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Volumn 32, Issue 3, 2008, Pages 275-285

Arasin 1, a proline-arginine-rich antimicrobial peptide isolated from the spider crab, Hyas araneus

Author keywords

Bioactive compounds; Cationic antibacterial peptides; Crustacea; Cysteine containing; Invertebrate immunology; Marine bioprospecting; Natural products; Proline rich

Indexed keywords

AMINO ACID; COMPLEMENTARY DNA; DISULFIDE; POLYPEPTIDE ANTIBIOTIC AGENT;

EID: 36549087177     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2007.06.002     Document Type: Article
Times cited : (107)

References (53)
  • 1
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman H.G. Peptide antibiotics and their role in innate immunity. Ann Rev Immunol 13 (1995) 61-92
    • (1995) Ann Rev Immunol , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 2
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat Rev Microbiol 3 (2005) 238-250
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 3
    • 0033847734 scopus 로고    scopus 로고
    • The millennium bugs-the need for and development of new antibacterials
    • Bax R., Mullan N., and Verhoef J. The millennium bugs-the need for and development of new antibacterials. Int J Antimicrob Agents 16 (2000) 51-59
    • (2000) Int J Antimicrob Agents , vol.16 , pp. 51-59
    • Bax, R.1    Mullan, N.2    Verhoef, J.3
  • 4
    • 0033814969 scopus 로고    scopus 로고
    • Peptide-based antibiotics: a potential answer to raging antimicrobial resistance
    • Mor A. Peptide-based antibiotics: a potential answer to raging antimicrobial resistance. Drug Dev Res 50 (2000) 440-447
    • (2000) Drug Dev Res , vol.50 , pp. 440-447
    • Mor, A.1
  • 5
    • 0036252092 scopus 로고    scopus 로고
    • Cationic peptides: distribution and mechanisms of resistance
    • Devine D.A., and Hancock R.E. Cationic peptides: distribution and mechanisms of resistance. Curr Pharm Des 8 (2002) 703-714
    • (2002) Curr Pharm Des , vol.8 , pp. 703-714
    • Devine, D.A.1    Hancock, R.E.2
  • 6
    • 0038364156 scopus 로고    scopus 로고
    • Cathelicidins-a family of multifunctional antimicrobial peptides
    • Bals R., and Wilson J.M. Cathelicidins-a family of multifunctional antimicrobial peptides. Cell Mol Life Sci 60 (2003) 711-720
    • (2003) Cell Mol Life Sci , vol.60 , pp. 711-720
    • Bals, R.1    Wilson, J.M.2
  • 7
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: antimicrobial peptides of innate immunity
    • Ganz T. Defensins: antimicrobial peptides of innate immunity. Nat Rev Immunol 3 (2003) 710-720
    • (2003) Nat Rev Immunol , vol.3 , pp. 710-720
    • Ganz, T.1
  • 8
    • 0034672657 scopus 로고    scopus 로고
    • Original involvement of antimicrobial peptides in mussel innate immunity
    • Mitta G., Vandenbulcke F., and Roch P. Original involvement of antimicrobial peptides in mussel innate immunity. FEBS Lett 486 (2000) 185-190
    • (2000) FEBS Lett , vol.486 , pp. 185-190
    • Mitta, G.1    Vandenbulcke, F.2    Roch, P.3
  • 9
    • 0036467504 scopus 로고    scopus 로고
    • The molecular basis of innate immunity in the horseshoe crab
    • Iwanaga S. The molecular basis of innate immunity in the horseshoe crab. Curr Opin Immunol 14 (2002) 87-95
    • (2002) Curr Opin Immunol , vol.14 , pp. 87-95
    • Iwanaga, S.1
  • 10
    • 2442580828 scopus 로고    scopus 로고
    • Involvement of penaeidins in defense reactions of the shrimp Litopenaeus stylirostris to a pathogenic vibrio
    • Munoz M., Vandenbulcke F., Garnier J., Gueguen Y., Bulet P., Saulnier D., et al. Involvement of penaeidins in defense reactions of the shrimp Litopenaeus stylirostris to a pathogenic vibrio. Cell Mol Life Sci 61 (2004) 961-972
    • (2004) Cell Mol Life Sci , vol.61 , pp. 961-972
    • Munoz, M.1    Vandenbulcke, F.2    Garnier, J.3    Gueguen, Y.4    Bulet, P.5    Saulnier, D.6
  • 11
    • 4644311383 scopus 로고    scopus 로고
    • Antimicrobial peptides from marine invertebrates
    • Tincu J.A., and Taylor S.W. Antimicrobial peptides from marine invertebrates. Antimicrob Agents Chemother 48 (2004) 3645-3654
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 3645-3654
    • Tincu, J.A.1    Taylor, S.W.2
  • 12
    • 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.S., 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 (1999) 350-357
    • (1999) Eur J Biochem , vol.264 , pp. 350-357
    • Relf, J.M.1    Chisholm, J.R.S.2    Kemp, G.D.3    Smith, V.J.4
  • 13
    • 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 4 (2002) 278-293
    • (2002) Mar Biotechnol , vol.4 , 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
  • 14
    • 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 (2006) 1490-1496
    • (2006) Mol Immunol , vol.43 , pp. 1490-1496
    • Hauton, C.1    Brockton, V.2    Smith, V.J.3
  • 15
    • 1642422727 scopus 로고    scopus 로고
    • Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Crassostrea gigas
    • Bachère E., Gueguen Y., Gonzalez M., de Lorgeril J., Garnier J., and Romestand B. Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Crassostrea gigas. Immunol Rev 198 (2004) 149-168
    • (2004) Immunol Rev , vol.198 , pp. 149-168
    • Bachère, E.1    Gueguen, Y.2    Gonzalez, M.3    de Lorgeril, J.4    Garnier, J.5    Romestand, B.6
  • 16
    • 27644520345 scopus 로고    scopus 로고
    • PenBase, the shrimp antimicrobial peptide penaeidin database: sequence-based classification and recommended nomenclature
    • Gueguen Y., Garnier J., Robert L., Lefranc M.P., Mougenot I., de Lorgeril J., et al. PenBase, the shrimp antimicrobial peptide penaeidin database: sequence-based classification and recommended nomenclature. Dev Comp Immunol 30 (2006) 283-288
    • (2006) Dev Comp Immunol , vol.30 , pp. 283-288
    • Gueguen, Y.1    Garnier, J.2    Robert, L.3    Lefranc, M.P.4    Mougenot, I.5    de Lorgeril, J.6
  • 17
    • 0035861645 scopus 로고    scopus 로고
    • Crustacean immunity. Antifungal peptides are generated from the c terminus of shrimp hemocyanin in response to microbial challenge
    • Destoumieux-Garzon D., Saulnier D., Garnier J., Jouffrey C., Bulet P., and Bachere E. Crustacean immunity. Antifungal peptides are generated from the c terminus of shrimp hemocyanin in response to microbial challenge. J Biol Chem 276 (2001) 47070-47077
    • (2001) J Biol Chem , vol.276 , pp. 47070-47077
    • Destoumieux-Garzon, D.1    Saulnier, D.2    Garnier, J.3    Jouffrey, C.4    Bulet, P.5    Bachere, E.6
  • 18
    • 0037424354 scopus 로고    scopus 로고
    • Processing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculus
    • Lee S.C., Lee B.L., and Söderhäll K. Processing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculus. J Biol Chem 278 (2003) 7927-7933
    • (2003) J Biol Chem , vol.278 , pp. 7927-7933
    • Lee, S.C.1    Lee, B.L.2    Söderhäll, K.3
  • 19
    • 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, Carinus 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, Carinus maenas. Eur J Biochem 240 (1996) 532-539
    • (1996) Eur J Biochem , vol.240 , pp. 532-539
    • Schnapp, D.1    Kemp, G.D.2    Smith, V.J.3
  • 20
    • 0025065276 scopus 로고
    • Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils
    • Frank R.W., Gennaro R., Schneider K., Przybylski M., and Romeo D. Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils. J Biol Chem 265 (1990) 18871-18874
    • (1990) J Biol Chem , vol.265 , pp. 18871-18874
    • Frank, R.W.1    Gennaro, R.2    Schneider, K.3    Przybylski, M.4    Romeo, D.5
  • 21
    • 0032791277 scopus 로고    scopus 로고
    • Callinectin, an antibacterial peptide from blue crab, Callinectes sapidus, hemocytes
    • Khoo L., Robinette D.W., and Noga E.J. Callinectin, an antibacterial peptide from blue crab, Callinectes sapidus, hemocytes. Mar Biotechnol 1 (1999) 44-51
    • (1999) Mar Biotechnol , vol.1 , pp. 44-51
    • Khoo, L.1    Robinette, D.W.2    Noga, E.J.3
  • 22
    • 33846395380 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., Kima Y.-A., Andréna T., and Söderhäll I. Antibacterial peptides in hemocytes and hematopoietic tissue from freshwater crayfish Pacifastacus leniusculus: characterization and expression pattern. Dev Comp Immunol 31 (2007) 441-455
    • (2007) Dev Comp Immunol , vol.31 , pp. 441-455
    • Jiravanichpaisal, P.1    Lee, S.Y.2    Kima, Y.-A.3    Andréna, T.4    Söderhäll, I.5
  • 24
    • 0347755460 scopus 로고    scopus 로고
    • APD: the antimicrobial peptide database
    • Wang Z., and Wang G. APD: the antimicrobial peptide database. Nucleic Acids Res 32 (2004) 590-592
    • (2004) Nucleic Acids Res , vol.32 , pp. 590-592
    • Wang, Z.1    Wang, G.2
  • 26
  • 27
    • 0033787915 scopus 로고    scopus 로고
    • Antibacterial activity of 15-residue lactoferricin derivatives
    • Strøm M.B., Rekdal Ø., and Svendsen J.S. Antibacterial activity of 15-residue lactoferricin derivatives. J Pept Res 56 (2000) 265-274
    • (2000) J Pept Res , vol.56 , pp. 265-274
    • Strøm, M.B.1    Rekdal, Ø.2    Svendsen, J.S.3
  • 29
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RTPCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RTPCR. Nucleic Acids Res 29 (2001) e45
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1
  • 30
    • 0001924808 scopus 로고    scopus 로고
    • The inducible antibacterial peptides of the hemipteran insect Palomena prasina: Identification of a unique family of proline-rich peptides and of a novel insect defensin
    • Chernysh S., Cociancich S., Briand J.-P., Hetru C., and Bulet P. The inducible antibacterial peptides of the hemipteran insect Palomena prasina: Identification of a unique family of proline-rich peptides and of a novel insect defensin. J Insect Physiol 42 (1996) 81-89
    • (1996) J Insect Physiol , vol.42 , pp. 81-89
    • Chernysh, S.1    Cociancich, S.2    Briand, J.-P.3    Hetru, C.4    Bulet, P.5
  • 31
    • 0026349223 scopus 로고
    • Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides
    • Agerberth B., Lee J.Y., Bergman T., Carlquist M., Boman H.G., Mutt V., et al. Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides. Eur J Biochem 202 (1991) 849-854
    • (1991) Eur J Biochem , vol.202 , pp. 849-854
    • Agerberth, B.1    Lee, J.Y.2    Bergman, T.3    Carlquist, M.4    Boman, H.G.5    Mutt, V.6
  • 32
    • 0029295070 scopus 로고
    • Determination of disulphide bridges in PG-2, an antimicrobial peptide from porcine leukocytes
    • Harwig S.S., Swiderek K.M., Lee T.D., and Lehrer R.I. Determination of disulphide bridges in PG-2, an antimicrobial peptide from porcine leukocytes. J Pept Sci 1 (1995) 207-215
    • (1995) J Pept Sci , vol.1 , pp. 207-215
    • Harwig, S.S.1    Swiderek, K.M.2    Lee, T.D.3    Lehrer, R.I.4
  • 33
    • 0023700978 scopus 로고
    • Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus)
    • Nakamura T., Furunaka H., Miyata T., Tokunaga F., Muta T., Niwa M., et al. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). J Biol Chem 263 (1988) 16709-16713
    • (1988) J Biol Chem , vol.263 , pp. 16709-16713
    • Nakamura, T.1    Furunaka, H.2    Miyata, T.3    Tokunaga, F.4    Muta, T.5    Niwa, M.6
  • 34
    • 0024741960 scopus 로고
    • Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activities
    • Miyata T., Tokunaga F., Yoneya T., Yoshikawa K., Iwanaga S., Niwa M., et al. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activities. J Biochem 106 (1989) 663-668
    • (1989) J Biochem , vol.106 , pp. 663-668
    • Miyata, T.1    Tokunaga, F.2    Yoneya, T.3    Yoshikawa, K.4    Iwanaga, S.5    Niwa, M.6
  • 36
    • 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
    • Silva Jr. P.I., Daffre S., and Bulet P. 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 (2000) 33464-33470
    • (2000) J Biol Chem , vol.275 , pp. 33464-33470
    • Silva Jr., P.I.1    Daffre, S.2    Bulet, P.3
  • 37
    • 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., Dorsselaer A.V., Rodriguez J., and Bachère E. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda). J Biol Chem 272 (1997) 28398-28406
    • (1997) J Biol Chem , vol.272 , pp. 28398-28406
    • Destoumieux, D.1    Bulet, P.2    Loew, D.3    Dorsselaer, A.V.4    Rodriguez, J.5    Bachère, E.6
  • 38
    • 0027216093 scopus 로고
    • Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine
    • Boman H.G., Agerberth B., and Boman A. Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Infect Immun 61 (1993) 2978-2984
    • (1993) Infect Immun , vol.61 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 39
    • 0028286667 scopus 로고
    • Apidaecin-type peptide antibiotics function through a nonporeforming mechanism involving stereospecificity
    • Casteels P., and Tempst P. Apidaecin-type peptide antibiotics function through a nonporeforming mechanism involving stereospecificity. Biochem Biophys Res Comm 199 (1994) 339-345
    • (1994) Biochem Biophys Res Comm , vol.199 , pp. 339-345
    • Casteels, P.1    Tempst, P.2
  • 40
    • 18544379571 scopus 로고    scopus 로고
    • Identification of crucial residues for the antibacterial activity of the proline-rich peptide, pyrrhocoricin
    • Kragol G., Hoffmann R., Chattergoon M.A., Lovas S., Cudic M., Bulet P., et al. Identification of crucial residues for the antibacterial activity of the proline-rich peptide, pyrrhocoricin. Eur J Biochem 269 (2002) 4226-4237
    • (2002) Eur J Biochem , vol.269 , pp. 4226-4237
    • Kragol, G.1    Hoffmann, R.2    Chattergoon, M.A.3    Lovas, S.4    Cudic, M.5    Bulet, P.6
  • 41
    • 0030449497 scopus 로고    scopus 로고
    • Endogenous vertebrate antibiotics. Defensins, protegrins, and other cysteine-rich antimicrobial peptides
    • Lehrer R.I., and Ganz T. Endogenous vertebrate antibiotics. Defensins, protegrins, and other cysteine-rich antimicrobial peptides. Ann N Y Acad Sci 797 (1996) 228-239
    • (1996) Ann N Y Acad Sci , vol.797 , pp. 228-239
    • Lehrer, R.I.1    Ganz, T.2
  • 42
    • 0141591738 scopus 로고    scopus 로고
    • Solution structure of the recombinant penaeidin-3, a shrimp antimicrobial peptide
    • Yang Y., Poncet J., Garnier J., Zatylny C., Bachère E., and Aumelas A. Solution structure of the recombinant penaeidin-3, a shrimp antimicrobial peptide. J Biol Chem 278 (2003) 36859-36867
    • (2003) J Biol Chem , vol.278 , pp. 36859-36867
    • Yang, Y.1    Poncet, J.2    Garnier, J.3    Zatylny, C.4    Bachère, E.5    Aumelas, A.6
  • 43
    • 0029020955 scopus 로고
    • A novel big defensin identified in horseshoe crab hemocytes: isolation, amino acid sequence, and antimicrobial activity
    • Saito T., Kawabata S., Shigenaga T., Takayenoki Y., Cho J., Nakajima H., et al. A novel big defensin identified in horseshoe crab hemocytes: isolation, amino acid sequence, and antimicrobial activity. J Biochem 117 (1995) 1131-1137
    • (1995) J Biochem , vol.117 , pp. 1131-1137
    • Saito, T.1    Kawabata, S.2    Shigenaga, T.3    Takayenoki, Y.4    Cho, J.5    Nakajima, H.6
  • 44
    • 0025308541 scopus 로고
    • Tachyplesins isolated from hemocytes of southeast aias horseshoe crabs (carcinoscorpius rotundicauda and Tachypleus gigas): identification of a new tachyplesin, tachyplesin III, and a processing intermediate of its precursor
    • Muta T., Fujimoto T., Nakajima H., and Iwanaga S. Tachyplesins isolated from hemocytes of southeast aias horseshoe crabs (carcinoscorpius rotundicauda and Tachypleus gigas): identification of a new tachyplesin, tachyplesin III, and a processing intermediate of its precursor. J Biochem 108 (1990) 261-266
    • (1990) J Biochem , vol.108 , pp. 261-266
    • Muta, T.1    Fujimoto, T.2    Nakajima, H.3    Iwanaga, S.4
  • 45
    • 0025644655 scopus 로고
    • Antimicrobial tachyplesin peptide precursor. cDNA cloning and cellular localization in the horseshoe crab (Tachypleus tridentatus)
    • Shigenaga T., Muta T., Toh Y., Tokonaga F., and Iwanaga S. Antimicrobial tachyplesin peptide precursor. cDNA cloning and cellular localization in the horseshoe crab (Tachypleus tridentatus). J Biol Chem 265 (1990) 21350-21354
    • (1990) J Biol Chem , vol.265 , pp. 21350-21354
    • Shigenaga, T.1    Muta, T.2    Toh, Y.3    Tokonaga, F.4    Iwanaga, S.5
  • 46
    • 0033490117 scopus 로고    scopus 로고
    • Mussel defensins are synthesised and processed in granulocytes then released into the plasma after bacterial challenge
    • Mitta G., Vandenbulcke F., Hubert F., and Roch P. Mussel defensins are synthesised and processed in granulocytes then released into the plasma after bacterial challenge. J Cell Sci 112 (1999) 4233-4242
    • (1999) J Cell Sci , vol.112 , pp. 4233-4242
    • Mitta, G.1    Vandenbulcke, F.2    Hubert, F.3    Roch, P.4
  • 47
    • 0029810861 scopus 로고    scopus 로고
    • Innate immunity. Isolation of several cystein-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis
    • Charlet M., Chernysh S., Philippe H., Hetru C., Hoffmann J.A., and Bulet P. Innate immunity. Isolation of several cystein-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis. J Biol Chem 271 (1996) 21808-21813
    • (1996) J Biol Chem , vol.271 , pp. 21808-21813
    • Charlet, M.1    Chernysh, S.2    Philippe, H.3    Hetru, C.4    Hoffmann, J.A.5    Bulet, P.6
  • 48
    • 0034725121 scopus 로고    scopus 로고
    • Involvement of mytilins in mussel antimicrobial defense
    • Mitta G., Vandenbulcke F., Hubert F., Salzet M., and Roch P. Involvement of mytilins in mussel antimicrobial defense. J Biol Chem 275 (2000) 12954-12962
    • (2000) J Biol Chem , vol.275 , pp. 12954-12962
    • Mitta, G.1    Vandenbulcke, F.2    Hubert, F.3    Salzet, M.4    Roch, P.5
  • 49
    • 0033022730 scopus 로고    scopus 로고
    • Antimicrobial peptides in insects; structure and function
    • Bulet P., Hetru C., Dimarcq J.L., and Hoffmann D. Antimicrobial peptides in insects; structure and function. Dev Comp Immunol 23 (1999) 329-344
    • (1999) Dev Comp Immunol , vol.23 , pp. 329-344
    • Bulet, P.1    Hetru, C.2    Dimarcq, J.L.3    Hoffmann, D.4
  • 50
    • 7544244554 scopus 로고    scopus 로고
    • Cloning of kuruma prawn Marsupenaeus japonicus crustin-like peptide cDNA and analysis of its expressiony
    • Rattanachai A., Hirono I., Ohira T., Takahashi Y., and Aoki T. Cloning of kuruma prawn Marsupenaeus japonicus crustin-like peptide cDNA and analysis of its expressiony. Fisheries Sci 70 (2004) 765-771
    • (2004) Fisheries Sci , vol.70 , pp. 765-771
    • Rattanachai, A.1    Hirono, I.2    Ohira, T.3    Takahashi, Y.4    Aoki, T.5
  • 51
    • 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 (2004) 513-525
    • (2004) Fish Shellfish Immunol , vol.16 , 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
  • 52
    • 0036274247 scopus 로고    scopus 로고
    • Expression and distribution of penaeidin antimicrobial peptides are regulated by haemocyte reactions in microbial challenged shrimp
    • Munoz M., Vandenbulcke F., Saulnier D., and Bachère E. Expression and distribution of penaeidin antimicrobial peptides are regulated by haemocyte reactions in microbial challenged shrimp. Eur J Biochem 269 (2002) 2678-2689
    • (2002) Eur J Biochem , vol.269 , pp. 2678-2689
    • Munoz, M.1    Vandenbulcke, F.2    Saulnier, D.3    Bachère, E.4
  • 53
    • 0032005367 scopus 로고    scopus 로고
    • Role of the prophenoloxidase-activating system in invertebrate immunity
    • Söderhäll K., and Cerenius L. Role of the prophenoloxidase-activating system in invertebrate immunity. Curr Opin Immunol 10 (1998) 23-28
    • (1998) Curr Opin Immunol , vol.10 , pp. 23-28
    • Söderhäll, K.1    Cerenius, L.2


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