메뉴 건너뛰기




Volumn 28, Issue 3, 2007, Pages 533-546

Purification and characterization of eight peptides from Galleria mellonella immune hemolymph

Author keywords

Antibacterial antimicrobial peptides; Galleria mellonella; Hemolymph; Insect immunity; Peptide purification

Indexed keywords

ANIONIC PEPTIDE 1; ANIONIC PEPTIDE 2; APOLIPOPHORECIN; CECROPIN D LIKE PEPTIDE; DEFENSIN; DEFENSIN LIKE PEPTIDE; PEPTIDE DERIVATIVE; PROLINE RICH PEPTIDE 1; PROLINE RICH PEPTIDE 2; UNCLASSIFIED DRUG;

EID: 33846794525     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2006.11.010     Document Type: Article
Times cited : (169)

References (69)
  • 1
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: basic facts and emerging concepts
    • Boman H.G. Antibacterial peptides: basic facts and emerging concepts. J Intern Med 254 (2003) 197-215
    • (2003) J Intern Med , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 2
    • 0037063976 scopus 로고    scopus 로고
    • Correlation between virulence of Candida albicans mutants in mice and Galleria mellonella larvae
    • Brennan M., Thomas D.Y., Whiteway M., and Kavanagh K. Correlation between virulence of Candida albicans mutants in mice and Galleria mellonella larvae. FEMS Immunol Med Microbiol 34 (2002) 153-157
    • (2002) FEMS Immunol Med Microbiol , vol.34 , pp. 153-157
    • Brennan, M.1    Thomas, D.Y.2    Whiteway, M.3    Kavanagh, K.4
  • 4
    • 0030048076 scopus 로고    scopus 로고
    • Isolation of an ovine pulmonary surfactant-associated anionic peptide bactericidal for Pasteurella haemolytica
    • Brogden K.A., De Lucca A.J., Bland J., and Elliott S. Isolation of an ovine pulmonary surfactant-associated anionic peptide bactericidal for Pasteurella haemolytica. Proc Natl Acad Sci USA 93 (1996) 412-416
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 412-416
    • Brogden, K.A.1    De Lucca, A.J.2    Bland, J.3    Elliott, S.4
  • 5
    • 0033022730 scopus 로고    scopus 로고
    • Antimicrobial peptides in insects; structure and function
    • Bulet P., Hetru C., Dimarcq J.-L., and Hoffmann D. Antimicrobial peptides in insects; structure and function. Dev Comp Immunol 23 (1999) 329-344
    • (1999) Dev Comp Immunol , vol.23 , pp. 329-344
    • Bulet, P.1    Hetru, C.2    Dimarcq, J.-L.3    Hoffmann, D.4
  • 6
    • 0344879740 scopus 로고    scopus 로고
    • Immune response in Hymenoptera
    • Brey P.T., and Hultmark D. (Eds), Chapman & Hall, London
    • Casteels P. Immune response in Hymenoptera. In: Brey P.T., and Hultmark D. (Eds). Molecular mechanisms of immune responses in insects (1998), Chapman & Hall, London 92-110
    • (1998) Molecular mechanisms of immune responses in insects , pp. 92-110
    • Casteels, P.1
  • 7
    • 0002711049 scopus 로고
    • Antibacterial immunity in Lepidoptera
    • Gupta A.P. (Ed), CRC Press, Boca Raton
    • Chadwick J.S., and Aston W.P. Antibacterial immunity in Lepidoptera. In: Gupta A.P. (Ed). Immunology of insects and other arthropods (1991), CRC Press, Boca Raton 347-370
    • (1991) Immunology of insects and other arthropods , pp. 347-370
    • Chadwick, J.S.1    Aston, W.P.2
  • 9
    • 0030746525 scopus 로고    scopus 로고
    • Effects of the anti-bacterial peptide cecropin B and its analogs, cecropins B-1 and B-2, on liposomes, bacteria and cancer cells
    • Chen H.M., Wang W., Smith D., and Chan S.C. Effects of the anti-bacterial peptide cecropin B and its analogs, cecropins B-1 and B-2, on liposomes, bacteria and cancer cells. Biochim Biophys Acta 1336 (1997) 171-179
    • (1997) Biochim Biophys Acta , vol.1336 , pp. 171-179
    • Chen, H.M.1    Wang, W.2    Smith, D.3    Chan, S.C.4
  • 10
    • 0001924808 scopus 로고    scopus 로고
    • The inducible antibacterial peptides of the hemipteran insect Palomena prasina: identification of a unique family of proline-rich peptides and of a novel insect defensin
    • Chernysh S., Cociancich S., Briand J.-P., Hetru C., and Bulet P. The inducible antibacterial peptides of the hemipteran insect Palomena prasina: identification of a unique family of proline-rich peptides and of a novel insect defensin. J Insect Physiol 42 (1996) 81-89
    • (1996) J Insect Physiol , vol.42 , pp. 81-89
    • Chernysh, S.1    Cociancich, S.2    Briand, J.-P.3    Hetru, C.4    Bulet, P.5
  • 11
    • 0343049009 scopus 로고    scopus 로고
    • Larval and pupal induction and N-terminal amino acid sequence of lysozyme from Heliothis virescens
    • Chung K.T., and Ourth D.D. Larval and pupal induction and N-terminal amino acid sequence of lysozyme from Heliothis virescens. J Insect Physiol 46 (2000) 563-572
    • (2000) J Insect Physiol , vol.46 , pp. 563-572
    • Chung, K.T.1    Ourth, D.D.2
  • 12
    • 0033983382 scopus 로고    scopus 로고
    • Development of an insect model for the in vivo pathogenicity testing of yeasts
    • Cotter G., Doyle S., and Kavanagh K. Development of an insect model for the in vivo pathogenicity testing of yeasts. FEMS Immunol Med Microbiol 27 (2000) 163-169
    • (2000) FEMS Immunol Med Microbiol , vol.27 , pp. 163-169
    • Cotter, G.1    Doyle, S.2    Kavanagh, K.3
  • 13
    • 0025860280 scopus 로고
    • Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation
    • Cruciani R.A., Barker J.L., Zasloff M., Chen H.C., and Colamonici O. Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation. Proc Natl Acad Sci USA 88 (1991) 3792-3796
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3792-3796
    • Cruciani, R.A.1    Barker, J.L.2    Zasloff, M.3    Chen, H.C.4    Colamonici, O.5
  • 14
    • 0035894426 scopus 로고    scopus 로고
    • Detection of antibacterial polypeptide activity in situ after sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Cytryńska M., Zdybicka-Barabas A., Jabloński P., and Jakubowicz T. Detection of antibacterial polypeptide activity in situ after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Anal Biochem 299 (2001) 274-276
    • (2001) Anal Biochem , vol.299 , pp. 274-276
    • Cytryńska, M.1    Zdybicka-Barabas, A.2    Jabloński, P.3    Jakubowicz, T.4
  • 15
    • 0024297452 scopus 로고
    • A family of bacteria-regulated, cecropin D-like peptides from Manduca sexta
    • Dickinson L., Russell V., and Dunn P.E. A family of bacteria-regulated, cecropin D-like peptides from Manduca sexta. J Biol Chem 263 (1988) 19424-19429
    • (1988) J Biol Chem , vol.263 , pp. 19424-19429
    • Dickinson, L.1    Russell, V.2    Dunn, P.E.3
  • 16
    • 0345096422 scopus 로고    scopus 로고
    • Virulence of Candida albicans mutants toward larval Galleria mellonella (Insecta, Lepidoptera, Galleridae)
    • Dunphy G.B., Oberholzer U., Whiteway M., Zakarian R.J., and Boomer I. Virulence of Candida albicans mutants toward larval Galleria mellonella (Insecta, Lepidoptera, Galleridae). Can J Microbiol 49 (2003) 514-524
    • (2003) Can J Microbiol , vol.49 , pp. 514-524
    • Dunphy, G.B.1    Oberholzer, U.2    Whiteway, M.3    Zakarian, R.J.4    Boomer, I.5
  • 17
    • 0033231380 scopus 로고    scopus 로고
    • Drosophila cecropin as an antifungal agent
    • Ekengren S., and Hultmark D. Drosophila cecropin as an antifungal agent. Insect Biochem Mol Biol 29 (1999) 965-972
    • (1999) Insect Biochem Mol Biol , vol.29 , pp. 965-972
    • Ekengren, S.1    Hultmark, D.2
  • 18
    • 0021767932 scopus 로고
    • The antibacterial effect of attacins from silk moth Hyalophora cecropia is directed against the outer membrane of Escherichia coli
    • Engström P., Carlsson A., Engström A., Tao Z.J., and Bennich H. The antibacterial effect of attacins from silk moth Hyalophora cecropia is directed against the outer membrane of Escherichia coli. EMBO J 3 (1984) 3347-3351
    • (1984) EMBO J , vol.3 , pp. 3347-3351
    • Engström, P.1    Carlsson, A.2    Engström, A.3    Tao, Z.J.4    Bennich, H.5
  • 21
    • 0032754032 scopus 로고    scopus 로고
    • Apolipophorin-III in Galleria mellonella potentiates hemolymph lytic activity
    • Halwani A.E., and Dunphy G.B. Apolipophorin-III in Galleria mellonella potentiates hemolymph lytic activity. Dev Comp Immunol 23 (1999) 563-570
    • (1999) Dev Comp Immunol , vol.23 , pp. 563-570
    • Halwani, A.E.1    Dunphy, G.B.2
  • 22
    • 0028095144 scopus 로고
    • Isolation and α-amidation of the non-amidated form of cecropin D from larvae of Bombyx mori
    • Hara S., Taniai K., Kato Y., and Yamakawa M. Isolation and α-amidation of the non-amidated form of cecropin D from larvae of Bombyx mori. Comp Biochem Physiol 108B (1994) 303-308
    • (1994) Comp Biochem Physiol , vol.108 B , pp. 303-308
    • Hara, S.1    Taniai, K.2    Kato, Y.3    Yamakawa, M.4
  • 23
    • 0029051008 scopus 로고
    • A novel antibacterial peptide family isolated from the silkworm, Bombyx mori
    • Hara S., and Yamakawa M. A novel antibacterial peptide family isolated from the silkworm, Bombyx mori. Biochem J 310 (1995) 651-656
    • (1995) Biochem J , vol.310 , pp. 651-656
    • Hara, S.1    Yamakawa, M.2
  • 24
    • 85008288464 scopus 로고
    • Cooperative antibacterial relationship between lebocin and cecropin D, antibacterial peptides isolated from the silkworm, Bombyx mori (Lepidoptera: Bombycidae)
    • Hara S., and Yamakawa M. Cooperative antibacterial relationship between lebocin and cecropin D, antibacterial peptides isolated from the silkworm, Bombyx mori (Lepidoptera: Bombycidae). Appl Entomol Zool 30 (1995) 606-608
    • (1995) Appl Entomol Zool , vol.30 , pp. 606-608
    • Hara, S.1    Yamakawa, M.2
  • 25
  • 26
    • 0029689192 scopus 로고    scopus 로고
    • Insect lysozymes
    • Jollès P. (Ed), Birkhäuser Verlag, Basel, Switzerland
    • Hultmark D. Insect lysozymes. In: Jollès P. (Ed). Lysozymes: model enzymes in biochemistry and biology (1996), Birkhäuser Verlag, Basel, Switzerland 87-102
    • (1996) Lysozymes: model enzymes in biochemistry and biology , pp. 87-102
    • Hultmark, D.1
  • 27
    • 3242752749 scopus 로고    scopus 로고
    • Is innate enough? The innate immune response in Drosophila
    • Irving P., Troxler L., and Hetru C. Is innate enough? The innate immune response in Drosophila. CR Biol 327 (2004) 557-570
    • (2004) CR Biol , vol.327 , pp. 557-570
    • Irving, P.1    Troxler, L.2    Hetru, C.3
  • 28
    • 0029132680 scopus 로고
    • Haemolymph immune proteins protect the insect body cavity from invading bacteria
    • Jarosz J. Haemolymph immune proteins protect the insect body cavity from invading bacteria. Comp Biochem Physiol C 111 (1995) 213-220
    • (1995) Comp Biochem Physiol C , vol.111 , pp. 213-220
    • Jarosz, J.1
  • 29
    • 1242351240 scopus 로고    scopus 로고
    • Exploiting the potential of insects for in vivo pathogenicity testing of microbial pathogens
    • Kavanagh K., and Reeves E.P. Exploiting the potential of insects for in vivo pathogenicity testing of microbial pathogens. FEMS Microbiol Rev 28 (2004) 101-112
    • (2004) FEMS Microbiol Rev , vol.28 , pp. 101-112
    • Kavanagh, K.1    Reeves, E.P.2
  • 30
    • 1242344146 scopus 로고    scopus 로고
    • Purification and cDNA cloning of a cecropin-like peptide from the great wax moth, Galleria mellonella
    • Kim C.H., Lee J.H., Kim I., Seo S.J., Son S.M., Lee K.Y., et al. Purification and cDNA cloning of a cecropin-like peptide from the great wax moth, Galleria mellonella. Mol Cells 17 (2004) 262-266
    • (2004) Mol Cells , vol.17 , pp. 262-266
    • Kim, C.H.1    Lee, J.H.2    Kim, I.3    Seo, S.J.4    Son, S.M.5    Lee, K.Y.6
  • 31
    • 0036375765 scopus 로고    scopus 로고
    • An anionic antimicrobial peptide from toad Bombina maxima
    • Lai R., Liu H., Hui Lee W., and Zhang Y. An anionic antimicrobial peptide from toad Bombina maxima. Biochem Biophys Res Commun 295 (2002) 796-799
    • (2002) Biochem Biophys Res Commun , vol.295 , pp. 796-799
    • Lai, R.1    Liu, H.2    Hui Lee, W.3    Zhang, Y.4
  • 32
    • 2542564201 scopus 로고    scopus 로고
    • Two novel non-cationic defensin-like peptides from haemolymph of the female tick, Amblyomma hebraeum
    • Lai R., Lomas L.O., Jonczy J., Turner P.C., and Rees H.H. Two novel non-cationic defensin-like peptides from haemolymph of the female tick, Amblyomma hebraeum. Biochem J 379 (2004) 681-685
    • (2004) Biochem J , vol.379 , pp. 681-685
    • Lai, R.1    Lomas, L.O.2    Jonczy, J.3    Turner, P.C.4    Rees, H.H.5
  • 33
    • 0033515629 scopus 로고    scopus 로고
    • Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity
    • Lamberty M., Ades S., Uttenweiler-Joseph S., Brookhart G., Bushey D., Hoffmann J.A., et al. Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity. J Biol Chem 274 (1999) 9320-9326
    • (1999) J Biol Chem , vol.274 , pp. 9320-9326
    • Lamberty, M.1    Ades, S.2    Uttenweiler-Joseph, S.3    Brookhart, G.4    Bushey, D.5    Hoffmann, J.A.6
  • 35
    • 27744608414 scopus 로고    scopus 로고
    • Immune challenge differentially affects transcript abundance of three antimicrobial peptides in hemocytes from the moth Pseudoplusia includens
    • Lavine M.D., Chen G., and Strand M.R. Immune challenge differentially affects transcript abundance of three antimicrobial peptides in hemocytes from the moth Pseudoplusia includens. Insect Biochem Mol Biol 35 (2005) 1335-1346
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 1335-1346
    • Lavine, M.D.1    Chen, G.2    Strand, M.R.3
  • 36
    • 10744221006 scopus 로고    scopus 로고
    • Purification, cDNA cloning and expression of an insect defensin from the great wax moth, Galleria mellonella
    • Lee Y.S., Yun E.K., Jang W.S., Kim I., Lee J.H., Park S.Y., et al. Purification, cDNA cloning and expression of an insect defensin from the great wax moth, Galleria mellonella. Insect Mol Biol 13 (2004) 65-72
    • (2004) Insect Mol Biol , vol.13 , pp. 65-72
    • Lee, Y.S.1    Yun, E.K.2    Jang, W.S.3    Kim, I.4    Lee, J.H.5    Park, S.Y.6
  • 38
    • 0010570777 scopus 로고
    • Insect immunity: cDNA clones coding for the precursor forms of cecropins A and D, antibacterial proteins from Hyalophora cecropia
    • Lidholm D.A., Gudmundsson G.H., Xanthopoulos K.G., and Boman H.G. Insect immunity: cDNA clones coding for the precursor forms of cecropins A and D, antibacterial proteins from Hyalophora cecropia. FEBS Lett 226 (1987) 8-12
    • (1987) FEBS Lett , vol.226 , pp. 8-12
    • Lidholm, D.A.1    Gudmundsson, G.H.2    Xanthopoulos, K.G.3    Boman, H.G.4
  • 39
    • 0029936309 scopus 로고    scopus 로고
    • Purification and characterization of lysozyme from hemolymph of Heliothis virescens larvae
    • Lockey T.D., and Ourth D.D. Purification and characterization of lysozyme from hemolymph of Heliothis virescens larvae. Biochem Biophys Res Commun 220 (1996) 502-508
    • (1996) Biochem Biophys Res Commun , vol.220 , pp. 502-508
    • Lockey, T.D.1    Ourth, D.D.2
  • 40
    • 0035757181 scopus 로고    scopus 로고
    • Antibacterial peptides of the moth Galleria mellonella
    • Mak P., Chmiel D., and Gacek G.J. Antibacterial peptides of the moth Galleria mellonella. Acta Biochim Pol 48 (2001) 1191-1195
    • (2001) Acta Biochim Pol , vol.48 , pp. 1191-1195
    • Mak, P.1    Chmiel, D.2    Gacek, G.J.3
  • 41
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • Matsuzaki K. Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochim Biophys Acta 1462 (1999) 1-10
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 42
    • 0028504387 scopus 로고
    • Preliminary experimental anticancer activity of cecropins
    • Moore A.J., Devine D.A., and Bibby M.C. Preliminary experimental anticancer activity of cecropins. Pept Res 7 (1994) 265-269
    • (1994) Pept Res , vol.7 , pp. 265-269
    • Moore, A.J.1    Devine, D.A.2    Bibby, M.C.3
  • 43
    • 0029587068 scopus 로고
    • Parallel induction of cecropin and lysozyme in larvae of the silkworm Bombyx mori
    • Morishima I., Horiba T., Iketani M., Nishioka E., and Yamano Y. Parallel induction of cecropin and lysozyme in larvae of the silkworm Bombyx mori. Dev Comp Immunol 19 (1995) 357-363
    • (1995) Dev Comp Immunol , vol.19 , pp. 357-363
    • Morishima, I.1    Horiba, T.2    Iketani, M.3    Nishioka, E.4    Yamano, Y.5
  • 44
    • 0028385708 scopus 로고
    • Structure and induction of a lysozyme gene from the tobacco hornworm, Manduca sexta
    • Mulnix A., and Dunn P.E. Structure and induction of a lysozyme gene from the tobacco hornworm, Manduca sexta. Insect Biochem Mol Biol 24 (1994) 271-281
    • (1994) Insect Biochem Mol Biol , vol.24 , pp. 271-281
    • Mulnix, A.1    Dunn, P.E.2
  • 46
    • 28444482821 scopus 로고    scopus 로고
    • An enhanced method for peptides sequencing by N-terminal derivatization and MS
    • Noga M., Lewandowski J., Suder P., and Silberring J. An enhanced method for peptides sequencing by N-terminal derivatization and MS. Proteomics 5 (2005) 4367-4375
    • (2005) Proteomics , vol.5 , pp. 4367-4375
    • Noga, M.1    Lewandowski, J.2    Suder, P.3    Silberring, J.4
  • 47
    • 0036633301 scopus 로고    scopus 로고
    • The short proline-rich antibacterial peptide family
    • Otvos Jr. L. The short proline-rich antibacterial peptide family. Cell Mol Life Sci 59 (2002) 1138-1150
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1138-1150
    • Otvos Jr., L.1
  • 48
    • 18544366816 scopus 로고    scopus 로고
    • Host defense peptides as new weapons in cancer treatment
    • Papo N., and Shai Y. Host defense peptides as new weapons in cancer treatment. Cell Mol Life Sci 62 (2005) 784-790
    • (2005) Cell Mol Life Sci , vol.62 , pp. 784-790
    • Papo, N.1    Shai, Y.2
  • 49
    • 4344699934 scopus 로고    scopus 로고
    • Effects of two hemolymph proteins on humoral immune defense reactions in the wax moth, Galleria mellonella
    • Park S.Y., Kim C.H., Jeong W.H., Lee J.H., Seo S.J., Han Y.S., et al. Effects of two hemolymph proteins on humoral immune defense reactions in the wax moth, Galleria mellonella. Dev Comp Immunol 29 (2005) 43-51
    • (2005) Dev Comp Immunol , vol.29 , pp. 43-51
    • Park, S.Y.1    Kim, C.H.2    Jeong, W.H.3    Lee, J.H.4    Seo, S.J.5    Han, Y.S.6
  • 50
    • 0015925730 scopus 로고
    • Studies on insect bacteriolytic enzymes. I. Lysozyme in haemolymph of Galleria mellonella and Bombyx mori
    • Powning R.F., and Davidson W.J. Studies on insect bacteriolytic enzymes. I. Lysozyme in haemolymph of Galleria mellonella and Bombyx mori. Comp Biochem Physiol 45B (1973) 669-686
    • (1973) Comp Biochem Physiol , vol.45 B , pp. 669-686
    • Powning, R.F.1    Davidson, W.J.2
  • 51
    • 0020355347 scopus 로고
    • Insect immunity: isolation and structure of cecropins B and D from pupae of the Chinese oak silk moth, Antheraea pernyi
    • Qu Z., Steiner H., Engstro{combining double acute accent}m A., Bennich H., and Boman H.G. Insect immunity: isolation and structure of cecropins B and D from pupae of the Chinese oak silk moth, Antheraea pernyi. Eur J Biochem 127 (1982) 219-224
    • (1982) Eur J Biochem , vol.127 , pp. 219-224
    • Qu, Z.1    Steiner, H.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 52
    • 2442538316 scopus 로고    scopus 로고
    • Primary structure and in vitro antibacterial properties of the Drosophila melanogaster attacin C pro-domain
    • Rabel D., Charlet M., Ehret-Sabatier L., Cavicchioli L., Cudic M., Otvos Jr. L., et al. Primary structure and in vitro antibacterial properties of the Drosophila melanogaster attacin C pro-domain. J Biol Chem 279 (2004) 14853-14859
    • (2004) J Biol Chem , vol.279 , pp. 14853-14859
    • Rabel, D.1    Charlet, M.2    Ehret-Sabatier, L.3    Cavicchioli, L.4    Cudic, M.5    Otvos Jr., L.6
  • 53
    • 4444297435 scopus 로고    scopus 로고
    • Correlation between gliotoxin production and virulence of Aspergillus fumigatus in Galleria mellonella
    • Reeves E.P., Messina C.G.M., Doyle S., and Kavanagh K. Correlation between gliotoxin production and virulence of Aspergillus fumigatus in Galleria mellonella. Mycopathologia 158 (2004) 73-79
    • (2004) Mycopathologia , vol.158 , pp. 73-79
    • Reeves, E.P.1    Messina, C.G.M.2    Doyle, S.3    Kavanagh, K.4
  • 54
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166 (1987) 368-379
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 55
    • 0025057464 scopus 로고
    • Locusta tachykinin I and II, two novel insect neuropeptides with homology to peptides from the vertebrate tachykinin family
    • Schoofs L., Holman G.M., Hayes T.K., Nachman R.J., and De Loof A. Locusta tachykinin I and II, two novel insect neuropeptides with homology to peptides from the vertebrate tachykinin family. FEBS Lett 261 (1990) 397-401
    • (1990) FEBS Lett , vol.261 , pp. 397-401
    • Schoofs, L.1    Holman, G.M.2    Hayes, T.K.3    Nachman, R.J.4    De Loof, A.5
  • 56
    • 0042970579 scopus 로고    scopus 로고
    • Cloning and expression of gallerimycin, an antifungal peptide expressed in immune response of greater wax moth larvae, Galleria mellonella
    • Schuhmann B., Seitz V., Vilcinskas A., and Podsiadlowski L. Cloning and expression of gallerimycin, an antifungal peptide expressed in immune response of greater wax moth larvae, Galleria mellonella. Arch Insect Biochem Physiol 53 (2003) 125-133
    • (2003) Arch Insect Biochem Physiol , vol.53 , pp. 125-133
    • Schuhmann, B.1    Seitz, V.2    Vilcinskas, A.3    Podsiadlowski, L.4
  • 57
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H., Hultmark D., Engstro{combining double acute accent}m A., Bennich H., and Boman H.G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292 (1981) 246-248
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 58
    • 0025809272 scopus 로고
    • Organization and expression of the immunoresponsive lysozyme gene in the giant silk moth, Hyalophora cecropia
    • Sun S.-C., Asling B., and Faye I. Organization and expression of the immunoresponsive lysozyme gene in the giant silk moth, Hyalophora cecropia. J Biol Chem 266 (1991) 6644-6649
    • (1991) J Biol Chem , vol.266 , pp. 6644-6649
    • Sun, S.-C.1    Asling, B.2    Faye, I.3
  • 59
    • 0036160153 scopus 로고    scopus 로고
    • How Drosophila combats microbial infection: a model to study innate immunity and host-pathogen interactions
    • Tzou P., De Gregorio E., and Lemaitre B. How Drosophila combats microbial infection: a model to study innate immunity and host-pathogen interactions. Curr Opin Microbiol 5 (2002) 102-110
    • (2002) Curr Opin Microbiol , vol.5 , pp. 102-110
    • Tzou, P.1    De Gregorio, E.2    Lemaitre, B.3
  • 60
    • 33645057448 scopus 로고    scopus 로고
    • Apolipophorin III: role model apolipoprotein
    • Weers P.M., and Ryan R.O. Apolipophorin III: role model apolipoprotein. Insect Biochem Mol Biol 36 (2006) 231-240
    • (2006) Insect Biochem Mol Biol , vol.36 , pp. 231-240
    • Weers, P.M.1    Ryan, R.O.2
  • 61
    • 0031761879 scopus 로고    scopus 로고
    • Primary structure of apolipophorin-III from the greater wax moth, Galleria mellonella
    • Weise C., Franke P., Kopacek P., and Wiesner A. Primary structure of apolipophorin-III from the greater wax moth, Galleria mellonella. J Protein Chem 17 (1998) 633-641
    • (1998) J Protein Chem , vol.17 , pp. 633-641
    • Weise, C.1    Franke, P.2    Kopacek, P.3    Wiesner, A.4
  • 62
    • 0842300362 scopus 로고    scopus 로고
    • A novel role for an insect apolipoprotein (apolipophorin III) in beta-1,3-glucan pattern recognition and cellular encapsulation reactions
    • Whitten M.M., Tew I.F., Lee B.L., and Ratcliffe N.A. A novel role for an insect apolipoprotein (apolipophorin III) in beta-1,3-glucan pattern recognition and cellular encapsulation reactions. J Immunol 172 (2004) 2177-2185
    • (2004) J Immunol , vol.172 , pp. 2177-2185
    • Whitten, M.M.1    Tew, I.F.2    Lee, B.L.3    Ratcliffe, N.A.4
  • 63
    • 33846803221 scopus 로고    scopus 로고
    • www.bbcm.univ.trieste.it/∼tossi/pag1.htm
  • 64
    • 0032994092 scopus 로고    scopus 로고
    • Immune proteins and their gene expression in the silkworm, Bombyx mori
    • Yamakawa M., and Tanaka H. Immune proteins and their gene expression in the silkworm, Bombyx mori. Dev Comp Immunol 23 (1999) 281-289
    • (1999) Dev Comp Immunol , vol.23 , pp. 281-289
    • Yamakawa, M.1    Tanaka, H.2
  • 65
    • 0035032985 scopus 로고    scopus 로고
    • Synergistic interactions between mammalian antimicrobial defense peptides
    • Yan H., and Hancock R.E. Synergistic interactions between mammalian antimicrobial defense peptides. Antimicrob Agents Chemother 45 (2001) 1558-1560
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 1558-1560
    • Yan, H.1    Hancock, R.E.2
  • 66
    • 0032923888 scopus 로고    scopus 로고
    • cDNA cloning and gene expression of cecropin D, an antibacterial protein in the silkworm, Bombyx mori
    • Yang J., Furukawa S., Sagisaka A., Ishibashi J., Taniai K., Shono T., et al. cDNA cloning and gene expression of cecropin D, an antibacterial protein in the silkworm, Bombyx mori. Comp Biochem Physiol B 122 (1999) 409-414
    • (1999) Comp Biochem Physiol B , vol.122 , pp. 409-414
    • Yang, J.1    Furukawa, S.2    Sagisaka, A.3    Ishibashi, J.4    Taniai, K.5    Shono, T.6
  • 67
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman M.R., and Yount N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 55 (2003) 27-55
    • (2003) Pharmacol Rev , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 68
    • 0036823772 scopus 로고    scopus 로고
    • Comparative study on characteristics of lysozymes from the hemolymph of three lepidopteran larvae, Galleria mellonella, Bombyx mori, Agrius convolvuli
    • Yu K.H., Kim K.N., Lee J.H., Lee H.S., Kim S.H., Cho K.Y., et al. Comparative study on characteristics of lysozymes from the hemolymph of three lepidopteran larvae, Galleria mellonella, Bombyx mori, Agrius convolvuli. Dev Comp Immunol 26 (2002) 707-713
    • (2002) Dev Comp Immunol , vol.26 , pp. 707-713
    • Yu, K.H.1    Kim, K.N.2    Lee, J.H.3    Lee, H.S.4    Kim, S.H.5    Cho, K.Y.6
  • 69
    • 0037726774 scopus 로고    scopus 로고
    • Identification by subtractive suppression hybridization of bacteria-induced genes expressed in Manduca sexta fat body
    • Zhu Y., Johnson T.J., Myers A.A., and Kanost M.R. Identification by subtractive suppression hybridization of bacteria-induced genes expressed in Manduca sexta fat body. Insect Biochem Mol Biol 33 (2003) 541-559
    • (2003) Insect Biochem Mol Biol , vol.33 , pp. 541-559
    • Zhu, Y.1    Johnson, T.J.2    Myers, A.A.3    Kanost, M.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.