메뉴 건너뛰기




Volumn 48, Issue 1, 1998, Pages 15-25

Gene-encoded peptide antibiotics and the concept of innate immunity: An update review

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE ANTIBIOTIC AGENT;

EID: 0031821708     PISSN: 03009475     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-3083.1998.00343.x     Document Type: Article
Times cited : (206)

References (97)
  • 1
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman HG. Peptide antibiotics and their role in innate immunity. Annu Rev Immun 1995;13:61-92.
    • (1995) Annu Rev Immun , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 2
    • 0029971979 scopus 로고    scopus 로고
    • Peptide antibiotics: Holy or heretic grails of innate immunity?
    • Boman H. Peptide antibiotics: holy or heretic grails of innate immunity? Scand J Immunol 1996;43:475-82.
    • (1996) Scand J Immunol , vol.43 , pp. 475-482
    • Boman, H.1
  • 6
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H, Hultmark D, Engström Å, Bennich H, Boman H.G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 1981;292:246-248.
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engström, Å.3    Bennich, H.4    Boman, H.G.5
  • 7
    • 0021032178 scopus 로고
    • Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages
    • Selsted M.E, Brown DM, DeLange R, Lehrer RI. Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages. J Biol Chem 1983;258:14485-9.
    • (1983) J Biol Chem , vol.258 , pp. 14485-14489
    • Selsted, M.E.1    Brown, D.M.2    DeLange, R.3    Lehrer, R.I.4
  • 9
    • 0001386491 scopus 로고
    • Antimicrobial Peptides
    • Chichester, PO19 IUD, UK: John Wiley & Sons Ltd
    • Boman HG, March J, Goode, J. eds. Antimicrobial Peptides. Ciba Symposium No. 186. Chichester, PO19 IUD, UK: John Wiley & Sons Ltd, 1994.
    • (1994) Ciba Symposium No. 186
    • Boman, H.G.1    March, J.2    Goode, J.3
  • 10
    • 0028964136 scopus 로고
    • Defensins in granules and non-phagocytic cells
    • Selsted ME, Ouellette AJ. Defensins in granules and non-phagocytic cells. Trends Cell Biol 1995;5:114-9.
    • (1995) Trends Cell Biol , vol.5 , pp. 114-119
    • Selsted, M.E.1    Ouellette, A.J.2
  • 11
    • 0030861378 scopus 로고    scopus 로고
    • Antimicrobial peptides of phagocytes and epithelia
    • Ganz T, Weiss J. Antimicrobial peptides of phagocytes and epithelia. Semin Hematol 1997;34:343-54.
    • (1997) Semin Hematol , vol.34 , pp. 343-354
    • Ganz, T.1    Weiss, J.2
  • 12
    • 0004294122 scopus 로고    scopus 로고
    • Ogra PL, Mestecky J, Lamm ME, Strober WM Jr, Bienenstock J, eds. New York: Academic Press (in press)
    • Lehrer RI, Bevins CL, Ganz T, In: Ogra PL, Mestecky J, Lamm ME, Strober WM Jr, Bienenstock J, eds. Mucosal Immunology. 2nd edn. New York: Academic Press (in press).
    • Mucosal Immunology. 2nd Edn.
    • Lehrer, R.I.1    Bevins, C.L.2    Ganz, T.3
  • 13
    • 0002684129 scopus 로고    scopus 로고
    • Antibacterial peptide protocols
    • New Jersey: Humana Press
    • Shafer WM, ed. Antibacterial peptide protocols. In: Methods in Molecular Biology, Vol. 78. New Jersey: Humana Press. 1997:259 pp.
    • (1997) Methods in Molecular Biology , vol.78
    • Shafer, W.M.1
  • 14
    • 0025818448 scopus 로고
    • Antibacterial peptides: Key components needed in immunity
    • Boman HG. Antibacterial peptides: key components needed in immunity. Cell 1991;65:205-7.
    • (1991) Cell , vol.65 , pp. 205-207
    • Boman, H.G.1
  • 15
    • 0026511839 scopus 로고
    • Antibiotic peptides as mediators of innate immunity
    • Zasloff M. Antibiotic peptides as mediators of innate immunity. Curr Opin Immun 1992;4:3-7.
    • (1992) Curr Opin Immun , vol.4 , pp. 3-7
    • Zasloff, M.1
  • 16
    • 0000919390 scopus 로고    scopus 로고
    • NO contest: Nitroc oxide plays complex roles in infections
    • Fang FC. NO contest: nitroc oxide plays complex roles in infections. ASM News 1997;63:668-73.
    • (1997) ASM News , vol.63 , pp. 668-673
    • Fang, F.C.1
  • 17
    • 0029061894 scopus 로고
    • K-lysin, a novel effector peptide of cytotoxic T and NK cells. structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity
    • Andersson M, Gunne H, Agerberth B et al. K-lysin, a novel effector peptide of cytotoxic T and NK cells. structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity. EMBO J 1995;14:1615-25.
    • (1995) EMBO J , vol.14 , pp. 1615-1625
    • Andersson, M.1    Gunne, H.2    Agerberth, B.3
  • 18
    • 0029877550 scopus 로고    scopus 로고
    • Coordinate induction of two antibiotic genes in tracheal epithelial cells exposed to the inflammatory mediators lipopolysaccharide and tumor necrosis factor-∝
    • Russell JP, Diamond G, Tarver AP, Scanlin TF, Bevins CL. Coordinate induction of two antibiotic genes in tracheal epithelial cells exposed to the inflammatory mediators lipopolysaccharide and tumor necrosis factor-∝. Infect Immun 1996;64:565-8.
    • (1996) Infect Immun , vol.64 , pp. 565-568
    • Russell, J.P.1    Diamond, G.2    Tarver, A.P.3    Scanlin, T.F.4    Bevins, C.L.5
  • 19
    • 0029047938 scopus 로고
    • Amphibian skin: A promising resource for antimicrobial peptides
    • Barra D, Simmaco M. Amphibian skin: a promising resource for antimicrobial peptides. TIBTECH 1995;13:205-9.
    • (1995) TIBTECH , vol.13 , pp. 205-209
    • Barra, D.1    Simmaco, M.2
  • 22
    • 0030957967 scopus 로고    scopus 로고
    • Isolation and characterizalion of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder
    • Cole AM, Weis P, Diamond G. Isolation and characterizalion of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder. J Biol Chem 1997;272:12008-13.
    • (1997) J Biol Chem , vol.272 , pp. 12008-12013
    • Cole, A.M.1    Weis, P.2    Diamond, G.3
  • 24
    • 0030836343 scopus 로고    scopus 로고
    • cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from the tunicate. Styela clava
    • Zhao CQ, Liaw L, Lee I.H, Lehrer RI. cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from the tunicate. Styela clava. FEBS Lett 1997;412:144-8.
    • (1997) FEBS Lett , vol.412 , pp. 144-148
    • Zhao, C.Q.1    Liaw, L.2    Lee, I.H.3    Lehrer, R.I.4
  • 25
    • 0030739528 scopus 로고    scopus 로고
    • cDNA cloning of Clavanins: Antimicrobial peptides of tunicate hemocytes
    • Zhao CQ. Liaw L, Lee IH, Lehrer RI. cDNA cloning of Clavanins: antimicrobial peptides of tunicate hemocytes. FEBS Lett 1997;410:490-2.
    • (1997) FEBS Lett , vol.410 , pp. 490-492
    • Zhao, C.Q.1    Liaw, L.2    Lee, I.H.3    Lehrer, R.I.4
  • 26
    • 0029842737 scopus 로고    scopus 로고
    • A member of the arthropod defensin family from edible Mediterranean mussels (Mytilus galloprovincialis)
    • Hubert F, Noel T, Roch P. A member of the arthropod defensin family from edible Mediterranean mussels (Mytilus galloprovincialis). Eur J Biochem 1996;240:302-6.
    • (1996) Eur J Biochem , vol.240 , pp. 302-306
    • Hubert, F.1    Noel, T.2    Roch, P.3
  • 27
    • 0030012702 scopus 로고    scopus 로고
    • Antibiotic proteins of polymorphonuclear leukocytes
    • Levy O. Antibiotic proteins of polymorphonuclear leukocytes. Eur J Haematol 1996;56:263-77.
    • (1996) Eur J Haematol , vol.56 , pp. 263-277
    • Levy, O.1
  • 28
    • 0002905116 scopus 로고
    • Cecropins: Antibacterial peptides from insects and pigs
    • Hoffmann J, Natori S, Janeway C, eds. Austin: RG Landes Biomedical Publisher
    • Boman HG. Cecropins: antibacterial peptides from insects and pigs. In: Hoffmann J, Natori S, Janeway C, eds. Phylogenetic Perspectives in Immunity: The Insect-Host Defense. Austin: RG Landes Biomedical Publisher. 1994:24-37.
    • (1994) Phylogenetic Perspectives in Immunity: the Insect-Host Defense , pp. 24-37
    • Boman, H.G.1
  • 29
    • 0031006967 scopus 로고    scopus 로고
    • D-amino acids in animal peptides
    • Kreil G. D-amino acids in animal peptides. Annu Rev Biochem 1997;66:337-45.
    • (1997) Annu Rev Biochem , vol.66 , pp. 337-345
    • Kreil, G.1
  • 30
    • 0031451521 scopus 로고    scopus 로고
    • Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity
    • Tossi A, Tarantino C, Romeo D. Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity. Eur J Biochem 1997;250:549-58.
    • (1997) Eur J Biochem , vol.250 , pp. 549-558
    • Tossi, A.1    Tarantino, C.2    Romeo, D.3
  • 31
    • 0000378555 scopus 로고    scopus 로고
    • Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 2 and cecropin A-melittin hybrid peptides
    • Shin SY, Lee MK, Kim KL, Hahm KS. Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 2 and cecropin A-melittin hybrid peptides. J Pept Res 1997;50:279-85.
    • (1997) J Pept Res , vol.50 , pp. 279-285
    • Shin, S.Y.1    Lee, M.K.2    Kim, K.L.3    Hahm, K.S.4
  • 32
    • 0024331982 scopus 로고
    • H.G. Antibacterial peptides from pig intestine: Isolation of a mammalian cecropin
    • Lee J-Y, Boman A, Sun C et al. H.G. Antibacterial peptides from pig intestine: Isolation of a mammalian cecropin. Proc Natl Acad Sci USA 1989;86:9159-62.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9159-9162
    • Lee, J.-Y.1    Boman, A.2    Sun, C.3
  • 33
    • 0030007916 scopus 로고    scopus 로고
    • Formation of pores in Escherichia coli cell membranes by a cecropin isolated from hemolymph of Heliothis virescens larvae
    • Lockey TD, Ourth DD. Formation of pores in Escherichia coli cell membranes by a cecropin isolated from hemolymph of Heliothis virescens larvae. Eur J Biochem 1996;236:263-71.
    • (1996) Eur J Biochem , vol.236 , pp. 263-271
    • Lockey, T.D.1    Ourth, D.D.2
  • 34
    • 0030071417 scopus 로고    scopus 로고
    • Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides
    • Fehlbaum P, Bulet P, Chernysh S et al. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proc Nail Acad Sci USA 1996;93:1221-5.
    • (1996) Proc Nail Acad Sci USA , vol.93 , pp. 1221-1225
    • Fehlbaum, P.1    Bulet, P.2    Chernysh, S.3
  • 35
    • 0031203411 scopus 로고    scopus 로고
    • Sensitivity of periodontal pathogens to the bactericidal activity of synthetic protegrins, antibiotic peptides derived from porcine leukocytes
    • Miyasaki KT, Iofel R, Lehrer RI. Sensitivity of periodontal pathogens to the bactericidal activity of synthetic protegrins, antibiotic peptides derived from porcine leukocytes. J Dent Res 1997;76:1453-9.
    • (1997) J Dent Res , vol.76 , pp. 1453-1459
    • Miyasaki, K.T.1    Iofel, R.2    Lehrer, R.I.3
  • 36
    • 0029978338 scopus 로고    scopus 로고
    • Intramolecular inhibition of human defensin HNP-1 by its propiece
    • Valore EV, Martin E, Harwig SSL, Ganz T. Intramolecular inhibition of human defensin HNP-1 by its propiece. J Clin Invest 1996;97:1624-9.
    • (1996) J Clin Invest , vol.97 , pp. 1624-1629
    • Valore, E.V.1    Martin, E.2    Harwig, S.S.L.3    Ganz, T.4
  • 37
    • 0030052689 scopus 로고    scopus 로고
    • Distinct temporal patterns of defensin mRNA regulation during drug-induced differentiation of human myeloid leukemia cells
    • Herwig S, Su Q, Zhang W, Ma Y, Tempst P. Distinct temporal patterns of defensin mRNA regulation during drug-induced differentiation of human myeloid leukemia cells. Blood 1996;87:350-64.
    • (1996) Blood , vol.87 , pp. 350-364
    • Herwig, S.1    Su, Q.2    Zhang, W.3    Ma, Y.4    Tempst, P.5
  • 38
    • 0030029451 scopus 로고    scopus 로고
    • Human enteric defensinsgene structure and developmental expression
    • Mallow EB, Harris A, Salzman N et al. Human enteric defensinsgene structure and developmental expression. J Biol Chem 1996;271:4038-45.
    • (1996) J Biol Chem , vol.271 , pp. 4038-4045
    • Mallow, E.B.1    Harris, A.2    Salzman, N.3
  • 39
    • 0028825285 scopus 로고
    • Solution structure of bovine neutrophil beta-defensin-12: The peptide fold of the beta-defensins is identical to that of the classical defensins
    • Zimmermann GR, Legault P, Selsted ME, Pardi A. Solution structure of bovine neutrophil beta-defensin-12: the peptide fold of the beta-defensins is identical to that of the classical defensins. Bio-chemistry 1995;34:13663-71.
    • (1995) Bio-chemistry , vol.34 , pp. 13663-13671
    • Zimmermann, G.R.1    Legault, P.2    Selsted, M.E.3    Pardi, A.4
  • 40
    • 0030949875 scopus 로고    scopus 로고
    • Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • Goldman MJ, Anderson GM, Stolzenberg ED, Kari UP, Zasloff M, Wilson JM. Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 1997;88:553-60.
    • (1997) Cell , vol.88 , pp. 553-560
    • Goldman, M.J.1    Anderson, G.M.2    Stolzenberg, E.D.3    Kari, U.P.4    Zasloff, M.5    Wilson, J.M.6
  • 41
    • 0030027096 scopus 로고    scopus 로고
    • Human enteric defensin genes: Chromosomal map position and a model for possible evolutionary relationships
    • Bevins CL, Jones DE, Dutra A, Schaffzin J, Muenke M. Human enteric defensin genes: chromosomal map position and a model for possible evolutionary relationships. Genomics 1996;31:95-106.
    • (1996) Genomics , vol.31 , pp. 95-106
    • Bevins, C.L.1    Jones, D.E.2    Dutra, A.3    Schaffzin, J.4    Muenke, M.5
  • 42
    • 0031213832 scopus 로고    scopus 로고
    • The human beta-defensin-I and alpha-defensins are encoded by adjacent genes: Two peptide families with differing disulfide topology share a common ancestry
    • Liu LD, Zhao CQ, Heng HHQ, Ganz T. The human beta-defensin-I and alpha-defensins are encoded by adjacent genes: two peptide families with differing disulfide topology share a common ancestry. Genomics 1997;43:316-20.
    • (1997) Genomics , vol.43 , pp. 316-320
    • Liu, L.D.1    Zhao, C.Q.2    Heng, H.H.Q.3    Ganz, T.4
  • 43
    • 0029819784 scopus 로고    scopus 로고
    • Paneth cell defensins: Endogenous peplide components of intestinal host defense
    • Ouellette AJ, Selsted ME. Paneth cell defensins: endogenous peplide components of intestinal host defense. FASEB J 1996;10:1280-9.
    • (1996) FASEB J , vol.10 , pp. 1280-1289
    • Ouellette, A.J.1    Selsted, M.E.2
  • 44
    • 0030913746 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial activity of human intestinal defensin 5
    • Porter EM, van Dam E, Valore EV, Ganz T. Broad-spectrum antimicrobial activity of human intestinal defensin 5. Infect Immun 1997;65:2396-401.
    • (1997) Infect Immun , vol.65 , pp. 2396-2401
    • Porter, E.M.1    Van Dam, E.2    Valore, E.V.3    Ganz, T.4
  • 45
    • 0029644729 scopus 로고
    • Refined three-dimentional solution structure of insect defensin
    • Cornet B, Bonmatin J-M, Hetru C et al. Refined three-dimentional solution structure of insect defensin. Curr Biol 1995;3:435-48.
    • (1995) Curr Biol , vol.3 , pp. 435-448
    • Cornet, B.1    Bonmatin, J.-M.2    Hetru, C.3
  • 47
    • 0028031219 scopus 로고
    • Molecular cloning of Bac 7, a proline- and arginine-rich antimicrobial peptide from bovine neutrophils
    • Scocchi M, Romeo D, Zanetti M. Molecular cloning of Bac 7, a proline- and arginine-rich antimicrobial peptide from bovine neutrophils. FEBS Lett 1994;352:197-200.
    • (1994) FEBS Lett , vol.352 , pp. 197-200
    • Scocchi, M.1    Romeo, D.2    Zanetti, M.3
  • 48
    • 0031009432 scopus 로고    scopus 로고
    • Identification of, a cathelinrelated antimicrobial peptide expressed in the embryonic and adult mouse
    • Gallo RL, Kim KJ, Bernfield M et al. Identification of, a cathelinrelated antimicrobial peptide expressed in the embryonic and adult mouse. J Biol Chem 1997;272:13088-93.
    • (1997) J Biol Chem , vol.272 , pp. 13088-13093
    • Gallo, R.L.1    Kim, K.J.2    Bernfield, M.3
  • 49
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti M, Gennaro R, Romeo D. Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett 1995;374:1 -5.
    • (1995) FEBS Lett , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 50
    • 0029129210 scopus 로고
    • Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: Comparative mapping of the locus for the human peptide antibiotic FALL-39
    • Gudmundsson GH, Magnusson KP, Chowdhary BP, Johansson M, Andersson L, Boman HG. Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39. Proc Natl Acad Sci USA 1995;92:7085-9.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7085-7089
    • Gudmundsson, G.H.1    Magnusson, K.P.2    Chowdhary, B.P.3    Johansson, M.4    Andersson, L.5    Boman, H.G.6
  • 51
    • 0029015666 scopus 로고
    • The structure of porcine protegrin genes
    • Zhao CQ, Ganz T, Lehrer RI. The structure of porcine protegrin genes. FEBS Lett 1995;368:197-202.
    • (1995) FEBS Lett , vol.368 , pp. 197-202
    • Zhao, C.Q.1    Ganz, T.2    Lehrer, R.I.3
  • 52
    • 0028839913 scopus 로고
    • Structures of genes for two cathelin-associated antimicrobial peptides: Prophenin-2 and PR-39
    • Zhao C, Ganz T, Lehrer RI. Structures of genes for two cathelin-associated antimicrobial peptides: prophenin-2 and PR-39. FEBS Lett 1995;376:130-4.
    • (1995) FEBS Lett , vol.376 , pp. 130-134
    • Zhao, C.1    Ganz, T.2    Lehrer, R.I.3
  • 53
    • 0029893253 scopus 로고    scopus 로고
    • The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes
    • Gudmundsson GH, Agerberth B, Odeberg J, Bergman T, Olsson B, Salcedo R. The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur J Biochem 1996;238:325-32.
    • (1996) Eur J Biochem , vol.238 , pp. 325-332
    • Gudmundsson, G.H.1    Agerberth, B.2    Odeberg, J.3    Bergman, T.4    Olsson, B.5    Salcedo, R.6
  • 54
    • 0030880531 scopus 로고    scopus 로고
    • The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils
    • Sorensen O, Arnljots K, Cowland JB, Bainton DF, Borregaard N. The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils. Blood 1997;90:2796-803.
    • (1997) Blood , vol.90 , pp. 2796-2803
    • Sorensen, O.1    Arnljots, K.2    Cowland, J.B.3    Bainton, D.F.4    Borregaard, N.5
  • 55
    • 0030997435 scopus 로고    scopus 로고
    • Granules of the human neutrophilic polymorphonuclear leukocyte
    • Borregaard N, Cowland JB. Granules of the human neutrophilic polymorphonuclear leukocyte. Blood 1997;89:3503-21.
    • (1997) Blood , vol.89 , pp. 3503-3521
    • Borregaard, N.1    Cowland, J.B.2
  • 56
    • 0029971227 scopus 로고    scopus 로고
    • Biochemical and antibacterial analysis of human wound and blister fluid
    • Frohm M, Gunne H, Bergman AC et al. Biochemical and antibacterial analysis of human wound and blister fluid. Eur J Biochem 1996;237:86-92.
    • (1996) Eur J Biochem , vol.237 , pp. 86-92
    • Frohm, M.1    Gunne, H.2    Bergman, A.C.3
  • 57
    • 0026565774 scopus 로고
    • Cecropia immunoresponsive factor, an insect immunoresponsive factor with DNA-binding properties similar to nuclear-factor kappaB
    • Sun SC, Faye I. Cecropia immunoresponsive factor, an insect immunoresponsive factor with DNA-binding properties similar to nuclear-factor kappaB. Eur J Biochem 1992;204:885-92.
    • (1992) Eur J Biochem , vol.204 , pp. 885-892
    • Sun, S.C.1    Faye, I.2
  • 58
    • 0022481133 scopus 로고
    • Multiple nuclear factors interact with the immunoglobulin enhancer sequence
    • Sen R, Baltimore D. Multiple nuclear factors interact with the immunoglobulin enhancer sequence. Cell 1986;46:705-16.
    • (1986) Cell , vol.46 , pp. 705-716
    • Sen, R.1    Baltimore, D.2
  • 59
    • 0029874138 scopus 로고    scopus 로고
    • The NF-kB and IkB proteins: New discoveries and insight
    • Baldwin S Jr. The NF-kB and IkB proteins: new discoveries and insight. Annu Rev Immunol 1996;14:649-83.
    • (1996) Annu Rev Immunol , vol.14 , pp. 649-683
    • Baldwin Jr., S.1
  • 60
    • 0002993113 scopus 로고    scopus 로고
    • Insect immune gene regulation
    • Bray PT, Hultmark D, eds. London: Chapman & Hall
    • Engström Y. Insect immune gene regulation. In: Bray PT, Hultmark D, eds. Molecular Mechanisms of Immune Response in Insects. London: Chapman & Hall; 1997; 211-44.
    • (1997) Molecular Mechanisms of Immune Response in Insects , pp. 211-244
    • Engström, Y.1
  • 61
    • 0029900207 scopus 로고    scopus 로고
    • Inducible expression of an antibiotic peptide gene in lipopolysaccharide-challenged tracheal epithelial cells
    • Diamond G, Russell J.P. Bevins CL. Inducible expression of an antibiotic peptide gene in lipopolysaccharide-challenged tracheal epithelial cells. Proc Natl Acad Sci USA 1996;93:5156-60.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5156-5160
    • Diamond, G.1    Russell, J.P.2    Bevins, C.L.3
  • 62
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the drosophila toll protein signals activation of adaptive immunity
    • Medzhitov RM. Preston-Hurlburt P. Janeway CAJ. A human homologue of the drosophila toll protein signals activation of adaptive immunity. Nature 1997;388:394-7.
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.M.1    Preston-Hurlburt, P.2    Janeway, C.A.J.3
  • 63
    • 0028865526 scopus 로고
    • A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the drosophila host defense
    • Lemaitre B, Kromermetzger E, Michaut L et al. A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the drosophila host defense. Proc Natl Acad Sci USA 1995;92:9465-9.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9465-9469
    • Lemaitre, B.1    Kromermetzger, E.2    Michaut, L.3
  • 64
    • 0030861832 scopus 로고    scopus 로고
    • Adjacent GATA and kB-like motifs regulate the expression of a Drosophila immune gene
    • Kadalayil L, Petersen UM, Engström Y. Adjacent GATA and kB-like motifs regulate the expression of a Drosophila immune gene. Nucl Acids Res l997;6:1233-9.
    • (1997) Nucl Acids Res , vol.6 , pp. 1233-1239
    • Kadalayil, L.1    Petersen, U.M.2    Engström, Y.3
  • 65
    • 0345646454 scopus 로고    scopus 로고
    • In vivo regulation of tissue specific and LPS inducible expression of Drosophila cecropin genes
    • Roos E, Björklund G, Engström Y. In vivo regulation of tissue specific and LPS inducible expression of Drosophila cecropin genes. Insect Mol Biol 1998;7:1-13.
    • (1998) Insect Mol Biol , vol.7 , pp. 1-13
    • Roos, E.1    Björklund, G.2    Engström, Y.3
  • 66
    • 0025959246 scopus 로고
    • The andropin gene and its product, a male-specific antibacterial peptide in Drosophila melanogaster
    • Samakovlis C, Kylsten P, Kimbrell DA, Engström Å, Hultmark D. The andropin gene and its product, a male-specific antibacterial peptide in Drosophila melanogaster. EMBO J 1991;10:163-9.
    • (1991) EMBO J , vol.10 , pp. 163-169
    • Samakovlis, C.1    Kylsten, P.2    Kimbrell, D.A.3    Engström, Å.4    Hultmark, D.5
  • 68
    • 0029858808 scopus 로고    scopus 로고
    • Molecular characterization of ceratotoxin c, a novel antibacterial female-specific peptide of the ceratotoxin family from the medfly ceratitis capitata
    • Rosetto M, Manetti AGO, Giordano PC et al. Molecular characterization of ceratotoxin c, a novel antibacterial female-specific peptide of the ceratotoxin family from the medfly ceratitis capitata. Eur J Biochem 1996;241:330-7.
    • (1996) Eur J Biochem , vol.241 , pp. 330-337
    • Rosetto, M.1    Manetti, A.G.O.2    Giordano, P.C.3
  • 70
    • 0030720063 scopus 로고    scopus 로고
    • Inhibition by glucocorticoids of the synthesis of antimicrobial peptides from amphibian skin
    • Simmaco M, Boman A, Mangoni ML et al. Inhibition by glucocorticoids of the synthesis of antimicrobial peptides from amphibian skin. FEBS Lett 1997;416:273-5.
    • (1997) FEBS Lett , vol.416 , pp. 273-275
    • Simmaco, M.1    Boman, A.2    Mangoni, M.L.3
  • 73
    • 0029873933 scopus 로고    scopus 로고
    • Structure and orientation of the mammalian antibacterial peptide cecropin pi within phospholipid membranes
    • Gazit E, Miller IR, Biggin PC, Sansom MSP, Shai Y. Structure and orientation of the mammalian antibacterial peptide cecropin pi within phospholipid membranes. J Mol Biol 1996;258:860-70.
    • (1996) J Mol Biol , vol.258 , pp. 860-870
    • Gazit, E.1    Miller, I.R.2    Biggin, P.C.3    Sansom, M.S.P.4    Shai, Y.5
  • 74
    • 0031034840 scopus 로고    scopus 로고
    • Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems
    • Lohner K, Latal A, Lehrer RI, Ganz T. Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems. Biochemistry 1997;36:1525-31.
    • (1997) Biochemistry , vol.36 , pp. 1525-1531
    • Lohner, K.1    Latal, A.2    Lehrer, R.I.3    Ganz, T.4
  • 75
    • 0030886178 scopus 로고    scopus 로고
    • The concentration-dependent membrane activity of cecropin A
    • Silvestro L, Gupta K, Weiser JN, Axelsen PH. The concentration-dependent membrane activity of cecropin A. Biochemistry 1997;36:11452-60.
    • (1997) Biochemistry , vol.36 , pp. 11452-11460
    • Silvestro, L.1    Gupta, K.2    Weiser, J.N.3    Axelsen, P.H.4
  • 76
    • 0030863833 scopus 로고    scopus 로고
    • Structural aspects of the interaction of peptidyl-glycylleucine-carboxyamide, a highly potent antimicrobial peptide from frog skin, with lipids
    • Latal A, Degovics G, Epand RF, Epand RM, Lohner K. Structural aspects of the interaction of peptidyl-glycylleucine-carboxyamide, a highly potent antimicrobial peptide from frog skin, with lipids. Eur J Biochem 1997;248:938-46.
    • (1997) Eur J Biochem , vol.248 , pp. 938-946
    • Latal, A.1    Degovics, G.2    Epand, R.F.3    Epand, R.M.4    Lohner, K.5
  • 77
    • 15644372264 scopus 로고    scopus 로고
    • Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjecent sites important for antifungal activity
    • de Samblanx GW, Goderis IJ, Thevissen K et al. Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjecent sites important for antifungal activity. J Biol Chem 1997;272:1171-9.
    • (1997) J Biol Chem , vol.272 , pp. 1171-1179
    • De Samblanx, G.W.1    Goderis, I.J.2    Thevissen, K.3
  • 78
    • 0027218376 scopus 로고
    • Defensin promotes fusion and lysis of negatively charged membranes
    • Fujii G, Selsted ME, Eisenberg D. Defensin promotes fusion and lysis of negatively charged membranes. Protein Sci 1993;2:1301-12.
    • (1993) Protein Sci , vol.2 , pp. 1301-1312
    • Fujii, G.1    Selsted, M.E.2    Eisenberg, D.3
  • 79
    • 0028286667 scopus 로고
    • Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity
    • Casteels P, Tempst P. Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity. Biochem Biophys Res Comm 1994;189:339-45.
    • (1994) Biochem Biophys Res Comm , vol.189 , pp. 339-345
    • Casteels, P.1    Tempst, P.2
  • 80
    • 0027216093 scopus 로고
    • Mechanisms of action on Escherichia coli of cecropin-PI and PR-39, 2 antibacterial peptides from pig intestine
    • Boman HG, Agerberth B, Boman A. Mechanisms of action on Escherichia coli of cecropin-PI and PR-39, 2 antibacterial peptides from pig intestine. Infect Immun 1993;61:2978-84.
    • (1993) Infect Immun , vol.61 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 81
    • 0028092047 scopus 로고
    • Syndecans, cell surface heparin sulfate proteoglycans. are induced by a prolin-rich antimicrobial peptide from wounds
    • Gallo RL, Ono M, Povsic T et al. Syndecans, cell surface heparin sulfate proteoglycans. are induced by a prolin-rich antimicrobial peptide from wounds. Proc Natl Acad Sci USA 1994;91:11035-9.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11035-11039
    • Gallo, R.L.1    Ono, M.2    Povsic, T.3
  • 82
    • 0029664907 scopus 로고    scopus 로고
    • PR-39, a proline-rich antibacterial peptide that inhibits phagocyte NADPH oxidase activity by binding to src homology 3 domains of p47(phox)
    • Shi JH, Ross CR, Leto TL, Sylte MJ, Mcvey D.S, Blecha F. PR-39, a proline-rich antibacterial peptide that inhibits phagocyte NADPH oxidase activity by binding to src homology 3 domains of p47(phox). Proc Natl Acad Sci USA 1996;93:6014-8.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6014-6018
    • Shi, J.H.1    Ross, C.R.2    Leto, T.L.3    Sylte, M.J.4    Mcvey, D.S.5    Blecha, F.6
  • 83
    • 0026802197 scopus 로고
    • Agents that increase permeability of the outer membrane
    • Vaara M. Agents that increase permeability of the outer membrane. Microbiol Rev 1992;56:395-411.
    • (1992) Microbiol Rev , vol.56 , pp. 395-411
    • Vaara, M.1
  • 84
    • 0028114658 scopus 로고
    • How bacteria resist killing by host-defense peptides
    • Groisman EA. How bacteria resist killing by host-defense peptides. Trends Microbiol 1994;2:444-9.
    • (1994) Trends Microbiol , vol.2 , pp. 444-449
    • Groisman, E.A.1
  • 86
    • 0025886806 scopus 로고
    • Attacin, an antibacterial protein from Hyalophora-cecropia, inhibits synthesis of outer membrane proteins in Escherichia-coli by interfering with omp gene transcription
    • Carlsson A, Engström P, Palva ET, Bennich H, Attacin, an antibacterial protein from Hyalophora-cecropia, inhibits synthesis of outer membrane proteins in Escherichia-coli by interfering with omp gene transcription. Infect Immun 1991;59:3040-5.
    • (1991) Infect Immun , vol.59 , pp. 3040-3045
    • Carlsson, A.1    Engström, P.2    Palva, E.T.3    Bennich, H.4
  • 87
    • 0030463948 scopus 로고    scopus 로고
    • Production of active bovine tracheal antimicrobial peptide in milk of transgenic mice
    • Yarus S, Rosen JM, Cole AM, Diamond G. Production of active bovine tracheal antimicrobial peptide in milk of transgenic mice. Proc Natl Acad Sci USA 1996;93:14118-21.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14118-14121
    • Yarus, S.1    Rosen, J.M.2    Cole, A.M.3    Diamond, G.4
  • 88
    • 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 WA, Elzer PH, Enright FM, Jaynes JM, Morrey JD, White KL. Interleukin 2 promoter/enhancer controlled expression of a synthetic cecropin-class lytic peptide in transgenic mice and subsequent resistance to Brucella abortus. Transgenic Res 1997;6:337-47.
    • (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
  • 89
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosquist R, Magnusson KE, Wolf-Watz H. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J 1994;13:964-72.
    • (1994) EMBO J , vol.13 , pp. 964-972
    • Rosquist, R.1    Magnusson, K.E.2    Wolf-Watz, H.3
  • 90
    • 0031440031 scopus 로고    scopus 로고
    • Homology between Immune responses in vertebrates and invertebrates: Does it exist?
    • Klein J. Homology between Immune responses in vertebrates and invertebrates: does it exist? Scand J Immunol 1997;46:558-64.
    • (1997) Scand J Immunol , vol.46 , pp. 558-564
    • Klein, J.1
  • 91
    • 0015524896 scopus 로고
    • Inducible antibacterial defence system in Drosophila
    • Boman HG, Nilsson I, Rasmuson B. Inducible antibacterial defence system in Drosophila. Nature 1972;237:232-5.
    • (1972) Nature , vol.237 , pp. 232-235
    • Boman, H.G.1    Nilsson, I.2    Rasmuson, B.3
  • 92
    • 0031133426 scopus 로고    scopus 로고
    • Macrophage triggering with cecropin a and melittinderived peptides induces type II nitric oxide synthase expression
    • Velasco M, Diaz-Guerra M, Diaz-Achirica P, Andreu D, Rivas L, Bosca L. Macrophage triggering with cecropin A and melittinderived peptides induces type II nitric oxide synthase expression. J Immunol 1997;158:4437-43.
    • (1997) J Immunol , vol.158 , pp. 4437-4443
    • Velasco, M.1    Diaz-Guerra, M.2    Diaz-Achirica, P.3    Andreu, D.4    Rivas, L.5    Bosca, L.6
  • 93
    • 0030684057 scopus 로고    scopus 로고
    • Psamodium activates the innate immune response of Anopheles gambiae mosquitos
    • Richman AM, Dimopoulos G, Seelay D, Kafatos FC, Psamodium activates the innate immune response of Anopheles gambiae mosquitos. EMBO J 1997;16:6114-9.
    • (1997) EMBO J , vol.16 , pp. 6114-6119
    • Richman, A.M.1    Dimopoulos, G.2    Seelay, D.3    Kafatos, F.C.4
  • 94
    • 0030987547 scopus 로고    scopus 로고
    • Wolbachia, normally a symbiont of Drosophila. can be virulent, causing degeneration and early death
    • Min KT, Benzer S, Wolbachia, normally a symbiont of Drosophila. can be virulent, causing degeneration and early death. Proc Natl Acad Sci USA 1997;94:10792-6.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10792-10796
    • Min, K.T.1    Benzer, S.2
  • 95
    • 0029923838 scopus 로고    scopus 로고
    • The origin of the eukaryotic cell
    • Gupta R, Golding G. The origin of the eukaryotic cell. TIBS 1996;21:166-71.
    • (1996) TIBS , vol.21 , pp. 166-171
    • Gupta, R.1    Golding, G.2
  • 96
    • 0031782954 scopus 로고    scopus 로고
    • Lanthabiotics: Biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria
    • Sahl HG, Bierbaum G. Lanthabiotics: biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria. Annu Rev Microbiol 1998;67:41-79.
    • (1998) Annu Rev Microbiol , vol.67 , pp. 41-79
    • Sahl, H.G.1    Bierbaum, G.2
  • 97
    • 0000842940 scopus 로고    scopus 로고
    • What is a pathogen?
    • Falkow S. What is a pathogen? ASM News 1997;63:359-366.
    • (1997) ASM News , vol.63 , pp. 359-366
    • Falkow, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.