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Volumn 288, Issue 20, 2013, Pages 14476-14487

Hemolymph melanization in the silkmoth Bombyx mori involves formation of a high molecular mass complex that metabolizes tyrosin

Author keywords

[No Author keywords available]

Indexed keywords

BOMBYX MORI; COMPLEX FORMATIONS; GEL-FILTRATION CHROMATOGRAPHY; HIGH-MOLECULAR-MASS COMPLEXES; MASS SPECTROMETRY ANALYSIS; PHENOLOXIDASES; PHENYLTHIOUREA; PROTEASE INHIBITOR;

EID: 84877881327     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.459222     Document Type: Article
Times cited : (57)

References (56)
  • 1
    • 44649197623 scopus 로고    scopus 로고
    • The proPO-system. Pros and cons for its role in invertebrate immunity
    • Cerenius, L., Lee, B. L., and Söderhäll, K. (2008) The proPO-system. Pros and cons for its role in invertebrate immunity. Trends Immunol. 29, 263-271
    • (2008) Trends Immunol. , vol.29 , pp. 263-271
    • Cerenius, L.1    Lee, B.L.2    Söderhäll, K.3
  • 2
    • 54849421830 scopus 로고    scopus 로고
    • Phenoloxidases in insect immunity
    • (Beckage, N. E., ed) Academic Press, Inc., San Diego
    • Kanost, M. R., and Gorman, M. J. (2008) Phenoloxidases in insect immunity. in Insect Immunology (Beckage, N. E., ed) pp. 69-96, Academic Press, Inc., San Diego
    • (2008) Insect Immunology , pp. 69-96
    • Kanost, M.R.1    Gorman, M.J.2
  • 3
    • 70349167463 scopus 로고    scopus 로고
    • The role of melanization and cytotoxic by-products in the cellular immune responses of Drosophila against parasitic wasps
    • (Genevieve, P., ed) Academic Press, Inc., San Diego
    • Nappi, A., Poirié, M., and Carton, Y. (2009) The role of melanization and cytotoxic by-products in the cellular immune responses of Drosophila against parasitic wasps. in Advances in Parasitology (Genevieve, P., ed) pp. 99-121, Academic Press, Inc., San Diego
    • (2009) Advances in Parasitology , pp. 99-121
    • Nappi, A.1    Poirié, M.2    Carton, Y.3
  • 4
    • 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, 2-9
    • (2002) Pigment Cell Res. , vol.15 , pp. 2-9
    • Sugumaran, M.1
  • 5
    • 1642463826 scopus 로고    scopus 로고
    • The prophenoloxidase-activating system in invertebrates
    • DOI 10.1111/j.0105-2896.2004.00116.x
    • Cerenius, L., and Söderhäll, K. (2004) The prophenoloxidase- activating system in invertebrates. Immunol. Rev. 198, 116-126 (Pubitemid 38406940)
    • (2004) Immunological Reviews , vol.198 , pp. 116-126
    • Cerenius, L.1    Soderhall, K.2
  • 6
    • 1642504737 scopus 로고    scopus 로고
    • Innate immune responses of a lepidopteran insect, Manduca sexta
    • DOI 10.1111/j.0105-2896.2004.0121.x
    • Kanost, M. R., Jiang, H., and Yu, X. Q. (2004) Innate immune responses of a lepidopteran insect, Manduca sexta. Immunol. Rev. 198, 97-105 (Pubitemid 38406938)
    • (2004) Immunological Reviews , vol.198 , pp. 97-105
    • Kanost, M.R.1    Jiang, H.2    Yu, X.-Q.3
  • 7
    • 77953138095 scopus 로고    scopus 로고
    • Regulation of melanization by glutathione in the moth Pseudoplusia includens
    • Clark, K. D., Lu, Z., and Strand, M. R. (2010) Regulation of melanization by glutathione in the moth Pseudoplusia includens. Insect Biochem. Mol. Biol. 40, 460-467
    • (2010) Insect Biochem. Mol. Biol. , vol.40 , pp. 460-467
    • Clark, K.D.1    Lu, Z.2    Strand, M.R.3
  • 8
    • 79959494955 scopus 로고    scopus 로고
    • Polydnaviruses
    • (Asgari, S., and Johnson, K., eds) Caister Academic Press, Norfolk, UK
    • Strand, M. R. (2010) Polydnaviruses. in Insect Virology (Asgari, S., and Johnson, K., eds) pp. 171-198, Caister Academic Press, Norfolk, UK
    • (2010) Insect Virology , pp. 171-198
    • Strand, M.R.1
  • 9
    • 37649008221 scopus 로고    scopus 로고
    • A novel polydnavirus protein inhibits the insect prophenoloxidase activation pathway
    • Beck, M. H., and Strand, M. R. (2007) A novel polydnavirus protein inhibits the insect prophenoloxidase activation pathway. Proc. Natl. Acad. Sci. U.S.A. 104, 19267-19272
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 19267-19272
    • Beck, M.H.1    Strand, M.R.2
  • 10
    • 52049086920 scopus 로고    scopus 로고
    • The viral protein Egf1.0 is a dual activity inhibitor of prophenoloxidase-activating proteinases 1 and 3 from Manduca sexta
    • Lu, Z., Beck, M. H., Wang, Y., Jiang, H., and Strand, M. R. (2008) The viral protein Egf1.0 is a dual activity inhibitor of prophenoloxidase-activating proteinases 1 and 3 from Manduca sexta. J. Biol. Chem. 283, 21325-21333
    • (2008) J. Biol. Chem. , vol.283 , pp. 21325-21333
    • Lu, Z.1    Beck, M.H.2    Wang, Y.3    Jiang, H.4    Strand, M.R.5
  • 11
    • 77953916901 scopus 로고    scopus 로고
    • Egf1.5 is a second phenoloxidase cascade inhibitor encoded by Microplitis demolitor bracovirus
    • Lu, Z., Beck, M. H., and Strand, M. R. (2010) Egf1.5 is a second phenoloxidase cascade inhibitor encoded by Microplitis demolitor bracovirus. Insect Biochem. Mol. Biol. 40, 497-505
    • (2010) Insect Biochem. Mol. Biol. , vol.40 , pp. 497-505
    • Lu, Z.1    Beck, M.H.2    Strand, M.R.3
  • 12
    • 15944404330 scopus 로고    scopus 로고
    • Melanogenesis and associated cytotoxic reactions: Applications to insect innate immunity
    • DOI 10.1016/j.ibmb.2005.01.014
    • Nappi, A. J., and Christensen, B. M. (2005) Melanogenesis and associated cytotoxic reactions. Applications to insect innate immunity. Insect Biochem. Mol. Biol. 35, 443-459 (Pubitemid 40440937)
    • (2005) Insect Biochemistry and Molecular Biology , vol.35 , Issue.5 , pp. 443-459
    • Nappi, A.J.1    Christensen, B.M.2
  • 13
    • 70350135449 scopus 로고    scopus 로고
    • Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymes
    • Li, Y., Wang, Y., Jiang, H., and Deng, J. (2009) Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymes. Proc. Natl. Acad. Sci. U.S.A. 106, 17002-17006
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 17002-17006
    • Li, Y.1    Wang, Y.2    Jiang, H.3    Deng, J.4
  • 14
    • 79953143032 scopus 로고    scopus 로고
    • Melanization in living organisms: A perspective of species evolution
    • Vavricka, C. J., Christensen, B. M., and Li, J. (2010) Melanization in living organisms: a perspective of species evolution. Protein Cell 1, 830-841
    • (2010) Protein Cell , vol.1 , pp. 830-841
    • Vavricka, C.J.1    Christensen, B.M.2    Li, J.3
  • 15
    • 0029112663 scopus 로고
    • Proenzyme of Manduca sexta phenol oxidase. Purification, activation, substrate specificity of the active enzyme, and molecular cloning
    • Hall, M., Scott, T., Sugumaran, M., Söderhäll, K., and Law, J. H. (1995) Proenzyme of Manduca sexta phenol oxidase. Purification, activation, substrate specificity of the active enzyme, and molecular cloning. Proc. Natl. Acad. Sci. U.S.A. 92, 7764-7768
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7764-7768
    • Hall, M.1    Scott, T.2    Sugumaran, M.3    Söderhäll, K.4    Law, J.H.5
  • 16
    • 0001592687 scopus 로고
    • Activation of pro-phenoloxidase by the activating enzyme of the silkworm, Bombyx mori
    • Ashida, M., and Dohke, K. (1980) Activation of pro-phenoloxidase by the activating enzyme of the silkworm, Bombyx mori. Insect Biochem. 10, 37-47
    • (1980) Insect Biochem. , vol.10 , pp. 37-47
    • Ashida, M.1    Dohke, K.2
  • 17
    • 0002657568 scopus 로고
    • Characterization of haemolymph protyrosinase and a cuticular activator from Manduca sexta (L.)
    • Aso, Y., Kramer, K. J., Hopkins, T. L., and Lookhart, G. L. (1985) Characterization of haemolymph protyrosinase and a cuticular activator from Manduca sexta (L.). Insect Biochem. 15, 9-17
    • (1985) Insect Biochem. , vol.15 , pp. 9-17
    • Aso, Y.1    Kramer, K.J.2    Hopkins, T.L.3    Lookhart, G.L.4
  • 18
    • 0033816833 scopus 로고    scopus 로고
    • Purification, characterization and molecular cloning of prophenoloxidases from Sarcophaga bullata
    • Chase, M. R., Raina, K., Bruno, J., and Sugumaran, M. (2000) Purification, characterization and molecular cloning of prophenoloxidases from Sarcophaga bullata. Insect Biochem. Mol. Biol. 30, 953-967
    • (2000) Insect Biochem. Mol. Biol. , vol.30 , pp. 953-967
    • Chase, M.R.1    Raina, K.2    Bruno, J.3    Sugumaran, M.4
  • 19
    • 0025042489 scopus 로고
    • High-pressure liquid chromatographic analysis of hemolymph plasma catecholamines in immune-reactive Aedes aegypti
    • DOI 10.1016/0022-2011(90)90110-R
    • Munkirs, D. D., Christensen, B. M., and Tracy, J. W. (1990) High-pressure liquid chromatographic analysis of hemolymph plasma catecholamines in immune-reactive Aedes aegypti. J. Invertebr. Pathol. 56, 267-279 (Pubitemid 20291309)
    • (1990) Journal of Invertebrate Pathology , vol.56 , Issue.2 , pp. 267-279
    • Munkirs, D.D.1    Christensen, B.M.2    Tracy, J.W.3
  • 20
    • 0000577229 scopus 로고
    • Catecholamines in haemolymph and cuticle during larval, pupal and adult development of Manduca sexta (L.)
    • Hopkins, T. L., Morgan, T. D., and Kramer, K. J. (1984) Catecholamines in haemolymph and cuticle during larval, pupal and adult development of Manduca sexta (L.). Insect Biochem. 14, 533-540
    • (1984) Insect Biochem. , vol.14 , pp. 533-540
    • Hopkins, T.L.1    Morgan, T.D.2    Kramer, K.J.3
  • 21
    • 0000040748 scopus 로고    scopus 로고
    • Tyrosine and catecholamine levels in the hemolymph of tobacco hornworm larvae, Manduca sexta, parasitized by the braconid wasp, Cotesia congregata, and in the developing parasitoids
    • Hopkins, T. L., Starkey, S. R., and Beckage, N. E. (1998) Tyrosine and catecholamine levels in the hemolymph of tobacco hornworm larvae, Manduca sexta, parasitized by the braconid wasp, Cotesia congregata, and in the developing parasitoids. Arch. Insect Biochem. Physiol. 38, 193-201 (Pubitemid 128680423)
    • (1998) Archives of Insect Biochemistry and Physiology , vol.38 , Issue.4 , pp. 193-201
    • Hopkins, T.L.1    Starkey, S.R.2    Beckage, N.E.3
  • 22
    • 0002513065 scopus 로고
    • Limited proteolysis of prophenoloxidase during activation by microbial products in insect plasma and effect of phenoloxidase on electrophoretic mobilities of plasma proteins
    • Ashida, M., and Yoshida, H. (1988) Limited proteolysis of prophenoloxidase during activation by microbial products in insect plasma and effect of phenoloxidase on electrophoretic mobilities of plasma proteins. Insect Biochem. 18, 11-19
    • (1988) Insect Biochem. , vol.18 , pp. 11-19
    • Ashida, M.1    Yoshida, H.2
  • 23
    • 0034661397 scopus 로고    scopus 로고
    • A new mechanism for the control of phenoloxidase activity: Inhibition and complex formation with quinone isomerase
    • DOI 10.1006/abbi.2000.1884
    • Sugumaran, M., Nellaiappan, K., and Valivittan, K. (2000) A new mechanism for the control of phenoloxidase activity. Inhibition and complex formation with quinone isomerase. Arch. Biochem. Biophys. 379, 252-260 (Pubitemid 30637461)
    • (2000) Archives of Biochemistry and Biophysics , vol.379 , Issue.2 , pp. 252-260
    • Sugumaran, M.1    Nellaiappan, K.2    Valivittan, K.3
  • 24
    • 15844393328 scopus 로고    scopus 로고
    • Characterization of a defense complex consisting of interleukin 1 and phenol oxidase from the hemolymph of the tobacco hornworm, Manduca sexta
    • DOI 10.1074/jbc.271.19.11035
    • Beck, G., Cardinale, S., Wang, L., Reiner, M., and Sugumaran, M. (1996) Characterization of a defense complex consisting of interleukin 1 and phenol oxidase from the hemolymph of the tobacco hornworm, Manduca sexta. J. Biol. Chem. 271, 11035-11038 (Pubitemid 26155925)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.19 , pp. 11035-11038
    • Beck, G.1    Cardinale, S.2    Wang, L.3    Reiner, M.4    Sugumaran, M.5
  • 25
    • 0034535375 scopus 로고    scopus 로고
    • Immulectin-2, a lipopolysaccharide-specific lectin from an insect, Manduca sexta, is induced in response to Gram-negative bacteria
    • DOI 10.1074/jbc.M003021200
    • Yu, X.-Q., and Kanost, M. R. (2000) Immulectin-2, a lipopolysaccharide- specific lectin from an insect, Manduca sexta, is induced in response to gram-negative bacteria. J. Biol. Chem. 275, 37373-37381 (Pubitemid 32004840)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.48 , pp. 37373-37381
    • Yu, X.-Q.1    Kanost, M.R.2
  • 26
    • 3242719716 scopus 로고    scopus 로고
    • Prophenoloxidase (proPO) activation in Manduca sexta: An analysis of molecular interactions among proPO, proPO-activating proteinase-3, and a cofactor
    • DOI 10.1016/j.ibmb.2004.03.008, PII S0965174804000487
    • Wang, Y., and Jiang, H. (2004) Prophenoloxidase (proPO) activation in Manduca sexta. An analysis of molecular interactions among proPO, proPO-activating proteinase-3, and a cofactor. Insect Biochem. Mol. Biol. 34, 731-742 (Pubitemid 38946540)
    • (2004) Insect Biochemistry and Molecular Biology , vol.34 , Issue.8 , pp. 731-742
    • Wang, Y.1    Jiang, H.2
  • 28
    • 29244478349 scopus 로고    scopus 로고
    • Crystal structure of a clip-domain serine protease and functional roles of the clip domains
    • DOI 10.1038/sj.emboj.7600891
    • Piao, S., Song, Y.-L., Kim, J. H., Park, S. Y., Park, J. W., Lee, B. L., Oh, B.-H., and Ha, N.-C. (2005) Crystal structure of a clip-domain serine protease and functional roles of the clip domains. EMBO J. 24, 4404-4414 (Pubitemid 41828914)
    • (2005) EMBO Journal , vol.24 , Issue.24 , pp. 4404-4414
    • Piao, S.1    Song, Y.-L.2    Jung, H.K.3    Sam, Y.P.4    Ji, W.P.5    Bok, L.L.6    Oh, B.-H.7    Ha, N.-C.8
  • 29
    • 0030760062 scopus 로고    scopus 로고
    • Isolation and identification of a plasmatocyte-spreading peptide from the hemolymph of the lepidopteran insect Pseudoplusia includens
    • DOI 10.1074/jbc.272.37.23440
    • Clark, K. D., Pech, L. L., and Strand, M. R. (1997) Isolation and identification of a plasmatocyte-spreading peptide from the hemolymph of the lepidopteran insect Pseudoplusia includens. J. Biol. Chem. 272, 23440-23447 (Pubitemid 27392487)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.37 , pp. 23440-23447
    • Clark, K.D.1    Pech, L.L.2    Strand, M.R.3
  • 30
    • 0001730096 scopus 로고
    • Immunolocalization of prophenoloxidase among hemocytes of the silkworm, Bombyx mori
    • Ashida, M., Ochiai, M., and Niki, T. (1988) Immunolocalization of prophenoloxidase among hemocytes of the silkworm, Bombyx mori. Tissue Cell 20, 599-610
    • (1988) Tissue Cell , vol.20 , pp. 599-610
    • Ashida, M.1    Ochiai, M.2    Niki, T.3
  • 31
    • 0034677596 scopus 로고    scopus 로고
    • A β1,3-glucan recognition protein from an insect, Manduca sexta, agglutinates microorganisms and activates the phenoloxidase cascade
    • DOI 10.1074/jbc.275.11.7505
    • Ma, C., and Kanost, M. R. (2000) A β1,3-glucan recognition protein from an insect, Manduca sexta, agglutinates microorganisms and activates the phenoloxidase cascade. J. Biol. Chem. 275, 7505-7514 (Pubitemid 30159646)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.11 , pp. 7505-7514
    • Ma, C.1    Kanost, M.R.2
  • 32
    • 0142211266 scopus 로고    scopus 로고
    • Characterization and Properties of a 1,3-β-D-Glucan Pattern Recognition Protein of Tenebrio molitor Larvae That Is Specifically Degraded by Serine Protease during Prophenoloxidase Activation
    • DOI 10.1074/jbc.M307475200
    • Zhang, R., Cho, H. Y., Kim, H. S., Ma, Y. G., Osaki, T., Kawabata S., Söderhäll, K., and Lee, B. L. (2003) Characterization and properties of a 1,3-β-D-glucan pattern recognition protein of Tenebrio molitor larvae that is specifically degraded by serine protease during prophenoloxidase activation. J. Biol. Chem. 278, 42072-42079 (Pubitemid 37310473)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.43 , pp. 42072-42079
    • Zhang, R.1    Cho, H.Y.2    Kim, H.S.3    Ma, Y.G.4    Osaki, T.5    Kawabata, S.-I.6    Soderhall, K.7    Lee, B.L.8
  • 33
    • 0034681346 scopus 로고    scopus 로고
    • A pattern-recognition protein for β-1,3-glucan
    • Ochiai, M., and Ashida, M. (2000) A pattern-recognition protein for β-1,3-glucan. J. Biol. Chem. 275, 4995-5002
    • (2000) J. Biol. Chem. , vol.275 , pp. 4995-5002
    • Ochiai, M.1    Ashida, M.2
  • 34
    • 0343415656 scopus 로고    scopus 로고
    • A lipopolysaccharide- and β-1,3-glucan-binding protein from hemocytes of the freshwater crayfish Pacifastacus leniusculus. Purification, characterization, and cDNA cloning
    • DOI 10.1074/jbc.275.2.1337
    • Lee, S. Y., Wang, R., and Söderhäll, K. (2000) A lipopolysaccharide- and β-1,3-glucan-binding protein from hemocytes of the freshwater crayfish Pacifastacus leniusculus. J. Biol. Chem. 275, 1337-1343 (Pubitemid 30051190)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.2 , pp. 1337-1343
    • Lee, S.Y.1    Wang, R.2    Soderhall, K.3
  • 35
    • 0942265564 scopus 로고    scopus 로고
    • Peptidoglycan Recognition Proteins Involved in 1,3-D-Glucan-dependent Prophenoloxidase Activation System of Insect
    • DOI 10.1074/jbc.M309821200
    • Lee, M. H., Osaki, T., Lee, J. Y., Baek, M. J., Zhang, R., Park, J. W., Kawabata, S., Söderhäll, K., and Lee, B. L. (2004) Peptidoglycan recognition proteins involved in 1,3-D-glucan-dependent prophenoloxidase activation system of insect. J. Biol. Chem. 279, 3218-3227 (Pubitemid 38140555)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3218-3227
    • Lee, M.H.1    Osaki, T.2    Lee, J.Y.3    Baek, M.J.4    Zhang, R.5    Park, J.W.6    Kawabata, S.-I.7    Soderhall, K.8    Lee, B.L.9
  • 36
    • 0002226805 scopus 로고
    • A cane sugar factor suppressing activation of prophenoloxidase in haemolymph of the silkworm, Bombyx mori
    • Ashida, M. (1981) A cane sugar factor suppressing activation of prophenoloxidase in haemolymph of the silkworm, Bombyx mori. Insect Biochem. 11, 57-65
    • (1981) Insect Biochem. , vol.11 , pp. 57-65
    • Ashida, M.1
  • 37
    • 0029162812 scopus 로고
    • Molecular cloning of insect pro-phenol oxidase.Acopper-containing protein homologous to arthropod hemocyanin
    • Kawabata, T., Yasuhara, Y., Ochiai, M., Matsuura, S., and Ashida, M. (1995) Molecular cloning of insect pro-phenol oxidase.Acopper-containing protein homologous to arthropod hemocyanin. Proc. Natl. Acad. Sci. U.S.A. 92, 7774-7778
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7774-7778
    • Kawabata, T.1    Yasuhara, Y.2    Ochiai, M.3    Matsuura, S.4    Ashida, M.5
  • 38
    • 0029011721 scopus 로고
    • Reexamination of properties of prophenoloxidase isolated from larval hemolymph of the silkworm, Bombyx mori
    • Yasuhara, Y., Koizumi, Y., Katagiri, C., and Ashida, M. (1995) Reexamination of properties of prophenoloxidase isolated from larval hemolymph of the silkworm, Bombyx mori. Arch. Biochem. Biophys. 320, 14-23
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 14-23
    • Yasuhara, Y.1    Koizumi, Y.2    Katagiri, C.3    Ashida, M.4
  • 39
    • 0032867624 scopus 로고    scopus 로고
    • Properties of phenoloxidases generated from prophenoloxidase with 2- propanol and the natural activator in Drosophila melanogaster
    • DOI 10.1023/A:1018730404305
    • Asada, N., and Sezaki, H. (1999) Properties of phenoloxidases generated from prophenoloxidase with 2-propanol and the natural activator in Drosophila melanogaster. Biochem. Genet. 37, 149-158 (Pubitemid 29491284)
    • (1999) Biochemical Genetics , vol.37 , Issue.5-6 , pp. 149-158
    • Asada, N.1    Sezaki, H.2
  • 40
    • 0037311545 scopus 로고    scopus 로고
    • Nonproteolytic serine proteinase homologs are involved in prophenoloxidase activation in the tobacco hornworm, Manduca sexta
    • DOI 10.1016/S0965-1748(02)00191-1
    • Yu, X.-Q., Jiang, H., Wang, Y., and Kanost, M. R. (2003) Nonproteolytic serine proteinase homologs are involved in prophenoloxidase activation in the tobacco hornworm, Manduca sexta. Insect Biochem. Mol. Biol. 33, 197-208 (Pubitemid 36154283)
    • (2003) Insect Biochemistry and Molecular Biology , vol.33 , Issue.2 , pp. 197-208
    • Yu, X.-Q.1    Jiang, H.2    Wang, Y.3    Kanost, M.R.4
  • 41
    • 0037965469 scopus 로고    scopus 로고
    • Tyrosinases from crustaceans form hexamers
    • DOI 10.1042/BJ20021058
    • Jaenicke, E., and Decker, H. (2003) Tyrosinases from crustaceans form hexamers. Biochem. J. 371, 515-523 (Pubitemid 36547635)
    • (2003) Biochemical Journal , vol.371 , Issue.2 , pp. 515-523
    • Jaenicke, E.1    Decker, H.2
  • 43
    • 35449000601 scopus 로고    scopus 로고
    • Characterization of tyrosine hydroxylase from Manduca sexta
    • DOI 10.1016/j.ibmb.2007.08.006, PII S0965174807002093
    • Gorman, M. J., An, C., and Kanost, M. R. (2007) Characterization of tyrosine hydroxylase from Manduca sexta. Insect Biochem. Mol. Biol. 37, 1327-1337 (Pubitemid 47625986)
    • (2007) Insect Biochemistry and Molecular Biology , vol.37 , Issue.12 , pp. 1327-1337
    • Gorman, M.J.1    An, C.2    Kanost, M.R.3
  • 45
    • 84868507801 scopus 로고    scopus 로고
    • Identification of plasma porteinase complexes with serpin-3 in Manduca sexta
    • Christen, J. M., Hiromasa, Y., An, C., and Kanost, M. R. (2012) Identification of plasma porteinase complexes with serpin-3 in Manduca sexta. Insect Biochem. Mol. Biol. 42, 946-955
    • (2012) Insect Biochem. Mol. Biol. , vol.42 , pp. 946-955
    • Christen, J.M.1    Hiromasa, Y.2    An, C.3    Kanost, M.R.4
  • 47
    • 0032514618 scopus 로고    scopus 로고
    • Pro-phenol oxidase activating proteinase from an insect, Manduca sexta: A bacteria-inducible protein similar to Drosophila easter
    • DOI 10.1073/pnas.95.21.12220
    • Jiang, H., Wang, Y., and Kanost, M. R. (1998) Pro-phenol oxidase activating proteinase from an insect, Manduca sexta. A bacteria-inducible protein similar to Drosophila easter. Proc. Natl. Acad. Sci. U.S.A. 95, 12220-12225 (Pubitemid 28483746)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.21 , pp. 12220-12225
    • Jiang, H.1    Wang, Y.2    Kanost, M.R.3
  • 48
    • 0033771124 scopus 로고    scopus 로고
    • A masquerade-like serine proteinease homologue is necessary for phenoloxidase activity in the coleopteran insect, Holotrichia diomphalia larvae
    • Kwon, T. H., Kim, M. S., Choi, H. W., Joo, C. H., Cho, M. Y., and Lee, B. L. (2000) A masquerade-like serine proteinease homologue is necessary for phenoloxidase activity in the coleopteran insect, Holotrichia diomphalia larvae. Eur. J. Biochem. 267, 6188-6196
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6188-6196
    • Kwon, T.H.1    Kim, M.S.2    Choi, H.W.3    Joo, C.H.4    Cho, M.Y.5    Lee, B.L.6
  • 49
    • 79952450525 scopus 로고    scopus 로고
    • Localization of the serine protease homology Bm- SPH-1 in nodules of E. coli-injected Bombyx mori larvae and functional analysis of its role in nodule formation
    • Sakamoto, M., Ohta, M., Suzuki, A., Takase, H., Yoshizawa, Y., Kitami, M., and Sato, R. (2011) Localization of the serine protease homology Bm- SPH-1 in nodules of E. coli-injected Bombyx mori larvae and functional analysis of its role in nodule formation. Dev. Comp. Immunol. 35, 611-619
    • (2011) Dev. Comp. Immunol. , vol.35 , pp. 611-619
    • Sakamoto, M.1    Ohta, M.2    Suzuki, A.3    Takase, H.4    Yoshizawa, Y.5    Kitami, M.6    Sato, R.7
  • 50
  • 51
    • 84869227842 scopus 로고    scopus 로고
    • Knowing your friends. Invertebrate innate immunity fosters beneficial bacterial symbioses
    • Nyholm, S. V., and Graf, J. (2012) Knowing your friends. Invertebrate innate immunity fosters beneficial bacterial symbioses. Nat. Rev. Microbiol. 10, 815-827
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 815-827
    • Nyholm, S.V.1    Graf, J.2
  • 52
    • 0015887922 scopus 로고
    • Studies on prephenoloxidase-activating enzyme from cuticle of the silworm Bombyx mori. I. Activation reaction by the enzyme
    • Dohke, K. (1973) Studies on prephenoloxidase-activating enzyme from cuticle of the silworm Bombyx mori. I. Activation reaction by the enzyme. Arch. Biochem. Biophys. 157, 203-209
    • (1973) Arch. Biochem. Biophys. , vol.157 , pp. 203-209
    • Dohke, K.1
  • 53
    • 15044357864 scopus 로고    scopus 로고
    • Melanization immune responses in mosquito vectors
    • DOI 10.1016/j.pt.2005.02.007
    • Christensen, B. M., Li, J., Chen, C. C., and Nappi, A. J. (2005) Melanization immune responses in mosquito vectors. Trends Parasitol. 21, 192-199 (Pubitemid 40381258)
    • (2005) Trends in Parasitology , vol.21 , Issue.4 , pp. 192-199
    • Christensen, B.M.1    Li, J.2    Chen, C.-C.3    Nappi, A.J.4
  • 54
    • 0034035531 scopus 로고    scopus 로고
    • Bacterial-injection-induced syntheses of N-β-alanyldopamine and dopa decarboxylase in the hemolymph of coleopteran insect, Tenebrio molitor larvae
    • DOI 10.1046/j.1432-1327.2000.01271.x
    • Kim, M. H., Joo, C. H., Cho, M. Y., Kwon, T. H., Lee, K. M., Natori, S., Lee, T. H., and Lee, B. L. (2000) Bacterial-injection induced synthesis of N-β-alanyldopamine and dopa decarboxylase in the hemolymph of coleopteran insect, Tenebrio molitor larvae. Eur. J. Biochem. 267, 2599-2608 (Pubitemid 30304255)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.9 , pp. 2599-2608
    • Kim, M.H.1    Joo, C.H.2    Cho, M.Y.3    Kwon, T.H.4    Lee, K.M.5    Natori, S.6    Lee, T.H.7    Lee, B.L.8
  • 55
    • 0037726774 scopus 로고    scopus 로고
    • Identification by subtractive suppression hybridization of bacteria-induced genes expressed in Manduca sexta fat body
    • DOI 10.1016/S0965-1748(03)00028-6
    • Zhu, Y., Johnson, T. J., Myers, A. A., and Kanost, M. R. (2003) Identification by substractive suppression hybridization of bacteria-induced genes expressed in Manduca sexta fat body. Insect Biochem. Mol. Biol. 33, 541-559 (Pubitemid 36572719)
    • (2003) Insect Biochemistry and Molecular Biology , vol.33 , Issue.5 , pp. 541-559
    • Zhu, Y.1    Johnson, T.J.2    Myers, A.A.3    Kanost, M.R.4
  • 56
    • 84877910480 scopus 로고    scopus 로고
    • Determination of Amino Acids in Cell Cultures and Fermentation Broths
    • Dionex Corp. Dionex Corp., Sunnyvale, CA
    • Dionex Corp. (2003) Determination of Amino Acids in Cell Cultures and Fermentation Broths, Dionex Application Note 150, p. 4, Dionex Corp., Sunnyvale, CA
    • (2003) Dionex Application Note 150 , pp. 4


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