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Volumn 43, Issue 1, 1999, Pages 1-11

Antifungal peptides: Novel therapeutic compounds against emerging pathogens

Author keywords

[No Author keywords available]

Indexed keywords

ACULEACIN A; ANTIFUNGAL AGENT; AUREOBASIDIN DERIVATIVE; BACTERICIDAL PERMEABILITY INCREASING PROTEIN; CECROPIN DERIVATIVE; CEPACIDINE DERIVATIVE; DEFENSIN DERIVATIVE; DERMASEPTIN; DROSOMYCIN; ECHINOCANDIN B DERIVATIVE; FR 900403; GALLINACIN DERIVATIVE; HELIOFERIN DERIVATIVE; HOLOTRICIN 3; ITURIN A DERIVATIVE; LACTOFERRICIN; MAGAININ 2; MULUNDOCANDIN DERIVATIVE; NIKKOMYCIN; PEPTIDE; PNEUMOCANDIN DERIVATIVE; POLYOXIN D; PROTEGRIN DERIVATIVE; SCHIZOTRIN A; SYRINGOMYCIN; THANATIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; WF 11899; ZEAMATIN;

EID: 0032958766     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.43.1.1     Document Type: Short Survey
Times cited : (320)

References (192)
  • 1
    • 0029039625 scopus 로고
    • Evaluation of water-soluble pneumocandin analogs L-733560, L-705589, and L-731373 with mouse models of disseminated aspergillosis, candidiasis, and cryptococcosis
    • Abruzzo, G. K., A. M. Flattery, C. J. Gill, L. Long, J. G. Smith, D. Krupa, V. B. Pikounis, H. Kroop, and K. Bartizal. 1995. Evaluation of water-soluble pneumocandin analogs L-733560, L-705589, and L-731373 with mouse models of disseminated aspergillosis, candidiasis, and cryptococcosis. Antimiciob. Agents Chemother. 39:1077-1081.
    • (1995) Antimiciob. Agents Chemother. , vol.39 , pp. 1077-1081
    • Abruzzo, G.K.1    Flattery, A.M.2    Gill, C.J.3    Long, L.4    Smith, J.G.5    Krupa, D.6    Pikounis, V.B.7    Kroop, H.8    Bartizal, K.9
  • 4
    • 0342445179 scopus 로고    scopus 로고
    • Efficacy of domain III peptide from bactericidal/permeability-increasing protein (BPI) in murine disseminated aspergillosis
    • abstr. B-16, American Society for Microbiology, Washington, D.C.
    • Ammons, S., K. Aardalen, S. Froebel, and R. Little. 1997. Efficacy of domain III peptide from bactericidal/permeability-increasing protein (BPI) in murine disseminated aspergillosis. abstr. B-16, p. 29. In Program and abstracts of the 37th Interscience Conference on Antimicrobial Agents and Chemotherapy. American Society for Microbiology, Washington, D.C.
    • (1997) Program and Abstracts of the 37th Interscience Conference on Antimicrobial Agents and Chemotherapy , pp. 29
    • Ammons, S.1    Aardalen, K.2    Froebel, S.3    Little, R.4
  • 6
    • 0015603328 scopus 로고
    • A new antibiotic, leucinostatin, derived from Penicillium lilacinum
    • Arai, T., Y. Mikami, T. Fukushima, T. Utsumi, and K. Yazawa. 1973. A new antibiotic, leucinostatin, derived from Penicillium lilacinum. J. Antibiot. 26:1606-1612.
    • (1973) J. Antibiot. , vol.26 , pp. 1606-1612
    • Arai, T.1    Mikami, Y.2    Fukushima, T.3    Utsumi, T.4    Yazawa, K.5
  • 8
    • 0018497379 scopus 로고
    • Papulacandin B: An inhibitor of glucan synthesis in yeast spheroplasts
    • Baguley, B. C., G. Rommele, J. Gruner, and W. Wehrlli. 1979. Papulacandin B: an inhibitor of glucan synthesis in yeast spheroplasts. Eur. J. Biochem. 97:345-351.
    • (1979) Eur. J. Biochem. , vol.97 , pp. 345-351
    • Baguley, B.C.1    Rommele, G.2    Gruner, J.3    Wehrlli, W.4
  • 12
    • 0029031373 scopus 로고
    • In vitro evaluation of the pneumocandin antifungal agent L-733560, a new water-soluble hybrid of L-705589 and L-731,373
    • Bartizal, K., T. Scott, G. K. Abnizzo, C. J. Gill, C. Pacholok, L. Lynch, and H. Kropp. 1995. In vitro evaluation of the pneumocandin antifungal agent L-733560, a new water-soluble hybrid of L-705589 and L-731,373. Antimicrob. Agents Chemother. 39:1070-1076.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1070-1076
    • Bartizal, K.1    Scott, T.2    Abruzzo, G.K.3    Gill, C.J.4    Pacholok, C.5    Lynch, L.6    Kropp, H.7
  • 13
    • 0027538146 scopus 로고
    • Correlation of cilofungin in vivo efficacy with its activity against Aspergillus fumigatus (1,3)-β-D-glucan synthase
    • Beaulieu, D. J. Tang, D. J. Zeckner, and T. R. Parr. 1993. Correlation of cilofungin in vivo efficacy with its activity against Aspergillus fumigatus (1,3)-β-D-glucan synthase. FEMS Microbiol. Lett. 108:133-138.
    • (1993) FEMS Microbiol. Lett. , vol.108 , pp. 133-138
    • Beaulieu1    Tang, D.J.2    Zeckner, D.J.3    Parr, T.R.4
  • 15
  • 18
    • 0000693569 scopus 로고
    • Echinocandin B, ein neuartiges polypetid antibioticum aus Aspergillus nidulans var echinlatus: Isolierung and baudsteine
    • Benz, F., F. Knuesel, J. Nuesch, H. Treicher, W. Voser, R. Nyfeler, and W. Keller-Schlerein. 1985. Echinocandin B, ein neuartiges Polypetid Antibioticum aus Aspergillus nidulans var echinlatus: Isolierung and Baudsteine. Helv. Chim. Acta 57:2459-2477.
    • (1985) Helv. Chim. Acta , vol.57 , pp. 2459-2477
    • Benz, F.1    Knuesel, F.2    Nuesch, J.3    Treicher, H.4    Voser, W.5    Nyfeler, R.6    Keller-Schlerein, W.7
  • 19
    • 0021357716 scopus 로고
    • Action of antifungal peptolipids from Bacillus subtilis on the cell membrane of Saccharomyces cerevisiae
    • Besson, F., M. Peypoux, J. Quentin, and G. Michel. 1984. Action of antifungal peptolipids from Bacillus subtilis on the cell membrane of Saccharomyces cerevisiae. J. Antibiot. 37:172-177.
    • (1984) J. Antibiot. , vol.37 , pp. 172-177
    • Besson, F.1    Peypoux, M.2    Quentin, J.3    Michel, G.4
  • 20
    • 77049287584 scopus 로고
    • Essais de traitement de dermatomycoses par l'iturine
    • Bloquiaux, S., and L. Delcambre. 1956. Essais de traitement de dermatomycoses par l'iturine. Arch. Belg. Derm. Syph. 12:224.
    • (1956) Arch. Belg. Derm. Syph. , vol.12 , pp. 224
    • Bloquiaux, S.1    Delcambre, L.2
  • 22
    • 0026673854 scopus 로고
    • Isolation and characterization of a 25 kDa antifungal protein from flax seeds
    • Borgmeyer, J. R., C. E. Smith, and Q. Khai Hutnk. 1992. Isolation and characterization of a 25 kDa antifungal protein from flax seeds. Biochem. Biophys. Res. Commun. 187:480-487.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 480-487
    • Borgmeyer, J.R.1    Smith, C.E.2    Khai Hutnk, Q.3
  • 24
    • 0027395308 scopus 로고
    • Solution structure of γ-1-P thionins from barley and wheat endosperm determined by 1H-NMR: A structural motif common to toxic arthropod proteins
    • Bruix, M., M. A. Jimenez, J. Santora, C. Gonzales, F. J. Colilla, E. Mendez, and M. Rico. 1993. Solution structure of γ-1-P thionins from barley and wheat endosperm determined by 1H-NMR: a structural motif common to toxic arthropod proteins. Biochemistry 132:715-724.
    • (1993) Biochemistry , vol.132 , pp. 715-724
    • Bruix, M.1    Jimenez, M.A.2    Santora, J.3    Gonzales, C.4    Colilla, F.J.5    Mendez, E.6    Rico, M.7
  • 25
    • 0019640696 scopus 로고
    • The significance of iron in infection
    • Bullen, J. J. 1981. The significance of iron in infection. Rev. Infect. Dis. 3:1127-1138.
    • (1981) Rev. Infect. Dis. , vol.3 , pp. 1127-1138
    • Bullen, J.J.1
  • 27
    • 0026699702 scopus 로고
    • Chitin biosynthesis in Candida albicans grown in vitro and in vivo and its inhibition by nikkomycin Z
    • Chapman, T., O. Kinsman, and J. Houston. 1992. Chitin biosynthesis in Candida albicans grown in vitro and in vivo and its inhibition by nikkomycin Z. Antimicrob. Agents Chemother. 36:1909-1914.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 1909-1914
    • Chapman, T.1    Kinsman, O.2    Houston, J.3
  • 28
    • 0023735907 scopus 로고
    • Synthetic magainin analogues with improved antimicrobial activity
    • Chen, H.-C., J. H. Boman, J. L. Morell, and C. M. Huang. 1988. Synthetic magainin analogues with improved antimicrobial activity. FEBS Lett. 236: 462-466.
    • (1988) FEBS Lett. , vol.236 , pp. 462-466
    • Chen, H.-C.1    Boman, J.H.2    Morell, J.L.3    Huang, C.M.4
  • 29
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • Christensen, B., J. Fink, R. B. Merrifield, and D. Mauzerall. 1988. Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc. Natl. Acad. Sci. USA 85:5072-5076.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 30
    • 0141622068 scopus 로고
    • A propos d'essais cliniques et biologiques sur l'iturine, antifongique noveau
    • Clairbois, J. P., and L. Delcambre. 1958. A propos d'essais cliniques et biologiques sur l'iturine, antifongique noveau. Arch. Belg. Derm. Syph. 14:63.
    • (1958) Arch. Belg. Derm. Syph. , vol.14 , pp. 63
    • Clairbois, J.P.1    Delcambre, L.2
  • 31
    • 0027249384 scopus 로고
    • Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus
    • Cociancich, S., A. Ghazi, A. Hetru, J. A. Hoffman, and L. Letellier. 1993. Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus. J. Biol. Chem. 260:19239-19245.
    • (1993) J. Biol. Chem. , vol.260 , pp. 19239-19245
    • Cociancich, S.1    Ghazi, A.2    Hetru, A.3    Hoffman, J.A.4    Letellier, L.5
  • 32
    • 0024519380 scopus 로고
    • Synthesis of new analogs of echinocandin B by enzymatic deacylation and chemical reacylation of the echinocandin B peptide: Synthesis of the antifungal agent cilofungin (LY121019)
    • Debono, M., B. J. Abbott, D. Fukuda, M. Barnhart, K. E. Willard, R. M. Molloy, K. H. Michel, J. R. Turner, T. F. Bulter, and A. H. Hunt. 1989. Synthesis of new analogs of echinocandin B by enzymatic deacylation and chemical reacylation of the echinocandin B peptide: synthesis of the antifungal agent cilofungin (LY121019). J. Antibiot. 42:389-397.
    • (1989) J. Antibiot. , vol.42 , pp. 389-397
    • Debono, M.1    Abbott, B.J.2    Fukuda, D.3    Barnhart, M.4    Willard, K.E.5    Molloy, R.M.6    Michel, K.H.7    Turner, J.R.8    Bulter, T.F.9    Hunt, A.H.10
  • 34
    • 0028004384 scopus 로고
    • Antibiotics that inhibit fungal cell wall development
    • Debono, M., and R. S. Gordee. 1994. Antibiotics that inhibit fungal cell wall development. Annu. Rev. Microbiol. 48:471-497.
    • (1994) Annu. Rev. Microbiol. , vol.48 , pp. 471-497
    • Debono, M.1    Gordee, R.S.2
  • 35
    • 0030854825 scopus 로고    scopus 로고
    • In vitro antifungal activity of pneumocandin L-743,872 against a variety of clinically important molds
    • Del Porta, M., W. A. Schell, and J. R. Perfect 1997. In vitro antifungal activity of pneumocandin L-743,872 against a variety of clinically important molds. Antimicrob. Agents Chemother. 41:1835-1836.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1835-1836
    • Del Porta, M.1    Schell, W.A.2    Perfect, J.R.3
  • 38
    • 0031646792 scopus 로고    scopus 로고
    • Fungicidal and binding properties of the natural peptides cecropin B and dermaseptin
    • De Lucca, A. J., J. M. Bland, T. J. Jacks, C. Grimm, and T. J. Walsh. 1998. Fungicidal and binding properties of the natural peptides cecropin B and dermaseptin. Med. Mycol. 36:291-298.
    • (1998) Med. Mycol. , vol.36 , pp. 291-298
    • De Lucca, A.J.1    Bland, J.M.2    Jacks, T.J.3    Grimm, C.4    Walsh, T.J.5
  • 40
    • 0025887095 scopus 로고
    • Effiicacy of cilofungin alone and in combination with amphotericin B in a murine model of disseminated aspergillosis
    • Denning, D. W., and D. A. Stephans. 1991. Effiicacy of cilofungin alone and in combination with amphotericin B in a murine model of disseminated aspergillosis. Antimicrob. Agents Chemother. 35:1329-1333.
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 1329-1333
    • Denning, D.W.1    Stephans, D.A.2
  • 41
    • 0025811874 scopus 로고
    • Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: Peptide isolation and cloning of cDNA
    • Diamond, G., M. Zasloff, H. Eck, M. Brasseur, W. L. Maloy, and C. L. Bevins. 1991. Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of cDNA. Proc. Natl. Acad. Sci. USA 88:3952-3956.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3952-3956
    • Diamond, G.1    Zasloff, M.2    Eck, H.3    Brasseur, M.4    Maloy, W.L.5    Bevins, C.L.6
  • 42
    • 0024319808 scopus 로고
    • Purification and antimicrobial properties of three defensins from rat neutrophils
    • Eisenhauer, P., S. Harwig, D. Szlarek, T. Ganz, M. Selsted, and R. Lehrer. 1989. Purification and antimicrobial properties of three defensins from rat neutrophils. Infect. Immun. 57:2021-2027.
    • (1989) Infect. Immun. , vol.57 , pp. 2021-2027
    • Eisenhauer, P.1    Harwig, S.2    Szlarek, D.3    Ganz, T.4    Selsted, M.5    Lehrer, R.6
  • 43
    • 0027162586 scopus 로고    scopus 로고
    • The bactericidal/permiability-increasing protein (BPI), a potent element in host-defense against gram-negative bacteria and lipopolysaccharide
    • Elsbach, P., and J. Weiss. 1997. The bactericidal/permiability-increasing protein (BPI), a potent element in host-defense against gram-negative bacteria and lipopolysaccharide. Immunobiology 187:417-429.
    • (1997) Immunobiology , vol.187 , pp. 417-429
    • Elsbach, P.1    Weiss, J.2
  • 44
    • 0031028654 scopus 로고    scopus 로고
    • Fungicidal action of aureobasidin A, a cyclic depsipeptide antifungal antibiotic, against Saccharomyces cerevisiae
    • Endo, M., K. Takesako, I. Kato, and H. Yamaguchi. 1997. Fungicidal action of aureobasidin A, a cyclic depsipeptide antifungal antibiotic, against Saccharomyces cerevisiae. Antimicrob. Agents Chemother. 41:672-676.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 672-676
    • Endo, M.1    Takesako, K.2    Kato, I.3    Yamaguchi, H.4
  • 45
    • 0030295028 scopus 로고    scopus 로고
    • Antifungal dynamics of LY 303366, an investigational echinocandin B analog, against Candida spp.
    • Ernst, M. E., M. E. Klepser, E. J. Wolfe, and M. A. Pfaller. 1996. Antifungal dynamics of LY 303366, an investigational echinocandin B analog, against Candida spp. Diagn. Microbiol. Infect. Dis. 26:125-131.
    • (1996) Diagn. Microbiol. Infect. Dis. , vol.26 , pp. 125-131
    • Ernst, M.E.1    Klepser, M.E.2    Wolfe, E.J.3    Pfaller, M.A.4
  • 46
    • 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., P. Bulet, S. Chernych, J.-P. Briand, J. P. Roussel, L. Letellier, C. Hetru, and J. A. Hoffmman. 1996. Structure-activity analysis of thanatin, a 21 -residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proc. Natl. Acad. Sci. USA 93:1221-1225.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1221-1225
    • Fehlbaum, P.1    Bulet, P.2    Chernych, S.3    Briand, J.-P.4    Roussel, J.P.5    Letellier, L.6    Hetru, C.7    Hoffmman, J.A.8
  • 47
    • 0028587829 scopus 로고
    • Insect immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides
    • Fehlbaum, P., P. Bulet, L. Michaut, N. Laguex, W. F. Broekaert, C. Hetru, and J. A. Hoffmman. 1994. Insect immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides. J. Biol. Chem. 269:33159-33163.
    • (1994) J. Biol. Chem. , vol.269 , pp. 33159-33163
    • Fehlbaum, P.1    Bulet, P.2    Michaut, L.3    Laguex, N.4    Broekaert, W.F.5    Hetru, C.6    Hoffmman, J.A.7
  • 48
    • 0030030826 scopus 로고    scopus 로고
    • Properties of voltage-gated ion channels formed by syringomycin-E in planar lipid bilayers
    • Feign, A. M., J. Y. Takemoto, R. Wangspa, J. H. Teeter, and J. G. Brand. 1996. Properties of voltage-gated ion channels formed by syringomycin-E in planar lipid bilayers. J. Membr. Biol. 149:41-47.
    • (1996) J. Membr. Biol. , vol.149 , pp. 41-47
    • Feign, A.M.1    Takemoto, J.Y.2    Wangspa, R.3    Teeter, J.H.4    Brand, J.G.5
  • 49
    • 0031039601 scopus 로고    scopus 로고
    • Pneumocandin L-743,872 enhances the activities of amphotericin B and fluconazole against Cryptococcus neoformans in vitro
    • Franzot, S., and A. Casadevall. 1997. Pneumocandin L-743,872 enhances the activities of amphotericin B and fluconazole against Cryptococcus neoformans in vitro. Antimicrob. Agents Chemother. 41:331-336.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 331-336
    • Franzot, S.1    Casadevall, A.2
  • 50
    • 0024583621 scopus 로고
    • L-671,329, a new antifungal agent. III. In vitro activity, toxicology, and efficacy in comparison to aculeacin
    • Fromtling, R., and G. K. Abruzzo. 1989. L-671,329, a new antifungal agent. III. In vitro activity, toxicology, and efficacy in comparison to aculeacin. J. Antibiot. 42:174-178.
    • (1989) J. Antibiot. , vol.42 , pp. 174-178
    • Fromtling, R.1    Abruzzo, G.K.2
  • 53
    • 0021042205 scopus 로고
    • Studies on peptide antibiotics, leucinostatins. I. Separation, physico-chemical properties and biological activities of leucinostatins A and B
    • Fukushima, K., T. Arai, Y. Mori, M. Tsuboi, and M. Suzuki. 1983. Studies on peptide antibiotics, leucinostatins. I. Separation, physico-chemical properties and biological activities of leucinostatins A and B. J. Antibiot. 36: 1606-1612.
    • (1983) J. Antibiot. , vol.36 , pp. 1606-1612
    • Fukushima, K.1    Arai, T.2    Mori, Y.3    Tsuboi, M.4    Suzuki, M.5
  • 54
    • 0027178725 scopus 로고
    • Isolation and physico-chemical characterization of an antifungal and antibacterial peptide produced by Bacillus licheniformis A 12
    • Gàlvez, A., M. Maqueda, M. Martinez-Bueno, M. Lebbadi, and E. Valdivia. 1993. Isolation and physico-chemical characterization of an antifungal and antibacterial peptide produced by Bacillus licheniformis A 12. Appl. Microbiol. Biotechnol. 38:438-442.
    • (1993) Appl. Microbiol. Biotechnol. , vol.38 , pp. 438-442
    • Gàlvez, A.1    Maqueda, M.2    Martinez-Bueno, M.3    Lebbadi, M.4    Valdivia, E.5
  • 57
    • 0030033020 scopus 로고    scopus 로고
    • Antifungal agents: Chemotherapeutic targets and immunologic strategies
    • Georgopapadakou, N. H., and T. J. Walsh. 1996. Antifungal agents: chemotherapeutic targets and immunologic strategies. Antimicrob. Agents Chemother. 40:279-291.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 279-291
    • Georgopapadakou, N.H.1    Walsh, T.J.2
  • 58
    • 0026009980 scopus 로고
    • Human neutrophil peptide defensins induce single strand DNA breaks in target cells
    • Gera, J. F., and A. Lichenstein. 1991. Human neutrophil peptide defensins induce single strand DNA breaks in target cells. Cell. Immunol. 138:108-120.
    • (1991) Cell. Immunol. , vol.138 , pp. 108-120
    • Gera, J.F.1    Lichenstein, A.2
  • 59
    • 0021224331 scopus 로고
    • In vitro and in vivo anti-Candida activity and toxicology of LY121019
    • Gordee, R. S., D. J. Zeckner, L. F. Ellis, A. L. Thakker, and L. C. Howard. 1984. In vitro and in vivo anti-Candida activity and toxicology of LY121019. J. Antibiot. 37:1054-1065.
    • (1984) J. Antibiot. , vol.37 , pp. 1054-1065
    • Gordee, R.S.1    Zeckner, D.J.2    Ellis, L.F.3    Thakker, A.L.4    Howard, L.C.5
  • 60
    • 0024155609 scopus 로고
    • Anti-Candida activity and toxicology of LY121019, a novel polypeptide antifungal antibiotic
    • Gardee, R. S., D. J. Zeckner, L. C. Howard, W. E. Alborn, Jr., and M. Debono. 1988. Anti-Candida activity and toxicology of LY121019, a novel polypeptide antifungal antibiotic. Ann. N. Y. Acad. Sci. 544:294-301.
    • (1988) Ann. N. Y. Acad. Sci. , vol.544 , pp. 294-301
    • Gardee, R.S.1    Zeckner, D.J.2    Howard, L.C.3    Alborn W.E., Jr.4    Debono, M.5
  • 61
    • 0026215455 scopus 로고
    • Adhesion of Candida albicans to epithelial cells effect of polyoxin D
    • Gottlieb, S., Z. Altboum, D. C. Savage, and E. Segal. 1991. Adhesion of Candida albicans to epithelial cells effect of polyoxin D. Mycopathology 115:197-216.
    • (1991) Mycopathology , vol.115 , pp. 197-216
    • Gottlieb, S.1    Altboum, Z.2    Savage, D.C.3    Segal, E.4
  • 64
    • 0017618472 scopus 로고
    • Papulacandin, a new antibiotic, active especially against yeasts
    • Gruner, J., and P. Traxler. 1977. Papulacandin, a new antibiotic, active especially against yeasts. Experientia 33:137.
    • (1977) Experientia , vol.33 , pp. 137
    • Gruner, J.1    Traxler, P.2
  • 65
    • 0345288055 scopus 로고    scopus 로고
    • The brucellacidal activity in transgenic mice expressing a synthetic cecropin-like peptide or in mice following exogenous peptide treatment
    • abstr. E-46, American Society for Microbiology, Washington, D.C.
    • Haggius, S. D., W. A. Reed, M. B. Fatemi, K. L. White, F. M. Enright, and P. H. Elzer. 1996. The brucellacidal activity in transgenic mice expressing a synthetic cecropin-like peptide or in mice following exogenous peptide treatment, abstr. E-46, p. 274. In Abstracts of the 96th General Meeting of the American Society for Microbiology 1996. American Society for Microbiology, Washington, D.C.
    • (1996) Abstracts of the 96th General Meeting of the American Society for Microbiology 1996 , pp. 274
    • Haggius, S.D.1    Reed, W.A.2    Fatemi, M.B.3    White, K.L.4    Enright, F.M.5    Elzer, P.H.6
  • 67
    • 4243473094 scopus 로고
    • Structure-function relationships of antimicrobial dermaseptins
    • H. L. S. Maia (ed.). Escom, Leiden, The Netherlands
    • Hani, K., P. Nicolas, and A. Mor. 1994. Structure-function relationships of antimicrobial dermaseptins, p. 47-49. In H. L. S. Maia (ed.). Proceedings of the 23rd European Peptide Symposium. Escom, Leiden, The Netherlands.
    • (1994) Proceedings of the 23rd European Peptide Symposium , pp. 47-49
    • Hani, K.1    Nicolas, P.2    Mor, A.3
  • 68
    • 0026320088 scopus 로고
    • Pseudomycins, a family of novel peptides from Pseudomonas syringae possing broad-spectrum antifungal activity
    • Harrison, L., D. B. Teplow, M. Rinaldi, and G. Strobel. 1991. Pseudomycins, a family of novel peptides from Pseudomonas syringae possing broad-spectrum antifungal activity. J. Gen. Microbiol. 137:2857-2865.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2857-2865
    • Harrison, L.1    Teplow, D.B.2    Rinaldi, M.3    Strobel, G.4
  • 70
    • 0029295070 scopus 로고
    • Determination of disulfide bridges in PG-2, an antimicrobial peptide from porcine leukocytes
    • Harwig, S. S. L., K. M. Swiderek, T. D. Lee, and R. I. Lehrer. 1995. Determination of disulfide bridges in PG-2, an antimicrobial peptide from porcine leukocytes. J. Pept. Res. 3:207-215.
    • (1995) J. Pept. Res. , vol.3 , pp. 207-215
    • Harwig, S.S.L.1    Swiderek, K.M.2    Lee, T.D.3    Lehrer, R.I.4
  • 71
    • 0029831079 scopus 로고    scopus 로고
    • Intramolecular disulfide bonds enhance the antimicrobial and lytic activities of protegrins at physiological sodium chloride concentrations
    • Harwig, S. S. L., L. A. Waring, H. J. Yang, Y. Cho, L. Tan, and R. I. Lehrer. 1996. Intramolecular disulfide bonds enhance the antimicrobial and lytic activities of protegrins at physiological sodium chloride concentrations. Eur. J. Biochem. 240:352-357.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 352-357
    • Harwig, S.S.L.1    Waring, L.A.2    Yang, H.J.3    Cho, Y.4    Tan, L.5    Lehrer, R.I.6
  • 72
    • 0026773163 scopus 로고
    • Positive interaction of nikkomycins and azoles against Candida albicans in vitro and in vivo
    • Hector, R. F., and K. Schaller. 1992. Positive interaction of nikkomycins and azoles against Candida albicans in vitro and in vivo. Antimicrob. Agents Chemother. 36:1284-1289.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 1284-1289
    • Hector, R.F.1    Schaller, K.2
  • 73
    • 0025355568 scopus 로고
    • Evaluation of nikkomycins X and Z in murine models of coccodomycosis, histoplasmosis, and blastomycosis
    • Hector, R. F., B. L. Zimmer, and D. Pappagianis. 1990. Evaluation of nikkomycins X and Z in murine models of coccodomycosis, histoplasmosis, and blastomycosis. Antimicrob. Agents Chemother. 34:587-593.
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 587-593
    • Hector, R.F.1    Zimmer, B.L.2    Pappagianis, D.3
  • 74
    • 0141902801 scopus 로고
    • Inhibition of cell wall synthesis: Nikkomycins
    • H. Yamaguchi, G. S. Kobayashi, and H. Takahish (ed.), Marcel Dekker, Inc., New York, N.Y.
    • Hector, R. F., B. L. Zimmer, and D. Pappagianis. 1991. Inhibition of cell wall synthesis: nikkomycins, p. 341-353. In H. Yamaguchi, G. S. Kobayashi, and H. Takahish (ed.), Recent progress in antifungal chemotherapy. Marcel Dekker, Inc., New York, N.Y.
    • (1991) Recent Progress in Antifungal Chemotherapy , pp. 341-353
    • Hector, R.F.1    Zimmer, B.L.2    Pappagianis, D.3
  • 76
    • 0016159750 scopus 로고
    • Studies of the mode of action of polyoxins. VI. Effect of polyoxin B on chitin synthesis in polyoxin-resistant strains of Alternaria kikuchiana
    • Hori, M., J. Eguchi, K. Kakiki, and T. Misato. 1974. Studies of the mode of action of polyoxins. VI. Effect of polyoxin B on chitin synthesis in polyoxin-resistant strains of Alternaria kikuchiana. J. Antibiot. 27:260-266.
    • (1974) J. Antibiot. , vol.27 , pp. 260-266
    • Hori, M.1    Eguchi, J.2    Kakiki, K.3    Misato, T.4
  • 77
    • 0016233882 scopus 로고
    • Interaction between polyoxin and active center of chitin synthetase
    • Hori, M., K. Kakiki, and T. Misato. 1974. Interaction between polyoxin and active center of chitin synthetase. Agric. Biol. Chem. 38:699-705.
    • (1974) Agric. Biol. Chem. , vol.38 , pp. 699-705
    • Hori, M.1    Kakiki, K.2    Misato, T.3
  • 78
    • 0344425014 scopus 로고    scopus 로고
    • Fungicidal properties from bactericidal/permiability-increasing protein (BPI) act synergistically with fluconazole on a variety of Candida strains
    • abstr. F-102, American Society of Microbiology, Washington, D.C.
    • Horwitz, A., P. Motchink, and R. Nadell. 1997. Fungicidal properties from bactericidal/permiability-increasing protein (BPI) act synergistically with fluconazole on a variety of Candida strains, abstr. F-102, p. 163. In Abstracts of the 37th Interscience Conference on Antimicrobial Agents and Chemotherapy. American Society of Microbiology, Washington, D.C.
    • (1997) Abstracts of the 37th Interscience Conference on Antimicrobial Agents and Chemotherapy , pp. 163
    • Horwitz, A.1    Motchink, P.2    Nadell, R.3
  • 79
    • 0027157001 scopus 로고
    • Purification, characterization, and cDNA cloning of an antifungal protein from the hemolymph of Sarcophaga peregina (flesh fly) larvae
    • Iijima, R., S. Kurata, and S. Natori. 1993. Purification, characterization, and cDNA cloning of an antifungal protein from the hemolymph of Sarcophaga peregina (flesh fly) larvae. J. Biol. Chem. 268:12055-12061.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12055-12061
    • Iijima, R.1    Kurata, S.2    Natori, S.3
  • 82
    • 0019208843 scopus 로고
    • Constituents of a peptidal antibiotic P168 produced by Paecilomyces lilacinus (Thom) Samson
    • Isogai, A., A. Suzuki, S. Higashikawa, S. Kuyama, and S. Tamura. 1980. Constituents of a peptidal antibiotic P168 produced by Paecilomyces lilacinus (Thom) Samson. Agric. Biol. Chem. 44:3029-3031.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 3029-3031
    • Isogai, A.1    Suzuki, A.2    Higashikawa, S.3    Kuyama, S.4    Tamura, S.5
  • 83
    • 0019119118 scopus 로고
    • Structure of peptidal antibiotic P168 produced by Paecilomyces lilacinus (Thom) Samson
    • Isogai, A., A. Suzuki, S. Higashikawa, S. Kuyama, and S. Tamura. 1980. Structure of peptidal antibiotic P168 produced by Paecilomyces lilacinus (Thom) Samson. Agric. Biol. Chem. 44:3033-3035.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 3033-3035
    • Isogai, A.1    Suzuki, A.2    Higashikawa, S.3    Kuyama, S.4    Tamura, S.5
  • 84
    • 0014682610 scopus 로고
    • Studies on polyoxins, antifungal antibiotics. XIII. The structure of polyoxins
    • Isono, K., K. Asahi, and S. Suzuki. 1969. Studies on polyoxins, antifungal antibiotics. XIII. The structure of polyoxins. J. Am. Chem. Soc. 91:7490-7505.
    • (1969) J. Am. Chem. Soc. , vol.91 , pp. 7490-7505
    • Isono, K.1    Asahi, K.2    Suzuki, S.3
  • 85
    • 0028148187 scopus 로고
    • WF11899A, B, and C novel antifungal lipopeptides. II. Biological properties
    • Iwamoto, T., A. Fuji, K. Nitta, S. Hashimoto, M. Okuhara, and M. Kohsaka. 1994. WF11899A, B, and C novel antifungal lipopeptides. II. Biological properties. J. Antibiot. 47:1092-1097.
    • (1994) J. Antibiot. , vol.47 , pp. 1092-1097
    • Iwamoto, T.1    Fuji, A.2    Nitta, K.3    Hashimoto, S.4    Okuhara, M.5    Kohsaka, M.6
  • 88
    • 0026250065 scopus 로고
    • Inhibition of some mycotoxigenic fungi by iturin A, a peptidolipid produced by Bacillus subtilis
    • Klich, M. A., A. R. Lax, and J. M. Bland. 1991. Inhibition of some mycotoxigenic fungi by iturin A, a peptidolipid produced by Bacillus subtilis. Mycotpathology 116:77-80.
    • (1991) Mycotpathology , vol.116 , pp. 77-80
    • Klich, M.A.1    Lax, A.R.2    Bland, J.M.3
  • 90
    • 0030779919 scopus 로고    scopus 로고
    • Comparison of the in vitro activities of the echinocadin LY303366, the pneumocandin MK-0991, and fluconazole against Candida species and Cryptococcus neoformans
    • Krishnarao, T. V., and J. N. Galgiani. 1997. Comparison of the in vitro activities of the echinocadin LY303366, the pneumocandin MK-0991, and fluconazole against Candida species and Cryptococcus neoformans. Antimicrob. Agents Chemother. 41:1957-1960.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1957-1960
    • Krishnarao, T.V.1    Galgiani, J.N.2
  • 93
    • 0030943354 scopus 로고    scopus 로고
    • Lipopeptide inhibitors of fungal glucan synthase
    • Kurtz, M. B., and C. M. Douglas. 1997. Lipopeptide inhibitors of fungal glucan synthase. J. Med. Vet. Mycol. 35:79-86.
    • (1997) J. Med. Vet. Mycol. , vol.35 , pp. 79-86
    • Kurtz, M.B.1    Douglas, C.M.2
  • 94
    • 84957790649 scopus 로고
    • Bacillomycin, an antibiotic from Bacillus subtilis active against pathogenic fungi
    • Landy, M., G. H. Warren, S. B. Roseman, and L. G. Colio. 1948. Bacillomycin, an antibiotic from Bacillus subtilis active against pathogenic fungi. Proc. Soc. Exp. Biol. Med. 67:539-541.
    • (1948) Proc. Soc. Exp. Biol. Med. , vol.67 , pp. 539-541
    • Landy, M.1    Warren, G.H.2    Roseman, S.B.3    Colio, L.G.4
  • 95
    • 0023202994 scopus 로고
    • Action of iturin A, an antifungal antibiotic from Bacillus subtilis on the yeast Saccharomyces cerevisiae. Modification of membrane permeability and lipid composition
    • Latoud, C., F. Peypoux, and G. Michel. 1987. Action of iturin A, an antifungal antibiotic from Bacillus subtilis on the yeast Saccharomyces cerevisiae. Modification of membrane permeability and lipid composition. J. Antibiot. 40:1588-1595.
    • (1987) J. Antibiot. , vol.40 , pp. 1588-1595
    • Latoud, C.1    Peypoux, F.2    Michel, G.3
  • 96
  • 97
    • 0030586288 scopus 로고    scopus 로고
    • Antimicrobial activity of a 13-amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides
    • Lawyer, C., S. Pai, M. Watebe, P. Borgia, T. Mashimo, L. Eagleton, and K. Watebe. 1996. Antimicrobial activity of a 13-amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides. FEBS Lett. 390:95-98.
    • (1996) FEBS Lett. , vol.390 , pp. 95-98
    • Lawyer, C.1    Pai, S.2    Watebe, M.3    Borgia, P.4    Mashimo, T.5    Eagleton, L.6    Watebe, K.7
  • 100
    • 0028608912 scopus 로고
    • Cepacidine A, a novel antifungal antibiotic produced by Pseudomonas cepacia. I. Taxonomy, production, isolation, and biological activity
    • Lee, C. H-, S. H. Kim, B. C. Hyun, J. W. Suh, C. Yon, C. O. Kim, Y. A. Lim, and C. S. Kim. 1994. Cepacidine A, a novel antifungal antibiotic produced by Pseudomonas cepacia. I. Taxonomy, production, isolation, and biological activity. J. Antibiot. 47:1402-1405.
    • (1994) J. Antibiot. , vol.47 , pp. 1402-1405
    • Lee, C.H.-.1    Kim, S.H.2    Hyun, B.C.3    Suh, J.W.4    Yon, C.5    Kim, C.O.6    Lim, Y.A.7    Kim, C.S.8
  • 101
    • 0029093121 scopus 로고
    • Purification and cDNA cloning of an antifungal protein from the hemolymph of Holotrichia diomphalia larvae
    • Lee, S. Y., H.-J. Moon, S. Kurata, S. Natori, and B. L. Lee. 1995. Purification and cDNA cloning of an antifungal protein from the hemolymph of Holotrichia diomphalia larvae. Biol. Pharm. Bull. 18:1049-1052.
    • (1995) Biol. Pharm. Bull. , vol.18 , pp. 1049-1052
    • Lee, S.Y.1    Moon, H.-J.2    Kurata, S.3    Natori, S.4    Lee, B.L.5
  • 103
    • 0023945703 scopus 로고
    • Modulation of the in situ candidacidal activity of human neutrophil defensins by target cell metabolism and divalent cations
    • Lehrer, R. I., T. Ganz, D. Szklarek, and M. E. Selsted. 1988. Modulation of the in situ candidacidal activity of human neutrophil defensins by target cell metabolism and divalent cations. J. Clin. Invest. 81:1829-1835.
    • (1988) J. Clin. Invest. , vol.81 , pp. 1829-1835
    • Lehrer, R.I.1    Ganz, T.2    Szklarek, D.3    Selsted, M.E.4
  • 104
    • 0027474382 scopus 로고
    • Defensins: Antimicrobial and cytotoxic peptides of mammalian cells
    • Lehrer, R. I., A. K. Lichtenstein, and T. Ganz. 1993. Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu. Rev. Immunol. 11:105-128.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 105-128
    • Lehrer, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 105
    • 0021847049 scopus 로고
    • Correlation of binding of rabbit granulocyte peptides to Candida albicans with candidacidal activity
    • Lehrer, R. I., D. Szklarek, T. Ganz, and M. E. Selsted. 1985. Correlation of binding of rabbit granulocyte peptides to Candida albicans with candidacidal activity. Infect. Immun. 49:207-211.
    • (1985) Infect. Immun. , vol.49 , pp. 207-211
    • Lehrer, R.I.1    Szklarek, D.2    Ganz, T.3    Selsted, M.E.4
  • 106
    • 0022617491 scopus 로고
    • Synergistic activity of rabbit granulocyte peptides against Candida albicans
    • Lehrer, R. I., D. Szklarek, T. Ganz, and M. E. Selsted. 1986. Synergistic activity of rabbit granulocyte peptides against Candida albicans. Infect. Immun. 52:902-904.
    • (1986) Infect. Immun. , vol.52 , pp. 902-904
    • Lehrer, R.I.1    Szklarek, D.2    Ganz, T.3    Selsted, M.E.4
  • 107
    • 0022529445 scopus 로고
    • In vitro killing of spores and hyphae of Aspergillus fumigatus and Rhizopus oryzae by rabbit neutrophil cationic peptides and bronchoalveolar macrophages
    • Levitz, S. M., M. E. Selsted, T. Ganz, R. I. Lehrer, and R. D. Diamond. 1986. In vitro killing of spores and hyphae of Aspergillus fumigatus and Rhizopus oryzae by rabbit neutrophil cationic peptides and bronchoalveolar macrophages. J. Infect. Dis. 154:483-489.
    • (1986) J. Infect. Dis. , vol.154 , pp. 483-489
    • Levitz, S.M.1    Selsted, M.E.2    Ganz, T.3    Lehrer, R.I.4    Diamond, R.D.5
  • 108
    • 0027466916 scopus 로고
    • Antibacterial 15-kDa isoforms (p15s) are members of a novel family of leukocyte proteins
    • Levy, O., J. Weiss, K. Zarember, C. E. Ooi, and P. Elsbach. 1993. Antibacterial 15-kDa isoforms (p15s) are members of a novel family of leukocyte proteins. J. Biol. Chem. 268:6058-6063.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6058-6063
    • Levy, O.1    Weiss, J.2    Zarember, K.3    Ooi, C.E.4    Elsbach, P.5
  • 110
    • 0028577142 scopus 로고
    • Cepacidine A, a novel antifungal antibiotic produced by Pseudomonas cepacia. II. Physico-chemical properties and structure elucidation
    • Lim, Y., J.-W. Suh, S. Kim, B. Hyun, C. Kim, and C. H. Lee. 1994. Cepacidine A, a novel antifungal antibiotic produced by Pseudomonas cepacia. II. Physico-chemical properties and structure elucidation. J. Antibiot. 47:1406-1416.
    • (1994) J. Antibiot. , vol.47 , pp. 1406-1416
    • Lim, Y.1    Suh, J.-W.2    Kim, S.3    Hyun, B.4    Kim, C.5    Lee, C.H.6
  • 113
    • 0029866830 scopus 로고    scopus 로고
    • In vitro activities of semisynthetic pneumocandin L-733,560 against fluconazole-resistant and -susceptible Candida albicans isolates
    • Martinez-Suarez, J. V., and J. L. Rodriguez-Tudela. 1996. In vitro activities of semisynthetic pneumocandin L-733,560 against fluconazole-resistant and -susceptible Candida albicans isolates. Antimicrob. Agents Chemother. 40: 1277-1279.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 1277-1279
    • Martinez-Suarez, J.V.1    Rodriguez-Tudela, J.L.2
  • 115
    • 0021798992 scopus 로고
    • Mechanism of action of nikkomycin and the peptide transport system of Candida albicans
    • McCarthy, P. J., P. F. Troke, and K. Gull. 1985. Mechanism of action of nikkomycin and the peptide transport system of Candida albicans. J. Gen. Microbiol. 131:775-780.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 775-780
    • McCarthy, P.J.1    Troke, P.F.2    Gull, K.3
  • 116
    • 0343168359 scopus 로고    scopus 로고
    • May 21, Merck & Co., White House Station, N.J.
    • Merck & Co. May 21,1996. Press release, business wire. Data on file. Merck & Co., White House Station, N.J.
    • (1996) Press Release, Business Wire. Data on File
  • 117
    • 0020326776 scopus 로고
    • Bacillomycin F, a new antibiotic of iturin group. Isolation and characterization
    • Mhammedi, A., F. Peypoux, F. Besson, and G. Michel. 1982. Bacillomycin F, a new antibiotic of iturin group. Isolation and characterization. J. Antibiot 35:306-311.
    • (1982) J. Antibiot , vol.35 , pp. 306-311
    • Mhammedi, A.1    Peypoux, F.2    Besson, F.3    Michel, G.4
  • 118
    • 0030583613 scopus 로고    scopus 로고
    • Determination of the disulfide array of the first inducible antifungal peptide from insects: Drosomycin from Drosophila melanogaster
    • Michaut, L., P. Fehlbaum, M. Moniatte, A. Van Dorsselaer, J.-M. Rechart, and P. Bulet, 1996. Determination of the disulfide array of the first inducible antifungal peptide from insects: drosomycin from Drosophila melanogaster. FEBS Lett. 395:6-10.
    • (1996) FEBS Lett. , vol.395 , pp. 6-10
    • Michaut, L.1    Fehlbaum, P.2    Moniatte, M.3    Van Dorsselaer, A.4    Rechart, J.-M.5    Bulet, P.6
  • 119
    • 0017741051 scopus 로고
    • On the mode of action of a new antifungal antibiotic, aculeacin A: Inhibition of cell wall synthesis in Saccharomyces cerevisiae
    • Mizoguchi, J., T. Saito, K. Mizuno, and K. Hayano. 1977. On the mode of action of a new antifungal antibiotic, aculeacin A: inhibition of cell wall synthesis in Saccharomyces cerevisiae. J. Antibiot. 30:308-313.
    • (1977) J. Antibiot. , vol.30 , pp. 308-313
    • Mizoguchi, J.1    Saito, T.2    Mizuno, K.3    Hayano, K.4
  • 121
    • 0022552103 scopus 로고
    • Transport and hydrolysis of peptides in Saccharomyces cerevisiae
    • Moneton, P., P. Sarthow, and F. Le Gaffic. 1986. Transport and hydrolysis of peptides in Saccharomyces cerevisiae. J. Gen. Microbiol. 132:2147-2153.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 2147-2153
    • Moneton, P.1    Sarthow, P.2    Le Gaffic, F.3
  • 122
    • 0028504387 scopus 로고
    • Preliminary experimental anticancer activity of cecropins
    • Moore, A. J., D. A. Devine, and M. C. Bibby. 1994. Preliminary experimental anticancer activity of cecropins. Pept. Res. 7:265-269.
    • (1994) Pept. Res. , vol.7 , pp. 265-269
    • Moore, A.J.1    Devine, D.A.2    Bibby, M.C.3
  • 123
    • 0028240042 scopus 로고
    • Structure, synthesis, and activity of dermaseptin b, a novel vertebrate defensive peptide from frog skin: Relationship to adenoregulin
    • Mor, A., M. Amiche, and P. Nicolas. 1994. Structure, synthesis, and activity of dermaseptin b, a novel vertebrate defensive peptide from frog skin: relationship to adenoregulin. Biochemistry 33:6642-6650.
    • (1994) Biochemistry , vol.33 , pp. 6642-6650
    • Mor, A.1    Amiche, M.2    Nicolas, P.3
  • 124
    • 0027988532 scopus 로고
    • The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific organisms
    • Mor, A., K. Hani, and P. Nicolas. 1994. The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific organisms. J. Biol. Chem. 269:31635-31641.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31635-31641
    • Mor, A.1    Hani, K.2    Nicolas, P.3
  • 125
    • 0025787585 scopus 로고
    • Isolation, amino acid sequence of dermaseptin, a novel antimicrobial peptide of amphibian skin
    • Mar, A., V. H. Nguyen, A. Delfour, D. Migliore-Samour, and P. Nicolas. 1991. Isolation, amino acid sequence of dermaseptin, a novel antimicrobial peptide of amphibian skin. Biochemistry 30:8824-8830.
    • (1991) Biochemistry , vol.30 , pp. 8824-8830
    • Mar, A.1    Nguyen, V.H.2    Delfour, A.3    Migliore-Samour, D.4    Nicolas, P.5
  • 126
    • 0020594265 scopus 로고
    • Structure of leucinostatin B, an uncoupler on mitochondria
    • Mori, Y., M. Suzuki, K. Fukushima, and T. Arai. 1983. Structure of leucinostatin B, an uncoupler on mitochondria. J. Antibiot. 36:1084-1086.
    • (1983) J. Antibiot. , vol.36 , pp. 1084-1086
    • Mori, Y.1    Suzuki, M.2    Fukushima, K.3    Arai, T.4
  • 127
    • 0023099502 scopus 로고
    • Mulundocandin, a new lipopeptide antibiotic. II. Structure elucidation
    • Mukhopadhyay, T., and B. N. Ganguli. 1986. Mulundocandin, a new lipopeptide antibiotic. II. Structure elucidation. J. Antibiot. 40:281-289.
    • (1986) J. Antibiot. , vol.40 , pp. 281-289
    • Mukhopadhyay, T.1    Ganguli, B.N.2
  • 130
    • 0001134345 scopus 로고    scopus 로고
    • Purification and properties of a new chitin-binding antifungal CB-1 from Bacillus licheniformis M-4
    • Oita, S., M. Horita, and S, O. Yanagi. 1996. Purification and properties of a new chitin-binding antifungal CB-1 from Bacillus licheniformis M-4. Biosci. Biotech. Biochem. 60:481-483.
    • (1996) Biosci. Biotech. Biochem. , vol.60 , pp. 481-483
    • Oita, S.1    Horita, M.2    Yanagi, O.3
  • 132
    • 0025665084 scopus 로고
    • Biologically active cyclopeptide alkaloids from Rhamnaceae plants
    • Panday, V. B., and S. Devi. 1990. Biologically active cyclopeptide alkaloids from Rhamnaceae plants. Planta Med. 56:649-650.
    • (1990) Planta Med. , vol.56 , pp. 649-650
    • Panday, V.B.1    Devi, S.2
  • 133
    • 0019435655 scopus 로고
    • Microbicidal cationic proteins of rabbit alveolar macrophages: Amino acid composition and functional attributes
    • Patterson-Delafield, J., D. Szklarek, R. J. Martinez, and R. I. Lehrer. 1981. Microbicidal cationic proteins of rabbit alveolar macrophages: amino acid composition and functional attributes. Infect. Immun. 31:723-731.
    • (1981) Infect. Immun. , vol.31 , pp. 723-731
    • Patterson-Delafield, J.1    Szklarek, D.2    Martinez, R.J.3    Lehrer, R.I.4
  • 134
    • 0019413648 scopus 로고
    • Effect of papulacandin B and aculeacin A on beta-(1,3) glucan synthase from Geotrichum latis
    • Perez, P., R. Varona, I. Garcia-Acha, and A. Duran. 1981. Effect of papulacandin B and aculeacin A on beta-(1,3) glucan synthase from Geotrichum latis. FEBS Lett. 129:249-252.
    • (1981) FEBS Lett. , vol.129 , pp. 249-252
    • Perez, P.1    Varona, R.2    Garcia-Acha, I.3    Duran, A.4
  • 135
    • 0027973157 scopus 로고
    • Schizotrin A: Novel antimicrobial cyclic peptide from a cyanobacterium
    • Pergament, I., and S. Carmelli. 1994. Schizotrin A: novel antimicrobial cyclic peptide from a cyanobacterium. Tetrahedron Lett. 35:8473-8476.
    • (1994) Tetrahedron Lett. , vol.35 , pp. 8473-8476
    • Pergament, I.1    Carmelli, S.2
  • 136
    • 0015720499 scopus 로고
    • Isoelement de l'acide 3-amino 12-mèthyl tétradé-canöique à partir de l'iturine, antibiotique de Bacillus subtilis
    • Peypoux, F., M. Guinand, G. Michel, L. Delcambre, B. C. Das, P. Varenne, and E. Lederer. 1973. Isoelement de l'acide 3-amino 12-mèthyl tétradé-canöique à partir de l'iturine, antibiotique de Bacillus subtilis. Tetrahedron 29:3455-3459.
    • (1973) Tetrahedron , vol.29 , pp. 3455-3459
    • Peypoux, F.1    Guinand, M.2    Michel, G.3    Delcambre, L.4    Das, B.C.5    Varenne, P.6    Lederer, E.7
  • 137
    • 0024402637 scopus 로고
    • Fungicidal activity of cilofungin (LY121019) alone and in combination with anticapsin or other antifungal agents
    • Pfaller, M., R. Gordee, T. Gerarden, M. Yu, and R. Wenzel. 1989. Fungicidal activity of cilofungin (LY121019) alone and in combination with anticapsin or other antifungal agents. Eur. J. Clin. Microbiol. Infect. Dis. 8:564-567.
    • (1989) Eur. J. Clin. Microbiol. Infect. Dis. , vol.8 , pp. 564-567
    • Pfaller, M.1    Gordee, R.2    Gerarden, T.3    Yu, M.4    Wenzel, R.5
  • 138
    • 0030896916 scopus 로고    scopus 로고
    • In vitro susceptibilities of clinical yeast isolates to a new echinocandin derivative, LY303366, and other antifungal agents
    • Pfaller, M. A., S. A. Meisser, and S. Coffman. 1997. In vitro susceptibilities of clinical yeast isolates to a new echinocandin derivative, LY303366, and other antifungal agents. Antimicrob. Agents Chemother. 41:763-766.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 763-766
    • Pfaller, M.A.1    Meisser, S.A.2    Coffman, S.3
  • 139
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Pouny, Y., D. Rapaport, A. Mor, P. Nicolas, and Y. Shai. 1992. Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry 31:12416-12423.
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 140
    • 0023219621 scopus 로고
    • Leucinostatins H and K, two novel peptide antibiotics with tertiary amino-oxide terminal group from Paecilomyces marquandii. Isolation, structure and biological activity
    • Radics, L. M., M. Katjar-Perady, C. G. Casinovi, C. Rossi, M. Ricci, and L. Tuttobelo. 1987. Leucinostatins H and K, two novel peptide antibiotics with tertiary amino-oxide terminal group from Paecilomyces marquandii. Isolation, structure and biological activity. J. Antibiot. 40:714-716.
    • (1987) J. Antibiot. , vol.40 , pp. 714-716
    • Radics, L.M.1    Katjar-Perady, M.2    Casinovi, C.G.3    Rossi, C.4    Ricci, M.5    Tuttobelo, L.6
  • 141
    • 0031239636 scopus 로고    scopus 로고
    • Interleukin 2 promoter/enhancer controlled expression of a synthetic cecropin-class lytic peptide in transgenic mice and subsequent resistance to Brucella abortus
    • Reed, W. A., P. H. Elzer, F. M. Enright, J. M. Jaynes, J. D. Morrey, and K. L. White. 1997. Interleukin 2 promoter/enhancer controlled expression of a synthetic cecropin-class lytic peptide in transgenic mice and subsequent resistance to Brucella abortus. Transgenic Res. 6:337-347.
    • (1997) Transgenic Res. , vol.6 , pp. 337-347
    • Reed, W.A.1    Elzer, P.H.2    Enright, F.M.3    Jaynes, J.M.4    Morrey, J.D.5    White, K.L.6
  • 142
    • 0023151750 scopus 로고
    • Mechanism of action of bacterial phytotoxin, syringomycin. Simultaneous measurement of early responses in yeasts and maize
    • Reidl, H. H., and J. Y. Takemoto. 1987. Mechanism of action of bacterial phytotoxin, syringomycin. Simultaneous measurement of early responses in yeasts and maize. Biochim. Biophys. Acta 898:56-59.
    • (1987) Biochim. Biophys. Acta , vol.898 , pp. 56-59
    • Reidl, H.H.1    Takemoto, J.Y.2
  • 143
    • 0020528432 scopus 로고
    • The biological significance of lactoferrin
    • Reiter, B. 1983. The biological significance of lactoferrin. Int. J. Tissue React. 5:87-96.
    • (1983) Int. J. Tissue React. , vol.5 , pp. 87-96
    • Reiter, B.1
  • 144
    • 0025063227 scopus 로고
    • Zeamatin, an antifungal protein from maize with membrane-permeabilizing activity
    • Roberts, W. K., and C. P. Selitrennikoff. 1990. Zeamatin, an antifungal protein from maize with membrane-permeabilizing activity. J. Gen. Microbiol. 136:1771-1778.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 1771-1778
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 146
    • 0026512684 scopus 로고
    • Efficacy of cilofungin therapy administered by continuous intravenous infusion for experimental disseminated candidiasis in rabbits
    • Rouse, M. S., B. M. Tallan, J. M. Steckelberg, N. K. Henry, and W. R. Wilson. 1992. Efficacy of cilofungin therapy administered by continuous intravenous infusion for experimental disseminated candidiasis in rabbits. Antimicrob. Agents Chemother. 36:56-58.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 56-58
    • Rouse, M.S.1    Tallan, B.M.2    Steckelberg, J.M.3    Henry, N.K.4    Wilson, W.R.5
  • 147
    • 0023134763 scopus 로고
    • Mulundocandin, a new lipopeptide antibiotic. I. Taxonomy, fermentation, isolation, and characterization
    • Roy, K., T. Mukhopadyay, G. C. S. Reddy, K. R. Desikan, and B. N. Ganguli. 1986. Mulundocandin, a new lipopeptide antibiotic. I. Taxonomy, fermentation, isolation, and characterization. J. Antibiot. 40:275-280.
    • (1986) J. Antibiot. , vol.40 , pp. 275-280
    • Roy, K.1    Mukhopadyay, T.2    Reddy, G.C.S.3    Desikan, K.R.4    Ganguli, B.N.5
  • 148
    • 0019202149 scopus 로고
    • Properties and structure of a peptide antibiotic no. 1907
    • Sato, M., T. Beppu, and K. Arima. 1980. Properties and structure of a peptide antibiotic no. 1907. Agric. Biol. Chem. 44:3037-3040.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 3037-3040
    • Sato, M.1    Beppu, T.2    Arima, K.3
  • 149
    • 0017375773 scopus 로고
    • Studies of aculeacin. II. Isolation and characterization of aculeacins B, C, D, E, F. and G
    • Satoi, S., A. Yagi, K. Asano, K. Mizuno, and T. Watanabe. 1977. Studies of aculeacin. II. Isolation and characterization of aculeacins B, C, D, E, F. and G. J. Antibiot. 30:303-307.
    • (1977) J. Antibiot. , vol.30 , pp. 303-307
    • Satoi, S.1    Yagi, A.2    Asano, K.3    Mizuno, K.4    Watanabe, T.5
  • 150
    • 0021145336 scopus 로고
    • Echinocandin inhibition of (1,3)-beta-D-glucan synthase from Candida albicans
    • Sawistowska-Schroder, E. T., D. Kerridge, and H. Perry. 1984. Echinocandin inhibition of (1,3)-beta-D-glucan synthase from Candida albicans. FEBS Lett. 173:134-138.
    • (1984) FEBS Lett. , vol.173 , pp. 134-138
    • Sawistowska-Schroder, E.T.1    Kerridge, D.2    Perry, H.3
  • 153
    • 0021990744 scopus 로고
    • In vitro effect of phagocyte cationic peptides on Coccidioides immitis
    • Segal, G. P., R. I. Lehrer, and M. E. Selsted. 1985. In vitro effect of phagocyte cationic peptides on Coccidioides immitis. J. Infect. Dis. 151:890-894.
    • (1985) J. Infect. Dis. , vol.151 , pp. 890-894
    • Segal, G.P.1    Lehrer, R.I.2    Selsted, M.E.3
  • 155
    • 0023270758 scopus 로고
    • Purification, primary structure, and antimicrobial activities of a guinea pig neutrophil defensin
    • Selsted, M., and S. Harwig. 1987. Purification, primary structure, and antimicrobial activities of a guinea pig neutrophil defensin. Infect. Immun. 55:2281-2286.
    • (1987) Infect. Immun. , vol.55 , pp. 2281-2286
    • Selsted, M.1    Harwig, S.2
  • 157
    • 0021854511 scopus 로고
    • Activity of rabbit leukocyte peptides against Candida albicans
    • Selsted, M., D. Szklarek, T. Ganz, and R. Lehrer. 1985. Activity of rabbit leukocyte peptides against Candida albicans. Infect. Immun. 49:202-206.
    • (1985) Infect. Immun. , vol.49 , pp. 202-206
    • Selsted, M.1    Szklarek, D.2    Ganz, T.3    Lehrer, R.4
  • 158
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning polypeptides
    • Shai, Y. 1995. Molecular recognition between membrane-spanning polypeptides. TIBS 20:460-464.
    • (1995) TIBS , vol.20 , pp. 460-464
    • Shai, Y.1
  • 159
    • 0029808503 scopus 로고    scopus 로고
    • In vitro antifungal and fungicidal activities and erythrocyte toxicities of cyclic lipodepsinonapeptides produced by Pseudomonas syringae pv. syringae
    • Sorensen, K. N., K.-H. Kim, and J. Y. Takemoto. 1996. In vitro antifungal and fungicidal activities and erythrocyte toxicities of cyclic lipodepsinonapeptides produced by Pseudomonas syringae pv. syringae. Antimicrob. Agents Chemother. 40:2710-2713.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 2710-2713
    • Sorensen, K.N.1    Kim, K.-H.2    Takemoto, J.Y.3
  • 160
    • 0031690767 scopus 로고    scopus 로고
    • Efficacy of syringomycin e in a murine model of vaginal candidiasis
    • Sorensen, K. N., A. A. Wangstrom, S. D. Allen, and J. Y. Takemoto. 1998. Efficacy of syringomycin E in a murine model of vaginal candidiasis. J. Antibiot. 51:743-749.
    • (1998) J. Antibiot. , vol.51 , pp. 743-749
    • Sorensen, K.N.1    Wangstrom, A.A.2    Allen, S.D.3    Takemoto, J.Y.4
  • 161
    • 0023851437 scopus 로고
    • Comparitive in vitro activity of LY121019 and amphotericin B against isolates of Candida species
    • Spitzer, E. D., S. J. Travis, and G. S. Kobayashi. 1988. Comparitive in vitro activity of LY121019 and amphotericin B against isolates of Candida species. Eur. J. Clin. Microbiol. Infect. Dis. 7:80-81.
    • (1988) Eur. J. Clin. Microbiol. Infect. Dis. , vol.7 , pp. 80-81
    • Spitzer, E.D.1    Travis, S.J.2    Kobayashi, G.S.3
  • 162
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner, H., D. Hultmark, A. Engstrom, H. Bennich, and H. G. Boman. 1981. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292:246-248.
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 163
    • 0026448914 scopus 로고
    • DNA sequence of an antibiotic dodecapeptide from neutrophils
    • Storici, P., G. Del Sal, C. Schneider, and D. Romeo. 1992. cDNA sequence of an antibiotic dodecapeptide from neutrophils. FEBS Lett. 314:187-190.
    • (1992) FEBS Lett. , vol.314 , pp. 187-190
    • Storici, P.1    Del Sal, G.2    Schneider, C.3    Romeo, D.4
  • 165
    • 0023736454 scopus 로고
    • Cilofungin (LY121019) inhibits Candida albicans (1,3)-β-D-glucan synthase activity
    • Taft, C. S., T. Stark, and C. P. Selitrannikoff. 1988. Cilofungin (LY121019) inhibits Candida albicans (1,3)-β-D-glucan synthase activity. Antimicrob. Agents Chemother. 32:1901-1903.
    • (1988) Antimicrob. Agents Chemother. , vol.32 , pp. 1901-1903
    • Taft, C.S.1    Stark, T.2    Selitrannikoff, C.P.3
  • 168
    • 0027376332 scopus 로고
    • Yeast genes involved in growth inhibition by Pseudomonas syringae pv. syringae syringomycin family lipodepsipeptides
    • Takemoto, J. Y., Y. Yaxin, S. D. Stock, and T. Miyakawa. 1993. Yeast genes involved in growth inhibition by Pseudomonas syringae pv. syringae syringomycin family lipodepsipeptides. FEMS Microbiol. Lett. 114:339-342.
    • (1993) FEMS Microbiol. Lett. , vol.114 , pp. 339-342
    • Takemoto, J.Y.1    Yaxin, Y.2    Stock, S.D.3    Miyakawa, T.4
  • 172
    • 0029984874 scopus 로고    scopus 로고
    • Sensitivity of fungi to nikkomycin Z
    • Tariq, V. N., and P. L. Develin. 1996. Sensitivity of fungi to nikkomycin Z. Fungal Genet. Biol. 20:4-11.
    • (1996) Fungal Genet. Biol. , vol.20 , pp. 4-11
    • Tariq, V.N.1    Develin, P.L.2
  • 173
    • 0026635585 scopus 로고
    • Analysis of two novel classes of antifungal proteins from radish (Raphanus sativus L.) seeds
    • Terras, F. R. G., I. J. Goderis, F. Van Leuven, J. Vanderleyden, and B. P. A. Cammue. 1992. Analysis of two novel classes of antifungal proteins from radish (Raphanus sativus L.) seeds. J. Biol. Chem. 267:15301-15309.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15301-15309
    • Terras, F.R.G.1    Goderis, I.J.2    Van Leuven, F.3    Vanderleyden, J.4    Cammue, B.P.A.5
  • 175
    • 0001945855 scopus 로고
    • Surface-active properties of antifungal lipopeptides produced by Bacillus subtilis
    • Thimon, L., F. Peypoux, R. Maget-Dana, and G. Michel. 1992. Surface-active properties of antifungal lipopeptides produced by Bacillus subtilis. J. Am. Oil Chem. Soc. 69:92-93.
    • (1992) J. Am. Oil Chem. Soc. , vol.69 , pp. 92-93
    • Thimon, L.1    Peypoux, F.2    Maget-Dana, R.3    Michel, G.4
  • 177
    • 0018425886 scopus 로고
    • Cyclopeptide-antibiotika aus Aspergillus arten. Structur der echinocandine C und D
    • Traber, R., C. Keller-Juslen, H. R. Loosli, M. Huhn, and A. Von Wartburg. 1979. Cyclopeptide-antibiotika aus Aspergillus arten. Structur der echinocandine C und D. Helv. Chim, Acta 62:1252-1267.
    • (1979) Helv. Chim, Acta , vol.62 , pp. 1252-1267
    • Traber, R.1    Keller-Juslen, C.2    Loosli, H.R.3    Huhn, M.4    Von Wartburg, A.5
  • 178
    • 0001368075 scopus 로고    scopus 로고
    • Echinocandin antifungal agents
    • W. R. Strohl (ed.), Marcel Dekker, Inc., New York, N.Y.
    • Turner, W. W., and W. L. Current. 1997. Echinocandin antifungal agents, p. 315-334. In W. R. Strohl (ed.), Biotechnology of antibiotic, 2nd ed. Marcel Dekker, Inc., New York, N.Y.
    • (1997) Biotechnology of Antibiotic, 2nd Ed. , pp. 315-334
    • Turner, W.W.1    Current, W.L.2
  • 180
    • 0030970811 scopus 로고    scopus 로고
    • In vitro activity of a new echinocandin. LY303366, compared with those of amphotericin B and fluconazole against clinical yeast isolates
    • Uzun, O., S. Kocagöz, Y. Çetinkaya, S. Arikan, and S. Ünal. 1997. In vitro activity of a new echinocandin. LY303366, compared with those of amphotericin B and fluconazole against clinical yeast isolates. Antimicrob. Agents Chemother. 41:1156-1157.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1156-1157
    • Uzun, O.1    Kocagöz, S.2    Çetinkaya, Y.3    Arikan, S.4    Ünal, S.5
  • 182
    • 0342378785 scopus 로고
    • Effects of cecropin and melittin analogs and hybrids on pro- and eukaryotic cells
    • J. E. River and G. R. Marshall (ed.), Peptides: chemistry, structure, and biology. Escom, Leiden, The Netherlands
    • Wade, D., R. B. Merrifield, and H. G. Boman. 1989. Effects of cecropin and melittin analogs and hybrids on pro- and eukaryotic cells, p. 120-121. In J. E. River and G. R. Marshall (ed.), Peptides: chemistry, structure, and biology. Proceedings of the 11th Peptide Symposium. Escom, Leiden, The Netherlands.
    • (1989) Proceedings of the 11th Peptide Symposium , pp. 120-121
    • Wade, D.1    Merrifield, R.B.2    Boman, H.G.3
  • 183
    • 0025775690 scopus 로고
    • Antifungal effects of the nonlinear pharmacokinetics of cilofungin, a 1,3-β-glucan synthetase inhibitor, during continuous and intermittent intravenous infusions in treatment of experimental disseminated candidiasis
    • Walsh, T. J., J. W. Lee, P. Kelly, J. Bacher, J. Lecciones, V. Thomas, C. Lyman, D. Coleman, R. Gordee, and P. A. Pizzo. 1991. Antifungal effects of the nonlinear pharmacokinetics of cilofungin, a 1,3-β-glucan synthetase inhibitor, during continuous and intermittent intravenous infusions in treatment of experimental disseminated candidiasis. Antimicrob. Agents Chemother. 35:1321-1328.
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 1321-1328
    • Walsh, T.J.1    Lee, J.W.2    Kelly, P.3    Bacher, J.4    Lecciones, J.5    Thomas, V.6    Lyman, C.7    Coleman, D.8    Gordee, R.9    Pizzo, P.A.10
  • 185
    • 0029097115 scopus 로고
    • Structure, function, and membrane integration of defensins
    • White, S. H., W. C. Wimley, and M. E. Selsted. 1995. Structure, function, and membrane integration of defensins. Curr. Opin. Struct. Biol. 5:521-527.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 521-527
    • White, S.H.1    Wimley, W.C.2    Selsted, M.E.3
  • 186
    • 0027465990 scopus 로고
    • Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
    • Yamauchi, K., M. Tomita, T. J. Giehl, and R. T. Ellison. 1993. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 61:719-728.
    • (1993) Infect. Immun. , vol.61 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison, R.T.4
  • 187
    • 0026694271 scopus 로고
    • Preparation and structure-activity relationships of simplified analogues of the antifungal agent cilofungin: Total synthesis approach
    • Zambias, R. A., M. L. Hammond, J. V. Heck, K. Bartizal, C. Trainor, G. Abruzzo, D. M. Schmatz, and K. M. Nollstadt. 1992. Preparation and structure-activity relationships of simplified analogues of the antifungal agent cilofungin: total synthesis approach. J. Med. Chem. 35:2843-2855.
    • (1992) J. Med. Chem. , vol.35 , pp. 2843-2855
    • Zambias, R.A.1    Hammond, M.L.2    Heck, J.V.3    Bartizal, K.4    Trainor, C.5    Abruzzo, G.6    Schmatz, D.M.7    Nollstadt, K.M.8
  • 189
    • 0027472180 scopus 로고
    • The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics
    • Zanetti, M., G. Del Sal, P. Storici, C. Schneider, and D. Romeo. 1993. The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics. J. Biol. Chem. 268:522-526.
    • (1993) J. Biol. Chem. , vol.268 , pp. 522-526
    • Zanetti, M.1    Del Sal, G.2    Storici, P.3    Schneider, C.4    Romeo, D.5
  • 190
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms and partial cDNA sequence of a precursor
    • Zasloff, M. 1987. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 84:5449-5453.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 191
    • 0030896919 scopus 로고    scopus 로고
    • In vitro activity of a new semisynthetic echinocandin, LY-303366, against systemic isolates of Candida species, Cryptococcus neoformans, Blastomyces dermatidis, and Aspergillus species
    • Zhanel, G. C., J. A. Karlowsky, G. A. Harding, T. V. Balko, S. A. Zelenitsky, M. Freisen, A. Kabani, M. Turik, and D. J. Hoban. 1997. In vitro activity of a new semisynthetic echinocandin, LY-303366, against systemic isolates of Candida species, Cryptococcus neoformans, Blastomyces dermatidis, and Aspergillus species. Antimicrob. Agents Chemother. 41:863-865.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 863-865
    • Zhanel, G.C.1    Karlowsky, J.A.2    Harding, G.A.3    Balko, T.V.4    Zelenitsky, S.A.5    Freisen, M.6    Kabani, A.7    Turik, M.8    Hoban, D.J.9
  • 192
    • 0001567974 scopus 로고
    • Effects of Pseudomonas syringae phytotoxin, syringomycin, on plasma membrane fractions of Rhodotorula pilimanae
    • Zhang, L., and J. Y. Takemoto. 1987. Effects of Pseudomonas syringae phytotoxin, syringomycin, on plasma membrane fractions of Rhodotorula pilimanae. Phytopathology 77:297-303.
    • (1987) Phytopathology , vol.77 , pp. 297-303
    • Zhang, L.1    Takemoto, J.Y.2


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