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Volumn 83, Issue 4, 2007, Pages 254-262

Toxicity assessment of peptaibols and contaminated sediments on Crassostrea gigas embryos

Author keywords

Bivalve bioassay; Embryotoxicity; Marine fungi; Mycotoxins; Risk assessment

Indexed keywords

ALAMETHICIN; MYCOTOXIN; PEPTAIBOL;

EID: 34347357493     PISSN: 0166445X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.aquatox.2007.04.009     Document Type: Article
Times cited : (23)

References (50)
  • 1
    • 34047218202 scopus 로고    scopus 로고
    • Guideline levels of chemical contamination used to assess sediment quality in coastal areas: a contribution to understanding false negative or false positive responses
    • Tremblay H., Locat J., and Galvez-Cloutier R. (Eds), Mitigation/Restoration. Univ, Laval, Québec
    • Amiard-Triquet C., Geffard O., Geffard A., Budzinski H., Amiard J.C., Fichet D., Pouliquen H., Berthelot Y., and His E. Guideline levels of chemical contamination used to assess sediment quality in coastal areas: a contribution to understanding false negative or false positive responses. In: Tremblay H., Locat J., and Galvez-Cloutier R. (Eds). Contaminated Sediments: Characterization, Evaluation (2003), Mitigation/Restoration. Univ, Laval, Québec 349-354
    • (2003) Contaminated Sediments: Characterization, Evaluation , pp. 349-354
    • Amiard-Triquet, C.1    Geffard, O.2    Geffard, A.3    Budzinski, H.4    Amiard, J.C.5    Fichet, D.6    Pouliquen, H.7    Berthelot, Y.8    His, E.9
  • 2
    • 0025832273 scopus 로고
    • Dynamics and aggregation of the peptide ion channel alamethicin. Measurements using spin-labeled peptides
    • Archer S.J., Ellena J.F., and Cafiso D.S. Dynamics and aggregation of the peptide ion channel alamethicin. Measurements using spin-labeled peptides. Biophys. J. 60 (1991) 389-398
    • (1991) Biophys. J. , vol.60 , pp. 389-398
    • Archer, S.J.1    Ellena, J.F.2    Cafiso, D.S.3
  • 3
    • 33748717370 scopus 로고    scopus 로고
    • Harzianin HB I, an 11-residue peptaibol from Trichoderma harzianum: isolation, sequence, solution synthesis and membrane activity
    • Augeven-Bour I., Rebuffat S., Auvin C., Goulard C., Prigent Y., and Bodo B. Harzianin HB I, an 11-residue peptaibol from Trichoderma harzianum: isolation, sequence, solution synthesis and membrane activity. J. Chem. Soc., Perkin Trans., I 10 (1997) 1587-1594
    • (1997) J. Chem. Soc., Perkin Trans., I , vol.10 , pp. 1587-1594
    • Augeven-Bour, I.1    Rebuffat, S.2    Auvin, C.3    Goulard, C.4    Prigent, Y.5    Bodo, B.6
  • 4
    • 33748832564 scopus 로고    scopus 로고
    • Structures of peptaibols antibiotics hypomurocin A and B from the ascomycetous fungus Hypocrea muroiana Hino et Katsumoto
    • Becker D., Kiess M., and Brückner H. Structures of peptaibols antibiotics hypomurocin A and B from the ascomycetous fungus Hypocrea muroiana Hino et Katsumoto. Lieb. Ann. Recueil. (1997) 767-772
    • (1997) Lieb. Ann. Recueil. , pp. 767-772
    • Becker, D.1    Kiess, M.2    Brückner, H.3
  • 5
    • 0344307473 scopus 로고    scopus 로고
    • Isolation, structure elucidation and biological activities of trichofumins A, B, C and D, new 11 and 13mer peptaibols from Trichoderma sp. HKI 0276
    • Berg A., Grigoriev P.A., Degenkolb T., Neuhof T., Härtl A., Schlegel B., and Gräfe U. Isolation, structure elucidation and biological activities of trichofumins A, B, C and D, new 11 and 13mer peptaibols from Trichoderma sp. HKI 0276. J. Pept. Sci. 9 (2003) 810-816
    • (2003) J. Pept. Sci. , vol.9 , pp. 810-816
    • Berg, A.1    Grigoriev, P.A.2    Degenkolb, T.3    Neuhof, T.4    Härtl, A.5    Schlegel, B.6    Gräfe, U.7
  • 6
    • 0017851240 scopus 로고
    • Trichotoxin A-40, a new membrane-exciting peptide. Part B. Voltage-dependent pore formation in bilayer lipid membranes and comparison with other alamethicin analogues
    • Boheim G., Irmscher G., and Jung G. Trichotoxin A-40, a new membrane-exciting peptide. Part B. Voltage-dependent pore formation in bilayer lipid membranes and comparison with other alamethicin analogues. Biochim. Biophys. Acta-Biomembr. 507 (1978) 485-506
    • (1978) Biochim. Biophys. Acta-Biomembr. , vol.507 , pp. 485-506
    • Boheim, G.1    Irmscher, G.2    Jung, G.3
  • 7
    • 0028226051 scopus 로고
    • Alamethicin: a peptide model for voltage gating and protein-membrane interactions
    • Cafiso D. Alamethicin: a peptide model for voltage gating and protein-membrane interactions. Annu. Rev. Biophys. Biomol. Struct. 23 (1994) 141-165
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 141-165
    • Cafiso, D.1
  • 8
    • 0034867234 scopus 로고    scopus 로고
    • Peptaibols: models for ion channels
    • Chugh J.K., and Wallace B.A. Peptaibols: models for ion channels. Biochem. Soc. Trans. 29 (2001) 565-570
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 565-570
    • Chugh, J.K.1    Wallace, B.A.2
  • 9
    • 0001239025 scopus 로고
    • Acute toxicity of heavy metals to some marine larvae
    • Connor P.M. Acute toxicity of heavy metals to some marine larvae. Mar. Pollut. Bull. 3 (1972) 190-192
    • (1972) Mar. Pollut. Bull. , vol.3 , pp. 190-192
    • Connor, P.M.1
  • 10
    • 0033374856 scopus 로고    scopus 로고
    • The ion-channel activity of longibrachins LGA I and LGB II: effects of Pro-2/Ala and Gln-18/Glu substitutions on the alamethicin voltage-gated membrane channels
    • Cosette P., Rebuffat S., Bodo B., and Molle G. The ion-channel activity of longibrachins LGA I and LGB II: effects of Pro-2/Ala and Gln-18/Glu substitutions on the alamethicin voltage-gated membrane channels. Biochim. Biophys. Acta-Biomembr. 1461 (1999) 113-122
    • (1999) Biochim. Biophys. Acta-Biomembr. , vol.1461 , pp. 113-122
    • Cosette, P.1    Rebuffat, S.2    Bodo, B.3    Molle, G.4
  • 11
    • 0345169941 scopus 로고    scopus 로고
    • The occurrence of peptaibols and structurally related peptaibiotics in fungi and their mass spectrometric identification via diagnostic fragment ions
    • Degenkolb T., Berg A., Gams W., Schlegel B., and Gräfe U. The occurrence of peptaibols and structurally related peptaibiotics in fungi and their mass spectrometric identification via diagnostic fragment ions. J. Pept. Sci. 9 (2003) 666-678
    • (2003) J. Pept. Sci. , vol.9 , pp. 666-678
    • Degenkolb, T.1    Berg, A.2    Gams, W.3    Schlegel, B.4    Gräfe, U.5
  • 12
    • 33745789916 scopus 로고    scopus 로고
    • Peptaibiomics: screening for polypeptide antibiotics (peptaibiotics) from plant-protective Trichoderma species
    • Degenkolb T., Gräfenham T., Berg A., Nirenberg H., Gams W., and Brückner H. Peptaibiomics: screening for polypeptide antibiotics (peptaibiotics) from plant-protective Trichoderma species. Chem. Biodivers. 3 (2006) 593-610
    • (2006) Chem. Biodivers. , vol.3 , pp. 593-610
    • Degenkolb, T.1    Gräfenham, T.2    Berg, A.3    Nirenberg, H.4    Gams, W.5    Brückner, H.6
  • 13
    • 4344584311 scopus 로고    scopus 로고
    • Helical kink and channel behaviour: a comparative study with the peptaibols alamethicin, trichotoxin and antiamoebin
    • Duclohier H. Helical kink and channel behaviour: a comparative study with the peptaibols alamethicin, trichotoxin and antiamoebin. Eur. Biophys. J. 33 (2004) 169-174
    • (2004) Eur. Biophys. J. , vol.33 , pp. 169-174
    • Duclohier, H.1
  • 15
    • 33750684705 scopus 로고    scopus 로고
    • Toxicity assessment of metabolites of fungal biocontrol agents using two different (Artemia salina and Daphnia magna) invertebrate bioassays
    • Favilla M., Macchia L., Gallo A., and Altomare C. Toxicity assessment of metabolites of fungal biocontrol agents using two different (Artemia salina and Daphnia magna) invertebrate bioassays. Food Chem. Toxicol. 44 (2006) 1922-1931
    • (2006) Food Chem. Toxicol. , vol.44 , pp. 1922-1931
    • Favilla, M.1    Macchia, L.2    Gallo, A.3    Altomare, C.4
  • 16
    • 1542269111 scopus 로고    scopus 로고
    • Effects of storage method and duration on the toxicity of marine sediments to embryos of Crassostrea gigas oysters
    • Geffard O., His E., Budzinski H., Chiffoleau J.F., Coynel A., and Etcheber H. Effects of storage method and duration on the toxicity of marine sediments to embryos of Crassostrea gigas oysters. Environ. Pollut. 129 (2004) 457-465
    • (2004) Environ. Pollut. , vol.129 , pp. 457-465
    • Geffard, O.1    His, E.2    Budzinski, H.3    Chiffoleau, J.F.4    Coynel, A.5    Etcheber, H.6
  • 18
    • 0030617331 scopus 로고    scopus 로고
    • A simplification the bivalve embryogenesis and larval development bioassay method for water quality assessment
    • His E., Seaman M.N.L., and Beiras R. A simplification the bivalve embryogenesis and larval development bioassay method for water quality assessment. Water Res. 31 (1997) 351-355
    • (1997) Water Res. , vol.31 , pp. 351-355
    • His, E.1    Seaman, M.N.L.2    Beiras, R.3
  • 19
    • 1142286236 scopus 로고    scopus 로고
    • The assessment of marine pollution: bioassays with bivalve embryos and larvae
    • His E., Beira R., and Seaman M.N.L. The assessment of marine pollution: bioassays with bivalve embryos and larvae. Adv. Mar. Biol. 37 (1999) 1-178
    • (1999) Adv. Mar. Biol. , vol.37 , pp. 1-178
    • His, E.1    Beira, R.2    Seaman, M.N.L.3
  • 21
    • 0028800416 scopus 로고
    • Studies on metabolites of mycoparasitic fungi. IV. Minor peptaibols of Trichoderma koningii
    • Huang Q., Tezuka Y., Hatanaka Y., Kikuchi T., Nishi A., and Tubaki K. Studies on metabolites of mycoparasitic fungi. IV. Minor peptaibols of Trichoderma koningii. Chem. Pharm. Bull. 43 (1995) 1663-1667
    • (1995) Chem. Pharm. Bull. , vol.43 , pp. 1663-1667
    • Huang, Q.1    Tezuka, Y.2    Hatanaka, Y.3    Kikuchi, T.4    Nishi, A.5    Tubaki, K.6
  • 22
    • 0029964664 scopus 로고    scopus 로고
    • Studies on metabolites of mycoparasitic fungi. V. Ion-spray ionization mass spectrometric analysis of trichokonin-II, a peptaibol mixture obtained from the culture broth of Trichoderma koningii
    • Huang Q., Tezuka Y., Hatanaka Y., Kikuchi T., Nishi A., and Tubaki K. Studies on metabolites of mycoparasitic fungi. V. Ion-spray ionization mass spectrometric analysis of trichokonin-II, a peptaibol mixture obtained from the culture broth of Trichoderma koningii. Chem. Pharm. Bull. 44 (1996) 590-593
    • (1996) Chem. Pharm. Bull. , vol.44 , pp. 590-593
    • Huang, Q.1    Tezuka, Y.2    Hatanaka, Y.3    Kikuchi, T.4    Nishi, A.5    Tubaki, K.6
  • 23
    • 0028920495 scopus 로고
    • Fungal metabolites. XVIII. New membrane-modifying peptides, Trichorozins I-IV, from the fungus Trichoderma harzianum
    • Iida A., Sanekata M., Wada S.I., Fujita T., Tanaka H., Enoky A., Fuse G., Kanai M., and Asami K. Fungal metabolites. XVIII. New membrane-modifying peptides, Trichorozins I-IV, from the fungus Trichoderma harzianum. Chem. Pharm. Bull. 43 (1995) 392-397
    • (1995) Chem. Pharm. Bull. , vol.43 , pp. 392-397
    • Iida, A.1    Sanekata, M.2    Wada, S.I.3    Fujita, T.4    Tanaka, H.5    Enoky, A.6    Fuse, G.7    Kanai, M.8    Asami, K.9
  • 24
    • 0344307468 scopus 로고    scopus 로고
    • Sequences of alamethicins F30 and F50 reconsidered and reconciled
    • Kirschbaum J., Krause C., Winzheimer R.K., and Brückner H. Sequences of alamethicins F30 and F50 reconsidered and reconciled. J. Pept. Sci. 9 (2003) 799-809
    • (2003) J. Pept. Sci. , vol.9 , pp. 799-809
    • Kirschbaum, J.1    Krause, C.2    Winzheimer, R.K.3    Brückner, H.4
  • 25
    • 33745088882 scopus 로고    scopus 로고
    • Peptaibiomics: an advanced, rapid and selective analysis of peptaibiotics/peptaibols by SPE/LC-ES-MS
    • Krause C., Kirschbaum J., and Brückner H. Peptaibiomics: an advanced, rapid and selective analysis of peptaibiotics/peptaibols by SPE/LC-ES-MS. Amino Acids 30 (2006) 435-443
    • (2006) Amino Acids , vol.30 , pp. 435-443
    • Krause, C.1    Kirschbaum, J.2    Brückner, H.3
  • 26
    • 0037164698 scopus 로고    scopus 로고
    • Ion transport across a phospholipid membrane mediated by the peptide trichogin GA IV
    • Kropracheva T., and Raap J. Ion transport across a phospholipid membrane mediated by the peptide trichogin GA IV. Biochim. Biophys. Acta 1567 (2002) 193-203
    • (2002) Biochim. Biophys. Acta , vol.1567 , pp. 193-203
    • Kropracheva, T.1    Raap, J.2
  • 27
    • 0036145674 scopus 로고    scopus 로고
    • Combined use of LC/MS and biological test during rapid identification of marine mycotoxins produced by Trichoderma koningii
    • Landreau A., Pouchus Y.F., Biard J.F., Sallenave-Namont C., Robiou du Pont T., and Verbist J.F. Combined use of LC/MS and biological test during rapid identification of marine mycotoxins produced by Trichoderma koningii. J. Microbiol. Meth. 48 (2002) 181-194
    • (2002) J. Microbiol. Meth. , vol.48 , pp. 181-194
    • Landreau, A.1    Pouchus, Y.F.2    Biard, J.F.3    Sallenave-Namont, C.4    Robiou du Pont, T.5    Verbist, J.F.6
  • 28
    • 0031884309 scopus 로고    scopus 로고
    • Directed biosynthesis of peptaibol antibiotics in two Trichoderma strains. I. Fermentation and isolation
    • Leclerc G., Rebuffat S., Goulard C., and Bodo B. Directed biosynthesis of peptaibol antibiotics in two Trichoderma strains. I. Fermentation and isolation. J. Antibiot. 51 (1998) 170-177
    • (1998) J. Antibiot. , vol.51 , pp. 170-177
    • Leclerc, G.1    Rebuffat, S.2    Goulard, C.3    Bodo, B.4
  • 29
    • 0035089485 scopus 로고    scopus 로고
    • Sequences and antimycoplamic properties of longibrachins LGB II and LGB III, two novel 20-resiude peptaibols from Trichoderma longibrachiatum
    • Leclerc G., Goulard C., Prigent Y., Bodo B., Wroblewski H., and Rebuffat S. Sequences and antimycoplamic properties of longibrachins LGB II and LGB III, two novel 20-resiude peptaibols from Trichoderma longibrachiatum. J. Nat. Prod. 64 (2001) 164-170
    • (2001) J. Nat. Prod. , vol.64 , pp. 164-170
    • Leclerc, G.1    Goulard, C.2    Prigent, Y.3    Bodo, B.4    Wroblewski, H.5    Rebuffat, S.6
  • 30
    • 0031025948 scopus 로고    scopus 로고
    • Interaction of the 14-residue peptaibols, harzianins HC, with lipid bilayers: permeability modifications and conductance properties
    • Lucaciu M., Rebuffat S., Goulard C., Duclohier H., Molle G., and Bodo B. Interaction of the 14-residue peptaibols, harzianins HC, with lipid bilayers: permeability modifications and conductance properties. Biochim. Biophys. Acta 1323 (1997) 85-96
    • (1997) Biochim. Biophys. Acta , vol.1323 , pp. 85-96
    • Lucaciu, M.1    Rebuffat, S.2    Goulard, C.3    Duclohier, H.4    Molle, G.5    Bodo, B.6
  • 31
    • 0019775722 scopus 로고
    • Toxicities of ten metals to Crassostrea gigas and Mytilus edulis embryos and Cancer magister larvae
    • Martin M., Osborn K.E., Billig P., and Glickstein N. Toxicities of ten metals to Crassostrea gigas and Mytilus edulis embryos and Cancer magister larvae. Mar. Pollut. Bull. 12 (1981) 305-308
    • (1981) Mar. Pollut. Bull. , vol.12 , pp. 305-308
    • Martin, M.1    Osborn, K.E.2    Billig, P.3    Glickstein, N.4
  • 32
    • 0026715210 scopus 로고
    • Morphological alterations accompanying the effect of peptaibiotics, alpha-aminoisobutyric acid-rich secondary metabolites of filamentous fungi, on Culex pipiens larvae
    • Matha V., Jegorov A., Kiess M., and Brückner H. Morphological alterations accompanying the effect of peptaibiotics, alpha-aminoisobutyric acid-rich secondary metabolites of filamentous fungi, on Culex pipiens larvae. Tissue Cell 24 (1992) 559-564
    • (1992) Tissue Cell , vol.24 , pp. 559-564
    • Matha, V.1    Jegorov, A.2    Kiess, M.3    Brückner, H.4
  • 37
    • 34347352340 scopus 로고    scopus 로고
    • Poirier, L., Amiard, J.C., Mondeguer, F., Quiniou, F., Ruiz, N., Pouchus, Y.F., Montagu, M., in press-a. Determination of peptaibol trace amounts in marine sediments by liquid chromatography/electrospray ionization - ion trap - mass spectrometry. J. Chromatogr. A.
  • 38
    • 34347351477 scopus 로고    scopus 로고
    • Poirier, L., Montagu, M., Landreau, A., Mohammed-Benkada, M., Grovel, O., Sallenave-Namont, C., Biard, J., Amiard-Triquet, C., Amiard, J.C., Pouchus, Y.F., in press-b. Peptaibols, stable markers of fungal development in the marine environment. Chem. Biodivers.
  • 39
    • 80052592466 scopus 로고    scopus 로고
    • Bio-indicateur de la toxicité potentielle de milieux aqueux: bio-essai "développement embryo-larvaire de bivalve
    • Ifremer (Ed) pp. 24
    • Quiniou F., His E., Delesmont R., and Caisey X. Bio-indicateur de la toxicité potentielle de milieux aqueux: bio-essai "développement embryo-larvaire de bivalve. In: Ifremer (Ed). Méthodes d'analyse en milieu marin, (2005) pp. 24
    • (2005) Méthodes d'analyse en milieu marin
    • Quiniou, F.1    His, E.2    Delesmont, R.3    Caisey, X.4
  • 40
    • 33748889116 scopus 로고    scopus 로고
    • Isolation and structural elucidation of the 11-residue peptaibol antibiotic, harzianin HK VI
    • Rebuffat S., Hlimi S., Prigent Y., Goulard C., and Bodo B. Isolation and structural elucidation of the 11-residue peptaibol antibiotic, harzianin HK VI. J. Chem. Soc., Perkin trans., I 16 (1996) 2021-2027
    • (1996) J. Chem. Soc., Perkin trans., I , vol.16 , pp. 2021-2027
    • Rebuffat, S.1    Hlimi, S.2    Prigent, Y.3    Goulard, C.4    Bodo, B.5
  • 41
    • 0002082310 scopus 로고    scopus 로고
    • The peptaibol antibiotics from Trichoderma soil fungi; structural diversity and membrane properties
    • Rebuffat S., Goulard C., Bodo B., and Roquebert M.F. The peptaibol antibiotics from Trichoderma soil fungi; structural diversity and membrane properties. Recent Res. Devel. Org. Bioorg. Chem. 3 (1999) 65-91
    • (1999) Recent Res. Devel. Org. Bioorg. Chem. , vol.3 , pp. 65-91
    • Rebuffat, S.1    Goulard, C.2    Bodo, B.3    Roquebert, M.F.4
  • 42
    • 0033753919 scopus 로고    scopus 로고
    • Two unprecedented natural Aib-peptides with the (Xaa-Yaa-Aib-Pro) motif and an unusual C-terminus: structures, membrane-modifying and antibacterial properties of pseudokonins KL III and KL VI from the fungus Trichoderma pseudokoningii
    • Rebuffat S., Goulard C., Hlimi S., and Bodo B. Two unprecedented natural Aib-peptides with the (Xaa-Yaa-Aib-Pro) motif and an unusual C-terminus: structures, membrane-modifying and antibacterial properties of pseudokonins KL III and KL VI from the fungus Trichoderma pseudokoningii. J. Pept. Sci. 6 (2000) 519-533
    • (2000) J. Pept. Sci. , vol.6 , pp. 519-533
    • Rebuffat, S.1    Goulard, C.2    Hlimi, S.3    Bodo, B.4
  • 43
    • 0032890014 scopus 로고    scopus 로고
    • Bioaccumulation of mycotoxins by shellfish: contamination of mussels by metabolites of a Trichoderma koningii strain isolated in the marine environment
    • Sallenave-Namont C., Pouchus Y.F., Bardouil M., Lassus P., Roquebert M.F., and Verbist J.F. Bioaccumulation of mycotoxins by shellfish: contamination of mussels by metabolites of a Trichoderma koningii strain isolated in the marine environment. Toxicon 37 (1999) 77-83
    • (1999) Toxicon , vol.37 , pp. 77-83
    • Sallenave-Namont, C.1    Pouchus, Y.F.2    Bardouil, M.3    Lassus, P.4    Roquebert, M.F.5    Verbist, J.F.6
  • 44
    • 0027817476 scopus 로고
    • Structure and function of channel-forming peptaibols. Q
    • Sansom M. Structure and function of channel-forming peptaibols. Q. Rev. Biophys. 26 (1993) 365-421
    • (1993) Rev. Biophys. , vol.26 , pp. 365-421
    • Sansom, M.1
  • 46
    • 0020797407 scopus 로고
    • A method for cooperative and non cooperative binding studies using non linear regression analysis on a microcomputer
    • Vindimian E., Robaut C., and Fillion G. A method for cooperative and non cooperative binding studies using non linear regression analysis on a microcomputer. J. Appl. Biochem. 5 (1983) 261-268
    • (1983) J. Appl. Biochem. , vol.5 , pp. 261-268
    • Vindimian, E.1    Robaut, C.2    Fillion, G.3
  • 47
    • 0029066604 scopus 로고
    • Fungal metabolites. XIX. Structural elucidation of channel-forming peptides, Trichorovins-I-XIV, from the fungus Trichoderma viridae
    • Wada S.I., Iida A., Akimoto N., Kanai M., Toyama N., and Fujita T. Fungal metabolites. XIX. Structural elucidation of channel-forming peptides, Trichorovins-I-XIV, from the fungus Trichoderma viridae. Chem. Pharm. Bull. 43 (1995) 910-915
    • (1995) Chem. Pharm. Bull. , vol.43 , pp. 910-915
    • Wada, S.I.1    Iida, A.2    Akimoto, N.3    Kanai, M.4    Toyama, N.5    Fujita, T.6
  • 48
    • 4344654907 scopus 로고    scopus 로고
    • Analysis of peptaibol sequence composition: Implications for in vivo synthesis and channel formation
    • Whitmore L., and Wallace B.A. Analysis of peptaibol sequence composition: Implications for in vivo synthesis and channel formation. Eur. Biophys. J. 33 (2004) 233-237
    • (2004) Eur. Biophys. J. , vol.33 , pp. 233-237
    • Whitmore, L.1    Wallace, B.A.2
  • 49
    • 0346494756 scopus 로고    scopus 로고
    • The peptaibol database: A database for sequences and structures of naturally occurring peptaibols
    • Whitmore L., and Wallace B.A. The peptaibol database: A database for sequences and structures of naturally occurring peptaibols. Nucleic Acids Res. 32 (2004) 593-594
    • (2004) Nucleic Acids Res. , vol.32 , pp. 593-594
    • Whitmore, L.1    Wallace, B.A.2
  • 50
    • 33745045234 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial activity and high stability of Trichokonins from Trichoderma koningii SMF2 against plant pathogens
    • Xiao-Yan S., Qing-Tao S., Shu-Tao X., Xiu-Lan C., Cai-Yun S., and Yu-Zhong Z. Broad-spectrum antimicrobial activity and high stability of Trichokonins from Trichoderma koningii SMF2 against plant pathogens. FEMS Microbiol. Lett. 260 (2006) 119-125
    • (2006) FEMS Microbiol. Lett. , vol.260 , pp. 119-125
    • Xiao-Yan, S.1    Qing-Tao, S.2    Shu-Tao, X.3    Xiu-Lan, C.4    Cai-Yun, S.5    Yu-Zhong, Z.6


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