메뉴 건너뛰기




Volumn 6, Issue 3, 2003, Pages 96-109

Antimicrobial peptides: A natural alternative to chemical antibiotics andapotential for applied biotechnology

Author keywords

Applied biotechnology; Innate response; Natural antibiotics

Indexed keywords

4 HYDROXYCINNAMALDEHYDE; ANDROCTONIN; ANTIMICROBIAL CATIONIC PEPTIDE; BACTERIOCIN; BREVININ; BUFORIN; CATHELICIDIN; CECROPIN; DEFENSIN; DERMASEPTIN; DERMICIDIN; ENKELYTIN; HISTATIN; HISTONE H2B; LACTOFERRICIN C; MAGAININ DERIVATIVE; N ALANYL 5 S GLUTATHIONYL 3,4 DIHYDROXYPHENYLALANINE; NATURAL PRODUCT; NISIN; PARASIN; PEDIOCIN; PEPTIDE B; PROTEGRIN; PROTEIN MIAMP2C; SAKACIN; TACHYPLESIN; THANATIN; THIONINE; THROMBOCIDIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 3042781052     PISSN: 07173458     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (165)

References (128)
  • 1
    • 0034680145 scopus 로고    scopus 로고
    • Toll-like receptors in the induction of the innate immune response
    • ADEREM, A. and ULEVITCH, R. Toll-like receptors in the induction of the innate immune response. Nature, 2000,vol. 406, no. 6797, p. 782-787.
    • (2000) Nature , vol.406 , Issue.6797 , pp. 782-787
    • Aderem, A.1    Ulevitch, R.2
  • 2
    • 0034886143 scopus 로고    scopus 로고
    • Toll-like receptors: Critical proteins linking innate and acquired immunity
    • AKIRA, S.; TAKEDA, K. and KAICHO, T. Toll-like receptors: Critical proteins linking innate and acquired immunity. Nature Immunology, 2001, vol. 2, no. 8, p. 675-680.
    • (2001) Nature Immunology , vol.2 , Issue.8 , pp. 675-680
    • Akira, S.1    Takeda, K.2    Kaicho, T.3
  • 3
    • 0034126229 scopus 로고    scopus 로고
    • Anti-tumor effect of N-beta-alanyl-5-S-glutathionyl dihydroxyphenylalanine (5-S-GAD), a novel anti-bacterial substance from an insect
    • AKIYAMA, N.; HIJIKATA, M.; KOBAYASHI, A.; YAMORI, T.; TSURUO, T. and NATORI, S. Anti-tumor effect of N-beta-alanyl-5-S-glutathionyl dihydroxyphenylalanine (5-S-GAD), a novel anti-bacterial substance from an insect. Anticancer Research, 2000, vol. 20, no. 1A, p. 357-362.
    • (2000) Anticancer Research , vol.20 , Issue.1 A , pp. 357-362
    • Akiyama, N.1    Hijikata, M.2    Kobayashi, A.3    Yamori, T.4    Tsuruo, T.5    Natori, S.6
  • 4
    • 0034960102 scopus 로고    scopus 로고
    • Lactoferrin and cyclic lactoferricin inhibit the entry of human cytomegalovirus into human fibroblasts
    • ANDERSEN, J.; OSBAKK, S.; VORLAND, L.; TRAAVIK, T. and GUTTEBERG, T. Lactoferrin and cyclic lactoferricin inhibit the entry of human cytomegalovirus into human fibroblasts. Antiviral Research, 2001, vol. 51, no. 2, p. 141-149.
    • (2001) Antiviral Research , vol.51 , Issue.2 , pp. 141-149
    • Andersen, J.1    Osbakk, S.2    Vorland, L.3    Traavik, T.4    Gutteberg, T.5
  • 5
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: An overview
    • ANDREU, D. and RIVAS, L. Animal antimicrobial peptides: an overview. Biopolymers, 1998, vol. 47, no. 6, p. 415-433.
    • (1998) Biopolymers , vol.47 , Issue.6 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 6
    • 0001216086 scopus 로고    scopus 로고
    • Epithelial antimicrobial peptides in host defence against infection
    • BALS, R. Epithelial antimicrobial peptides in host defence against infection (Review). Respiratory Research, 2000, vol. 1, no. 3, p. 141-150.
    • (2000) Respiratory Research , vol.1 , Issue.3 , pp. 141-150
    • Bals, R.1
  • 7
    • 0027488740 scopus 로고
    • Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy
    • BECHINGER, B.; ZASLOFF, M. and OPELLA, S.J. Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy. Protein Sciences, 1993, vol. 2, no. 12, p. 2077-2084.
    • (1993) Protein Sciences , vol.2 , Issue.12 , pp. 2077-2084
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 8
    • 0009129319 scopus 로고    scopus 로고
    • The role of thionins in the resistance of plants
    • Datta, S.K., Muthukrishnan, S. eds., CRC Press
    • BOHLMANN, H. The role of thionins in the resistance of plants. In: DATTA, S.K., MUTHUKRISHNAN, S. eds. Pathogenesis-related proteins in plants, CRC Press, 1999, p. 207-234.
    • (1999) Pathogenesis-Related Proteins in Plants , pp. 207-234
    • Bohlmann, H.1
  • 9
    • 0031821708 scopus 로고    scopus 로고
    • Gene-encoded peptide antibiotics and the concept of innate immunity: An update review
    • BOMAN, H. Gene-encoded peptide antibiotics and the concept of innate immunity: an update review. Scandinavian Journal Immunology, 1998, vol. 48, no. 1, p. 15-25.
    • (1998) Scandinavian Journal Immunology , vol.48 , Issue.1 , pp. 15-25
    • Boman, H.1
  • 10
    • 0028933794 scopus 로고
    • Peptide antibiotics ant their role in innate immunity
    • BOMAN, H. Peptide antibiotics ant their role in innate immunity. Annual Review of Immunology, 1995, vol. 13, p. 61-92.
    • (1995) Annual Review of Immunology , vol.13 , pp. 61-92
    • Boman, H.1
  • 12
    • 0026734641 scopus 로고
    • Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins
    • BROEKAERT, W.; MARIEN, W.; TERRAS, F.; DE BOLLE, M.; PROOST, P.; VAN DAMME, J.; DILLEN, L.; CLAEYS, M.; REES, S. and VANDERLEYDEN, J. Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins. Biochemistry, 1992, vol. 31, no. 17, p. 4308-4314.
    • (1992) Biochemistry , vol.31 , Issue.17 , pp. 4308-4314
    • Broekaert, W.1    Marien, W.2    Terras, F.3    De Bolle, M.4    Proost, P.5    Van Damme, J.6    Dillen, L.7    Claeys, M.8    Rees, S.9    Vanderleyden, J.10
  • 13
    • 0030048076 scopus 로고    scopus 로고
    • Isolation of an ovine pulmonary surfactant-associated anionic peptide bactericidal for Pasteurella haemolytica
    • BROGDEN, K.; DE LUCCA, A.; BLAND, J. and ELLIOTT, S. Isolation of an ovine pulmonary surfactant-associated anionic peptide bactericidal for Pasteurella haemolytica. Proceeding National Academy of Sciences USA, 1996, vol. 93, no. 1, p. 412-416.
    • (1996) Proceeding National Academy of Sciences USA , vol.93 , Issue.1 , pp. 412-416
    • Brogden, K.1    De Lucca, A.2    Bland, J.3    Elliott, S.4
  • 14
    • 24444433563 scopus 로고    scopus 로고
    • Induction of innate immune responses by E. coli and purified LPS correlate to organ- and cell-specific expression of Toll-like receptors within the human urinary tract
    • In press
    • BŠCKHED, F.; SŠDERHŠLL, M.; EKMAN, P.; NORMARK, S. and RICHTER-DAHLFORS, A. Induction of innate immune responses by E. coli and purified LPS correlate to organ- and cell-specific expression of Toll-like receptors within the human urinary tract. Cellular Microbiology, vol. 5. In press, 2003.
    • (2003) Cellular Microbiology , vol.5
    • Bšckhed, F.1    Sšderhšll, M.2    Ekman, P.3    Normark, S.4    Richter-Dahlfors, A.5
  • 16
    • 0038315346 scopus 로고    scopus 로고
    • MSI-99, a magainin analogue, imparts enhanced disease resistance in transgenic tobacco and banana
    • CHAKRABARTI, A.; GANAPATHI, T.R.; MUKHERJEE, P.K. and BAPAT, V.A. MSI-99, a magainin analogue, imparts enhanced disease resistance in transgenic tobacco and banana. Planta, 2003, vol. 216, no. 4, p. 587-596.
    • (2003) Planta , vol.216 , Issue.4 , pp. 587-596
    • Chakrabarti, A.1    Ganapathi, T.R.2    Mukherjee, P.K.3    Bapat, V.A.4
  • 18
    • 0035975639 scopus 로고    scopus 로고
    • Inactivation of frog virus 3 and channel catfish virus by esculentin-2P and ranatuerin-2P, two antimicrobial peptides isolated from frog skin
    • CHINCHAR, V.G.; WANG, J.; MURTI, G.; CAREY, C. and ROLLINS-SMITH, L. Inactivation of frog virus 3 and channel catfish virus by esculentin-2P and ranatuerin-2P, two antimicrobial peptides isolated from frog skin. Virology, 2001, vol. 288, p. 351-357.
    • (2001) Virology , vol.288 , pp. 351-357
    • Chinchar, V.G.1    Wang, J.2    Murti, G.3    Carey, C.4    Rollins-Smith, L.5
  • 19
    • 0033915249 scopus 로고    scopus 로고
    • Characterization of a fish antimicrobial peptide: Gene expression subcellular localization and spectrum of activity
    • COLE, A.M.; DAROUICHE, R.O.; LEGARDA, D.; CONNELL, N. and DIAMON, G. Characterization of a fish antimicrobial peptide: gene expression subcellular localization and spectrum of activity. Antimicrobial Agents Chemotherapy, 2000, vol. 44, no. 8, p. 2039-2045.
    • (2000) Antimicrobial Agents Chemotherapy , vol.44 , Issue.8 , pp. 2039-2045
    • Cole, A.M.1    Darouiche, R.O.2    Legarda, D.3    Connell, N.4    Diamon, G.5
  • 20
    • 0037472811 scopus 로고    scopus 로고
    • Antibacterial activity of peptides derived from envelope glycoproteins of HIV-1
    • COLE, A.M.; LIAO, H.I.; GANZ, T. and YANG, O.O. Antibacterial activity of peptides derived from envelope glycoproteins of HIV-1. FEBS Letters, 2003, vol. 535, no. 1-3, p. 195-199.
    • (2003) FEBS Letters , vol.535 , Issue.1-3 , pp. 195-199
    • Cole, A.M.1    Liao, H.I.2    Ganz, T.3    Yang, O.O.4
  • 21
    • 0037235102 scopus 로고    scopus 로고
    • Expression of antimicrobial defensins in the male reproductive tract of rats, mice, and humans
    • COM, E.; BOURGEON, F.; EVRARD, B.; GANZ, T.; COLLEU, D.; JEGOU, B. and PINEAU, C. Expression of antimicrobial defensins in the male reproductive tract of rats, mice, and humans. Biology of Reproduction, 2003, vol. 68, p. 95-104.
    • (2003) Biology of Reproduction , vol.68 , pp. 95-104
    • Com, E.1    Bourgeon, F.2    Evrard, B.3    Ganz, T.4    Colleu, D.5    Jegou, B.6    Pineau, C.7
  • 23
    • 0036214967 scopus 로고    scopus 로고
    • Intracellular targets of antibacterial peptides
    • CUDIC, M. and OTVOS, JR. Intracellular targets of antibacterial peptides. Current Drug Targets, 2002, vol. 3, p. 101-106.
    • (2002) Current Drug Targets , vol.3 , pp. 101-106
    • Cudic, M.1    Otvos, J.R.2
  • 24
    • 0035859020 scopus 로고    scopus 로고
    • Plant pathogens and integrated defense responses to infection
    • DANGL, J.L. and JONES, J. D. Plant pathogens and integrated defense responses to infection. Nature, 2001, vol. 411, no. 6839, p. 826-833.
    • (2001) Nature , vol.411 , Issue.6839 , pp. 826-833
    • Dangl, J.L.1    Jones, J.D.2
  • 25
    • 0035947641 scopus 로고    scopus 로고
    • SDS-induced phenoloxidase activity of hemocyanins from Limulus polyphemus, Eurypelma californicum, and Cancer magister
    • DECKER, H.; RYAN, M.; JAENICKE, E. and TERWILLIGER N. SDS-induced phenoloxidase activity of hemocyanins from Limulus polyphemus, Eurypelma californicum, and Cancer magister. Journal of Biological Chemistry, 2001, vol. 276, no. 2, p. 17796-17799.
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.2 , pp. 17796-17799
    • Decker, H.1    Ryan, M.2    Jaenicke, E.3    Terwilliger, N.4
  • 26
    • 0033971949 scopus 로고    scopus 로고
    • Antifungal peptides: Potential candidates for the treatment of fungal infections
    • DE LUCCA, A.J. Antifungal peptides: potential candidates for the treatment of fungal infections. Expert Opinion on Investigational Drugs,2000, vol. 9, no. 2, p. 273-299.
    • (2000) Expert Opinion on Investigational Drugs , vol.9 , Issue.2 , pp. 273-299
    • De Lucca, A.J.1
  • 27
    • 0035861645 scopus 로고    scopus 로고
    • Crustacean immunity. Antifungal peptides are generated from the C terminus of shrimp hemocyanin in response to microbial challenge
    • DESTOUMIEUX-GARZON, D.; SAULNIER, D.; GARNIER, J.; JOUFFREY, C.; BULET, P. and BACHERE, E. Crustacean immunity. Antifungal peptides are generated from the C terminus of shrimp hemocyanin in response to microbial challenge. Journal of Biological Chemistry, 2001, vol. 276, no. 45, p. 47070-47077.
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.45 , pp. 47070-47077
    • Destoumieux-Garzon, D.1    Saulnier, D.2    Garnier, J.3    Jouffrey, C.4    Bulet, P.5    Bachere, E.6
  • 28
    • 0032411402 scopus 로고    scopus 로고
    • Cysteine-rich antimicrobial peptides in invertebrates
    • DIMARCQ, J.L.; BULET, P.; HEBRU, CH. and HOFFMANN, J. Cysteine-rich antimicrobial peptides in invertebrates. Biopolymers, 1998, vol. 47, p. 465-477.
    • (1998) Biopolymers , vol.47 , pp. 465-477
    • Dimarcq, J.L.1    Bulet, P.2    Hebru, C.H.3    Hoffmann, J.4
  • 29
    • 0001066226 scopus 로고    scopus 로고
    • How intracellular bacteria survive: Surface modifications that promote resistance to host innate immune responses
    • ERNST, R.K.; GUINA, T. and MILLER, S.I. How intracellular bacteria survive: surface modifications that promote resistance to host innate immune responses. Journal of Infectious Diseases, 1999, vol. 179, no. suppl. 2, p. S326-30.
    • (1999) Journal of Infectious Diseases , vol.179 , Issue.SUPPL. 2
    • Ernst, R.K.1    Guina, T.2    Miller, S.I.3
  • 32
    • 0034252292 scopus 로고    scopus 로고
    • Innate immunity-beginning to fulfil its promise?
    • FEARON, D.T. Innate immunity-beginning to fulfil its promise? Nature Immunology, 2000, vol. 2, p. 102-103.
    • (2000) Nature Immunology , vol.2 , pp. 102-103
    • Fearon, D.T.1
  • 33
    • 0041848440 scopus 로고    scopus 로고
    • Comparative studies of immunity proteins of pediocin-like bacteriocins
    • FIMLAND, G.; EIJSINK, V.G. and NISSEN-MEYER, J. Comparative studies of immunity proteins of pediocin-like bacteriocins. Microbiology, 2002, vol. 148, p. 3661-3670.
    • (2002) Microbiology , vol.148 , pp. 3661-3670
    • Fimland, G.1    Eijsink, V.G.2    Nissen-Meyer, J.3
  • 36
    • 0036831170 scopus 로고    scopus 로고
    • The role of hepcidin in iron sequestration during infections and in the pathogenesis of anemia of chronic disease
    • GANZ, T. The role of hepcidin in iron sequestration during infections and in the pathogenesis of anemia of chronic disease. Israeli Medical Association Journal, 2002, vol. 4, no. 11, p. 1043-1045.
    • (2002) Israeli Medical Association Journal , vol.4 , Issue.11 , pp. 1043-1045
    • Ganz, T.1
  • 39
    • 0033863168 scopus 로고    scopus 로고
    • Structural features and biological activities of the cathelicidin-derived antimicrobial peptides
    • GENNARO, R. and ZANETTI, M. Structural features and biological activities of the cathelicidin-derived antimicrobial peptides. Biopolymers, 2000, vol. 55, no. 1, p. 31-49.
    • (2000) Biopolymers , vol.55 , Issue.1 , pp. 31-49
    • Gennaro, R.1    Zanetti, M.2
  • 40
    • 0033871574 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides: Towards clinical applications
    • HANCOCK, R.E.W. Cationic antimicrobial peptides: towards clinical applications. Expert Opinion on Investigational Drugs, 2000, vol. 9, p. 1723-1729.
    • (2000) Expert Opinion on Investigational Drugs , vol.9 , pp. 1723-1729
    • Hancock, R.E.W.1
  • 42
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • HANCOCK, R.E.W. and LEHRER, R. Cationic peptides: a new source of antibiotics. Trends in Biotechnology, 1998, vol. 16, p. 82-88.
    • (1998) Trends in Biotechnology , vol.16 , pp. 82-88
    • Hancock, R.E.W.1    Lehrer, R.2
  • 46
    • 0036167107 scopus 로고    scopus 로고
    • Drosophila innate immunity: An evolutionary perspective
    • HOFFMANN, J.A. and REICHHART, J.M. Drosophila innate immunity: an evolutionary perspective. Nature Immunology, 2002, vol. 3, no. 2, p. 121-126.
    • (2002) Nature Immunology , vol.3 , Issue.2 , pp. 121-126
    • Hoffmann, J.A.1    Reichhart, J.M.2
  • 47
    • 0033591428 scopus 로고    scopus 로고
    • Phylogenetic perspectives in innate immunity
    • HOFFMANN, J.A.; KAFATOS F.C.; JANEWAY C.A. and EZEKOWITZ R.A. Phylogenetic perspectives in innate immunity. Science, 1999, vol. 284, no. 5418, p. 1313-1318.
    • (1999) Science , vol.284 , Issue.5418 , pp. 1313-1318
    • Hoffmann, J.A.1    Kafatos, F.C.2    Janeway, C.A.3    Ezekowitz, R.A.4
  • 48
    • 0037228233 scopus 로고    scopus 로고
    • Transcriptional profile of the Escherichia coli response to the antimicrobial insect peptide cecropin A
    • HONG, R.W.; SHCHEPETOV, M.; WEISER, J.N.; AXELSEN, P.H. Transcriptional profile of the Escherichia coli response to the antimicrobial insect peptide cecropin A. Antimicrobial Agents and Chemotherapy, 2003, vol. 47, no. 1, p. 1-6.
    • (2003) Antimicrobial Agents and Chemotherapy , vol.47 , Issue.1 , pp. 1-6
    • Hong, R.W.1    Shchepetov, M.2    Weiser, J.N.3    Axelsen, P.H.4
  • 49
    • 0029842737 scopus 로고    scopus 로고
    • A member of the arthropod defensin family from edible mediterranean mussels (Mytilus galloprovincialis)
    • HUBERT, F.; NEL, T. and ROCH, P. A member of the arthropod defensin family from edible mediterranean mussels (Mytilus galloprovincialis). European Journal of Biochemistry, 1996, vol. 240, no. 1, p. 302-306.
    • (1996) European Journal of Biochemistry , vol.240 , Issue.1 , pp. 302-306
    • Hubert, F.1    Nel, T.2    Roch, P.3
  • 50
    • 0018820115 scopus 로고
    • Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • HULTMARK, D.; STEINER, H.; RASMUSON, T. and BOMAN, H.G. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia. European Journal of Biochemistry, 1980, vol. 106, no. 1, p. 7-16.
    • (1980) European Journal of Biochemistry , vol.106 , Issue.1 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 52
    • 0028990155 scopus 로고
    • Bacteriocins of gram-positive bacteria
    • JACK, R.W.; TAGG, J.R. and RAY, B. Bacteriocins of gram-positive bacteria. Microbiology Review, 1995, vol. 59, no. 2, p. 171-200.
    • (1995) Microbiology Review , vol.59 , Issue.2 , pp. 171-200
    • Jack, R.W.1    Tagg, J.R.2    Ray, B.3
  • 53
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • JAMES C.; ROVERSI, P. and TAWFIK, D.S. Antibody multispecificity mediated by conformational diversity. Science, 2003, vol. 299, no. 5611, p. 1362-1367.
    • (2003) Science , vol.299 , Issue.5611 , pp. 1362-1367
    • James, C.1    Roversi, P.2    Tawfik, D.S.3
  • 55
    • 0026663308 scopus 로고
    • Genetics of ribosomally synthesized peptide antibiotics
    • KOLTER, R. and MORENO F. Genetics of ribosomally synthesized peptide antibiotics. Annual Review of Microbiology, 1992, vol. 46, p. 141-163.
    • (1992) Annual Review of Microbiology , vol.46 , pp. 141-163
    • Kolter, R.1    Moreno, F.2
  • 56
    • 0035853022 scopus 로고    scopus 로고
    • The antibacterial pyrrhocoricin inhibits the ATPase action of DnaK and prevents chaperone-assisted protein folding
    • KRAGOL, G.; LOVAS, S.; VARADI, G.; CONDIE B.A.; HOFFMANN R. and OTVOS L. Jr. The antibacterial pyrrhocoricin inhibits the ATPase action of DnaK and prevents chaperone-assisted protein folding. Biochemistry, 2001, vol. 40, no. 10, p. 3016-3026.
    • (2001) Biochemistry , vol.40 , Issue.10 , pp. 3016-3026
    • Kragol, G.1    Lovas, S.2    Varadi, G.3    Condie, B.A.4    Hoffmann, R.5    Otvos Jr., L.6
  • 59
    • 0035830902 scopus 로고    scopus 로고
    • Insect immunity. Constitutive expression of a cysteine-rich antifungal and a linear antibacterial peptide in termite insect
    • LAMBERTY, M.; ZACHARY, D.; LANOT, R.; BORDEREAU, C.; ROBERT, A.; HOFFMANN, J.A. and BULET, P. Insect immunity. constitutive expression of a cysteine-rich antifungal and a linear antibacterial peptide in termite insect. Journal of Biological Chemistry, 2001, vol. 276, no. 6, p. 4085-4092.
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.6 , pp. 4085-4092
    • Lamberty, M.1    Zachary, D.2    Lanot, R.3    Bordereau, C.4    Robert, A.5    Hoffmann, J.A.6    Bulet, P.7
  • 61
    • 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.L.; PARK, K.T. and PARK, H.Y. Isolation of p-hydroxycinnamaldehyde as an antibacterial substance from the saw fly, Acantholyda parki S. FEBS Letters, 1999, vol. 442, no. 1, p. 53-56.
    • (1999) FEBS Letters , vol.442 , Issue.1 , pp. 53-56
    • Leem, J.Y.1    Jeong, I.L.2    Park, K.T.3    Park, H.Y.4
  • 62
    • 0029889071 scopus 로고    scopus 로고
    • Purification and characterization of N-alanyl-5-S-gluthathionyl-3,4- dihydroxyphenylalanine, a novel antibacterial substance of Sarcophaga peregrina (Flesh fly)
    • LEEM, J.Y. Purification and characterization of N-alanyl-5-S- gluthathionyl-3,4-dihydroxyphenylalanine, a novel antibacterial substance of Sarcophaga peregrina (Flesh fly). Journal of Biological Chemistry, 1996, vol. 271, no. 23, p. 13573-13577.
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.23 , pp. 13573-13577
    • Leem, J.Y.1
  • 63
    • 0036467390 scopus 로고    scopus 로고
    • Defensin of vertebrate animals
    • LEHRER, R.I. and GANZ, T. Defensin of vertebrate animals. Current Opinion in Immunology, 2002, vol. 14, no. 1, p. 96-102.
    • (2002) Current Opinion in Immunology , vol.14 , Issue.1 , pp. 96-102
    • Lehrer, R.I.1    Ganz, T.2
  • 64
    • 0029819455 scopus 로고    scopus 로고
    • Characterization and ion channel activities of novel antibacterial proteins from the skin mucosa of carp (Cyprinus carpio)
    • LEMAITRE, C.; ORANGE, N.; SAGLIO, P.; SAINT, N.; GAGNON, J. and MOLLE, G. Characterization and ion channel activities of novel antibacterial proteins from the skin mucosa of carp (Cyprinus carpio). European Journal of Biochemistry, 1996, vol. 240, no. 1, p. 143-149.
    • (1996) European Journal of Biochemistry , vol.240 , Issue.1 , pp. 143-149
    • Lemaitre, C.1    Orange, N.2    Saglio, P.3    Saint, N.4    Gagnon, J.5    Molle, G.6
  • 65
    • 0036712603 scopus 로고    scopus 로고
    • Ligatoxin B, a new cytotoxic protein with a novel helix-turn-helix DNA-binding domain from the mistletoe Phoradendron liga
    • LI,S.S.; GULLBO, J.; LINDHOLM, P.; LARSSON, R.; THUNBERG, E.; SAMUELSSON, G.; BOHLIN, L. and CLAESON, P. Ligatoxin B, a new cytotoxic protein with a novel helix-turn-helix DNA-binding domain from the mistletoe Phoradendron liga. Biochemistry Journal, 2002, vol. 366, no. 2, 405-413.
    • (2002) Biochemistry Journal , vol.366 , Issue.2 , pp. 405-413
    • Li, S.S.1    Gullbo, J.2    Lindholm, P.3    Larsson, R.4    Thunberg, E.5    Samuelsson, G.6    Bohlin, L.7    Claeson, P.8
  • 66
    • 0037218616 scopus 로고    scopus 로고
    • By IL-1 Signaling, monocyte-derived cells dramatically enhance the epidermal antimicrobial response to lipopolysaccharide
    • LIU, L.; ROBERTS, A.A. and GANZ, T. By IL-1 Signaling, monocyte-derived cells dramatically enhance the epidermal antimicrobial response to lipopolysaccharide. Journal of Immunology, 2003, vol. 170, no. 1, p. 575-580.
    • (2003) Journal of Immunology , vol.170 , Issue.1 , pp. 575-580
    • Liu, L.1    Roberts, A.A.2    Ganz, T.3
  • 67
    • 0034001189 scopus 로고    scopus 로고
    • Purification, characterization, and molecular cloning of the gene of a seed-specific antimicrobial protein from pokeweed
    • LIU, Y.; LUO, J.; XU, C.; REN, F.; PENG, C.; WU, G. and ZHAO, J. Purification, characterization, and molecular cloning of the gene of a seed-specific antimicrobial protein from pokeweed. Plant Physiology, 2000, vol. 122, no. 4, p. 1015-1024.
    • (2000) Plant Physiology , vol.122 , Issue.4 , pp. 1015-1024
    • Liu, Y.1    Luo, J.2    Xu, C.3    Ren, F.4    Peng, C.5    Wu, G.6    Zhao, J.7
  • 68
    • 17644433467 scopus 로고    scopus 로고
    • Strong synergy between a eukaryotic antimicrobial peptide and bacteriocins from lactic acid bacteria
    • LÜDERS, T.; BIRKEMO, G.A.; FIMLAND, G.; NISSEN-MEYER, J. and NES, I.F. Strong synergy between a eukaryotic antimicrobial peptide and bacteriocins from lactic acid bacteria. Applied and Environmental Microbiology, 2003, vol. 69, no. 3, p. 1797-1799.
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.3 , pp. 1797-1799
    • Lüders, T.1    Birkemo, G.A.2    Fimland, G.3    Nissen-Meyer, J.4    Nes, I.F.5
  • 70
    • 0036178451 scopus 로고    scopus 로고
    • The solution structure of gomesin an antimicrobial cysteine-rich peptide from spider
    • MANDARD, N.; BULET, P.; CAILLE, A.; DAFFRE, S. and VOVELLE, F. The solution structure of gomesin an antimicrobial cysteine-rich peptide from spider. European Journal of Biochemistry, 2002, vol. 269, no. 4, p. 1190-1198.
    • (2002) European Journal of Biochemistry , vol.269 , Issue.4 , pp. 1190-1198
    • Mandard, N.1    Bulet, P.2    Caille, A.3    Daffre, S.4    Vovelle, F.5
  • 71
    • 0032738363 scopus 로고    scopus 로고
    • Androctonin, a novel antimicrobial peptide from scorpion Androctonus australis: Solution structure and molecular dynamics simulations in the presence of a lipid monolayer
    • MANDARD, N.; SY, D.; MAUFRAIS, C.; BONMATIN J.M.; BULET, P.; HETRU, C. and VOVELLE, F. Androctonin, a novel antimicrobial peptide from scorpion Androctonus australis: solution structure and molecular dynamics simulations in the presence of a lipid monolayer. Journal of Biomolecular Structure and. Dynamics, 1999, vol. 17, no. 2, p. 367-380.
    • (1999) Journal of Biomolecular Structure and Dynamics , vol.17 , Issue.2 , pp. 367-380
    • Mandard, N.1    Sy, D.2    Maufrais, C.3    Bonmatin, J.M.4    Bulet, P.5    Hetru, C.6    Vovelle, F.7
  • 72
    • 0030997078 scopus 로고    scopus 로고
    • Purification, characterisation and cDNA cloning of an antimicrobial peptide from Macadamia integrifolia
    • MARCUS, J.P.; GOULTER, K.C.; GREEN, J.L.; HARRISON, S.J. and MANNERS, J.M. Purification, characterisation and cDNA cloning of an antimicrobial peptide from Macadamia integrifolia. European Journal of Biochemistry, 1997, vol. 244, no. 3, p. 743-749.
    • (1997) European Journal of Biochemistry , vol.244 , Issue.3 , pp. 743-749
    • Marcus, J.P.1    Goulter, K.C.2    Green, J.L.3    Harrison, S.J.4    Manners, J.M.5
  • 73
    • 0035717170 scopus 로고    scopus 로고
    • Cell-free production of biologically active polypeptides: Application to the synthesis of antibacterial peptide cecropin
    • MARTEMYANOV, K.A.; SHIROKOV, V.A.; KURNASOV, O.V.; GUDKOV, A.T. and SPIRIN, A.S. Cell-free production of biologically active polypeptides: Application to the synthesis of antibacterial peptide cecropin. Protein Expression and Purification, 2001, vol. 21, no. 3, p. 456-461.
    • (2001) Protein Expression and Purification , vol.21 , Issue.3 , pp. 456-461
    • Martemyanov, K.A.1    Shirokov, V.A.2    Kurnasov, O.V.3    Gudkov, A.T.4    Spirin, A.S.5
  • 74
    • 0032693639 scopus 로고    scopus 로고
    • Why and how peptide-lipid interaction utilized for self defense? Magainins and tachyplesins as archetypes
    • MATSUZAKI, K. Why and how peptide-lipid interaction utilized for self defense? Magainins and tachyplesins as archetypes. Biochimica et Biophysca Acta, 1999, vol. 1462, no. 1-2, p. 1-10.
    • (1999) Biochimica et Biophysca Acta , vol.1462 , Issue.1-2 , pp. 1-10
    • Matsuzaki, K.1
  • 75
    • 0033490117 scopus 로고    scopus 로고
    • Mussel defensins are synthesised and processed in granulocytes then released into the plasma after bacterial challenge
    • MITTA, G.; VANDENBULCKE, F.; HUBERT, F. and ROCH, P. Mussel defensins are synthesised and processed in granulocytes then released into the plasma after bacterial challenge. Journal of Cell Sciences, 1999, vol. 112, no. 23, p. 4233-4242.
    • (1999) Journal of Cell Sciences , vol.112 , Issue.23 , pp. 4233-4242
    • Mitta, G.1    Vandenbulcke, F.2    Hubert, F.3    Roch, P.4
  • 76
    • 0037157179 scopus 로고    scopus 로고
    • Production of recombinant antimicrobial peptide in transgenic plants using a modified VMA intein expression system
    • MORASSUTTI, C.; DE AMICIS, F.; SKERLAVAJ, B.; ZANETTI, M. and MARCHETTI, S. Production of recombinant antimicrobial peptide in transgenic plants using a modified VMA intein expression system. FEBS Letters, 2002, vol. 519, no. 1-3, p. 141-146.
    • (2002) FEBS Letters , vol.519 , Issue.1-3 , pp. 141-146
    • Morassutti, C.1    De Amicis, F.2    Skerlavaj, B.3    Zanetti, M.4    Marchetti, S.5
  • 77
    • 0037393277 scopus 로고    scopus 로고
    • Expression of penaeidin antimicrobial peptides in early larval stages of the shrimp Penaeus vannamei
    • MUÑOZ, M.; VANDENBULCKE, F.; GUEGUEN, Y. and BACHÈRE, E. Expression of penaeidin antimicrobial peptides in early larval stages of the shrimp Penaeus vannamei. Developmental and Comparative Immunology, 2003, vol. 27, no. 4, p. 283-289.
    • (2003) Developmental and Comparative Immunology , vol.27 , Issue.4 , pp. 283-289
    • Muñoz, M.1    Vandenbulcke, F.2    Gueguen, Y.3    Bachère, E.4
  • 78
    • 0036274247 scopus 로고    scopus 로고
    • Expression and distribution of penaeidin antimicrobial peptides are regulated by haemocyte reactions in microbial challenged shrimp
    • MUÑOZ, M.; VANDENBULCKE, F.; SAULNIER, D.; and BACHÈRE, E. Expression and distribution of penaeidin antimicrobial peptides are regulated by haemocyte reactions in microbial challenged shrimp. European Journal of Biochemistry, 2002, vol. 269, no. 45, p. 2678-2689.
    • (2002) European Journal of Biochemistry , vol.269 , Issue.45 , pp. 2678-2689
    • Muñoz, M.1    Vandenbulcke, F.2    Saulnier, D.3    Bachère, E.4
  • 79
    • 0035933371 scopus 로고    scopus 로고
    • Two isoforms of a member of the arthropod defensin family from the soft tick, Ornithodoros moubata (Acari: Argasidae)
    • NAKAJIMA Y.; VAN DER GOES VAN NATERS-YASUI, A.; TAYLOR, D. and YAMAKAWA M. Two isoforms of a member of the arthropod defensin family from the soft tick, Ornithodoros moubata (Acari: Argasidae). Insect Biochemistry and Molecular Biology, 2001, vol. 31, no. 8, p. 747-751.
    • (2001) Insect Biochemistry and Molecular Biology , vol.31 , Issue.8 , pp. 747-751
    • Nakajima, Y.1    Van Der Goes Van Naters-Yasui, A.2    Taylor, D.3    Yamakawa, M.4
  • 80
    • 0037073952 scopus 로고    scopus 로고
    • Catalytic antibody bridges innate and adaptive immunity
    • NATHAN, C. Catalytic antibody bridges innate and adaptive immunity. Science, 2002, vol. 298, no. 5601, p. 2143-2144.
    • (2002) Science , vol.298 , Issue.5601 , pp. 2143-2144
    • Nathan, C.1
  • 81
    • 0033542413 scopus 로고    scopus 로고
    • Emergence of vancomycin tolerance in Streptococcus pneumoniae
    • NOVAK, R.; HENRIQUES, B.; CHARPENTIER, E.; NORMARK, S. and TUOMANEN, E. Emergence of vancomycin tolerance in Streptococcus pneumoniae. Nature, 1999, vol. 399, no. 6736, p. 590-591.
    • (1999) Nature , vol.399 , Issue.6736 , pp. 590-591
    • Novak, R.1    Henriques, B.2    Charpentier, E.3    Normark, S.4    Tuomanen, E.5
  • 82
    • 0035292313 scopus 로고    scopus 로고
    • Classification and mode of action of membrane-active bacteriocins produced by gram-positive bacteria
    • OSCÁRIZ, J.C. and PISABARRO, A.G. Classification and mode of action of membrane-active bacteriocins produced by gram-positive bacteria. International Microbiology, 2001, vol. 4, no. 1, p. 13-19.
    • (2001) International Microbiology , vol.4 , Issue.1 , pp. 13-19
    • Oscáriz, J.C.1    Pisabarro, A.G.2
  • 83
    • 0033763238 scopus 로고    scopus 로고
    • Transgenic plants expressing cationic peptide chimeras exibit broad-spectrum resistance to phytopathogens
    • OSUKY, M.; ZHOU, G.; OSUSKA, L.; HANCOCK, R.E.W.; KAY, W.W. and MISRA, S. Transgenic plants expressing cationic peptide chimeras exibit broad-spectrum resistance to phytopathogens. Nature Biotechnology, 2000, vol. 18, no. 11, p. 1162-1166.
    • (2000) Nature Biotechnology , vol.18 , Issue.11 , pp. 1162-1166
    • Osuky, M.1    Zhou, G.2    Osuska, L.3    Hancock, R.E.W.4    Kay, W.W.5    Misra, S.6
  • 84
    • 0033754189 scopus 로고    scopus 로고
    • Antibacterial peptides isolated from insects
    • OTVOS, L. Jr. Antibacterial peptides isolated from insects. Journal of Peptide Sciences, 2000, vol. 6, no. 10, p. 497-511.
    • (2000) Journal of Peptide Sciences , vol.6 , Issue.10 , pp. 497-511
    • Otvos Jr., L.1
  • 85
    • 0033674821 scopus 로고    scopus 로고
    • Characterization and cDNA cloning of two glycine-and histidin-rich antimicrobial peptides from the roots of shepherd's purse, Capsella bursa-pastor
    • PARK, C.J.; PARK, C.B.; HONG S.S.; LEE, H.S.; LEE, S.Y. and KIM, S.C. Characterization and cDNA cloning of two glycine-and histidin-rich antimicrobial peptides from the roots of shepherd's purse, Capsella bursa-pastor. Plant Molecular Biology, 2000, vol. 44, no. 2, p. 187-197.
    • (2000) Plant Molecular Biology , vol.44 , Issue.2 , pp. 187-197
    • Park, C.J.1    Park, C.B.2    Hong, S.S.3    Lee, H.S.4    Lee, S.Y.5    Kim, S.C.6
  • 86
    • 0032561422 scopus 로고    scopus 로고
    • Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus
    • PARK, I.Y. Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus. FEBS Letters, 1998, vol. 437, no.3, p. 258-262.
    • (1998) FEBS Letters , vol.437 , Issue.3 , pp. 258-262
    • Park, I.Y.1
  • 87
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • PARK, C.B.; KIM, H.S. and KIM, S.C. Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochemical Biophysical Research Communication, 1998, vol. 244, no. 1, p. 253-257.
    • (1998) Biochemical Biophysical Research Communication , vol.244 , Issue.1 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 89
    • 0035038578 scopus 로고    scopus 로고
    • Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurodicin
    • PATRZYKAT, A.; ZHANG, L.; MENDOZA, V.; IWAMA, G.K. and HANCOCK, R.E.W. Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurodicin. Antimicrobial Agents Chemotherapy, 2001, vol. 45, no. 5, p. 1337-1342.
    • (2001) Antimicrobial Agents Chemotherapy , vol.45 , Issue.5 , pp. 1337-1342
    • Patrzykat, A.1    Zhang, L.2    Mendoza, V.3    Iwama, G.K.4    Hancock, R.E.W.5
  • 90
    • 0036532403 scopus 로고    scopus 로고
    • How do bacteria resist human antimicrobial peptides?
    • PESCHEL, A. How do bacteria resist human antimicrobial peptides? Trends in Microbiology, 2002, vol. 10, no. 4, p. 179-196.
    • (2002) Trends in Microbiology , vol.10 , Issue.4 , pp. 179-196
    • Peschel, A.1
  • 91
    • 0021263092 scopus 로고
    • Fungistatic and fungicidal activity of human parotid salivary histidine-rich polypeptides on Candida albicans
    • POLLOCK, J.J.; DENPITIYA, L.; MACKAY, B.J. and IACONO, V.J. Fungistatic and fungicidal activity of human parotid salivary histidine-rich polypeptides on Candida albicans. Infection and Immunity, 1984, vol. 40, no. 3, p. 702-707.
    • (1984) Infection and Immunity , vol.40 , Issue.3 , pp. 702-707
    • Pollock, J.J.1    Denpitiya, L.2    Mackay, B.J.3    Iacono, V.J.4
  • 92
    • 0037442855 scopus 로고    scopus 로고
    • An amphibian antimicrobial peptide variant expressed in Nicotiana tabacum confers resistance to phytopathogens
    • PONTI, D.; MANGONI, M.L.; MIGNOGNA, G.; SIMMACO M. and BARRA D. An amphibian antimicrobial peptide variant expressed in Nicotiana tabacum confers resistance to phytopathogens. Biochemical Journal, 2003, vol. 15, no. 370, p. 121-127.
    • (2003) Biochemical Journal , vol.15 , Issue.370 , pp. 121-127
    • Ponti, D.1    Mangoni, M.L.2    Mignogna, G.3    Simmaco, M.4    Barra, D.5
  • 93
    • 0033594420 scopus 로고    scopus 로고
    • Antibacterial peptide from Helicobacter pylori
    • PUTSEP, K.; BRANDEN, C.I.; BOMAN, H.G. and NORMARK, S. Antibacterial peptide from Helicobacter pylori. Nature, 1999, vol. 398, no. 6729, p. 671-672.
    • (1999) Nature , vol.398 , Issue.6729 , pp. 671-672
    • Putsep, K.1    Branden, C.I.2    Boman, H.G.3    Normark, S.4
  • 98
    • 0034913684 scopus 로고    scopus 로고
    • Vertebrate innate immunity resembles a mosaic of invertebrate immune responses
    • SALZET, M. Vertebrate innate immunity resembles a mosaic of invertebrate immune responses. Trends in Immunology, 2001, vol. 22, no. 6, p. 285-288.
    • (2001) Trends in Immunology , vol.22 , Issue.6 , pp. 285-288
    • Salzet, M.1
  • 99
    • 0035156142 scopus 로고    scopus 로고
    • Involvement of pro-enkephalin-derived peptides in immunity
    • SALZET, M. and TASIEMSKI, A. Involvement of pro-enkephalin-derived peptides in immunity. Developmental and Comparative Immunology, 2001, vol. 25, no. 3, p. 177-185.
    • (2001) Developmental and Comparative Immunology , vol.25 , Issue.3 , pp. 177-185
    • Salzet, M.1    Tasiemski, A.2
  • 100
    • 0346034649 scopus 로고    scopus 로고
    • Tryptophan-rich antimicrobial peptides: Comparative properties and membrane interactions
    • SCHIBLI, D.J.; EPAND, R.F.; VOGEL, A.J. and EPAND, R.M. Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions. Biochemistry and Cellular Biology, 2002, vol. 80, no. 5, p. 667-677.
    • (2002) Biochemistry and Cellular Biology , vol.80 , Issue.5 , pp. 667-677
    • Schibli, D.J.1    Epand, R.F.2    Vogel, A.J.3    Epand, R.M.4
  • 101
    • 0000284412 scopus 로고    scopus 로고
    • Potential of antagonistic microorganisms and bacteriocins for the biological preservation of food
    • SCHILLINGER, U.; GEISEN, R. and HOLZAPFEL, W.H. Potential of antagonistic microorganisms and bacteriocins for the biological preservation of food. Trends in Food Sciences and Technology, 1996, vol. 7, no. 5, p. 158-164.
    • (1996) Trends in Food Sciences and Technology , vol.7 , Issue.5 , pp. 158-164
    • Schillinger, U.1    Geisen, R.2    Holzapfel, W.H.3
  • 103
    • 0032544607 scopus 로고    scopus 로고
    • Novel defensin subfamily from spinach (Spinacia oleracea)
    • SEGURA, A.; MORENO, M.; MOLINA, A. and GARCÍA-OLMEDO, F. Novel defensin subfamily from spinach (Spinacia oleracea). FEBS Letters, 1998, vol. 435, no. 13, p. 159-162.
    • (1998) FEBS Letters , vol.435 , Issue.13 , pp. 159-162
    • Segura, A.1    Moreno, M.2    Molina, A.3    García-Olmedo, F.4
  • 105
    • 0034721871 scopus 로고    scopus 로고
    • Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family
    • SILVA, Jr.P.I.; DAFFRE, S. and BULET, P. Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family. Journal of Biological Chemistry, 2000, vol. 275, no. 43, p. 33464-33470.
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.43 , pp. 33464-33470
    • Silva Jr., P.I.1    Daffre, S.2    Bulet, P.3
  • 106
    • 0032444189 scopus 로고    scopus 로고
    • Antimicrobial peptide from amphibian skin: What do they tell us?
    • SIMMACO, M.; MIGNOGNA, G. and BARRA, D. Antimicrobial peptide from amphibian skin: What do they tell us? Biopolymers, 1998, vol. 47, no. 6, p. 435-450.
    • (1998) Biopolymers , vol.47 , Issue.6 , pp. 435-450
    • Simmaco, M.1    Mignogna, G.2    Barra, D.3
  • 108
    • 0037198693 scopus 로고    scopus 로고
    • A component of innate immunity prevents bacterial biofilm development
    • SINGH, P.K.; PARSEK, M.R.; GREENBERG, E.P. and WELSH, M.J. A component of innate immunity prevents bacterial biofilm development. Nature, 2002, vol. 417, no. 6888, p. 552-555.
    • (2002) Nature , vol.417 , Issue.6888 , pp. 552-555
    • Singh, P.K.1    Parsek, M.R.2    Greenberg, E.P.3    Welsh, M.J.4
  • 110
    • 0034740811 scopus 로고    scopus 로고
    • P-I3-kinase p85 is a target molecule of proline-rich antimicrobial peptide to suppress proliferation of ras-transformed cells
    • TANAKA, K. P-I3 - kinase p85 is a target molecule of proline-rich antimicrobial peptide to suppress proliferation of ras - transformed cells. Japanese Journal of Cancer Research, 2001, vol. 92, no. 9, p. 959-967.
    • (2001) Japanese Journal of Cancer Research , vol.92 , Issue.9 , pp. 959-967
    • Tanaka, K.1
  • 111
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produces in primate leukocytes by the ligation of two truncated alpha-defensins
    • TANG, Y.Q.; YUANG, J.; OSAPAY, G.D.; OSAPAY, K.; TRAN, D.; MILLER, C.J.; OUELLETTE, A.J. and SELSTED, M.E. A cyclic antimicrobial peptide produces in primate leukocytes by the ligation of two truncated alpha-defensins. Science, 1999, vol. 286, no. 5439, p. 498-502.
    • (1999) Science , vol.286 , Issue.5439 , pp. 498-502
    • Tang, Y.Q.1    Yuang, J.2    Osapay, G.D.3    Osapay, K.4    Tran, D.5    Miller, C.J.6    Ouellette, A.J.7    Selsted, M.E.8
  • 113
    • 0032751756 scopus 로고    scopus 로고
    • Permeabilization of fungal membranes by plant defensins inhibits fungal
    • THEVISSEN, K.; TERRAS, F.R.G. and BROEKAERT, W.F. Permeabilization of fungal membranes by plant defensins inhibits fungal. Applied and Environmental Microbiology, 1999, vol. 65, no. 12, p. 5451-5458.
    • (1999) Applied and Environmental Microbiology , vol.65 , Issue.12 , pp. 5451-5458
    • Thevissen, K.1    Terras, F.R.G.2    Broekaert, W.F.3
  • 114
    • 0036257512 scopus 로고    scopus 로고
    • Molecular diversity in gene-encoded, cationic antimicrobials polypeptides
    • TOSSI, A. and SANDRI, L. Molecular diversity in gene-encoded, cationic antimicrobials polypeptides. Current Pharmaceutical Design, 2002, vol. 8, no. 9, p. 743-761.
    • (2002) Current Pharmaceutical Design , vol.8 , Issue.9 , pp. 743-761
    • Tossi, A.1    Sandri, L.2
  • 115
    • 0032319580 scopus 로고    scopus 로고
    • Human salivary histatins: Promising anti-fungal therapeutic agents
    • TSAI, H. and BOBEK, L.A. Human salivary histatins: promising anti-fungal therapeutic agents. Critical Reviews in Oral Biology and Medicine, 1998, vol. 9, no. 4, p. 480-497.
    • (1998) Critical Reviews in Oral Biology and Medicine , vol.9 , Issue.4 , pp. 480-497
    • Tsai, H.1    Bobek, L.A.2
  • 116
    • 0037133259 scopus 로고    scopus 로고
    • Constitutive expression of a single antimicrobial peptide can restore wild-type resistance to infection in immunodeficient Drosophila mutants
    • TZOU, P.; REICHART, J.M. and LEMAITRE, B. Constitutive expression of a single antimicrobial peptide can restore wild-type resistance to infection in immunodeficient Drosophila mutants. Proceedings of the National Academy of Science USA, 2002, vol. 99, no. 4, p. 2152-2157.
    • (2002) Proceedings of the National Academy of Science USA , vol.99 , Issue.4 , pp. 2152-2157
    • Tzou, P.1    Reichart, J.M.2    Lemaitre, B.3
  • 117
    • 0036154401 scopus 로고    scopus 로고
    • Rapid two-step procedure for large-scale purification of Pediocin-like bacteriocins and other cationic antimicrobial peptides from complex culture medium
    • UTENG, M.; HAUGE, H.H.; BRONDZ, I.; NISSEN-MEYER, J. and FIMLAND, G. Rapid two-step procedure for large-scale purification of Pediocin-like bacteriocins and other cationic antimicrobial peptides from complex culture medium. Applied and Environmental Microbiology, 2002, vol. 68, no. 2, p. 952-956.
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.2 , pp. 952-956
    • Uteng, M.1    Hauge, H.H.2    Brondz, I.3    Nissen-Meyer, J.4    Fimland, G.5
  • 118
    • 0035206410 scopus 로고    scopus 로고
    • Quest for antimicrobial genes to engineer disease-resistant crops
    • VAN DER BIESEN, E.A. Quest for antimicrobial genes to engineer disease-resistant crops. Trends in Plant Sciences, 2001, vol. 6, no. 3, p. 89-91.
    • (2001) Trends in Plant Sciences , vol.6 , Issue.3 , pp. 89-91
    • Van Der Biesen, E.A.1
  • 119
    • 84915805738 scopus 로고    scopus 로고
    • Antimicrobial peptides: New weapons to control parasitic infections?
    • In press
    • VIZIOLI, J. and SALZET, M. Antimicrobial peptides: new weapons to control parasitic infections? Trends in Parasitology, 2003, vol. 19, In press.
    • (2003) Trends in Parasitology , vol.19
    • Vizioli, J.1    Salzet, M.2
  • 120
    • 0036842381 scopus 로고    scopus 로고
    • Antimicrobial peptides from animals: Focus on invertebrates
    • VIZIOLI, J., and SALZET, M. Antimicrobial peptides from animals: focus on invertebrates. Trends in Pharmacological Sciences, 2002, vol. 23, no. 11, p. 494-496.
    • (2002) Trends in Pharmacological Sciences , vol.23 , Issue.11 , pp. 494-496
    • Vizioli, J.1    Salzet, M.2
  • 122
    • 0032698902 scopus 로고    scopus 로고
    • Porcine pulmonary surfactant preparations contain the antibacterial peptide prophenin and a C-terminal 18-residue fragment thereof
    • WANG, Y.; GRIFFITHS W.J.; CURSTEDT, T. and JOHANSSON, J. Porcine pulmonary surfactant preparations contain the antibacterial peptide prophenin and a C-terminal 18-residue fragment thereof. FEBS Letters, 1999, vol. 460, no. 2, p. 257-262.
    • (1999) FEBS Letters , vol.460 , Issue.2 , pp. 257-262
    • Wang, Y.1    Griffiths, W.J.2    Curstedt, T.3    Johansson, J.4
  • 123
    • 0034106065 scopus 로고    scopus 로고
    • Tenehtium-99m labeled antimicrobial peptide discriminate between bacterial infection and sterile inflammations
    • WELLING, M.M.; PAULUSMA-ANNEMA, A.; BALTER, H.S.; PAUWELS, E.K. and NIBBERING, P.H. Tenehtium-99m labeled antimicrobial peptide discriminate between bacterial infection and sterile inflammations. European Journal of Nuclear Medicine, 2000, vol. 27, no. 3, p. 292-301.
    • (2000) European Journal of Nuclear Medicine , vol.27 , Issue.3 , pp. 292-301
    • Welling, M.M.1    Paulusma-Annema, A.2    Balter, H.S.3    Pauwels, E.K.4    Nibbering, P.H.5
  • 124
    • 0002220941 scopus 로고
    • Biologically functional proteins of milk and peptides derived from milk proteins
    • YAMAUCHI, K. Biologically functional proteins of milk and peptides derived from milk proteins. Bulletin IDF, 1992, vol. 272, no. 1, p. 51-58.
    • (1992) Bulletin IDF , vol.272 , Issue.1 , pp. 51-58
    • Yamauchi, K.1
  • 125
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • ZASLOFF, M. Antimicrobial peptides of multicellular organisms. Nature, 2002, vol. 415, no. 6870, p. 389-395.
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 126
    • 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. Proceeding of the National Academy of Sciences USA, 1987, vol. 84, no. 9, p. 5449-5453.
    • (1987) Proceeding of the National Academy of Sciences USA , vol.84 , Issue.9 , pp. 5449-5453
    • Zasloff, M.1
  • 127
    • 0036898746 scopus 로고    scopus 로고
    • Genomic organization and regulation of three cecropin genes in Anopheles gambiae
    • ZHENG, X.L. and ZHENG, A.L. Genomic organization and regulation of three cecropin genes in Anopheles gambiae. Insect Molecular Biology, 2002, vol. 11, no. 6, p. 517-525.
    • (2002) Insect Molecular Biology , vol.11 , Issue.6 , pp. 517-525
    • Zheng, X.L.1    Zheng, A.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.