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Volumn 8, Issue 4, 2013, Pages

Demonstration of Cytotoxicity against Wasps by Pierisin-1: A Possible Defense Factor in the Cabbage White Butterfly

Author keywords

[No Author keywords available]

Indexed keywords

CYTOTOXIC FACTOR; MESSENGER RNA; PIERISIN 1; UNCLASSIFIED DRUG; CYTOTOXIN; INSECT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PIERISIN PROTEIN, INSECT;

EID: 84876514134     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0060539     Document Type: Article
Times cited : (10)

References (57)
  • 1
    • 0032844523 scopus 로고    scopus 로고
    • Molecular cloning of an apoptosis-inducing protein, pierisin, from cabbage butterfly: Possible involvement of ADP-ribosylation in its activity
    • Watanabe M, Kono T, Matsushima-Hibiya Y, Kanazawa T, Nishisaka N, et al. (1999) Molecular cloning of an apoptosis-inducing protein, pierisin, from cabbage butterfly: possible involvement of ADP-ribosylation in its activity. Proc Natl Acad Sci U S A. 96(19)p. 10608-13.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.19 , pp. 10608-10613
    • Watanabe, M.1    Kono, T.2    Matsushima-Hibiya, Y.3    Kanazawa, T.4    Nishisaka, N.5
  • 2
    • 0030466451 scopus 로고    scopus 로고
    • Presence in Pieris rapae of cytotoxic activity against human carcinoma cells
    • Koyama K, Wakabayashi K, Masutani M, Koiwai K, Watanabe M, et al. (1996) Presence in Pieris rapae of cytotoxic activity against human carcinoma cells. Jpn J Cancer Res. 87(12)p. 1259-62.
    • (1996) Jpn J Cancer Res , vol.87 , Issue.12 , pp. 1259-1262
    • Koyama, K.1    Wakabayashi, K.2    Masutani, M.3    Koiwai, K.4    Watanabe, M.5
  • 3
    • 0038321939 scopus 로고    scopus 로고
    • Identification of glycosphingolipid receptors for pierisin-1, a guanine-specific ADP-ribosylating toxin from the cabbage butterfly
    • Matsushima-Hibiya Y, Watanabe M, Hidari KI, Miyamoto D, Suzuki Y, et al. (2003) Identification of glycosphingolipid receptors for pierisin-1, a guanine-specific ADP-ribosylating toxin from the cabbage butterfly. J Biol Chem. 278(11)p. 9972-8.
    • (2003) J Biol Chem , vol.278 , Issue.11 , pp. 9972-9978
    • Matsushima-Hibiya, Y.1    Watanabe, M.2    Hidari, K.I.3    Miyamoto, D.4    Suzuki, Y.5
  • 4
    • 0035940453 scopus 로고    scopus 로고
    • Mono(ADP-ribosyl)ation of 2′-deoxyguanosine residue in DNA by an apoptosis-inducing protein, pierisin-1, from cabbage butterfly
    • Takamura-Enya T, Watanabe M, Totsuka Y, Kanazawa T, Matsushima-Hibiya Y, et al. (2001) Mono(ADP-ribosyl)ation of 2′-deoxyguanosine residue in DNA by an apoptosis-inducing protein, pierisin-1, from cabbage butterfly. Proc Natl Acad Sci U S A. 98(22)p. 12414-9.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.22 , pp. 12414-12419
    • Takamura-Enya, T.1    Watanabe, M.2    Totsuka, Y.3    Kanazawa, T.4    Matsushima-Hibiya, Y.5
  • 5
    • 40649123801 scopus 로고    scopus 로고
    • Distribution of cytotoxic and DNA ADP-ribosylating activity in crude extracts from butterflies among the family Pieridae
    • Matsumoto Y, Nakano T, Yamamoto M, Matsushima-Hibiya Y, Odagiri K, et al. (2008) Distribution of cytotoxic and DNA ADP-ribosylating activity in crude extracts from butterflies among the family Pieridae. Proc Natl Acad Sci U S A. 105(7)p. 2516-20.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.7 , pp. 2516-2520
    • Matsumoto, Y.1    Nakano, T.2    Yamamoto, M.3    Matsushima-Hibiya, Y.4    Odagiri, K.5
  • 6
    • 70149090591 scopus 로고    scopus 로고
    • Molecular cloning of apoptosis-inducing Pierisin-like proteins, from two species of white butterfly, Pieris melete and Aporia crataegi
    • Yamamoto M, Nakano T, Matsushima-Hibiya Y, Totsuka Y, Takahashi-Nakaguchi A, et al. (2009) Molecular cloning of apoptosis-inducing Pierisin-like proteins, from two species of white butterfly, Pieris melete and Aporia crataegi. Comp Biochem Physiol B Biochem Mol Biol. 154(3)p. 326-33.
    • (2009) Comp Biochem Physiol B Biochem Mol Biol , vol.154 , Issue.3 , pp. 326-333
    • Yamamoto, M.1    Nakano, T.2    Matsushima-Hibiya, Y.3    Totsuka, Y.4    Takahashi-Nakaguchi, A.5
  • 7
    • 0033835640 scopus 로고    scopus 로고
    • Purification and cloning of pierisin-2, an apoptosis-inducing protein from the cabbage butterfly, Pieris brassicae
    • Matsushima-Hibiya Y, Watanabe M, Kono T, Kanazawa T, Koyama K, et al. (2000) Purification and cloning of pierisin-2, an apoptosis-inducing protein from the cabbage butterfly, Pieris brassicae. Eur J Biochem. 267(18)p. 5742-50.
    • (2000) Eur J Biochem , vol.267 , Issue.18 , pp. 5742-5750
    • Matsushima-Hibiya, Y.1    Watanabe, M.2    Kono, T.3    Kanazawa, T.4    Koyama, K.5
  • 8
    • 33750015246 scopus 로고    scopus 로고
    • Bacillus sphaericus mosquitocidal toxin (MTX) and pierisin: The enigmatic offspring from the family of ADP-ribosyltransferases
    • Carpusca I, Jank T, Aktories K (2006) Bacillus sphaericus mosquitocidal toxin (MTX) and pierisin: the enigmatic offspring from the family of ADP-ribosyltransferases. Mol Microbiol. 62(3)p. 621-30.
    • (2006) Mol Microbiol , vol.62 , Issue.3 , pp. 621-630
    • Carpusca, I.1    Jank, T.2    Aktories, K.3
  • 9
    • 7444265252 scopus 로고    scopus 로고
    • Developmental stage-specific expression and tissue distribution of pierisin-1, a guanine-specific ADP-ribosylating toxin, in Pieris rapae
    • Watanabe M, Nakano T, Shiotani B, Matsushima-Hibiya Y, Kiuchi M, et al. (2004) Developmental stage-specific expression and tissue distribution of pierisin-1, a guanine-specific ADP-ribosylating toxin, in Pieris rapae. Comp Biochem Physiol A Mol Integr Physiol. 139(2)p. 125-31.
    • (2004) Comp Biochem Physiol a Mol Integr Physiol , vol.139 , Issue.2 , pp. 125-131
    • Watanabe, M.1    Nakano, T.2    Shiotani, B.3    Matsushima-Hibiya, Y.4    Kiuchi, M.5
  • 10
    • 34250711204 scopus 로고    scopus 로고
    • A multilayered defense against infection: Combinatorial control of insect immune genes
    • Uvell H, Engstrom Y (2007) A multilayered defense against infection: combinatorial control of insect immune genes. Trends Genet. 23(7)p. 342-9.
    • (2007) Trends Genet , vol.23 , Issue.7 , pp. 342-349
    • Uvell, H.1    Engstrom, Y.2
  • 11
    • 43249114465 scopus 로고    scopus 로고
    • Positive and negative regulation of the Drosophila immune response
    • Aggarwal K, Silverman N (2008) Positive and negative regulation of the Drosophila immune response. BMB Rep. 41(4)p. 267-77.
    • (2008) BMB Rep , vol.41 , Issue.4 , pp. 267-277
    • Aggarwal, K.1    Silverman, N.2
  • 12
    • 0035999729 scopus 로고    scopus 로고
    • Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects
    • Sugumaran M (2002) Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects. Pigment Cell Res. 15(1)p. 2-9.
    • (2002) Pigment Cell Res , vol.15 , Issue.1 , pp. 2-9
    • Sugumaran, M.1
  • 13
    • 1642463826 scopus 로고    scopus 로고
    • The prophenoloxidase-activating system in invertebrates
    • Cerenius L, Soderhall K (2004) The prophenoloxidase-activating system in invertebrates. Immunol Rev. 198p. 116-26.
    • (2004) Immunol Rev , vol.198 p , pp. 116-126
    • Cerenius, L.1    Soderhall, K.2
  • 14
    • 0036784566 scopus 로고    scopus 로고
    • Insect hemocytes and their role in immunity
    • Lavine MD, Strand MR (2002) Insect hemocytes and their role in immunity. Insect Biochem Mol Biol. 32(10)p. 1295-309.
    • (2002) Insect Biochem Mol Biol , vol.32 , Issue.10 , pp. 1295-1309
    • Lavine, M.D.1    Strand, M.R.2
  • 15
    • 0020284248 scopus 로고
    • Cellular recognition of foreign materials by Bombyx mori phagocytes: I. Immunocompetent cells
    • Wago H (1982) Cellular recognition of foreign materials by Bombyx mori phagocytes: I. Immunocompetent cells. Dev Comp Immunol. 6(4)p. 591-9.
    • (1982) Dev Comp Immunol , vol.6 , Issue.4 , pp. 591-599
    • Wago, H.1
  • 16
    • 0020730572 scopus 로고
    • Cellular recognition of foreign materials by Bombyx mori phagocytes: II. Role of hemolymph and phagocyte filopodia in the cellular reactions
    • Wago H (1983) Cellular recognition of foreign materials by Bombyx mori phagocytes: II. Role of hemolymph and phagocyte filopodia in the cellular reactions. Dev Comp Immunol. 7(2)p. 199-208.
    • (1983) Dev Comp Immunol , vol.7 , Issue.2 , pp. 199-208
    • Wago, H.1
  • 17
    • 0018884630 scopus 로고
    • Humoral factors promoting the adhesive properties of the granular cells and plasmatocytes of the silkworm, Bombyxmori, and their possible role in the initial cellular reactions to foreignness
    • Wago H (1980) Humoral factors promoting the adhesive properties of the granular cells and plasmatocytes of the silkworm, Bombyxmori, and their possible role in the initial cellular reactions to foreignness. Cell Immunol. 54(1)p. 155-69.
    • (1980) Cell Immunol , vol.54 , Issue.1 , pp. 155-169
    • Wago, H.1
  • 18
    • 0030057057 scopus 로고    scopus 로고
    • Insect immunity: Early events in the encapsulation process of parasitoid (Leptopilina boulardi) eggs in resistant and susceptible strains of Drosophila
    • Russo J, Dupas S, Frey F, Carton Y, Brehelin M (1996) Insect immunity: early events in the encapsulation process of parasitoid (Leptopilina boulardi) eggs in resistant and susceptible strains of Drosophila. Parasitology. 112 (Pt 1)p. 135-42.
    • (1996) Parasitology , vol.112 , Issue.Pt 1 , pp. 135-142
    • Russo, J.1    Dupas, S.2    Frey, F.3    Carton, Y.4    Brehelin, M.5
  • 19
    • 0035133118 scopus 로고    scopus 로고
    • Immunogenetic aspects of the cellular immune response of Drosophila against parasitoids
    • Carton Y, Nappi AJ (2001) Immunogenetic aspects of the cellular immune response of Drosophila against parasitoids. Immunogenetics. 52(3-4)p. 157-164.
    • (2001) Immunogenetics , vol.52 , Issue.3-4 , pp. 157-164
    • Carton, Y.1    Nappi, A.J.2
  • 20
    • 84940941470 scopus 로고
    • Regulation of insect hemolymph phenoloxidases
    • (N. Beckage, S.N. Thompson, B.A. Federici, eds.) Academic Press
    • Sugumaran M, Kanost MR (1993) Regulation of insect hemolymph phenoloxidases. Parasites and Pathogens of Insects. (N. Beckage, S.N. Thompson, B.A. Federici, eds.) Academic Press.: p. pp. 317-342.
    • (1993) Parasites and Pathogens of Insects , pp. 317-342
    • Sugumaran, M.1    Kanost, M.R.2
  • 21
    • 70349167463 scopus 로고    scopus 로고
    • The role of melanization and cytotoxic by-products in the cellular immune responses of Drosophila against parasitic wasps
    • Nappi A, Poirie M, Carton Y (2009) The role of melanization and cytotoxic by-products in the cellular immune responses of Drosophila against parasitic wasps. Adv Parasitol. 70p. 99-121.
    • (2009) Adv Parasitol , pp. 99-121
    • Nappi, A.1    Poirie, M.2    Carton, Y.3
  • 22
    • 15944404330 scopus 로고    scopus 로고
    • Melanogenesis and associated cytotoxic reactions: Applications to insect innate immunity
    • Nappi AJ, Christensen BM (2005) Melanogenesis and associated cytotoxic reactions: applications to insect innate immunity.Insect Biochem Mol Biol. 35(5)p. 443-59.
    • (2005) Insect Biochem Mol Biol , vol.35 , Issue.5 , pp. 443-459
    • Nappi, A.J.1    Christensen, B.M.2
  • 23
    • 0036009753 scopus 로고    scopus 로고
    • Isolation of a protein lethal to the endoparasitoid Cotesia kariyai from entomopoxvirus-infected larvae of Mythimna separata
    • Okuno S, Nakai M, Hiraoka T, Kunimi Y (2002) Isolation of a protein lethal to the endoparasitoid Cotesia kariyai from entomopoxvirus-infected larvae of Mythimna separata. Insect Biochem Mol Biol. 32(5)p. 559-66.
    • (2002) Insect Biochem Mol Biol , vol.32 , Issue.5 , pp. 559-566
    • Okuno, S.1    Nakai, M.2    Hiraoka, T.3    Kunimi, Y.4
  • 24
    • 33750991592 scopus 로고    scopus 로고
    • Physiological suppression of the larval parasitoid Glyptapanteles pallipes by the polyembryonic parasitoid Copidosoma floridanum
    • Uka D, Hiraoka T, Iwabuchi K (2006) Physiological suppression of the larval parasitoid Glyptapanteles pallipes by the polyembryonic parasitoid Copidosoma floridanum. J Insect Physiol. 52(11-12)p. 1137-42.
    • (2006) J Insect Physiol , vol.52 , Issue.11-12 , pp. 1137-1142
    • Uka, D.1    Hiraoka, T.2    Iwabuchi, K.3
  • 25
    • 0000571934 scopus 로고
    • Facultative hyperparasitism by the egg parasitoid Trichogramma pretiosum (Hymenoptera:Trichogrammatidae)
    • Strand MR, Vinson SB (1984) Facultative hyperparasitism by the egg parasitoid Trichogramma pretiosum (Hymenoptera:Trichogrammatidae). Annals of the Entomological Society of America 77p. 679-686.
    • (1984) Annals of the Entomological Society of America , pp. 679-686
    • Strand, M.R.1    Vinson, S.B.2
  • 26
    • 0024190935 scopus 로고
    • Multiparasitism of the green pea aphid, Myzus persicae: Competition in the egg stage between Aphidius matricariae and Ephedrus cerasicola
    • Hagver EB (1988) Multiparasitism of the green pea aphid, Myzus persicae: competition in the egg stage between Aphidius matricariae and Ephedrus cerasicola. Entomologia Experimentalis et Applicata. 47p. 275-282.
    • (1988) Entomologia Experimentalis Et Applicata , pp. 275-282
    • Hagver, E.B.1
  • 27
    • 0001687313 scopus 로고
    • Toxic Factor Produced by a Granulosis Virus in Armyworm Larva: Effect on Apanteles militaris
    • Kaya HK (1970) Toxic Factor Produced by a Granulosis Virus in Armyworm Larva: Effect on Apanteles militaris. Science. 168(3928)p. 251-253.
    • (1970) Science , vol.168 , Issue.3928 , pp. 251-253
    • Kaya, H.K.1
  • 28
    • 69249152571 scopus 로고    scopus 로고
    • Bacteriophages encode factors required for protection in a symbiotic mutualism
    • Oliver KM, Degnan PH, Hunter MS, Moran NA (2009) Bacteriophages encode factors required for protection in a symbiotic mutualism. Science. 325(5943)p. 992-4.
    • (2009) Science , vol.325 , Issue.5943 , pp. 992-994
    • Oliver, K.M.1    Degnan, P.H.2    Hunter, M.S.3    Moran, N.A.4
  • 29
    • 0037452704 scopus 로고    scopus 로고
    • Facultative bacterial symbionts in aphids confer resistance to parasitic wasps
    • Oliver KM, Russell JA, Moran NA, Hunter MS (2003) Facultative bacterial symbionts in aphids confer resistance to parasitic wasps. Proc Natl Acad Sci U S A. 100(4)p. 1803-7.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.4 , pp. 1803-1807
    • Oliver, K.M.1    Russell, J.A.2    Moran, N.A.3    Hunter, M.S.4
  • 30
    • 2442666308 scopus 로고    scopus 로고
    • Enzymatic properties of pierisin-1 and its N-terminal domain, a guanine-specific ADP-ribosyltransferase from the cabbage butterfly
    • Watanabe M, Enomoto S, Takamura-Enya T, Nakano T, Koyama K, et al. (2004) Enzymatic properties of pierisin-1 and its N-terminal domain, a guanine-specific ADP-ribosyltransferase from the cabbage butterfly. J Biochem. 135(4)p. 471-7.
    • (2004) J Biochem , vol.135 , Issue.4 , pp. 471-477
    • Watanabe, M.1    Enomoto, S.2    Takamura-Enya, T.3    Nakano, T.4    Koyama, K.5
  • 31
    • 0032909027 scopus 로고    scopus 로고
    • Is the surface of endoparasitic wasp eggs and larvae covered by a limited coagulation reaction?
    • Kinuthia W, Li DM, Schmidt O, Theopold U (1999) Is the surface of endoparasitic wasp eggs and larvae covered by a limited coagulation reaction? Journal of Insect Physiology. 45(5)p. 501-506.
    • (1999) Journal of Insect Physiology , vol.45 , Issue.5 , pp. 501-506
    • Kinuthia, W.1    Li, D.M.2    Schmidt, O.3    Theopold, U.4
  • 32
    • 0004291402 scopus 로고    scopus 로고
    • Chapman and Hall, London
    • Quicke DLJ (1997) Parasitic Wasps. Chapman and Hall, London. p.470 pp.
    • (1997) Parasitic Wasps , pp. 470
    • Quicke, D.L.J.1
  • 33
    • 32444440512 scopus 로고    scopus 로고
    • Development of the anal vesicle, salivary glands and gut in the egg-larval parasitoid Chelonus inanitus: Tools to take up nutrients and to manipulate the host?
    • Kaeslin M, Wyler T, Grossniklaus-Burgin C, Lanzrein B (2006) Development of the anal vesicle, salivary glands and gut in the egg-larval parasitoid Chelonus inanitus: tools to take up nutrients and to manipulate the host? J Insect Physiol. 52(3)p. 269-81.
    • (2006) J Insect Physiol , vol.52 , Issue.3 , pp. 269-281
    • Kaeslin, M.1    Wyler, T.2    Grossniklaus-Burgin, C.3    Lanzrein, B.4
  • 34
    • 0035058105 scopus 로고    scopus 로고
    • Control mechanisms of the prophenoloxidase cascade
    • Sugumaran M (2001) Control mechanisms of the prophenoloxidase cascade. Adv Exp Med Biol. 484p. 289-98.
    • (2001) Adv Exp Med Biol , vol.484 p , pp. 289-298
    • Sugumaran, M.1
  • 35
    • 84858006006 scopus 로고    scopus 로고
    • Nucleotide sequence and chromosomal localization of the gene for pierisin-1, a DNA ADP-ribosylating protein, in the cabbage butterfly Pieris rapae
    • Yamamoto M, Takahashi-Nakaguchi A, Matsushima-Hibiya Y, Nakano T, Totsuka Y, et al. (2011) Nucleotide sequence and chromosomal localization of the gene for pierisin-1, a DNA ADP-ribosylating protein, in the cabbage butterfly Pieris rapae. Genetica. 139(10)p. 1251-8.
    • (2011) Genetica , vol.139 , Issue.10 , pp. 1251-1258
    • Yamamoto, M.1    Takahashi-Nakaguchi, A.2    Matsushima-Hibiya, Y.3    Nakano, T.4    Totsuka, Y.5
  • 36
    • 67649723451 scopus 로고    scopus 로고
    • Genome-wide transcriptomic profiling of Anopheles gambiae hemocytes reveals pathogen-specific signatures upon bacterial challenge and Plasmodium berghei infection
    • Baton LA, Robertson A, Warr E, Strand MR, Dimopoulos G (2009) Genome-wide transcriptomic profiling of Anopheles gambiae hemocytes reveals pathogen-specific signatures upon bacterial challenge and Plasmodium berghei infection. BMC Genomics. 10p. 257.
    • (2009) BMC Genomics , vol.10 p , pp. 257
    • Baton, L.A.1    Robertson, A.2    Warr, E.3    Strand, M.R.4    Dimopoulos, G.5
  • 37
    • 33644850267 scopus 로고    scopus 로고
    • Genome-wide gene expression in response to parasitoid attack in Drosophila
    • Wertheim B, Kraaijeveld AR, Schuster E, Blanc E, Hopkins M, et al. (2005) Genome-wide gene expression in response to parasitoid attack in Drosophila. Genome Biol. 6(11) R94.
    • (2005) Genome Biol , vol.6 , Issue.11
    • Wertheim, B.1    Kraaijeveld, A.R.2    Schuster, E.3    Blanc, E.4    Hopkins, M.5
  • 38
    • 1942485935 scopus 로고    scopus 로고
    • Genetic analysis of contributions of dorsal group and JAK-Stat92E pathway genes to larval hemocyte concentration and the egg encapsulation response in Drosophila
    • Sorrentino RP, Melk JP, Govind S (2004) Genetic analysis of contributions of dorsal group and JAK-Stat92E pathway genes to larval hemocyte concentration and the egg encapsulation response in Drosophila. Genetics. 166(3)p. 1343-56.
    • (2004) Genetics , vol.166 , Issue.3 , pp. 1343-1356
    • Sorrentino, R.P.1    Melk, J.P.2    Govind, S.3
  • 39
    • 0029110524 scopus 로고
    • Immunological basis for compatibility in parasitoid-host relationships
    • Strand MR, Pech LL (1995) Immunological basis for compatibility in parasitoid-host relationships. Annu Rev Entomol. 40p. 31-56.
    • (1995) Annu Rev Entomol , vol.40 p , pp. 31-56
    • Strand, M.R.1    Pech, L.L.2
  • 40
    • 0002638054 scopus 로고
    • Host-regulating factors associated with parasitic Hymenoptera
    • Hedin. PA (ed), Washington, DC: ACS Symp. Series No. 449
    • Coudron T (1991) Host-regulating factors associated with parasitic Hymenoptera. Hedin. PA (ed): Naturally Occurring Pest Bioregulators. Washington, DC: ACS Symp. Series No. 449: p. pp 41-65.
    • (1991) Naturally Occurring Pest Bioregulators , pp. 41-65
    • Coudron, T.1
  • 41
    • 0028161048 scopus 로고
    • Passive protection of eggs from the parasitoid, Cotesia rubecula, in the host, Pieris rapae
    • Asgari S, Schmidt O (1994) Passive protection of eggs from the parasitoid, Cotesia rubecula, in the host, Pieris rapae. Journal of Insect Physiology. 40(9)p. 789-795.
    • (1994) Journal of Insect Physiology , vol.40 , Issue.9 , pp. 789-795
    • Asgari, S.1    Schmidt, O.2
  • 42
    • 0032584137 scopus 로고    scopus 로고
    • A protein with protective properties against the cellular defense reactions in insects
    • Asgari S, Theopold U, Wellby C, Schmidt O (1998) A protein with protective properties against the cellular defense reactions in insects. Proc Natl Acad Sci U S A. 95(7)p. 3690-5.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.7 , pp. 3690-3695
    • Asgari, S.1    Theopold, U.2    Wellby, C.3    Schmidt, O.4
  • 43
    • 0000229255 scopus 로고
    • The role of Apanteles glomeratus venom in the defensive response of its host, Pieirs rapae crucivora
    • Kitano H (1986) The role of Apanteles glomeratus venom in the defensive response of its host, Pieirs rapae crucivora. Journal of Insect Physiology. 32p. 369-375.
    • (1986) Journal of Insect Physiology , pp. 369-375
    • Kitano, H.1
  • 44
    • 0013388723 scopus 로고
    • Resistance of Apanteles eggs to the haemocytic encapsulation by their habitual host, Pieris
    • Kitano H, Nakatsuji N (1978) Resistance of Apanteles eggs to the haemocytic encapsulation by their habitual host, Pieris. Journal of Insect Physiology. 24p. 261-271.
    • (1978) Journal of Insect Physiology , pp. 261-271
    • Kitano, H.1    Nakatsuji, N.2
  • 45
    • 0036098832 scopus 로고    scopus 로고
    • Detailed characterization of polydnavirus immunoevasive proteins in an endoparasitoid wasp
    • Tanaka K, Matsumoto H, Hayakawa Y (2002) Detailed characterization of polydnavirus immunoevasive proteins in an endoparasitoid wasp. Eur J Biochem. 269(10)p. 2557-66.
    • (2002) Eur J Biochem , vol.269 , Issue.10 , pp. 2557-2566
    • Tanaka, K.1    Matsumoto, H.2    Hayakawa, Y.3
  • 46
    • 33746211231 scopus 로고    scopus 로고
    • A calreticulin-like protein from endoparasitoid venom fluid is involved in host hemocyte inactivation
    • Zhang G, Schmidt O, Asgari S (2006) A calreticulin-like protein from endoparasitoid venom fluid is involved in host hemocyte inactivation. Dev Comp Immunol. 30(9)p. 756-64.
    • (2006) Dev Comp Immunol , vol.30 , Issue.9 , pp. 756-764
    • Zhang, G.1    Schmidt, O.2    Asgari, S.3
  • 47
    • 0029860741 scopus 로고    scopus 로고
    • Host haemocyte inactivation by an insect parasitoid: Transient expression of a polydnavirus gene
    • Asgari S, Hellers M, Schmidt O (1996) Host haemocyte inactivation by an insect parasitoid: transient expression of a polydnavirus gene. J Gen Virol. 77 (Pt 10)p. 2653-62.
    • (1996) J Gen Virol , vol.77 , Issue.Pt 10 , pp. 2653-2662
    • Asgari, S.1    Hellers, M.2    Schmidt, O.3
  • 48
    • 0141993544 scopus 로고    scopus 로고
    • A serine proteinase homolog venom protein from an endoparasitoid wasp inhibits melanization of the host hemolymph
    • Asgari S, Zhang G, Zareie R, Schmidt O (2003) A serine proteinase homolog venom protein from an endoparasitoid wasp inhibits melanization of the host hemolymph. Insect Biochem Mol Biol. 33(10)p. 1017-24.
    • (2003) Insect Biochem Mol Biol , vol.33 , Issue.10 , pp. 1017-1024
    • Asgari, S.1    Zhang, G.2    Zareie, R.3    Schmidt, O.4
  • 49
    • 0037827753 scopus 로고    scopus 로고
    • Characterization of a novel protein with homology to C-type lectins expressed by the Cotesia rubecula bracovirus in larvae of the lepidopteran host, Pieris rapae
    • Glatz R, Schmidt O, Asgari S (2003) Characterization of a novel protein with homology to C-type lectins expressed by the Cotesia rubecula bracovirus in larvae of the lepidopteran host, Pieris rapae. J Biol Chem. 278(22)p. 19743-50.
    • (2003) J Biol Chem , vol.278 , Issue.22 , pp. 19743-19750
    • Glatz, R.1    Schmidt, O.2    Asgari, S.3
  • 50
    • 1942438639 scopus 로고    scopus 로고
    • Negative regulation of prophenoloxidase (proPO) activation by a clip-domain serine proteinase homolog (SPH) from endoparasitoid venom
    • Zhang G, Lu ZQ, Jiang H, Asgari S (2004) Negative regulation of prophenoloxidase (proPO) activation by a clip-domain serine proteinase homolog (SPH) from endoparasitoid venom. Insect Biochem Mol Biol. 34(5)p. 477-83.
    • (2004) Insect Biochem Mol Biol , vol.34 , Issue.5 , pp. 477-483
    • Zhang, G.1    Lu, Z.Q.2    Jiang, H.3    Asgari, S.4
  • 51
    • 12544252114 scopus 로고    scopus 로고
    • Mechanism of reduction in the number of the circulating hemocytes in the Pseudaletia separata host parasitized by Cotesia kariyai
    • Teramoto T, Tanaka T (2004) Mechanism of reduction in the number of the circulating hemocytes in the Pseudaletia separata host parasitized by Cotesia kariyai. J Insect Physiol. 50(12)p. 1103-11.
    • (2004) J Insect Physiol , vol.50 , Issue.12 , pp. 1103-1111
    • Teramoto, T.1    Tanaka, T.2
  • 52
    • 0028430582 scopus 로고
    • Expression of polydnavirus genes from the parasitoid wasp Cotesia kariyai in two noctuid hosts
    • Hayakawa Y, Yazaki K, Yamanaka A, Tanaka T (1994) Expression of polydnavirus genes from the parasitoid wasp Cotesia kariyai in two noctuid hosts. Insect Mol Biol. 3(2)p. 97-103.
    • (1994) Insect Mol Biol , vol.3 , Issue.2 , pp. 97-103
    • Hayakawa, Y.1    Yazaki, K.2    Yamanaka, A.3    Tanaka, T.4
  • 53
    • 0032005367 scopus 로고    scopus 로고
    • Role of the prophenoloxidase-activating system in invertebrate immunity
    • Soderhall K, Cerenius L (1998) Role of the prophenoloxidase-activating system in invertebrate immunity. Curr Opin Immunol. 10(1)p. 23-8.
    • (1998) Curr Opin Immunol , vol.10 , Issue.1 , pp. 23-28
    • Soderhall, K.1    Cerenius, L.2
  • 54
    • 44649197623 scopus 로고    scopus 로고
    • The proPO-system: Pros and cons for its role in invertebrate immunity
    • Cerenius L, Lee BL, Soderhall K (2008) The proPO-system: pros and cons for its role in invertebrate immunity. Trends Immunol. 29(6)p. 263-71.
    • (2008) Trends Immunol , vol.29 , Issue.6 , pp. 263-271
    • Cerenius, L.1    Lee, B.L.2    Soderhall, K.3
  • 55
    • 40549103093 scopus 로고    scopus 로고
    • CLIP-domain serine proteases in Drosophila innate immunity
    • Jang IH, Nam HJ, Lee WJ (2008) CLIP-domain serine proteases in Drosophila innate immunity. BMB Rep. 41(2)p. 102-7.
    • (2008) BMB Rep , vol.41 , Issue.2 , pp. 102-107
    • Jang, I.H.1    Nam, H.J.2    Lee, W.J.3
  • 56
    • 54449085542 scopus 로고    scopus 로고
    • Molecular control of phenoloxidase-induced melanin synthesis in an insect
    • Kan H, Kim CH, Kwon HM, Park JW, Roh KB, et al. (2008) Molecular control of phenoloxidase-induced melanin synthesis in an insect. J Biol Chem. 283(37)p. 25316-23.
    • (2008) J Biol Chem , vol.283 , Issue.37 , pp. 25316-25323
    • Kan, H.1    Kim, C.H.2    Kwon, H.M.3    Park, J.W.4    Roh, K.B.5
  • 57
    • 0033065143 scopus 로고    scopus 로고
    • The roles of Sarcophaga defense molecules in immunity and metamorphosis
    • Natori S, Shiraishi H, Hori S, Kobayashi A (1999) The roles of Sarcophaga defense molecules in immunity and metamorphosis. Dev Comp Immunol. 23(4-5)p. 317-28.
    • (1999) Dev Comp Immunol , vol.23 , Issue.4-5 , pp. 317-328
    • Natori, S.1    Shiraishi, H.2    Hori, S.3    Kobayashi, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.