메뉴 건너뛰기




Volumn 56, Issue 1-2, 1999, Pages 32-46

Epithelial antimicrobial peptides: Innate local host response elements

Author keywords

Antimicrobial peptides; Cystic fibrosis; Defensin; Epithelia; Innate immunity; Peptide antibiotics

Indexed keywords

CYTOKINE; DEFENSIN; POLYPEPTIDE ANTIBIOTIC AGENT;

EID: 0033213989     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050004     Document Type: Review
Times cited : (139)

References (115)
  • 3
    • 0026802379 scopus 로고
    • Isolation and characterization of a novel class of plant antimicrobial peptides from Mirabilis jalapa I., seeds
    • Cammue B. P. A., De Bolle M. F. C., Terras S. F. R., Proost P., Van Damme J., Rees S. B. et al. (1992) Isolation and characterization of a novel class of plant antimicrobial peptides from Mirabilis jalapa I., seeds. J. Biol. Chem. 267: 2228-2233
    • (1992) J. Biol. Chem. , vol.267 , pp. 2228-2233
    • Cammue, B.P.A.1    De Bolle, M.F.C.2    Terras, S.F.R.3    Proost, P.4    Van Damme, J.5    Rees, S.B.6
  • 4
    • 84954938477 scopus 로고
    • A lethal toxic substance for brewing yeast in wheat and barley
    • Okada T., Yoshizumi H, and Terashima Y. (1970) A lethal toxic substance for brewing yeast in wheat and barley. Agric. Biol. Chem. 34: 1084-1088
    • (1970) Agric. Biol. Chem. , vol.34 , pp. 1084-1088
    • Okada, T.1    Yoshizumi, H.2    Terashima, Y.3
  • 5
    • 0026635585 scopus 로고
    • Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds
    • Terras F. R. G., Schoofs H., De Bolle M. F. C., Van Leuven F., Rees S. B., Vanderleyden J. et al. (1992) Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds. J. Biol. Chem. 267: 15301-15309
    • (1992) J. Biol. Chem. , vol.267 , pp. 15301-15309
    • Terras, F.R.G.1    Schoofs, H.2    De Bolle, M.F.C.3    Van Leuven, F.4    Rees, S.B.5    Vanderleyden, J.6
  • 6
    • 0029379573 scopus 로고
    • A potent antimicrobial protein from onion (Allium cepa L.) seeds showing sequence homology to plant lipid transfer proteins
    • Cammue B. P. A., Thevissen K., Hendriks M., Eggermont K., Goderis I. J., Proost P. et al. (1995) A potent antimicrobial protein from onion (Allium cepa L.) seeds showing sequence homology to plant lipid transfer proteins. Plant Physiol. 109: 445-455
    • (1995) Plant Physiol. , vol.109 , pp. 445-455
    • Cammue, B.P.A.1    Thevissen, K.2    Hendriks, M.3    Eggermont, K.4    Goderis, I.J.5    Proost, P.6
  • 7
    • 0028518533 scopus 로고
    • Thionins: Properties, possible biological roles and mechanisms of action
    • Florack D. E. A. and Stiekema W. J. (1994) Thionins: properties, possible biological roles and mechanisms of action. Plant Mol. Biol. 26: 25-37
    • (1994) Plant Mol. Biol. , vol.26 , pp. 25-37
    • Florack, D.E.A.1    Stiekema, W.J.2
  • 8
    • 0029411206 scopus 로고
    • An Arabidopsis thaliana thionin gene is inducible via a signal transduction pathway different from that for pathogenesis-related proteins
    • Epple P., Apel K. and Bohlmann H. (1995) An Arabidopsis thaliana thionin gene is inducible via a signal transduction pathway different from that for pathogenesis-related proteins. Plant Physiol. 109: 813-820
    • (1995) Plant Physiol. , vol.109 , pp. 813-820
    • Epple, P.1    Apel, K.2    Bohlmann, H.3
  • 9
    • 0026741278 scopus 로고
    • Jasmonic acid/methyl jasmonate accumulate in wounded soybean hypocotyls and modulate wound gene expression
    • Creelman R. A., Tierney M. L. and Mullet J. E. (1992) Jasmonic acid/methyl jasmonate accumulate in wounded soybean hypocotyls and modulate wound gene expression. Proc. Natl. Acad. Sci. USA. 89: 4938-4941
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4938-4941
    • Creelman, R.A.1    Tierney, M.L.2    Mullet, J.E.3
  • 10
    • 0029347190 scopus 로고
    • Plant defensins: Novel antimicrobial peptides as components of the host defence system
    • Broekaert W. F., Terras F. R. G. Cammue B. P. A. and Osborn R. W. (1995) Plant defensins: novel antimicrobial peptides as components of the host defence system. Plant Physiol. 108: 1353-1358
    • (1995) Plant Physiol. , vol.108 , pp. 1353-1358
    • Broekaert, W.F.1    Terras, F.R.G.2    Cammue, B.P.A.3    Osborn, R.W.4
  • 13
    • 0028271965 scopus 로고
    • Pseudothionin-Stl, a potato peptide active against potato pathogens
    • Moreno M., Segura A. and Garcia-Olmedo F. (1994) Pseudothionin-Stl, a potato peptide active against potato pathogens. Eur. J. Biochem. 223: 135-139
    • (1994) Eur. J. Biochem. , vol.223 , pp. 135-139
    • Moreno, M.1    Segura, A.2    Garcia-Olmedo, F.3
  • 15
    • 0030331042 scopus 로고    scopus 로고
    • Pathogen-induced systemic activation of a plant defensin gene in Arabidopsis follows a salicylic acid-independent pathway
    • Penninckx I. A. M. A., Eggermont K., Terras F. R. G., Thomma B. P. H. J., De Samblanx G. W., Buchala A. et al. (1996) Pathogen-induced systemic activation of a plant defensin gene in Arabidopsis follows a salicylic acid-independent pathway. Plant Cell 8: 2309-2323
    • (1996) Plant Cell , vol.8 , pp. 2309-2323
    • Penninckx, I.A.M.A.1    Eggermont, K.2    Terras, F.R.G.3    Thomma, B.P.H.J.4    De Samblanx, G.W.5    Buchala, A.6
  • 16
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H., Hultmark D., Engström A., Bennich H. and Boman H. G. (1981) Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292: 246-248
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engström, A.3    Bennich, H.4    Boman, H.G.5
  • 17
    • 0024454751 scopus 로고
    • Apidaecins: Antibacterial peptides from honeybess
    • Casteels P., Ampe C., Jacobs F., Vaeck M. and Tempst P. (1989) Apidaecins: antibacterial peptides from honeybess. EMBO J. 8: 2387-2391
    • (1989) EMBO J. , vol.8 , pp. 2387-2391
    • Casteels, P.1    Ampe, C.2    Jacobs, F.3    Vaeck, M.4    Tempst, P.5
  • 18
    • 0025058306 scopus 로고
    • Isolation and characterization of abaecin, a major antibacterial response peptide in the honeybee (Apis mellifera)
    • Casteels P., Ampe C., Riviere L., Damme J. V., Elicone C., Fleming M. et al. (1990) Isolation and characterization of abaecin, a major antibacterial response peptide in the honeybee (Apis mellifera). Eur. J. Biochem. 187: 381-386
    • (1990) Eur. J. Biochem. , vol.187 , pp. 381-386
    • Casteels, P.1    Ampe, C.2    Riviere, L.3    Damme, J.V.4    Elicone, C.5    Fleming, M.6
  • 19
    • 0027201086 scopus 로고
    • A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution
    • Bulet P., Dimarcq J. L., Hetru C., Lagueux M., Charlet M., Hegy G. et al. (1993) A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution. J. Biol. Chem. 286: 14893-14897
    • (1993) J. Biol. Chem. , vol.286 , pp. 14893-14897
    • Bulet, P.1    Dimarcq, J.L.2    Hetru, C.3    Lagueux, M.4    Charlet, M.5    Hegy, G.6
  • 20
    • 20244363184 scopus 로고
    • Insect immunity: Isolation from immune blood of the dipteran Phormia terranorae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides
    • Lambert J., Keppi E., Dimarcq J. L., Wicker C., Reichhart J. M., Dunbar B. et al. (1989) Insect immunity: isolation from immune blood of the dipteran Phormia terranorae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides. Proc. Natl. Acad. Sci. USA. 86: 262-266
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 262-266
    • Lambert, J.1    Keppi, E.2    Dimarcq, J.L.3    Wicker, C.4    Reichhart, J.M.5    Dunbar, B.6
  • 21
    • 0026791975 scopus 로고
    • The immune system evolved to discriminate infectious nonself from noninfectious self
    • Janeway C. A. Jr. (1992) The immune system evolved to discriminate infectious nonself from noninfectious self. Immunol. Today 13: 11-16
    • (1992) Immunol. Today , vol.13 , pp. 11-16
    • Janeway C.A., Jr.1
  • 22
    • 0028587829 scopus 로고
    • Insect immunity: Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides
    • Fehlbaum P., Bulet P., Michaut L., Lagueux M., Brockaert W. F., Hetru C. et al. (1994) Insect immunity: septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides. J. Biol. Chem. 269: 33159-33163
    • (1994) J. Biol. Chem. , vol.269 , pp. 33159-33163
    • Fehlbaum, P.1    Bulet, P.2    Michaut, L.3    Lagueux, M.4    Brockaert, W.F.5    Hetru, C.6
  • 23
    • 0032473360 scopus 로고    scopus 로고
    • A drosomycin-GFP reporter transgene reveals a local immune response in Drosophila that is not dependent on the Toll pathway
    • Ferrandon D., Jung A. C., Criqui M.-C., Lemaitre B., Uttenweiler-Joseph S., Michaut L. et al. (1998) A drosomycin-GFP reporter transgene reveals a local immune response in Drosophila that is not dependent on the Toll pathway. EMBO J. 17: 1217-1227
    • (1998) EMBO J. , vol.17 , pp. 1217-1227
    • Ferrandon, D.1    Jung, A.C.2    Criqui, M.-C.3    Lemaitre, B.4    Uttenweiler-Joseph, S.5    Michaut, L.6
  • 24
    • 0028865526 scopus 로고
    • A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophilia host defense
    • Lemaitre B., Kromer-Metzger F., Michaut L., Nicolas E., Meister M., Georgel P. et al. (1995) A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophilia host defense. Proc. Natl. Acad. Sci. USA. 92: 9465-9469
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9465-9469
    • Lemaitre, B.1    Kromer-Metzger, F.2    Michaut, L.3    Nicolas, E.4    Meister, M.5    Georgel, P.6
  • 25
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette spatzle Toll/cactus controls the potent antifungal response in Drosophila adults
    • Lemaitre B., Nicolas E., Michaul L., Reichhart J. M. and Hoffmann J. A. (1996) The dorsoventral regulatory gene cassette spatzle Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 86: 973-983
    • (1996) Cell , vol.86 , pp. 973-983
    • Lemaitre, B.1    Nicolas, E.2    Michaul, L.3    Reichhart, J.M.4    Hoffmann, J.A.5
  • 26
    • 0030739528 scopus 로고    scopus 로고
    • CDNA cloning of clavanins: Antimicrobial peptides of tunicate hemocytes
    • Zhao C., Liaw L., Lee I. H. and Lehrer R. I. (1997) cDNA cloning of clavanins: antimicrobial peptides of tunicate hemocytes. FEBS Lett. 410: 490-492
    • (1997) FEBS Lett. , vol.410 , pp. 490-492
    • Zhao, C.1    Liaw, L.2    Lee, I.H.3    Lehrer, R.I.4
  • 27
    • 0001505184 scopus 로고    scopus 로고
    • Styelins, broad-spectrum antimicrobial peptides from the solitary tunicate
    • Lee I. H., Cho Y. and Lehrer R. I. (1997) Styelins, broad-spectrum antimicrobial peptides from the solitary tunicate, Styela clava. Comp. Biochem. Physiol. B. 118: 515-521
    • (1997) Styela Clava. Comp. Biochem. Physiol. B. , vol.118 , pp. 515-521
    • Lee, I.H.1    Cho, Y.2    Lehrer, R.I.3
  • 28
    • 0029020955 scopus 로고
    • A novel big defensin identified in horseshoe crab hemocytes: Isolation, amino acid sequence, and antibacterial activity
    • Saito T., Kawabata S., Shigenaga T., Takayenoki Y., Cho J., Nakajima H. et al. (1995) A novel big defensin identified in horseshoe crab hemocytes: isolation, amino acid sequence, and antibacterial activity. J. Biochem. (Tokyo) 117: 1131-1137
    • (1995) J. Biochem. (Tokyo) , vol.117 , pp. 1131-1137
    • Saito, T.1    Kawabata, S.2    Shigenaga, T.3    Takayenoki, Y.4    Cho, J.5    Nakajima, H.6
  • 29
    • 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. (1997) Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (decapoda). J. Biol. Chem. 272: 28398-28406
    • (1997) J. Biol. Chem. , vol.272 , pp. 28398-28406
    • Destoumieux, D.1    Bulet, P.2    Loew, D.3    Van Dorsselaer, A.4    Rodriguez, J.5    Bachère, E.6
  • 30
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff M. (1987) Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA. 84: 5449-5453
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 31
    • 0023100945 scopus 로고
    • Biosynthesis and degradation of peptides derived from Xenopus laeris prohormones
    • Giovannini M. G., Poulter L., Gibson B. W. and Williams D. H. (1987) Biosynthesis and degradation of peptides derived from Xenopus laeris prohormones. Biochem. J. 243: 113-120
    • (1987) Biochem. J. , vol.243 , pp. 113-120
    • Giovannini, M.G.1    Poulter, L.2    Gibson, B.W.3    Williams, D.H.4
  • 32
    • 0024286949 scopus 로고
    • Antimicrobial properties of peptides from Xenopus granular gland secretions
    • Soravia E., Martini G. and Zasloff M. (1988) Antimicrobial properties of peptides from Xenopus granular gland secretions. FEBS Lett. 228: 337-340
    • (1988) FEBS Lett. , vol.228 , pp. 337-340
    • Soravia, E.1    Martini, G.2    Zasloff, M.3
  • 33
    • 0029047938 scopus 로고
    • Amphibian skin: A promising resource for antimicrobial peptides
    • Barra D. and Simmaco M. (1995) Amphibian skin: a promising resource for antimicrobial peptides. Trends Biotechnol. 13: 205-209
    • (1995) Trends Biotechnol. , vol.13 , pp. 205-209
    • Barra, D.1    Simmaco, M.2
  • 34
    • 0028964136 scopus 로고
    • Defensins in granules of phagocytic and non-phagocytic cells
    • Selsted M. E. and Ouellette A. J. (1995) Defensins in granules of phagocytic and non-phagocytic cells. Trends Cell Biol. 5: 114-119
    • (1995) Trends Cell Biol. , vol.5 , pp. 114-119
    • Selsted, M.E.1    Ouellette, A.J.2
  • 35
    • 0029051685 scopus 로고
    • Defensins and other endogenous peptide antibiotics of vertebrates
    • Martin E., Ganz T. and Lehrer R. I. (1995) Defensins and other endogenous peptide antibiotics of vertebrates. J. Leukocyte Biol. 58: 128-136
    • (1995) J. Leukocyte Biol. , vol.58 , pp. 128-136
    • Martin, E.1    Ganz, T.2    Lehrer, R.I.3
  • 36
    • 0030449497 scopus 로고    scopus 로고
    • Endogenous vertebrate antibodies defensins, protegrins, and other cysteine-rich antimicrobial peptides
    • Lehrer R. I. and Ganz T. (1996) Endogenous vertebrate antibodies defensins, protegrins, and other cysteine-rich antimicrobial peptides. Ann. NY Acad. Sci. 797: 228-239
    • (1996) Ann. NY Acad. Sci. , vol.797 , pp. 228-239
    • Lehrer, R.I.1    Ganz, T.2
  • 38
    • 0026712324 scopus 로고
    • Cryptdins: Antimicrobial defensins of the murine small intestine
    • Eisenhauer P. B., Harwig S. S. and Lehrer R. I. (1992) Cryptdins: antimicrobial defensins of the murine small intestine. Infect. Immun. 60: 3556-3565
    • (1992) Infect. Immun. , vol.60 , pp. 3556-3565
    • Eisenhauer, P.B.1    Harwig, S.S.2    Lehrer, R.I.3
  • 39
    • 0026645526 scopus 로고
    • Mouse neutrophils lack defensins
    • Eisenhauer P. B. and Lehrer R. I. (1992) Mouse neutrophils lack defensins. Infect. Immun. 60: 3446-3447
    • (1992) Infect. Immun. , vol.60 , pp. 3446-3447
    • Eisenhauer, P.B.1    Lehrer, R.I.2
  • 40
    • 0028051542 scopus 로고
    • Mouse Paneth cell defensins: Primary structures and antibacterial activities of numerous cryptdin isoforms
    • Ouellette A. J., Hsieh M. M., Nosek M. T., Cano-Gauci D. F., Huttner K. M., Buick R. N. et al. (1994) Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms. Infect. Immun. 62: 5040-5047
    • (1994) Infect. Immun. , vol.62 , pp. 5040-5047
    • Ouellette, A.J.1    Hsieh, M.M.2    Nosek, M.T.3    Cano-Gauci, D.F.4    Huttner, K.M.5    Buick, R.N.6
  • 41
    • 0029738094 scopus 로고    scopus 로고
    • Positional specificity of defensin gene expression reveals Paneth cell heterogeneity in mouse small intestine
    • Darmoul D. and Ouellette A. J. (1996) Positional specificity of defensin gene expression reveals Paneth cell heterogeneity in mouse small intestine. Am. J. Physiol. Gastrointest. Liver Physiol. 271: G68-G74
    • (1996) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.271
    • Darmoul, D.1    Ouellette, A.J.2
  • 43
    • 0026660392 scopus 로고
    • Enteric defensins: Antibiotic peptide components of intestinal host defense
    • Selsted M. E., Miller S. I., Henschen A. H. and Ouellette A. J. (1992) Enteric defensins: antibiotic peptide components of intestinal host defense. J. Cell Biol. 118: 929-936
    • (1992) J. Cell Biol. , vol.118 , pp. 929-936
    • Selsted, M.E.1    Miller, S.I.2    Henschen, A.H.3    Ouellette, A.J.4
  • 45
    • 0030778218 scopus 로고    scopus 로고
    • Antimicrobial protection of the mouse testis: Synthesis of defensins of the cryptdin family
    • Grandjean V., Vincent S., Martin L., Rassoulzadegan M. and Cuzin F. (1997) Antimicrobial protection of the mouse testis: synthesis of defensins of the cryptdin family. Biol. Reprod. 57: 1115-1122
    • (1997) Biol. Reprod. , vol.57 , pp. 1115-1122
    • Grandjean, V.1    Vincent, S.2    Martin, L.3    Rassoulzadegan, M.4    Cuzin, F.5
  • 46
    • 0026457997 scopus 로고
    • Paneth cells of the human small intestine express an antimicrobial peptide gene
    • Jones D. E. and Bevins C. L. (1992) Paneth cells of the human small intestine express an antimicrobial peptide gene. J. Biol. Chem. 267: 23216-23225
    • (1992) J. Biol. Chem. , vol.267 , pp. 23216-23225
    • Jones, D.E.1    Bevins, C.L.2
  • 47
    • 0027390031 scopus 로고
    • Defensin-6 mRNA in human Paneth cells: Implications for antimicrobial peptides in host defense of the human bowel
    • Jones D. E. and Bevins C. L. (1993) Defensin-6 mRNA in human Paneth cells: implications for antimicrobial peptides in host defense of the human bowel. FEBS Lett. 315: 187-192
    • (1993) FEBS Lett. , vol.315 , pp. 187-192
    • Jones, D.E.1    Bevins, C.L.2
  • 48
    • 0030914439 scopus 로고    scopus 로고
    • Localization of human intestinal defensin 5 in Paneth cell granules
    • Porter E. M., Liu L., Oren A., Anton P. A. and Ganz T. (1997) Localization of human intestinal defensin 5 in Paneth cell granules. Infect. Immun. 65: 2389-2395
    • (1997) Infect. Immun. , vol.65 , pp. 2389-2395
    • Porter, E.M.1    Liu, L.2    Oren, A.3    Anton, P.A.4    Ganz, T.5
  • 49
    • 0030731743 scopus 로고    scopus 로고
    • Paneth cells and innate immunity in the crypt microenvironment
    • Ouellette A. J. (1997) Paneth cells and innate immunity in the crypt microenvironment. Gastroenterology 113: 1779-1784
    • (1997) Gastroenterology , vol.113 , pp. 1779-1784
    • Ouellette, A.J.1
  • 50
    • 0032436008 scopus 로고    scopus 로고
    • Isolation of human intestinal defensins from ileal neobladder urine
    • Porter E. M., Poles M. A., Lee J. S., Naitoh J., Bevins C. L. and Ganz T. (1998) Isolation of human intestinal defensins from ileal neobladder urine. FEBS Lett. 434: 272-276
    • (1998) FEBS Lett. , vol.434 , pp. 272-276
    • Porter, E.M.1    Poles, M.A.2    Lee, J.S.3    Naitoh, J.4    Bevins, C.L.5    Ganz, T.6
  • 51
    • 0030913746 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial activity of human intestinal defensin 5
    • Porter E. M., Van Dam E., Valore E. V. and Ganz T. (1997) Broad-spectrum antimicrobial activity of human intestinal defensin 5. Infect. Immun. 65: 2396-2401
    • (1997) Infect. Immun. , vol.65 , pp. 2396-2401
    • Porter, E.M.1    Van Dam, E.2    Valore, E.V.3    Ganz, T.4
  • 52
    • 0031898688 scopus 로고    scopus 로고
    • Gene expression, immunolocalization, and secretion of human defensin-5 in human female reproductive tract
    • Quayle A. J., Porter E. M., Nussbaum A. A., Wang Y. M., Brabee C., Yip K. P. et al. (1998) Gene expression, immunolocalization, and secretion of human defensin-5 in human female reproductive tract. Am. J. Pathol. 152: 1247-1258
    • (1998) Am. J. Pathol. , vol.152 , pp. 1247-1258
    • Quayle, A.J.1    Porter, E.M.2    Nussbaum, A.A.3    Wang, Y.M.4    Brabee, C.5    Yip, K.P.6
  • 53
    • 0032168228 scopus 로고    scopus 로고
    • Molecule of the month β-defensins: Endogenous antibiotics of the innate host defense response
    • Diamond G. and Bevins C. L. (1998) Molecule of the month β-defensins: endogenous antibiotics of the innate host defense response. Clin. Immunol. Immunopathol. 88: 221-225
    • (1998) Clin. Immunol. Immunopathol. , vol.88 , pp. 221-225
    • Diamond, G.1    Bevins, C.L.2
  • 54
    • 0027514011 scopus 로고
    • Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils
    • Selsted M. E., Tang Y. Q., Morris W. L., McGuire P. A., Novotny M. J., Smith W. et al. (1993) Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. J. Biol. Chem. 268: 6641-6648
    • (1993) J. Biol. Chem. , vol.268 , pp. 6641-6648
    • Selsted, M.E.1    Tang, Y.Q.2    Morris, W.L.3    McGuire, P.A.4    Novotny, M.J.5    Smith, W.6
  • 56
    • 0025811874 scopus 로고
    • Tracheal antimicrobial peptide, a cystein-rich peptide from mammalian tracheal mucosa: Peptide isolation and cloning of a cDNA
    • Diamond G., Zasloff M., Eck H., Brasseur M., Maloy W. L. and Bevins C. L. (1991) Tracheal antimicrobial peptide, a cystein-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of a cDNA. Proc. Natl. Acad. Sci. USA 88: 3952-3956
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3952-3956
    • Diamond, G.1    Zasloff, M.2    Eck, H.3    Brasseur, M.4    Maloy, W.5    Bevins, L.C.L.6
  • 57
    • 0029900207 scopus 로고    scopus 로고
    • Inducible expression of an antibiotic peptide gene in lipopolysaccharide-challenged tracheal epithelial cells
    • Diamond G., Russell J. P. and Bevins C. L. (1996) Inducible expression of an antibiotic peptide gene in lipopolysaccharide-challenged tracheal epithelial cells. Proc. Natl. Acad. Sci. USA 93: 5156-5160
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5156-5160
    • Diamond, G.1    Russell, J.P.2    Bevins, C.L.3
  • 58
    • 0026557911 scopus 로고
    • Insect immunity: Developmental and inducible activity of the Drosophila diptericin promoter
    • Reichhart J. M., Meister M., Dimarcq J. L., Zachary D., Hoffmann D., Ruiz C. et al. (1992) Insect immunity: developmental and inducible activity of the Drosophila diptericin promoter. EMBO J. 11: 1469-1477
    • (1992) EMBO J. , vol.11 , pp. 1469-1477
    • Reichhart, J.M.1    Meister, M.2    Dimarcq, J.L.3    Zachary, D.4    Hoffmann, D.5    Ruiz, C.6
  • 59
    • 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 alpha
    • Russell J. P., Diamond G., Tarver A. P., Scanlin T. F. and Bevins C. L. (1996) Coordinate induction of two antibiotic genes in tracheal epithelial cells exposed to the inflammatory mediators lipopolysaccharide and tumor necrosis factor alpha. Infect. Immun. 64: 1565-1568
    • (1996) Infect. Immun. , vol.64 , pp. 1565-1568
    • Russell, J.P.1    Diamond, G.2    Tarver, A.P.3    Scanlin, T.F.4    Bevins, C.L.5
  • 60
    • 0028902757 scopus 로고
    • Epithelial antibiotics induced at sites of inflammation
    • Schonwetter B. S., Stolzenberg E. D. and Zasloff M. A. (1995) Epithelial antibiotics induced at sites of inflammation. Science 267: 1645-1648
    • (1995) Science , vol.267 , pp. 1645-1648
    • Schonwetter, B.S.1    Stolzenberg, E.D.2    Zasloff, M.A.3
  • 61
    • 0031882530 scopus 로고    scopus 로고
    • Expression of beta-defensin genes in bovine alveolar macrophages
    • Ryan L. K., Rhodes J., Bhat M. and Diamond G. (1998) Expression of beta-defensin genes in bovine alveolar macrophages. Infect. Immun. 66: 878-881
    • (1998) Infect. Immun. , vol.66 , pp. 878-881
    • Ryan, L.K.1    Rhodes, J.2    Bhat, M.3    Diamond, G.4
  • 63
    • 15644370080 scopus 로고    scopus 로고
    • Enteric β-defensin: Molecular cloning and characterization of a gene with inducible intestinal epithelial cell expression associated with Cryptosporidium parvum infection
    • Tarver A. P., Clark D. P., Diamond G., Russell J. P., Erdjument-Bromage H., Tempst P. et al. (1998) Enteric β-defensin: molecular cloning and characterization of a gene with inducible intestinal epithelial cell expression associated with Cryptosporidium parvum infection. Infect. Immun. 66: 1045-1056
    • (1998) Infect. Immun. , vol.66 , pp. 1045-1056
    • Tarver, A.P.1    Clark, D.P.2    Diamond, G.3    Russell, J.P.4    Erdjument-Bromage, H.5    Tempst, P.6
  • 64
    • 0031937280 scopus 로고    scopus 로고
    • Antimicrobial peptide expression is developmentally regulated in the ovine gastrointestinal tract
    • Huttner K. M., Brezinski-Caliguri D. J., Mahoney M. M. and Diamond G. (1998) Antimicrobial peptide expression is developmentally regulated in the ovine gastrointestinal tract. J. Nutr. 128 (Suppl.): 297S-299S
    • (1998) J. Nutr. , vol.128 , Issue.SUPPL.
    • Huttner, K.M.1    Brezinski-Caliguri, D.J.2    Mahoney, M.M.3    Diamond, G.4
  • 65
    • 0030747618 scopus 로고    scopus 로고
    • The mouse genome encodes a single homolog of the antimicrobial peptide human β-defensin 1
    • Huttner K. M., Kozak C. A. and Bevins C. L. (1997) The mouse genome encodes a single homolog of the antimicrobial peptide human β-defensin 1. FEBS Lett. 413: 45-49
    • (1997) FEBS Lett. , vol.413 , pp. 45-49
    • Huttner, K.M.1    Kozak, C.A.2    Bevins, C.L.3
  • 66
    • 0031913244 scopus 로고    scopus 로고
    • Mouse β-defensin 1 is a salt-sensitive antimicrobial peptide present in epithelia of the lung and urogenital tract
    • Bals R., Goldman M. J. and Wilson J. M. (1998) Mouse β-defensin 1 is a salt-sensitive antimicrobial peptide present in epithelia of the lung and urogenital tract. Infect. Immun. 66: 1225-1232
    • (1998) Infect. Immun. , vol.66 , pp. 1225-1232
    • Bals, R.1    Goldman, M.J.2    Wilson, J.M.3
  • 68
    • 0032898451 scopus 로고    scopus 로고
    • A novel mouse beta defensin, Defb2, which is upregulated in the airways by lipopolysaccharide
    • Morrison G. M., Davidson D. J. and Doring J. R. (1999) A novel mouse beta defensin, Defb2, which is upregulated in the airways by lipopolysaccharide. FEBS Lett. 442: 112-116
    • (1999) FEBS Lett. , vol.442 , pp. 112-116
    • Morrison, G.M.1    Davidson, D.J.2    Doring, J.R.3
  • 71
    • 0030949875 scopus 로고    scopus 로고
    • Human β-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • Goldman M. J., Anderson G. M., Stolzenberg E. D., Kari U. P., Zasloff M. and Wilson J. M. (1997) Human β-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 88: 553-560
    • (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
  • 72
    • 0030569343 scopus 로고    scopus 로고
    • Widespread expression of beta-defensin hBD-1 in human secretory glands and epithelial cells
    • Zhao C. Q., Wang I. and Lehrer R. I. (1996) Widespread expression of beta-defensin hBD-1 in human secretory glands and epithelial cells. FEBS Lett. 396: 319-322
    • (1996) FEBS Lett. , vol.396 , pp. 319-322
    • Zhao, C.Q.1    Wang, I.2    Lehrer, R.I.3
  • 73
    • 0029870085 scopus 로고    scopus 로고
    • Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid
    • Smith J. J., Travis S. M., Greenberg E. P. and Welsh M. J. (1996) Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid. Cell 85: 229-236
    • (1996) Cell , vol.85 , pp. 229-236
    • Smith, J.J.1    Travis, S.M.2    Greenberg, E.P.3    Welsh, M.J.4
  • 74
    • 0031581544 scopus 로고    scopus 로고
    • Expression of natural peptide antibiotics in human skin
    • Fulton C., Anderson G. M., Zasloff M., Bull R. and Quinn A.G. (1997) Expression of natural peptide antibiotics in human skin. Lancet 350: 1750-1751
    • (1997) Lancet , vol.350 , pp. 1750-1751
    • Fulton, C.1    Anderson, G.M.2    Zasloff, M.3    Bull, R.4    Quinn, A.G.5
  • 75
    • 0031662487 scopus 로고    scopus 로고
    • Expression of the peptide antibiotic human β-defensin 1 in cultured gingival epithelial cells and gingival tissue
    • Krisanaprakornkit S., Weinberg A., Perez C. N. and Dale B. A. (1998) Expression of the peptide antibiotic human β-defensin 1 in cultured gingival epithelial cells and gingival tissue. Infect. Immun. 66: 4222-4228
    • (1998) Infect. Immun. , vol.66 , pp. 4222-4228
    • Krisanaprakornkit, S.1    Weinberg, A.2    Perez, C.N.3    Dale, B.A.4
  • 76
    • 0031213832 scopus 로고    scopus 로고
    • The human β-defensin-l and α-defensins are encoded by adjacent genes: Two peptides families with differing disulfide topology share a common ancestry
    • Liu L., Zhao C., Heng H. H. Q. and Ganz T. (1997) The human β-defensin-l and α-defensins are encoded by adjacent genes: two peptides families with differing disulfide topology share a common ancestry. Genomics 43: 316-320
    • (1997) Genomics , vol.43 , pp. 316-320
    • Liu, L.1    Zhao, C.2    Heng, H.H.Q.3    Ganz, T.4
  • 80
    • 0032575664 scopus 로고    scopus 로고
    • Identification of human beta-defensin-2 in respiratory tract and plasma and its increase in bacterial pneumonia
    • Hiratsuka T., Nakazato M., Date Y., Ashitani J., Minematsu T., Chino N. et al. (1998) Identification of human beta-defensin-2 in respiratory tract and plasma and its increase in bacterial pneumonia. Biochem. Biophys. Res. Commun. 249: 943-947
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 943-947
    • Hiratsuka, T.1    Nakazato, M.2    Date, Y.3    Ashitani, J.4    Minematsu, T.5    Chino, N.6
  • 81
    • 0032169557 scopus 로고    scopus 로고
    • Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung
    • Bals R., Wang X., Wu Z., Freeman T., Bafna V., Zasloff M. et al. (1998) Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung. J. Clin. Invest. 102: 874-880
    • (1998) J. Clin. Invest , vol.102 , pp. 874-880
    • Bals, R.1    Wang, X.2    Wu, Z.3    Freeman, T.4    Bafna, V.5    Zasloff, M.6
  • 82
    • 0032548181 scopus 로고    scopus 로고
    • Structure and mapping of the human beta-defensin HBD-2 gene and its expression at sites of inflammation
    • Liu L., Wang L., Jia H. P., Zhao C., Heng H. H. Q., Schutte B. C. et al. (1998) Structure and mapping of the human beta-defensin HBD-2 gene and its expression at sites of inflammation. Gene 222: 237-244
    • (1998) Gene , vol.222 , pp. 237-244
    • Liu, L.1    Wang, L.2    Jia, H.P.3    Zhao, C.4    Heng, H.H.Q.5    Schutte, B.C.6
  • 85
    • 0032541661 scopus 로고    scopus 로고
    • Toll-like receptor-2 mediates lipopolysaccharide-induced cellular signalling
    • Yang R. B., Mark M. R., Gray A., Huang Y., Xie M. H., Zhang M. et al. (1998) Toll-like receptor-2 mediates lipopolysaccharide-induced cellular signalling. Nature 395: 284-288
    • (1998) Nature , vol.395 , pp. 284-288
    • Yang, R.B.1    Mark, M.R.2    Gray, A.3    Huang, Y.4    Xie, M.H.5    Zhang, M.6
  • 86
  • 87
    • 0032548181 scopus 로고    scopus 로고
    • Structure and mapping of the human beta-defensin HBD-2 gene and its expression at sites of inflammation
    • Liu L., Wang L., Jia H.P., Zhao C., Heng H. H., Schutte B. C. et al. (1998) Structure and mapping of the human beta-defensin HBD-2 gene and its expression at sites of inflammation. Gene 222: 237-244
    • (1998) Gene , vol.222 , pp. 237-244
    • Liu, L.1    Wang, L.2    Jia, H.P.3    Zhao, C.4    Heng, H.H.5    Schutte, B.C.6
  • 88
    • 0029870085 scopus 로고    scopus 로고
    • Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid
    • Smith J. J., Travis S. M., Greenberg E. P. and Welsh M. J. (1996) Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid. Cell 85: 229-236
    • (1996) Cell , vol.85 , pp. 229-236
    • Smith, J.J.1    Travis, S.M.2    Greenberg, E.P.3    Welsh, M.J.4
  • 92
    • 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. (1998) Antileukoprotease in human skin: an antibiotic peptide constitutively produced by keratinocytes. Biochem. Biophys. Res. Commun. 248: 904-909
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 904-909
    • Wiedow, O.1    Harder, J.2    Bartels, J.3    Streit, V.4    Christophers, E.5
  • 93
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti M., Gennaro R. and Romeo D. (1995) Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett. 374: 1-5
    • (1995) FEBS Lett. , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 94
    • 0030956070 scopus 로고    scopus 로고
    • The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders
    • Frohm M., Agerberth B., Ahangari G., Stahle-Backdahl M., Liden S., Wigzell H. et al (1997) The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J. Biol. Chem. 272: 15258-15263
    • (1997) J. Biol. Chem. , vol.272 , pp. 15258-15263
    • Frohm, M.1    Agerberth, B.2    Ahangari, G.3    Stahle-Backdahl, M.4    Liden, S.5    Wigzell, H.6
  • 95
    • 0032482980 scopus 로고    scopus 로고
    • The peptide antibiotic LL-37 hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface
    • Bals R., Wang X., Zasloff M. and Wilson J. M. (1998) The peptide antibiotic LL-37 hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface. Proc. Natl. Acad. Sci. USA 95: 9541-9546
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9541-9546
    • Bals, R.1    Wang, X.2    Zasloff, M.3    Wilson, J.M.4
  • 96
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob
    • Turner J., Cho Y., Dinh N. N., Waring A. J. and Lehrer R. I. (1998) Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob. Agents Chemother. 42: 2206-2214
    • (1998) Agents Chemother. , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3    Waring, A.J.4    Lehrer, R.I.5
  • 97
    • 0029097115 scopus 로고
    • Structure, function, and membrane integration of defensins
    • White S. H., Wimley W. C. and Selsted M. E. (1995) Structure, function, and membrane integration of defensins. Curr. Opin. Struct. Biol. 5: 521-527
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 521-527
    • White, S.H.1    Wimley, W.C.2    Selsted, M.E.3
  • 98
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melitlin: Structure-function study
    • Oren Z. and Shai Y. (1997) Selective lysis of bacteria but not mammalian cells by diastereomers of melitlin: structure-function study. Biochemistry 36: 1826-1835
    • (1997) Biochemistry , vol.36 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 100
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethiein
    • Bechinger B. (1997) Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethiein. J. Membrane Biol. 156: 197-211
    • (1997) J. Membrane Biol. , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 102
    • 0027395308 scopus 로고
    • Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: A structural motif common to toxic arthropod proteins
    • Bruix M., Jimenez M. A., Santoro J., Gonzalez C., Colilla F. J., Mendez E. et al. (1993) Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: a structural motif common to toxic arthropod proteins. Biochemistry 32: 715-724
    • (1993) Biochemistry , vol.32 , pp. 715-724
    • Bruix, M.1    Jimenez, M.A.2    Santoro, J.3    Gonzalez, C.4    Colilla, F.J.5    Mendez, E.6
  • 103
    • 0027981211 scopus 로고
    • Structure and dynamics of the neutrophil defensins NP-2, NP-5, and HNP-1: NMR studies of amide hydrogen exchange kinetics
    • Skalicky J. J., Selsted M. E. and Pardi A. (1994) Structure and dynamics of the neutrophil defensins NP-2, NP-5, and HNP-1: NMR studies of amide hydrogen exchange kinetics. Proteins 20: 52-67
    • (1994) Proteins , vol.20 , pp. 52-67
    • Skalicky, J.J.1    Selsted, M.E.2    Pardi, A.3
  • 104
    • 0025903814 scopus 로고
    • Crystal structure of defensin HNP-3, an amphiphilic doner: Mechanisms of membrane permeabilization
    • Hill C. P., Yee J., Selsted M. E. and Eisenberg D. (1991) Crystal structure of defensin HNP-3, an amphiphilic doner: mechanisms of membrane permeabilization. Science 251: 1481-1485
    • (1991) Science , vol.251 , pp. 1481-1485
    • Hill, C.P.1    Yee, J.2    Selsted, M.E.3    Eisenberg, D.4
  • 105
    • 0028286667 scopus 로고
    • Apidaecin-type peptide antibiotics function through a non-pore-forming mechanism involving stereospecificity
    • Casteels P. and Tempst P. (1994) Apidaecin-type peptide antibiotics function through a non-pore-forming mechanism involving stereospecificity. Biochem. Biophys. Res. Commun. 189: 339-345
    • (1994) Biochem. Biophys. Res. Commun. , vol.189 , pp. 339-345
    • Casteels, P.1    Tempst, P.2
  • 106
    • 0027216093 scopus 로고
    • Mechanisms of action on Escherichia coli of cecropin PI and PR-39, two antibacterial peptides from pig intestine
    • Boman H. G., Agerberth B. and Boman A. (1993) Mechanisms of action on Escherichia coli of cecropin PI and PR-39, two antibacterial peptides from pig intestine. Infect. Immun. 61: 2978-2984
    • (1993) Infect. Immun. , vol.61 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 108
    • 0023644485 scopus 로고
    • Interaction between liposomes and sarcotoxin IA, a potent antibacterial protein of Sarcophaga peregrina (flesh gly)
    • Nakajima Y., Qu X. M. and Natori S. (1987) Interaction between liposomes and sarcotoxin IA, a potent antibacterial protein of Sarcophaga peregrina (flesh gly). J. Biol. Chem. 262: 1665-1669
    • (1987) J. Biol. Chem. , vol.262 , pp. 1665-1669
    • Nakajima, Y.1    Qu, X.M.2    Natori, S.3
  • 110
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock R. E. W. and Lehrer R. (1998) Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16: 82-88
    • (1998) Trends Biotechnol. , vol.16 , pp. 82-88
    • Hancock, R.E.W.1    Lehrer, R.2
  • 111
    • 0029809576 scopus 로고    scopus 로고
    • PhoP-PhoQ activates transcriiption of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance
    • Gunn J. S. and Miller S. I. (1996) PhoP-PhoQ activates transcriiption of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance. J. Bacteriol. 178: 6857-6864
    • (1996) J. Bacteriol. , vol.178 , pp. 6857-6864
    • Gunn, J.S.1    Miller, S.I.2
  • 112
    • 0030984298 scopus 로고    scopus 로고
    • Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ
    • Guo L., Lim K. B., Gunn J. S., Bainbridge B., Darveau R. P., Hackett M. et al. (1997) Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ. Science 276: 250-253
    • (1997) Science , vol.276 , pp. 250-253
    • Guo, L.1    Lim, K.B.2    Gunn, J.S.3    Bainbridge, B.4    Darveau, R.P.5    Hackett, M.6
  • 113
    • 0032539553 scopus 로고    scopus 로고
    • Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family
    • Shafer W. M., Qu X., Waring A. J. and Lehrer R. I. (1998) Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family. Proc. Natl. Acad. Sci. USA 95: 1829-1833
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1829-1833
    • Shafer, W.M.1    Qu, X.2    Waring, A.J.3    Lehrer, R.I.4
  • 114
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dlt operon in Staphylocoecus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • Peschel A., Otto M., Jack R. W., Kalbacher H., Jung G. and Götz F. (1999) Inactivation of the dlt operon in Staphylocoecus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J. Biol. Chem. 274: 8405-8410
    • (1999) J. Biol. Chem. , vol.274 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.W.3    Kalbacher, H.4    Jung, G.5    Götz, F.6
  • 115
    • 0032006219 scopus 로고    scopus 로고
    • Antimicrobial proteins in induced plant defense
    • Fritig B., Heitz T. and Legrand M. (1998) Antimicrobial proteins in induced plant defense. Curr. Opin. Immunol. 10: 16-22
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 16-22
    • Fritig, B.1    Heitz, T.2    Legrand, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.