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Volumn 30, Issue 6, 2006, Pages 545-556

Discovery of immune-related genes expressed in hemocytes of the tarantula spider Acanthoscurria gomesiana

Author keywords

Antimicrobial peptides; Coagulation; Expressed sequence tags (ESTs); Hemocyanin; Hemocytes; Innate immunity; Lectins; Serine proteases

Indexed keywords

COMPLEMENTARY DNA; HEMOCYANIN; LECTIN;

EID: 33644805393     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2005.09.001     Document Type: Article
Times cited : (19)

References (52)
  • 2
    • 0031934614 scopus 로고    scopus 로고
    • New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions
    • S. Iwanaga, S. Kawabata, and T. Muta New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions J Biochem (Tokyo) 123 1 1998 1 15
    • (1998) J Biochem (Tokyo) , vol.123 , Issue.1 , pp. 1-15
    • Iwanaga, S.1    Kawabata, S.2    Muta, T.3
  • 3
    • 20444506858 scopus 로고    scopus 로고
    • Recent advances in the innate immunity of invertebrate animals
    • S. Iwanaga, and B.L. Lee Recent advances in the innate immunity of invertebrate animals J Biochem Mol Biol 38 2 2005 128 150
    • (2005) J Biochem Mol Biol , vol.38 , Issue.2 , pp. 128-150
    • Iwanaga, S.1    Lee, B.L.2
  • 4
    • 1642463826 scopus 로고    scopus 로고
    • The prophenoloxidase-activating system in invertebrates
    • L. Cerenius, and K. Soderhall The prophenoloxidase-activating system in invertebrates Immunol Rev 198 2004 116 126
    • (2004) Immunol Rev , vol.198 , pp. 116-126
    • Cerenius, L.1    Soderhall, K.2
  • 5
    • 1642422727 scopus 로고    scopus 로고
    • Insights into the anti-microbial defense of marine invertebrates: The penaeid shrimps and the oyster Crassostrea gigas
    • E. Bachere, Y. Gueguen, M. Gonzalez, J. de Lorgeril, J. Garnier, and B. Romestand Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Crassostrea gigas Immunol Rev 198 1 2004 149 168
    • (2004) Immunol Rev , vol.198 , Issue.1 , pp. 149-168
    • Bachere, E.1    Gueguen, Y.2    Gonzalez, M.3    De Lorgeril, J.4    Garnier, J.5    Romestand, B.6
  • 6
    • 0034721871 scopus 로고    scopus 로고
    • Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family
    • P.I. Silva Jr, S. Daffre, and P. Bulet Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family J Biol Chem 275 43 2000 33464 33470
    • (2000) J Biol Chem , vol.275 , Issue.43 , pp. 33464-33470
    • Silva Jr., P.I.1    Daffre, S.2    Bulet, P.3
  • 7
    • 0141993540 scopus 로고    scopus 로고
    • Molecular cloning, expression analysis and cellular localization of gomesin, an anti-microbial peptide from hemocytes of the spider Acanthoscurria gomesiana
    • D.M. Lorenzini, A.H. Fukuzawa, P.I. da Silva Jr, G. Machado-Santelli, A.T. Bijovsky, and S. Daffre Molecular cloning, expression analysis and cellular localization of gomesin, an anti-microbial peptide from hemocytes of the spider Acanthoscurria gomesiana Insect Biochem Mol Biol 33 10 2003 1011 1016
    • (2003) Insect Biochem Mol Biol , vol.33 , Issue.10 , pp. 1011-1016
    • Lorenzini, D.M.1    Fukuzawa, A.H.2    Da Silva Jr., P.I.3    Machado-Santelli, G.4    Bijovsky, A.T.5    Daffre, S.6
  • 8
    • 0038460892 scopus 로고    scopus 로고
    • Acanthoscurrin: A novel glycine-rich antimicrobial peptide constitutively expressed in the hemocytes of the spider Acanthoscurria gomesiana
    • D.M. Lorenzini, P.I. da Silva Jr, A.C. Fogaca, P. Bulet, and S. Daffre Acanthoscurrin: a novel glycine-rich antimicrobial peptide constitutively expressed in the hemocytes of the spider Acanthoscurria gomesiana Dev Comp Immunol 27 9 2003 781 791
    • (2003) Dev Comp Immunol , vol.27 , Issue.9 , pp. 781-791
    • Lorenzini, D.M.1    Da Silva Jr., P.I.2    Fogaca, A.C.3    Bulet, P.4    Daffre, S.5
  • 11
    • 0034927549 scopus 로고    scopus 로고
    • Immune gene discovery by expressed sequence tag analysis of hemocytes and hepatopancreas in the Pacific White Shrimp, Litopenaeus vannamei, and the Atlantic White Shrimp, L. setiferus
    • P.S. Gross, T.C. Bartlett, C.L. Browdy, R.W. Chapman, and G.W. Warr Immune gene discovery by expressed sequence tag analysis of hemocytes and hepatopancreas in the Pacific White Shrimp, Litopenaeus vannamei, and the Atlantic White Shrimp, L. setiferus Dev Comp Immunol 25 7 2001 565 577
    • (2001) Dev Comp Immunol , vol.25 , Issue.7 , pp. 565-577
    • Gross, P.S.1    Bartlett, T.C.2    Browdy, C.L.3    Chapman, R.W.4    Warr, G.W.5
  • 12
    • 0036202550 scopus 로고    scopus 로고
    • Potential indicators of stress response identified by expressed sequence tag analysis of hemocytes and embryos from the American oyster, Crassostrea virginica
    • M.J. Jenny, A.H. Ringwood, E.R. Lacy, A.J. Lewitus, J.W. Kempton, and P.S. Gross Potential indicators of stress response identified by expressed sequence tag analysis of hemocytes and embryos from the American oyster, Crassostrea virginica Mar Biotechnol (NY) 4 1 2002 81 93
    • (2002) Mar Biotechnol (NY) , vol.4 , Issue.1 , pp. 81-93
    • Jenny, M.J.1    Ringwood, A.H.2    Lacy, E.R.3    Lewitus, A.J.4    Kempton, J.W.5    Gross, P.S.6
  • 13
    • 0037330033 scopus 로고    scopus 로고
    • Comparative gene analysis of Biomphalaria glabrata hemocytes pre- and post-exposure to miracidia of Schistosoma mansoni
    • N. Raghavan, A.N. Miller, M. Gardner, P.C. FitzGerald, A.R. Kerlavage, and D.A. Johnston Comparative gene analysis of Biomphalaria glabrata hemocytes pre- and post-exposure to miracidia of Schistosoma mansoni Mol Biochem Parasitol 126 2 2003 181 191
    • (2003) Mol Biochem Parasitol , vol.126 , Issue.2 , pp. 181-191
    • Raghavan, N.1    Miller, A.N.2    Gardner, M.3    Fitzgerald, P.C.4    Kerlavage, A.R.5    Johnston, D.A.6
  • 14
    • 12944263712 scopus 로고    scopus 로고
    • Anopheles gambiae pilot gene discovery project: Identification of mosquito innate immunity genes from expressed sequence tags generated from immune-competent cell lines
    • G. Dimopoulos, T.L. Casavant, S. Chang, T. Scheetz, C. Roberts, and M. Donohue Anopheles gambiae pilot gene discovery project: identification of mosquito innate immunity genes from expressed sequence tags generated from immune-competent cell lines Proc Natl Acad Sci USA 97 12 2000 6619 6624
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.12 , pp. 6619-6624
    • Dimopoulos, G.1    Casavant, T.L.2    Chang, S.3    Scheetz, T.4    Roberts, C.5    Donohue, M.6
  • 15
    • 0037173047 scopus 로고    scopus 로고
    • Genome expression analysis of Anopheles gambiae: Responses to injury, bacterial challenge, and malaria infection
    • G. Dimopoulos, G.K. Christophides, S. Meister, J. Schultz, K.P. White, and C. Barillas-Mury Genome expression analysis of Anopheles gambiae: responses to injury, bacterial challenge, and malaria infection Proc Natl Acad Sci USA 99 13 2002 8814 8819
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.13 , pp. 8814-8819
    • Dimopoulos, G.1    Christophides, G.K.2    Meister, S.3    Schultz, J.4    White, K.P.5    Barillas-Mury, C.6
  • 16
    • 0345051044 scopus 로고    scopus 로고
    • Normalization and subtraction: Two approaches to facilitate gene discovery
    • M.F. Bonaldo, G. Lennon, and M.B. Soares Normalization and subtraction: two approaches to facilitate gene discovery Genome Res 6 9 1996 791 806
    • (1996) Genome Res , vol.6 , Issue.9 , pp. 791-806
    • Bonaldo, M.F.1    Lennon, G.2    Soares, M.B.3
  • 17
    • 0036467504 scopus 로고    scopus 로고
    • The molecular basis of innate immunity in the horseshoe crab
    • S. Iwanaga The molecular basis of innate immunity in the horseshoe crab Curr Opin Immunol 14 1 2002 87 95
    • (2002) Curr Opin Immunol , vol.14 , Issue.1 , pp. 87-95
    • Iwanaga, S.1
  • 20
    • 0036230465 scopus 로고    scopus 로고
    • Annotated expressed sequence tags and cDNA microarrays for studies of brain and behavior in the honey bee
    • C.W. Whitfield, M.R. Band, M.F. Bonaldo, C.G. Kumar, L. Liu, and J.R. Pardinas Annotated expressed sequence tags and cDNA microarrays for studies of brain and behavior in the honey bee Genome Res 12 4 2002 555 566
    • (2002) Genome Res , vol.12 , Issue.4 , pp. 555-566
    • Whitfield, C.W.1    Band, M.R.2    Bonaldo, M.F.3    Kumar, C.G.4    Liu, L.5    Pardinas, J.R.6
  • 21
    • 0034671529 scopus 로고    scopus 로고
    • Complete sequence of the 24-mer hemocyanin of the tarantula Eurypelma californicum. Structure and intramolecular evolution of the subunits
    • R. Voit, G. Feldmaier-Fuchs, T. Schweikardt, H. Decker, and T. Burmester Complete sequence of the 24-mer hemocyanin of the tarantula Eurypelma californicum. Structure and intramolecular evolution of the subunits J Biol Chem 275 50 2000 39339 39344
    • (2000) J Biol Chem , vol.275 , Issue.50 , pp. 39339-39344
    • Voit, R.1    Feldmaier-Fuchs, G.2    Schweikardt, T.3    Decker, H.4    Burmester, T.5
  • 22
    • 1242343403 scopus 로고    scopus 로고
    • Recent findings on phenoloxidase activity and antimicrobial activity of hemocyanins
    • H. Decker, and E. Jaenicke Recent findings on phenoloxidase activity and antimicrobial activity of hemocyanins Dev Comp Immunol 28 7-8 2004 673 687
    • (2004) Dev Comp Immunol , vol.28 , Issue.7-8 , pp. 673-687
    • Decker, H.1    Jaenicke, E.2
  • 23
    • 0032476016 scopus 로고    scopus 로고
    • Tarantula hemocyanin shows phenoloxidase activity
    • H. Decker, and T. Rimke Tarantula hemocyanin shows phenoloxidase activity J Biol Chem 273 40 1998 25889 25892
    • (1998) J Biol Chem , vol.273 , Issue.40 , pp. 25889-25892
    • Decker, H.1    Rimke, T.2
  • 24
    • 0034703094 scopus 로고    scopus 로고
    • A link between blood coagulation and prophenol oxidase activation in arthropod host defense
    • T. Nagai, and S. Kawabata A link between blood coagulation and prophenol oxidase activation in arthropod host defense J Biol Chem 275 38 2000 29264 29267
    • (2000) J Biol Chem , vol.275 , Issue.38 , pp. 29264-29267
    • Nagai, T.1    Kawabata, S.2
  • 25
    • 0035920142 scopus 로고    scopus 로고
    • Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides
    • T. Nagai, T. Osaki, and S. Kawabata Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides J Biol Chem 276 29 2001 27166 27170
    • (2001) J Biol Chem , vol.276 , Issue.29 , pp. 27166-27170
    • Nagai, T.1    Osaki, T.2    Kawabata, S.3
  • 26
    • 0036178451 scopus 로고    scopus 로고
    • The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider
    • N. Mandard, P. Bulet, A. Caille, S. Daffre, and F. Vovelle The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider Eur J Biochem 269 4 2002 1190 1198
    • (2002) Eur J Biochem , vol.269 , Issue.4 , pp. 1190-1198
    • Mandard, N.1    Bulet, P.2    Caille, A.3    Daffre, S.4    Vovelle, F.5
  • 27
    • 33644793901 scopus 로고    scopus 로고
    • Alanine series of the antimicrobial peptide gomesin: A structure-activity relationship study
    • A. Miranda, M.A. Fázio, M.T.M. Miranda, S. Daffre, and W.T. Lamas Alanine series of the antimicrobial peptide gomesin: a structure-activity relationship study J Pep Sci Suppl 10 2004 179
    • (2004) J Pep Sci , Issue.10 SUPPL. , pp. 179
    • Miranda, A.1    Fázio, M.A.2    Miranda, M.T.M.3    Daffre, S.4    Lamas, W.T.5
  • 28
    • 0036630804 scopus 로고    scopus 로고
    • Gene expression in haemocytes of kuruma prawn, Penaeus japonicus, in response to infection with WSSV by EST approach
    • J. Rojtinnakorn, I. Hirono, T. Itami, Y. Takahashi, and T. Aoki Gene expression in haemocytes of kuruma prawn, Penaeus japonicus, in response to infection with WSSV by EST approach Fish Shellfish Immunol 13 1 2002 69 83
    • (2002) Fish Shellfish Immunol , vol.13 , Issue.1 , pp. 69-83
    • Rojtinnakorn, J.1    Hirono, I.2    Itami, T.3    Takahashi, Y.4    Aoki, T.5
  • 29
    • 8744288933 scopus 로고    scopus 로고
    • Immune-responsive lysozymes from hemocytes of the American dog tick, Dermacentor variabilis and an embryonic cell line of the Rocky Mountain wood tick, D. andersoni
    • J.A. Simser, K.R. Macaluso, A. Mulenga, and A.F. Azad Immune-responsive lysozymes from hemocytes of the American dog tick, Dermacentor variabilis and an embryonic cell line of the Rocky Mountain wood tick, D. andersoni Insect Biochem Mol Biol 34 12 2004 1235 1246
    • (2004) Insect Biochem Mol Biol , vol.34 , Issue.12 , pp. 1235-1246
    • Simser, J.A.1    MacAluso, K.R.2    Mulenga, A.3    Azad, A.F.4
  • 30
    • 0037443403 scopus 로고    scopus 로고
    • Increased inflammation in lysozyme M-deficient mice in response to Micrococcus luteus and its peptidoglycan
    • T. Ganz, V. Gabayan, H.I. Liao, L. Liu, A. Oren, and T. Graf Increased inflammation in lysozyme M-deficient mice in response to Micrococcus luteus and its peptidoglycan Blood 101 6 2003 2388 2392
    • (2003) Blood , vol.101 , Issue.6 , pp. 2388-2392
    • Ganz, T.1    Gabayan, V.2    Liao, H.I.3    Liu, L.4    Oren, A.5    Graf, T.6
  • 31
    • 0033953792 scopus 로고    scopus 로고
    • The clip-domain family of serine proteinases in arthropods
    • H. Jiang, and M.R. Kanost The clip-domain family of serine proteinases in arthropods Insect Biochem Mol Biol 30 2 2000 95 105
    • (2000) Insect Biochem Mol Biol , vol.30 , Issue.2 , pp. 95-105
    • Jiang, H.1    Kanost, M.R.2
  • 32
    • 0037025213 scopus 로고    scopus 로고
    • Activation of Drosophila toll during fungal infection by a blood serine protease
    • P. Ligoxygakis, N. Pelte, J.A. Hoffmann, and J.M. Reichhart Activation of Drosophila toll during fungal infection by a blood serine protease Science 297 5578 2002 114 116
    • (2002) Science , vol.297 , Issue.5578 , pp. 114-116
    • Ligoxygakis, P.1    Pelte, N.2    Hoffmann, J.A.3    Reichhart, J.M.4
  • 33
    • 0742305683 scopus 로고    scopus 로고
    • A serine protease zymogen functions as a pattern-recognition receptor for lipopolysaccharides
    • S. Ariki, K. Koori, T. Osaki, K. Motoyama, K. Inamori, and S. Kawabata A serine protease zymogen functions as a pattern-recognition receptor for lipopolysaccharides Proc Natl Acad Sci USA 101 4 2004 953 958
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.4 , pp. 953-958
    • Ariki, S.1    Koori, K.2    Osaki, T.3    Motoyama, K.4    Inamori, K.5    Kawabata, S.6
  • 34
    • 0033813364 scopus 로고    scopus 로고
    • Definition of endotoxin binding sites in horseshoe crab factor C recombinant sushi proteins and neutralization of endotoxin by sushi peptides
    • N.S. Tan, M.L. Ng, Y.H. Yau, P.K. Chong, B. Ho, and J.L. Ding Definition of endotoxin binding sites in horseshoe crab factor C recombinant sushi proteins and neutralization of endotoxin by sushi peptides Faseb J 14 12 2000 1801 1813
    • (2000) Faseb J , vol.14 , Issue.12 , pp. 1801-1813
    • Tan, N.S.1    Ng, M.L.2    Yau, Y.H.3    Chong, P.K.4    Ho, B.5    Ding, J.L.6
  • 35
    • 1642463804 scopus 로고    scopus 로고
    • The lectin-complement pathway-its role in innate immunity and evolution
    • T. Fujita, M. Matsushita, and Y. Endo The lectin-complement pathway-its role in innate immunity and evolution Immunol Rev 198 2004 185 202
    • (2004) Immunol Rev , vol.198 , pp. 185-202
    • Fujita, T.1    Matsushita, M.2    Endo, Y.3
  • 36
    • 0035831034 scopus 로고    scopus 로고
    • Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae
    • E.A. Levashina, L.F. Moita, S. Blandin, G. Vriend, M. Lagueux, and F.C. Kafatos Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae Cell 104 5 2001 709 718
    • (2001) Cell , vol.104 , Issue.5 , pp. 709-718
    • Levashina, E.A.1    Moita, L.F.2    Blandin, S.3    Vriend, G.4    Lagueux, M.5    Kafatos, F.C.6
  • 37
    • 0028979353 scopus 로고
    • Alpha 2-macroglobulin-mediated clearance of proteases from the plasma of the American horseshoe crab, Limulus polyphemus
    • R. Melchior, J.P. Quigley, and P.B. Armstrong Alpha 2-macroglobulin- mediated clearance of proteases from the plasma of the American horseshoe crab, Limulus polyphemus J Biol Chem 270 22 1995 13496 13502
    • (1995) J Biol Chem , vol.270 , Issue.22 , pp. 13496-13502
    • Melchior, R.1    Quigley, J.P.2    Armstrong, P.B.3
  • 38
    • 0037136419 scopus 로고    scopus 로고
    • Animal lectins: A historical introduction and overview
    • D.C. Kilpatrick Animal lectins: a historical introduction and overview Biochim Biophys Acta 1572 2-3 2002 187 197
    • (2002) Biochim Biophys Acta , vol.1572 , Issue.2-3 , pp. 187-197
    • Kilpatrick, D.C.1
  • 39
    • 0032994092 scopus 로고    scopus 로고
    • Immune proteins and their gene expression in the silkworm, Bombyx mori
    • M. Yamakawa, and H. Tanaka Immune proteins and their gene expression in the silkworm, Bombyx mori Dev Comp Immunol 23 4-5 1999 281 289
    • (1999) Dev Comp Immunol , vol.23 , Issue.4-5 , pp. 281-289
    • Yamakawa, M.1    Tanaka, H.2
  • 40
    • 4243869181 scopus 로고    scopus 로고
    • Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen
    • S. Gokudan, T. Muta, R. Tsuda, K. Koori, T. Kawahara, and N. Seki Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen Proc Natl Acad Sci USA 96 18 1999 10086 10091
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.18 , pp. 10086-10091
    • Gokudan, S.1    Muta, T.2    Tsuda, R.3    Koori, K.4    Kawahara, T.5    Seki, N.6
  • 41
    • 0032102107 scopus 로고    scopus 로고
    • Sialic-acid-binding lectin from the slug Limax flavus - Cloning, expression of the polypeptide, and tissue localization
    • S. Kurachi, Z. Song, M. Takagaki, Q. Yang, H.C. Winter, and K. Kurachi Sialic-acid-binding lectin from the slug Limax flavus - cloning, expression of the polypeptide, and tissue localization Eur J Biochem 254 2 1998 217 222
    • (1998) Eur J Biochem , vol.254 , Issue.2 , pp. 217-222
    • Kurachi, S.1    Song, Z.2    Takagaki, M.3    Yang, Q.4    Winter, H.C.5    Kurachi, K.6
  • 42
    • 0030831258 scopus 로고    scopus 로고
    • A family of fibrinogen-related proteins that precipitates parasite-derived molecules is produced by an invertebrate after infection
    • C.M. Adema, L.A. Hertel, R.D. Miller, and E.S. Loker A family of fibrinogen-related proteins that precipitates parasite-derived molecules is produced by an invertebrate after infection Proc Natl Acad Sci USA 94 16 1997 8691 8696
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.16 , pp. 8691-8696
    • Adema, C.M.1    Hertel, L.A.2    Miller, R.D.3    Loker, E.S.4
  • 43
    • 0037061482 scopus 로고    scopus 로고
    • Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli
    • M. Ramet, P. Manfruelli, A. Pearson, B. Mathey-Prevot, and R.A. Ezekowitz Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli Nature 416 6881 2002 644 648
    • (2002) Nature , vol.416 , Issue.6881 , pp. 644-648
    • Ramet, M.1    Manfruelli, P.2    Pearson, A.3    Mathey-Prevot, B.4    Ezekowitz, R.A.5
  • 44
    • 0035856990 scopus 로고    scopus 로고
    • Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein
    • T. Michel, J.M. Reichhart, J.A. Hoffmann, and J. Royet Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein Nature 414 6865 2001 756 759
    • (2001) Nature , vol.414 , Issue.6865 , pp. 756-759
    • Michel, T.1    Reichhart, J.M.2    Hoffmann, J.A.3    Royet, J.4
  • 45
    • 0037108754 scopus 로고    scopus 로고
    • Overexpression of a pattern-recognition receptor, peptidoglycan- recognition protein-LE, activates imd/relish-mediated antibacterial defense and the prophenoloxidase cascade in Drosophila larvae
    • A. Takehana, T. Katsuyama, T. Yano, Y. Oshima, H. Takada, and T. Aigaki Overexpression of a pattern-recognition receptor, peptidoglycan-recognition protein-LE, activates imd/relish-mediated antibacterial defense and the prophenoloxidase cascade in Drosophila larvae Proc Natl Acad Sci USA 99 21 2002 13705 13710
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.21 , pp. 13705-13710
    • Takehana, A.1    Katsuyama, T.2    Yano, T.3    Oshima, Y.4    Takada, H.5    Aigaki, T.6
  • 46
    • 0037311545 scopus 로고    scopus 로고
    • Nonproteolytic serine proteinase homologs are involved in prophenoloxidase activation in the tobacco hornworm, Manduca sexta
    • X.Q. Yu, H. Jiang, Y. Wang, and M.R. Kanost Nonproteolytic serine proteinase homologs are involved in prophenoloxidase activation in the tobacco hornworm, Manduca sexta Insect Biochem Mol Biol 33 2 2003 197 208
    • (2003) Insect Biochem Mol Biol , vol.33 , Issue.2 , pp. 197-208
    • Yu, X.Q.1    Jiang, H.2    Wang, Y.3    Kanost, M.R.4
  • 48
    • 0036134963 scopus 로고    scopus 로고
    • Toll-like receptors: How they work and what they do
    • B. Beutler Toll-like receptors: how they work and what they do Curr Opin Hematol 9 1 2002 2 10
    • (2002) Curr Opin Hematol , vol.9 , Issue.1 , pp. 2-10
    • Beutler, B.1
  • 49
    • 0036167107 scopus 로고    scopus 로고
    • Drosophila innate immunity: An evolutionary perspective
    • J.A. Hoffmann, and J.M. Reichhart Drosophila innate immunity: an evolutionary perspective Nat Immunol 3 2 2002 121 126
    • (2002) Nat Immunol , vol.3 , Issue.2 , pp. 121-126
    • Hoffmann, J.A.1    Reichhart, J.M.2
  • 50
    • 0032992545 scopus 로고    scopus 로고
    • Cell adhesion molecules in invertebrate immunity
    • M.W. Johansson Cell adhesion molecules in invertebrate immunity Dev Comp Immunol 23 4-5 1999 303 315
    • (1999) Dev Comp Immunol , vol.23 , Issue.4-5 , pp. 303-315
    • Johansson, M.W.1
  • 51
    • 0033514933 scopus 로고    scopus 로고
    • The crayfish plasma clotting protein: A vitellogenin-related protein responsible for clot formation in crustacean blood
    • M. Hall, R. Wang, R. van Antwerpen, L. Sottrup-Jensen, and K. Soderhall The crayfish plasma clotting protein: a vitellogenin-related protein responsible for clot formation in crustacean blood Proc Natl Acad Sci USA 96 5 1999 1965 1970
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.5 , pp. 1965-1970
    • Hall, M.1    Wang, R.2    Van Antwerpen, R.3    Sottrup-Jensen, L.4    Soderhall, K.5
  • 52
    • 0037131348 scopus 로고    scopus 로고
    • Proline-rich cell surface antigens of horseshoe crab hemocytes are substrates for protein cross-linking with a clotting protein coagulin
    • T. Osaki, N. Okino, F. Tokunaga, S. Iwanaga, and S. Kawabata Proline-rich cell surface antigens of horseshoe crab hemocytes are substrates for protein cross-linking with a clotting protein coagulin J Biol Chem 277 42 2002 40084 40090
    • (2002) J Biol Chem , vol.277 , Issue.42 , pp. 40084-40090
    • Osaki, T.1    Okino, N.2    Tokunaga, F.3    Iwanaga, S.4    Kawabata, S.5


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