum bicolor (L) Moench) have sequence homologies with wheat gamma-purothionins
    • Bloch C., and Richardson M. A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds of sorghum (Sorghum bicolor (L) Moench) have sequence homologies with wheat gamma-purothionins. FEBS Lett. 279 (1991) 101-104
    • (1991) FEBS Lett. , vol.279 , pp. 101-104
    • Bloch, C.1    Richardson, M.2
  • 9
    • 0036681427 scopus 로고    scopus 로고
    • Inhibition of trypsin by cow-pea thionin: characterization, molecular modeling, and docking
    • Melo F.R., Ridgen D.J., Franco O.L., Mello L.V., Ary M.B., Grossi-de-Sa M.F., et al. Inhibition of trypsin by cow-pea thionin: characterization, molecular modeling, and docking. Proteins 48 (2002) 311-319
    • (2002) Proteins , vol.48 , pp. 311-319
    • Melo, F.R.1    Ridgen, D.J.2    Franco, O.L.3    Mello, L.V.4    Ary, M.B.5    Grossi-de-Sa, M.F.6
  • 10
    • 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 G.M., Condron R., Hughes A.B., and Polya G.M. Defense proteins from seed of Cassia fistula include a lipid transfer protein homologue and a protease inhibitory plant defensin. Plant Sci. 159 (2000) 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
  • 11
    • 0029347190 scopus 로고
    • Plant defensins: novel antimicrobial peptides as components of the host defense system
    • Broekaert W.F., Terras F.R.G., Cammue B.P.A., and Osborn R.W. Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol. 108 (1995) 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
  • 13
    • 23944488734 scopus 로고    scopus 로고
    • Plant γ-thionins: novel insights on the mechanism of action of a multi-functional class of defense proteins
    • Pelegrini P.B., and Franco O.L. Plant γ-thionins: novel insights on the mechanism of action of a multi-functional class of defense proteins. Int. J. Biochem. Cell Biol. 37 (2005) 2239-2253
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 2239-2253
    • Pelegrini, P.B.1    Franco, O.L.2
  • 14
    • 13844322064 scopus 로고    scopus 로고
    • Defensins-components of the innate immune system in plants
    • Lay F.T., and Anderson M.A. Defensins-components of the innate immune system in plants. Curr. Protein Pept. Sci. 6 (2005) 85-101
    • (2005) Curr. Protein Pept. Sci. , vol.6 , pp. 85-101
    • Lay, F.T.1    Anderson, M.A.2
  • 15
    • 33846108632 scopus 로고    scopus 로고
    • Defensins knowledgebase: a manually curated database and information source focused on the defensins family of antimicrobial peptides
    • Seebah S., Suresh A., Zhuo S., Choong Y.H., Chua H., Chuon D., Beuerman R., and Verma C. Defensins knowledgebase: a manually curated database and information source focused on the defensins family of antimicrobial peptides. Nucleic Acids Res. Database issue (2007) D265-D268
    • (2007) Nucleic Acids Res. , Issue.Database issue
    • Seebah, S.1    Suresh, A.2    Zhuo, S.3    Choong, Y.H.4    Chua, H.5    Chuon, D.6    Beuerman, R.7    Verma, C.8
  • 16
  • 19
    • 0346665520 scopus 로고    scopus 로고
    • Isolation and properties of floral defensins from ornamental tobacco and petunia
    • Lay F.T., Brugliera F., and Anderson M.A. Isolation and properties of floral defensins from ornamental tobacco and petunia. Plant Physiol. 131 (2003) 1283-1293
    • (2003) Plant Physiol. , vol.131 , pp. 1283-1293
    • Lay, F.T.1    Brugliera, F.2    Anderson, M.A.3
  • 21
    • 15644372264 scopus 로고    scopus 로고
    • Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjacent sites important for antifungal activity
    • De Samblanx G.W., Goderis I.J., Thevissen K., Raemaekers R., Fant F., Borremans F., et al. Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjacent sites important for antifungal activity. J. Biol. Chem. 272 (1997) 1171-1179
    • (1997) J. Biol. Chem. , vol.272 , pp. 1171-1179
    • De Samblanx, G.W.1    Goderis, I.J.2    Thevissen, K.3    Raemaekers, R.4    Fant, F.5    Borremans, F.6
  • 22
  • 24
    • 0028271965 scopus 로고
    • Pseudothionin-St1, a potato peptide active against potato pathogens
    • Moreno M., Segura A., and Garcia-Olmedo F. Pseudothionin-St1, a potato peptide active against potato pathogens. Eur. J. Biochem. 223 (1994) 135-139
    • (1994) Eur. J. Biochem. , vol.223 , pp. 135-139
    • Moreno, M.1    Segura, A.2    Garcia-Olmedo, F.3
  • 25
    • 0030935921 scopus 로고    scopus 로고
    • Fabatins: new antimicrobial plant peptides
    • Zhang Y., and Lewis K. Fabatins: new antimicrobial plant peptides. Fems Microbiol. Lett. 149 (1997) 59-64
    • (1997) Fems Microbiol. Lett. , vol.149 , pp. 59-64
    • Zhang, Y.1    Lewis, K.2
  • 26
    • 0032436013 scopus 로고    scopus 로고
    • Functional and structural features of gamma-zeathionins, a new class of sodium channel blockers
    • Kushmerick C., Castro M.D., Cruz J.S., Bloch C., and Beirao P.S.L. Functional and structural features of gamma-zeathionins, a new class of sodium channel blockers. FEBS Lett. 440 (1998) 302-306
    • (1998) FEBS Lett. , vol.440 , pp. 302-306
    • Kushmerick, C.1    Castro, M.D.2    Cruz, J.S.3    Bloch, C.4    Beirao, P.S.L.5
  • 27
    • 4444295137 scopus 로고    scopus 로고
    • Differential antifungal and calcium channel-blocking activity among structurally related plant defensins
    • Spelbrink R.G., Dilmac N., Allen A., Smith T.J., and Hockerman G.H. Differential antifungal and calcium channel-blocking activity among structurally related plant defensins. Plant Physiol. 135 (2004) 2055-2067
    • (2004) Plant Physiol. , vol.135 , pp. 2055-2067
    • Spelbrink, R.G.1    Dilmac, N.2    Allen, A.3    Smith, T.J.4    Hockerman, G.H.5
  • 28
    • 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.J., Pelaez F., Limas G.G., Mendez R., Soriano F., Salinas M., and 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. 194 (1990) 533-539
    • (1990) Eur. J. Biochem. , vol.194 , pp. 533-539
    • Mendez, E.1    Moreno, A.2    Colilla, F.J.3    Pelaez, F.4    Limas, G.G.5    Mendez, R.6    Soriano, F.7    Salinas, M.8    de Haro, C.9
  • 29
    • 0029897150 scopus 로고    scopus 로고
    • Primary structure of omega-hordothionin, a member of a novel family of thionins from barley endosperm, and its inhibition of protein synthesis in eukaryotic and prokaryotic cell-free systems
    • Mendez E., Rocher A., Calero M., Girbes T., and L.CitoresSoriano F. Primary structure of omega-hordothionin, a member of a novel family of thionins from barley endosperm, and its inhibition of protein synthesis in eukaryotic and prokaryotic cell-free systems. Eur. J. Biochem. 239 (1996) 67-73
    • (1996) Eur. J. Biochem. , vol.239 , pp. 67-73
    • Mendez, E.1    Rocher, A.2    Calero, M.3    Girbes, T.4    L.CitoresSoriano, F.5
  • 31
    • 0036399722 scopus 로고    scopus 로고
    • A novel plant defensin-like gene of winter wheat is specifically induced during cold acclimation
    • Koeke M., Okamoto T., Tsuda S., and Imai R. A novel plant defensin-like gene of winter wheat is specifically induced during cold acclimation. Biochem. Biophys. Res. Commun. 298 (2002) 46-53
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 46-53
    • Koeke, M.1    Okamoto, T.2    Tsuda, S.3    Imai, R.4
  • 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., and 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. 13 (2000) 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
  • 37
    • 33744457032 scopus 로고    scopus 로고
    • Identification of phytotoxic substances from early growth of barnyard grass (Echinochloa crusgalli) root exudates
    • Xuan T.D., Chung I.M., Khanh T.D., and Tawata S. Identification of phytotoxic substances from early growth of barnyard grass (Echinochloa crusgalli) root exudates. J. Chem. Ecol. 32 (2006) 895-906
    • (2006) J. Chem. Ecol. , vol.32 , pp. 895-906
    • Xuan, T.D.1    Chung, I.M.2    Khanh, T.D.3    Tawata, S.4
  • 40
    • 0026666034 scopus 로고
    • Purification and characterization of a novel antimicrobial peptide from maize (Zea mays L.) kernels
    • Duvick J.P., Rood T., Rao A.G., and Marshak D.R. Purification and characterization of a novel antimicrobial peptide from maize (Zea mays L.) kernels. J. Biol. Chem. 267 (1992) 18814-18820
    • (1992) J. Biol. Chem. , vol.267 , pp. 18814-18820
    • Duvick, J.P.1    Rood, T.2    Rao, A.G.3    Marshak, D.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.