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Volumn 211, Issue 4, 2006, Pages 315-322

Host defence peptides from invertebrates - emerging antimicrobial strategies

Author keywords

Antibiotics; Antimicrobial peptides; Cationic peptides; Innate immunity; Invertebrate immunity

Indexed keywords

ANTIFUNGAL AGENT; ANTIINFECTIVE AGENT; CATHELICIDIN; CATION; DEFENSIN; HELIOMYCIN DERIVATIVE; IMMUNOMODULATING AGENT; PATTERN RECOGNITION RECEPTOR; PEPTIDE DERIVATIVE; POLYPEPTIDE ANTIBIOTIC AGENT; POLYPHEMUSIN; SAPECIN B DERIVATIVE; SERINE PROTEINASE; SYNTHETIC PEPTIDE; TACHYCITIN; TACHYPLESIN; UNCLASSIFIED DRUG;

EID: 33646532402     PISSN: 01712985     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.imbio.2005.10.017     Document Type: Review
Times cited : (238)

References (56)
  • 1
    • 1642422727 scopus 로고    scopus 로고
    • Insights into the antimicrobial 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 antimicrobial 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
  • 2
    • 0029730738 scopus 로고    scopus 로고
    • A conserved signalling pathway: the Drosophila Toll-dorsal pathway
    • Belvin M.P., and Anderson K.V. A conserved signalling pathway: the Drosophila Toll-dorsal pathway. Annu. Rev. Cell Dev. Biol. 12 (1996) 393-416
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 393-416
    • Belvin, M.P.1    Anderson, K.V.2
  • 4
    • 1642545489 scopus 로고    scopus 로고
    • Antimicrobial peptides: from invertebrates to vertebrates
    • Bulet P., Stocklin R., and Menin L. Antimicrobial peptides: from invertebrates to vertebrates. Immunol. Rev. 198 (2004) 169-184
    • (2004) Immunol. Rev. , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 5
    • 0033572799 scopus 로고    scopus 로고
    • Activation of human neutrophils by a synthetic antimicrobial peptide, KLKLLLLLKLK-NH2, via cell surface calreticulin
    • Cho J.H., Homma K., Kanegasaki S., and Nato S. Activation of human neutrophils by a synthetic antimicrobial peptide, KLKLLLLLKLK-NH2, via cell surface calreticulin. Eur. J. Biochem. 266 (1999) 878-885
    • (1999) Eur. J. Biochem. , vol.266 , pp. 878-885
    • Cho, J.H.1    Homma, K.2    Kanegasaki, S.3    Nato, S.4
  • 7
    • 0002993113 scopus 로고    scopus 로고
    • Insect immune gene regulation
    • Brey P.T., and Hultmark D. (Eds), Chapman and Hall, London
    • Engstrom Y. Insect immune gene regulation. In: Brey P.T., and Hultmark D. (Eds). Molecular Mechanism of Immune Responses In Insects (1998), Chapman and Hall, London 211-244
    • (1998) Molecular Mechanism of Immune Responses In Insects , pp. 211-244
    • Engstrom, Y.1
  • 8
    • 2942670459 scopus 로고    scopus 로고
    • Can innate immunity be enhanced to treat microbial infections?
    • Finlay B.B., and Hancock R.E.W. Can innate immunity be enhanced to treat microbial infections?. Nat. Rev. Microbiol. 2 (2004) 497-504
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 497-504
    • Finlay, B.B.1    Hancock, R.E.W.2
  • 9
    • 0029824838 scopus 로고    scopus 로고
    • Antiendotoxin activity of cationic peptide antimicrobial agents
    • Gough M., Hancock R.E.W., and Kelly N.M. Antiendotoxin activity of cationic peptide antimicrobial agents. Infect. Immun. 64 (1996) 4922-4927
    • (1996) Infect. Immun. , vol.64 , pp. 4922-4927
    • Gough, M.1    Hancock, R.E.W.2    Kelly, N.M.3
  • 11
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defences
    • Hancock R.E.W., and Diamond G. The role of cationic antimicrobial peptides in innate host defences. Trends Microbiol 9 (2000) 402-410
    • (2000) Trends Microbiol , vol.9 , pp. 402-410
    • Hancock, R.E.W.1    Diamond, G.2
  • 12
    • 0035984978 scopus 로고    scopus 로고
    • Clinical development of cationic antimicrobial peptides: from natural to novel antibiotics
    • Hancock R.E.W., and Patrzykat A. Clinical development of cationic antimicrobial peptides: from natural to novel antibiotics. Curr. Drug Targets 2 (2002) 79-83
    • (2002) Curr. Drug Targets , vol.2 , pp. 79-83
    • Hancock, R.E.W.1    Patrzykat, A.2
  • 13
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • Hancock R.E.W., and Rozek A. Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol. Lett. 206 (2002) 143-149
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 143-149
    • Hancock, R.E.W.1    Rozek, A.2
  • 15
    • 23444451770 scopus 로고    scopus 로고
    • High-throughput generation of small antibacterial peptides with improved activity
    • Hilpert K., Volkmer-Engert R., Walter T., and Hancock R.E.W. High-throughput generation of small antibacterial peptides with improved activity. Nat. Biotech. 23 (2005) 1008-1012
    • (2005) Nat. Biotech. , vol.23 , pp. 1008-1012
    • Hilpert, K.1    Volkmer-Engert, R.2    Walter, T.3    Hancock, R.E.W.4
  • 16
    • 0037012956 scopus 로고    scopus 로고
    • Specific interactions of the antimicrobial peptide cyclic B-sheet tachyplesin I with lipopolysaccharides
    • Hirakura Y., Kobayashi S., and Matsuzaki M. Specific interactions of the antimicrobial peptide cyclic B-sheet tachyplesin I with lipopolysaccharides. Biochim. Biophys. Acta 1562 (2002) 32-36
    • (2002) Biochim. Biophys. Acta , vol.1562 , pp. 32-36
    • Hirakura, Y.1    Kobayashi, S.2    Matsuzaki, M.3
  • 17
    • 0242581687 scopus 로고    scopus 로고
    • The immune response of Drosophila
    • Hoffmann J.A. The immune response of Drosophila. Nature 426 (2003) 33-38
    • (2003) Nature , vol.426 , pp. 33-38
    • Hoffmann, J.A.1
  • 18
    • 1642504763 scopus 로고    scopus 로고
    • Primitive immune systems
    • Hoffmann J.A. Primitive immune systems. Immunol. Rev. 198 (2004) 5-9
    • (2004) Immunol. Rev. , vol.198 , pp. 5-9
    • Hoffmann, J.A.1
  • 19
    • 0036167107 scopus 로고    scopus 로고
    • Drosophila innate immunity: an evolutionary perspective
    • Hoffmann J.A., and Reichhart J. Drosophila innate immunity: an evolutionary perspective. Nat. Immunol 3 (2002) 121-126
    • (2002) Nat. Immunol , vol.3 , pp. 121-126
    • Hoffmann, J.A.1    Reichhart, J.2
  • 20
    • 0037228233 scopus 로고    scopus 로고
    • Transcriptional profile of the Escherichia coli response to the antimicrobial insect peptide cecropin A
    • Hong R.W., Shchepetov M., Weiser J.N., and Axelsen P.H. Transcriptional profile of the Escherichia coli response to the antimicrobial insect peptide cecropin A. Antimicrob. Agents Chemother. 47 (2003) 1-6
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 1-6
    • Hong, R.W.1    Shchepetov, M.2    Weiser, J.N.3    Axelsen, P.H.4
  • 21
    • 0033973826 scopus 로고    scopus 로고
    • Signaling mechanism in the antimicrobial defense of Drosophila
    • Imler J.L., and Hoffmann J.A. Signaling mechanism in the antimicrobial defense of Drosophila. Curr. Opin. Microbiol. 3 (2000) 16-22
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 16-22
    • Imler, J.L.1    Hoffmann, J.A.2
  • 22
    • 0032159526 scopus 로고    scopus 로고
    • Evolution and phylogeny of defense molecules associated with innate immunity in horseshoe crab
    • Iwanaga S., and Kawabata S. Evolution and phylogeny of defense molecules associated with innate immunity in horseshoe crab. Front. Biosci. 3 (1998) D973-D984
    • (1998) Front. Biosci. , vol.3
    • Iwanaga, S.1    Kawabata, S.2
  • 23
    • 20444506858 scopus 로고    scopus 로고
    • Recent advances in the innate immunity of invertebrate animals
    • Iwanaga S., and Lee B.L. Recent advances in the innate immunity of invertebrate animals. J. Biochem. Mol. Biol. 38 (2005) 128-150
    • (2005) J. Biochem. Mol. Biol. , vol.38 , pp. 128-150
    • Iwanaga, S.1    Lee, B.L.2
  • 24
    • 0031934614 scopus 로고    scopus 로고
    • New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structure and functions
    • Iwanaga S., Kawabata S., and Muta T. New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structure and functions. J. Biochem. 123 (1998) 1-15
    • (1998) J. Biochem. , vol.123 , pp. 1-15
    • Iwanaga, S.1    Kawabata, S.2    Muta, T.3
  • 25
    • 0035853022 scopus 로고    scopus 로고
    • The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding
    • Kragol G., Lovas S., Varadi G., Condie B.A., Hoffmann R., and Otvos Jr. L. The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding. Biochemistry 40 (2001) 3016-3026
    • (2001) Biochemistry , vol.40 , pp. 3016-3026
    • Kragol, G.1    Lovas, S.2    Varadi, G.3    Condie, B.A.4    Hoffmann, R.5    Otvos Jr., L.6
  • 26
    • 0035834050 scopus 로고    scopus 로고
    • Solution structures of the antifungal heliomicin and a selected variant with both antibacterial and antifungal activities
    • Lamberty M., Caille A., Landon C., Tassin-Moindrot S., Hetru C., Bulet P., and Vovelle F. Solution structures of the antifungal heliomicin and a selected variant with both antibacterial and antifungal activities. Biochemistry 40 (2001) 11995-12003
    • (2001) Biochemistry , vol.40 , pp. 11995-12003
    • Lamberty, M.1    Caille, A.2    Landon, C.3    Tassin-Moindrot, S.4    Hetru, C.5    Bulet, P.6    Vovelle, F.7
  • 28
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defense
    • Lehrer R.I., and Ganz T. Antimicrobial peptides in mammalian and insect host defense. Curr. Opin. Immunol. 11 (1999) 23-27
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 23-27
    • Lehrer, R.I.1    Ganz, T.2
  • 29
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults
    • Lemaitre B., Nicholas E., Michaut L., Reichhart J.M., and Hoffmann J.A. The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 86 (1996) 973-983
    • (1996) Cell , vol.86 , pp. 973-983
    • Lemaitre, B.1    Nicholas, E.2    Michaut, L.3    Reichhart, J.M.4    Hoffmann, J.A.5
  • 30
    • 17644433467 scopus 로고    scopus 로고
    • Strong synergy between a eukaryotic antimicrobial peptide and bacteriocins from lactic acid bacteria
    • Luders T., Birkemo G.A., Fimland G., Nissen-Meyer J., and Nes I.F. Strong synergy between a eukaryotic antimicrobial peptide and bacteriocins from lactic acid bacteria. Appl. Environ. Microbiol. 69 (2003) 1797-1799
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 1797-1799
    • Luders, T.1    Birkemo, G.A.2    Fimland, G.3    Nissen-Meyer, J.4    Nes, I.F.5
  • 32
    • 0033214630 scopus 로고    scopus 로고
    • Myticin a novel cysteine-rich antimicrobial peptide isolated from hemocytes and plasma of mussel Mytilus galloprovincialis
    • Mitta G., Hubert F., Noel T., and Roch P. Myticin a novel cysteine-rich antimicrobial peptide isolated from hemocytes and plasma of mussel Mytilus galloprovincialis. Eur. J. Biochem. 264 (1999) 1-9
    • (1999) Eur. J. Biochem. , vol.264 , pp. 1-9
    • Mitta, G.1    Hubert, F.2    Noel, T.3    Roch, P.4
  • 34
    • 0001649653 scopus 로고    scopus 로고
    • In vitro activity of the Limulus antimicrobial peptide tachyplesin I on marine bivalve pathogens
    • Morvan A., Iwanaga S., Comps M., and Bachere E. In vitro activity of the Limulus antimicrobial peptide tachyplesin I on marine bivalve pathogens. J. Invertebr. Pathol. 69 (1997) 177-182
    • (1997) J. Invertebr. Pathol. , vol.69 , pp. 177-182
    • Morvan, A.1    Iwanaga, S.2    Comps, M.3    Bachere, E.4
  • 35
    • 0030756736 scopus 로고    scopus 로고
    • Chemotherapeutic activity of synthetic antimicrobial peptides: correlation between chemotherapeutic activity and neutrophil-activating activity
    • Nakajima Y., Alvarez-Bravo J., Cho J.H., Homma K.I., Kanegasaki S., and Natori S. Chemotherapeutic activity of synthetic antimicrobial peptides: correlation between chemotherapeutic activity and neutrophil-activating activity. FEBS Lett 415 (1997) 64-66
    • (1997) FEBS Lett , vol.415 , pp. 64-66
    • Nakajima, Y.1    Alvarez-Bravo, J.2    Cho, J.H.3    Homma, K.I.4    Kanegasaki, S.5    Natori, S.6
  • 36
    • 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., and Iwanaga S. 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    Iwanaga, S.6
  • 37
    • 0021764392 scopus 로고
    • Anti-LPS factor in the horseshoe crab, Tachypleus tridentatus: its hemolytic activity on the red blood cell sensitized with lipopolysaccharide
    • Ohashi M.K., Niwa T., Nakamura T., Morita T., and Iwanaga S. Anti-LPS factor in the horseshoe crab, Tachypleus tridentatus: its hemolytic activity on the red blood cell sensitized with lipopolysaccharide. FEBS Lett 176 (1984) 207-210
    • (1984) FEBS Lett , vol.176 , pp. 207-210
    • Ohashi, M.K.1    Niwa, T.2    Nakamura, T.3    Morita, T.4    Iwanaga, S.5
  • 38
    • 0036168570 scopus 로고    scopus 로고
    • Sublethal Concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in E. coli
    • Patrzykat A., Friedrich C.L., Zhang L., Mendoza V., and Hancock R.E.W. Sublethal Concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in E. coli. Antimicrob. Agents Chemother. 46 (2002) 605-614
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 605-614
    • Patrzykat, A.1    Friedrich, C.L.2    Zhang, L.3    Mendoza, V.4    Hancock, R.E.W.5
  • 39
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers J.P., and Hancock R.E.W. The relationship between peptide structure and antibacterial activity. Peptides 24 (2004) 1681-1691
    • (2004) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.W.2
  • 40
    • 0031239636 scopus 로고    scopus 로고
    • Interleukin 2 promoter/enhancer controlled expression of a synthetic cecropin-class lytic peptide in transgenic mice and subsequent resistance to Brucella abortus
    • Reed W.A., Elzer P.H., Enright F.M., Jaynes J.M., Morrey J.D., and White K.L. Interleukin 2 promoter/enhancer controlled expression of a synthetic cecropin-class lytic peptide in transgenic mice and subsequent resistance to Brucella abortus. Transgenic Res 6 (1997) 337-347
    • (1997) Transgenic Res , vol.6 , pp. 337-347
    • Reed, W.A.1    Elzer, P.H.2    Enright, F.M.3    Jaynes, J.M.4    Morrey, J.D.5    White, K.L.6
  • 41
    • 0034913684 scopus 로고    scopus 로고
    • Vertebrate innate immunity resembles a mosaic of invertebrate immune responses
    • Salzet M. Vertebrate innate immunity resembles a mosaic of invertebrate immune responses. Trends Immunol 22 (2001) 285-288
    • (2001) Trends Immunol , vol.22 , pp. 285-288
    • Salzet, M.1
  • 42
    • 0035660908 scopus 로고    scopus 로고
    • Neuroimmunology of opioids from invertebrates to humans
    • Salzet M. Neuroimmunology of opioids from invertebrates to humans. Neuroendocrinol. Letts. 22 (2001) 467-474
    • (2001) Neuroendocrinol. Letts. , vol.22 , pp. 467-474
    • Salzet, M.1
  • 43
    • 0036607940 scopus 로고    scopus 로고
    • Antimicrobial peptides are signaling molecules
    • Salzet M. Antimicrobial peptides are signaling molecules. Trends Immunol 23 (2002) 283-284
    • (2002) Trends Immunol , vol.23 , pp. 283-284
    • Salzet, M.1
  • 44
    • 0034665513 scopus 로고    scopus 로고
    • An α-helical cationic antimicrobial peptide selectively modulates macrophage response to LPS and directly alters macrophage gene expression
    • Scott M.G., Rosenberger C.M., Gold M.R., Finlay B.B., and Hancock R.E.W. An α-helical cationic antimicrobial peptide selectively modulates macrophage response to LPS and directly alters macrophage gene expression. J. Immunol. 165 (2000) 3358-3365
    • (2000) J. Immunol. , vol.165 , pp. 3358-3365
    • Scott, M.G.1    Rosenberger, C.M.2    Gold, M.R.3    Finlay, B.B.4    Hancock, R.E.W.5
  • 45
    • 0036785559 scopus 로고    scopus 로고
    • The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses
    • Scott M.G., Davidson D.J., Gold M.R., Bowdish D.M., and Hancock R.E.W. The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses. J. Immunol. 169 (2002) 3883-3891
    • (2002) J. Immunol. , vol.169 , pp. 3883-3891
    • Scott, M.G.1    Davidson, D.J.2    Gold, M.R.3    Bowdish, D.M.4    Hancock, R.E.W.5
  • 46
    • 0019386682 scopus 로고
    • Sequence and specificity of two antimicrobial proteins in insect immunity
    • Steiner H., Hultmark D., Engstrom A., Bennich H., and Boman H.G. Sequence and specificity of two antimicrobial proteins in insect immunity. Nature 292 (1981) 246-248
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 47
    • 0343092000 scopus 로고    scopus 로고
    • High affinity LPS binding domain(s) in recombinant Factor C of a horseshoe crab neutralizes LPS-induced lethality
    • Tan N.S., Ho B., and Ding J.L. High affinity LPS binding domain(s) in recombinant Factor C of a horseshoe crab neutralizes LPS-induced lethality. FASEB J 14 (2000) 859-887
    • (2000) FASEB J , vol.14 , pp. 859-887
    • Tan, N.S.1    Ho, B.2    Ding, J.L.3
  • 48
    • 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
    • Tan N.S., Ng M.L.P., Yau Y.H., Chong P.K.W., Ho B., and Ding J.L. Definition of endotoxin binding sites in horseshoe crab Factor C recombinant sushi proteins and neutralization of endotoxin by sushi peptides. FASEB J 14 (2000) 1801-1813
    • (2000) FASEB J , vol.14 , pp. 1801-1813
    • Tan, N.S.1    Ng, M.L.P.2    Yau, Y.H.3    Chong, P.K.W.4    Ho, B.5    Ding, J.L.6
  • 49
    • 0020416253 scopus 로고
    • Limulus anti-LPS factor: an anticoagulant which inhibits the endotoxin-mediated activation of Limulus coagulation system
    • Tanaka S.T., Nakamura T., Morita T., and Iwanaga S. Limulus anti-LPS factor: an anticoagulant which inhibits the endotoxin-mediated activation of Limulus coagulation system. Biochem. Biophys. Res. Commun. 105 (1982) 717-723
    • (1982) Biochem. Biophys. Res. Commun. , vol.105 , pp. 717-723
    • Tanaka, S.T.1    Nakamura, T.2    Morita, T.3    Iwanaga, S.4
  • 50
    • 4644311383 scopus 로고    scopus 로고
    • Antimicrobial peptides from marine invertebrate
    • Tincu J.A., and Taylor S.W. Antimicrobial peptides from marine invertebrate. Antimicrob. Agents Chemother. 48 (2004) 3645-3654
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 3645-3654
    • Tincu, J.A.1    Taylor, S.W.2
  • 51
    • 0033941532 scopus 로고    scopus 로고
    • A Limulus antilipopolysaccharide factor-derived peptide exhibits a new immunological activity with potential applicability in infectious diseases
    • Vallespi M.G., Glaria L.A., Reyes O., Garray H.E., Ferrero J., and Araña M.J. A Limulus antilipopolysaccharide factor-derived peptide exhibits a new immunological activity with potential applicability in infectious diseases. Clin. Diagn. Lab. Immunol. 7 (2000) 669-675
    • (2000) Clin. Diagn. Lab. Immunol. , vol.7 , pp. 669-675
    • Vallespi, M.G.1    Glaria, L.A.2    Reyes, O.3    Garray, H.E.4    Ferrero, J.5    Araña, M.J.6
  • 52
    • 0037317595 scopus 로고    scopus 로고
    • A Limulus anti-LPS factor-derived peptide modulates cytokine gene expression and promotes resolution of bacterial acute infection in mice
    • Vallespi M.G., Alvarez-Obregon J.C., Rodriguez-Alonso I., Montero T., Garay H., Reyes O., and Arana M.J. A Limulus anti-LPS factor-derived peptide modulates cytokine gene expression and promotes resolution of bacterial acute infection in mice. Int. Immunopharmacol. 3 (2003) 247-256
    • (2003) Int. Immunopharmacol. , vol.3 , pp. 247-256
    • Vallespi, M.G.1    Alvarez-Obregon, J.C.2    Rodriguez-Alonso, I.3    Montero, T.4    Garay, H.5    Reyes, O.6    Arana, M.J.7
  • 53
    • 0035059407 scopus 로고    scopus 로고
    • Properties of the prophenoloxidase activating enzyme of the freshwater crayfish, Pacifastacus leniusculus
    • Wang R., Lee S.Y., Cerenius L., and Söderhäll K. Properties of the prophenoloxidase activating enzyme of the freshwater crayfish, Pacifastacus leniusculus. Eur. J. Biochem. 268 (2001) 895-902
    • (2001) Eur. J. Biochem. , vol.268 , pp. 895-902
    • Wang, R.1    Lee, S.Y.2    Cerenius, L.3    Söderhäll, K.4
  • 54
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 55
    • 84939584807 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides - an update
    • Zhang L., and Falla T.J. Cationic antimicrobial peptides - an update. Expert Opin. Invest Drugs 9 (2004) 1723-1729
    • (2004) Expert Opin. Invest Drugs , vol.9 , pp. 1723-1729
    • Zhang, L.1    Falla, T.J.2
  • 56
    • 0034727645 scopus 로고    scopus 로고
    • Interaction of polyphemusin I and structural analogs with bacterial membranes, lipopolysaccharide, and lipid monolayers
    • Zhang L., Scott M.G., Yan H., Mayer L.D., and Hancock R.E.W. Interaction of polyphemusin I and structural analogs with bacterial membranes, lipopolysaccharide, and lipid monolayers. Biochemistry 39 (2000) 14504-14514
    • (2000) Biochemistry , vol.39 , pp. 14504-14514
    • Zhang, L.1    Scott, M.G.2    Yan, H.3    Mayer, L.D.4    Hancock, R.E.W.5


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