메뉴 건너뛰기




Volumn 21, Issue 6, 2003, Pages 465-499

Ribosomally synthesized peptides with antimicrobial properties: Biosynthesis, structure, function, and applications

Author keywords

Antimicrobial peptides; Bacteriocins; Defensins; Peptide antibiotics

Indexed keywords

ANTIBIOTICS; BACTERIA; BIOSYNTHESIS; MICROORGANISMS;

EID: 0142183723     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0734-9750(03)00077-6     Document Type: Article
Times cited : (255)

References (218)
  • 1
    • 0029587431 scopus 로고
    • Bacteriocins: Modes of action and potentials in food preservation and control of food poisoning
    • Abee T., Krockel L., Hill C. Bacteriocins: modes of action and potentials in food preservation and control of food poisoning. Int. J. Food Microbiol. 28:1995;169-185.
    • (1995) Int. J. Food Microbiol. , vol.28 , pp. 169-185
    • Abee, T.1    Krockel, L.2    Hill, C.3
  • 2
    • 0026349223 scopus 로고
    • Amino acid sequence of PR-39: Isolation from pig testine of a new member of the family of proline-arginine rich antibacterial peptides
    • Agerberth B., Lee J.-Y., Bergman T., Carlquist M., Boman H.G., Mutt V. Amino acid sequence of PR-39: isolation from pig testine of a new member of the family of proline-arginine rich antibacterial peptides. Eur. J. Biochem. 202:1991;849-854.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 849-854
    • Agerberth, B.1    Lee, J.-Y.2    Bergman, T.3    Carlquist, M.4    Boman, H.G.5    Mutt, V.6
  • 3
    • 0034332193 scopus 로고    scopus 로고
    • The human antimicrobial and chemotactic peptides LL-37 and α-defensins are expressed by specific lymphocyte and monocyte populations
    • Agerberth B., Charo J., Werr J., Olsson B., Idali F., Lindbom L.et al. The human antimicrobial and chemotactic peptides LL-37 and α-defensins are expressed by specific lymphocyte and monocyte populations. Blood. 96:2000;3086-3093.
    • (2000) Blood , vol.96 , pp. 3086-3093
    • Agerberth, B.1    Charo, J.2    Werr, J.3    Olsson, B.4    Idali, F.5    Lindbom, L.6
  • 4
    • 0036166552 scopus 로고    scopus 로고
    • Antimicrobial peptides isolated from the skin secretions of Chinese red belly toad Bombina maxima
    • Ali M.F., Soto A., Knoop F.C., Conlon J.M. Antimicrobial peptides isolated from the skin secretions of Chinese red belly toad Bombina maxima. Peptides. 23:2002;427-435.
    • (2002) Peptides , vol.23 , pp. 427-435
    • Ali, M.F.1    Soto, A.2    Knoop, F.C.3    Conlon, J.M.4
  • 5
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: An overview
    • Andreu D., Rivas L. Animal antimicrobial peptides: an overview. Biopolymers. 47:1998;415-433.
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 7
    • 0030012762 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins
    • Aymerich T., Holo H., Havastein L.S., Hugas M., Garriga M., Nes I.F. Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins. Appl. Environ. Microbiol. 62:1996;1676-1682.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1676-1682
    • Aymerich, T.1    Holo, H.2    Havastein, L.S.3    Hugas, M.4    Garriga, M.5    Nes, I.F.6
  • 8
    • 0029047938 scopus 로고
    • Amphibian skin: A promising resource for antimicrobial peptides
    • Barra D., Simmaco M. Amphibian skin: a promising resource for antimicrobial peptides. Trends Biotechnol. 13:1995;205-209.
    • (1995) Trends Biotechnol. , vol.13 , pp. 205-209
    • Barra, D.1    Simmaco, M.2
  • 10
    • 0035815466 scopus 로고    scopus 로고
    • A novel heterodimeric antimicrobial peptide from the tree-frog Phyllomedusa distincta
    • Batista C.V.F., Scaloni A., Rigden D.J., Silva L.R., Romero A.R., Dukor R.et al. A novel heterodimeric antimicrobial peptide from the tree-frog Phyllomedusa distincta. FEBS Lett. 494:2001;85-89.
    • (2001) FEBS Lett. , vol.494 , pp. 85-89
    • Batista, C.V.F.1    Scaloni, A.2    Rigden, D.J.3    Silva, L.R.4    Romero, A.R.5    Dukor, R.6
  • 12
    • 0036137074 scopus 로고    scopus 로고
    • In vitro antiviral activity of dermaseptins against herpes simplex virus type 1
    • Belaid A., Aouni M., Khelifa R., Trabelsi A., Jemmali M., Hani K. In vitro antiviral activity of dermaseptins against herpes simplex virus type 1. J. Med. Virol. 66:2002;229-234.
    • (2002) J. Med. Virol. , vol.66 , pp. 229-234
    • Belaid, A.1    Aouni, M.2    Khelifa, R.3    Trabelsi, A.4    Jemmali, M.5    Hani, K.6
  • 13
    • 0003123005 scopus 로고
    • Mechanism of channel-forming lantibiotics in black lipid membranes
    • G. Jung, & H.-G. Sahl. Leiden: ESCOM
    • Benz R., Jung G., Sahl H.-G. Mechanism of channel-forming lantibiotics in black lipid membranes. Jung G., Sahl H.-G. Nisin and novel lantibiotics. 1991;359-372 ESCOM, Leiden.
    • (1991) Nisin and novel lantibiotics , pp. 359-372
    • Benz, R.1    Jung, G.2    Sahl, H.-G.3
  • 14
    • 0028694311 scopus 로고
    • Antimicrobial peptides as agents of mucosal immunity
    • H.G. Bomam, J. Marsh, & J.A. Goode. New York: Wiley
    • Bevins C.L. Antimicrobial peptides as agents of mucosal immunity. Bomam H.G., Marsh J., Goode J.A. Antimicrobial peptides. 1994;250-269 Wiley, New York.
    • (1994) Antimicrobial peptides , pp. 250-269
    • Bevins, C.L.1
  • 15
    • 0031733351 scopus 로고    scopus 로고
    • Heterologous expression of the bacteriocin mesentericin Y105 using the dedicated transport system and the general secretion pathway
    • Biet F., Berjeaud J.M., Worobo R.W., Cenatempo Y., Fremaux C. Heterologous expression of the bacteriocin mesentericin Y105 using the dedicated transport system and the general secretion pathway. Microbiology. 144:1998;2845-2854.
    • (1998) Microbiology , vol.144 , pp. 2845-2854
    • Biet, F.1    Berjeaud, J.M.2    Worobo, R.W.3    Cenatempo, Y.4    Fremaux, C.5
  • 17
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman H.G. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13:1995;61-92.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 18
    • 0029971979 scopus 로고    scopus 로고
    • Peptide antibiotics: Holy or heretic grails of innate immunity?
    • Boman H.G. Peptide antibiotics: holy or heretic grails of innate immunity? Scand. J. Immunol. 43:1996;475-482.
    • (1996) Scand. J. Immunol. , vol.43 , pp. 475-482
    • Boman, H.G.1
  • 20
    • 0029347190 scopus 로고
    • Plant defensins: Novel anti-microbial peptides as components of the host defense system
    • Broekaert W.F., Terras F.R.G., Cammue B.P.A., Osborn R.W. Plant defensins: novel anti-microbial peptides as components of the host defense system. Plant Physiol. 108:1995;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
  • 21
    • 0023806662 scopus 로고
    • Structure and expression of the gene encoding the presursor of nisin, a small protein antibiotic
    • Buchman G.W., Banerjee S., Hansen J.N. Structure and expression of the gene encoding the presursor of nisin, a small protein antibiotic. J. Biol. Chem. 263:1988;16260-16266.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16260-16266
    • Buchman, G.W.1    Banerjee, S.2    Hansen, J.N.3
  • 22
    • 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. A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution. J. Biol. Chem. 268:1993;14893-14897.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14893-14897
    • Bulet, P.1    Dimarcq, J.L.2    Hetru, C.3    Lagueux, M.4    Charlet, M.5    Hegy, G.6
  • 24
    • 0031736824 scopus 로고    scopus 로고
    • Use of a genetically enhanced, pediocin-producing starter culture, Lactococcus lactis subsp. lactis MM217, to contro Listeria monocytogenes in Cheddar cheese
    • Buyong N., Kok J., Luchansky J.B. Use of a genetically enhanced, pediocin-producing starter culture, Lactococcus lactis subsp. lactis MM217, to contro Listeria monocytogenes in Cheddar cheese. Appl. Environ. Microbiol. 64:1998;4842-4845.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4842-4845
    • Buyong, N.1    Kok, J.2    Luchansky, J.B.3
  • 27
    • 0024454751 scopus 로고
    • Apidaecins: Antibacterial peptides from honeybees
    • Casteels P., Ampe C., Jacobs F., Vaeck M., Tempst P. Apidaecins: antibacterial peptides from honeybees. EMBO J. 8:1989;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
  • 28
    • 0030038197 scopus 로고    scopus 로고
    • Identification of defensin-1, defensin-2 and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils
    • Chertov O., Michiel D.F., Xu L., Wang J.M., Tani K., Murphy W.J.et al. Identification of defensin-1, defensin-2 and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils. J. Biol. Chem. 271:1996;2935-2940.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2935-2940
    • Chertov, O.1    Michiel, D.F.2    Xu, L.3    Wang, J.M.4    Tani, K.5    Murphy, W.J.6
  • 29
    • 0027424936 scopus 로고
    • Pediocin PA-1, a bacteriocin from Pediococcus acidilactici PAC1.0, forms hydrophilic pores in the cytoplasmic membrane of target cells
    • Chikindas M.L., Garcia-Garcera M.J., Driessen A.M., Lederboer A.M., Nissen-Meyer J., Nes I.F.et al. Pediocin PA-1, a bacteriocin from Pediococcus acidilactici PAC1.0, forms hydrophilic pores in the cytoplasmic membrane of target cells. Appl. Environ. Microbiol. 59:1993;3577-3584.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3577-3584
    • Chikindas, M.L.1    Garcia-Garcera, M.J.2    Driessen, A.M.3    Lederboer, A.M.4    Nissen-Meyer, J.5    Nes, I.F.6
  • 31
    • 0028177604 scopus 로고
    • Ranalexin: A novel antimicrobial peptide from bullfrog skin, structurally related to the bacterial antibiotic, polymyxin
    • Clark D.P., Durell S., Maloy W.L., Zasloff M. Ranalexin: a novel antimicrobial peptide from bullfrog skin, structurally related to the bacterial antibiotic, polymyxin. J. Biol. Chem. 269:1994;10849-10855.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10849-10855
    • Clark, D.P.1    Durell, S.2    Maloy, W.L.3    Zasloff, M.4
  • 32
    • 0032851505 scopus 로고    scopus 로고
    • Cloning and expression of the pediocin operon in Streptococcus thermophilus and other lactic fermentation bacteria
    • Coderre P.E., Somkuti G.A. Cloning and expression of the pediocin operon in Streptococcus thermophilus and other lactic fermentation bacteria. Curr. Microbiol. 39:1999;295-301.
    • (1999) Curr. Microbiol. , vol.39 , pp. 295-301
    • Coderre, P.E.1    Somkuti, G.A.2
  • 33
    • 0002236517 scopus 로고
    • Applications and interactions of bacteriocins from lactic acid bacteria in food and beverages
    • D.G. Hoover, & L.R. Steenson. USA: Academic Press
    • Daeschel M.A. Applications and interactions of bacteriocins from lactic acid bacteria in food and beverages. Hoover D.G., Steenson L.R. Bacteriocins of lactic acid bacteria. 1993;63-91 Academic Press, USA.
    • (1993) Bacteriocins of lactic acid bacteria , pp. 63-91
    • Daeschel, M.A.1
  • 36
    • 0021131604 scopus 로고
    • Isolation and characterization of microcin E492 from Klebsiella pneumoniae
    • De Lorenzo V. Isolation and characterization of microcin E492 from Klebsiella pneumoniae. Arch. Microbiol. 139:1984;72-75.
    • (1984) Arch. Microbiol. , vol.139 , pp. 72-75
    • De Lorenzo, V.1
  • 37
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
    • de Ruyter P.G.G.A., Kuipers O.P., de Vos W.M. Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl. Environ. Microbiol. 62:1996;3662-3667.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3662-3667
    • De Ruyter, P.G.G.A.1    Kuipers, O.P.2    De Vos, W.M.3
  • 38
    • 0033152420 scopus 로고    scopus 로고
    • Gene expression systems for lactic acid bacteria
    • de Vos W.M. Gene expression systems for lactic acid bacteria. Curr. Opin. Microbiol. 2:1999;289-295.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 289-295
    • De Vos, W.M.1
  • 40
    • 0029900207 scopus 로고    scopus 로고
    • Inducible expression of an antibiotic peptide gene in lipopolysaccharide-challenged tracheal apithelial cells
    • Diamond G., Russell J.P., Bevins C.L. Inducible expression of an antibiotic peptide gene in lipopolysaccharide-challenged tracheal apithelial cells. Proc. Natl. Acad. Sci. U. S. A. 93:1996;5156-5160.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 5156-5160
    • Diamond, G.1    Russell, J.P.2    Bevins, C.L.3
  • 41
    • 0025313209 scopus 로고
    • Insect immunity: Expression of the two major inducible antibacterial peptides, defensin and diptericin, in Phormia terranovae
    • Dimarcq J.L., Zachary D., Hoffmann J.A., Hoffmann D., Reichart J.-L. Insect immunity: expression of the two major inducible antibacterial peptides, defensin and diptericin, in Phormia terranovae. EMBO J. 9:1990;2507-2515.
    • (1990) EMBO J. , vol.9 , pp. 2507-2515
    • Dimarcq, J.L.1    Zachary, D.2    Hoffmann, J.A.3    Hoffmann, D.4    Reichart, J.-L.5
  • 42
    • 0032411402 scopus 로고    scopus 로고
    • Cysteine-rich antimicrobial peptides in invertebrates
    • Dimarcq J.L., Bulet P., Hetru C., Hoffmann J. Cysteine-rich antimicrobial peptides in invertebrates. Biopolymers. 47:1998;465-478.
    • (1998) Biopolymers , vol.47 , pp. 465-478
    • Dimarcq, J.L.1    Bulet, P.2    Hetru, C.3    Hoffmann, J.4
  • 43
    • 0025356864 scopus 로고
    • Analysis of the genetic determinants for the production of the peptide antibiotic nisin
    • Dodd H.M., Horn N., Gasson M.J. Analysis of the genetic determinants for the production of the peptide antibiotic nisin. J. Gen. Microbiol. 136:1990;555-566.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 555-566
    • Dodd, H.M.1    Horn, N.2    Gasson, M.J.3
  • 45
    • 0037025297 scopus 로고    scopus 로고
    • Direct interaction of dermaseptin S4 aminoheptanoyl derivative with intraerythrocytic malaria parasite leading to increased specific antiparasitic activity culture
    • Efron L., Dagan A., Gaidukov L., Ginsburg H., Mor A. Direct interaction of dermaseptin S4 aminoheptanoyl derivative with intraerythrocytic malaria parasite leading to increased specific antiparasitic activity culture. J. Biol. Chem. 277:2002;24067-24072.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24067-24072
    • Efron, L.1    Dagan, A.2    Gaidukov, L.3    Ginsburg, H.4    Mor, A.5
  • 46
    • 9444225012 scopus 로고    scopus 로고
    • Mode of action of the antimicrobial peptide indoolicin
    • Falla T.J., Karunaratne D.N., Hancock R.E.W. Mode of action of the antimicrobial peptide indoolicin. J. Biol. Chem. 271:1996;19298-19303.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19298-19303
    • Falla, T.J.1    Karunaratne, D.N.2    Hancock, R.E.W.3
  • 47
    • 0025951915 scopus 로고
    • Listeria monocytogenes, a food-born pathogen
    • Farber J.M., Peterkin P.I. Listeria monocytogenes, a food-born pathogen. Microbiol. Rev. 55:1991;476-511.
    • (1991) Microbiol. Rev. , vol.55 , pp. 476-511
    • Farber, J.M.1    Peterkin, P.I.2
  • 48
    • 0034818366 scopus 로고    scopus 로고
    • Affinity driven malecular transfer from erythrocyte membrane to target cells
    • Feder R., Nehushtai R., Mor A. Affinity driven malecular transfer from erythrocyte membrane to target cells. Peptides. 22:2001;440-447.
    • (2001) Peptides , vol.22 , pp. 440-447
    • Feder, R.1    Nehushtai, R.2    Mor, A.3
  • 49
    • 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., Briand J.-P., Roussel J.-P., Letellier L.et al. Structure activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proc. Natl. Acad. Sci. U. S. A. 93:1996;1221-1225.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1221-1225
    • Fehlbaum, P.1    Bulet, P.2    Chernysh, S.3    Briand, J.-P.4    Roussel, J.-P.5    Letellier, L.6
  • 50
    • 0036038834 scopus 로고    scopus 로고
    • A novel antimicrobial function for a ribosomal peptide from rainbow trout skin
    • Fernandes J.M.O., Smith V.J. A novel antimicrobial function for a ribosomal peptide from rainbow trout skin. Biochem. Biophys. Res. Comm. 296:2002;167-171.
    • (2002) Biochem. Biophys. Res. Comm. , vol.296 , pp. 167-171
    • Fernandes, J.M.O.1    Smith, V.J.2
  • 51
    • 0029938277 scopus 로고    scopus 로고
    • The effect of nisin on Listeria monocytogenes in culture medium and long-life cottage cheese
    • Ferreira M.A.S.S., Lund B.M. The effect of nisin on Listeria monocytogenes in culture medium and long-life cottage cheese. Lett. Appl. Microbiol. 22:1996;433-438.
    • (1996) Lett. Appl. Microbiol. , vol.22 , pp. 433-438
    • Ferreira, M.A.S.S.1    Lund, B.M.2
  • 52
    • 0029833708 scopus 로고    scopus 로고
    • New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: The C-terminal region is important for determining specificity
    • Fimland G., Blingsmo O., Sletten K., Jung G., Nes I.F., Nissen-Meyer J. New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: the C-terminal region is important for determining specificity. Appl. Environ. Microbiol. 62:1996;3313-3318.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3313-3318
    • Fimland, G.1    Blingsmo, O.2    Sletten, K.3    Jung, G.4    Nes, I.F.5    Nissen-Meyer, J.6
  • 53
    • 0036230805 scopus 로고    scopus 로고
    • Characterization of the genetic locus responsible for the production of ABP-118, a novel bacteriocin produced by the probiotic bacterium Lactobacillus salivarius subsp. Salivarius UCC118
    • Flynn S., van Sinderen D., Thornton G.M., Holo H., Nes I.F., Collins J.K. Characterization of the genetic locus responsible for the production of ABP-118, a novel bacteriocin produced by the probiotic bacterium Lactobacillus salivarius subsp. Salivarius UCC118. Microbiology. 148:2002;973-984.
    • (2002) Microbiology , vol.148 , pp. 973-984
    • Flynn, S.1    Van Sinderen, D.2    Thornton, G.M.3    Holo, H.4    Nes, I.F.5    Collins, J.K.6
  • 57
    • 0029094242 scopus 로고
    • Mesentericin Y105 gene clusters in Leuconostoc mesenteroides Y105
    • Fremaux C., Hechard Y., Cenatiempo Y. Mesentericin Y105 gene clusters in Leuconostoc mesenteroides Y105. Microbiology. 141:1995;1637-1645.
    • (1995) Microbiology , vol.141 , pp. 1637-1645
    • Fremaux, C.1    Hechard, Y.2    Cenatiempo, Y.3
  • 58
    • 0028707742 scopus 로고
    • Biosynthesis of defensins and other antimicrobial peptides
    • H.G. Bomam, J. Marsh, & J.A. Goode. New York: Wiley
    • Ganz T. Biosynthesis of defensins and other antimicrobial peptides. Bomam H.G., Marsh J., Goode J.A. Antimicrobial peptides. 1994;62-76 Wiley, New York.
    • (1994) Antimicrobial peptides , pp. 62-76
    • Ganz, T.1
  • 59
    • 0033569682 scopus 로고    scopus 로고
    • Defensins and host defense
    • Ganz T. Defensins and host defense. Science. 286:1999;420-421.
    • (1999) Science , vol.286 , pp. 420-421
    • Ganz, T.1
  • 60
    • 0032005344 scopus 로고    scopus 로고
    • Antimicrobial peptides of vertebrates
    • Ganz T., Lehler R.I. Antimicrobial peptides of vertebrates. Curr. Opin. Immunol. 10:1998;41-44.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 41-44
    • Ganz, T.1    Lehler, R.I.2
  • 61
    • 0032425948 scopus 로고    scopus 로고
    • Plant defense peptides
    • Garcia-Olmedo F.et al. Plant defense peptides. Biopolymers. 47:1998;479-491.
    • (1998) Biopolymers , vol.47 , pp. 479-491
    • Garcia-Olmedo, F.1
  • 62
    • 0036589172 scopus 로고    scopus 로고
    • Two-peptide bacteriocins produced by lactic acid bacteria
    • Garneau S., Martin N., Vederas J.C. Two-peptide bacteriocins produced by lactic acid bacteria. Biochimie. 84:2002;577-592.
    • (2002) Biochimie , vol.84 , pp. 577-592
    • Garneau, S.1    Martin, N.2    Vederas, J.C.3
  • 63
    • 0027953945 scopus 로고
    • Mode of action of the antibacterial cecropin B2: A spectrofluorimetric study
    • Gazit E., Lee W.-J., Brey P.T., Shai Y. Mode of action of the antibacterial cecropin B2: a spectrofluorimetric study. Biochemistry. 33:1994;10681-10692.
    • (1994) Biochemistry , vol.33 , pp. 10681-10692
    • Gazit, E.1    Lee, W.-J.2    Brey, P.T.3    Shai, Y.4
  • 64
    • 0026354641 scopus 로고
    • Bombinin-like peptides with antimicrobial activity from skin secretions of the asian toad, Bombina orientalis
    • Gibson B.W., Tang D., Mandrell R., Kelly M., Spindel E.R. Bombinin-like peptides with antimicrobial activity from skin secretions of the asian toad, Bombina orientalis. J. Biol. Chem. 266:1991;23103-23111.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23103-23111
    • Gibson, B.W.1    Tang, D.2    Mandrell, R.3    Kelly, M.4    Spindel, E.R.5
  • 65
    • 0027971912 scopus 로고
    • Genetic structure of the Enterococcus faecalis plasmid pAD1-encoded cytolytic toxin system and its relationship to lantibiotic determinants
    • Gilmore M.S., Segarra R.A., Booth M.C., Bogie C.P., Hall L.R., Clewell D.B. Genetic structure of the Enterococcus faecalis plasmid pAD1-encoded cytolytic toxin system and its relationship to lantibiotic determinants. J. Bacteriol. 176:1994;7335-7344.
    • (1994) J. Bacteriol. , vol.176 , pp. 7335-7344
    • Gilmore, M.S.1    Segarra, R.A.2    Booth, M.C.3    Bogie, C.P.4    Hall, L.R.5    Clewell, D.B.6
  • 66
    • 0033851437 scopus 로고    scopus 로고
    • Post-translationally modified bacteriocins - The lantibiotics
    • Gudder A., Wiedemann I., Sahl H.-G. Post-translationally modified bacteriocins - the lantibiotics. Biopolymers. 55:2000;62-73.
    • (2000) Biopolymers , vol.55 , pp. 62-73
    • Gudder, A.1    Wiedemann, I.2    Sahl, H.-G.3
  • 67
    • 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
    • Gudmudsson G.H., Magnusson K.P., Chowdhary B.P., Johansson M., Andersson L., Boman H.G. 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. U. S. A. 92:1995;7085-7089.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 7085-7089
    • Gudmudsson, G.H.1    Magnusson, K.P.2    Chowdhary, B.P.3    Johansson, M.4    Andersson, L.5    Boman, H.G.6
  • 68
    • 0029893253 scopus 로고    scopus 로고
    • The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes
    • Gudmundsson G.H., 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. 328:1996;325-332.
    • (1996) Eur. J. Biochem. , vol.328 , pp. 325-332
    • Gudmundsson, G.H.1    Agerberth, B.2    Odeberg, J.3    Bergman, T.4    Olsson, B.5    Salcedo, R.6
  • 69
    • 0024354115 scopus 로고
    • Effects of magainins and cecropin on the sporogonic development of malaria parasites in mosquitoes
    • Gwadz R.W., Kaslow D., Lee J.Y., Maloy W.L., Zasloff M., Miller L.H. Effects of magainins and cecropin on the sporogonic development of malaria parasites in mosquitoes. Infect. Immun. 57:1989;2628-2633.
    • (1989) Infect. Immun. , vol.57 , pp. 2628-2633
    • Gwadz, R.W.1    Kaslow, D.2    Lee, J.Y.3    Maloy, W.L.4    Zasloff, M.5    Miller, L.H.6
  • 70
    • 0029609285 scopus 로고
    • Moricin, A novel type of antibacterial peptide isolated from the silkworm, Bombyx mori
    • Hara S., Yamakawa M. Moricin, A novel type of antibacterial peptide isolated from the silkworm, Bombyx mori. J. Biol. Chem. 270:1995;29923-29927.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29923-29927
    • Hara, S.1    Yamakawa, M.2
  • 73
    • 0025719296 scopus 로고
    • Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum
    • Hastings J.W., Sailer M., Johnson K., Roy K.L., Vederas J.C., Stiles M.E. Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum. J. Bacteriol. 173:1991;7491-7500.
    • (1991) J. Bacteriol. , vol.173 , pp. 7491-7500
    • Hastings, J.W.1    Sailer, M.2    Johnson, K.3    Roy, K.L.4    Vederas, J.C.5    Stiles, M.E.6
  • 74
    • 0035941062 scopus 로고    scopus 로고
    • The antimicrobial peptides lactofeeicin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm
    • Haukland H.H., Ulvatne H., Sandvik K., Vorland L.H. The antimicrobial peptides lactofeeicin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm. FEBS Lett. 508:2001;389-393.
    • (2001) FEBS Lett. , vol.508 , pp. 389-393
    • Haukland, H.H.1    Ulvatne, H.2    Sandvik, K.3    Vorland, L.H.4
  • 75
    • 0027080504 scopus 로고
    • Characterization and purification of mesentericin Y105, an anti-Listeria bacteriocin from Leuconostoc mesenteroides
    • Héchard Y., Derijard D.B., Latellier F., Cenatiampo Y. Characterization and purification of mesentericin Y105, an anti-Listeria bacteriocin from Leuconostoc mesenteroides. J. Gen. Microbiol. 138:1992;2725-2731.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2725-2731
    • Héchard, Y.1    Derijard, D.B.2    Latellier, F.3    Cenatiampo, Y.4
  • 76
    • 0026724915 scopus 로고
    • Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilacttici PAC-1.0
    • Henderson J.T., Chopko A.L., Van Wassenaar P.D. Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilacttici PAC-1.0. Arch. Biochem. Biophys. 295:1992;5-12.
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 5-12
    • Henderson, J.T.1    Chopko, A.L.2    Van Wassenaar, P.D.3
  • 77
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8:1992;67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 78
  • 79
    • 0027077825 scopus 로고
    • Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706
    • Holck A., Axelsson L., Birkeland S.-E., Aukrust T., Blom H. Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706. J. Gen. Microbiol. 138:1992;2715-2720.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2715-2720
    • Holck, A.1    Axelsson, L.2    Birkeland, S.-E.3    Aukrust, T.4    Blom, H.5
  • 80
    • 0025861639 scopus 로고
    • Lactococcin, A, a new bacteriocin from Lactococcus lactis subsp. cremoris: Isolation and characterization of the protein and its gene
    • Holo H., Nilssen O., Nes I.F. Lactococcin, A, a new bacteriocin from Lactococcus lactis subsp. cremoris: isolation and characterization of the protein and its gene. J. Bacteriol. 173:1991;3879-3887.
    • (1991) J. Bacteriol. , vol.173 , pp. 3879-3887
    • Holo, H.1    Nilssen, O.2    Nes, I.F.3
  • 81
    • 0035081130 scopus 로고    scopus 로고
    • Plantaricin W from Lactobacillus plantarum belongs to a new family of two-petide lantibiotics
    • Holo H., Jeknic Z., Daeschel M., Stevanovic S., Nes I.F. Plantaricin W from Lactobacillus plantarum belongs to a new family of two-petide lantibiotics. Microbiology. 147:2001;643-651.
    • (2001) Microbiology , vol.147 , pp. 643-651
    • Holo, H.1    Jeknic, Z.2    Daeschel, M.3    Stevanovic, S.4    Nes, I.F.5
  • 82
    • 0028876862 scopus 로고
    • Biological preservation of foods with reference to protective cultures, bacteriocins and food-grade enzymes
    • Holzapfel W.H., Geisen R., Schillinger U. Biological preservation of foods with reference to protective cultures, bacteriocins and food-grade enzymes. Int. J. Food Microbiol. 24:1995;343-362.
    • (1995) Int. J. Food Microbiol. , vol.24 , pp. 343-362
    • Holzapfel, W.H.1    Geisen, R.2    Schillinger, U.3
  • 83
    • 0025739039 scopus 로고
    • Nisin biosynthesis genes are encoded by a novel conjugative transposon
    • Horn N., Swindell S., Dodd H., Gasson M.J. Nisin biosynthesis genes are encoded by a novel conjugative transposon. Mol. Gen. Genetics. 228:1991;129-135.
    • (1991) Mol. Gen. Genetics , vol.228 , pp. 129-135
    • Horn, N.1    Swindell, S.2    Dodd, H.3    Gasson, M.J.4
  • 85
    • 0030176383 scopus 로고    scopus 로고
    • Bacteriocin J46, a new bacteriocin produced by Lactococcus lactis subsp. cremoris J46: Isolation and characterization of the protein and its gene
    • Hout E., Meghrous J., Barrena-Gonzalez C., Petitdemange H. Bacteriocin J46, a new bacteriocin produced by Lactococcus lactis subsp. cremoris J46: isolation and characterization of the protein and its gene. Anaerobe. 2:1996;137-145.
    • (1996) Anaerobe , vol.2 , pp. 137-145
    • Hout, E.1    Meghrous, J.2    Barrena-Gonzalez, C.3    Petitdemange, H.4
  • 86
    • 0028724575 scopus 로고
    • Drosophila as a model system for antibacterial peptides
    • H.G. Bomam, J. Marsh, & J.A. Goode. New York: Wiley
    • Hultmark D. Drosophila as a model system for antibacterial peptides. Bomam H.G., Marsh J., Goode J.A. Antimicrobial petides. 1994;107-122 Wiley, New York.
    • (1994) Antimicrobial petides , pp. 107-122
    • Hultmark, D.1
  • 87
    • 0029167301 scopus 로고
    • The codon usage of the nisin Z operon in Lactococcus lactis N8 suggests a non-lactococcal origin of the conjugative nisin-sucrose transposon
    • Immonen Y., Ye S., Ra R., Qiao M., Paulin L., Saris P.E.J. The codon usage of the nisin Z operon in Lactococcus lactis N8 suggests a non-lactococcal origin of the conjugative nisin-sucrose transposon. Sequence. 5:1995;203-218.
    • (1995) Sequence , vol.5 , pp. 203-218
    • Immonen, Y.1    Ye, S.2    Ra, R.3    Qiao, M.4    Paulin, L.5    Saris, P.E.J.6
  • 88
    • 0036170116 scopus 로고    scopus 로고
    • Antimicrobial peptides with atypical structural features from the skin of the Japanese brown frog Rana japonica
    • Isaacson T., Soto A., Iwamuro S., Knoop F.C., Conlon J.M. Antimicrobial peptides with atypical structural features from the skin of the Japanese brown frog Rana japonica. Peptides. 23:2002;419-425.
    • (2002) Peptides , vol.23 , pp. 419-425
    • Isaacson, T.1    Soto, A.2    Iwamuro, S.3    Knoop, F.C.4    Conlon, J.M.5
  • 89
    • 0029741789 scopus 로고    scopus 로고
    • Characterization of the chemical and antimicrobial properties of piscicolin 126, a bacteriocin produced by Carnobacterium piscicola JG 126
    • Jack R.W., Wan J., Gordon J., Harmark K., Davidson B.E., Hillier A.J.et al. Characterization of the chemical and antimicrobial properties of piscicolin 126, a bacteriocin produced by Carnobacterium piscicola JG 126. Appl. Environ. Microbiol. 62:1996;2897-2903.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2897-2903
    • Jack, R.W.1    Wan, J.2    Gordon, J.3    Harmark, K.4    Davidson, B.E.5    Hillier, A.J.6
  • 90
    • 0022465775 scopus 로고
    • Characterization and purification of helveticin J and evidense for a chromosomally determined bacteriocin produced by Lactobacillus helveticus 481
    • Joerger M.C., Klaenhammer T.R. Characterization and purification of helveticin J and evidense for a chromosomally determined bacteriocin produced by Lactobacillus helveticus 481. J. Bacteriol. 167:1986;439-446.
    • (1986) J. Bacteriol. , vol.167 , pp. 439-446
    • Joerger, M.C.1    Klaenhammer, T.R.2
  • 93
    • 0028921701 scopus 로고
    • Isolation and characterization of acidocin A and cloning of the bacteriocin gene from Lactobacillus acidophilus
    • Kanatani K., Oshimura M., Sano K. Isolation and characterization of acidocin A and cloning of the bacteriocin gene from Lactobacillus acidophilus. Appl. Environ. Microbiol. 61:1995;1061-1067.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1061-1067
    • Kanatani, K.1    Oshimura, M.2    Sano, K.3
  • 95
    • 0035183366 scopus 로고    scopus 로고
    • Antimicrobial peptides from the skin of the Japanese mountain frog, Rana ornativentris
    • Kim J.B., Iwamuro S., Knoop F.C., Conlon J.M. Antimicrobial peptides from the skin of the Japanese mountain frog, Rana ornativentris. J. Pept. Res. 58:2001;349-356.
    • (2001) J. Pept. Res. , vol.58 , pp. 349-356
    • Kim, J.B.1    Iwamuro, S.2    Knoop, F.C.3    Conlon, J.M.4
  • 96
    • 0027199706 scopus 로고
    • Genetics of bacteriocins produced by lactic acid bacteria
    • Klaenhammer T.R. Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiol. Rev. 12:1993;39-86.
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 39-86
    • Klaenhammer, T.R.1
  • 97
    • 0030721749 scopus 로고    scopus 로고
    • Controlled gene expression systems for lactic acid bacteria: Transferable nisin-inducible cassettes for Lactococcus, Leuconostoc, and Lactobacillus spp.
    • Kleerebezem M., Beerthuyzen M.M., vaughan E.E., de Vos W.M., Kuipers O.P. Controlled gene expression systems for lactic acid bacteria: transferable nisin-inducible cassettes for Lactococcus, Leuconostoc, and Lactobacillus spp. Appl. Environ. Microbiol. 63:1997;4581-4584.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4581-4584
    • Kleerebezem, M.1    Beerthuyzen, M.M.2    Vaughan, E.E.3    De Vos, W.M.4    Kuipers, O.P.5
  • 98
    • 0027169823 scopus 로고
    • Protegrins: Leucocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins
    • Kokryakov V.N., Harwig S.S.L., Panyutich E.A., Shevchenko A.A., Aleshina G.M., Shamova O.V.et al. Protegrins: leucocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins. FEBS Lett. 327:1993;231-236.
    • (1993) FEBS Lett. , vol.327 , pp. 231-236
    • Kokryakov, V.N.1    Harwig, S.S.L.2    Panyutich, E.A.3    Shevchenko, A.A.4    Aleshina, G.M.5    Shamova, O.V.6
  • 99
    • 0026663308 scopus 로고
    • Genetics of ribosomally synthesized peptide antibiotics
    • Kolter R., Moreno F. Genetics of ribosomally synthesized peptide antibiotics. Annu. Rev. Microbiol. 46:1992;141-163.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 141-163
    • Kolter, R.1    Moreno, F.2
  • 100
    • 0028695274 scopus 로고
    • Antimicrobial peptides from amphibian skin: An overview
    • H.G. Bomam, J. Marsh, & J.A. Goode. New York: Wiley
    • Kreil G. Antimicrobial peptides from amphibian skin: an overview. Bomam H.G., Marsh J., Goode J.A. Antimicrobial peptides. 1994;77-90 Wiley, New York.
    • (1994) Antimicrobial peptides , pp. 77-90
    • Kreil, G.1
  • 104
    • 0037053317 scopus 로고    scopus 로고
    • Structural requirements for potent versus seãlective cytoxicity for antimicrobial dermaseptin S4 derivatives
    • Kustanovich I., Shalev D.E., Mikhlin M., Gaidukov L., Mor A. Structural requirements for potent versus seãlective cytoxicity for antimicrobial dermaseptin S4 derivatives. J. Biol. Chem. 277:2002;16941-16951.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16941-16951
    • Kustanovich, I.1    Shalev, D.E.2    Mikhlin, M.3    Gaidukov, L.4    Mor, A.5
  • 107
    • 0029889071 scopus 로고    scopus 로고
    • Purification and characterization of N-β-alanyl-5-S-gluthathionyl-3, 4-dihydroxyphenylalanine, a novel antibacterial substance of Sarcophaga peregrina (Flesh fly)
    • Leem J.Y., Nishimura C., Kurata S., Shimada I., Kobayashi A., Natori S. Purification and characterization of N-β-alanyl-5-S-gluthathionyl-3,4- dihydroxyphenylalanine, a novel antibacterial substance of Sarcophaga peregrina (Flesh fly). J. Biol. Chem. 271:1996;13573-13577.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13573-13577
    • Leem, J.Y.1    Nishimura, C.2    Kurata, S.3    Shimada, I.4    Kobayashi, A.5    Natori, S.6
  • 108
    • 0032946285 scopus 로고    scopus 로고
    • Isolation of p-hydroxycinnamaldehyde as an antibacterial substance from the saw fly. Acantholyda parki S.
    • Leem J.Y., Jeong I.J., Park K.T., Park H.Y. Isolation of p-hydroxycinnamaldehyde as an antibacterial substance from the saw fly. Acantholyda parki S. FEBS Lett. 442:1999;53-56.
    • (1999) FEBS Lett. , vol.442 , pp. 53-56
    • Leem, J.Y.1    Jeong, I.J.2    Park, K.T.3    Park, H.Y.4
  • 109
    • 0029121699 scopus 로고
    • Genetic analysis of acidocin, B, a novel bacteriocin produced by Lactobacilllus acidophilus
    • Leer R.J., van der Vossen J.M., van Giezen M., van Noort J.M., Pouwels P.H. Genetic analysis of acidocin, B, a novel bacteriocin produced by Lactobacilllus acidophilus. Microbiology. 141:1995;1629-1635.
    • (1995) Microbiology , vol.141 , pp. 1629-1635
    • Leer, R.J.1    Van Der Vossen, J.M.2    Van Giezen, M.3    Van Noort, J.M.4    Pouwels, P.H.5
  • 110
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defense
    • Lehler R.I., 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
    • Lehler, R.I.1    Ganz, T.2
  • 111
    • 0027474382 scopus 로고
    • Defensins: Antimicrobial and cytotoxic peptides in mammalian cells
    • Lehler R.I., Lichtenstein A.K., Ganz T. Defensins: antimicrobial and cytotoxic peptides in mammalian cells. Annu. Rev. Immunol. 11:1993;105-128.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 105-128
    • Lehler, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 112
    • 0035077760 scopus 로고    scopus 로고
    • Enhanced disease resistance conferred by expression of an antimicrobial magainin analog in transgenic tobacco
    • Li Q., Laerence C.B., Xing H.-Y., Babbitt R.A., Bass W.T., Maiti I.B., Everett N.P. Enhanced disease resistance conferred by expression of an antimicrobial magainin analog in transgenic tobacco. Planta. 212:2001;635-639.
    • (2001) Planta , vol.212 , pp. 635-639
    • Li, Q.1    Laerence, C.B.2    Xing, H.-Y.3    Babbitt, R.A.4    Bass, W.T.5    Maiti, I.B.6    Everett, N.P.7
  • 113
    • 0015663984 scopus 로고
    • Additional antibiotic inhibitors of peptidoglycan biosynthesis
    • Linnet P.E., Strominger J.L. Additional antibiotic inhibitors of peptidoglycan biosynthesis. Antimicrob. Agents Chemother. 4:1973;231-236.
    • (1973) Antimicrob. Agents Chemother. , vol.4 , pp. 231-236
    • Linnet, P.E.1    Strominger, J.L.2
  • 114
    • 0029584314 scopus 로고
    • Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptide
    • Mahoney M.M., Lee A.Y., Brezinski-Caliguri D.J., Huttner K.M. Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptide. FEBS Lett. 377:1995;519-522.
    • (1995) FEBS Lett. , vol.377 , pp. 519-522
    • Mahoney, M.M.1    Lee, A.Y.2    Brezinski-Caliguri, D.J.3    Huttner, K.M.4
  • 115
    • 0001093341 scopus 로고
    • Inhibition of Listeria monocytogenes in Camembert cheese made with a nisin-producing starter
    • Maisnier-Patin S., Deschamps N., Tatini S.R., Richard J. Inhibition of Listeria monocytogenes in Camembert cheese made with a nisin-producing starter. Le Lait. 72:1992;249-263.
    • (1992) Le Lait , vol.72 , pp. 249-263
    • Maisnier-Patin, S.1    Deschamps, N.2    Tatini, S.R.3    Richard, J.4
  • 116
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides S.C. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60:1996;512-538.
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 117
    • 0029051685 scopus 로고
    • Defensins and other endogenous antibiotics of vertebrates
    • Martin E., Ganz T., Lehler R.I. Defensins and other endogenous antibiotics of vertebrates. J. Leukoc. Biol. 58:1995;128-136.
    • (1995) J. Leukoc. Biol. , vol.58 , pp. 128-136
    • Martin, E.1    Ganz, T.2    Lehler, R.I.3
  • 118
    • 0033856851 scopus 로고    scopus 로고
    • Heterologous co-production of enterocin A and pediocin PA-1 by Lactococcus lactis: Detection by specific peptide-directed antibodies
    • Martinez J.M., Kok J., Sanders J.W., Hernandez P.E. Heterologous co-production of enterocin A and pediocin PA-1 by Lactococcus lactis: detection by specific peptide-directed antibodies. Appl. Environ. Microbiol. 66:2000;3543-3549.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3543-3549
    • Martinez, J.M.1    Kok, J.2    Sanders, J.W.3    Hernandez, P.E.4
  • 119
    • 0026681413 scopus 로고
    • Cloning, expression, and nucleotide sequence of genes involved in production of pediocin PA-1, a bacteriocin from Pediococcus acidilactici PAC1.0
    • Marugg J.D., Gonzalez C.F., Kunka B.S., Ledeboer A.M., Pucci M.J., Toonen M.Y.et al. Cloning, expression, and nucleotide sequence of genes involved in production of pediocin PA-1, a bacteriocin from Pediococcus acidilactici PAC1.0. Appl. Environ. Microbiol. 58:1992;2360-2367.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2360-2367
    • Marugg, J.D.1    Gonzalez, C.F.2    Kunka, B.S.3    Ledeboer, A.M.4    Pucci, M.J.5    Toonen, M.Y.6
  • 120
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers for forming a pore
    • Matsuzaki K., Murase O., Fujii N., Miyajima K. Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers for forming a pore. Biochemistry. 34:1995;128-136.
    • (1995) Biochemistry , vol.34 , pp. 128-136
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 121
    • 0034693283 scopus 로고    scopus 로고
    • Induction of synthesis of an antimicrobial peptide in the skin of the freeze-tolerant frog, Rana sylvatica, in response to environmental stimuli
    • Mattute B., Storey K.B., Knoop F.C., Conlon J.M. Induction of synthesis of an antimicrobial peptide in the skin of the freeze-tolerant frog, Rana sylvatica, in response to environmental stimuli. FEBS Lett. 483:2002;135-138.
    • (2002) FEBS Lett. , vol.483 , pp. 135-138
    • Mattute, B.1    Storey, K.B.2    Knoop, F.C.3    Conlon, J.M.4
  • 122
    • 0029802390 scopus 로고    scopus 로고
    • Expression of the antimicrobial peptide carnobacteriocin B2 by a signal peptide-dependent general secretory pathway
    • McCormick J.K., Worobo R.W., Stiles M.E. Expression of the antimicrobial peptide carnobacteriocin B2 by a signal peptide-dependent general secretory pathway. Appl. Environ. Microbiol. 62:1996;4095-4099.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4095-4099
    • McCormick, J.K.1    Worobo, R.W.2    Stiles, M.E.3
  • 123
    • 0031767742 scopus 로고    scopus 로고
    • Genetic characterization and heterologous expression of brochocin-C, an antibotulinal, two-peptide bacteriocin produced by Brochothrix campestris ATCC 43754
    • McCormick J.K., Poon A., Sailer M., Gao Y., Roy K.L., McMullen L.M.et al. Genetic characterization and heterologous expression of brochocin-C, an antibotulinal, two-peptide bacteriocin produced by Brochothrix campestris ATCC 43754. Appl. Environ. Microbiol. 64:1998;4757-4766.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4757-4766
    • McCormick, J.K.1    Poon, A.2    Sailer, M.3    Gao, Y.4    Roy, K.L.5    McMullen, L.M.6
  • 124
    • 0034830455 scopus 로고    scopus 로고
    • Involvement of Rel factors in the expression of antimicrobial peptide genes in amphibia
    • Miele R., Björklund G., Barra D., Simmaco M., Engström Y. Involvement of Rel factors in the expression of antimicrobial peptide genes in amphibia. Eur. J. Biochem. 268:2001;443-449.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 443-449
    • Miele, R.1    Björklund, G.2    Barra, D.3    Simmaco, M.4    Engström, Y.5
  • 125
    • 0027370683 scopus 로고
    • Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata
    • Mignogna G., Simmaco M., Kreil G., Barra D. Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata. EMBO J. 12:1993;4829-4832.
    • (1993) EMBO J. , vol.12 , pp. 4829-4832
    • Mignogna, G.1    Simmaco, M.2    Kreil, G.3    Barra, D.4
  • 126
    • 0031985197 scopus 로고    scopus 로고
    • Production of active chimeric pediocin PA-1 in Escherichia coli in the absence of processing and secretion genes from Pediococcus pap operon
    • Miller K.W., Schamber R., Chen Y., Ray B. Production of active chimeric pediocin PA-1 in Escherichia coli in the absence of processing and secretion genes from Pediococcus pap operon. Appl. Environ. Microbiol. 64:1998;14-20.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 14-20
    • Miller, K.W.1    Schamber, R.2    Chen, Y.3    Ray, B.4
  • 129
    • 0000649090 scopus 로고    scopus 로고
    • Biologically based preservation systems and probiotic bacteria
    • M.P. Doyle, L.R. Beuchat, & T.J. Montville. USA: ASM Press
    • Montville T.J., Winkowski K. Biologically based preservation systems and probiotic bacteria. Doyle M.P., Beuchat L.R., Montville T.J. Food microbiology. Fundamentals and frontiers. 1997;557-576 ASM Press, USA.
    • (1997) Food microbiology. Fundamentals and frontiers , pp. 557-576
    • Montville, T.J.1    Winkowski, K.2
  • 131
    • 0033814969 scopus 로고    scopus 로고
    • Peptide-based antibiotics: A potential answer to raging antimicrobial resistance
    • Mor A. Peptide-based antibiotics: a potential answer to raging antimicrobial resistance. Drug Dev. Res. 50:2000;440-447.
    • (2000) Drug Dev. Res. , vol.50 , pp. 440-447
    • Mor, A.1
  • 132
    • 0028009870 scopus 로고
    • Isolation and structure of novel defensin peptides from frog skin
    • Mor A., Nicolas P. Isolation and structure of novel defensin peptides from frog skin. Eur. J. Biochem. 219:1994;145-154.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 145-154
    • Mor, A.1    Nicolas, P.2
  • 134
    • 0033199626 scopus 로고    scopus 로고
    • Development of a lacticin 3147-enriched whey powder with inhibitory activity against foodborne pathogens
    • Morgan S.M., Galvin M., Kelly J., Ross R.P., Hill C. Development of a lacticin 3147-enriched whey powder with inhibitory activity against foodborne pathogens. J. Food Protection. 62:1999;1011-1016.
    • (1999) J. Food Protection , vol.62 , pp. 1011-1016
    • Morgan, S.M.1    Galvin, M.2    Kelly, J.3    Ross, R.P.4    Hill, C.5
  • 135
    • 0034757671 scopus 로고    scopus 로고
    • Evaluation of a spray dried lacticin 3147 powder for the control of Listeria monocytogenes and Bacillus cereus in a range of food systems
    • Morgan S.M., Galvin M., Ross R.P., Hill C. Evaluation of a spray dried lacticin 3147 powder for the control of Listeria monocytogenes and Bacillus cereus in a range of food systems. Lett. Appl. Microbiol. 33:2001;387-391.
    • (2001) Lett. Appl. Microbiol. , vol.33 , pp. 387-391
    • Morgan, S.M.1    Galvin, M.2    Ross, R.P.3    Hill, C.4
  • 136
    • 0025872592 scopus 로고
    • Purification and aminoacid sequence of lactocin S, a bacteriocin produced by Lactobacillus sake L45
    • Mortverdt C.I., Nissen-Meyr J., Sletten K., Nes I.F. Purification and aminoacid sequence of lactocin S, a bacteriocin produced by Lactobacillus sake L45. Appl. Environ. Microbiol. 57:1991;1829-1834.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1829-1834
    • Mortverdt, C.I.1    Nissen-Meyr, J.2    Sletten, K.3    Nes, I.F.4
  • 140
    • 0026759323 scopus 로고
    • Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici
    • Nieto Lozano J.C., Nissen-Meyer J., Sletten K., Pelaz C., Nes I.F. Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici. J. Gen. Microbiol. 138:1992;1985-1990.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1985-1990
    • Nieto Lozano, J.C.1    Nissen-Meyer, J.2    Sletten, K.3    Pelaz, C.4    Nes, I.F.5
  • 142
    • 0030974953 scopus 로고    scopus 로고
    • Ribosomally synthesized antimicrobial peptides: Their function, structure, biogenesis, and mechanism of action
    • Nissen-Meyer J., Nes I.F. Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action. Arch. Microbiol. 167:1997;67-77.
    • (1997) Arch. Microbiol. , vol.167 , pp. 67-77
    • Nissen-Meyer, J.1    Nes, I.F.2
  • 143
    • 0027292711 scopus 로고
    • Association of the lactococcin A immunity factor with the cell membrane: Purification and characterization of the immunity factor
    • Nissen-Meyer J., Havarstein L.S., Holo H., Sletten K., Nes I.F. Association of the lactococcin A immunity factor with the cell membrane: purification and characterization of the immunity factor. J. Gen. Microbiol. 139:1993;1503-1509.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 1503-1509
    • Nissen-Meyer, J.1    Havarstein, L.S.2    Holo, H.3    Sletten, K.4    Nes, I.F.5
  • 144
    • 0035834573 scopus 로고    scopus 로고
    • Pseudin-2: An antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog
    • Olson L., Soto A.M., Knoop F.C., Conlon J.M. Pseudin-2: an antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog. Biochem. Biophys. Res. Commun. 288:2001;1001-1005.
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 1001-1005
    • Olson, L.1    Soto, A.M.2    Knoop, F.C.3    Conlon, J.M.4
  • 145
    • 0032561422 scopus 로고    scopus 로고
    • An antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus
    • Park I.Y., Park C.B., Kim S., Kim S.C., Parasin I. An antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus. FEBS Lett. 437:1998;258-262.
    • (1998) FEBS Lett. , vol.437 , pp. 258-262
    • Park, I.Y.1    Park, C.B.2    Kim, S.3    Kim, S.C.4    Parasin, I.5
  • 146
    • 0035913957 scopus 로고    scopus 로고
    • Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata
    • Park S., Park S.H., Ahn H.C., Kim S., Kim S.S., Lee B.J. Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata. FEBS Lett. 507:2001;95-100.
    • (2001) FEBS Lett. , vol.507 , pp. 95-100
    • Park, S.1    Park, S.H.2    Ahn, H.C.3    Kim, S.4    Kim, S.S.5    Lee, B.J.6
  • 147
    • 0035038578 scopus 로고    scopus 로고
    • Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin
    • Patrzykat A., Zhang L., Mendoza G., Iwama G., Hancock R. Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin. Antimicrob. Agents Chemother. 45:2001;1337-1342.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1337-1342
    • Patrzykat, A.1    Zhang, L.2    Mendoza, G.3    Iwama, G.4    Hancock, R.5
  • 148
    • 0026543167 scopus 로고
    • Purification and partial characterization of lacticin 481, a lanthionine-containing bacteriocin produced by Lactococcus lactis subsp. lactis CNRZ481
    • Piard J.C., Muriana P.M., Desmazeaud M.J., Klanhammer T.R. Purification and partial characterization of lacticin 481, a lanthionine-containing bacteriocin produced by Lactococcus lactis subsp. lactis CNRZ481. Appl. Environ. Microbiol. 58:1992;279-284.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 279-284
    • Piard, J.C.1    Muriana, P.M.2    Desmazeaud, M.J.3    Klanhammer, T.R.4
  • 150
    • 0028363167 scopus 로고
    • Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV17B
    • Quadri L.E.N., Sailer M., Roy K.L., Vederas J.C., Stiles M.E. Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV17B. J. Biol. Chem. 269:1994;12204-12221.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12204-12221
    • Quadri, L.E.N.1    Sailer, M.2    Roy, K.L.3    Vederas, J.C.4    Stiles, M.E.5
  • 151
    • 0028915914 scopus 로고
    • Characterization of the protein conferring immunity to the antimicrobial peptide carnobacteriocin B2 and expression of Carnobacteriocin B2 and BM1
    • Quadri L.E.N., Sailer M., Terebiznik M.R., Roy K.L., Vederas J.C., Stiles M.E. Characterization of the protein conferring immunity to the antimicrobial peptide carnobacteriocin B2 and expression of Carnobacteriocin B2 and BM1. J. Bacteriol. 177:1995;1144-1151.
    • (1995) J. Bacteriol. , vol.177 , pp. 1144-1151
    • Quadri, L.E.N.1    Sailer, M.2    Terebiznik, M.R.3    Roy, K.L.4    Vederas, J.C.5    Stiles, M.E.6
  • 152
    • 0029819784 scopus 로고    scopus 로고
    • Paneth cell defensins: Endogenous peptide components of intestinal host defense
    • Quellette A.J., Selsted M. Paneth cell defensins: endogenous peptide components of intestinal host defense. FASEB J. 10:1996;1280-1289.
    • (1996) FASEB J. , vol.10 , pp. 1280-1289
    • Quellette, A.J.1    Selsted, M.2
  • 153
    • 0037005996 scopus 로고    scopus 로고
    • Current status of defensins and their role in innate and adaptive immunity
    • Raj P.A., Dentino A.R. Current status of defensins and their role in innate and adaptive immunity. FEMS Microbiol. Lett. 206:2002;9-18.
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 9-18
    • Raj, P.A.1    Dentino, A.R.2
  • 154
    • 0034194257 scopus 로고    scopus 로고
    • Large-scale synthesis and functional elements for the antimicrobial activity of defensins
    • Raj P.A., Antonyraj K.J., Karunakaran T. Large-scale synthesis and functional elements for the antimicrobial activity of defensins. Biochem. J. 347:2000;633-641.
    • (2000) Biochem. J. , vol.347 , pp. 633-641
    • Raj, P.A.1    Antonyraj, K.J.2    Karunakaran, T.3
  • 155
    • 0026573214 scopus 로고
    • Characterization of the novel nisin-sucrose conjugative transposon Tn5276 and its integration into Lactococcus lactis
    • Rauch P.J.G., De Vos W.M. Characterization of the novel nisin-sucrose conjugative transposon Tn5276 and its integration into Lactococcus lactis. J. Bacteriol. 174:1992;1280-1287.
    • (1992) J. Bacteriol. , vol.174 , pp. 1280-1287
    • Rauch, P.J.G.1    De Vos, W.M.2
  • 158
    • 0036589206 scopus 로고    scopus 로고
    • Bacteriocin diversity: Ecological and evolutionary perspectives
    • Riley M.A., Wertz J.E. Bacteriocin diversity: ecological and evolutionary perspectives. Biochimie. 84:2002;357-364.
    • (2002) Biochimie , vol.84 , pp. 357-364
    • Riley, M.A.1    Wertz, J.E.2
  • 159
    • 0036900093 scopus 로고    scopus 로고
    • Antimicrobial peptides from amphibian skin: An expanding scenario
    • Rinaldi A.C. Antimicrobial peptides from amphibian skin: an expanding scenario. Curr. Opin. Chem. Biol. 6:2002;799-804.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 799-804
    • Rinaldi, A.C.1
  • 160
    • 0028293918 scopus 로고
    • Cloning, expression and nucleotide sequence of genes involved in production of lactococcin DR, a bacteriocin from Lactococcus lactis
    • Rince A., Dufour A., Le Pogam S., Thualt D., Bourgeois C.M., Le Pennec J.P. Cloning, expression and nucleotide sequence of genes involved in production of lactococcin DR, a bacteriocin from Lactococcus lactis. Appl. Environ. Microbiol. 60:1994;1652-1657.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1652-1657
    • Rince, A.1    Dufour, A.2    Le Pogam, S.3    Thualt, D.4    Bourgeois, C.M.5    Le Pennec, J.P.6
  • 161
    • 0033664277 scopus 로고    scopus 로고
    • Leukocyte antimicrobial peptides: Multifunctional effector molecules of innate immunity
    • Risso A. Leukocyte antimicrobial peptides: multifunctional effector molecules of innate immunity. J. Leukoc. Biol. 68:2000;785-792.
    • (2000) J. Leukoc. Biol. , vol.68 , pp. 785-792
    • Risso, A.1
  • 162
    • 0011934846 scopus 로고    scopus 로고
    • Cecropins and their hybrid peptides as versatile templates in the development of membrane-active antibiotic agents
    • in press. Menestrina, G, Lazzarovici, P, editors. New York: Harwood Academic
    • Rivas L, Andreu D, in press. Cecropins and their hybrid peptides as versatile templates in the development of membrane-active antibiotic agents. In: Menestrina, G, Lazzarovici, P, editors. Pore-forming peptides and protein toxins. Cellular and molecular mechanisms of toxin action. New York: Harwood Academic.
    • Pore-forming peptides and protein toxins. Cellular and molecular mechanisms of toxin action
    • Rivas, L.1    Andreu, D.2
  • 164
    • 0023746603 scopus 로고
    • Structure and bactericicdal activity of an antibiotic dodecapeptide purified from bovine neutrophils
    • Romeo D., Skerlavaj B., Bolognesi M., Gennar R. Structure and bactericicdal activity of an antibiotic dodecapeptide purified from bovine neutrophils. J. Biol. Chem. 263:1988;9573-9575.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9573-9575
    • Romeo, D.1    Skerlavaj, B.2    Bolognesi, M.3    Gennar, R.4
  • 165
    • 0037113945 scopus 로고    scopus 로고
    • Preservation and fermentation: Past, present and future
    • Ross Paul R., Morgan S., Hill C. Preservation and fermentation: past, present and future. Int. J. Food Microbiol. 79:2002;3-16.
    • (2002) Int. J. Food Microbiol. , vol.79 , pp. 3-16
    • Ross Paul, R.1    Morgan, S.2    Hill, C.3
  • 166
    • 0021993065 scopus 로고
    • Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on artificial membrane vesicles
    • Ruhr E., Sahl H.-G. Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on artificial membrane vesicles. Antimicrob. Agents Chemother. 27:1985;841-845.
    • (1985) Antimicrob. Agents Chemother. , vol.27 , pp. 841-845
    • Ruhr, E.1    Sahl, H.-G.2
  • 167
    • 0029670684 scopus 로고    scopus 로고
    • An application in cheddar cheese manufacture for a strain of Lactococcus lactis producing a novelbroad spectrum bacteriocin lacticin 3147
    • Ryan M.P., Rea M.C., Hill C., Ross R.P. An application in cheddar cheese manufacture for a strain of Lactococcus lactis producing a novelbroad spectrum bacteriocin lacticin 3147. Appl. Env. Microbiol. 62:1996;612-619.
    • (1996) Appl. Env. Microbiol. , vol.62 , pp. 612-619
    • Ryan, M.P.1    Rea, M.C.2    Hill, C.3    Ross, R.P.4
  • 168
    • 0033621484 scopus 로고    scopus 로고
    • Extensive post-translational modification, including a serine to D-alanine conversion, in the two-component lantibiotic, lacticin 3147
    • Ryan M.P., Jack R., Josten W., Sahl H.G., Jung G., Ross R.P.et al. Extensive post-translational modification, including a serine to D-alanine conversion, in the two-component lantibiotic, lacticin 3147. J. Biol. Chem. 274:1999;37544-37550.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37544-37550
    • Ryan, M.P.1    Jack, R.2    Josten, W.3    Sahl, H.G.4    Jung, G.5    Ross, R.P.6
  • 169
    • 0035135297 scopus 로고    scopus 로고
    • Heterologous expression of lacticin 3147 in Enterococcus faecalis: Comparison of biological activity with cytolysin
    • Ryan M.P., McAuliffe O., Ross R.P., Hill C. Heterologous expression of lacticin 3147 in Enterococcus faecalis: comparison of biological activity with cytolysin. Lett. Appl. Microbiol. 32:1999;71-77.
    • (1999) Lett. Appl. Microbiol. , vol.32 , pp. 71-77
    • Ryan, M.P.1    McAuliffe, O.2    Ross, R.P.3    Hill, C.4
  • 170
    • 0035377203 scopus 로고    scopus 로고
    • Strategy for manipulation of cheese flora using combinations of lacticin 3147-producing and -resistant cultures
    • Ryan M.P., Ross R.P., Hill C. Strategy for manipulation of cheese flora using combinations of lacticin 3147-producing and -resistant cultures. Appl. Environ. Microbiol. 67:2001;2699-2704.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2699-2704
    • Ryan, M.P.1    Ross, R.P.2    Hill, C.3
  • 172
    • 0004238325 scopus 로고
    • Gene-encoded antibiotics made in bacteria
    • H.G. Bomam, J. Marsh, & J.A. Goode. New York: Wiley
    • Sahl H.-G. Gene-encoded antibiotics made in bacteria. Bomam H.G., Marsh J., Goode J.A. Antimicrobial peptides. 1994;27-53 Wiley, New York.
    • (1994) Antimicrobial peptides , pp. 27-53
    • Sahl, H.-G.1
  • 173
    • 0031782954 scopus 로고    scopus 로고
    • Lantibiotics: Biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria
    • Sahl H.-G., Bierbaum G. Lantibiotics: biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria. Annu. Rev. Microbiol. 52:1998;41-79.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 41-79
    • Sahl, H.-G.1    Bierbaum, G.2
  • 174
    • 0023491341 scopus 로고
    • Voltage-dependent depolarization of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin
    • Sahl H.-G., Kordel M., Benz R. Voltage-dependent depolarization of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin. Arch. Microbiol. 149:1987;120-124.
    • (1987) Arch. Microbiol. , vol.149 , pp. 120-124
    • Sahl, H.-G.1    Kordel, M.2    Benz, R.3
  • 175
    • 0029055380 scopus 로고
    • Biosynthesis and biological activities of lantibiotics with unique post-translational modifications
    • Sahl H.-G., Jack R.W., Bierbaum G. Biosynthesis and biological activities of lantibiotics with unique post-translational modifications. Eur. J. Biochem. 230:1995;827-853.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 827-853
    • Sahl, H.-G.1    Jack, R.W.2    Bierbaum, G.3
  • 177
    • 0030809809 scopus 로고    scopus 로고
    • A chloride-inducible gene expression cassette and ist use in induced lysis of Lactococcus lactis
    • Sanders J.W., Venema G., Kok J. A chloride-inducible gene expression cassette and ist use in induced lysis of Lactococcus lactis. Appl. Environ. Microbiol. 63:1997;4877-4882.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4877-4882
    • Sanders, J.W.1    Venema, G.2    Kok, J.3
  • 178
    • 0031984335 scopus 로고    scopus 로고
    • A chloride-inducible acid resistance mechanism in Lactococcus lactis and its regulation
    • Sanders J.W., Leenhouts K., Burgoorn J., Brands J.R., Venema G., Kok J. A chloride-inducible acid resistance mechanism in Lactococcus lactis and its regulation. Mol. Microbiol. 27:1998;299-310.
    • (1998) Mol. Microbiol. , vol.27 , pp. 299-310
    • Sanders, J.W.1    Leenhouts, K.2    Burgoorn, J.3    Brands, J.R.4    Venema, G.5    Kok, J.6
  • 179
  • 180
    • 0000284412 scopus 로고    scopus 로고
    • Potential of antagonistic microorganisms and bacteriocins for the biological preservation of foods
    • Schillinger U., Geisen R., Holzapfel W.H. Potential of antagonistic microorganisms and bacteriocins for the biological preservation of foods. Trends Food Sci. Technol. 7:1996;158-164.
    • (1996) Trends Food Sci. Technol. , vol.7 , pp. 158-164
    • Schillinger, U.1    Geisen, R.2    Holzapfel, W.H.3
  • 181
    • 0028902757 scopus 로고
    • Epithelial antibiotics induced at sites of inflammation
    • Schonwetter B.S., Stolzenberg E.D., Zasloff M. Epithelial antibiotics induced at sites of inflammation. Science. 267:1995;1645-1648.
    • (1995) Science , vol.267 , pp. 1645-1648
    • Schonwetter, B.S.1    Stolzenberg, E.D.2    Zasloff, M.3
  • 182
    • 0033213989 scopus 로고    scopus 로고
    • Epithelial antimicrobial peptides: Innate local host response elements
    • Schröder J.M. Epithelial antimicrobial peptides: innate local host response elements. Cell. Mol. Life Sci. 56:1999;32-46.
    • (1999) Cell. Mol. Life Sci. , vol.56 , pp. 32-46
    • Schröder, J.M.1
  • 183
    • 0028964136 scopus 로고
    • Defensins in granules of phagocytic and non-phagocytic cells
    • Selsted M.E., Quellette A.J. Defensins in granules of phagocytic and non-phagocytic cells. Trends Cell Biol. 5:1995;114-119.
    • (1995) Trends Cell Biol. , vol.5 , pp. 114-119
    • Selsted, M.E.1    Quellette, A.J.2
  • 184
    • 0021032178 scopus 로고
    • Primary structure of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages
    • Selsted M.E., Brown D.M., DeLange R.J., Lehler R.I. Primary structure of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages. J. Biol. Chem. 258:1983;14485-14489.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14485-14489
    • Selsted, M.E.1    Brown, D.M.2    DeLange, R.J.3    Lehler, R.I.4
  • 185
    • 0032079138 scopus 로고    scopus 로고
    • Plasmodium gallinaccum: Differential killing of some mosquito stages of the parasite by insect defensin
    • Shahabuddin M., Fields I., Bulet P., Hoffmann J.A., Miller L.H. Plasmodium gallinaccum: differential killing of some mosquito stages of the parasite by insect defensin. Exp. Parasitol. 89:1998;103-112.
    • (1998) Exp. Parasitol. , vol.89 , pp. 103-112
    • Shahabuddin, M.1    Fields, I.2    Bulet, P.3    Hoffmann, J.A.4    Miller, L.H.5
  • 186
    • 0037062560 scopus 로고    scopus 로고
    • Structural consequences of carboxyamidation of dermaseptin S3
    • Shalev D.E., Mor A., Kustanovich I. Structural consequences of carboxyamidation of dermaseptin S3. Biochemistry. 41:2002;7312-7317.
    • (2002) Biochemistry , vol.41 , pp. 7312-7317
    • Shalev, D.E.1    Mor, A.2    Kustanovich, I.3
  • 188
    • 0034721871 scopus 로고    scopus 로고
    • Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acantoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family
    • Silva P.I. Jr., Daffre S., Bulet P. Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acantoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family. J. Biol. Chem. 275:2000;33464-33470.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33464-33470
    • Silva P.I., Jr.1    Daffre, S.2    Bulet, P.3
  • 190
    • 0027164860 scopus 로고
    • Brochocin-C, a new bacteriocin produced by Brochothrix campestris
    • Siragusa G.R., Nettles Cutter C. Brochocin-C, a new bacteriocin produced by Brochothrix campestris. Appl. Environ. Microbiol. 59:1993;2326-2328.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 2326-2328
    • Siragusa, G.R.1    Nettles Cutter, C.2
  • 192
    • 0010688294 scopus 로고    scopus 로고
    • Biosynthesis of the lantibiotic lactocin S: Heterologous expression of a two-operon gene cluster encoding regulatory, biosynthestic, and immunity functions
    • Veldhoven, The Netherlands: FEMS
    • Skaugen M., Christie V.H., Nes I.F. Biosynthesis of the lantibiotic lactocin S: heterologous expression of a two-operon gene cluster encoding regulatory, biosynthestic, and immunity functions. Abstracts of the sixth symposium on lactic acid bacteria: genetics, metabolism and applications. 1999;C86 FEMS, Veldhoven, The Netherlands.
    • (1999) Abstracts of the sixth symposium on lactic acid bacteria: Genetics, metabolism and applications , pp. 86
    • Skaugen, M.1    Christie, V.H.2    Nes, I.F.3
  • 194
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H., Hultmark D., Engstrom A., Bennich H., Boman H.G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature. 1981;246-248.
    • (1981) Nature , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 195
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leucocytes by the ligation of two truncated α-defensins
    • Tang Y.Q., Yuan J., Osapay G., Osapay K., Tran D., Miller C.J.et al. A cyclic antimicrobial peptide produced in primate leucocytes by the ligation of two truncated α-defensins. Science. 286:1999;498-502.
    • (1999) Science , vol.286 , pp. 498-502
    • Tang, Y.Q.1    Yuan, J.2    Osapay, G.3    Osapay, K.4    Tran, D.5    Miller, C.J.6
  • 196
    • 0024797674 scopus 로고
    • Monocyte-chemotactic activity of defensins from human neutrophils
    • Territo M.C.et al. Monocyte-chemotactic activity of defensins from human neutrophils. J. Clin. Invest. 84:1989;2017-2020.
    • (1989) J. Clin. Invest. , vol.84 , pp. 2017-2020
    • Territo, M.C.1
  • 197
    • 0026802510 scopus 로고
    • Characterization of the bacteriocin curvacin A from Lactobacillus curvatus LTH1174 and sacacin from L. sake LTH673
    • Tichaczek P.S., Nissen-Meyer J., Nes I.F., Vogel R.F., Hammes W.P. Characterization of the bacteriocin curvacin A from Lactobacillus curvatus LTH1174 and sacacin from L. sake LTH673. Syst. Appl. Microbiol. 15:1992;460-468.
    • (1992) Syst. Appl. Microbiol. , vol.15 , pp. 460-468
    • Tichaczek, P.S.1    Nissen-Meyer, J.2    Nes, I.F.3    Vogel, R.F.4    Hammes, W.P.5
  • 198
    • 0028294292 scopus 로고
    • Identification and characterization of a primary antibacterial domain in CAP18, a lipopolysasccharide binding protein from rabbit leucocytes
    • Tossi A., Scocchi M., Skerlavaj B., Gennaro R. Identification and characterization of a primary antibacterial domain in CAP18, a lipopolysasccharide binding protein from rabbit leucocytes. FEBS Lett. 339:1994;108-112.
    • (1994) FEBS Lett. , vol.339 , pp. 108-112
    • Tossi, A.1    Scocchi, M.2    Skerlavaj, B.3    Gennaro, R.4
  • 200
    • 0036692989 scopus 로고    scopus 로고
    • Lantibiotics produced by lactic acid bacteria: Structure, function and applications
    • Twomey D., Ross R.P., Ryan M., Meaney B., Hill C. Lantibiotics produced by lactic acid bacteria: structure, function and applications. Antonie van Leeuwenhoek. 82:2002;165-185.
    • (2002) Antonie van Leeuwenhoek , vol.82 , pp. 165-185
    • Twomey, D.1    Ross, R.P.2    Ryan, M.3    Meaney, B.4    Hill, C.5
  • 201
    • 0026332723 scopus 로고
    • The bacteriocin lactococcin A specifically increases permeability of lactococcal cytoplasmic membranes in a voltage-independent, protein-mediated manner
    • van Belkum M.J., Kok J., Venema G., Holo H., Nes I.F., Konings W.N.et al. The bacteriocin lactococcin A specifically increases permeability of lactococcal cytoplasmic membranes in a voltage-independent, protein-mediated manner. J. Bacteriol. 173:1991;7934-7941.
    • (1991) J. Bacteriol. , vol.173 , pp. 7934-7941
    • Van Belkum, M.J.1    Kok, J.2    Venema, G.3    Holo, H.4    Nes, I.F.5    Konings, W.N.6
  • 202
    • 0030944568 scopus 로고    scopus 로고
    • Double-glycine-type leader peptides direct secretion of bacteriocins by ABC transporters: Colicin V secretion in Lactococcus lactis
    • van Belkum M.J., Worobo R.W., Stiles M.E. Double-glycine-type leader peptides direct secretion of bacteriocins by ABC transporters: colicin V secretion in Lactococcus lactis. Mol. Microbiol. 23:1997;1293-1301.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1293-1301
    • Van Belkum, M.J.1    Worobo, R.W.2    Stiles, M.E.3
  • 203
    • 0033452745 scopus 로고    scopus 로고
    • Defensins: Key players or bystanders in infection, injury, and repair in the lung? J
    • Van Wetering S., Sterk P.J., rabe K.F., Hiemstra P.S. Defensins: key players or bystanders in infection, injury, and repair in the lung? J. Allergy Clin. Immunol. 104:1999;1131-1138.
    • (1999) Allergy Clin. Immunol. , vol.104 , pp. 1131-1138
    • Van Wetering, S.1    Sterk, P.J.2    Rabe, K.F.3    Hiemstra, P.S.4
  • 205
    • 0033759007 scopus 로고    scopus 로고
    • Inhibition of recombinant adeno-associated virus (rAAV) transduction by bronchial secretions from cystic fibrosis patients
    • Virella-Lowell I., Poirier A., Chesnut K.A., Brantly M., Flotte T.R. Inhibition of recombinant adeno-associated virus (rAAV) transduction by bronchial secretions from cystic fibrosis patients. Gene Ther. 7:2000;1783-1789.
    • (2000) Gene Ther. , vol.7 , pp. 1783-1789
    • Virella-Lowell, I.1    Poirier, A.2    Chesnut, K.A.3    Brantly, M.4    Flotte, T.R.5
  • 206
    • 0036842381 scopus 로고    scopus 로고
    • Antimicrobial peptides from animals: Focus on invertebrates
    • Vizioli J., Salzet M. Antimicrobial peptides from animals: focus on invertebrates. Trends Pharmacol. Sci. 23:2002;494-496.
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 494-496
    • Vizioli, J.1    Salzet, M.2
  • 209
    • 0035910508 scopus 로고    scopus 로고
    • Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and the inhibition of cell wall biosynthesis for potent antibiotic activity
    • Wiedemann I., Breukink E., van Kraaij C., Kuipers O., Bierbaum G., de Kruijff B.et al. Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and the inhibition of cell wall biosynthesis for potent antibiotic activity. J. Biol. Chem. 276:2002;1772-1779.
    • (2002) J. Biol. Chem. , vol.276 , pp. 1772-1779
    • Wiedemann, I.1    Breukink, E.2    Van Kraaij, C.3    Kuipers, O.4    Bierbaum, G.5    De Kruijff, B.6
  • 210
    • 0032313341 scopus 로고    scopus 로고
    • Epithelial antimicrobial peptides: Review and significance for oral applications
    • Wienberg A., Krisanaprokornkit S., Dale B.A. Epithelial antimicrobial peptides: review and significance for oral applications. Crit. Rev. Oral Biol. Med. 9:1996;399-414.
    • (1996) Crit. Rev. Oral Biol. Med. , vol.9 , pp. 399-414
    • Wienberg, A.1    Krisanaprokornkit, S.2    Dale, B.A.3
  • 211
    • 0033569408 scopus 로고    scopus 로고
    • β-defensins: Linking innate and adaptive immunity through dendritic and T-cell CCR6
    • Yang D., Chertov O., Bykoskaia S.N., Chen Q., Buffo M.J., Shogan J.et al. β-defensins: linking innate and adaptive immunity through dendritic and T-cell CCR6. Science. 286:1999;525-528.
    • (1999) Science , vol.286 , pp. 525-528
    • Yang, D.1    Chertov, O.2    Bykoskaia, S.N.3    Chen, Q.4    Buffo, M.J.5    Shogan, J.6
  • 212
    • 0033844287 scopus 로고    scopus 로고
    • Human neutrophil defensins selectively chemoattract naive T and immature dendritic cells
    • Yang D., Chen Q., Chertov O., Oppenheim J.J. Human neutrophil defensins selectively chemoattract naive T and immature dendritic cells. J. Leukocyte Biol. 68:2000;9-14.
    • (2000) J. Leukocyte Biol. , vol.68 , pp. 9-14
    • Yang, D.1    Chen, Q.2    Chertov, O.3    Oppenheim, J.J.4
  • 213
    • 0036606951 scopus 로고    scopus 로고
    • Mammalian defensins in immunity: More than just microbicidal
    • Yang D., Biragyn A., Kwak L.W., Oppenheim J.J. Mammalian defensins in immunity: more than just microbicidal. Trends Immunol. 23:2002;291-296.
    • (2002) Trends Immunol. , vol.23 , pp. 291-296
    • Yang, D.1    Biragyn, A.2    Kwak, L.W.3    Oppenheim, J.J.4
  • 214
    • 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. 374:1995;1-5.
    • (1995) FEBS Lett. , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 215
    • 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. 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. U. S. A. 84:1987;5449-5453.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 216
    • 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
  • 217
    • 0028839913 scopus 로고
    • Structures of genes for two cathelin-associated antimicrobial peptides: Prophenin-2 and PR-39
    • Zhao C., Ganz T., Lehler R.I. Structures of genes for two cathelin-associated antimicrobial peptides: prophenin-2 and PR-39. FEBS Lett. 376:1995;130-134.
    • (1995) FEBS Lett. , vol.376 , pp. 130-134
    • Zhao, C.1    Ganz, T.2    Lehler, R.I.3
  • 218
    • 0029015666 scopus 로고
    • The structure of porcine protegrin genes
    • Zhao C., Ganz T., Lehler R.I. The structure of porcine protegrin genes. FEBS Lett. 368:1995;197-202.
    • (1995) FEBS Lett. , vol.368 , pp. 197-202
    • Zhao, C.1    Ganz, T.2    Lehler, R.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.