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Volumn 24, Issue 11, 2003, Pages 1681-1691

The relationship between peptide structure and antibacterial activity

Author keywords

Antimicrobial cationic peptide; Polyphemusin; Structure

Indexed keywords

ANTIINFECTIVE AGENT; ANTINEOPLASTIC AGENT; ANTIVIRUS AGENT; BETA DEFENSIN; CIRCULIN; DEFENSIN; DROSOMYCIN; GOMISIN; HELIOMYCIN; HEPCIDIN; HEPCIDIN 20; HEPCIDIN 25; INDOLICIDIN; INDOLICIDIN DERIVATIVE; LACTOFERRICIN; LEUCOCIN A; MAGAININ 2; MEDITERRANEAN MUSSEL DEFENSIN; MEMBRANE LIPID; MORICIN; OVISPIRIN 1; PEPTIDE DERIVATIVE; PROTEGRIN; RAMOPLANIN; SAPECIN; TACHYSTATIN A; THANATIN; THETA DEFENSIN; THIONINE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 1042278915     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2003.08.023     Document Type: Article
Times cited : (795)

References (102)
  • 1
    • 0027945728 scopus 로고
    • Killing of Giardia lamblia by cryptdins and cationic neutrophil peptides
    • Aley S.B., Zimmerman M., Hetsko M., Selsted M.E., Gillin F.D. Killing of Giardia lamblia by cryptdins and cationic neutrophil peptides. Infect. Immun. 62:1994;5397-5403.
    • (1994) Infect. Immun. , vol.62 , pp. 5397-5403
    • Aley, S.B.1    Zimmerman, M.2    Hetsko, M.3    Selsted, M.E.4    Gillin, F.D.5
  • 2
    • 0036301039 scopus 로고    scopus 로고
    • Solution structure of Pisum sativum defensin 1 by high resolution NMR: Plant defensins, identical backbone with different mechanisms of action
    • Almeida M.S., Cabral K.M., Kurtenbach E., Almeida F.C., Valente A.P. Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical backbone with different mechanisms of action. J. Mol. Biol. 315:2002;749-757.
    • (2002) J. Mol. Biol. , vol.315 , pp. 749-757
    • Almeida, M.S.1    Cabral, K.M.2    Kurtenbach, E.3    Almeida, F.C.4    Valente, A.P.5
  • 3
    • 0027166016 scopus 로고
    • Anticancer efficacy of magainin 2 and analogue peptides
    • Baker M.A., Maloy W.L., Zasloff M., Jacob L.S. Anticancer efficacy of magainin 2 and analogue peptides. Cancer Res. 53:1993;3052-3057.
    • (1993) Cancer Res. , vol.53 , pp. 3052-3057
    • Baker, M.A.1    Maloy, W.L.2    Zasloff, M.3    Jacob, L.S.4
  • 4
    • 0035188391 scopus 로고    scopus 로고
    • Structure determination of human and murine beta-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.et al. Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity. Protein Sci. 10:2001;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
  • 5
    • 0025001650 scopus 로고
    • All-D-magainin: Chirality, antimicrobial activity and proteolytic resistance
    • Bessalle R., Kapitkovsky A., Gorea A., Shalit I., Fridkin M. All-D-magainin: chirality, antimicrobial activity and proteolytic resistance. FEBS Lett. 274:1990;151-155.
    • (1990) FEBS Lett. , vol.274 , pp. 151-155
    • Bessalle, R.1    Kapitkovsky, A.2    Gorea, A.3    Shalit, I.4    Fridkin, M.5
  • 6
    • 15844379770 scopus 로고    scopus 로고
    • A phospholipid acts as a chaperone in assembly of a membrane transport protein
    • Bogdanov M., Sun J., Kaback H.R., Dowhan W. A phospholipid acts as a chaperone in assembly of a membrane transport protein. J. Biol. Chem. 271:1996;11615-11618.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11615-11618
    • Bogdanov, M.1    Sun, J.2    Kaback, H.R.3    Dowhan, W.4
  • 10
    • 0033534366 scopus 로고    scopus 로고
    • Solution structure by NMR of circulin A: A macrocyclic knotted peptide having anti-HIV activity
    • Daly N.L., Koltay A., Gustafson K.R., Boyd M.R., Casas-Finet J.R., Craik D.J. Solution structure by NMR of circulin A: a macrocyclic knotted peptide having anti-HIV activity. J. Mol. Biol. 285:1999;333-345.
    • (1999) J. Mol. Biol. , vol.285 , pp. 333-345
    • Daly, N.L.1    Koltay, A.2    Gustafson, K.R.3    Boyd, M.R.4    Casas-Finet, J.R.5    Craik, D.J.6
  • 11
    • 0035919725 scopus 로고    scopus 로고
    • Optimization of the antimicrobial activity of magainin peptides by modification of charge
    • Dathe M., Nikolenko H., Meyer J., Beyermann M., Bienert M. Optimization of the antimicrobial activity of magainin peptides by modification of charge. FEBS Lett. 501:2001;146-150.
    • (2001) FEBS Lett. , vol.501 , pp. 146-150
    • Dathe, M.1    Nikolenko, H.2    Meyer, J.3    Beyermann, M.4    Bienert, M.5
  • 12
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bilayers
    • Ehrenstein G., Lecar H. Electrically gated ionic channels in lipid bilayers. Q. Rev. Biophys. 10:1977;1-34.
    • (1977) Q. Rev. Biophys. , vol.10 , pp. 1-34
    • Ehrenstein, G.1    Lecar, H.2
  • 13
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand R.M., Vogel H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta. 1462:1999;11-28.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 14
    • 0030198873 scopus 로고    scopus 로고
    • Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes
    • Fahrner R.L., Dieckmann T., Harwig S.S., Lehrer R.I., Eisenberg D., Feigon J. Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes. Chem. Biol. 3:1996;543-550.
    • (1996) Chem. Biol. , vol.3 , pp. 543-550
    • Fahrner, R.L.1    Dieckmann, T.2    Harwig, S.S.3    Lehrer, R.I.4    Eisenberg, D.5    Feigon, J.6
  • 15
    • 9444225012 scopus 로고    scopus 로고
    • Mode of action of the antimicrobial peptide indolicidin
    • Falla T.J., Karunaratne D.N., Hancock R.E.W. Mode of action of the antimicrobial peptide indolicidin. J. Biol. Chem. 271:1996;19298-19303.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19298-19303
    • Falla, T.J.1    Karunaratne, D.N.2    Hancock, R.E.W.3
  • 17
    • 0030071417 scopus 로고    scopus 로고
    • Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides
    • Fehlbaum P., Bulet P., Chernysh S., Briand J.P., Roussel J.P., Letellier L.et al. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proc. Natl. Acad. Sci. U.S.A. 93:1996;1221-1225.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1221-1225
    • Fehlbaum, P.1    Bulet, P.2    Chernysh, S.3    Briand, J.P.4    Roussel, J.P.5    Letellier, L.6
  • 18
    • 0000870269 scopus 로고    scopus 로고
    • Three-dimensional structure of leucocin a in trifluoroethanol and dodecylphosphocholine micelles: Spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria
    • Fregeau Gallagher N.L., Sailer M., Niemczura W.P., Nakashima T.T., Stiles M.E., Vederas J.C. Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria. Biochemistry. 36:1997;15062-15072.
    • (1997) Biochemistry , vol.36 , pp. 15062-15072
    • Fregeau Gallagher, N.L.1    Sailer, M.2    Niemczura, W.P.3    Nakashima, T.T.4    Stiles, M.E.5    Vederas, J.C.6
  • 21
    • 0035968224 scopus 로고    scopus 로고
    • Structure and mechanism of action of an indolicidin peptide derivative with improved activity against Gram-positive bacteria
    • Friedrich C.L., Rozek A., Patrzykat A., Hancock R.E.W. Structure and mechanism of action of an indolicidin peptide derivative with improved activity against Gram-positive bacteria. J. Biol. Chem. 276:2001;24015-24022.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24015-24022
    • Friedrich, C.L.1    Rozek, A.2    Patrzykat, A.3    Hancock, R.E.W.4
  • 23
    • 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., Suzuki T., Ohashi W., Yagami T., Tanaka S., Ueda K.et al. Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276:2001;5836-5840.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6
  • 24
    • 0028092047 scopus 로고
    • Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds
    • Gallo R.L., Ono M., Povsic T., Page C., Eriksson E., Klagsbrun M.et al. Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds. Proc. Natl. Acad. Sci. U.S.A. 91:1994;11035-11039.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 11035-11039
    • Gallo, R.L.1    Ono, M.2    Povsic, T.3    Page, C.4    Eriksson, E.5    Klagsbrun, M.6
  • 25
    • 0035909081 scopus 로고    scopus 로고
    • Solution structure of PAFP-S: A new knottin-type antifungal peptide from the seeds of Phytolacca americana
    • Gao G.H., Liu W., Dai J.X., Wang J.F., Hu Z., Zhang Y.et al. Solution structure of PAFP-S: a new knottin-type antifungal peptide from the seeds of Phytolacca americana. Biochemistry. 40:2001;10973-10978.
    • (2001) Biochemistry , vol.40 , pp. 10973-10978
    • Gao, G.H.1    Liu, W.2    Dai, J.X.3    Wang, J.F.4    Hu, Z.5    Zhang, Y.6
  • 26
    • 0031062621 scopus 로고    scopus 로고
    • 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution
    • 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution J. Biomol. NMR. 9:1997;127-135.
    • (1997) J. Biomol. NMR , vol.9 , pp. 127-135
    • Gesell, J.1    Zasloff, M.2    Opella, S.J.3
  • 28
    • 0031761654 scopus 로고    scopus 로고
    • In vitro activities of membrane-active peptides against Gram-positive and Gram-negative aerobic bacteria
    • Giacometti A., Cirioni O., Greganti G., Quarta M., Scalise G. In vitro activities of membrane-active peptides against Gram-positive and Gram-negative aerobic bacteria. Antimicrob. Agents Chemother. 42:1998;3320-3324.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 3320-3324
    • Giacometti, A.1    Cirioni, O.2    Greganti, G.3    Quarta, M.4    Scalise, G.5
  • 29
    • 0034882516 scopus 로고    scopus 로고
    • On the mechanism whereby cationic lipids promote intracellular delivery of polynucleic acids
    • Hafez I.M., Maurer N., Cullis P.R. On the mechanism whereby cationic lipids promote intracellular delivery of polynucleic acids. Gene Ther. 8:2001;1188-1196.
    • (2001) Gene Ther. , vol.8 , pp. 1188-1196
    • Hafez, I.M.1    Maurer, N.2    Cullis, P.R.3
  • 30
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock R.E.W. Peptide antibiotics. Lancet. 349:1997;418-422.
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.W.1
  • 32
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock R.E.W., Lehrer R. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16:1998;82-88.
    • (1998) Trends Biotechnol. , vol.16 , pp. 82-88
    • Hancock, R.E.W.1    Lehrer, R.2
  • 33
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • Hancock R.E.W., Rozek A. Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol. Lett. 206:2002;143-149.
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 143-149
    • Hancock, R.E.W.1    Rozek, A.2
  • 35
    • 0035115807 scopus 로고    scopus 로고
    • Effects of peptide dimerization on pore formation: Antiparallel disulfide-dimerized magainin 2 analogue
    • Hara T., Kodama H., Kondo M., Wakamatsu K., Takeda A., Tachi T.et al. Effects of peptide dimerization on pore formation: antiparallel disulfide-dimerized magainin 2 analogue. Biopolymers. 58:2001;437-446.
    • (2001) Biopolymers , vol.58 , pp. 437-446
    • Hara, T.1    Kodama, H.2    Kondo, M.3    Wakamatsu, K.4    Takeda, A.5    Tachi, T.6
  • 36
    • 0037042209 scopus 로고    scopus 로고
    • Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori
    • Hemmi H., Ishibashi J., Hara S., Yamakawa M. Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori. FEBS Lett. 518:2002;33-38.
    • (2002) FEBS Lett. , vol.518 , pp. 33-38
    • Hemmi, H.1    Ishibashi, J.2    Hara, S.3    Yamakawa, M.4
  • 37
    • 0025903814 scopus 로고
    • Crystal structure of defensin HNP-3, an amphiphilic dimer: Mechanisms of membrane permeabilization
    • Hill C.P., Yee J., Selsted M.E., Eisenberg D. Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization. Science. 251:1991;1481-1485.
    • (1991) Science , vol.251 , pp. 1481-1485
    • Hill, C.P.1    Yee, J.2    Selsted, M.E.3    Eisenberg, D.4
  • 38
    • 0037012956 scopus 로고    scopus 로고
    • Specific interactions of the antimicrobial peptide cyclic beta-sheet tachyplesin I with lipopolysaccharides
    • Hirakura Y., Kobayashi S., Matsuzaki K. Specific interactions of the antimicrobial peptide cyclic beta-sheet tachyplesin I with lipopolysaccharides. Biochim. Biophys. Acta. 1562:2002;32-36.
    • (2002) Biochim. Biophys. Acta , vol.1562 , pp. 32-36
    • Hirakura, Y.1    Kobayashi, S.2    Matsuzaki, K.3
  • 39
    • 0037228233 scopus 로고    scopus 로고
    • Transcriptional profile of the Escherichia coli response to the antimicrobial insect peptide cecropin a
    • Hong R.W., Shchepetov M., Weiser J.N., Axelsen P.H. Transcriptional profile of the Escherichia coli response to the antimicrobial insect peptide cecropin A. Antimicrob. Agents Chemother. 47:2003;1-6.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 1-6
    • Hong, R.W.1    Shchepetov, M.2    Weiser, J.N.3    Axelsen, P.H.4
  • 40
    • 0035914442 scopus 로고    scopus 로고
    • The structure of human beta-defensin-1: New insights into structural properties of beta-defensins
    • Hoover D.M., Chertov O., Lubkowski J. The structure of human beta-defensin-1: new insights into structural properties of beta-defensins. J. Biol. Chem. 276:2001;39021-39026.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39021-39026
    • Hoover, D.M.1    Chertov, O.2    Lubkowski, J.3
  • 41
    • 0037020241 scopus 로고    scopus 로고
    • The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis
    • Hunter H.N., Fulton D.B., Ganz T., Vogel H.J. The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis. J. Biol. Chem. 277:2002;37597-37603.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37597-37603
    • Hunter, H.N.1    Fulton, D.B.2    Ganz, T.3    Vogel, H.J.4
  • 42
    • 0032454840 scopus 로고    scopus 로고
    • Structure-function relationships of antimicrobial peptides
    • Hwang P.M., Vogel H.J. Structure-function relationships of antimicrobial peptides. Biochem. Cell. Biol. 76:1998;235-246.
    • (1998) Biochem. Cell. Biol. , vol.76 , pp. 235-246
    • Hwang, P.M.1    Vogel, H.J.2
  • 43
    • 84903421873 scopus 로고    scopus 로고
    • Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin
    • Hwang P.M., Zhou N., Shan X., Arrowsmith C.H., Vogel H.J. Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry. 37:1998;4288-4298.
    • (1998) Biochemistry , vol.37 , pp. 4288-4298
    • Hwang, P.M.1    Zhou, N.2    Shan, X.3    Arrowsmith, C.H.4    Vogel, H.J.5
  • 44
    • 0034044911 scopus 로고    scopus 로고
    • In vitro characterization of the anticancer activity of membrane-active cationic peptides. I. Peptide-mediated cytotoxicity and peptide-enhanced cytotoxic activity of doxorubicin against wild-type and p-glycoprotein over-expressing tumor cell lines
    • Johnstone S.A., Gelmon K., Mayer L.D., Hancock R.E.W., Bally M.B. In vitro characterization of the anticancer activity of membrane-active cationic peptides. I. Peptide-mediated cytotoxicity and peptide-enhanced cytotoxic activity of doxorubicin against wild-type and p-glycoprotein over-expressing tumor cell lines. Anticancer Drug Des. 15:2000;151-160.
    • (2000) Anticancer Drug Des. , vol.15 , pp. 151-160
    • Johnstone, S.A.1    Gelmon, K.2    Mayer, L.D.3    Hancock, R.E.W.4    Bally, M.B.5
  • 45
    • 0024396374 scopus 로고
    • Magainin 2 amide and analogues. Antimicrobial activity, membrane depolarization and susceptibility to proteolysis
    • Juretic D., Chen H.C., Brown J.H., Morell J.L., Hendler R.W., Westerhoff H.V. Magainin 2 amide and analogues. Antimicrobial activity, membrane depolarization and susceptibility to proteolysis. FEBS Lett. 249:1989;219-223.
    • (1989) FEBS Lett. , vol.249 , pp. 219-223
    • Juretic, D.1    Chen, H.C.2    Brown, J.H.3    Morell, J.L.4    Hendler, R.W.5    Westerhoff, H.V.6
  • 47
    • 0025078937 scopus 로고
    • Antimicrobial peptide, tachyplesin I, isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus). NMR determination of the beta-sheet structure
    • Kawano K., Yoneya T., Miyata T., Yoshikawa K., Tokunaga F., Terada Y.et al. Antimicrobial peptide, tachyplesin I, isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus). NMR determination of the beta-sheet structure. J. Biol. Chem. 265:1990;15365-15367.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15365-15367
    • Kawano, K.1    Yoneya, T.2    Miyata, T.3    Yoshikawa, K.4    Tokunaga, F.5    Terada, Y.6
  • 48
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 1996;14(51-55):29-32.
    • (1996) J Mol Graph , vol.14 , Issue.51-55 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 49
    • 0035853022 scopus 로고    scopus 로고
    • The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding
    • Kragol G., Lovas S., Varadi G., Condie B.A., Hoffmann R., Otvos L. Jr. The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding. Biochemistry. 40:2001;3016-3026.
    • (2001) Biochemistry , vol.40 , pp. 3016-3026
    • Kragol, G.1    Lovas, S.2    Varadi, G.3    Condie, B.A.4    Hoffmann, R.5    Otvos, L.Jr.6
  • 50
    • 0029794009 scopus 로고    scopus 로고
    • 3D structure of ramoplanin: A potent inhibitor of bacterial cell wall synthesis
    • Kurz M., Guba W. 3D structure of ramoplanin: a potent inhibitor of bacterial cell wall synthesis. Biochemistry. 35:1996;12570-12575.
    • (1996) Biochemistry , vol.35 , pp. 12570-12575
    • Kurz, M.1    Guba, W.2
  • 51
    • 0037108278 scopus 로고    scopus 로고
    • Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives
    • Laederach A., Andreotti A.H., Fulton D.B. Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives. Biochemistry. 41:2002;12359-12368.
    • (2002) Biochemistry , vol.41 , pp. 12359-12368
    • Laederach, A.1    Andreotti, A.H.2    Fulton, D.B.3
  • 52
    • 0035834050 scopus 로고    scopus 로고
    • Solution structures of the antifungal heliomicin and a selected variant with both antibacterial and antifungal activities
    • Lamberty M., Caille A., Landon C., Tassin-Moindrot S., Hetru C., Bulet P.et al. Solution structures of the antifungal heliomicin and a selected variant with both antibacterial and antifungal activities. Biochemistry. 40:2001;11995-12003.
    • (2001) Biochemistry , vol.40 , pp. 11995-12003
    • Lamberty, M.1    Caille, A.2    Landon, C.3    Tassin-Moindrot, S.4    Hetru, C.5    Bulet, P.6
  • 53
    • 0030750976 scopus 로고    scopus 로고
    • Solution structure of drosomycin, the first inducible antifungal protein from insects
    • Landon C., Sodano P., Hetru C., Hoffmann J., Ptak M. Solution structure of drosomycin, the first inducible antifungal protein from insects. Protein Sci. 6:1997;1878-1884.
    • (1997) Protein Sci. , vol.6 , pp. 1878-1884
    • Landon, C.1    Sodano, P.2    Hetru, C.3    Hoffmann, J.4    Ptak, M.5
  • 54
    • 0024391711 scopus 로고
    • Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity
    • Lehrer R.I., Barton A., Daher K.A., Harwig S.S., Ganz T., Selsted M.E. Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity. J. Clin. Invest. 84:1989;553-561.
    • (1989) J. Clin. Invest. , vol.84 , pp. 553-561
    • Lehrer, R.I.1    Barton, A.2    Daher, K.A.3    Harwig, S.S.4    Ganz, T.5    Selsted, M.E.6
  • 55
    • 0036178451 scopus 로고    scopus 로고
    • The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider
    • Mandard N., Bulet P., Caille A., Daffre S., Vovelle F. The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider. Eur. J. Biochem. 269:2002;1190-1198.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1190-1198
    • Mandard, N.1    Bulet, P.2    Caille, A.3    Daffre, S.4    Vovelle, F.5
  • 56
    • 0031696867 scopus 로고    scopus 로고
    • Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from proton two-dimensional nuclear magnetic resonance data
    • Mandard N., Sodano P., Labbe H., Bonmatin J.M., Bulet P., Hetru C.et al. Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from proton two-dimensional nuclear magnetic resonance data. Eur. J. Biochem. 256:1998;404-410.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 404-410
    • Mandard, N.1    Sodano, P.2    Labbe, H.3    Bonmatin, J.M.4    Bulet, P.5    Hetru, C.6
  • 57
    • 0032738363 scopus 로고    scopus 로고
    • Androctonin, a novel antimicrobial peptide from scorpion Androctonus australis: Solution structure and molecular dynamics simulations in the presence of a lipid monolayer
    • Mandard N., Sy D., Maufrais C., Bonmatin J.M., Bulet P., Hetru C.et al. Androctonin, a novel antimicrobial peptide from scorpion Androctonus australis: solution structure and molecular dynamics simulations in the presence of a lipid monolayer. J. Biomol. Struct. Dyn. 17:1999;367-380.
    • (1999) J. Biomol. Struct. Dyn. , vol.17 , pp. 367-380
    • Mandard, N.1    Sy, D.2    Maufrais, C.3    Bonmatin, J.M.4    Bulet, P.5    Hetru, C.6
  • 58
    • 0029664883 scopus 로고    scopus 로고
    • 1H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus
    • 1H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus J. Mol. Biol. 258:1996;322-333.
    • (1996) J. Mol. Biol. , vol.258 , pp. 322-333
    • Martins, J.C.1    Maes, D.2    Loris, R.3    Pepermans, H.A.4    Wyns, L.5    Willem, R.6
  • 60
    • 0031740520 scopus 로고    scopus 로고
    • Magainins as paradigm for the mode of action of pore forming polypeptides
    • Matsuzaki K. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim. Biophys. Acta. 1376:1998;391-400.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 391-400
    • Matsuzaki, K.1
  • 61
    • 0025977855 scopus 로고
    • Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers
    • Matsuzaki K., Harada M., Funakoshi S., Fujii N., Miyajima K. Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers. Biochim. Biophys. Acta. 1063:1991;162-170.
    • (1991) Biochim. Biophys. Acta , vol.1063 , pp. 162-170
    • Matsuzaki, K.1    Harada, M.2    Funakoshi, S.3    Fujii, N.4    Miyajima, K.5
  • 62
  • 63
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore
    • Matsuzaki K., Murase O., Fujii N., Miyajima K. Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore. Biochemistry. 34:1995;6521-6526.
    • (1995) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 64
    • 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. 34:1995;12553-12559.
    • (1995) Biochemistry , vol.34 , pp. 12553-12559
    • Matsuzaki, K.1    Murase, O.2    Miyajima, K.3
  • 66
    • 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. 1327:1997;119-130.
    • (1997) Biochim. Biophys. Acta , vol.1327 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.2    Harada, M.3    Fujii, N.4    Miyajima, K.5
  • 67
    • 0030757152 scopus 로고    scopus 로고
    • Membrane permeabilization mechanisms of a cyclic antimicrobial peptide, tachyplesin I, and its linear analog
    • Matsuzaki K., Yoneyama S., Fujii N., Miyajima K., Yamada K., Kirino Y.et al. Membrane permeabilization mechanisms of a cyclic antimicrobial peptide, tachyplesin I, and its linear analog. Biochemistry. 36:1997;9799-9806.
    • (1997) Biochemistry , vol.36 , pp. 9799-9806
    • Matsuzaki, K.1    Yoneyama, S.2    Fujii, N.3    Miyajima, K.4    Yamada, K.5    Kirino, Y.6
  • 69
    • 0028816218 scopus 로고
    • Bidesmosidic triterpenoidal saponins from the roots of Symphytum officinale
    • Mohammad F.V., Noorwala M., Ahmad V.U., Sener B. Bidesmosidic triterpenoidal saponins from the roots of Symphytum officinale. Planta Med. 61:1995;94.
    • (1995) Planta Med. , vol.61 , pp. 94
    • Mohammad, F.V.1    Noorwala, M.2    Ahmad, V.U.3    Sener, B.4
  • 70
    • 0025805388 scopus 로고
    • Inhibitory effect of tachyplesin I on the proliferation of human immunodeficiency virus in vitro
    • Morimoto M., Mori H., Otake T., Ueba N., Kunita N., Niwa M.et al. Inhibitory effect of tachyplesin I on the proliferation of human immunodeficiency virus in vitro. Chemotherapy. 37:1991;206-211.
    • (1991) Chemotherapy , vol.37 , pp. 206-211
    • Morimoto, M.1    Mori, H.2    Otake, T.3    Ueba, N.4    Kunita, N.5    Niwa, M.6
  • 71
    • 0026076922 scopus 로고
    • Direct virus inactivation of tachyplesin I and its isopeptides from horseshoe crab hemocytes
    • Murakami T., Niwa M., Tokunaga F., Miyata T., Iwanaga S. Direct virus inactivation of tachyplesin I and its isopeptides from horseshoe crab hemocytes. Chemotherapy. 37:1991;327-334.
    • (1991) Chemotherapy , vol.37 , pp. 327-334
    • Murakami, T.1    Niwa, M.2    Tokunaga, F.3    Miyata, T.4    Iwanaga, S.5
  • 72
    • 0023700978 scopus 로고
    • Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure
    • Nakamura T., Furunaka H., Miyata T., Tokunaga F., Muta T., Iwanaga S.et al. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure. J. Biol. Chem. 263:1988;16709-16713.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16709-16713
    • Nakamura, T.1    Furunaka, H.2    Miyata, T.3    Tokunaga, F.4    Muta, T.5    Iwanaga, S.6
  • 73
    • 0033061716 scopus 로고    scopus 로고
    • NMR structural characterization of cecropin A(1-8)-magainin 2(1-12) and cecropin a (1-8)-melittin (1-12) hybrid peptides
    • Oh D., Shin S.Y., Kang J.H., Hahm K.S., Kim K.L., Kim Y. NMR structural characterization of cecropin A(1-8)-magainin 2(1-12) and cecropin A (1-8)-melittin (1-12) hybrid peptides. J. Pept. Res. 53:1999;578-589.
    • (1999) J. Pept. Res. , vol.53 , pp. 578-589
    • Oh, D.1    Shin, S.Y.2    Kang, J.H.3    Hahm, K.S.4    Kim, K.L.5    Kim, Y.6
  • 74
    • 0034601806 scopus 로고    scopus 로고
    • Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures
    • Oh D., Shin S.Y., Lee S., Kang J.H., Kim S.D., Ryu P.D.et al. Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures. Biochemistry. 39:2000;11855-11864.
    • (2000) Biochemistry , vol.39 , pp. 11855-11864
    • Oh, D.1    Shin, S.Y.2    Lee, S.3    Kang, J.H.4    Kim, S.D.5    Ryu, P.D.6
  • 75
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic alpha-helical antimicrobial peptides
    • Oren Z., Shai Y. Mode of action of linear amphipathic alpha-helical antimicrobial peptides. Biopolymers. 47:1998;451-463.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 76
    • 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. 244:1998;253-257.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 77
    • 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. U.S.A. 97:2000;8245-8250.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 78
    • 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.W. Sublethal concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in Escherichia coli. Antimicrob. Agents Chemother. 46:2002;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.W.5
  • 79
    • 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. 31:1992;12416-12423.
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 80
    • 0032815802 scopus 로고    scopus 로고
    • Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds
    • Rao A.G. Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds. Arch. Biochem. Biophys. 361:1999;127-134.
    • (1999) Arch. Biochem. Biophys. , vol.361 , pp. 127-134
    • Rao, A.G.1
  • 81
    • 0028785891 scopus 로고
    • Non-bilayer lipids are required for efficient protein transport across the plasma membrane of Escherichia coli
    • Rietveld A.G., Koorengevel M.C., de Kruijff B. Non-bilayer lipids are required for efficient protein transport across the plasma membrane of Escherichia coli. EMBO J. 14:1995;5506-5513.
    • (1995) EMBO J. , vol.14 , pp. 5506-5513
    • Rietveld, A.G.1    Koorengevel, M.C.2    De Kruijff, B.3
  • 82
    • 0034719121 scopus 로고    scopus 로고
    • Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles
    • Rozek A., Friedrich C.L., Hancock R.E.W. Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry. 39:2000;15765-15774.
    • (2000) Biochemistry , vol.39 , pp. 15765-15774
    • Rozek, A.1    Friedrich, C.L.2    Hancock, R.E.W.3
  • 83
    • 0036231767 scopus 로고    scopus 로고
    • Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides
    • Sawai M.V., Waring A.J., Kearney W.R., McCray P.B. Jr., Forsyth W.R., Lehrer R.I.et al. Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides. Protein Eng. 15:2002;225-232.
    • (2002) Protein Eng. , vol.15 , pp. 225-232
    • Sawai, M.V.1    Waring, A.J.2    Kearney, W.R.3    McCray, P.B.Jr.4    Forsyth, W.R.5    Lehrer, R.I.6
  • 84
    • 0037040913 scopus 로고    scopus 로고
    • The solution structures of the human beta-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. Jr.et al. The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus. J. Biol. Chem. 277:2002;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 Jr. et al., P.B.6
  • 85
    • 0033592961 scopus 로고    scopus 로고
    • Structure of the antimicrobial peptide tritrpticin bound to micelles: A distinct membrane-bound peptide fold
    • Schibli D.J., Hwang P.M., Vogel H.J. Structure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold. Biochemistry. 38:1999;16749-16755.
    • (1999) Biochemistry , vol.38 , pp. 16749-16755
    • Schibli, D.J.1    Hwang, P.M.2    Vogel, H.J.3
  • 87
    • 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. 1462:1999;55-70.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 88
    • 0032031434 scopus 로고    scopus 로고
    • Mechanism of antimicrobial action of indolicidin
    • Subbalakshmi C., Sitaram N. Mechanism of antimicrobial action of indolicidin. FEMS Microbiol. Lett. 160:1998;91-96.
    • (1998) FEMS Microbiol. Lett. , vol.160 , pp. 91-96
    • Subbalakshmi, C.1    Sitaram, N.2
  • 91
    • 0037184029 scopus 로고    scopus 로고
    • NMR structure of PW2 bound to SDS micelles. A tryptophan-rich anticoccidial peptide selected from phage display libraries
    • Tinoco L.W., Da Silva A. Jr., Leite A., Valente A.P., Almeida F.C. NMR structure of PW2 bound to SDS micelles. A tryptophan-rich anticoccidial peptide selected from phage display libraries. J. Biol. Chem. 277:2002;36351-36356.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36351-36356
    • Tinoco, L.W.1    Da Silva, A.Jr.2    Leite, A.3    Valente, A.P.4    Almeida, F.C.5
  • 92
    • 0035836463 scopus 로고    scopus 로고
    • Three-dimensional structure of RTD-1, a cyclic antimicrobial defensin from Rhesus macaque leukocytes
    • Trabi M., Schirra H.J., Craik D.J. Three-dimensional structure of RTD-1, a cyclic antimicrobial defensin from Rhesus macaque leukocytes. Biochemistry. 40:2001;4211-4221.
    • (2001) Biochemistry , vol.40 , pp. 4211-4221
    • Trabi, M.1    Schirra, H.J.2    Craik, D.J.3
  • 94
    • 0033598699 scopus 로고    scopus 로고
    • Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria
    • Wang Y., Henz M.E., Gallagher N.L., Chai S., Gibbs A.C., Yan L.Z.et al. Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria. Biochemistry. 38:1999;15438-15447.
    • (1999) Biochemistry , vol.38 , pp. 15438-15447
    • Wang, Y.1    Henz, M.E.2    Gallagher, N.L.3    Chai, S.4    Gibbs, A.C.5    Yan, L.Z.6
  • 95
    • 0033151774 scopus 로고    scopus 로고
    • Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli
    • Wu M., Maier E., Benz R., Hancock R.E.W. Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry. 38:1999;7235-7242.
    • (1999) Biochemistry , vol.38 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.W.4
  • 96
    • 0034727642 scopus 로고    scopus 로고
    • Solution structure and activity of the synthetic four-disulfide bond Mediterranean mussel defensin (MGD-1)
    • Yang Y.S., Mitta G., Chavanieu A., Calas B., Sanchez J.F., Roch P.et al. Solution structure and activity of the synthetic four-disulfide bond Mediterranean mussel defensin (MGD-1). Biochemistry. 39:2000;14436-14447.
    • (2000) Biochemistry , vol.39 , pp. 14436-14447
    • Yang, Y.S.1    Mitta, G.2    Chavanieu, A.3    Calas, B.4    Sanchez, J.F.5    Roch, P.6
  • 97
    • 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. 31:1992;2998-3004.
    • (1992) Biochemistry , vol.31 , pp. 2998-3004
    • Yonezawa, A.1    Kuwahara, J.2    Fujii, N.3    Sugiura, Y.4
  • 98
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. U.S.A. 84:1987;5449-5453.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 99
    • 0023854883 scopus 로고
    • Antimicrobial activity of synthetic magainin peptides and several analogues
    • Zasloff M., Martin B., Chen H.C. Antimicrobial activity of synthetic magainin peptides and several analogues. Proc. Natl. Acad. Sci. U.S.A. 85:1988;910-913.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 910-913
    • Zasloff, M.1    Martin, B.2    Chen, H.C.3
  • 100
    • 0033594986 scopus 로고    scopus 로고
    • Influence of proline residues on the antibacterial and synergistic activities of alpha-helical peptides
    • Zhang L., Benz R., Hancock R.E.W. Influence of proline residues on the antibacterial and synergistic activities of alpha-helical peptides. Biochemistry. 38:1999;8102-8111.
    • (1999) Biochemistry , vol.38 , pp. 8102-8111
    • Zhang, L.1    Benz, R.2    Hancock, R.E.W.3
  • 101
    • 0035929565 scopus 로고    scopus 로고
    • Interaction of cationic antimicrobial peptides with model membranes
    • Zhang L., Rozek A., Hancock R.E.W. Interaction of cationic antimicrobial peptides with model membranes. J. Biol. Chem. 276:2001;35714-35722.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35714-35722
    • Zhang, L.1    Rozek, A.2    Hancock, R.E.W.3
  • 102
    • 0028825285 scopus 로고
    • Solution structure of bovine neutrophil beta-defensin-12: The peptide fold of the beta-defensins is identical to that of the classical defensins
    • Zimmermann G.R., Legault P., Selsted M.E., Pardi A. Solution structure of bovine neutrophil beta-defensin-12: the peptide fold of the beta-defensins is identical to that of the classical defensins. Biochemistry. 34:1995;13663-13671.
    • (1995) Biochemistry , vol.34 , pp. 13663-13671
    • Zimmermann, G.R.1    Legault, P.2    Selsted, M.E.3    Pardi, A.4


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