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Volumn 77, Issue 4, 2005, Pages 466-475

Mammalian defensins: Structures and mechanism of antibiotic activity

Author keywords

Human defensin 3; Membrane depolarization; Staphylococci

Indexed keywords

ANTIBIOTIC AGENT; DEFENSIN; NISIN;

EID: 16844373436     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1189/jlb.0804452     Document Type: Conference Paper
Times cited : (186)

References (58)
  • 1
    • 0031821708 scopus 로고    scopus 로고
    • Gene-encoded peptide antibiotics and the concept of innate immunity: An update review
    • Boman, H. G. (1998) Gene-encoded peptide antibiotics and the concept of innate immunity: an update review. Scand. J. Immunol. 48, 15-25.
    • (1998) Scand. J. Immunol. , vol.48 , pp. 15-25
    • Boman, H.G.1
  • 3
    • 0033962266 scopus 로고    scopus 로고
    • Innate immunity and the normal microflora
    • Boman, H.G. (2000) Innate immunity and the normal microflora. Immunol. Rev. 173, 5-16.
    • (2000) Immunol. Rev. , vol.173 , pp. 5-16
    • Boman, H.G.1
  • 4
    • 0032005344 scopus 로고    scopus 로고
    • Antimicrobial peptides of vertebrates
    • Ganz, T., Lehrer, R. I. (1998) Antimicrobial peptides of vertebrates. Curr. Opin. Immunol. 10, 41-44.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 41-44
    • Ganz, T.1    Lehrer, R.I.2
  • 5
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defenses
    • Hancock, R. E., Diamond, G. (2000) The role of cationic antimicrobial peptides in innate host defenses. Trends Microbiol. 8, 402-410.
    • (2000) Trends Microbiol. , vol.8 , pp. 402-410
    • Hancock, R.E.1    Diamond, G.2
  • 6
    • 0036257512 scopus 로고    scopus 로고
    • Molecular diversity in gene-encoded, cationic antimicrobial polypeptides
    • Tossi, A., Sandri, L. (2002) Molecular diversity in gene-encoded, cationic antimicrobial polypeptides. Curr. Pharm. Des. 8, 743-761.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 743-761
    • Tossi, A.1    Sandri, L.2
  • 7
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms. Nature 415, 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 9
    • 0034252293 scopus 로고    scopus 로고
    • Secretion of microbicidal α-defensins by intestinal Paneth cells in response to bacteria
    • Ayabe, T., Satchell, D. P., Wilson, C. L., Parks, W. C., Selsted, M. E., Ouellette, A. J. (2000) Secretion of microbicidal α-defensins by intestinal Paneth cells in response to bacteria. Nat. Immunol. 1, 113-118.
    • (2000) Nat. Immunol. , vol.1 , pp. 113-118
    • Ayabe, T.1    Satchell, D.P.2    Wilson, C.L.3    Parks, W.C.4    Selsted, M.E.5    Ouellette, A.J.6
  • 10
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and characterization of human β-defensin-3, a novel human inducible peptide antibiotic
    • Harder, J., Bartels, J., Christophers, E., Schroder, J. M. (2001) Isolation and characterization of human β-defensin-3, a novel human inducible peptide antibiotic. J. Biol. Chem. 276, 5707-5713.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schroder, J.M.4
  • 13
    • 0035163451 scopus 로고    scopus 로고
    • Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds
    • Cole, A. M., Shi, J., Ceccarelli, A., Kim, Y. H., Park, A., Ganz, T. (2001) Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds. Blood 97, 297-304.
    • (2001) Blood , vol.97 , pp. 297-304
    • Cole, A.M.1    Shi, J.2    Ceccarelli, A.3    Kim, Y.H.4    Park, A.5    Ganz, T.6
  • 15
    • 0037068959 scopus 로고    scopus 로고
    • Deficiency of antibacterial peptides in patients with morbus Kostmann: An observation study
    • Putsep, K., Carlsson, G., Boman, H. G., Andersson, M. (2002) Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study. Lancet 360, 1144-1149.
    • (2002) Lancet , vol.360 , pp. 1144-1149
    • Putsep, K.1    Carlsson, G.2    Boman, H.G.3    Andersson, M.4
  • 16
    • 0035126317 scopus 로고    scopus 로고
    • Downregulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator
    • Islam, D., Bandholtz, L., Nilsson, J., Wigzell, H., Christensson, B., Agerberth, B., Gudmundsson, G. (2001) Downregulation of bactericidal peptides in enteric infections: a novel immune escape mechanism with bacterial DNA as a potential regulator. Nat. Med. 7, 180-185.
    • (2001) Nat. Med. , vol.7 , pp. 180-185
    • Islam, D.1    Bandholtz, L.2    Nilsson, J.3    Wigzell, H.4    Christensson, B.5    Agerberth, B.6    Gudmundsson, G.7
  • 17
    • 0036532403 scopus 로고    scopus 로고
    • How do bacteria resist human antimicrobial peptides?
    • Peschel, A. (2002) How do bacteria resist human antimicrobial peptides? Trends Microbiol. 10, 179-186.
    • (2002) Trends Microbiol. , vol.10 , pp. 179-186
    • Peschel, A.1
  • 18
    • 0033794504 scopus 로고    scopus 로고
    • Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium
    • Gunn, J. S., Ryan, S. S., Van Velkinburgh, J. C., Ernst, R. K., Miller, S. I. (2000) Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium. Infect. Immun. 68, 6139-6146.
    • (2000) Infect. Immun. , vol.68 , pp. 6139-6146
    • Gunn, J.S.1    Ryan, S.S.2    Van Velkinburgh, J.C.3    Ernst, R.K.4    Miller, S.I.5
  • 20
    • 0037099263 scopus 로고    scopus 로고
    • Staphylococcus aureus strains lacking D-alanine modifications of teichoic acids are highly susceptible to human neutrophil killing and are virulence attenuated in mice
    • Collins, L. V., Kristian, S. A., Weidenmaier, C., Faigle, M., Van Kessel, K. P., Van Strijp, J. A., Gotz, F., Neumeister, B., Peschel, A. (2002) Staphylococcus aureus strains lacking D-alanine modifications of teichoic acids are highly susceptible to human neutrophil killing and are virulence attenuated in mice. J. Infect. Dis. 186, 214-219.
    • (2002) J. Infect. Dis. , vol.186 , pp. 214-219
    • Collins, L.V.1    Kristian, S.A.2    Weidenmaier, C.3    Faigle, M.4    Van Kessel, K.P.5    Van Strijp, J.A.6    Gotz, F.7    Neumeister, B.8    Peschel, A.9
  • 21
    • 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. (2003) MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing. Infect. Immun. 71, 546-549.
    • (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
  • 23
    • 0036606951 scopus 로고    scopus 로고
    • Mammalian defensins in immunity: More than just microbicidal
    • Yang, D., Biragyn, A., Kwak, L. W., Oppenheim, J. J. (2002) Mammalian defensins in immunity: more than just microbicidal. Trends Immunol. 23, 291-296.
    • (2002) Trends Immunol. , vol.23 , pp. 291-296
    • Yang, D.1    Biragyn, A.2    Kwak, L.W.3    Oppenheim, J.J.4
  • 24
    • 2542480000 scopus 로고    scopus 로고
    • Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense
    • Yang, D., Biragyn, A., Hoover, D. M., Lubkowski, J., Oppenheim, J. J. (2004) Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense. Annu. Rev. Immunol. 22, 181-215.
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 181-215
    • Yang, D.1    Biragyn, A.2    Hoover, D.M.3    Lubkowski, J.4    Oppenheim, J.J.5
  • 25
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, α-helical antimicrobial peptides
    • Tossi, A., Sandri, L., Giangaspero, A. (2000) Amphipathic, α-helical antimicrobial peptides. Biopolymers 55, 4-30.
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 26
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: An overview
    • Andreu, D., Rivas, L. (1998) Animal antimicrobial peptides: an overview. Biopolymers 47, 415-433.
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 27
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic α-helical antimicrobial peptides
    • Oren, Z., Shai, Y. (1998) Mode of action of linear amphipathic α-helical antimicrobial peptides. Biopolymers 47, 451-463.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 28
    • 0008589659 scopus 로고    scopus 로고
    • Wiley and Sons, New York
    • Tossi, A., ed. (2000) Biopolymers 55, Wiley and Sons, New York, 1-98.
    • (2000) Biopolymers , vol.55 , pp. 1-98
    • Tossi, A.1
  • 29
    • 0032441635 scopus 로고    scopus 로고
    • Wiley and Sons, New York
    • Andreu, D., ed. (1998) Biopolymers 47, Wiley and Sons, New York, 413-497,
    • (1998) Biopolymers , vol.47 , pp. 413-497
    • Andreu, D.1
  • 30
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • Huang, H. W. (2000) Action of antimicrobial peptides: two-state model. Biochemistry 39, 8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 32
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • Hancock, R. E., Rozek, A. (2002) Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol. Lett. 206, 143-149.
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 143-149
    • Hancock, R.E.1    Rozek, A.2
  • 33
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai, Y. (2002) Mode of action of membrane active antimicrobial peptides. Biopolymers 66, 236-248.
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 34
    • 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. (1996) An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry 35, 11361-11368.
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 35
    • 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. (1998) 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) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 36
    • 0037428394 scopus 로고    scopus 로고
    • Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes
    • Takeshima, K., Chikushi, A., Lee, K. K., Yonehara, S., Matsuzaki, K. (2003) Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes. J. Biol. Chem. 278, 1310-1315.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1310-1315
    • Takeshima, K.1    Chikushi, A.2    Lee, K.K.3    Yonehara, S.4    Matsuzaki, K.5
  • 37
    • 16844381949 scopus 로고    scopus 로고
    • Overview: Antimicrobial peptides, as seen from a rearview mirror
    • (R. E. Hancock, D. R. Devine, eds.), Cambridge, UK, Cambridge University Press
    • Lehrer, R. (2004) Overview: antimicrobial peptides, as seen from a rearview mirror. In Mammalian Host Defense Peptides (R. E. Hancock, D. R. Devine, eds.), Cambridge, UK, Cambridge University Press, 5-8.
    • (2004) Mammalian Host Defense Peptides , pp. 5-8
    • Lehrer, R.1
  • 38
    • 0001860958 scopus 로고
    • Induction of autolysis of Staphylococcus simulans 22 by Pep5 and nisin and influence of the cationic peptides on the activity of the autolytic enzymes
    • (G. Jung, H. Sahl, eds.), Leiden, The Netherlands, Escom
    • Bierbaum, G., Sahl, H. (1991) Induction of autolysis of Staphylococcus simulans 22 by Pep5 and nisin and influence of the cationic peptides on the activity of the autolytic enzymes. In Nisin and Novel Lantibiotics (G. Jung, H. Sahl, eds.), Leiden, The Netherlands, Escom, 386-396.
    • (1991) Nisin and Novel Lantibiotics , pp. 386-396
    • Bierbaum, G.1    Sahl, H.2
  • 39
    • 0031782954 scopus 로고    scopus 로고
    • Lantibiotics: Biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria
    • Sahl, H. G., Bierbaum, G. (1998) Lantibiotics: biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria. Annu. Rev. Microbiol. 52, 41-79.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 41-79
    • Sahl, H.G.1    Bierbaum, G.2
  • 40
    • 0021993065 scopus 로고
    • Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles
    • Ruhr, E., Sahl, H. G. (1985) Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles. Antimicrob. Agents Chemother. 27, 841-845.
    • (1985) Antimicrob. Agents Chemother. , vol.27 , pp. 841-845
    • Ruhr, E.1    Sahl, H.G.2
  • 41
    • 0003107982 scopus 로고
    • Pore formation in bacterial membranes by cationic lantibiotics
    • (G. Jung, H. Sahl, eels.), Leiden, The Netherlands, Escom
    • Sahl, H. (1991) Pore formation in bacterial membranes by cationic lantibiotics. In Nisin and Novel Lantibiotics (G. Jung, H. Sahl, eels.), Leiden, The Netherlands, Escom, 347-358.
    • (1991) Nisin and Novel Lantibiotics , pp. 347-358
    • Sahl, H.1
  • 43
    • 0030969611 scopus 로고    scopus 로고
    • The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation
    • Brotz, H., Bierbaum, G., Reynolds, P. E., Sahl, H. G. (1997) The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation. Eur. J. Biochem. 246, 193-199.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 193-199
    • Brotz, H.1    Bierbaum, G.2    Reynolds, P.E.3    Sahl, H.G.4
  • 44
    • 0031784281 scopus 로고    scopus 로고
    • Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics
    • Brotz, H., Josten, M., Wiedemann, I., Schneider, U., Gotz, F., Bierbaum, G., Sahl, H. G. (1998) Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics. Mol. Microbiol. 30, 317-327.
    • (1998) Mol. Microbiol. , vol.30 , pp. 317-327
    • Brotz, H.1    Josten, M.2    Wiedemann, I.3    Schneider, U.4    Gotz, F.5    Bierbaum, G.6    Sahl, H.G.7
  • 45
  • 46
    • 0035910508 scopus 로고    scopus 로고
    • Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity
    • Wiedemann, I., Breukink, E., van Kraaij, C., Kuipers, O. P., Bierbaum, G., de Kruijff, B., Sahl, H. G. (2001) Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity. J. Biol. Chem. 276, 1772-1779.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1772-1779
    • Wiedemann, I.1    Breukink, E.2    Van Kraaij, C.3    Kuipers, O.P.4    Bierbaum, G.5    De Kruijff, B.6    Sahl, H.G.7
  • 47
    • 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. (1987) Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-L- alanine amidase. J. Bacteriol. 169, 5452-5458.
    • (1987) J. Bacteriol. , vol.169 , pp. 5452-5458
    • Bierbaum, G.1    Sahl, H.G.2
  • 48
    • 0035871890 scopus 로고    scopus 로고
    • Cationic peptides from leukocytes might kill bacteria by activating their autolytic enzymes causing bacteriolysis: Why are publications proposing this concept never acknowledged?
    • Ginsburg, I. (2001) Cationic peptides from leukocytes might kill bacteria by activating their autolytic enzymes causing bacteriolysis: why are publications proposing this concept never acknowledged? Blood 97, 2530-2531.
    • (2001) Blood , vol.97 , pp. 2530-2531
    • Ginsburg, I.1
  • 49
    • 0028825285 scopus 로고
    • Solution structure of bovine neutrophil β-defensin-12: The peptide fold of the β-defensins is identical to that of the classical defensins
    • Zimmermann, G. R., Legault, P., Selsted, M. E., Pardi, A. (1995) Solution structure of bovine neutrophil β-defensin-12: the peptide fold of the β-defensins is identical to that of the classical defensins. Biochemistry 34, 13663-13671.
    • (1995) Biochemistry , vol.34 , pp. 13663-13671
    • Zimmermann, G.R.1    Legault, P.2    Selsted, M.E.3    Pardi, A.4
  • 51
    • 0035188391 scopus 로고    scopus 로고
    • Structure determination of human and murine β-defensins reveals structural conservation in the absence of significant sequence similarity
    • Bauer, F., Schweimer, K., Kluver, E., Conejo-Garcia, J. R., Forssmann, W. G., Rosch, P., Adermann, K., Sticht, H. (2001) Structure determination of human and murine β-defensins reveals structural conservation in the absence of significant sequence similarity. Protein Sci. 10, 2470-2479.
    • (2001) Protein Sci. , vol.10 , pp. 2470-2479
    • Bauer, F.1    Schweimer, K.2    Kluver, E.3    Conejo-Garcia, J.R.4    Forssmann, W.G.5    Rosch, P.6    Adermann, K.7    Sticht, H.8
  • 52
    • 0035914442 scopus 로고    scopus 로고
    • The structure of human β-defensin-1: New insights into structural properties of β-defensins
    • Hoover, D. M., Chertov, O., Lubkowski, J. (2001) The structure of human β-defensin-1: new insights into structural properties of β-defensins. J. Biol. Chem. 276, 39021-39026.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39021-39026
    • Hoover, D.M.1    Chertov, O.2    Lubkowski, J.3
  • 53
    • 0037040913 scopus 로고    scopus 로고
    • The solution structures of the human β-defensins lead to a better understanding of the potent bactericidal activity of hBD3 against Staphylococcus aureus
    • Schibli, D. J., Hunter, H. N., Aseyev, V., Starner, T. D., Wiencek, J. M., McCray, P. B., Tack, B. F., Vogel, H. J. (2002) The solution structures of the human β-defensins lead to a better understanding of the potent bactericidal activity of hBD3 against Staphylococcus aureus. J. Biol. Chem. 277, 8279-8289.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8279-8289
    • Schibli, D.J.1    Hunter, H.N.2    Aseyev, V.3    Starner, T.D.4    Wiencek, J.M.5    McCray, P.B.6    Tack, B.F.7    Vogel, H.J.8
  • 56
    • 0031451521 scopus 로고    scopus 로고
    • Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity
    • Tossi, A., Tarantino, C., Romeo, D. (1997) Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity. Eur. J. Biochem. 250, 549-558.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 549-558
    • Tossi, A.1    Tarantino, C.2    Romeo, D.3
  • 57
    • 1242352887 scopus 로고    scopus 로고
    • In vitro activity and mode of action of diastereomeric antimicrobial peptides against bacterial clinical isolates
    • Pag, U., Oedenkoven, M., Papo, N., Oren, Z., Shai, Y., Sahl, H. G. (2004) In vitro activity and mode of action of diastereomeric antimicrobial peptides against bacterial clinical isolates. J. Antimicrob. Chemother. 53, 230-239.
    • (2004) J. Antimicrob. Chemother. , vol.53 , pp. 230-239
    • Pag, U.1    Oedenkoven, M.2    Papo, N.3    Oren, Z.4    Shai, Y.5    Sahl, H.G.6
  • 58
    • 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. (2002) Sublethal concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in Escherichia coli. Antimicrob. Agents Chemother. 46, 605-614.
    • (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


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