메뉴 건너뛰기




Volumn 32, Issue 1, 2008, Pages 61-70

Cloning, expression and antimicrobial activity of crustinPm1, a major isoform of crustin, from the black tiger shrimp Penaeus monodon

Author keywords

Antimicrobial peptide; Crustin; Penaeus monodon; WAP domain

Indexed keywords

ANTIINFECTIVE AGENT; CRUSTIN PM1; UNCLASSIFIED DRUG;

EID: 36349029136     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2007.04.004     Document Type: Article
Times cited : (114)

References (50)
  • 1
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand R.M., and Vogel H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim Biophys Acta 1462 1-2 (1999) 11-28
    • (1999) Biochim Biophys Acta , vol.1462 , Issue.1-2 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 2
    • 0029104873 scopus 로고
    • Antimicrobial peptides
    • Rao A.G. Antimicrobial peptides. Mol Plant Microbe Interact 8 1 (1995) 6-13
    • (1995) Mol Plant Microbe Interact , vol.8 , Issue.1 , pp. 6-13
    • Rao, A.G.1
  • 3
    • 0037068941 scopus 로고    scopus 로고
    • Innate immunity, antimicrobial peptides and protection of the oral cavity
    • Zasloff M. Innate immunity, antimicrobial peptides and protection of the oral cavity. Lancet 360 9340 (2002) 1116-1117
    • (2002) Lancet , vol.360 , Issue.9340 , pp. 1116-1117
    • Zasloff, M.1
  • 4
    • 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 3 (2003) 197-215
    • (2003) J Intern Med , vol.254 , Issue.3 , pp. 197-215
    • Boman, H.G.1
  • 5
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defences
    • Hancock R.E., and Diamond G. The role of cationic antimicrobial peptides in innate host defences. Trends Microbiol 8 9 (2000) 402-410
    • (2000) Trends Microbiol , vol.8 , Issue.9 , pp. 402-410
    • Hancock, R.E.1    Diamond, G.2
  • 6
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: from invertebrates to vertebrates
    • Bulet P., Stocklin R., and Menin L. Anti-microbial peptides: from invertebrates to vertebrates. Immunol Rev 198 1 (2004) 169-184
    • (2004) Immunol Rev , vol.198 , Issue.1 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 7
    • 0029762649 scopus 로고    scopus 로고
    • Purification and characterization of a proline-rich antibacterial peptide, with sequence similarity to bactenecin-7, from the haemocytes of the shore crab, Carcinus maenas
    • Schnapp D., Kemp G.D., and Smith V.J. Purification and characterization of a proline-rich antibacterial peptide, with sequence similarity to bactenecin-7, from the haemocytes of the shore crab, Carcinus maenas. Eur J Biochem 240 3 (1996) 532-539
    • (1996) Eur J Biochem , vol.240 , Issue.3 , pp. 532-539
    • Schnapp, D.1    Kemp, G.D.2    Smith, V.J.3
  • 8
    • 84972222998 scopus 로고
    • Antibacterial activity in the haemocytes of the shore crab Carcinus maenas
    • Chisholm J.R.S., and Smith V.J. Antibacterial activity in the haemocytes of the shore crab Carcinus maenas. J Mar Biol Ass UK 72 (1992) 529-542
    • (1992) J Mar Biol Ass UK , vol.72 , pp. 529-542
    • Chisholm, J.R.S.1    Smith, V.J.2
  • 9
    • 0033198883 scopus 로고    scopus 로고
    • Purification and characterization of a cysteine-rich 11.5-kDa antibacterial protein from the granular haemocytes of the shore crab, Carcinus maenas
    • Relf J.M., Chisholm J.R., Kemp G.D., and Smith V.J. Purification and characterization of a cysteine-rich 11.5-kDa antibacterial protein from the granular haemocytes of the shore crab, Carcinus maenas. Eur J Biochem 264 2 (1999) 350-357
    • (1999) Eur J Biochem , vol.264 , Issue.2 , pp. 350-357
    • Relf, J.M.1    Chisholm, J.R.2    Kemp, G.D.3    Smith, V.J.4
  • 10
    • 0035058194 scopus 로고    scopus 로고
    • Antimicrobial proteins in crustaceans
    • Smith V.J., and Chisholm J.R. Antimicrobial proteins in crustaceans. Adv Exp Med Biol 484 (2001) 95-112
    • (2001) Adv Exp Med Biol , vol.484 , pp. 95-112
    • Smith, V.J.1    Chisholm, J.R.2
  • 11
    • 0030692830 scopus 로고    scopus 로고
    • Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda)
    • Destoumieux D., Bulet P., Loew D., Van Dorsselaer A., Rodriguez J., and Bachère E. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda). J Biol Chem 272 45 (1997) 28398-28406
    • (1997) J Biol Chem , vol.272 , Issue.45 , pp. 28398-28406
    • Destoumieux, D.1    Bulet, P.2    Loew, D.3    Van Dorsselaer, A.4    Rodriguez, J.5    Bachère, E.6
  • 12
    • 0036380652 scopus 로고    scopus 로고
    • Diversity of the penaeidin antimicrobial peptides in two shrimp species
    • Cuthbertson B.J., Shepard E.F., Chapman R.W., and Gross P.S. Diversity of the penaeidin antimicrobial peptides in two shrimp species. Immunogenetics 54 6 (2002) 442-445
    • (2002) Immunogenetics , vol.54 , Issue.6 , pp. 442-445
    • Cuthbertson, B.J.1    Shepard, E.F.2    Chapman, R.W.3    Gross, P.S.4
  • 13
    • 9944233151 scopus 로고    scopus 로고
    • Antimicrobial peptides discovered in the black tiger shrimp Penaeus monodon using the EST approach
    • Supungul P., Klinbunga S., Pichyangkura R., Hirono I., Aoki T., and Tassanakajon A. Antimicrobial peptides discovered in the black tiger shrimp Penaeus monodon using the EST approach. Dis Aquat Organ 61 1-2 (2004) 123-135
    • (2004) Dis Aquat Organ , vol.61 , Issue.1-2 , pp. 123-135
    • Supungul, P.1    Klinbunga, S.2    Pichyangkura, R.3    Hirono, I.4    Aoki, T.5    Tassanakajon, A.6
  • 14
    • 1842833453 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of Ch-penaeidin, an antimicrobial peptide from Chinese shrimp, Fenneropenaeus chinensis
    • Kang C.J., Wang J.X., Zhao X.F., Yang X.M., Shao H.L., and Xiang J.H. Molecular cloning and expression analysis of Ch-penaeidin, an antimicrobial peptide from Chinese shrimp, Fenneropenaeus chinensis. Fish Shellfish Immunol 16 4 (2004) 513-525
    • (2004) Fish Shellfish Immunol , vol.16 , Issue.4 , pp. 513-525
    • Kang, C.J.1    Wang, J.X.2    Zhao, X.F.3    Yang, X.M.4    Shao, H.L.5    Xiang, J.H.6
  • 15
    • 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
    • Gross P.S., Bartlett T.C., Browdy C.L., Chapman R.W., and Warr G.W. 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
  • 16
    • 28244463332 scopus 로고    scopus 로고
    • Molecular cloning and expression profile of putative antilipopolysaccharide factor in Chinese shrimp (Fenneropenaeus chinensis)
    • Liu F., Liu Y., Li F., Dong B., and Xiang J. Molecular cloning and expression profile of putative antilipopolysaccharide factor in Chinese shrimp (Fenneropenaeus chinensis). Mar Biotechnol (NY) 7 6 (2005) 600-608
    • (2005) Mar Biotechnol (NY) , vol.7 , Issue.6 , pp. 600-608
    • Liu, F.1    Liu, Y.2    Li, F.3    Dong, B.4    Xiang, J.5
  • 17
    • 20644460364 scopus 로고    scopus 로고
    • Recombinant expression and anti-microbial activity of anti-lipopolysaccharide factor (ALF) from the black tiger shrimp Penaeus monodon
    • Somboonwiwat K., Marcos M., Tassanakajon A., Klinbunga S., Aumelas A., Romestand B., et al. Recombinant expression and anti-microbial activity of anti-lipopolysaccharide factor (ALF) from the black tiger shrimp Penaeus monodon. Dev Comp Immunol 29 10 (2005) 841-851
    • (2005) Dev Comp Immunol , vol.29 , Issue.10 , pp. 841-851
    • Somboonwiwat, K.1    Marcos, M.2    Tassanakajon, A.3    Klinbunga, S.4    Aumelas, A.5    Romestand, B.6
  • 18
    • 0036071479 scopus 로고    scopus 로고
    • Crustins, homologues of an 11.5-kDa antibacterial peptide, from two species of penaeid shrimp, Litopenaeus vannamei and Litopenaeus setiferus
    • Bartlett T.C., Cuthbertson B.J., Shepard E.F., Chapman R.W., Gross P.S., and Warr G.W. Crustins, homologues of an 11.5-kDa antibacterial peptide, from two species of penaeid shrimp, Litopenaeus vannamei and Litopenaeus setiferus. Mar Biotechnol (NY) 4 3 (2002) 278-293
    • (2002) Mar Biotechnol (NY) , vol.4 , Issue.3 , pp. 278-293
    • Bartlett, T.C.1    Cuthbertson, B.J.2    Shepard, E.F.3    Chapman, R.W.4    Gross, P.S.5    Warr, G.W.6
  • 20
    • 2442485800 scopus 로고    scopus 로고
    • cDNA sequence encoding an 11.5-kDa antibacterial peptide of the shrimp Penaeus monodon
    • Chen J.Y., Pan C.Y., and Kuo C.M. cDNA sequence encoding an 11.5-kDa antibacterial peptide of the shrimp Penaeus monodon. Fish Shellfish Immunol 16 5 (2004) 659-664
    • (2004) Fish Shellfish Immunol , vol.16 , Issue.5 , pp. 659-664
    • Chen, J.Y.1    Pan, C.Y.2    Kuo, C.M.3
  • 22
    • 7544244554 scopus 로고    scopus 로고
    • Cloning of kuruma prawn Marsupenaeus japonicus crustin-like peptide cCNA and analysis of its expression
    • Rattanachai A., Hirono I., Ohira T., Takahashi Y., and Aoki T. Cloning of kuruma prawn Marsupenaeus japonicus crustin-like peptide cCNA and analysis of its expression. Fish Sci 70 5 (2004) 765-771
    • (2004) Fish Sci , vol.70 , Issue.5 , pp. 765-771
    • Rattanachai, A.1    Hirono, I.2    Ohira, T.3    Takahashi, Y.4    Aoki, T.5
  • 23
    • 33845643045 scopus 로고    scopus 로고
    • Cloning and recombinant expression of a crustin-like gene from Chinese shrimp, Fenneropenaeus chinensis
    • Zhang J., Li F., Wang Z., and Xiang J. Cloning and recombinant expression of a crustin-like gene from Chinese shrimp, Fenneropenaeus chinensis. J Biotechnol 127 4 (2007) 605-614
    • (2007) J Biotechnol , vol.127 , Issue.4 , pp. 605-614
    • Zhang, J.1    Li, F.2    Wang, Z.3    Xiang, J.4
  • 24
    • 33644829821 scopus 로고    scopus 로고
    • Cloning of a crustin-like, single whey-acidic-domain, antibacterial peptide from the haemocytes of the European lobster, Homarus gammarus, and its response to infection with bacteria
    • Hauton C., Brockton V., and Smith V.J. Cloning of a crustin-like, single whey-acidic-domain, antibacterial peptide from the haemocytes of the European lobster, Homarus gammarus, and its response to infection with bacteria. Mol Immunol 43 9 (2006) 1490-1496
    • (2006) Mol Immunol , vol.43 , Issue.9 , pp. 1490-1496
    • Hauton, C.1    Brockton, V.2    Smith, V.J.3
  • 25
    • 1042278118 scopus 로고    scopus 로고
    • Inducible transcript expressed by reactive epithelial cells at sites of olfactory sensory neuron proliferation
    • Stoss T.D., Nickell M.D., Hardin D., Derby C.D., and McClintock T.S. Inducible transcript expressed by reactive epithelial cells at sites of olfactory sensory neuron proliferation. J Neurobiol 58 3 (2004) 355-368
    • (2004) J Neurobiol , vol.58 , Issue.3 , pp. 355-368
    • Stoss, T.D.1    Nickell, M.D.2    Hardin, D.3    Derby, C.D.4    McClintock, T.S.5
  • 26
    • 85190527696 scopus 로고    scopus 로고
    • Antibacterial peptides in hemocytes and hematopoietic tissue from freshwater crayfish Pacifastacus leniusculus: Characterization and expression pattern
    • Jiravanichpaisal P., Lee S.Y., Kim Y.A., Andren T., and Söderhäll I. Antibacterial peptides in hemocytes and hematopoietic tissue from freshwater crayfish Pacifastacus leniusculus: Characterization and expression pattern. Dev Comp Immunol (2006)
    • (2006) Dev Comp Immunol
    • Jiravanichpaisal, P.1    Lee, S.Y.2    Kim, Y.A.3    Andren, T.4    Söderhäll, I.5
  • 27
    • 0040469390 scopus 로고
    • The 2.5 A X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine alpha-chymotrypsin
    • Grütter M.G., Fendrich G., Huber R., and Bode W. The 2.5 A X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine alpha-chymotrypsin. EMBO J 7 2 (1988) 345-351
    • (1988) EMBO J , vol.7 , Issue.2 , pp. 345-351
    • Grütter, M.G.1    Fendrich, G.2    Huber, R.3    Bode, W.4
  • 28
    • 0027177831 scopus 로고
    • Crystallization of a complex between an elastase-specific inhibitor elafin and porcine pancreatic elastase
    • Tsunemi M., Matsuura Y., Sakakibara S., and Katsube Y. Crystallization of a complex between an elastase-specific inhibitor elafin and porcine pancreatic elastase. J Mol Biol 232 1 (1993) 310-311
    • (1993) J Mol Biol , vol.232 , Issue.1 , pp. 310-311
    • Tsunemi, M.1    Matsuura, Y.2    Sakakibara, S.3    Katsube, Y.4
  • 29
    • 0034581627 scopus 로고    scopus 로고
    • The role of secretory leukocyte proteinase inhibitor and elafin (elastase-specific inhibitor/skin-derived antileukoprotease) as alarm antiproteinases in inflammatory lung disease
    • Sallenave J.M. The role of secretory leukocyte proteinase inhibitor and elafin (elastase-specific inhibitor/skin-derived antileukoprotease) as alarm antiproteinases in inflammatory lung disease. Respir Res 1 2 (2000) 87-92
    • (2000) Respir Res , vol.1 , Issue.2 , pp. 87-92
    • Sallenave, J.M.1
  • 30
    • 0032896270 scopus 로고    scopus 로고
    • Endogenous mucosal antiviral factors of the oral cavity
    • Shugars D.C. Endogenous mucosal antiviral factors of the oral cavity. J Infect Dis 179 Suppl 3 (1999) S431
    • (1999) J Infect Dis , vol.179 , Issue.SUPPL. 3
    • Shugars, D.C.1
  • 31
    • 0032581354 scopus 로고    scopus 로고
    • Antileukoprotease in human skin: an antibiotic peptide constitutively produced by keratinocytes
    • Wiedow O., Harder J., Bartels J., Streit V., and Christophers E. Antileukoprotease in human skin: an antibiotic peptide constitutively produced by keratinocytes. Biochem Biophys Res Commun 248 3 (1998) 904-909
    • (1998) Biochem Biophys Res Commun , vol.248 , Issue.3 , pp. 904-909
    • Wiedow, O.1    Harder, J.2    Bartels, J.3    Streit, V.4    Christophers, E.5
  • 34
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 36
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: an application to display phylogenetic trees on personal computers
    • Page R.D. TreeView: an application to display phylogenetic trees on personal computers. Comput Appl Biosci 12 4 (1996) 357-358
    • (1996) Comput Appl Biosci , vol.12 , Issue.4 , pp. 357-358
    • Page, R.D.1
  • 37
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 1-2 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , Issue.1-2 , pp. 248-254
    • Bradford, M.M.1
  • 38
    • 11244323393 scopus 로고    scopus 로고
    • Antimicrobial activity of histones from hemocytes of the Pacific white shrimp
    • Patat S.A., Carnegie R.B., Kingsbury C., Gross P.S., Chapman R., and Schey K.L. Antimicrobial activity of histones from hemocytes of the Pacific white shrimp. Eur J Biochem 271 23-24 (2004) 4825-4833
    • (2004) Eur J Biochem , vol.271 , Issue.23-24 , pp. 4825-4833
    • Patat, S.A.1    Carnegie, R.B.2    Kingsbury, C.3    Gross, P.S.4    Chapman, R.5    Schey, K.L.6
  • 39
    • 0027528472 scopus 로고
    • Functional and chemical characterization of hymenoptaecin, an antibacterial polypeptide that is infection inducible in the Honey bee (Apis mellifera)
    • Casteels P., Ampe C., Jacobs F., and Tempst P. Functional and chemical characterization of hymenoptaecin, an antibacterial polypeptide that is infection inducible in the Honey bee (Apis mellifera). J Biol Chem 268 10 (1993) 7044-7054
    • (1993) J Biol Chem , vol.268 , Issue.10 , pp. 7044-7054
    • Casteels, P.1    Ampe, C.2    Jacobs, F.3    Tempst, P.4
  • 40
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen J.D., Nielsen H., von Heijne G., and Brunak S. Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 340 4 (2004) 783-795
    • (2004) J Mol Biol , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von Heijne, G.3    Brunak, S.4
  • 41
    • 33748776554 scopus 로고    scopus 로고
    • Gene characterisation, isoforms and recombinant expression of carcinin, an antibacterial protein from the shore crab, Carcinus maenas
    • Brockton V., Hammond J.A., and Smith V.J. Gene characterisation, isoforms and recombinant expression of carcinin, an antibacterial protein from the shore crab, Carcinus maenas. Mol Immunol 44 5 (2007) 943-949
    • (2007) Mol Immunol , vol.44 , Issue.5 , pp. 943-949
    • Brockton, V.1    Hammond, J.A.2    Smith, V.J.3
  • 42
    • 1242296295 scopus 로고    scopus 로고
    • Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata
    • Ali M.F., Lips K.R., Knoop F.C., Fritzsch B., Miller C., and Conlon J.M. Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata. Biochim Biophys Acta 1601 1 (2002) 55-63
    • (2002) Biochim Biophys Acta , vol.1601 , Issue.1 , pp. 55-63
    • Ali, M.F.1    Lips, K.R.2    Knoop, F.C.3    Fritzsch, B.4    Miller, C.5    Conlon, J.M.6
  • 43
    • 0022479785 scopus 로고
    • The acid-stable proteinase inhibitor of human mucous secretions (HUSI-I, antileukoprotease). Complete amino acid sequence as revealed by protein and cDNA sequencing and structural homology to whey proteins and Red Sea turtle proteinase inhibitor
    • Seemuller U., Arnhold M., Fritz H., Wiedenmann K., Machleidt W., Heinzel R., et al. The acid-stable proteinase inhibitor of human mucous secretions (HUSI-I, antileukoprotease). Complete amino acid sequence as revealed by protein and cDNA sequencing and structural homology to whey proteins and Red Sea turtle proteinase inhibitor. FEBS Lett 199 1 (1986) 43-48
    • (1986) FEBS Lett , vol.199 , Issue.1 , pp. 43-48
    • Seemuller, U.1    Arnhold, M.2    Fritz, H.3    Wiedenmann, K.4    Machleidt, W.5    Heinzel, R.6
  • 44
    • 0025168332 scopus 로고
    • Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence
    • Wiedow O., Schröder J.M., Gregory H., Young J.A., and Christophers E. Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence. J Biol Chem 265 25 (1990) 14791-14795
    • (1990) J Biol Chem , vol.265 , Issue.25 , pp. 14791-14795
    • Wiedow, O.1    Schröder, J.M.2    Gregory, H.3    Young, J.A.4    Christophers, E.5
  • 45
  • 46
    • 0034821325 scopus 로고    scopus 로고
    • Regulation of adenovirus-mediated elafin transgene expression by bacterial lipopolysaccharide
    • Simpson A.J., Cunningham G.A., Porteous D.J., Haslett C., and Sallenave J.M. Regulation of adenovirus-mediated elafin transgene expression by bacterial lipopolysaccharide. Hum Gene Ther 12 11 (2001) 1395-1406
    • (2001) Hum Gene Ther , vol.12 , Issue.11 , pp. 1395-1406
    • Simpson, A.J.1    Cunningham, G.A.2    Porteous, D.J.3    Haslett, C.4    Sallenave, J.M.5
  • 47
    • 0037442202 scopus 로고    scopus 로고
    • Mouse SWAM1 and SWAM2 are antibacterial proteins composed of a single whey acidic protein motif
    • Hagiwara K., Kikuchi T., Endo Y., Huqun A., Usui K., Takahashi M., et al. Mouse SWAM1 and SWAM2 are antibacterial proteins composed of a single whey acidic protein motif. J Immunol 170 4 (2003) 1973-1979
    • (2003) J Immunol , vol.170 , Issue.4 , pp. 1973-1979
    • Hagiwara, K.1    Kikuchi, T.2    Endo, Y.3    Huqun, A.4    Usui, K.5    Takahashi, M.6
  • 48
    • 1642463826 scopus 로고    scopus 로고
    • The prophenoloxidase-activating system in invertebrates
    • Cerenius L., and Söderhäll K. The prophenoloxidase-activating system in invertebrates. Immunol Rev 198 1 (2004) 116-126
    • (2004) Immunol Rev , vol.198 , Issue.1 , pp. 116-126
    • Cerenius, L.1    Söderhäll, K.2
  • 49
    • 85190527696 scopus 로고    scopus 로고
    • Antibacterial peptides in hemocytes and hematopoietic tissue from freshwater crayfish Pacifastacus leniusculus: characterization and expression pattern
    • Available online 2 October 2006
    • Jiravanichpaisal P., Lee S.Y., Kim Y.A., Andren T., and Söderhäll I. Antibacterial peptides in hemocytes and hematopoietic tissue from freshwater crayfish Pacifastacus leniusculus: characterization and expression pattern. Dev Comp Immunol 12 (2006) 123 Available online 2 October 2006
    • (2006) Dev Comp Immunol , vol.12 , pp. 123
    • Jiravanichpaisal, P.1    Lee, S.Y.2    Kim, Y.A.3    Andren, T.4    Söderhäll, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.