메뉴 건너뛰기




Volumn 3, Issue 3, 2005, Pages 238-250

Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?

Author keywords

[No Author keywords available]

Indexed keywords

ALAMETHICIN; ANIONIC PEPTIDE; APIDAECIN; BUFORIN II; CAERIN 1 1; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CECROPIN A; DEFENSIN; DEFENSIN 1; DEFENSIN 2; DERMASEPTIN; DROSOCIN; HISTATIN; INDOLICIDIN; MAGAININ 2; MELITTIN; MERSACIDIN; MICROCIN 25; PEPTIDE; PEXIGANAN ACETATE; PLEUROCIDIN; POLYPEPTIDE ANTIBIOTIC AGENT; PR 26; PR 39; PROTEGRIN; PYRRHOCORICIN; TACHYPLESIN; UNCLASSIFIED DRUG;

EID: 14544282377     PISSN: 17401526     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrmicro1098     Document Type: Review
Times cited : (4828)

References (162)
  • 1
    • 1642305923 scopus 로고
    • Antimicrobial factors of normal tissues and fluids
    • Skarnes, R. C. & Watson, D. W. Antimicrobial factors of normal tissues and fluids. Bacteriol. Rev. 21, 273-294 (1957).
    • (1957) Bacteriol. Rev. , vol.21 , pp. 273-294
    • Skarnes, R.C.1    Watson, D.W.2
  • 2
    • 0000646464 scopus 로고
    • On a remarkable bacteriolytic element found in tissues and secretions
    • Fleming, A. On a remarkable bacteriolytic element found in tissues and secretions. Proc. R. Soc. London. B Biol. Sci. 93 306-317 (1922).
    • (1922) Proc. R. Soc. London. B Biol. Sci. , vol.93 , pp. 306-317
    • Fleming, A.1
  • 3
    • 0000617857 scopus 로고
    • Phagocytin: A bactericidal substance from polymorphonuclear leucocytes
    • Hirsch, J. G. Phagocytin: a bactericidal substance from polymorphonuclear leucocytes. J. Exp. Med. 103, 589-611 (1956).
    • (1956) J. Exp. Med. , vol.103 , pp. 589-611
    • Hirsch, J.G.1
  • 4
    • 0000255408 scopus 로고
    • Antibacterial and enzymic basic proteins from leukocyte lysosomes: Separation and identification
    • Zeya, H. I. & Spitznagel, J. K. Antibacterial and enzymic basic proteins from leukocyte lysosomes: separation and identification. Science 142, 1085-1087 (1963).
    • (1963) Science , vol.142 , pp. 1085-1087
    • Zeya, H.I.1    Spitznagel, J.K.2
  • 5
    • 14544286390 scopus 로고
    • Interaction of Gram-negative bacteria with the lysosomal fraction of polymorphonuclear leukocytes. II. Changes in the cell envelope of Escherichia coli
    • Friedberg, D., Friedberg, I. & Shilo, M. Interaction of Gram-negative bacteria with the lysosomal fraction of polymorphonuclear leukocytes. II. Changes in the cell envelope of Escherichia coli. Infect. Immun. 1, 311-331 (1970).
    • (1970) Infect. Immun. , vol.1 , pp. 311-331
    • Friedberg, D.1    Friedberg, I.2    Shilo, M.3
  • 6
    • 14544286390 scopus 로고
    • Interaction of Gram-negative bacteria with the lysosomal fraction of polymorphonuclear leukocytes. I. Role of cell wall composition of Salmonella typhimurium
    • Friedberg, D. & Shilo, M. Interaction of Gram-negative bacteria with the lysosomal fraction of polymorphonuclear leukocytes. I. Role of cell wall composition of Salmonella typhimurium. Infect. Immun. 1, 305-318 (1970).
    • (1970) Infect Immun. , vol.1 , pp. 305-318
    • Friedberg, D.1    Shilo, M.2
  • 7
    • 0016428571 scopus 로고
    • Partial characterization and purification of a rabbit granulocyte factor that increases permeability of Escherichia coli
    • Weiss, J., Franson, R. C., Beckerdite, S., Schmeidler, K. & Elsbach, P. Partial characterization and purification of a rabbit granulocyte factor that increases permeability of Escherichia coli. J. Clin. Invest. 55, 33-42 (1975).
    • (1975) J. Clin. Invest. , vol.55 , pp. 33-42
    • Weiss, J.1    Franson, R.C.2    Beckerdite, S.3    Schmeidler, K.4    Elsbach, P.5
  • 8
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner, H., Hultmark, D., Engstrom, A., Bennich, H. & Boman, H. G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292, 246-248 (1981).
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 10
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff, M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl Acad. Sci. USA 84, 5449-5453 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 11
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • Ganz, T. Defensins: antimicrobial peptides of innate immunity. Nature Rev. Immunol. 3, 710-720 (2003).
    • (2003) Nature Rev. Immunol. , vol.3 , pp. 710-720
    • Ganz, T.1
  • 13
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature 415, 389-395 (2002).
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 15
    • 0036842381 scopus 로고    scopus 로고
    • Antimicrobial peptides from animals: Focus on invertebrates
    • Vizioli, J. & Salzet, M. Antimicrobial peptides from animals: focus on invertebrates. Trends Pharmacol. Sci. 23, 494-496 (2002).
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 494-496
    • Vizioli, J.1    Salzet, M.2
  • 16
    • 0035879198 scopus 로고    scopus 로고
    • Cutting edge: IFN-inducible ELR-CXC chemokines display defensin-like antimicrobial activity
    • Cole, A. M. et al. Cutting edge: IFN-inducible ELR-CXC chemokines display defensin-like antimicrobial activity. J. Immunol. 167, 623-627 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 623-627
    • Cole, A.M.1
  • 17
    • 0036893696 scopus 로고    scopus 로고
    • Antimicrobial peptides from human platelets
    • Tang, Y. Q., Yeaman, M. R. & Selsted, M. E. Antimicrobial peptides from human platelets. Infect. Immun. 70, 6524-6533 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 6524-6533
    • Tang, Y.Q.1    Yeaman, M.R.2    Selsted, M.E.3
  • 18
    • 0142093059 scopus 로고    scopus 로고
    • Many chemokines including CCL20/MIP-3α display antimicrobial activity
    • Yang, D. et al. Many chemokines including CCL20/MIP-3α display antimicrobial activity. J. Leukoc. Biol. 74, 448-455 (2003).
    • (2003) J Leukoc. Biol. , vol.74 , pp. 448-455
    • Yang, D.1
  • 19
    • 0037025067 scopus 로고    scopus 로고
    • Direct antimicrobial properties of substance P
    • Kowalska, K., Carr, D. B. & Lipkowski, A. W. Direct antimicrobial properties of substance P. Life Sci. 71, 747-750 (2002).
    • (2002) Life Sci. , vol.71 , pp. 747-750
    • Kowalska, K.1    Carr, D.B.2    Lipkowski, A.W.3
  • 20
    • 0037445828 scopus 로고    scopus 로고
    • Adrenomedullin and mucosal defence: Interaction between host and microorganism
    • Allaker, R. P. & Kapas, S. Adrenomedullin and mucosal defence: interaction between host and microorganism. Regul. Pept. 112, 147-152 (2003).
    • (2003) Regul. Pept. , vol.112 , pp. 147-152
    • Allaker, R.P.1    Kapas, S.2
  • 21
    • 0032576977 scopus 로고    scopus 로고
    • Bactericidal domain of lactoferrin: Detection, quantitation, and characterization of lactoferricin in serum by SELDI affinity mass spectrometry
    • Kuwata, H., Yip, T. T., Yip, C. L., Tomita, M. & Hutchens, T. W. Bactericidal domain of lactoferrin: detection, quantitation, and characterization of lactoferricin in serum by SELDI affinity mass spectrometry. Biochem. Biophys. Res. Commun. 245, 764-773 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 764-773
    • Kuwata, H.1    Yip, T.T.2    Yip, C.L.3    Tomita, M.4    Hutchens, T.W.5
  • 22
    • 0033022708 scopus 로고    scopus 로고
    • Isolation and identification of three bactericidal domains in the bovine α-lactalbumin molecule
    • Pellegrini, A., Thomas, U., Bramaz, N., Hunziker, P. & von Fellenberg, R. Isolation and identification of three bactericidal domains in the bovine α-lactalbumin molecule. Biochim. Biophys. Acta 1426, 439-448 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 439-448
    • Pellegrini, A.1    Thomas, U.2    Bramaz, N.3    Hunziker, P.4    von Fellenberg, R.5
  • 23
    • 0037683515 scopus 로고    scopus 로고
    • Human hemoglobin-derived peptides exhibit antimicrobial activity: A class of host defense peptides
    • Liepke, C. et al. Human hemoglobin-derived peptides exhibit antimicrobial activity: a class of host defense peptides. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 791, 345-356 (2003).
    • (2003) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.791 , pp. 345-356
    • Liepke, C.1
  • 24
    • 2942670459 scopus 로고    scopus 로고
    • Can innate immunity be enhanced to treat microbial infections?
    • Finlay, B. B. & Hancock, R. E. Can innate immunity be enhanced to treat microbial infections? Nature Rev. Microbiol. 2 497-504 (2004).
    • (2004) Nature Rev. Microbiol. , vol.2 , pp. 497-504
    • Finlay, B.B.1    Hancock, R.E.2
  • 25
    • 0035984978 scopus 로고    scopus 로고
    • Clinical development of cationic antimicrobial peptides: From natural to novel antibiotics
    • Hancock, R. E. & Patrzykat, A. Clinical development of cationic antimicrobial peptides: from natural to novel antibiotics. Curr. Drug Targets Infect. Disord. 2, 79-83 (2002).
    • (2002) Curr. Drug Targets Infect. Disord. , vol.2 , pp. 79-83
    • Hancock, R.E.1    Patrzykat, A.2
  • 26
    • 0033863168 scopus 로고    scopus 로고
    • Structural features and biological activities of the cathelicidin-derived antimicrobial peptides
    • Gennaro, R. & Zanetti, M. Structural features and biological activities of the cathelicidin-derived antimicrobial peptides. Biopolymers 55, 31-49 (2000).
    • (2000) Biopolymers , vol.55 , pp. 31-49
    • Gennaro, R.1    Zanetti, M.2
  • 27
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock, R. E. W. Peptide antibiotics. Lancet 349 418-422 (1997).
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.W.1
  • 28
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman, H. G. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13, 61-92 (1995).
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 29
    • 0031771562 scopus 로고    scopus 로고
    • Detection of anionic antimicrobial peptides in ovine bronchoalveolar lavage fluid and respiratory epithelium
    • Brogden, K. A., Ackermann, M. & Huttner, K. M. Detection of anionic antimicrobial peptides in ovine bronchoalveolar lavage fluid and respiratory epithelium. Infect. Immun. 66, 5948-5954 (1998 ).
    • (1998) Infect. Immun. , vol.66 , pp. 5948-5954
    • Brogden, K.A.1    Ackermann, M.2    Huttner, K.M.3
  • 30
    • 0030048076 scopus 로고    scopus 로고
    • Isolation of an ovine pulmonary surfactant-associated anionic peptide bactericidal for Pasteurella haemolytica
    • Brogden, K. A., De Lucca, A. J., Bland, J. & Elliott, S. Isolation of an ovine pulmonary surfactant-associated anionic peptide bactericidal for Pasteurella haemolytica. Proc. Natl Acad. Sci. USA 93, 412-416 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 412-416
    • Brogden, K.A.1    De Lucca, A.J.2    Bland, J.3    Elliott, S.4
  • 31
    • 0032783033 scopus 로고    scopus 로고
    • Differences in the concentrations of small, anionic, antimicrobial peptides in bronchoalveolar lavage fluid and in respiratory epithelia of patients with and without cystic fibrosis
    • Brogden, K. A., Ackermann, M. R., McCray, P. B. Jr & Huttner, K. M. Differences in the concentrations of small, anionic, antimicrobial peptides in bronchoalveolar lavage fluid and in respiratory epithelia of patients with and without cystic fibrosis. Infect. Immun. 67, 4256-4259 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 4256-4259
    • Brogden, K.A.1    Ackermann, M.R.2    McCray Jr., P.B.3    Huttner, K.M.4
  • 32
    • 0030845025 scopus 로고    scopus 로고
    • Small, anionic, and charge-neutralizing propeptide fragments of zymogens are antimicrobial
    • Brogden, K. A., Ackermann, M. & Huttner, K. M. Small, anionic, and charge-neutralizing propeptide fragments of zymogens are antimicrobial. Antimicrob. Agents Chem. 41, 1615-1617 (1997).
    • (1997) Antimicrob. Agents Chem. , vol.41 , pp. 1615-1617
    • Brogden, K.A.1    Ackermann, M.2    Huttner, K.M.3
  • 33
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, α-helical antimicrobial peptides
    • Tossi, A., Sandri, L. & Giangaspero, A. Amphipathic, α-helical antimicrobial peptides. Biopolymers 55, 4-30 (2000).
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 34
    • 0032488904 scopus 로고    scopus 로고
    • Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37
    • Johansson, J., Gudmundsson, G. H., Rottenberg, M. E., Berndt, K. D. & Agerberth, B. Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. J. Biol. Chem. 273 3718-3724 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 3718-3724
    • Johansson, J.1    Gudmundsson, G.H.2    Rottenberg, M.E.3    Berndt, K.D.4    Agerberth, B.5
  • 35
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II
    • Park, C. B., Yi, K. S., Matsuzaki, K., Kim, M. S. & Kim, S. C. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II. Proc. Natl Acad. Sci. USA 97, 8245-8250 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 36
    • 0036633301 scopus 로고    scopus 로고
    • The short proline-rich antibacterial peptide family
    • Otvos, L., Jr. The short proline-rich antibacterial peptide family. Cell. Mol. Life Sci. 59, 1138-1150 (2002).
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1138-1150
    • Otvos Jr., L.1
  • 37
    • 0027474382 scopus 로고
    • Defensins: Antimicrobial and cytotoxic peptides of mammalian cells
    • Lehrer, R. I., Lichtenstein, A. K. & Ganz, T. Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu. Rev. Immunol. 11, 105-128 (1993).
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 105-128
    • Lehrer, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 39
    • 0036829619 scopus 로고    scopus 로고
    • Immunology. Versatile defensins
    • Ganz, T. Immunology. Versatile defensins. Science 298, 977-979 (2002).
    • (2002) Science , vol.298 , pp. 977-979
    • Ganz, T.1
  • 40
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated α-defensins
    • Tang, Y. Q. et al. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated α-defensins. Science 286, 498-502 (1999).
    • (1999) Science , vol.286 , pp. 498-502
    • Tang, Y.Q.1
  • 41
    • 0037031240 scopus 로고    scopus 로고
    • Two states of cyclic antimicrobial peptide RTD-1 in lipid bilayers
    • Weiss, T. M. et al. Two states of cyclic antimicrobial peptide RTD-1 in lipid bilayers. Biochemistry 41, 10070-10076 (2002).
    • (2002) Biochemistry , vol.41 , pp. 10070-10076
    • Weiss, T.M.1
  • 42
    • 4444383056 scopus 로고    scopus 로고
    • SPAG11/isoform HE2C, an atypical anionic β-defensin-like peptide
    • von Horsten, H. H., Schafer, B. & Kirchhoff, C. SPAG11/isoform HE2C, an atypical anionic β-defensin-like peptide. Peptides 25, 1223-1233 (2004).
    • (2004) Peptides , vol.25 , pp. 1223-1233
    • von Horsten, H.H.1    Schafer, B.2    Kirchhoff, C.3
  • 43
    • 0034775147 scopus 로고    scopus 로고
    • Congeners of SMAP29 kill ovine pathogens and induce ultrastructural damage in bacterial cells
    • Kalfa, V. C. et al. Congeners of SMAP29 kill ovine pathogens and induce ultrastructural damage in bacterial cells. Antimicrob. Agents Chemother. 45, 3256-3261 (2001).
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 3256-3261
    • Kalfa, V.C.1
  • 44
    • 0024391711 scopus 로고
    • Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity
    • Lehrer, R. I. et al. Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity. J. Clin. Invest. 84, 553-561 (1989).
    • (1989) J. Clin. Invest. , vol.84 , pp. 553-561
    • Lehrer, R.I.1
  • 45
    • 3042550167 scopus 로고    scopus 로고
    • The androgen-regulated epididymal sperm-binding protein, human β-defensin 118 (DEFB118) (formerly ESC42), is an antimicrobial β-defensin
    • Yenugu, S., Hamil, K. G., Radhakrishnan, Y., French, F. S. & Hall, S. H. The androgen-regulated epididymal sperm-binding protein, human β-defensin 118 (DEFB118) (formerly ESC42), is an antimicrobial β-defensin. Endocrinology 145, 3165-3173 (2004).
    • (2004) Endocrinology , vol.145 , pp. 3165-3173
    • Yenugu, S.1    Hamil, K.G.2    Radhakrishnan, Y.3    French, F.S.4    Hall, S.H.5
  • 46
    • 0030971376 scopus 로고    scopus 로고
    • Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: Pore formation by melittin
    • Ladokhin, A. S., Selsted, M. E. & White, S. H. Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: pore formation by melittin. Biophys. J. 72, 1762-1766 (1997).
    • (1997) Biophys. J. , vol.72 , pp. 1762-1766
    • Ladokhin, A.S.1    Selsted, M.E.2    White, S.H.3
  • 47
    • 0030790179 scopus 로고    scopus 로고
    • Pore formation and translocation of melittin
    • Matsuzaki, K., Yoneyama, S. & Miyajima, K. Pore formation and translocation of melittin. Biophys. J. 73, 831-838 (1997).
    • (1997) Biophys. J. , vol.73 , pp. 831-838
    • Matsuzaki, K.1    Yoneyama, S.2    Miyajima, K.3
  • 48
    • 0031872031 scopus 로고    scopus 로고
    • Release of aqueous contents from phospholipid vesicles induced by cecropin A (1-8) magainin 2 (1-12) hybrid and its analogues
    • Kang, J. H., Shin, S. Y., Jang, S. Y., Lee, M. K. & Hahm, K. S. Release of aqueous contents from phospholipid vesicles induced by cecropin A (1-8) magainin 2 (1-12) hybrid and its analogues. J. Peptide Res. 52, 45-50 (1998).
    • (1998) J. Peptide Res. , vol.52 , pp. 45-50
    • Kang, J.H.1    Shin, S.Y.2    Jang, S.Y.3    Lee, M.K.4    Hahm, K.S.5
  • 49
    • 0030827974 scopus 로고    scopus 로고
    • Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins
    • Hristova, K., Selsted, M. E. & White, S. H. Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins. J. Biol. Chem. 272, 24224-24233 (1997).
    • (1997) J Biol. Chem. , vol.272 , pp. 24224-24233
    • Hristova, K.1    Selsted, M.E.2    White, S.H.3
  • 50
    • 0034767060 scopus 로고    scopus 로고
    • Comparison of the membrane association of two antimicrobial peptides, magainin 2 and indolicidin
    • Zhao, H., Mattila, J. P., Holopainen, J. M. & Kinnunen, P. K. Comparison of the membrane association of two antimicrobial peptides, magainin 2 and indolicidin. Biophys. J. 81, 2979-2991 (2001).
    • (2001) Biophys. J. , vol.81 , pp. 2979-2991
    • Zhao, H.1    Mattila, J.P.2    Holopainen, J.M.3    Kinnunen, P.K.4
  • 51
    • 0028818140 scopus 로고
    • Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers
    • Matsuzaki, K., Murase, O. & Miyajima, K. Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers. Biochemistry 34, 12553-12559 (1995).
    • (1995) Biochemistry , vol.34 , pp. 12553-12559
    • Matsuzaki, K.1    Murase, O.2    Miyajima, K.3
  • 52
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • Christensen, B., Fink, J., Merrifield, R. B. & Mauzerall, D. Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc. Natl Acad. Sci. USA 85, 5072-5076 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 53
    • 0030007916 scopus 로고    scopus 로고
    • Formation of pores in Escherichia coli cell membranes by a cecropin isolated from hemolymph of Heliothis virescens larvae
    • Lockey, T. D. & Ourth, D. D. Formation of pores in Escherichia coli cell membranes by a cecropin isolated from hemolymph of Heliothis virescens larvae. Eur. J. Biochem. 236, 263-271 (1996).
    • (1996) Eur. J. Biochem. , vol.236 , pp. 263-271
    • Lockey, T.D.1    Ourth, D.D.2
  • 54
    • 0025021992 scopus 로고
    • Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes
    • Kagan, B. L., Selsted, M. E., Ganz, T. & Lehrer, R. I. Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes. Proc. Natl Acad. Sci. USA 87, 210-214 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 210-214
    • Kagan, B.L.1    Selsted, M.E.2    Ganz, T.3    Lehrer, R.I.4
  • 55
    • 1642359643 scopus 로고    scopus 로고
    • Energetics of pore formation induced by membrane active peptides
    • Lee, M. T., Chen, F. Y. & Huang, H. W. Energetics of pore formation induced by membrane active peptides. Biochemistry 43 3590-3599 (2004).
    • (2004) Biochemistry , vol.43 , pp. 3590-3599
    • Lee, M.T.1    Chen, F.Y.2    Huang, H.W.3
  • 56
    • 0025278431 scopus 로고
    • Method of oriented circular dichroism
    • Wu, Y., Huang, H. W. & Olah, G. A. Method of oriented circular dichroism. Biophys. J. 57, 797-806 (1990).
    • (1990) Biophys. J. , vol.57 , pp. 797-806
    • Wu, Y.1    Huang, H.W.2    Olah, G.A.3
  • 57
    • 0031022395 scopus 로고    scopus 로고
    • Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids
    • Ladokhin, A. S., Selsted, M. E. & White, S. H. Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids. Biophys. J. 72, 794-805 (1997).
    • (1997) Biophys. J. , vol.72 , pp. 794-805
    • Ladokhin, A.S.1    Selsted, M.E.2    White, S.H.3
  • 58
    • 0031001261 scopus 로고    scopus 로고
    • Conformations and orientations of aromatic amino acid residues of tachyplesin I in phospholipid membranes
    • Oishi, O. et al. Conformations and orientations of aromatic amino acid residues of tachyplesin I in phospholipid membranes. Biochemistry 36, 4352-4359 (1997).
    • (1997) Biochemistry , vol.36 , pp. 4352-4359
    • Oishi, O.1
  • 59
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
    • Turner, J., Cho, Y., Dinh, N. N., Waring, A. J. & Lehrer, R. I. Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob. Agents Chemother. 42, 2206-2214 (1998).
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3    Waring, A.J.4    Lehrer, R.I.5
  • 60
    • 0028240042 scopus 로고
    • Structure, synthesis, and activity of dermaseptin b, a novel vertebrate defensive peptide from frog skin: Relationship with adenoregulin
    • Mor, A., Amiche, M. & Nicolas, P. Structure, synthesis, and activity of dermaseptin b, a novel vertebrate defensive peptide from frog skin: relationship with adenoregulin. Biochemistry 33, 6642-6650 (1994).
    • (1994) Biochemistry , vol.33 , pp. 6642-6650
    • Mor, A.1    Amiche, M.2    Nicolas, P.3
  • 61
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • Bechinger, B. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta 1462, 157-183 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 62
    • 0037031254 scopus 로고    scopus 로고
    • Solid-state NMR investigations of peptide-lipid interaction and orientation of a β-sheet antimicrobial peptide, protegrin
    • Yamaguchi, S., Hong, T., Waring, A, Lehrer, R. I., & Hong, M. Solid-state NMR investigations of peptide-lipid interaction and orientation of a β-sheet antimicrobial peptide, protegrin. Biochemistry 41, 9852-9862 (2002).
    • (2002) Biochemistry , vol.41 , pp. 9852-9862
    • Yamaguchi, S.1    Hong, T.2    Waring, A.3    Lehrer, R.I.4    Hong, M.5
  • 63
    • 0027488740 scopus 로고
    • Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy
    • Bechinger, B., Zasloff, M. & Opella, S. J. Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy. Protein Sci. 2, 2077-2084 (1993).
    • (1993) Protein Sci. , vol.2 , pp. 2077-2084
    • Bechinger, B.1    Zasloff, M.2    Opella, S.J.3
  • 64
    • 0034804339 scopus 로고    scopus 로고
    • Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy
    • Yamaguchi, S. et al. Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy. Biophys. J. 81, 2203-2214 (2001).
    • (2001) Biophys. J. , vol.81 , pp. 2203-2214
    • Yamaguchi, S.1
  • 65
    • 0038052326 scopus 로고    scopus 로고
    • Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37
    • Henzler Wildman, K. A., Lee, D. K. & Ramamoorthy, A. Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37. Biochemistry 42, 6545-6558 (2003).
    • (2003) Biochemistry , vol.42 , pp. 6545-6558
    • Henzler Wildman, K.A.1    Lee, D.K.2    Ramamoorthy, A.3
  • 66
    • 3342900055 scopus 로고    scopus 로고
    • Solid-state NMR investigation of the selective perturbation of lipid bilayers by the cyclic antimicrobial peptice RTD-1
    • Buffy, J. J. et al. Solid-state NMR investigation of the selective perturbation of lipid bilayers by the cyclic antimicrobial peptice RTD-1. Biochemistry 43, 9800-9812 (2004).
    • (2004) Biochemistry , vol.43 , pp. 9800-9812
    • Buffy, J.J.1
  • 67
    • 3042772810 scopus 로고    scopus 로고
    • Conformation of peptides in lipid membranes studied by X-ray grazing incidence scattering
    • Spaar, A., Munster, C. & Salditt, T. Conformation of peptides in lipid membranes studied by X-ray grazing incidence scattering. Biophys. J. 87, 396-407 (2004).
    • (2004) Biophys. J. , vol.87 , pp. 396-407
    • Spaar, A.1    Munster, C.2    Salditt, T.3
  • 68
    • 0028790410 scopus 로고
    • Antimicrobial peptide pores in membranes detected by neutron in-plane scattering
    • He, K., Ludtke, S. J., Huang, H. W. & Worcester, D. L. Antimicrobial peptide pores in membranes detected by neutron in-plane scattering. Biochemistry 34, 15614-15618 (1995).
    • (1995) Biochemistry , vol.34 , pp. 15614-15618
    • He, K.1    Ludtke, S.J.2    Huang, H.W.3    Worcester, D.L.4
  • 69
    • 0029904095 scopus 로고    scopus 로고
    • Membrane pores induced by magainin
    • Ludtke, S. J. et al. Membrane pores induced by magainin. Biochemistry 35, 13723-13728 (1996).
    • (1996) Biochemistry , vol.35 , pp. 13723-13728
    • Ludtke, S.J.1
  • 70
    • 0031849949 scopus 로고    scopus 로고
    • Neutron off-plane scattering of aligned membranes. I. Method of measurement
    • Yang, L., Harroun, T. A., Heller, W. T., Weiss, T. M. & Huang, H. W. Neutron off-plane scattering of aligned membranes. I. Method of measurement. Biophys. J. 75, 641-645 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 641-645
    • Yang, L.1    Harroun, T.A.2    Heller, W.T.3    Weiss, T.M.4    Huang, H.W.5
  • 71
    • 0032725432 scopus 로고    scopus 로고
    • Supramolecular structures of peptide assemblies in membranes by neutron off-plane scattering: Method of analysis
    • Yang, L., Weiss, T. M., Harroun, T. A., Heller, W. T. & Huang, H. W. Supramolecular structures of peptide assemblies in membranes by neutron off-plane scattering: method of analysis. Biophys. J. 77, 2648-2656 (1999).
    • (1999) Biophys. J. , vol.77 , pp. 2648-2656
    • Yang, L.1    Weiss, T.M.2    Harroun, T.A.3    Heller, W.T.4    Huang, H.W.5
  • 72
    • 0038778549 scopus 로고    scopus 로고
    • Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
    • Chen, F. Y., Lee, M. T. & Huang, H. W. Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation. Biophys. J. 84, 3751-3758 (2003).
    • (2003) Biophys. J. , vol.84 , pp. 3751-3758
    • Chen, F.Y.1    Lee, M.T.2    Huang, H.W.3
  • 73
    • 0027216093 scopus 로고
    • Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine
    • Boman, H. G., Agerberth, B. & Boman, A. Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Infect. Immun. 61, 2978-2984 (1993).
    • (1993) Infect. Immun. , vol.61 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 74
    • 0030886178 scopus 로고    scopus 로고
    • The concentration-dependent membrane activity of cecropin A
    • Silvestro, L., Gupta, K., Weiser, J. N. & Axelsen, P. H. The concentration-dependent membrane activity of cecropin A. Biochemistry 36, 11452-11460 (1997).
    • (1997) Biochemistry , vol.36 , pp. 11452-11460
    • Silvestro, L.1    Gupta, K.2    Weiser, J.N.3    Axelsen, P.H.4
  • 75
    • 0033003473 scopus 로고    scopus 로고
    • Biological properties of structurally related α-helical cationic antimicrobial peptides
    • Scott, M. G., Yan, H. & Hancock, R. E. Biological properties of structurally related α-helical cationic antimicrobial peptides. Infect. Immun. 67, 2005-2009 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 2005-2009
    • Scott, M.G.1    Yan, H.2    Hancock, R.E.3
  • 76
    • 0032752132 scopus 로고    scopus 로고
    • Interaction of cationic peptides with lipoteichoic acid and gram- positive bacteria
    • Scott, M. G., Gold, M. R. & Hancock, R. E. Interaction of cationic peptides with lipoteichoic acid and gram- positive bacteria. Infect. Immun. 67, 6445-6453 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 6445-6453
    • Scott, M.G.1    Gold, M.R.2    Hancock, R.E.3
  • 77
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • Huang, H. W. Action of antimicrobial peptides: two-state model. Biochemistry 39, 8347-8352 (2000).
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 78
    • 0029594533 scopus 로고
    • Membrane thinning caused by magainin 2
    • Ludtke, S., He, K. & Huang, H. Membrane thinning caused by magainin 2. Biochemistry 34, 16764-16769 (1995).
    • (1995) Biochemistry , vol.34 , pp. 16764-16769
    • Ludtke, S.1    He, K.2    Huang, H.3
  • 79
    • 0034635136 scopus 로고    scopus 로고
    • Membrane thinning effect of the β-sheet antimicrobial protegrin
    • Heller, W. T. et al. Membrane thinning effect of the β-sheet antimicrobial protegrin. Biochemistry 39, 139-145 (2000).
    • (2000) Biochemistry , vol.39 , pp. 139-145
    • Heller, W.T.1
  • 80
    • 0029022547 scopus 로고
    • X-ray diffraction study of lipid bilayer membranes interacting with amphiphilic helical peptides: Diphytanoyl phosphatidylcholine with alamethicin at low concentrations
    • Wu, Y., He, K., Ludtke, S. J. & Huang, H. W. X-ray diffraction study of lipid bilayer membranes interacting with amphiphilic helical peptides: diphytanoyl phosphatidylcholine with alamethicin at low concentrations. Biophys. J. 68, 2361-2369 (1995).
    • (1995) Biophys. J. , vol.68 , pp. 2361-2369
    • Wu, Y.1    He, K.2    Ludtke, S.J.3    Huang, H.W.4
  • 81
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • Yang, L., Harroun, T. A., Weiss, T. M., Ding, L. & Huang, H. W. Barrel-stave model or toroidal model? A case study on melittin pores. Biophys. J. 81, 1475-1485 (2001).
    • (2001) Biophys. J. , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 82
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bilayers
    • Ehrenstein, G. & Lecar, H. Electrically gated ionic channels in lipid bilayers. Q. Rev. Biophys. 10, 1-34 (1977).
    • (1977) Q. Rev. Biophys. , vol.10 , pp. 1-34
    • Ehrenstein, G.1    Lecar, H.2
  • 83
    • 0030028241 scopus 로고    scopus 로고
    • Neutron scattering in the plane of membranes: Structure of alamethicin pores
    • He, K., Ludtke, S. J., Worcester, D. L. & Huang, H. W. Neutron scattering in the plane of membranes: structure of alamethicin pores. Biophys. J. 70, 2659-2666 (1996).
    • (1996) Biophys. J. , vol.70 , pp. 2659-2666
    • He, K.1    Ludtke, S.J.2    Worcester, D.L.3    Huang, H.W.4
  • 84
    • 0036226098 scopus 로고    scopus 로고
    • Size distribution of barrel-stave aggregates of membrane peptides: Influence of the bilayer lateral pressure profile
    • Cantor, R. S. Size distribution of barrel-stave aggregates of membrane peptides: influence of the bilayer lateral pressure profile. Biophys. J. 82, 2520-2525 (2002).
    • (2002) Biophys. J. , vol.82 , pp. 2520-2525
    • Cantor, R.S.1
  • 85
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Pouny, Y,. Rapaport, D., Mor, A., Nicolas, P. & Shai, Y. Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry 31, 12416-12423 (1992).
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 86
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462, 55-70 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 87
    • 0035479424 scopus 로고    scopus 로고
    • 'Detergent-like' permeabilization of anionic lipid vesicles by melittin
    • Ladokhin, A. S. & White, S. H. 'Detergent-like' permeabilization of anionic lipid vesicles by melittin. Biochim. Biophys. Acta 1514, 253-260 (2001).
    • (2001) Biochim. Biophys. Acta , vol.1514 , pp. 253-260
    • Ladokhin, A.S.1    White, S.H.2
  • 88
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic, α-helical antimicrobial peptides
    • Oren, Z. & Shai, Y. Mode of action of linear amphipathic, α-helical antimicrobial peptides. Biopolymers 47, 451-463 (1998).
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 89
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • Matsuzaki, K., Murase, O., Fujii, N. & Miyajima, K. An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry 35, 11361-11368 (1996).
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 90
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • Hallock, K. J., Lee, D. K. & Ramamoorthy, A. MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophys. J. 84, 3052-3060 (2003).
    • (2003) Biophys. J. , vol.84 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.K.2    Ramamoorthy, A.3
  • 91
    • 0032566283 scopus 로고    scopus 로고
    • Relationship of membrane curvature to the formation of pores by magainin 2
    • Matsuzaki, K. et al. Relationship of membrane curvature to the formation of pores by magainin 2. Biochemistry 37, 11856-11863 (1998).
    • (1998) Biochemistry , vol.37 , pp. 11856-11863
    • Matsuzaki, K.1
  • 92
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria
    • Matsuzaki, K., Sugishita, K., Harada, M, Fujii, N. & Miyajima, K. Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria. Biochim. Biophys. Acta 1327, 119-130 (1997).
    • (1997) Biochim. Biophys. Acta , vol.1327 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.2    Harada, M.3    Fujii, N.4    Miyajima, K.5
  • 93
    • 0027218376 scopus 로고
    • Defensins promote fusion and lysis of negatively charged membranes
    • Fujii, G., Selsted, M. E. & Eisenberg, D. Defensins promote fusion and lysis of negatively charged membranes. Protein Sci. 2 1301-1312 (1993).
    • (1993) Protein Sci. , vol.2 , pp. 1301-1312
    • Fujii, G.1    Selsted, M.E.2    Eisenberg, D.3
  • 94
    • 0028061984 scopus 로고
    • Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric pores
    • Wimley, W. C., Selsted, M. E. & White, S. H. Interactions between human defensins and lipid bilayers: evidence for formation of multimeric pores. Protein Sci. 3, 1362-1373 (1994)
    • (1994) Protein Sci. , vol.3 , pp. 1362-1373
    • Wimley, W.C.1    Selsted, M.E.2    White, S.H.3
  • 95
    • 0027249384 scopus 로고
    • Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus
    • Cociancich, S., Ghazi, A., Hetru, C., Hoffmann, J. A. & Letellier, L. Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus. J. Biol. Chem. 268, 19239-19245 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 19239-19245
    • Cociancich, S.1    Ghazi, A.2    Hetru, C.3    Hoffmann, J.A.4    Letellier, L.5
  • 96
    • 1042289728 scopus 로고    scopus 로고
    • Channel-forming membrane permeabilization by an antibacterial protein, sapecin: Determination of membrane-buried and oligomerization surfaces by NMR
    • Takeuchi, K. et al. Channel-forming membrane permeabilization by an antibacterial protein, sapecin: determination of membrane-buried and oligomerization surfaces by NMR. J. Biol. Chem. 279, 4981-4987 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 4981-4987
    • Takeuchi, K.1
  • 97
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: Their potential to modulate activity on model membranes and biological cells
    • Dathe, M. & Wieprecht, T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1462, 71-87 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 98
    • 0036467404 scopus 로고    scopus 로고
    • General aspects of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphipathic helical model peptides
    • Dathe, M. et al. General aspects of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphipathic helical model peptides. Biochim. Biophys. Acta 1558, 171-186 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1558 , pp. 171-186
    • Dathe, M.1
  • 99
    • 0028327442 scopus 로고
    • Anion pores from magainins and related defensive peptides
    • Duclohier, H. Anion pores from magainins and related defensive peptides. Toxicology 87, 175-188 (1994).
    • (1994) Toxicology , vol.87 , pp. 175-188
    • Duclohier, H.1
  • 100
    • 0024396374 scopus 로고
    • Magainin 2 amide and analogues. Antimicrobial activity, membrane depolarization and susceptibility to proteolysis
    • Juretic, D. et al. Magainin 2 amide and analogues. Antimicrobial activity, membrane depolarization and susceptibility to proteolysis. FEBS Lett. 249, 219-223 (1989).
    • (1989) FEBS Lett. , vol.249 , pp. 219-223
    • Juretic, D.1
  • 102
    • 0023547233 scopus 로고
    • Autolytic system of Staphylococcus simulans 22: Influence of cationic peptides on activity of N-acetylmuramoyl-L-alanine amidase
    • Bierbaum, G. & Sahl, H. G. Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-L-alanine amidase. J. Bacteriol. 169 5452-5458 (1987).
    • (1987) J. Bacteriol. , vol.169 , pp. 5452-5458
    • Bierbaum, G.1    Sahl, H.G.2
  • 103
    • 0037416988 scopus 로고    scopus 로고
    • Modulation of the activity of secretory phospholipase A2 by antimicrobial peptides
    • Zhao, H. & Kinnunen, P. K. Modulation of the activity of secretory phospholipase A2 by antimicrobial peptides. Antimicrob. Agents Chemother. 47, 965-971 (2003).
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 965-971
    • Zhao, H.1    Kinnunen, P.K.2
  • 104
    • 0032949646 scopus 로고    scopus 로고
    • Structural requirements for cellular uptake of α-helical amphipathic peptides
    • Scheller, A. et al. Structural requirements for cellular uptake of α-helical amphipathic peptides. J. Pept. Sci. 5, 185-194 (1999).
    • (1999) J. Pept. Sci. , vol.5 , pp. 185-194
    • Scheller, A.1
  • 105
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • Futaki, S. et al. Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276, 5836-5840 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 5836-5840
    • Futaki, S.1
  • 106
    • 0346460957 scopus 로고    scopus 로고
    • Cell-penetrating peptides. A re-evaluation of the mechanism of cellular uptake
    • Richard, J. P. et al. Cell-penetrating peptides. A re-evaluation of the mechanism of cellular uptake. J. Biol. Chem. 278, 585-590 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 585-590
    • Richard, J.P.1
  • 107
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia, J. S., Stan, R. V. & Dowdy, S. F. Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nature Med. 10, 310-315 (2004).
    • (2004) Nature Med. , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 108
    • 0027528472 scopus 로고
    • Functional and chemical characterization of hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera)
    • Casteels, P., Ampre, C., Jacobs, F. & Tempst, P. Functional and chemical characterization of hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera). J. Biol. Chem. 268, 7044-7054 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 7044-7054
    • Casteels, P.1    Ampre, C.2    Jacobs, F.3    Tempst, P.4
  • 109
    • 0030032395 scopus 로고    scopus 로고
    • Antibacterial activity of a synthetic peptide (PR-26) derived from PR-39, a proline-arginine-rich neutrophil antimicrobial peptide
    • Shi, J. et al. Antibacterial activity of a synthetic peptide (PR-26) derived from PR-39, a proline-arginine-rich neutrophil antimicrobial peptide. Antimicrob. Agents Chemother. 40, 115-121 (1996).
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 115-121
    • Shi, J.1
  • 110
    • 0032031434 scopus 로고    scopus 로고
    • Mechanism of antimicrobial action of indolicidin
    • Subbalakshmi, C. & Sitaram, N. Mechanism of antimicrobial action of indolicidin. FEMS Microbiol. Lett. 160, 91-96 (1998).
    • (1998) FEMS Microbiol. Lett. , vol.160 , pp. 91-96
    • Subbalakshmi, C.1    Sitaram, N.2
  • 111
    • 0026526445 scopus 로고
    • Microcin 25, a novel antimicrobial peptide produced by Escherichia coli
    • Salomon, R. A. & Farias, R. N. Microcin 25, a novel antimicrobial peptide produced by Escherichia coli. J. Bacteriol. 174, 7428-7435 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 7428-7435
    • Salomon, R.A.1    Farias, R.N.2
  • 113
    • 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. & 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. Biochem. Biophys. Res. Commun. 244, 253-257 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 114
    • 0026550672 scopus 로고
    • Binding of tachyplesin I to DNA revealed by footprinting analysis: Significant contribution of secondary structure to DNA binding and implication for biological action
    • Yonezawa, A., Kuwahara, J., Fujii, N. & Sugiura, Y. Binding of tachyplesin I to DNA revealed by footprinting analysis: significant contribution of secondary structure to DNA binding and implication for biological action Biochemistry 31, 2998-3004 (1992)
    • (1992) Biochemistry , vol.31 , pp. 2998-3004
    • Yonezawa, A.1    Kuwahara, J.2    Fujii, N.3    Sugiura, Y.4
  • 115
    • 0036168570 scopus 로고    scopus 로고
    • Sublethal concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in Escherichia coli
    • Patrzykat, A., Friedrich, C. L., Zhang, L., Mendoza, V. & Hancock, R. E. Sublethal concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in Escherichia coli. Antimicrob. Agents Chemother. 46, 605-614 (2002).
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 605-614
    • Patrzykat, A.1    Friedrich, C.L.2    Zhang, L.3    Mendoza, V.4    Hancock, R.E.5
  • 116
    • 1642267482 scopus 로고    scopus 로고
    • Histatins: Antimicrobial peptides with therapeutic potential
    • Kavanagh, K. & Dowd, S. Histatins: antimicrobial peptides with therapeutic potential. J. Pharm. Pharmacol. 56, 285-289 (2004.)
    • (2004) J. Pharm. Pharmacol. , vol.56 , pp. 285-289
    • Kavanagh, K.1    Dowd, S.2
  • 117
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: An overview
    • Andreu, D. & Rivas, L. Animal antimicrobial peptides: an overview. Biopolymers 47, 415-433 (1998).
    • (1998) Biopolymers. , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 118
    • 0034700271 scopus 로고    scopus 로고
    • Interaction between heat shock proteins and antimicrobial peptides
    • Otvos, L. Jr. et al. Interaction between heat shock proteins and antimicrobial peptides. Biochemistry 39, 14150-14159 (2000).
    • (2000) Biochemistry , vol.39 , pp. 14150-14159
    • Otvos Jr., L.1
  • 119
    • 0035853022 scopus 로고    scopus 로고
    • The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding
    • Kragol, G. et al. The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding Biochemistry 40, 3016-3026 (2001).
    • (2001) Biochemistry , vol.40 , pp. 3016-3026
    • Kragol, G.1
  • 120
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the d/t operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • Peschel, A. et al. Inactivation of the d/t operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J. Biol. Chem. 274 8405-8410 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 8405-8410
    • Peschel, A.1
  • 121
    • 0037218495 scopus 로고    scopus 로고
    • MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing
    • Kristian, S. A., Durr, M., Van Strijp, J. A., Neumeister, B & Peschel, A. MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing. Infect. Immun. 71, 546-549 (2003)
    • (2003) Infect. Immun. , vol.71 , pp. 546-549
    • Kristian, S.A.1    Durr, M.2    Van Strijp, J.A.3    Neumeister, B.4    Peschel, A.5
  • 122
    • 0035821289 scopus 로고    scopus 로고
    • Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with L-lysine
    • Peschel, A. at al. Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with L-lysine. J. Exp. Med. 193, 1067-1076 (2001).
    • (2001) J. Exp. Med. , vol.193 , pp. 1067-1076
    • Peschel, A.1
  • 123
    • 9244224674 scopus 로고    scopus 로고
    • Capsule polysaccharide mediates bacterial resistance to antimicrobial peptides
    • Campos, M. A. et al. Capsule polysaccharide mediates bacterial resistance to antimicrobial peptides. Infect. Immun. 72, 7107-7114 (2004).
    • (2004) Infect. Immun. , vol.72 , pp. 7107-7114
    • Campos, M.A.1
  • 126
    • 0141484326 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides activate a two-component regulatory system, PmrA-PmrB, that regulates resistance to polymyxin B and cationic antimicrobial peptides in Pseudomonas aeruginosa
    • McPhee, J. B., Lewenza, S. & Hancock, R. E. Cationic antimicrobial peptides activate a two-component regulatory system, PmrA-PmrB, that regulates resistance to polymyxin B and cationic antimicrobial peptides in Pseudomonas aeruginosa. Mol. Microbiol. 50, 205-217 (2003).
    • (2003) Mol. Microbiol. , vol.50 , pp. 205-217
    • McPhee, J.B.1    Lewenza, S.2    Hancock, R.E.3
  • 127
    • 0030984298 scopus 로고    scopus 로고
    • Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ
    • Guo, L. et al. Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ. Science 276, 250-253 (1997).
    • (1997) Science , vol.276 , pp. 250-253
    • Guo, L.1
  • 128
    • 0032538292 scopus 로고    scopus 로고
    • Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides
    • Guo, L. et al. Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides. Cell 95 189-198 (1998).
    • (1998) Cell , vol.95 , pp. 189-198
    • Guo, L.1
  • 129
    • 0032992831 scopus 로고    scopus 로고
    • The Salmonella typhi melittin resistance gene pqaB affects intracellular growth in PMA-differentiated U937 cells, polymyxin B resistance and lipopolysaccharide
    • Baker, S. J., Gunn, J. S. & Morona, R. The Salmonella typhi melittin resistance gene pqaB affects intracellular growth in PMA-differentiated U937 cells, polymyxin B resistance and lipopolysaccharide. Microbiology 145, 367-378 (1999).
    • (1999) Microbiology , vol.145 , pp. 367-378
    • Baker, S.J.1    Gunn, J.S.2    Morona, R.3
  • 130
    • 0029873652 scopus 로고    scopus 로고
    • Role of yadA in resistance to killing of Yersinia enterocolitica by antimicrobial polypeptides of human granulocytes
    • Visser, L. G., Hiemstra, R. S., Van Den Barselaar, M. T., Ballieux, P. A. & Van Furth, R. Role of yadA in resistance to killing of Yersinia enterocolitica by antimicrobial polypeptides of human granulocytes. Infect. Immun. 64, 1653-1658 (1996)
    • (1996) Infect. Immun. , vol.64 , pp. 1653-1658
    • Visser, L.G.1    Hiemstra, R.S.2    Van Den Barselaar, M.T.3    Ballieux, P.A.4    Van Furth, R.5
  • 131
    • 0027445662 scopus 로고
    • Molecular genetic analysis of a locus required for resistance to antimicrobial peptides in Salmonella typhimurium
    • Parra-Lopez, C., Baer, M. T. & Groisman, E., A. Molecular genetic analysis of a locus required for resistance to antimicrobial peptides in Salmonella typhimurium. EMBO J. 12, 4053-4062 (1993).
    • (1993) EMBO J. , vol.12 , pp. 4053-4062
    • Parra-Lopez, C.1    Baer, M.T.2    Groisman, E.A.3
  • 132
    • 0028114658 scopus 로고
    • How bacteria resist killing by host-defense peptides
    • Groisman, E. A. How bacteria resist killing by host-defense peptides. Trends Microbiol. 2, 444-448 (1994).
    • (1994) Trends Microbiol. , vol.2 , pp. 444-448
    • Groisman, E.A.1
  • 133
    • 0029845913 scopus 로고    scopus 로고
    • Multidrug efflux pumps of Gram-negative bacteria
    • Nikaido, H. Multidrug efflux pumps of Gram-negative bacteria. J. Bacteriol. 178, 5853-5859 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 5853-5859
    • Nikaido, H.1
  • 134
    • 0032539553 scopus 로고    scopus 로고
    • Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family
    • Shafer, W. M., Qu, X., Waring, A. J. & Lehrer, R. I. Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family. Proc. Natl Acad. Sci, USA 95, 1829-1833 (1998).
    • (1998) Proc. Natl. Acad. Sci, USA , vol.95 , pp. 1829-1833
    • Shafer, W.M.1    Qu, X.2    Waring, A.J.3    Lehrer, R.I.4
  • 135
    • 0026048043 scopus 로고
    • A novel endopeptidase from Xenopus that recognizes α-helical secondary structure
    • Resnick, N. M., Maloy, W. L., Guy, H. R. & Zasloff, M. A novel endopeptidase from Xenopus that recognizes α-helical secondary structure. Cell 66, 541-554 (1991).
    • (1991) Cell , vol.66 , pp. 541-554
    • Resnick, N.M.1    Maloy, W.L.2    Guy, H.R.3    Zasloff, M.4
  • 136
    • 0028364818 scopus 로고
    • Isolation and characterization of a gene, pmrD, from Salmonella typhimurium that confers resistance to polymyxin when expressed in multiple copies
    • Roland, K. L., Esther, C. R. & Spitznagel, J. K. Isolation and characterization of a gene, pmrD, from Salmonella typhimurium that confers resistance to polymyxin when expressed in multiple copies. J. Bacteriol. 176, 3589-3597 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 3589-3597
    • Roland, K.L.1    Esther, C.R.2    Spitznagel, J.K.3
  • 137
    • 4544254599 scopus 로고    scopus 로고
    • Proteus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides
    • Belas, R., Manos, J. & Suvanasuthi, R. Proteus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides. Infect. Immun. 72, 5159-5167 (2004).
    • (2004) Infect. Immun. , vol.72 , pp. 5159-5167
    • Belas, R.1    Manos, J.2    Suvanasuthi, R.3
  • 138
    • 9644255763 scopus 로고    scopus 로고
    • Degradation of human antimicrobial peptide LL-37 by Staphylococcus aureus-derived proteinases
    • Sieprawska-Lupa, M. et al. Degradation of human antimicrobial peptide LL-37 by Staphylococcus aureus-derived proteinases. Antimicrob. Agents Chemother. 48, 4673-4679 (2004).
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 4673-4679
    • Sieprawska-Lupa, M.1
  • 139
    • 0036218636 scopus 로고    scopus 로고
    • Cathelicidins: Microbicidal activity, mechanisms of action, and roles in innate immunity
    • Ramanathan, B., Davis, E. G., Ross, C.R & Blecha, F. Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity. Microbes Infect. 4, 361-372 (2002).
    • (2002) Microbes Infect. , vol.4 , pp. 361-372
    • Ramanathan, B.1    Davis, E.G.2    Ross, C.R.3    Blecha, F.4
  • 140
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers, J. R. & Hancock, R. E. The relationship between peptide structure and antibacterial activity. Peptides 24, 1681-1691 (2003).
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.R.1    Hancock, R.E.2
  • 142
    • 2442515355 scopus 로고    scopus 로고
    • Multidimensional signatures in antimicrobial peptides
    • Yount, N. Y. & Yeaman, M. R. Multidimensional signatures in antimicrobial peptides. Proc. Natl Acad. Sci. USA 101, 7363-7368 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7363-7368
    • Yount, N.Y.1    Yeaman, M.R.2
  • 143
    • 0028924198 scopus 로고
    • Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2
    • Matsuzaki, K., Sugishita, K., Fujii, N. & Miyajima, K. Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2. Biochemistry 34, 3423-3429 (1995).
    • (1995) Biochemistry , vol.34 , pp. 3423-3429
    • Matsuzaki, K.1    Sugishita, K.2    Fujii, N.3    Miyajima, K.4
  • 144
    • 0033591467 scopus 로고    scopus 로고
    • Bacterial biofilms: A common cause of persistent infections
    • Costerton, J. W, Stewart, P. S. & Greenberg, E. P. Bacterial biofilms: a common cause of persistent infections. Science 284 1318-1322 (1999).
    • (1999) Science , vol.284 , pp. 1318-1322
    • Costerton, J.W.1    Stewart, P.S.2    Greenberg, E.P.3
  • 145
    • 0037198693 scopus 로고    scopus 로고
    • A component of innate immunity prevents bacterial biofilm development
    • Singh, P. K., Parsek, M. R., Greenberg, E. P. & Welsh, M. J. A component of innate immunity prevents bacterial biofilm development. Nature 417, 552-555 (2002).
    • (2002) Nature , vol.417 , pp. 552-555
    • Singh, P.K.1    Parsek, M.R.2    Greenberg, E.P.3    Welsh, M.J.4
  • 146
  • 147
    • 0035198723 scopus 로고    scopus 로고
    • Dermcidin: A novel human antibiotic peptide secreted by sweat glands
    • Schittek, B. et al. Dermcidin: a novel human antibiotic peptide secreted by sweat glands. Nature Immunol. 2, 1133-1137 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 1133-1137
    • Schittek, B.1
  • 148
    • 0037362455 scopus 로고    scopus 로고
    • Ascaris nematodes from pig and human make three antibacterial peptides: Isolation of cecropin P1 and two ASABF peptides
    • Andersson, M., Boman, A. & Boman, H. G. Ascaris nematodes from pig and human make three antibacterial peptides: isolation of cecropin P1 and two ASABF peptides. Cell. Mol. Life Sci. 60 599-606 (2003).
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 599-606
    • Andersson, M.1    Boman, A.2    Boman, H.G.3
  • 149
    • 0032808386 scopus 로고    scopus 로고
    • Purification and properties of proline-rich antimicrobial peptides from sheep and goat leukocytes
    • Shamova, O. et al. Purification and properties of proline-rich antimicrobial peptides from sheep and goat leukocytes. Infect. Immun. 67, 4106-4111 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 4106-4111
    • Shamova, O.1
  • 150
    • 0028839913 scopus 로고
    • Structures of genes for two cathelin-associated antimicrobial peptides: Prophenin-2 and PR-39
    • Zhao, C., Ganz, T. & Lehrer, R. I. Structures of genes for two cathelin-associated antimicrobial peptides: prophenin-2 and PR-39. FEBS Lett. 376, 130-134 (1995).
    • (1995) FEBS Lett. , vol.376 , pp. 130-134
    • Zhao, C.1    Ganz, T.2    Lehrer, R.I.3
  • 151
    • 0026722445 scopus 로고
    • Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils
    • Selsted, M. E. et al. Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils. J. Biol. Chem. 267, 4292-4295 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 4292-4295
    • Selsted, M.E.1
  • 152
    • 0034736299 scopus 로고    scopus 로고
    • Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris
    • Basir, Y. J., Knoop, F. C., Dulka, J. & Conlon, J. M. Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. Biochim. Biophys. Acta 1543, 95-105 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 95-105
    • Basir, Y.J.1    Knoop, F.C.2    Dulka, J.3    Conlon, J.M.4
  • 153
    • 0027169823 scopus 로고
    • Protegrins: Leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins
    • Kokryalkov, V. N. et al. Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins. FEBS Lett. 327, 231-236 (1993).
    • (1993) FEBS Lett. , vol.327 , pp. 231-236
    • Kokryalkov, V.N.1
  • 155
    • 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. et al. 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).
    • (1994) J. Biol. Chem. , vol.269 , pp. 33159-33163
    • Fehlbaum, P.1
  • 156
    • 0029111532 scopus 로고
    • Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles
    • Gazit, E., Boman, A., Boman, H. G. & Shai, Y. Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles. Biochemistry 34, 11479-11488 (1995).
    • (1995) Biochemistry , vol.34 , pp. 11479-11488
    • Gazit, E.1    Boman, A.2    Boman, H.G.3    Shai, Y.4
  • 157
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning polypeptides
    • Shai, Y. Molecular recognition between membrane-spanning polypeptides. Trends Biochem. Sci. 20, 460-464 (1995).
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 460-464
    • Shai, Y.1
  • 158
    • 0034023711 scopus 로고    scopus 로고
    • 13C NMR spectroscopy
    • 13C NMR spectroscopy. Biophys. J. 78, 2405-2417 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 2405-2417
    • Naito, A.1
  • 159
    • 0030852756 scopus 로고    scopus 로고
    • The solution structure activity of caerin 1.1, an antimicrobial peptide from the Australian green tree frog, Litoria splendida
    • Wong, H., Bowie, J. H. & Carver, J. A. The solution structure activity of caerin 1.1, an antimicrobial peptide from the Australian green tree frog, Litoria splendida. Eur. J. Biochem. 247, 545-557 (1997).
    • (1997) Eur. J. Biochem. , vol.247 , pp. 545-557
    • Wong, H.1    Bowie, J.H.2    Carver, J.A.3
  • 160
    • 0026244229 scopus 로고
    • MolScript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. MolScript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 161
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A. & Bacon, D. J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505-524 (1997).
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 162
    • 2942754299 scopus 로고    scopus 로고
    • Molecular mechanism of peptide induced pores in membranes
    • Huang, H.W. Molecular mechanism of peptide induced pores in membranes. Phys. Rev. Lett. 92, 198304-1 - 198304-4 (2004).
    • (2004) Phys. Rev. Lett. , vol.92
    • Huang, H.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.